# Patent

## Title
Crystal structure of an angiotensin-converting enzyme (ACE) and uses thereof

## Abstract

The present invention relates to a crystal of ACE protein. The present invention further relates to methods, processes, ACE modulators, pharmaceutical compositions and uses of ACE crystal and the structure coordinates thereof.

## Background
This application is a U.S. National Phase Application pursuant to 35 U.S.C. 371 of International Application No. PCT/GB2003/003966 which was filed Sep. 12, 2003, claiming benefit of priority of British Patent Application No. 0221169.6 filed Sep. 12, 2002. The entire disclosure of each of the foregoing applications is incorporated herein by reference.
FIELD OF INVENTION
The present invention relates to a crystal. In particular, the present invention relates to a crystal of ACE protein.
The present invention further relates to methods, processes, ACE modulators, pharmaceutical compositions and uses of the ACE crystal and the structure co-ordinates thereof.
BACKGROUND TO THE INVENTION
Angiotensin converting enzyme (peptidyl dipeptidase A, EC 3.4.15.1, ACE) is a membrane-anchored dipeptidyl carboxypeptidase that is essential for blood pressure regulation and electrolyte homeostasis via the renin-angiotensin-aldosterone system. The enzyme is a zinc metalloprotease that converts the inactive peptide angiotensin I to angiotensin II, a potent vasoconstrictor. ACE, like many diverse membrane-bound ectoproteins, is released from the membrane by a membrane protease or secretase (1). An understanding of this cleavage-secretion mechanism is important for the development of therapeutic strategies to address the different pathologies caused by defects in the function of the secretase. Substrate determinants that specify cleavage by secretases remain incompletely characterised, but may include the physico-chemical properties of the juxtamembrane (“stalk”) sequence or unidentified recognition motifs of the stalk or the extracellular domain. Cleavage of ACE occurs in the stalk sequence and the solubilizing protease is constrained topologically, in terms of the number of residues between the cleavage site and the proximal extracellular domain of ACE. However, the ACE secretase appears to be remarkably versatile in terms of its substrate specificity (2,3).
The active sites of ACE and carboxypeptidase A, a prototypic zinc metalloprotease, are understood to be very similar and this similarity is exploited in the design of the first generation of ACE inhibitors. The clinical success of these inhibitors—such as captopril and enalapril—in the treatment of hypertension and congestive heart failure is well established. However, the side effects such as persistent cough which effects up to 20% of patients and angioedema which is less common, together with limitations such as their contraindication in patients with impaired renal function and decreased efficacy in patients with low-renin hypertension, underscore the need for more specific and selective inhibitors.
There are two isoforms of ACE that are transcribed from the same gene in a tissue specific manner. In somatic tissues it exists as a glycoprotein composed of a single large polypeptide chain of 1277 amino acids whereas the germinal form is synthesised as a lower molecular mass isozyme and is thought to play a role in sperm maturation and the binding of sperm to the oviduct epithelium. The somatic form consists of two domains (N- and C-domain), each containing an active site with a conserved HEXXH zinc-binding motif and a glutamate some 24 residues downstream which forms the third zinc ligand (Williams et al., 1994). The two domains differ in their substrate specificities; inhibitor and chloride activation profiles; and physiological functions. There are two N-domain-specific substrates: the hemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) which controls hematopoietic stem cell differentiation and proliferation; and the bradykinin potentiating peptide angiotensin-(1-7). On the other hand, both active sites catalyse the hydrolysis of angiotensin I and the vasodilator bradykinin with similar efficiency. However, inhibition of the N-domain with a phosphinic peptide RXP407 has no effect on blood pressure regulation (Junot et al., 2001) and, furthermore, expression of the N-domain only, in transgenic mice produced a phenotype similar to the ACE knockout mice (Esther et al., 1997). Thus, the C-domain appears to be necessary and sufficient for controlling blood pressure and cardiovascular function. Testis ACE (tACE) is identical to the C-terminal half of somatic ACE, except for a unique 36-residue sequence constituting its amino terminus, thus this isoform is selected for initial efforts to obtain a three-dimensional structure.
The cDNA sequence of human testicular ACE has been described (Ehlers et al. (1989) Proc. Nat. Acad. Sci. 86: 7741-7745) and the predicted protein consists of a 732-residue preprotein including a 31-residue signal peptide. The mature polypeptide has a molecular weight of 80,073 (unglycosylated form).
Despite the pivotal role of ACE, there have been no reports disclosing that suitable crystals have been or could be obtained for this enzyme and so the X-ray crystallographic analysis of such proteins has been impossible.
SUMMARY OF THE INVENTION
The present invention is based upon the seminal finding of the first three-dimensional structure of the ACE protein.
Peptidases, for example, thermolysin and carboxypeptidase A that have been used in comparative molecular field analysis and 3D quantitative structure-activity relationship studies of ACE (Waller & Marshall, 1993) show no homology with the structure of ACE described herein. Surprisingly, ACE shows significant structural homology with that of neurolysin, a member of the M3 family of thimet oligopeptidases. The two proteins do not share any amino acid sequence identity (close to random score), yet when the two structures are optimally superimposed using DALI server (Hohn & Sander, 1999), there is noticeable match with a root mean square (r.m.s.) deviation of 4.0 Å for 143 Cα atoms. Accordingly, the structure presented herein may be used for the development of novel, highly selective ACE modulators with the potential for greater efficacy, fewer side effects and treatment of new indications.
Thus, in a first aspect, the present invention relates to a crystal of ACE protein.
Preferably, the ACE protein is underglycosylated.
Preferably, the ACE protein is underglycosylated by removing one or more glycosylation sites and/or one or more partially glycosylated sites. More preferably, the underglycosylated ACE protein is deglycosylated at amino acids 337 and 586 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No 2.
Preferably, the crystal comprises atoms arranged in a spatial relationship represented by at least a portion of the structure co-ordinates of Table A or Table B.
Preferably, the crystal belongs to the space group P212121.
Preferably, the crystal has the unit cell dimensions: a=56.47 Å, b=84.90 Å and c=133.99 Å.
Preferably, the crystal is a crystal of human ACE protein.
Preferably, the crystal further comprises an entity bound to the ACE protein or a portion thereof. More preferably, the entity is bound to the ACE protein or a portion thereof by contacting one or more residues of the ACE protein selected from: His384, Ala385, Lys542, Tyr551, Tyr554, Glu415 and His544. More preferably, the entity modulates the activity of ACE. More preferably, the entity is an inhibitor of ACE—such as lisinopril or a derivative thereof.
In a second aspect, the present invention relates to a method of preparing a crystal of ACE protein comprising the steps of: (a) culturing host cells comprising an underglycosylated ACE protein; (b) purifying the underglycosylated ACE protein; and (c) crystallising the underglycosylated ACE protein.
Preferably, the ACE protein is underglycosylated by removing one or more glycosylation sites and/or one or more partially glycosylated sites. More preferably, the underglycosylated ACE protein is deglycosylated at amino acids 337 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No 2.
Preferably, the ACE protein is crystallised using about 10 mM HEPES and about 0.1% PMSF with an equal volume of a reservoir solution containing about 15% PEG 4000, about 50 mM CH3COONa.3H2O pH 4.7 and about 10 μM ZnSO4.7H2O.
Preferably, the crystal that is prepared has a structure defined by at least a portion of the structure co-ordinates of Table A or Table B.
Preferably, the crystal belongs to the space group P212121.
Preferably, the crystal has the unit cell dimensions: a=56.47 Å, b=84.90 Å and c=133.99 Å.
Preferably, the ACE protein is human ACE protein.
Preferably, the crystal further comprises an entity bound to the ACE protein. More preferably, the entity modulates the activity of ACE. More preferably, the entity is an inhibitor of ACE—such as lisinopril or a derivative thereof. More preferably, the crystal that is prepared has a structure defined by at least a portion of the structure co-ordinates of Table B.
In a third aspect, the present invention relates to a method of screening for a modulator of ACE wherein the method comprises the use of a crystal according to the present invention. Preferably, the method comprises the steps of: (a) providing at least a portion of the structure co-ordinates of Table A or Table B; (b) employing at least a portion of the structure co-ordinates of Table A or Table B to design or select or synthesise a putative modulator of ACE; (c) contacting the putative modulator of ACE with ACE or a mutant, variant, homologue, derivative or fragment thereof in the presence of a substrate; and (d) screening the putative modulator of ACE in an assay for the potential to modulate ACE.
Preferably, at least a portion of the structure co-ordinates of Table A or Table B and/or the putative modulator of ACE and/or the substrate are provided on a machine-readable data storage medium comprising a data storage material encoded with machine readable data.
Preferably, the putative ACE modulator is from a library of compounds.
Preferably, the putative ACE modulator is selected from a database.
Preferably, the putative ACE modulator is designed de novo.
Preferably, the putative ACE modulator is designed from a known ACE modulator.
Preferably, the design or selection of the putative ACE modulator is performed in conjunction with computer modelling.
Preferably, the putative ACE modulator is useful in the prevention and/or treatment of an ACE related disorder. More preferably, the ACE related disorder is hypertension.
In a fourth aspect, the present invention relates to a process comprising the steps of: (a) performing the method according to the third aspect of the present invention; (b) identifying one or more modulators of ACE; and (c) preparing a quantity of those one or more ACE modulators.
In a fifth aspect, the present invention relates to a process comprising the steps of: (a) performing the method according to the third aspect of the present invention; (b) identifying one or more ACE modulators; and (c) preparing a pharmaceutical composition comprising those one or more identified ACE modulators.
In a sixth aspect, the present invention relates to a process comprising the steps of: (a) performing the method according to the third aspect of the present invention; (b) identifying one or more ACE modulators; (c) modifying those one or more ACE modulators; and (d) optionally preparing a pharmaceutical composition comprising those one or more ACE modulators.
In a seventh aspect, the present invention relates to a method of obtaining structural information about a molecule or a molecular complex of unknown structure by using at least a portion of the structure co-ordinates of ACE, comprising the steps of: (a) generating X-ray diffraction data from a crystallised molecule or molecular complex; (b) applying at least a portion of the structure co-ordinates of ACE to said X-ray diffraction pattern to generate a three dimensional electron density map of at least a portion of the molecule or molecular complex; and (c) using all or a portion of the structure co-ordinates of ACE to generate homology models of ACE.
In an eighth aspect, the present invention relates to an ACE modulator identified by the method according to the third aspect of the present invention. Preferably, the ACE modulator inhibits ACE.
In a ninth aspect, the present invention relates to a pharmaceutical composition comprising an ACE modulator according to the seventh aspect of the present invention and a pharmaceutically acceptable carrier, diluent, excipient or adjuvant or any combination thereof.
In a tenth aspect, the present invention relates to a method of preventing and/or treating an ACE related disorder comprising administering a modulator of ACE according to the seventh aspect of the present invention and/or a pharmaceutical according to the eighth aspect of the present invention, wherein said modulator of ACE or said pharmaceutical is capable of causing a beneficial preventative and/or therapeutic effect.
In an eleventh aspect, the present invention relates to a computer for producing a three-dimensional representation of ACE wherein said computer comprises: (a) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprises the structure co-ordinates of ACE; (b) a working memory for storing instructions for processing said computer-readable data; (c) a central-processing unit coupled to said working memory and to said computer-readable data storage medium for processing said computer-machine readable data into said three-dimensional representation; and (d) a display coupled to said central-processing unit for displaying said three-dimensional representation.
In a twelfth aspect, the present invention relates to a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data is defined by at least a portion of the structure co-ordinates of ACE in Table A or Table B.
In a thirteenth aspect, the present invention relates to the use of an ACE crystal in the preparation of a medicament to prevent and/or treat an ACE related disorder. Preferably, the ACE related disorder is hypertension.
In a fourteenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B to screen for modulators of ACE.
In a fifteenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B to solve the structure of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of ACE.
In a sixteenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B in molecular design techniques to design, select and synthesise modulators of ACE.
In a seventeenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B in the development of compounds that can isomerise to reaction intermediates in the chemical reaction of a substrate or other compound that binds to ACE.
In an eighteenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B to screen small molecule databases for chemical entities or compounds that modulate ACE.
In a nineteenth aspect, the present invention relates to the use of at least a portion of the structure co-ordinates of Table A or Table B to solve the structure of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of ACE. Preferably, the structure of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of ACE is solved using molecular replacement.
In a twentieth aspect, the present invention relates to the expression vectors pLEN-tACEΔ36g(1, 2, 3, 4) and pLEN-tACEΔ36g(1,3).
DETAILED DESCRIPTION OF THE INVENTION
ACE Protein
ACE (EC 3.4.15.1) is a peptidyldipeptide hydrolase. It catalyzes the hydrolysis of the penultimate peptide bond at the C-terminal end of a variety of acylated tripeptides and larger polypeptides having an unblocked alpha-carboxy group having a free C-terminus. The reactivity of the enzyme varies markedly depending on the substrate.
As used herein, the term “ACE protein” includes all vertebrate and mammalian forms and is intended to cover mutants, variants, homologues, derivatives and fragments thereof. Preferably, the mutants, variants, homologues, derivatives and fragments thereof have the activity of the naturally occurring ACE.
There are two isoforms of ACE that are transcribed from the same gene in a tissue specific manner. In somatic tissues, it exists as a glycoprotein composed of a single large polypeptide chain of 1277 amino acids whereas the germinal form is synthesised as a lower molecular mass isozyme and is thought to play a role in sperm maturation and the binding of sperm to the oviduct epithelium. The somatic form consists of two domains (N- and C-domain), each containing an active site with a conserved HEXXH zinc-binding motif and a glutamate some 24 residues downstream which forms the third zinc ligand (Williams et al., 1994). The two domains differ in their substrate specificities; inhibitor and chloride activation profiles; and physiological functions. There are two N-domain-specific substrates: the hemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) which controls hematopoietic stem cell differentiation and proliferation; and the bradykinin potentiating peptide angiotensin-(1-7). On the other hand, both active sites catalyse the hydrolysis of angiotensin I and the vasodilator bradykinin with similar efficiency. However, inhibition of the N-domain with a phosphinic peptide RXP407 had no effect on blood pressure regulation (Junot et al., 2001) and, furthermore, expression of the N-domain only, in transgenic mice produced a phenotype similar to the ACE knockout mice Esther et al., 1997). Thus, the C-domain appears to be necessary and sufficient for controlling blood pressure and cardiovascular function. Testis ACE (tACE) is identical to the C-terminal half of somatic ACE, except for a unique 36-residue sequence constituting its amino terminus.
Further background teachings on ACE have been presented by Victor A. McKusick et al. at http://www3.ncbi.nlm.nih.gov/Omim/searchornim.htm. The following information concerning ACE has been extracted from that source.

    
    
        Angiotensin I-converting enzyme or kininase II, is a dipeptidyl carboxypeptidase that plays an important role in blood pressure regulation and electrolyte balance by hydrolyzing angiotensin I into angiotensin II, a potent vasopressor, and aldosterone-stimulating peptide. The enzyme is also able to inactivate bradykinin, a potent vasodilator.
        Ehlers et al. (1989) Proc. Nat. Acad. Sci. 86: 7741-7745 determined the cDNA sequence for human testicular ACE. The predicted protein is identical, from residue 37 to its C terminus, to the second half or C-terminal domain of the endothelial ACE sequence. The inferred protein sequence consists of a 732-residue preprotein including a 31-residue signal peptide. The mature polypeptide has a molecular weight of 80,073.
        Howard et al. (1990) Mol. Cell. Biol. 10: 4294-4302, found that the testis-specific form of ACE has its own promoter within intron 12, is encoded by the 3-prime region of the gene, and is found only in postmeiotic spermatogenic cells and sperm.
        Although angiotensin-converting enzyme has been studied primarily in the context of its role in blood pressure regulation, this widely distributed enzyme has many other physiologic functions. The ACE gene encodes 2 isoymes. The somatic ACE isozyme is expressed in many tissues, including vascular endothelial cells, renal epithelial cells, and testicular Leydig cells, whereas the testicular or germinal ACE isozyme is expressed only in sperm Ramaraj et al., (1998) J. Clin. Invest. 102: 371-378.
        Brown et al. (1996) Clin. Pharmacol. Therapeutics 60: 8-13 found an association between the use of certain ACE inhibitors (lisinopril or enalapril vs captopril) and emergent angioedema in the African-American population of Tennessee. The adjusted relative risk of angioedema was 4.5 (95% CI, 2.9-6.8) in blacks compared to whites. The African-American patients were more severely affected: 7 of the 8 patients admitted to the intensive care unit were black, as were all patients who required intubation. African-American users of ACE inhibitors tended to be younger and female when compared to their white counterparts. The rate of angioedema was highest within the first 30 days of use (5.79 per 1000 patient-years) compared to long-term use (1.04 per 1000 patient-years).
        Large-scale trials of therapy for heart failure showed improvements in outcome with ACE inhibitors and beta-blockers. These results led to the recommendation that all patients who have heart failure accompanied by a low ejection fraction and who can tolerate ACE inhibitors and beta-blockers should be treated with both agents. Exner et al. (2001) New Eng. J. Med. 344: 1351-1357 focused on the fact that black patients with heart failure have a poorer prognosis than white patients and performed a study comparing racial groups. They found that whereas therapy with enalapril is associated with significant reduction in the risk of hospitalization for heart failure among white patients with left ventricular function, it had no such effect in similar black patients. The explanation for the lesser response to the ACE inhibitor in black patients was not clear.
        Mattei et al. (1989) Cytogenet. Cell Genet. 51: 1041 assigned the ACE gene to 17q23 by in situ hybridization. Using a DNA marker at the growth hormone gene locus, which they characterized as ‘extremely polymorphic’ and which showed no recombination with ACE, Jeunemaitre et al. (1992) Nature Genet. 1: 72-75, mapped ACE to 17q22-q24, consistent with the in situ hybridization mapping to 17q23. A demonstration of linkage between the ACE locus and elevated blood pressure in a rat model of hypertension pointed to ACE as a candidate gene in human hypertension. In studies of hypertensive families, they found no evidence to support linkage between the ACE locus and the disease, however.
        Krege et al. (1995) Nature 375: 146-148 investigated the role of the ACE gene in blood pressure control and reproduction using mice generated to carry an insertional mutation that was designed to inactivate both forms of Ace. All homozygous female mutants were found to be fertile, but the fertility of homozygous male mutants was greatly reduced. Heterozygous males but not females had blood pressures that were 15 to 20 mm Hg less than normal, although both male and female heterozygotes had reduced serum Ace activity.
        Although significant ACE activity is found in plasma, the majority of the enzyme is bound to tissue such as vascular endothelium. Esther et al. (1997), J. Clin. Invest. 99: 2375-2385, used targeted homologous recombination to create mice expressing a form of ACE that lacks the C-terminal half of the molecule. This modified ACE protein was catalytically active but entirely secreted from cells. Mice that expressed only this modified ACE had significant plasma ACE activity but no tissue-bound enzyme. These animals had low blood pressure, renal vascular thickening, and a urine-concentrating defect. The phenotype was very similar to that of completely ACE-deficient mice previously reported, except that the renal pathology was less severe. These studies strongly supported the concept that the tissue-bound ACE is essential for the control of blood pressure and the structure and function of the kidney.
        ACE gene knockout mice lack both isozymes and exhibit low blood pressure, kidney dysfunctions, and male infertility. Ramaraj et al. (1998) J. Clin. Invest. 102: 371-378, reported the use of a sperm-specific promoter and interbreeding of transgenic and gene knockout mice for generating a mouse strain that expressed ACE only in sperm. The experimental mice maintained the kidney defects of ACE −/− mice, but unlike the knockout strain, the males were fertile. Thus, Ramaraj et al. (1998) established that the role of ACE in male fertility is completely dependent on its exclusive expression in sperm. Their study demonstrated how transgenic and knockout techniques can be combined for ascribing a specific physiologic function to the expression of a multifunctional protein in a given tissue.
        Hagaman et al. (1998) Proc. Nat. Acad. Sci. 95: 2552-2557 used transgenic mice lacking somatic and testis ACE to investigate the male fertility defect They demonstrated that mice lacking both somatic and testis ACE isozymes have defects in sperm transport within the oviducts and in binding to zonae pellucidae. Males generated by gene targeting experiments that lack somatic ACE but retain testis ACE are fertile. Both male and female mice lacking angiotensinogen have normal fertility. The authors found that males heterozygous for the mutation inactivating both ACE enzymes had offspring of wildtype and heterozygous genotypes at the same frequency, suggesting that sperm carrying the mutation are not at a selective disadvantage.
    
    


Nephropathy of type I diabetes is associated with the D allele of the insertion/deletion (I/D) polymorphism in intron 16 of the ACE gene. The D allele determines higher enzyme levels. To address causality underlying this association, Huang et al. (2001) Proc. Nat. Acad. Sci. 98: 13330-13334 induced diabetes in mice having 1, 2, or 3 copies of the Ace gene, normal blood pressure, and an enzyme level range (65-162% of wildtype) comparable to that seen in humans. Twelve weeks later, the 3-copy diabetic mice had increased blood pressures and overt proteinuria. Proteinuria was correlated to plasma ACE level in the 3-copy diabetic mice. Thus, a modest genetic increase in ACE levels was sufficient to cause nephropathy in diabetic mice.
Crystal
In one aspect of the present invention, there is provided a crystal of ACE protein.
As used herein, the term “crystal” means a structure (such as a three dimensional (3D) solid aggregate) in which the plane faces intersect at definite angles and in which there is a regular structure (such as internal structure) of the constituent chemical species. Thus, the term “crystal” can include any one of: a solid physical crystal form such as an experimentally prepared crystal, a 3D model based on the crystal structure, a representation thereof—such as a schematic representation thereof, a diagrammatic representation thereof, or a data set thereof for a computer.
The crystals of the present invention may be prepared by purifying ACE protein and then crystallising the purified protein. The ACE protein may also be prepared by expressing a nucleotide sequence encoding the ACE protein in a suitable host cell.
In a preferred embodiment, the crystals of the present invention are prepared by purifying underglycosylated ACE protein and then crystallising the purified underdeglycosylated protein. The underdeglycosylated ACE protein may also be prepared by expressing a nucleotide sequence encoding the underdeglycosylated ACE protein in a suitable host cell.
ACE may be purified using various methods known to a person skilled in the art, for example, from conditioned media by affinity chromatography on a Sepharose-28-lisinopril affinity resin (Yu et al. 1997). The protein may be quantified by amino acid analysis and assayed for activity using the substrate hippuryl-L-histidyl-L-leucine, as described previously (Ehlers, M R E, Chen, Y-N, Riordan, J F (1991) Proc. Natl. Acad. Sci. USA 88, 1009-1013).
The purified ACE proteins may be stored at −20° C. in 10 mM HEPES and 0.1% PMSF.
Concentration may be performed with the aid of a filtration system and the protein concentrate may be immediately used for crystallisation purposes. The protein concentrate may be crystallised using, for example, the vapour diffusion hanging drop method at a temperature of from about 1° C. to about 30° C., preferably from about 4° C. to about 20° C., more preferably at about 16° C. The crystallisation temperature may be dependent on the additives present in the protein solution.
Typically, the best crystals for ACE proteins are grown at 16° C. by the vapour diffusion hanging drop method by mixing 2 μl of the protein solution at  ̃11.5 mg/ml in 10 mM HEPES and 0.1% PMSF with an equal volume of a reservoir solution containing 15% PEG 4000, 50 mM CH3COONa.3H2O pH 4.7 and 10 μM ZnSO4.7H2O. Crystals usually appear within 2 weeks and grow to their maximum size after about a month.
The design of ACE inhibitors has been based upon the assumption that the structure of ACE is related to that of peptidases—such as thermolysin (MA clan, M2 family) and carboxypeptidase A (MC clan, M14 family) as evidenced by comparative molecular field analysis and 3D quantitative structure-activity relationship studies of ACE (Waller & Marshall, 1993). Marshall & Cramer (1988) Trends Pharamacol. Sci. 9, 285-289 have also reported the development of predictive models for inhibitors of ACE and thermolysin. Surprisingly, the structure of ACE described herein, shows no structural homology with thermolysin but shows significant structural homology with neurolysin, a member of the M3 family of thimet oligopeptidases. Therefore, the structure presented herein, may be effectively used for the development of novel, highly selective ACE modulators with the potential for greater efficacy, fewer side effects and treatment of new indications. In addition, the unanticipated similarity with neurolysin has shown the structural conservation amongst an merging family of peptidases with a common evolutionary origin.
Without wishing to be bound by theory, it appears that the core structure of the two proteins is highly similar with different loop structures on the outer surface in the case of neurolysin. Indeed like ACE, neurolysin also belongs to the family of metallopeptidases bearing the HEXXH active site motif (Rawlings and Barrett, 1995; Brown et al., 2001). The striking similarity also extends to the active site region in neurolysin consisting of a deep narrow channel that divides the molecule into two halves. It has been speculated that using the flexible secondary structure elements in the active site cavity, the neuropeptidase can effectively cleave a variety of small peptides. Likewise in ACE, the geometry of the active site groove clearly accounts for ACE's inability to hydrolyse large, folded substrates. Furthermore, the enzyme's preference for oligopeptide substrates of about thirteen residues or less suggests that the substrate does not have the same freedom to extend outside of the channel during catalysis. Peptidases—such as thermolysin (MA clan, M4 family) and carboxypeptidase A (MC clan, M14 family)—which have been used in comparative molecular field analysis and 3D quantitative structure-activity relationship studies (Waller & Marshall, 1993) show no structural homology with ACE.
A crystal according to any one of the preceding claims comprising atoms arranged in a spatial relationship represented by at least a portion of the structure co-ordinates of Table A or Table B.
Preferably, the crystal belongs to the space group P212121 and has a unit cell with dimensions of: a=56.47 Å, b=84.90 Å, c=133.99 Å.
Preferably, the crystal is a crystal of human ACE protein.
Complexes may be obtained by growing the crystals in the presence of an entity—such as a test compound. In these experiments the protein solution is mixed with the entity and an equal volume of the reservoir solution before setting up the crystallisation. Single crystals suitable for diffraction work typically appear after about 4 weeks.
Typically, the protein comprising ACE is purified to homogeneity for crystallisation. Purity of ACE may be measured by typical techniques such as SDS-PAGE, mass spectrometry and hydrophobic HPLC.
The crystal structure of the invention may contain a portion—such as at least 25%, at least 50%, at least 75%, or preferably at least 90%, at least 95%, at least 98%, or at least 99%—of the co-ordinates listed in Table A or Table B. Preferably, the crystal structure of the invention contains all of the co-ordinates listed in Table A or Table B.
Preferably, the crystal is usable in X-ray crystallography techniques.
Preferably, the crystals used can withstand exposure to X-ray beams used to produce diffraction pattern data necessary to solve the X-ray crystallographic structure.
Preferably, prior to data collection, the crystals are flash-cooled at about 100 K in a cryoprotectant. More preferably, cryoprotectant contains 15% PEG 4000, 50 mM CH3COONa.3H2O pH 4.7, 10 μM ZnSO4.7H2O and 25% glycerol.
The X-ray data may be collected at a Synchrotron Radiation Source. Preferably, the X-ray data are collected at a Synchrotron Radiation Source at 100° K.
Preferably, the crystal has a resolution determined by X-ray crystallography of about 3.5 Å or less, more preferably a resolution of about 2.8 Å or less, more preferably, a resolution of about 2 Å or less, more preferably, a resolution of about 1.5 Å or less, most preferably, 1 Å or less.
Deglycosylation and Underglycosylated
Many proteins in eukaryotic cells are glycoproteins that contain oligosaccharide chains covalently linked to certain amino acids. Glycosylation is known to affect protein folding, localisation and trafficking, protein solubility, antigenicity, biological activity and half-life, as well as cell-cell interactions.
Protein glycosylation can be divided into four main categories mainly depending on the linkage between the amino acid and the sugar. These are N-linked glycosylation, O-linked glycosylation, C-mannosylation and GPI anchor attachments. N-glycosylation is characterised by the addition of a sugar to the amino group of an asparagine. In O-glycosylation, a sugar is attached to the hydroxyl group of a serine or threonine residue.
For N-glycosylation, the sequence motif Asn-Xaa-Ser/Thr (wherein Xaa is any amino acid other than Pro) has been defined as a prerequisite for glycosylation. Although rare, the sequence motif Asn-Xaa-Cys can also be an acceptor site. N-glycans can be subdivided into three distinct groups called ‘high mannose type’, ‘hybrid type’, and ‘complex type’, with the common pentasaccharide core—Manp(alpha1,6)-(anp(alpha1,3))-Manp(beta1,4)-GlcpNAc(beta1,4) GlcpNAc(beta1,N)-Asn—occurring in all three groups. The relationship between all three types can be ascribed to the fact that they originate from one precursor oligosaccharide which contains the described common pentasaccharide core Man3-GlcNAc2, and some additional sugar residues and the non-reducing end, and is then processed enzymatically to yield these three types. Since the hydroxyl group of Ser/Thr is thought to be involved in hydrogen bonding during the enzymatic attachment of the oligosaccharide precursor molecule to yield a favourable conformation for the action of the oligosaccharyltransferase, it has been suggested for proline that the steric hindrance might be too large (Kornfeld (1985) Ann. Rev. Biochem. 54: 631-64), preventing glycosylation at Pro containing sites. The negative influence of aspartic acid towards glycosylation can be ascribed to the negative charge on the side chain of this residue. In addition some cases have been reported where Ser/Thr is replaced by cysteine. While Ser replacement by Cys generally leads to decreased glycosylation, it has been shown (Kasturi 1995 J. Biol. Chem. 270: 14756-61) that substitution by Thr at a given potential glycosylation site can lead to increased glycosylation. This is in accordance with the model of hydrogen bonding being an important factor during the attachment of the precursor molecule to the protein. Although there are usually many potential glycosylation sites in a protein it has been estimated that glycosylation occurs only at one third of them. Mostly at those sites where the surrounding amino acids allow the formation of a beta turn.
Various glycoforms of ACE have been described. By way of example, Sadhukhan & Sen (3a) disrupted specific glycosylation sites in rabbit tACE to elucidate the glycosylation requirements for the expression and processing of active testis ACE. There are five potential N-linked glycosylation sites in the rabbit tACE sequence, with an additional six in the somatic form (4a). A null mutant, where all five sites had been disrutpted, behaved similarly to wild-type tACE expressed in the presence of the glycosylation-inhibitor, tunicamycin. It was degraded intracellularly and failed to be detected in culture medium, confirming previous findings that tACE requires N-linked glycosylation to be expressed in an active form (5a and 3a). Expression of the remaining mutants showed a preference for N-linked glycosylation at the N-terminus and that the presence of sugars at a single N-terminal site was necessary and sufficient to produce enzymatically-active tACE that was solubilised. The presence of glycosylation is not site-specific, as mutants that have either the first site or second site intact are expressed and active. However, glycosylation at the third site alone is not sufficient to produce active protein in HeLa cells, albeit this mutant was expressed in yeast (3a), indicating that the requirements for glycosylation are cell-specific.
In human testis ACE O-linked sugars are not necessary for expression, implicating the N-linked sugars in this role (6a). N-linked glycosylation of human tACE expressed in CHO cells at each site has been identified by MALDI-TOF mass spectrometry (7a). There are seven potential N-linked sites in human tACE, five of which are complementary to the sites in rabbit tACE (7a). The unique sites lie within the ectodomain (the fourth site) and in the juxtamembrane stalk region, adjacent to the cleavage site (the seventh site). As with the rabbit form, there appears to be a preference for glycosylation at the N-terminus as evidenced by MALDI-TOF mass spectrometry of glyosylation sites (7a). Inhibition of complex oligosaccharide formation using a glucosidase I inhibitor N-butyldeoxynojirimycin (NB-DNJ) led to the production of an active glycoform that was electrophoretically homogeneous (7a).
Suitably, the crystal of the ACE protein may comprise de-glycosylated ACE protein or a fragment thereof. For example, the deglycosylated ACE may comprise the sequence presented as SEQ ID No. 2.
To deglycosylate the ACE protein, various methods known to a person skilled in the art may be used. Both chemical and enzymatic methods may be used for removing oligosaccharides from glycoproteins. Hydrazinolysis of glycoproteins (Kuraya, N & Hase (1992) J Biochem (Tokyo) 112:122-126), is capable of removing both N- and O-linked sugars, although this results in the complete destruction of the protein component and is therefore not suitable if recovery of the protein is desirable. Milder chemical methods such as trifluoromethanesulphonic acid (TFMS) may be used, however this may result in incomplete sugar removal and partial protein destruction. Other methods—such as site directed mutagenesis of glycosylated amino acids may also be used.
Suitably, enzymatic methods may be used which provide for complete sugar removal with no protein degradation.
Use of the enzyme PNGase F is an effective method of removing virtually all N-linked oligosaccharides from glycoproteins (Tarentino & Plummer (1994). Methods in Enzymol 230: 44-57). The oligosaccharide is left intact and therefore suitable for further analysis (the asparagine residue from which the sugar was removed is deaminated to aspartic acid, the only modification to the protein).
Other commonly used endoglycosidases include Endoglycosidase H (Kobata (1979) Anal Biochem 100:1-14) and Endoglycosidase F (Trimble & Tarentino (1991) J. Biochem. 266:1646-1651). In a preferred method, the ACE protein is digested with Endoglycosidase H (30 mU) in a suitable buffer—such as 100 mM sodium phosphate, 0.1 mM ZnCl2 and 1% BSA, pH 6.0 for 16 h at 37° C. The endo H-treated protein is passed through a lectin affinity column consisting of equal parts of concanavalin A, wheat germ, and lentil lectin, after equilibration with 20 mM Tris-HCl, 0.5 M NaCl at pH 7.4. The deglycosylated ACE is collected in the flowthrough. Free oligosaccharides and any other impurities are removed from the flowthrough fraction by a final lisinopril-Sepharose affinity chromatography step. The homogeneity of the ACE protein after deglycosylation is confirmed by SDS-PAGE on a 4-20% acrylamide gel and MALDI-TOF mass spectrometry.
Commercially available kits may also be used—such as the E-DEGLY kit (Sigma-Aldrich, UK) and the GlycoFree Deglycosylation Kit (Glyco, Novato, USA) which removes both N- and O-linked glycans from glycoproteins.
Preferably, ACE is crystallised using underglycosylated ACE protein.
As used herein, the term “underglycosylated” means that one or more of the oligosaccharide chains covalently linked to amino acids in the glycosylated protein are no longer present.
By way of example only, testis ACE is glycosylated at amino acids 72, 90 and 109 and glycosylated partially at amino acids 155, 337 and 586. Accordingly, the “underglycosylated” testis ACE may not be glycosylated a one or more of amino acids 72, 90, 109, 155, 337 and 586.
The underglycosylated ACE protein may be prepared using various methods—such as site directed mutagenesis and glycosylation inhibition methods. For example, glycosylation inhibition methods using NB-DNJ may prevent the formation of complex oligosaccharides. NB-DNJ inhibits glucosidase I and prevents maturation of the sugars.
Preferably, the underglycosylated ACE protein is prepared by culturing host cells in the presence of N-butyldeoxynojirimycin (NB-DNJ).
Preferably, underglycosylated ACE protein is prepared using site-directed mutagenesis. More preferably, the underglycosylated ACE protein comprises a mutation at amino acid 337 of SEQ ID No. 2 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No. 2.
Underglycosylated mutants may yield crystals in the orthorhombic, P212121 space group that diffract to 2.8 Å or less. Moreover, crystals from a truncated mutant of tACE that only have simple high mannose oligosaccharides are also grown in the orthorhombic space group P212121 which may diffract to better than 2.0 Å resolution.
Preparing a Crystal of Ace Protein
In another aspect, the present invention relates to a method of preparing a crystal of ACE protein, comprising the steps of (a) culturing host cells comprising an underglycosylated ACE protein; (b) purifying the underglycosylated ACE protein; and (c) crystallising the underglycosylated ACE protein.
Preferably, the ACE protein is underglycosylated by removing one or more glycosylation sites and/or one or more partially glycosylated sites. More preferably, the underglycosylated ACE protein comprises a mutation at amino acid 337 of SEQ ID No 2 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No 2.
The ACE protein may be underglycosylated and purified using the methods described herein.
Preferably, the ACE protein is crystallised using about 10 mM HEPES and about 0.1% PMSF with an equal volume of a reservoir solution containing about 15% PEG 4000, about 50 mM CH3COONa.3H2O pH 4.7 and about 10 μM ZnSO4.7H2O.
Preferably, the ACE protein is crystallised in the presence of an entity, for example, a modulator of ACE.
Modulators of Ace
The role of ACE in the pathogenesis of hypertension has resulted in a search for modulators (eg. inhibitors) of the enzyme that could act as antihypertensive drugs (eg. U.S. Pat. No. 3,891,616, U.S. Pat. No. 3,947,575, U.S. Pat. No. 4,052,511 and U.S. Pat. No. 4,053,651). Therapeutic vasodepressors—such as Captopril and D-2-methyl-3-mercaptopropanoyl-L-proline—have been synthesised as ACE inhibitors. Numerous synthetic peptide derivatives have also been shown to be ACE inhibitors as disclosed in U.S. Pat. No. 3,832,337.
Natural substances that inhibit ACE include snake venom and those derived from foodstuffs—such as ACE inhibiting peptides produced by enzymatic hydrolysis of proteins, such as casein or fish meat protein (by Hiroyuki Ukeda, Nippon Nogei Kagaku Kaishi (Journal of Japan Society for Bioscience, Biotechnology, and Agrochemistry, 66(1), 25-29 (1992)).
ACE inhibiting synthetic substances include captopril (D-2-methyl-3-mercaptopropanoyl-L-proline) which has already been put to practical application as an orally administered vasodepressor.
However, many ACE inhibiting substances exhibit side effects in many cases and special attention needs be exercised in safety aspects.
The present invention permits the use of molecular design techniques to design, select and synthesise chemical entities and compounds, including ACE modulating compounds, capable of binding to ACE, in whole or in part.
Thus, in a further aspect, the present invention relates to a method of screening for a modulator of ACE wherein the method comprises the use of a crystal of ACE.
Preferably, the method comprises the steps of: (a) providing at least a portion of the structure co-ordinates of Table A or Table B; (b) employing at least a portion of the structure co-ordinates of Table A or Table B to design or select or synthesise a putative modulator of ACE; (c) contacting the putative modulator of ACE with ACE or a mutant, variant, homologue, derivative or fragment thereof in the presence of a substrate; and (d) screening the putative modulator of ACE in an assay for the potential to modulate ACE.
By way of example, the structure co-ordinates may be used to design compounds that bind to the enzyme and may alter the physical properties of the compounds (eg. solubility) or the enzyme itself. This invention may be used to design compounds that act as modulators—such as competitive inhibitors—of ACE by binding to all or a portion of the active site of ACE. Compounds may also be designed that act as non-competitive inhibitors of ACE. These as non-competitive inhibitors may bind to all or a portion of ACE already bound to its substrate and may be more potent and specific than known ACE inhibitors that compete only for the ACE active site. Similarly, non-competitive inhibitors that bind to and inhibit ACE whether or not it is bound to another chemical entity may be designed using the structure co-ordinates of ACE as described herein.
By way of example, it may be found that the COOH-binding active site residue differs between the N and C domain active sites and/or that it may be amenable to the incorporation of a functionality that can covalently modify this residue to produce an irreversible inhibitor design. It has long been assumed that the COOH-binding residue is a positively charged arginine (M. A. Ondetti & D. W. Cushman (1981) in Biochemical Regulation of Blood Pressure (R. L. Soffer, ed.), Wiley, New York, 165-204), but the ACE-lisinopril X-ray crystal structure described herein, shows that it is a lysine, in the case of the C-domain active site. This may present an opportunity for covalent modification, by, for example, the introduction of an alkyl halide or halo-ketone functionality into the inhibitors that can alkylate the lysine amine, or α-ketone or aldehyde that can form a Schiff's base with the lysine amine, or the use of activated ester or thioester groups, or other modified carboxyl groups susceptible to nucleophilic attack.
In a preferred embodiment, at least a portion of the structure co-ordinates of Table A or Table B and/or the putative modulator of ACE and/or the substrate are provided on a machine-readable data storage medium comprising a data storage material encoded with machine readable data.
An ACE crystal may be probed with a variety of different chemical entities or test compounds to determine optimal sites for interaction between modulators of ACE and the enzyme. For example, X-ray diffraction data collected from crystals grown in the presence of chemical entities or test compounds may allow the elucidation of how the chemical entities or test compounds interact with ACE. Molecules that bind to those sites can then be designed and synthesised and tested for their ACE modulating activity.
The present invention may also allow the development of compounds that can isomerise to reaction intermediates in the chemical reaction of a substrate or other compound that binds to ACE. Thus, the time-dependent analysis of structural changes in ACE during its interaction with other molecules may be performed. The reaction intermediates of ACE may also be deduced from the reaction product in co-complex with ACE. Such information is especially useful to design improved analogues of known ACE modulators or to design new ACE modulators based on the reaction intermediates of the ACE enzyme and ACE-modulator complex. This may provide a new route for designing ACE modulators with high specificity and stability. Preferably, this provides a new route for designing ACE modulators with high specificity, high stability and low toxicity.
Small molecule databases or test compounds may be screened for chemical entities or compounds that can bind in whole, or in part, to ACE. Thus, in a preferred embodiment, the putative ACE modulator is from a library of compounds or a database. In this screening, the quality of fit of such entities or compounds to the binding site may be judged by various methods—such as shape complementarity or estimated interaction energy (Meng, E. C. et al., J. Comp. Chem., 13, pp. 505-524 (1992)).
Because ACE protein or a mutant, variant, homologue, derivative or fragment thereof may crystallise in more than one crystal form, the structure co-ordinates of ACE, or portions thereof, may be particularly useful to solve the structure of other crystal forms of ACE. They may also be used to solve the structure of ACE mutants, ACE variants, ACE homologues, ACE derivatives, ACE fragments and ACE complexes.
Preferably, the structure co-ordinates of ACE are used to solve the structure of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of ACE. By way of example, molecular replacement may be used. In this method, the unknown crystal structure, whether it is another crystal form of ACE, an ACE mutant, an ACE variant, an ACE homologue (eg. another protein with significant amino acid sequence homology to any functional domain of ACE), an ACE derivative, an ACE fragments or an ACE co-complex may be determined using the ACE structure co-ordinates of the present invention. This method will provide a more accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.
In a preferred embodiment of the present invention, the ACE crystal further comprises an entity bound to the ACE protein or a portion thereof. For example, ACE may be crystallised in complex with an entity that is an inhibitor of ACE eg. lisinopril.
Preferably, the entity is bound to the ACE protein or a portion thereof by contacting one or more residues of the ACE protein selected from: His384, Ala385, Lys542, Tyr551, Tyr554, Glu415 and His544.
The crystal structures of a series of such complexes may then be solved by molecular replacement or in combination with MAD (Multiwavelength Anomalous Dispersion) and/or MIRAS (Multiple Isomorphous Replacement with Anomalous Scattering) procedures—and compared with that of wild-type ACE. Potential sites for modification within the binding sites of the enzyme may thus be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between ACE and a chemical entity or compound.
The structures and complexes of ACE may be refined using computer software—such as X-PLOR (Meth. Enzymol., vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985)), MLPHARE (Collaborative computational project Number 4. The CCP4 Suite: Programs for Protein Crystallography (1994) Acta Crystallogr. D 50, 760-763) and SHARP [De La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameters refinement in the MIR and MAD methods (1997) Methods Enzymol. 276, 472-494). Preferably, the complexes are refined using the program CNS (Brünger et al. (1998) Acta Crystallogr. D 54, 905-921). During the final stages of refinement water molecules, ions and inhibitor molecules may be inserted in the structure. This information may thus be used to optimise known classes of ACE modulators, eg. ACE inhibitors, and more importantly, to design and synthesise novel classes of ACE modulators.
The overall figure of merit may be improved by iterative solvent flattening, phase combination and phase extension with the program SOLOMON [Abrahams, J. P. & Leslie, A. G. W. Methods used in structure determination of bovine mitochondrial F1 ATPase. (1996) Acta Crystallogr. D 52, 110-119].
The structure co-ordinates of ACE mutants provided in this invention also facilitate the identification of related proteins or enzymes analogous to ACE in function, structure or both, thereby further leading to novel therapeutic modes for treating or preventing ACE related diseases.
The design of compounds that bind to or modulate ACE according to the present invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with ACE. Non-covalent molecular interactions important in the association of ACE with its substrate may include hydrogen bonding, van der Waals and hydrophobic interactions. Second, the compound must be able to assume a conformation that allows it to associate with ACE. Although certain portions of the compound may not directly participate in the association with ACE, those portions may still influence the overall conformation of the molecule. This may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of a binding site of ACE, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with ACE.
The potential modulating or binding effect of a chemical compound on ACE may be analysed prior to its actual synthesis and testing by the use of computer modelling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association with ACE, then synthesis and testing of the compound may be obviated. However, if computer modelling indicates a strong interaction, the molecule may be synthesised and tested for its ability to bind to ACE and modulate (eg. inhibit) using the fluorescent substrate assay of Thronberry et al. (2000) Methods Enzymol. 322, pp 100-110. In this manner, synthesis of inactive compounds may be avoided.
A modulating or other binding compound of ACE may be computationally evaluated and designed by means of a series of steps in which chemical entities or test compounds are screened and selected for their ability to associate ACE.
A person skilled in the art may use one of several methods to screen chemical entities or test compounds for their ability to associate with ACE and more particularly with the individual binding sites of ACE. This process may begin by visual inspection of, for example, the active site on the computer screen based on the ACE co-ordinates of the present invention. Selected chemical entities or test compounds may then be positioned in a variety of orientations, or docked, with ACE. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimisation and molecular dynamics with standard molecular mechanics force fields—such as CHARMM and AMBER.
Specialised computer programs may also assist in the process of selecting chemical entities or test compounds. These include but are not limited to MCSS (Miranker and Karplus (1991) Proteins: Structure, Function and Genetics, 11, pp. 29-34); GRID (Goodford (1985) J. Med. Chem., 28, pp. 849-857) and AUTODOCK (Goodsell and Olsen (1990), Proteins: Structure. Function, and Genetics, 8, pp. 195-202.
Once suitable chemical entities or test compounds have been selected, they may be assembled into a single compound—such as an ACE modulator. Assembly may proceed by visual inspection of the relationship of the chemical entities or test compounds in relation to the structure co-ordinates of ACE. This may be followed by manual model building using software—such as Quanta, Sybyl or O [Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A 47, 110-119].
Refinement of the model may be carried out using the program CNS [Brünger, A. T. et al. Crystallography & NMR System: A new software suite for macromolecular structure determination. (1998) Acta Crystallogr. D 54, 905-921].
Various programs may be used by a skilled person to connect the individual chemical entities or test compounds—such as 3D Database systems (Martin (1992) J. Med. Chem., 35, pp. 2145-2154) and CAVEAT (Bartlett et al. (1989) Royal Chem. Soc. 78, pp. 182-196).
Rather than build an ACE inhibitor one chemical entity at a time, modulating or other ACE binding compounds may be designed as a whole or de novo using either an empty binding site or optionally including some portion(s) of a known inhibitor(s). Such compounds may be designed using programs that may include but are not limited to LEGEND (Nishibata and Itai (1991) Tetrahedron, 47, p. 8985) and LUDI (Bohm (1992) J. Comp. Aid. Molec. Design, 6, pp. 61-78).
Other molecular modelling techniques may also be employed in accordance with this invention—such as those described by Cohen et al., J. Med. Chem., 33, pp. 883-894 (1990); Navia and Murcko (1992) Current Opinions in Structural Biology, 2, pp. 202-210 (1992).
Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to ACE may be computationally evaluated. Specific computer software may be used to evaluate the efficiency of binding (eg. to evaluate compound deformation energy and electrostatic interaction)—such as QUANTA/CHARMM (Accelrys Inc., USA) and Insight II/Discover (Biosym Technologies Inc., San Diego, Calif., USA). These programs may be implemented, for instance, using a suitable workstation. Other hardware systems and software packages will be known to those persons skilled in the art.
Once an ACE-modulating compound has been selected or designed, as described above, substitutions may be made (eg. in atoms or side groups) to improve or modify the binding properties. The substitutions may be conservative ie. the replacement group may have approximately the same size, shape, hydrophobicity and charge as the original group. Such substituted chemical compounds may then be analysed for efficiency of binding to ACE by the same computer methods described above.
Test compounds and modulators of ACE etc. which are identified using the crystal and the methods of the present invention may be screened in assays. Screening can be, for example in vitro, in cell culture, and/or in vivo. Biological screening assays preferably centre on activity-based response models, binding assays (which measure how well a compound binds), and bacterial, yeast and animal cell lines (which measure the biological effect of a compound in a cell). The assays can be automated for high capacity-high throughput screening (HTS) in which large numbers of compounds can be tested to identify compounds with the desired activity.
Current screening technologies are described in Handbook of Drug Screening, edited by Ramakrishna Seethala, Prabhavathi B. Fernandes. New York, N.Y., Marcel Dekker, (2001).
Ace Related Disorders
ACE related disorders include, but are not limited to, treatment of high blood pressure; treatment of heart failure; prolonging survival of patients who have had a heart attack; preventing death by heart attack and stroke in patients with vascular disease and in diabetics with other vascular risk factors; prolonging survival of patients with weak heart muscle; helping leaking heart valves; preserving kidney function in diabetics; and the treatment of new indications (e.g. polycythemia). Special groups of patients may also be treated with ACE inhibitors, including: patients with chronic pulmonary disease; patients with schleroderma; patients with atherosclerosis; and patients with hyperuricemia.
Ace Constructs
The ACE proteins produced by a host recombinant cell may be secreted or may be contained intracellularly depending on the nucleotide sequence and/or the vector used.
As will be understood by those of skill in the art, expression vectors containing an ACE encoding nucleotide sequence or a mutant, variant, homologue, derivative or fragment thereof, may be designed with signal sequences which direct secretion of the ACE coding sequences through a particular prokaryotic or eukaryotic cell membrane.
The ACE encoding sequence may be fused (eg. ligated) to nucleotide sequences encoding a polypeptide domain which will facilitate purification of soluble proteins (Kroll D J et al (1993) DNA Cell Biol 12:441-53). Preferably, the polypeptide domain which facilitates purification of soluble proteins is fused in frame with the ACE encoding sequence. Such purification facilitating domains include, but are not limited to, metal chelating peptides—such as histidine-tryptophan modules that allow purification on immobilised metals (Porath J (1992) Protein Expr Purif 3, 263-281), protein A domains that allow purification on immobilised immunoglobulin, and the domain utilised in the FLAGS extension/affinity purification system (Immunex Corp, Seattle, Wash.). The inclusion of a cleavable linker sequence such as Factor XA or enterokinase (Invitrogen, San Diego, Calif.) between the purification domain and ACE is useful to facilitate purification.
Preferably, the ACE construct is pEE-ACEΔNJ which encodes human tACE that lacks the heavily O-glycosylated, 36-residue N-terminal sequence and is truncated after Ser625, thereby lacking most of the juxtamembrane stalk as well as the transmembrane and cytoplasmic domains as described in (7a).
In another preferred embodiment, the ACE construct comprises an underglycosylated ACE, constructed by the removal of one or more glycosylation sites—such as one or more N-linked glycosylation sites. Glycosylation may be abolished using various methods known to a person skilled in the art as previously described. Preferably, a truncated form of tACE (tACEΔ36 lacking the first N-terminal 36 residues as well as the cytoplasmic domain is used for the construction of mutants (7a) and mutagenic oligonucleotides then used for altering the sites that are glycosylated. Preferably, the nucleotide sequence of each fragment is confirmed by DNA sequencing to ensure that only the desired mutation is created.
Preferably, the ACE construct comprising underglycosylated ACE is pLEN-tACEΔ36g(1, 2, 3, 4) or is pLEN-tACEΔ36g(1, 3).
Host Cells
As used herein, the term “host cell” refers to any cell that comprises nucleotide sequences that are of use in the present invention, for example, nucleotide sequences encoding ACE.
Host cells may be transformed or transfected with a nucleotide sequence contained in a vector e.g. a cloning vector. Preferably, said nucleotide sequence is carried in a vector for the replication and/or expression of the nucleotide sequence. The cells will be chosen to be compatible with the said vector and may for example be prokaryotic (for example bacterial), fungal, yeast or plant cells.
The gram-negative bacterium E. coli is widely used as a host for cloning nucleotide sequences. This organism is also widely used for heterologous nucleotide sequence expression. However, large amounts of heterologous protein tend to accumulate inside the cell. Subsequent purification of the desired protein from the bulk of E. coli intracellular proteins can sometimes be difficult.
In contrast to E. coli, bacteria from the genus Bacillus are very suitable as heterologous hosts because of their capability to secrete proteins into the culture medium. Other bacteria suitable as hosts are those from the genera Streptomyces and Pseudomonas. 
Depending on the nature of the polynucleotide and/or the desirability for further processing of the expressed protein, eukaryotic hosts including yeasts or other fungi may be preferred. In general, yeast cells are preferred over fungal cells because yeast cells are easier to manipulate. However, some proteins are either poorly secreted from the yeast cell, or in some cases are not processed properly (e.g. hyperglycosylation in yeast). In these instances, a different fungal host organism should be selected.
Examples of expression hosts are fungi—such as Aspergillus species (such as those described in EP-A-0184438 and EP-A-0284603) and Trichoderma species; bacteria—such as Bacillus species (such as those described in EP-A-0134048 and EP-A-0253455), Streptomyces species and Pseudomonas species; yeasts—such as Kluyveromyces species (such as those described in EP-A-0096430 and EP-A-0301670) and Saccharomyces species; and mammalian cells—such as CHO-K1 cells.
The use of host cells may provide for post-translational modifications (eg. glycosylation) as may be needed to confer optimal biological activity on recombinant expression products of the present invention.
Aspects of the present invention also relate to host cells comprising the ACE constructs of the present invention. The ACE constructs may comprise a nucleotide sequence for replication and expression of the sequence. The cells will be chosen to be compatible with the vector and may for example be prokaryotic (for example bacterial), fungal, yeast or plant cells.
In a preferred embodiment, the host cells are mammalian cells—such as CHO-K1 cells. CHO-K1 cells expressing ACE may be grown and maintained in accordance with Yu et al. (1997).
Nucleotide Sequences
As used herein, the term “nucleotide sequence” refers to nucleotide sequences, oligonucleotide sequences, polynucleotide sequences and variants, homologues, fragments and derivatives thereof (such as portions thereof) which comprise the nucleotide sequences encoding ACE, for example, testis ACE or somatic ACE.
The nucleotide sequence may be DNA or RNA of genomic or synthetic or recombinant origin, which may be double-stranded or single-stranded whether representing the sense or antisense strand or combinations thereof.
Preferably, the term nucleotide sequence is prepared by use of recombinant DNA techniques (e.g. recombinant DNA). The nucleotide sequences may include within them synthetic or modified nucleotides. A number of different types of modification to oligonucleotides are known in the art. These include methylphosphonate and phosphorothioate backbones, addition of acridine or polylysine chains at the 3′ and/or 5′ ends of the molecule. For the purposes of the present invention, it is to be understood that the nucleotide sequences described herein may be modified by any method available in the art.
It will be understood by a skilled person that numerous different nucleotide sequences can encode the same protein as a result of the degeneracy of the genetic code. In addition, it is to be understood that skilled persons may, using routine techniques, make nucleotide substitutions that do not substantially affect the activity encoded by the nucleotide sequence of the present invention to reflect the codon usage of any particular host organism in which the target is to be expressed. Thus, the terms “variant”, “homologue” or “derivative” in relation to nucleotide sequences include any substitution of, variation of, modification of, replacement of, deletion of or addition of one (or more) nucleic acids from or to the sequence providing the resultant nucleotide sequence encodes a functional protein according to the present invention (or even a modulator of ACE according to the present invention if said modulator comprises a nucleotide sequence or an amino acid sequence).
Amino Acid Sequences
As used herein, the term “amino acid sequence” is synonymous with the term “polypeptide” and/or the term “protein”. In some instances, the term “amino acid sequence” is synonymous with the term “peptide”. In some instances, the term “amino acid sequence” is synonymous with the term “protein”.
Aspects of the present invention concern the use of amino acid sequences, which may be available in databases. These amino acid sequences may comprise ACE proteins.
The amino acid sequence may be isolated from a suitable source, or it may be made synthetically or it may be prepared by use of recombinant DNA techniques.
Preferably, ACE comprises SEQ ID No. 1 or SEQ ID No. 2, or a mutant, variant, homologue, derivative or fragment thereof. More preferably, ACE comprises SEQ ID No. 2, or a mutant, variant, homologue, derivative or fragment thereof.
Purity
Preferably the protein solution used for crystallisation is at least 97.5% pure. More preferably, the protein solution used for crystallisation is at least 99.0% pure. Most preferably, the protein solution used for crystallisation is at least 99.5% pure.
Model
As used herein, the term “model” refers to a structural model such as a three dimensional (3D) structural model (or representation thereof) comprising ACE.
Test compounds can be modelled that bind spatially and preferentially to ACE—such as to bind spatially and preferentially to ACE—for example, the active site of ACE.
Preferably, the crystal model comprising ACE is built from all or a portion of the structure co-ordinates presented in Table A or Table B.
Mutant
As used herein, the term “mutant” refers to ACE comprising any one or more changes in the wild-type ACE sequence shown as SEQ ID No. 1 or one or more changes in the native ACE sequence shown as SEQ ID No. 2.
The term “mutant” is not limited to any of the mutations described herein which are reflected in amino acid substitutions of the amino acid residues in ACE, but may also include, but are not limited to, other deletions or insertions of nucleotides which may result in changes in the amino acid residues in the amino acid sequence of ACE.
In a preferred embodiment, mutations are located at amino acids 337 of SEQ ID No. 2 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No. 2.
The present invention also enables the solving of the crystal structure of ACE mutants. More particularly, by virtue of the present invention, the location of the active site of ACE based on its crystal structure permits the identification of desirable sites for mutation. For example, one or more mutations may be directed to a particular site—such as the active site—or combination of sites of ACE. Similarly, only a location on, at or near the enzyme surface may be replaced, resulting in an altered surface charge of one or more charge units, as compared to the wild-type enzyme. Alternatively, an amino acid residue in ACE may be chosen for replacement based on its hydrophilic or hydrophobic characteristics.
Such mutants may be characterised by any one of several different properties as compared with wild-type ACE. For example, such mutants may have altered surface charge of one or more charge units, or have an increased stability to subunit dissociation, or an altered substrate specificity in comparison with, or a higher specific activity than, wild-type ACE.
The mutants may be prepared in a number of ways that are known by a person skilled in the art. For example, mutations may be introduced by means of oligonucleotide-directed mutagenesis or other conventional methods. Alternatively, mutants of ACE may be generated by site specific replacement of a particular amino acid with an unnaturally occurring amino acid. This may be achieved by growing a host organism capable of expressing either the wild-type or mutant polypeptide on a growth medium depleted of one or more natural amino acids but enriched in one or more corresponding unnaturally occurring amino acids.
The expression, activity (eg. kinetic constants) and/or the crystallisation properties of the mutants may be determined using the methods described herein.
Variants/Homologues/Derivatives/Fragments
The ACE described herein is intended to include any polypeptide, which has the activity of the naturally occurring ACE and includes all vertebrate and mammalian forms. Such terms also include polypeptides that differ from naturally occurring forms of ACE by having amino acid deletions, substitutions, and additions, but which retain the activity of ACE.
The term “variant” is used to mean a naturally occurring polypeptide or nucleotide sequences which differs from a wild-type or a native sequence.
The term “fragment” indicates that a polypeptide or nucleotide sequence comprises a fraction of a wild-type or a native sequence. It may comprise one or more large contiguous sections of sequence or a plurality of small sections. The sequence may also comprise other elements of sequence, for example, it may be a fusion protein with another protein. Preferably the sequence comprises at least 50%, more preferably at least 65%, more preferably at least 80%, most preferably at least 90% of the wild-type sequence.
The present invention also encompasses the use of variants, homologues and derivatives of nucleotide and amino acid sequences. Here, the term “homologue” means an entity having a certain homology with amino acid sequences or nucleotide sequences. Here, the term “homology” can be equated with “identity”.
In the present context, an homologous sequence is taken to include an amino acid sequence which may be at least 75, 85 or 90% identical, preferably at least 95 or 98% identical to the subject sequence—such as ACE or a functional domain thereof.
Although homology can also be considered in terms of similarity (i.e. amino acid residues having similar chemical properties/functions), it is preferred to express homology in terms of sequence identity.
A significantly homologous amino acid sequence is taken to include an amino acid sequence which may be at least 75, 85 or 90% identical, preferably at least 95 or 98% identical to the subject sequence—such as ACE or a functional domain thereof.
An homologous sequence is taken to include a nucleotide sequence which may be at least 75, 85 or 90% identical, preferably at least 95 or 98% identical to the subject sequence—such as ACE or a functional domain thereof.
Homology comparisons can be conducted by eye, or more usually, with the aid of readily available sequence comparison programs. These commercially available computer programs can calculate % homology between two or more sequences.
% homology may be calculated over contiguous sequences, i.e. one sequence is aligned with the other sequence and each amino acid in one sequence is directly compared with the corresponding amino acid in the other sequence, one residue at a time. This is called an “ungapped” alignment. Typically, such ungapped alignments are performed only over a relatively short number of residues.
Although this is a very simple and consistent method, it fails to take into consideration that, for example, in an otherwise identical pair of sequences, one insertion or deletion will cause the following amino acid residues to be put out of alignment, thus potentially resulting in a large reduction in % homology when a global alignment is performed. Consequently, most sequence comparison methods are designed to produce optimal alignments that take into consideration possible insertions and deletions without penalising unduly the overall homology score. This is achieved by inserting “gaps” in the sequence alignment to try to maximise local homology.
However, these more complex methods assign “gap penalties” to each gap that occurs in the alignment so that, for the same number of identical amino acids, a sequence alignment with as few gaps as possible—reflecting higher relatedness between the two compared sequences—will achieve a higher score than one with many gaps. “Affine gap costs” are typically used that charge a relatively high cost for the existence of a gap and a smaller penalty for each subsequent residue in the gap. This is the most commonly used gap scoring system. High gap penalties will of course produce optimised alignments with fewer gaps. Most alignment programs allow the gap penalties to be modified. However, it is preferred to use the default values when using such software for sequence comparisons. For example when using the GCG Wisconsin Bestfit package the default gap penalty for amino acid sequences is −12 for a gap and −4 for each extension.
Calculation of maximum % homology therefore firstly requires the production of an optimal alignment, taking into consideration gap penalties. A suitable computer program for carrying out such an alignment is the GCG Wisconsin Bestfit package (University of Wisconsin, U.S.A.; Devereux et al., 1984, Nucleic Acids Research 12:387). Examples of other software than can perform sequence comparisons include, but are not limited to, the BLAST package (see Ausubel et al., 1999 ibid—Chapter 18), FASTA (Atschul et al., 1990, J. Mol. Biol., 403-410) and the GENEWORKS suite of comparison tools. Both BLAST and FASTA are available for offline and online searching (see Ausubel et al., 1999 ibid, pages 7-58 to 7-60). However, for some applications, it is preferred to use the GCG Bestfit program. A new tool, called BLAST 2 Sequences is also available for comparing protein and nucleotide sequence (see FEMS Microbiol Left 1999 174(2): 247-50; FEMS Microbiol Lett 1999 177(1): 187-8)
Although the final % homology can be measured in terms of identity, the alignment process itself is typically not based on an all-or-nothing pair comparison. Instead, a scaled similarity score matrix is generally used that assigns scores to each pairwise comparison based on chemical similarity or evolutionary distance. An example of such a matrix commonly used is the BLOSUM62 matrix—the default matrix for the BLAST suite of programs. GCG Wisconsin programs generally use either the public default values or a custom symbol comparison table if supplied (see user manual for further details). For some applications, it is preferred to use the public default values for the GCG package, or in the case of other software, the default matrix, such as BLOSUM62.
Once the software has produced an optimal alignment, it is possible to calculate % homology, preferably % sequence identity. The software typically does this as part of the sequence comparison and generates a numerical result.
By way of example, homologous sequences of ACE include, but are not limited to human ACES somatic ACE (accession number: J04144), human ACET testis ACE (accession number: M26657), human ACEH/ACE2 (accession numbers: AAF78220; BAB40370; AAF99721), chimp ACET (accession number: AF193487—2), rabbit ACET mature protein (accession number: P22968), rabbit ACET full pre-protein (accession number: P22968), mouse ACET testis ACE (accession number: P22967), bovine Cdom ACES C-domain, rat Cdom ACES C-domain (derived from accession number P47820; starting D616), human Ndom ACES N-domain (derived from accession number P12821 (J04144)), chimp Ndom ACES N-domain (derived from accession number AF193487—1), rabbit Ndom ACES N-domain (derived from P12822), bovine Ndom (Bovine {Bos taurus} ACES N-domain), mouse Ndom ACES N-domain (derived from accession number P09470), rat Ndom ACES N-domain (derived from accession number P47820), chick ACE (partial ACE accession number Q10751), dros AnCE (derived from accession number Q10714), dros ACEr (derived from accession number X96913), buffalo fly ACE (derived from accession number Q10715), and silkworm ACE (derived from accession number BAA97657), tick ACE (derived from accession number U62809).
The sequences may also have deletions, insertions or substitutions of amino acid residues, which produce a silent change and result in a functionally equivalent substance. Deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues as long as the secondary binding activity of the substance is retained. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; and amino acids with uncharged polar head groups having similar hydrophilicity values include leucine, isoleucine, valine, glycine, alanine, asparagine, glutamine, serine, threonine, phenylalanine, and tyrosine.
Conservative substitutions may be made, for example according to the Table below. Amino acids in the same block in the second column and preferably in the same line in the third column may be substituted for each other:

















ALIPHATIC
Non-polar
G A P





I L V




Polar - uncharged
C S T M





N Q




Polar - charged
D E





K R



AROMATIC

H F W Y










Homologous substitution (substitution and replacement are both used herein to mean the interchange of an existing amino acid residue, with an alternative residue) may occur i.e. like-for-like substitution such as basic for basic, acidic for acidic, polar for polar etc. Non-homologous substitution may also occur i.e. from one class of residue to another or alternatively involving the inclusion of unnatural amino acids such as ornithine (hereinafter referred to as Z), diaminobutyric acid ornithine (hereinafter referred to as B), norleucine omithine (hereinafter referred to as O), pyriylalanine, thienylalanine, naphthylalanine and phenylglycine.
Replacements may also be made by unnatural amino acids include; alpha* and alpha-disubstituted* amino acids, N-alkyl amino acids*, lactic acid*, halide derivatives of natural amino acids such as trifluorotyrosine*, p-Cl-phenylalanine*, p-Br-phenylalanine*, p-I-phenylalanine*, L-allyl-glycine*, β-alanine*, L-α-amino butyric acid*, L-γ-amino butyric acid*, L-α-amino isobutyric acid*, L-ε-amino caproic acid#, 7-amino heptanoic acid*, L-methionine sulfone#*, L-norleucine*, L-norvaline*, p-nitro-L-phenylalanine*, L-hydroxyproline#, L-thioproline*, methyl derivatives of phenylalanine (Phe) such as 4-methyl-Phe*, pentamethyl-Phe*, L-Phe (4-amino)#, L-Tyr (methyl)*, L-Phe (4-isopropyl)*, L-Tic (1,2,3,4-tetrahydroisoquinoline-3-carboxyl acid)*, L-diaminopropionic acid# and L-Phe (4-benzyl)*. The notation * has been utilised for the purpose of the discussion above (relating to homologous or non-homologous substitution), to indicate the hydrophobic nature of the derivative whereas # has been utilised to indicate the hydrophilic nature of the derivative, #* indicates amphipathic characteristics.
The term “derivative” or “derivatised” as used herein includes chemical modification of an entity—such as test compound or an ACE modulator. Illustrative of such chemical modifications would be replacement of hydrogen by a halo group, an alkyl group, an acyl group or an amino group.
Variant amino acid sequences may include suitable spacer groups that may be inserted between any two amino acid residues of the sequence including alkyl groups such as methyl, ethyl or propyl groups in addition to amino acid spacers such as glycine or β-alanine residues. A further form of variation, involves the presence of one or more amino acid residues in peptoid form, will be well understood by those skilled in the art. For the avoidance of doubt, “the peptoid form” is used to refer to variant amino acid residues wherein the α-carbon substituent group is on the residue's nitrogen atom rather than the α-carbon. Processes for preparing peptides in the peptoid form are known in the art, for example Simon R J et al., PNAS (1992) 89(20), 9367-9371 and Horwell D C, Trends Biotechnol. (1995) 13(4), 132-134.
Test Compounds
As used herein, the term “test compound” includes, but is not limited to, a compound which may be obtainable from or produced by any suitable source, whether natural or not.
The test compound may be designed or obtained from a library of compounds, which may comprise peptides, as well as other compounds, such as small organic molecules and particularly new lead compounds. By way of example, the test compound may be a natural substance, a biological macromolecule, or an extract made from biological materials—such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic test compound, a semi-synthetic test compound, a structural or functional mimetic, a peptide, a peptidomimetics, a derivatised test compound, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesiser or by recombinant techniques or combinations thereof, a recombinant test compound, a natural or a non-natural test compound, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof The test compound may even be a compound that is a modulator of ACE—such as a known inhibitor of ACE—that has been modified in some way eg. by recombinant DNA techniques or chemical synthesis techniques.
Typically, the test compound will be prepared by recombinant DNA techniques and/or chemical synthesis techniques.
Once a test compound capable of interacting ACE has been identified, further steps may be carried out to select and/or to modify the test compounds and/or to modify existing compounds, such that they are able to modulate ACE.
Modulating Ace
As herein, the term “modulating” refers to preventing, suppressing, inhibiting, alleviating, restorating, elevating, increasing or otherwise affecting ACE.
The term “ACE modulator” may refer to a single entity or a combination of entities.
The ACE modulator may be an antagonist or an agonist of ACE.
As used herein, the term “agonist” means any entity, which is capable of interacting (eg. binding) with ACE and which is capable of increasing a proportion of the ACE that is in an active form, resulting in an increased biological response.
As used herein, the term “antagonist” means any entity, which is capable of interacting (eg. binding) with ACE and which is capable of decreasing (eg. inhibiting) a proportion of the ACE that is in an active form, resulting in a decreased biological response.
Preferably, the ACE modulators of the present invention are antagonists of ACE.
The modulator of ACE may be an organic compound or other chemical. The modulator of ACE may be a compound, which is obtainable from or produced by any suitable source, whether natural or artificial. The modulator of ACE may be an amino acid molecule, a polypeptide, or a chemical derivative thereof, or a combination thereof. The modulator of ACE may even be a polynucleotide molecule—which may be a sense or an anti-sense molecule. The modulator of ACE may even be an antibody.
The modulator of ACE may be designed or obtained from a library of compounds, which may comprise peptides, as well as other compounds, such as small organic molecules.
By way of example, the modulator of ACE may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic agent, a semi-synthetic agent, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised agent, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesiser or by recombinant techniques or combinations thereof, a recombinant agent, an antibody, a natural or a non-natural agent, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof).
Typically, the modulator of ACE will be an organic compound. Typically, the organic compounds will comprise two or more hydrocarbyl groups. Here, the term “hydrocarbyl group” means a group comprising at least C and H and may optionally comprise one or more other suitable substituents. Examples of such substituents may include halo-, alkoxy-, nitro-, an alkyl group, a cyclic group etc. In addition to the possibility of the substituents being a cyclic group, a combination of substituents may form a cyclic group. If the hydrocarbyl group comprises more than one C then those carbons need not necessarily be linked to each other. For example, at least two of the carbons may be linked via a suitable element or group. Thus, the hydrocarbyl group may contain hetero atoms. Suitable hetero atoms will be apparent to those skilled in the art and include, for instance, sulphur, nitrogen and oxygen. For some applications, preferably the modulator of ACE comprises at least one cyclic group. The cyclic group may be a polycyclic group, such as a non-fused polycyclic group. For some applications, the modulator of ACE comprises at least the one of said cyclic groups linked to another hydrocarbyl group.
The modulator of ACE may contain halo groups, for example, fluoro, chloro, bromo or iodo groups.
The modulator of ACE may contain one or more of alkyl, alkoxy, alkenyl, alkylene and alkenylene groups—which may be unbranched- or branched-chain.
The modulator of ACE may be in the form of a pharmaceutically acceptable salt—such as an acid addition salt or a base salt—or a solvate thereof, including a hydrate thereof. For a review on suitable salts see Berge et al, (1977) J. Pharm. Sci. 66, 1-19.
The modulator of ACE may be structurally novel modulators of ACE.
The modulators of ACE may be analogues of known modulators of ACE—such as known inhibitors of ACE (for example, snake venom, peptides produced by enzymatic hydrolysis of casein or fish meat protein, or Benazepril, Captopril, Cilazapril, Enalapril, Fosinopril, Lisinopril, Moexipril, Perindopril, Quinapril, Ramipril, Trandolapril and Enalaprilat.
Preferably, the ACE modulators have improved properties over those previously available, for example, fewer side effects—such as cough (eg. dry, persistent); fever and chills; hoarseness; swelling of face, mouth, hands, or feet; trouble in swallowing or breathing; itching of skin; yellow eyes or skin; dizziness, light-headedness, or fainting; skin rash, with or without itching; fever, or joint pain; abdominal pain, abdominal distention; nausea, or vomiting; chest pain, confusion; irregular heartbeat; nervousness; numbness or tingling in hands, feet, or lips; weakness or heaviness of legs; headache, diarrhoea; loss of taste; nausea; unusual tiredness.
The modulator of ACE may be a mimetic.
The modulator of ACE may also be chemically modified.
The modulator of ACE may be capable of displaying other therapeutic properties.
The modulator of ACE may be used in combination with one or more other pharmaceutically active agents.
If combinations of active agents are administered, then they may be administered simultaneously, separately or sequentially.
Mimetic
As used herein, the term “mimetic” relates to any chemical which includes, but is not limited to, a peptide, polypeptide, antibody or other organic chemical which has the same qualitative activity or effect as a known compound. That is, the mimetic is a functional equivalent of a known compound.
Stereo and Geometric Isomers
Modulators of ACE may exist as stereoisomers and/or geometric isomers—e.g. they may possess one or more asymmetric and/or geometric centres and so may exist in two or more stereoisomeric and/or geometric forms. The present invention contemplates the use of all the individual stereoisomers and geometric isomers, and mixtures thereof.
Pharmaceutical Salt
Modulators of ACE may be administered in the form of a pharmaceutically acceptable salt.
Pharmaceutically-acceptable salts are well known to those skilled in the art, and for example include those mentioned by Berge et al, (1977) J. Pharm. Sci., 66, 1-19. Suitable acid addition salts are formed from acids which form non-toxic salts and include the hydrochloride, hydrobromide, hydroiodide, nitrate, sulphate, bisulphate, phosphate, hydrogenphosphate, acetate, trifluoroacetate, gluconate, lactate, salicylate, citrate, tartrate, ascorbate, succinate, maleate, fumarate, gluconate, formate, benzoate, methanesulphonate, ethanesulphonate, benzenesulphonate and p-toluenesulphonate salts.
When one or more acidic moieties are present, suitable pharmaceutically acceptable base addition salts can be formed from bases which form non-toxic salts and include the aluminium, calcium, lithium, magnesium, potassium, sodium, zinc, and pharmaceutically-active amines such as diethanolamine, salts.
A pharmaceutically acceptable salt of a modulator of ACE may be readily prepared by mixing together solutions of the modulator of ACE and the desired acid or base, as appropriate. The salt may precipitate from solution and be collected by filtration or may be recovered by evaporation of the solvent.
The modulator of ACE may exist in polymorphic form.
The modulator of ACE may contain one or more asymmetric carbon atoms and therefore exists in two or more stereoisomeric forms. Where a modulator of ACE contains an alkenyl or alkenylene group, cis (E) and trans (Z) isomerism may also occur. The present invention includes the individual stereoisomers of the modulator of ACE and, where appropriate, the individual tautomeric forms thereof, together with mixtures thereof.
Separation of diastereoisomers or cis and trans isomers may be achieved by conventional techniques, e.g. by fractional crystallisation, chromatography or H.P.L.C. of a stereoisomeric mixture of the modulator of ACE or a suitable salt or derivative thereof An individual enantiomer of the modulator of ACE may also be prepared from a corresponding optically pure intermediate or by resolution, such as by H.P.L.C. of the corresponding racemate using a suitable chiral support or by fractional crystallisation of the diastereoisomeric salts formed by reaction of the corresponding racemate with a suitable optically active acid or base, as appropriate.
The modulator of ACE may also include all suitable isotopic variations of the modulator of ACE or a pharmaceutically acceptable salt thereof. An isotopic variation of an modulator of ACE or a pharmaceutically acceptable salt thereof is defined as one in which at least one atom is replaced by an atom having the same atomic number but an atomic mass different from the atomic mass usually found in nature. Examples of isotopes that can be incorporated into the modulator of ACE and pharmaceutically acceptable salts thereof include isotopes of hydrogen, carbon, nitrogen, oxygen, phosphorus, sulphur, fluorine and chlorine such as 2H, 3H, 13C, 14C, 15N, 17O, 18O, 31P, 32P, 35S, 18F and 36Cl, respectively. Certain isotopic variations of the modulator of ACE and pharmaceutically acceptable salts thereof, for example, those in which a radioactive isotope such as 3H or 14C is incorporated, are useful in drug and/or substrate tissue distribution studies. Tritiated, i.e., 3H, and carbon-14, i.e., 14C, isotopes are particularly preferred for their ease of preparation and detectability. Further, substitution with isotopes such as deuterium, i.e., 2H, may afford certain therapeutic advantages resulting from greater metabolic stability, for example, increased in vivo half-life or reduced dosage requirements and hence may be preferred in some circumstances. Isotopic variations of the modulator of ACE and pharmaceutically acceptable salts thereof of this invention can generally be prepared by conventional procedures using appropriate isotopic variations of suitable reagents.
It will be appreciated by those skilled in the art that the agent may be derived from a prodrug. Examples of prodrugs include entities that have certain protected group(s) and which may not possess pharmacological activity as such, but may, in certain instances, be administered (such as orally or parenterally) and thereafter metabolised in the body to form the modulator of ACE which is pharmacologically active.
It will be further appreciated that certain moieties known as “pro-moieties”, for example as described in “Design of Prodrugs” by H. Bundgaard, Elsevier, 1985 (the disclosured of which is hereby incorporated by reference), may be placed on appropriate functionalities of the modulator of ACE. Such prodrugs are also included within the scope of the invention.
Pharmaceutically Active Salt
The modulator of ACE may be administered as a pharmaceutically acceptable salt. Typically, a pharmaceutically acceptable salt may be readily prepared by using a desired acid or base, as appropriate. The salt may precipitate from solution and be collected by filtration or may be recovered by evaporation of the solvent.
Chemical Synthesis Methods
The modulator of ACE of the present invention may be prepared by chemical synthesis techniques.
It will be apparent to those skilled in the art that sensitive functional groups may need to be protected and deprotected during synthesis of a compound of the invention. This may be achieved by conventional techniques, for example as described in “Protective Groups in Organic Synthesis” by T W Greene and P G M Wuts, John Wiley and Sons Inc. (1991), and by P. J. Kocienski, in “Protecting Groups”, Georg Thieme Verlag (1994).
It is possible during some of the reactions that any stereocentres present could, under certain conditions, be racemised, for example if a base is used in a reaction with a substrate having an having an optical centre comprising a base-sensitive group. This is possible during e.g. a guanylation step. It should be possible to circumvent potential problems such as this by choice of reaction sequence, conditions, reagents, protection/deprotection regimes, etc. as is well-known in the art.
The compounds and salts may be separated and purified by conventional methods.
Separation of diastereomers may be achieved by conventional techniques, e.g. by fractional crystallisation, chromatography or H.P.L.C. of a stereoisomeric mixture of a compound of formula (I) or a suitable salt or derivative thereof. An individual enantiomer of a compound of formula (I) may also be prepared from a corresponding optically pure intermediate or by resolution, such as by H.P.L.C. of the corresponding racemate using a suitable chiral support or by fractional crystallisation of the diastereomeric salts formed by reaction of the corresponding racemate with a suitably optically active acid or base.
ACE, modulators of ACE or variants, homologues, derivatives, fragments or mimetics thereof may be produced using chemical methods to synthesise the ACE or the modulator of ACE in whole or in part. For example, a ACE peptide or a modulator of ACE that is a peptide can be synthesised by solid phase techniques, cleaved from the resin, and purified by preparative high performance liquid chromatography (e.g., Creighton (1983) Proteins Structures And Molecular Principles, WH Freeman and Co, New York N.Y.). The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure; Creighton, supra).
Synthesis of peptides (or variants, homologues, derivatives, fragments or mimetics thereof) may be performed using various solid-phase techniques (Roberge J Y et al (1995) Science 269: 202-204) and automated synthesis may be achieved, for example, using the ABI 43 1 A Peptide Synthesizer (Perkin Elmer) in accordance with the instructions provided by the manufacturer. Additionally, the amino acid sequences comprising the modulator of ACE, may be altered during direct synthesis and/or combined using chemical methods with a sequence from other subunits, or any part thereof, to produce a variant modulator of ACE.
Chemical Modification
The modulator of ACE may be a chemically modified modulator of ACE.
The chemical modification of a modulator of ACE may either enhance or reduce interactions between the modulator of ACE and the target—such as hydrogen bonding interactions, charge interactions, hydrophobic interactions, van der Waals interactions or dipole interactions.
In one aspect, the modulator of ACE may act as a model (for example, a template) for the development of other compounds.
Pharmaceutical Compositions
The components may be administered alone but will generally be administered as a pharmaceutical composition—e.g. when the components are in a mixture with a suitable pharmaceutical excipient, diluent or carrier selected with regard to the intended route of administration and standard pharmaceutical practice.
For example, the components can be administered in the form of tablets, capsules, ovules, elixirs, solutions or suspensions, which may contain flavouring or colouring agents, for immediate-, delayed-, modified-, sustained-, pulsed- or controlled-release applications.
If the pharmaceutical is a tablet, then the tablet may contain excipients such as microcrystalline cellulose, lactose, sodium citrate, calcium carbonate, dibasic calcium phosphate and glycine, disintegrants such as starch (preferably corn, potato or tapioca starch), sodium starch glycollate, croscarmellose sodium and certain complex silicates, and granulation binders—such as polyvinylpyrrolidone, hydroxypropylmethylcellulose (HPMC), hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally, lubricating agents—such as magnesium stearate, stearic acid, glyceryl behenate and talc may be included.
Solid compositions of a similar type may also be employed as fillers in gelatin capsules. Preferred excipients in this regard include lactose, starch, a cellulose, milk sugar or high molecular weight polyethylene glycols. For aqueous suspensions and/or elixirs, the modulator of ACE may be combined with various sweetening or flavouring agents, colouring matter or dyes, with emulsifying and/or suspending agents and with diluents such as water, ethanol, propylene glycol and glycerin, and combinations thereof.
The routes for administration (delivery) may include, but are not limited to, one or more of oral (e.g. as a tablet, capsule, or as an ingestable solution), topical, mucosal (e.g. as a nasal spray or aerosol for inhalation), nasal, parenteral (e.g. by an injectable form), gastrointestinal, intraspinal, intraperitoneal, intramuscular, intravenous, intraventricular, intrauterine, intraocular, intradermal, intracranial, intratracheal, intravaginal, intracerebroventricular, intracerebral, subcutaneous, ophthalmic (including intravitreal or intracameral), transdermal, rectal, buccal, vaginal, epidural, sublingual.
Pharmaceutical compositions of the present invention may comprise a therapeutically effective amount of ACE, one or more modulators of ACE or combinations thereof.
The pharmaceutical compositions may be for human or animal usage in human and veterinary medicine and will typically comprise any one or more of a pharmaceutically acceptable diluent, carrier, or excipient. Acceptable carriers or diluents for therapeutic use are well known in the pharmaceutical art, and are described, for example, in Remington's Pharmaceutical Sciences, Mack Publishing Co. (A. R. Gennaro edit. 1985). The choice of pharmaceutical carrier, excipient or diluent can be selected with regard to the intended route of administration and standard pharmaceutical practice. The pharmaceutical compositions may comprise as—or in addition to—the carrier, excipient or diluent any suitable binder(s), lubricant(s), suspending agent(s), coating agent(s), solubilising agent(s).
Preservatives, stabilizers, dyes and even flavouring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid and esters of p-hydroxybenzoic acid. Antioxidants and suspending agents may be also used.
There may be different composition/formulation requirements dependent on the different delivery systems. By way of example, the pharmaceutical composition of the present invention may be formulated to be administered using a mini-pump or by a mucosal route, for example, as a nasal spray or aerosol for inhalation or ingestable solution, or parenterally in which the composition is formulated by an injectable form, for delivery, by, for example, an intravenous, intramuscular or subcutaneous route.
Alternatively, the formulation may be designed to be administered by a number of routes.
If the modulator of ACE is to be administered mucosally through the gastrointestinal mucosa, it should be able to remain stable during transit though the gastrointestinal tract; for example, it should be resistant to proteolytic degradation, stable at acid pH and resistant to the detergent effects of bile.
Where appropriate, the pharmaceutical compositions may be administered by inhalation, in the form of a suppository or pessary, topically in the form of a lotion, solution, cream, ointment or dusting powder, by use of a skin patch, orally in the form of tablets containing excipients such as starch or lactose, or in capsules or ovules either alone or in admixture with excipients, or in the form of elixirs, solutions or suspensions containing flavouring or colouring agents, or the pharmaceutical compositions can be injected parenterally, for example intravenously, intramuscularly or subcutaneously. For parenteral administration, the compositions may be best used in the form of a sterile aqueous solution which may contain other substances, for example enough salts or monosaccharides to make the solution isotonic with blood. For buccal or sublingual administration the compositions may be administered in the form of tablets or lozenges which can be formulated in a conventional manner.
The modulators of ACE may be used in combination with a cyclodextrin. Cyclodextrins are known to form inclusion and non-inclusion complexes with drug molecules. Formation of a drug-cyclodextrin complex may modify the solubility, dissolution rate, bioavailability and/or stability property of a drug molecule. Drug-cyclodextrin complexes are generally useful for most dosage forms and administration routes. As an alternative to direct complexation with the drug the cyclodextrin may be used as an auxiliary additive, e.g. as a carrier, diluent or solubiliser. Alpha-, beta- and gamma-cyclodextrins are most commonly used and suitable examples are described in WO-A-91/11172, WO-A-94/02518 and WO-A-98/55148.
If the modulator of ACE is a protein, then said protein may be prepared in situ in the subject being treated. In this respect, nucleotide sequences encoding said protein may be delivered by use of non-viral techniques (e.g. by use of liposomes) and/or viral techniques (e.g. by use of retroviral vectors) such that the said protein is expressed from said nucleotide sequence.
Dose Levels
Typically, a physician will determine the actual dosage which will be most suitable for an individual subject. The specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability and length of action of that compound, the age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the individual undergoing therapy.
Formulation
The component(s) may be formulated into a pharmaceutical composition, such as by mixing with one or more of a suitable carrier, diluent or excipient, by using techniques that are known in the art.
Vector
Aspects of the present invention relate to a vector comprising a nucleotide sequence—such as a nucleotide sequence encoding ACE or a modulator of ACE—administered to a subject.
Preferably, ACE or the modulator of ACE is prepared and/or delivered using a genetic vector.
As it is well known in the art, a vector is a tool that allows or facilitates the transfer of an entity from one environment to another. In accordance with the present invention, and by way of example, some vectors used in recombinant DNA techniques allow entities, such as a segment of DNA (such as a heterologous DNA segment, such as a heterologous cDNA segment), to be transferred into a host and/or a target cell for the purpose of replicating the vectors comprising nucleotide sequences and/or expressing the proteins encoded by the nucleotide sequences. Examples of vectors used in recombinant DNA techniques include, but are not limited to, plasmids, chromosomes, artificial chromosomes or viruses.
The term “vector” includes expression vectors and/or transformation vectors.
The term “expression vector” means a construct capable of in vivo or in vitrolex vivo expression.
The term “transformation vector” means a construct capable of being transferred from one species to another.
Regulatory Sequences
In some applications, nucleotide sequences are operably linked to a regulatory sequence which is capable of providing for the expression of the nucleotide sequence, such as by a chosen host cell. By way of example, a vector comprising the ACE nucleotide sequence is operably linked to such a regulatory sequence i.e. the vector is an expression vector.
The term “operably linked” refers to a juxtaposition wherein the components described are in a relationship permitting them to function in their intended manner. A regulatory sequence “operably linked” to a coding sequence is ligated in such a way that expression of the coding sequence is achieved under conditions compatible with the control sequences.
The term “regulatory sequences” includes promoters and enhancers and other expression regulation signals.
The term “promoter” is used in the normal sense of the art, e.g. an RNA polymerase binding site.
Enhanced expression of a nucleotide sequence, for example, a nucleotide sequence encoding ACE—may also be achieved by the selection of heterologous regulatory regions, e.g. promoter, secretion leader and terminator regions, which serve to increase expression and, if desired, secretion levels of the protein of interest from the chosen expression host and/or to provide for the inducible control of the expression of ACE. In eukaryotes, polyadenylation sequences may be operably connected to the ACE nucleotide sequence.
Preferably, the ACE nucleotide sequence is operably linked to at least a promoter.
Aside from the promoter native to the gene encoding the ACE nucleotide sequence, other promoters may be used to direct expression of the ACE polypeptide. The promoter may be selected for its efficiency in directing the expression of the ACE nucleotide sequence in the desired expression host.
In another embodiment, a constitutive promoter may be selected to direct the expression of the ACE nucleotide sequence of the present invention. Such an expression construct may provide additional advantages since it circumvents the need to culture the expression hosts on a medium containing an inducing substrate.
Hybrid promoters may also be used to improve inducible regulation of the expression construct.
The promoter can additionally include features to ensure or to increase expression in a suitable host. For example, the features can be conserved regions such as a Pribnow Box or a TATA box. The promoter may even contain other sequences to affect (such as to maintain, enhance, decrease) the levels of expression of the ACE nucleotide sequence. For example, suitable other sequences include the Sh1-intron or an ADH intron. Other sequences include inducible elements—such as temperature, chemical, light or stress inducible elements. Also, suitable elements to enhance transcription or translation may be present.
Expression Vector
Preferably, nucleotide sequences—such as nucleotide sequences encoding ACE or modulators of ACE—are inserted into a vector that is operably linked to a control sequence that is capable of providing for the expression of the coding sequence by the host cell.
Nucleotide sequences produced by a host recombinant cell may be secreted or may be contained intracellularly depending on the sequence and/or the vector used. As will be understood by those of skill in the art, expression vectors can be designed with signal sequences, which direct secretion of the nucleotide sequence through a particular prokaryotic or eukaryotic cell membrane.
The expression vector may be pEE-tACEΔ36NJ which encodes human tACE that lacks the heavily O-glycosylated, 36-residue N-terminal sequence and is truncated after Ser625, thereby lacking most of the juxtamembrane stalk as well as the transmembrane and cytoplasmic domains.
In a preferred aspect, the expression vector is pLEN-tACEΔ36g(n), where n is a set of numbers defining the available N-linked glycosylation sites.
Preferably, the expression vectors are stably expressed in CHO cells as described previously (Ehlers et al. (1996) Biochemistry 35, 9549-9559). More preferably, the expression vectors are pLEN-tACEΔ36g(1, 2, 3, 4) and pLEN-tACEΔ36g(1,3).
Fusion Proteins
ACE or a modulator of ACE may be expressed as a fusion protein to aid extraction and purification and/or delivery of the modulator of ACE or the ACE protein to an individual and/or to facilitate the development of a screen for modulators of ACE.
Examples of fusion protein partners include glutathione-S-transferase (GST), 6×His, GAL4 (DNA binding and/or transcriptional activation domains) and β-galactosidase.
It may also be convenient to include a proteolytic cleavage site between the fusion protein partner and the protein sequence of interest to allow removal of fusion protein sequences. Preferably, the fusion protein will not hinder the activity of the protein of interest.
The fusion protein may comprise an antigen or an antigenic determinant fused to the substance of the present invention. In this embodiment, the fusion protein may be a non-naturally occurring fusion protein comprising a substance, which may act as an adjuvant in the sense of providing a generalised stimulation of the immune system. The antigen or antigenic determinant may be attached to either the amino or carboxy terminus of the substance.
Organism
The term “organism” in relation to the present invention includes any organism that could comprise ACE and/or modulators of ACE. Examples of organisms may include mammals, fungi, yeast or plants.
Preferably, the organism is a mammal. More preferably, the organism is a human.
Transformation
As indicated earlier, the host organism can be a prokaryotic or a eukaryotic organism. Examples of suitable prokaryotic hosts include E. coli and Bacillus subtilis. Teachings on the transformation of prokaryotic hosts are well documented in the art, for example see Sambrook et al Molecular Cloning: A Laboratory Manual, 2nd edition, 1989, Cold Spring Harbor Laboratory Press) and Ausubel et al., Current Protocols in Molecular Biology (1995), John Wiley & Sons, Inc. Examples of suitable eukaryotic hosts include mammalian cells.
If a prokaryotic host is used then the nucleotide sequence—such as the ACE nucleotide sequence—may need to be suitably modified before transformation—such as by removal of introns.
Thus, the present invention also relates to the transformation of a host cell with a nucleotide sequence—such as ACE or a modulator of ACE. Host cells transformed. with the nucleotide sequence may be cultured under conditions suitable for the expression and recovery of the encoded protein from cell culture. The protein produced by a recombinant cell may be secreted or may be contained intracellularly depending on the sequence and/or the vector used. As will be understood by those of skill in the art, expression vectors containing coding sequences can be designed with signal sequences which direct secretion of the coding sequences through a particular prokaryotic or eukaryotic cell membrane. Other recombinant constructions may join the coding sequence to nucleotide sequence encoding a polypeptide domain, which will facilitate purification of soluble proteins (Kroll D J et al (1993) DNA Cell Biol 12:441-53) e.g. 6-His or Glutathione-S-transferase.
Transfection
Vectors comprising for example, the ACE nucleotide sequence, may be introduced into host cells, for example, mammalian cells, using a variety of methods.
Typical transfection methods include electroporation, DNA biolistics, lipid-mediated transfection, compacted DNA-mediated transfection, liposomes, immunoliposomes, lipofectin, cationic agent-mediated, cationic facial amphiphiles (CFAs) (Nature Biotech. (1996) 14, 556), multivalent cations such as spermine, cationic lipids or polylysine, 1,2,-bis(oleoyloxy)-3-(trimethylammonio)propane (DOTAP)-cholesterol complexes (Wolff and Trubetskoy 1998 Nature Biotechnology 16: 421) and combinations thereof.
Uptake of nucleic acid constructs by mammalian cells is enhanced by several known transfection techniques for example those including the use of transfection agents. Example of these agents include cationic agents (for example calcium phosphate and DEAE-dextran) and lipofectants (for example lipofectamTM and transfectamTM). Typically, nucleic acid constructs are mixed with the transfection agent to produce a composition.
Such methods are described in many standard laboratory manuals—such as Sambrook et al., Molecular Cloning: A Laboratory Manual, 2d ed. (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
General Recombinant DNA Methodology Techniques
The present invention employs, unless otherwise indicated, conventional techniques of chemistry, molecular biology, microbiology, recombinant DNA and immunology, which are within the capabilities of a person of ordinary skill in the art. Such techniques are explained in the literature. See, for example, J. Sambrook, E. F. Fritsch, and T. Maniatis, 1989, Molecular Cloning: A Laboratory Manual, Second Edition, Books 1-3, Cold Spring Harbor Laboratory Press; Ausubel, F. M. et al. (1995 and periodic supplements; Current Protocols in Molecular Biology, ch. 9, 13, and 16, John Wiley & Sons, New York, N.Y.); B. Roe, J. Crabtree, and A. Kahn, 1996, DNA Isolation and Sequencing: Essential Techniques, John Wiley & Sons; J. M. Polak and James O'D. McGee, 1990, In Situ Hybridization: Principles and Practice; Oxford University Press; M. J. Gait (Editor), 1984, Oligonucleotide Synthesis: A Practical Approach, Irl Press; and, D. M. J. Lilley and J. E. Dahlberg, 1992, Methods of Enzymology: DNA Structure Part A: Synthesis and Physical Analysis of DNA Methods in Enzymology, Academic Press. Each of these general texts is herein incorporated by reference.



DESCRIPTION OF THE DRAWINGS
FIG. 1 is a schematic presentation of wild-type tACE (tACE) and tACEΔ36 glycosylation mutants. Glycosylation sites are shown with boxes, glycosylated always (black box), glycosylated partially (grey box) and unglycosylated (open box). The O-glycosylated region at the N-terminus of (tACE), which is absent in tACEΔ36, is shown with a stippled box. TM is the transmembrane domain.
FIG. 2 illustrates the expression of tACE glycosylation mutants. Proteins are immunodetected from detergent-solubilised cells (A) and from harvested medium (B) with rabbit anti-human tACE antibody (at 1:2000). The estimated protein size is indicated. Lanes contain tACEΔ36 (A36), untreated CHO cells (CHO) and ACE glycosylation mutants tACEΔ36-g(n) where n equals the number of sites that are glycosylated.
FIGS. 3 illustrates the effect of tunicamycin on the expression and processing of tACE. CHO cells expressing wild-type tACE are treated with the glycosylation inhibitor tunicamycin for up to 24 h. Cell lysate from untreated (a) and treated (b) cells are analysed at the indicated times by Western blotting, protein molecular weights are given.
FIG. 4 illustrates the effect of phorbol ester on the levels of ACE activity. Results are expressed as percentage soluble of total (soluble plus cell associated) ACE activity. Lanes show wild-type tACE (tACE), tACEΔ36 (Δ36) and glycosylation mutants tACEΔ36 g(n), where n gives the number of sites that are glycosylated. CHO cells were grown either in the absence (open bars) or the presence (filled bars) of phorbol 12, 13-butyrate.
FIG. 5 represents the orthorhombic crystals of tACEΔ36.
FIG. 6 schematically illustrates a general purpose computer (132) of the type that may be used in accordance with the present invention. The computer (132) includes a central processing unit (134), a read only memory (136), a random access memory (138), a hard disk drive (140), a display driver (142) and display (144) and a user input/output circuit (146) with a keyboard (148) and mouse (150) all connected via a common bus (152). The central processing unit (134) may execute program instructions stored within the ROM (136), the RAM (138) or the hard disk drive (140) to carry out processing of signal values that may be stored within the RAM (138) or the hard disk drive (140). The program may be written in a wide variety of different programming languages. The computer program itself may be stored and distributed on a recording medium, such as a compact disc, or may be downloaded over a network link (not illustrated). The general purpose computer (132) when operating under control of an appropriate computer program effectively forms an apparatus for performing aspects of the present invention.
FIG. 7 illustrates the overview of the testis ACE structure. (a) Ribbon diagram of the molecule looking down on the active site. The molecule can be divided into 2 halves as domains I and II show in cyan and pink respectively. The active site zinc ion and the lisinopril molecule are shown in yellow. The two chloride ions are shown as black spheres. (b) The molecular surface representation showing the active site groove. (c) The structure-sequence relationship in ACE (SEQ ID NO: 2). The secondary structure elements (domain I-cyan; domain II-pink) follow the same colour code as in (a). The important residues which are involved in binding are marked-zinc ligands (yellow), chloride binding residues (C11-light green, C12-dark green), lisinopril binding residues (cyan) and glycosylation sites (open boxes).
FIG. 8 illustrates details of the active site. (a) Zinc co-ordination in the native structure. Bound zinc ion, acetate ion (AC) and part of the butyl succinate moiety (LIG) are shown. (b) Details of lisinopril (LIS) interactions. Bound zinc ion is also shown.
FIG. 9 illustrates the comparison of (a) ACE and (b) Neurolysin folds. The same view as in FIG. 7a has been retained.



The invention will now be further described by way of Examples, which are meant to serve to assist one of ordinary skill in the art in carrying out the invention and are not intended in any way to limit the scope of the invention.
EXAMPLES
Example 1
Materials & Methods
Materials
Endoproteinase Lys-C and Asp-N, peptide-N-glycosidase F (PNGase F), endoglycosidase H (endo H), neuraminidase, and O-glycosidase are purchased from Roche Biochemicals. Cyanogen bromide, trifluoroacetic acid, and calibration standards (angiotensin, insulin, myoglobin, oxidised insulin B-chain, and TPCK-treated trypsin) are from Sigma Chemical Co. Glycosylation inhibitor N-butyldeoxynojirimycin (NB-DNJ) was a kind gift from Dr. F. Platt, University of Oxford, UK.
Construction of Expression Vectors
pEE-ACEΔ36NJ encodes human tACE that lacks the heavily O-glycosylated, 36-residue N-terminal sequence and is truncated after Ser625, thereby lacking most of the juxtamembrane stalk as well as the transmembrane and cytoplasmic domains, and is constructed as follows. The 5′ half of the ACE cDNA in the plasmid pLEN-ACE-JMΔ24 is excised by digestion with BamHI and NheI and replaced with the similarly digested fragment from plasmid pLEN-ACEΔ36N. pLEN-ACE-JMΔ24 has an engineered EcoRI site at nucleotide (nt) 1984 in the ACE cDNA. The sequence between nt 1854 (the start of the unique BclI site) and nt 1990 (the end of the codon for Ser625) in the native ACE cDNA are amplified by the polymerase chain reaction, using a 3′ primer that contains two stop codons (TAA and TAG) after the Ser625 codon, followed by an EcoRI site. The recombinant sequence is inserted into the pLEN-ACE—36N/JMΔ24 hybrid cut with BclI and EcoRI, to generate pLEN-ACEΔ36NJ. The ACEΔ36NJ coding sequence is excised by digestion of unique XbaI (generated after first subcloning in pBluescript) and EcoRI sites and inserted into the polylinker of the expression vector pEE14, to generate pEE-ACEΔ36NJ.
Cell Culture and Transfections
CHO-K1 cells stably transfected with pLEN-ACE glycosylation mutants are grown and maintained in standard media (50% Ham's F-12/50% DME medium supplemented with 20 mM Hepes, pH 7.3) containing 2% fetal bovine serum (heated to 65° C. for 15 mins before use) and 40 μM Zn Cl2. In addition, native CHO-K1 cells are cotransfected with pEE-ACEΔ36NJ (10 μg) and pSV2NEO (1 μg) by the calcium phosphate precipitate method and clones stably resistant to G418 (Geneticin, Gibco-BRL) are selected and assayed for ACE activity, by procedures detailed previously (9,11). Clones stably expressing pEE-ACEΔ36NJ are further selected for resistance to methionine sulfoximine and then amplified, as described (Davis, S J, Davies, E A, Barclay, A N, Daenke, S, Bodian, D L, Jones, E Y, Stuart, D I, Butters, T D, Dwek, R A, and van der Merwe, P A (1995) J Biol Chem 270, 369-375). Methionine sulfoximine-amplified cells are grown first in GMEM-10 (Gibco-BRL) containing 10% dialyzed fetal bovine serum (FBS) (Gibco-BRL) and 1.5 mM NB-DNJ for 3 days and then refed with GMEM-10, 5% dialyzed FBS, 2 mM NB-DNJ. This medium is changed twice over a period of 9 days before harvesting.
Enzyme Purification
Soluble, recombinant tACE (wild-type, ACEΔ36NJ and ACE glycosylation mutants), is purified from conditioned media by affinity chromatography on a Sepharose-28-lisinopril affinity resin. The protein is quantitated by amino acid analysis and assayed for activity using the substrate hippuryl-L-histidyl-L-leucine, as described (Ehlers, MRE, Chen, Y-N, Riordan, J F (1991) Proc Natl Acad Sci USA 88, 1009-1013).
Deglycosylation of ACE
tACEΔ36NJ (12.5 nmol) purified from cultures treated with NB-DNJ is digested with endo H (30 mU) in 100 mM sodium phosphate, 0.1 mM ZnCl2, 1% BSA, pH 6.0 for 16 h at 37° C. The endo H-treated ACE is passed through a lectin affinity column consisting of equal parts of concanavalin A, wheat germ, and lentil lectin, after equilibration with 20 mM Tris-HCl, 0.5 M NaCl at pH 7.4. The deglycosylated ACE is collected in the flowthrough. Free oligosaccharides and any other impurities are removed from, the flowthrough fraction by a final lisinopril-Sepharose affinity chromatography step. The homogeneity of the tACEΔ36NJ after deglycosylation is confirmed by SDS-PAGE on a 4-20% acrylamide gel and MALDI-TOF mass spectrometry.
Construction of Glycosylation Mutants
Minimally glycosylated isoforms of human testis ACE are constructed by the removal of a combination of N-linked glycosylation sites. Glycosylation is abolished by site-directed mutagenesis of the site of attachment in the recognition sequon (Asn-X-Ser/Thr) through a conserved transition of the Asn to a Gln residue. A truncated form of tACE (tACEΔ36 lacking the first N-terminal 36 residues is used for the construction of all mutants. tACEΔ36 cDNA is divided into four fragments and introduced into pGEM-11Zf(+) to facilitate site-directed mutagenesis. An Eco47III site is introduced into pGEM-11Zf(+) for cloning of the first and second tACEΔ36 fragments. A 146 bp BamHI/NheI digested pBR329 fragment that contains an Eco47III site is ligated to BamHI/XbaI digested pGEM. The following mutagenic oligonucleotides are used for altering the consensus sites for N-linked glycosylation: g1-F, g2-F, g3-F, g4-F, g5-F, g6-F, g1-R, g2-R and g3-R, with the number referring to each complementary recognition sequon. The mutagenic oligonucleotides encode the Asn to Gln transition (underlined) at the glycosylation sites and a silent mutation that alters a restriction enzyme recognition site (highlighted in italics). Mutated residues are indicated by bold type:
Forward primers:








g1-F (40-mer):



5′-GAGGCCA TTGGAACTACAACACCCAGATCACCACAGAG-3′


(SEQ ID NO: 3)


 


g2-F (36-mer):


5′-ATGCAAATAGCCCAGCACACCCT AAGTACGGCACC-3′


(SEQ ID NO: 4)


 


g3-F (40-mer):


5′-GAAGTTTGATGT AACCAGTTGCAGCAGACCACTATCAAG-3′


(SEQ ID NO: 5)


 


g4-F (30-mer):


5′-GTGTGCCACCCGCAAGG AGCTGCCTGCAG-3′


(SEQ ID NO: 6)


 


g5-F (36-mer):


5′-CCGTGCCTCCTGA TTCTGGCAGAAGTCGATGCTGG-3′


(SEQ ID NO: 7)


 


g6-F (36-mer):


5′-ACGGGCCAGCCCCAGATGAGCGC TCGGCC-3′


(SEQ ID NO: 8)






Reverse primers are complementary to the forward primers:








g1-R (40-mer):



5′-CTCTGTGGTGATCTGGGTGTTGTAGTTCCAATTGGCCTCG-3′


(SEQ ID NO: 9)


 


g2-R (36-mer):


5′-GGTGCCGTACTTAAGGGTGTGCTGGGCTATTTGCAT-3′


(SEQ ID NO: 10)


 


g3-R (40-mer):


5′-CTTGATAGTGGTCTGCTGCAACTGGTTAACATCAAACTTC-3′


(SEQ ID NO: 11)






In the first fragment a cDNA-containing mutation at one site served as a template for the mutagenesis of the second site thus generating five variants with either one or two sites out of the firs three eliminated. The fourth, fifth and sixth sites (N155, N337 and N586) are eliminated from fragments 2, 3 and 4 respectively using primers g4-F, g5-F, g6-F. The nucleotide sequence of each fragment is confirmed by sequencing to ensure that only the desired mutation has been created. The four fragments are reassembled to produce eight tACEΔ36 glycosylation mutants (FIG. 1).
The mutants are introduced into the mammalian expression vector, pLEN, to facilitate the production of underglycosylated tACEΔ36 protein. The expression vectors pLEN-tACEΔ36g(n), where n is a set of numbers defining the available N-linked glycosylation sites, are stably expressed in CHO cells as described previously Ehlers et al. (1996) Biochemistry 35, 9549-9559). Similarly, wild-type tACE (tACE-wt), retaining its 36-residue N-terminus as well as the transmembrane region and juxtamembrane stalk, is stably expressed in CHO cells. A deletion mutant, tACEΔ36NJ, truncated after Ser625, and thus lacking the cytoplasmic and TM domains as well as most of the juxtamembrane stalk, is constructed (Yu et al. (1997) J. Biol. Chem. 272, 3511-3519). The vector pEE14-ACEΔ36NJ is transfected into CHO cells and clones stably expressing the mutant are amplified using methionine sulfoxamine, as described (Yu et al. (1997) J. Biol. Chem. 272, 3511-3519).
Inhibition of tACE Glycosylation in Presence of Tunicamycin
CHO cells expressing tACE-wt are grown to confluence in 6-well plates and induced overnight in 2% medium in the absence and presence of 5 μg/ml tunicamycin. Fresh medium is added and cells are grown in the absence and presence of 5 μg/ml tunicamycin. At 6, 8, 12, 16, 20 and 24 hours detergent-solubilised cell samples are collected. After separating the proteins on 10% SDS-PAGE they are immunodetected by Western blotting.
Western Blot Analysis of Glycosylation Mutants
tACE-wt, tACEΔ36, tACEΔ36-g1, -g2, -g3, -g12, -g13, -g23, -g123 and -g1234 are immunodetected by Western blotting of cell lysates and harvested medium from transfected CHO cells. Proteins are separated on 10% SDS-PAGE and transferred to nitrocellulose membrane (Hybond-C, Amersham). The membrane is probed with a polyclonal rabbit anti-human tACE antibody. The membrane is developed using the ECL chemiluminescence kit (Amersham) and visualised on autoradiographic film, as per instructions.
Analysis of Release Kinetics and Cleavage Sites
After selection for stable transfectants, kinetic analyses of rates of accumulation of soluble (released) ACE activity and changes in membrane-bound ACE activity are performed in the presence and absence of 1 μM phorbol 12,13 dibutyrate (Schwager et al. (1998) Biochemistry 37, 15449-15456). Identification of the stalk cleavage sites and analysis of the C-terminal glycosylation site in the released (soluble) protein is carried out using limited proteolysis and MALDI-TOF mass spectrometry by methods described previously (Schwager et al. (1998) Biochemistry 37, 15449-15456).
Determination of Kinetic Constants for tACE Hydrolysis of Hippuryl-L-histidyl-L-leucine (Hip-His-Leu)
The enzyme is purified from harvest medium via lisinopril affinity chromatography and rates of substrate hydrolysis are determined. Assays are performed in 100 mM potassium phosphate pH 8.3 containing 300 mM NaCl. Initial velocities are calculated over a range of Hip-His-Leu concentrations (0.2-5.0 mM) under initial rate conditions and fit to the Michaelis-Menten equation. Km and Vmax values are determined by non-linear regression analysis. Turnover numbers (kcat) and specificity constants (kcat/Km) are determined using a calculated molecular mass of 100 kDa.
Mass Spectrometry
Mass spectrometry is used to verify the glycan occupancy of some of the glycosylation sites of the mutant proteins. All mass spectra are obtained on a MALDI/TOF/MS instrument (Voyager-Elite Biospectrometry Workstation, PerSeptive Biosystems, Inc.). A nitrogen laser (337 nm) is used for desorption ionization. Measurements are carried out either in the linear or reflectron mode with mass accuracies of 0.1% and 0.01%, respectively. Spectra are collected over a hundred laser shots.
Typical matrices used in these experiments are 3,5-dimethoxy-4-hydroxycinnamic acid (sinapinic acid) and α-cyano-4-hydroxycinnamic acid (Aldrich). About 1 μl of sample solution was mixed with 2 μl of the matrix solution (10 mg/ml in 50% v/v CH3CN and H2O). A 0.5 μl volume (containing 1-10 pmol of peptide or peptide mixture) of the above solution is loaded on the sample plate and allowed to dry.
Crystallisation
The purified tACE-ACEΔ36NJ and ACE glycosylation mutants are stored at −20° C. in 10 mM HEPES and 0.1% PMSF. Extensive crystallisation trials using commercially available crystal screen conditions (Hampton Research) are tried. In addition ammonium sulphate, PEG and MPD matrices are also tried. The best crystals for these proteins are grown at 16° C. by the vapour diffusion hanging drop method by mixing 2 μl of the protein solution at  ̃11.5 mg/ml in 10 mM HEPES and 0.1% PMSF with an equal volume of a reservoir solution containing 15% PEG 4000 (Fluka), 50 mM CH3COONa.3H2O (Sigma Chemical Company) pH 4.7 and 10 μM ZnSO4.7H2O (Aldrich Chemical Company). Crystals usually appear within 2 weeks and grow to their maximum size after about a month. The crystals belong to P212121 space group, with 1 molecule in the crystallographic asymmetric unit and some 49% of the crystal volume occupied by the solvent (cell dimensions: a=56.47 Å, b=84.90 Å, c=133.99 Å, Δ=90°, β=90° and γ=90°). tACE-ACEΔ36NJ crystals diffract to 2 Å while tACE-ACEΔ36NJ-g13 and tACE-ACEΔ36NJ-g1234 crystals diffract to 3.0 Å and 2.8 Å respectively on a Synchrotron Radiation Source. All crystals are isomorphous.
The tACE-lisinopril (lisinopril.dihydrate) inhibitor complex is obtained by growing the crystals in the presence of inhibitor. In these experiments the protein solution is mixed with 10 mM of the inhibitor and mixed with an equal volume of the reservoir solution before setting up the crystallisation. Single crystals belonging to the P212121 orthorhombic space group (isomorphous with the native crystals) suitable for diffraction work appear after about 4 weeks.
X-Ray Diffraction Data Collection
Before data collection, all crystals are flash-cooled at 100 K in a cryoprotectant containing 15% PEG 4000, 50 mM CH3COONa.3H2O pH 4.7, 10 μM ZnSO4.7H2O and 25% glycerol with and without respective entities—such as ACE inhibitors. All the X-ray data are collected at 100° K. using a Synchrotron Radiation Source (ESRF-Grenoble, France). Multi-wavelength anomalous dispersion (MAD) data are collected with crystals of tACE-lisinopril complex at peak of Zn K-edge (1.2825 Å), inflection (1.28322 Å) and remote (0.95373 Å) wavelengths. An anomalous dataset at long wavelength (1.7712 Å), the closest possible wavelength to Sulphur K-edge is also collected. All other heavy atom data sets are collected at the SRS-Daresbury (UK) and processed with anomalous signal. Out of more than 32 soaks with different heavy atoms, only three are found to be useful in phasing. These three (Pt, Pd & Os) derivatives are prepared by soaking the tACE-lisinopril complex crystals for  ̃10 to 60 minutes in the presence of 1-5 mM heavy atom solutions. Raw data images are indexed and scaled using the DENZO and SCALEPACK modules of the HKL suite [Otwinowski M and Minor W. (1997) Methods Enzymol 276, 307-326].
Example 2
Expression of Glycosylation Mutants in CHO Cells and the Kinetics of Release
The role of N-linked glycosylation in the expression and processing of tACEΔ36 is investigated to establish the minimal glycosylation requirements for the expression of correctly folded enzymatically-active protein. The eight glycosylation mutants constructed are transfected into CHO cells and the effect of deglycosylation on the activity, expression and processing of tACEΔ36 is assessed by enzyme assays, immunodetection and cleavage site analysis.
Western blot analysis of cellular and soluble tACEΔ36 glycoforms reveal proteins with increased mobility relative to glycosylated wild type tACE (tACE-wt) (FIG. 2) and which is dependent upon on their degree of glycosylation. Furthermore, differences are detected in the expression and processing of the various glycoforms. Comparatively low levels of tACEΔ36-g2 protein in cellular extracts (FIG. 2A), and its absence in the harvest medium (FIG. 2B), may suggest intracellular degradation and/or deficient processing of the protein. Whilst tACEΔ36-g1 demonstrates comparable levels of expression to the other proteins (FIG. 2A), processing and solubilisation appears to be less efficient than tACEΔ36-g3, -g123, and -g1234 (FIG. 2B). Tunicamycin partially inhibits the formation of mature, glycosylated tACE-wt. Western blot analysis of cellular tACE-wt in the absence of tunicamycin reveals a 105 kDa mature, glycosylated protein (FIG. 3). In the presence of tunicamycin an additional smaller, deglycosylated 85 kDa protein is detected (FIG. 3).
The Km and kcat values obtained for the hydrolysis of Hip-His-Leu by tACE (Table 3) are in agreement with those previously published for the C-fragment of the human endothelial isoform (Km=2.0 mM) (10). Differences in the kinetic constants of glycosylated and under-glycosylated tACEΔ36 mutants are negligible and are not considered sufficiently different to reflect major alterations in the conformation and activity of the protein. Glycosylation of tACEΔ36 at one (tACEΔ36-g3) or two (tACEΔ36-g13) N-terminal glycosylation sequons is sufficient in maintaining the functional integrity of the enzyme. Furthermore, treatment of cells expressing tACEΔ36NJ with the glucosidase I inhibitor NB-DNJ, do not alter the kinetic properties of the expressed enzymes.
Example 3
Kinetics of Release and Analysis of Juxtamembrane Cleavage Sites
Independent transfections of CHO cells with tACEΔ36-g1, -g12, -g123 and -g1234 are performed which yield consistent results for each mutant (FIG. 4). All glycosylation mutants show similar levels of phorbol ester stimulation. Thus, N-linked glycosylation does not appear to affect solubilisation of the membrane-anchored enzyme. Further protein analysis is performed to: 1) identify the C-terminal peptide to determine whether cleavage of tACEΔ36-g1, -g13 and -g1234 occurs at the same residues as tACE and 2) to investigate the glycosylation status of the seventh recognition sequon which lies seven residues proximal to the tACE cleavage site. The mass spectra of endoproteinase Lys-C digested peptides of tACEΔ36-g1, -g13 and -g1234 reveal three [M+H]+ ions of m/z 1698.7, 1690.5 and 1690.9, respectively (Table 2), which are in close agreement with the theoretical mass of the C-terminal peptide (calculated m/z 1690.8).
Thus, tACEΔ36-g1, -g13 and -g1234 proteolysis occurs between Arg627 and Ser628, which is at the same site as tACE-wt. The spectra of the mutant tACEΔ36NJ reveals a [M+H]+ ion at m/z 1463.1 which corresponds to the calculated mass of the peptide Leu614 to Ser625 confirming that truncation occurs at Ser625 and that there is no further limited proteolysis of the C-terminus (Table 2).
Example 4
Structure of ACE
The crystal structure of the native ACE enzyme is determined to 2.0 Å resolution. The structure from residues 71-648 adopts an overall ellipsoid shape (dimensions  ̃72 Å×57 Å×48 Å) with a central groove that extends for about 30 Å into the molecule and effectively divides the protein into two “domains” (labelled I and II, FIG. 7a,b). On top of the molecule there is a N-terminal “flap” that allows access to the active site cleft Like the recently determined zinc-peptidase structure-neurolysin, ACE is also bristling with helices and is comprised of twenty α-helices (with almost equal distribution of helices in both domains) and seven 310-helices (FIG. 7c). This makes the molecular architecture very compact and rigid as observed from the thermal parameters (crystallographic B-factors) for the structure. The only β-structure which accounts for 4% of all residues occurs as six relatively short strands, two of which are located near the active site (FIG. 7a). The boundaries of the groove are provided by domain II (α13, α14, α15, α17, β4) with part of the domain I forming the flap (α1, α2, α3). In addition the base of the scaffold is formed by helices α6 and α8 and helix α15 serves as an anchor.
Eight C-terminal residues are disordered in the crystal structure and most of this flexible region constitutes the unconstrained juxtamembrane region distal to the wild-type ACE cleavage site. The α-helix from Ala 620 to His 641(α20) defines the C-terminal boundary of the ectodomain and this is in agreement with previous ACE mutagenesis and cleavage-secretion studies (Ehlers et al., 1996; Chubb et al., 2002). Residues Ser 466-Gly 469 are disordered in the structure. Five hundred and four ordered water molecules were identified in the native structure. All six glycosylation sites (g1-6, FIG. 7c) are exposed and g1 site is closest to the N-terminus of the molecule. Sketchy density was observed for N-linked carbohydrates in all the glycosylation sites (FIG. 7c) and modelled as N-acetylglucosamine (NAG) in the native structure. The co-ordinates of underglycosylated tACEΔ36NJ ACE are shown in Table A.
Example 5
Zinc Co-ordination
ACE belongs to the gluzincin family of metalloproteases (Hooper, 1994). Zinc is known to be an important catalytic component of ACE. In the structure, the active site helices α13 and α14 define the substrate binding cleft of this peptidase. One highly ordered zinc ion (B-factor-16.34 Å2) is bound at the active site. The helix α13 contains the HEXXH zinc binding motif (known to be important for the catalytic activity of ACE, Wei et al., 1991), with its two zinc coordinating histidines (His 414 and His 418) and Glu 442 (from α14 helix) acts as the third ligand (FIG. 7c). Additional coordination is provided by an acetate ion (from the crystallization medium) bound at the active site of the native enzyme (FIG. 8a). It has been reported previously that the recruitment of zinc ion in ACE catalysis is analogous to that in thermolysin (Williams et al., 1994; Corvol et al., 1995) and our structural data shows that the zinc binding sites in both proteins are indeed very similar (r.m.s. deviation 1.52 Å) except the acetate ion which is replaced by a water molecule in the coordination sphere in thermolysin. The active site pocket in ACE is occupied by 3 ordered water molecules. In addition, a stretch of clear electron density (at 3σ level) was observed ( ̃5 Å away from the zinc ion) at the active site which is interpreted as part of butyl succinate (FIG. 8a).
Example 6
Activation of ACE by Chloride Ions
Substrate hydrolysis by ACE is activated by chloride anions and, whereas some substrates can be cleaved in the absence of chloride, it is an absolute requirement for angiotensin I (Bunning and Riordan, 1983; Shapiro et al., 1983). Our structure revealed the location of two chloride ions (FIG. 7a, c). The first chloride ion (Cl1, 20.7 Å away from the zinc ion) is bound to three ligands, Arg 520 (NH1), Arg 217 (NE), Trp 516 (NE1) and water and is surrounded by a hydrophobic shell of four tryptophans. The second anion (C12, 10.4 Å away from the zinc ion) is bound to Arg 553 (NE) in agreement with previous report showing Arg 1098 (the analogous Arg residue in the C-domain of somatic ACE) is critical for chloride dependence of ACE activity (Liu et al., 2001). Tyr 255 and a water molecule are the other two C12 ligands. The two chloride ions (separated by 20.3 Å) in ACE are bound almost in a triangular conformation—in accordance with the near equatorial coordination and accommodation of planar trigonal anions in α-amylase where the chloride ions are involved in the allosteric activation (Aghajari et al., 2002). In addition, the anchoring of Domain II on Domain I scaffold appears to be mediated by the chloride ions.
Mutating Arg 1098 to a lysine resulted in a 100-fold reduction in chloride binding affinity as well as a decrease in substrate affinity (Liu et al., 2001). This might be due to the contact with the NE atom of arginine as opposed to an NH1 or NH2 atom with lysine which would permit free rotation of the basic terminal nitrogens. Recent studies suggest that the affinity of chloride binding to ACE is directly related to the interactions between the chloride and enzyme as well as the substrate (Liu et al., 2001). However, based on the location of both chloride ions in the 3D structure make the latter interaction unlikely. Nevertheless, there is a van der Waals contact between C12 and Pro 438 (α14) that could be responsible for maintaining the active site cleft in a conformation which favours substrate accessibility and binding. Indeed α14 contain the third zinc co-ordinating ligand Glu 442. Thus, the chloride interactions likely cause the enzyme to adopt conformations that permit higher affinity substrate binding and that it is not important in substrate binding per se.
Example 7
Structure Determination and Refinement of an ACE-lisinopril Complex
The crystal structure of tACE bound to the potent lisinopril inhibitor (Ki=27×1010M, Wei et al., 1991) complex is determined by a combination of MAD and MIRAS (Multiple Isomorphous Replacement with Anomalous Scattering) procedures. The position of zinc atom is unambiguously identified using the anomalous difference Patterson maps calculated using diffractions data at peak wavelength. The MAD phases thus obtained are not very strong and thus additional phase information is obtained using MIRAS procedures with three—Platinum (K2PtCl4), Palladium (K2PdCl4) and Osmium (OsCl3) heavy atom derivatives. The identified Zn site is used to obtain the starting phases in each derivative. Double difference Fourier maps calculated using FFT routine in CCP4 program [Collaborative computational project Number 4. The CCP4 Suite: Programs for Protein Crystallography (1994) Acta Crystallogr. D 50, 760-763] gave the first major binding site and the phases from the combined Zn and first major site are used to get additional major/minor sites for each derivative. All heavy atom binding sites and the Zn site are refined to 2.8 Å resolution using the program MLPHARE [Collaborative computational project Number 4. The CCP4 Suite: Programs for Protein Crystallography (1994) Acta Crystallogr. D 50, 760-763] and SHARP [De La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameters refinement in the MIR and MAD methods (1997) Methods Enzymol. 276, 472-494]. The overall figure of merit from SHARP is 0.38 (at 2.8 Å resolution) and is improved to 0.89 (at 2.0 Å) by iterative solvent flattening, phase combination and phase extension with the program SOLOMON [Abrahams, J. P. & Leslie, A. G. W. Methods used in structure determination of bovine mitochondrial F1 ATPase. (1996) Acta Crystallogr. D 52, 110-119]. Model building is carried out manually using the program O [Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A 47, 110-119]. Refinement of the model is carried out using the program CNS [Brünger, A. T. et al. Crystallography & NMR System: A new software suite for macromolecular structure determination. (1998) Acta Crystallogr. D 54, 905-921]. During the final stages of refinement water molecules, zinc ion and the inhibitor molecule are inserted in the respective structure. Both the native and inhibitor complex structures are refined at 2.0 Å resolution with  ̃94% residues in the maximum allowed region and no residue in the disallowed region of the Ramachandran map. The final structure of the tACE and ACE-lisinopril complex has an Rfree [Brünger, A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structure. (1992) Nature 355, 472-475] of 22.08 and 21.88%, and a final Rcryst of 18.29 and 18.14% respectively.
Highly ordered binding of the inhibitor (overall B-factor 15.26 Å2) in an extended conformation with the aromatic phenyl group stretching towards the flap (FIG. 7a) and its lysine side chain parallel to the HEXXH motif (Table 1). Upon complex formation no significant rearrangement of active site residues was observed. The P1 carboxylate of lisinopril which is substituted for the normal substrate scissile amide carbonyl is well positioned to bind to the active site zinc (located between subsites S1 and S1′). Thus lisinopril provides a coordinating atom (provided by an acetate ion in the native structure, FIG. 8a), while the other three (two histidines and a glutamic acid) being the same as in the native structure (FIG. 8b). The phenyl ethyl group binds to the S1 subsite and the lysyl amine to Glu 193 via van der Waals interactions at the S1′ subsite of ACE. Surprisingly, the C-terminal carboxylate which is thought to interact with a positively charged arginine residue instead binds to a lysine (Lys 542) as well as Tyr 551. The high affinity is attributable to the presence of the S-configuration aromatic, aralkyl or aliphatic groups able to bind to the S1 site (Brenner et al., 1990). The contact residues for the lisinopril complex are shown in Table 1. The co-ordinates of the underglycosylated tACEΔ36NJ ACE-lisinopril complex are shown in Table B.
Example 8
The Homology of ACE with Other Metallopeptidases
ACE belongs to the M2 family of zinc binding metallopeptidases which falls under the umbrella of the MA clan. Outside the HEXXH metal coordinating signature sequence of this family there is little sequence similarity between ACE and other members of the family. Surprisingly, peptidases such as thermolysin (MA clan, M4 family) and carboxypeptidase A (MC clan, M14 family) which have been used in comparative molecular field analysis and 3D quantitative structure-activity relationship studies (Waller & Marshall, 1993) showed no structural homology with ACE.
Surprisingly, structural comparison of ACE with other protein structures using the DALI server (Holm and Sander, 1999) showed significant structural homology with that of neurolysin (Brown et al., 2001), a protein involved in neurotensin metabolism (FIG. 3a, b). Neurolysin is a member of the M3 family of thimet oligopeptidases and like ACE, belongs to the family of metallopeptidases bearing the HEXXH active site motif (Rawlings and Barrett, 1995; Brown et al., 2001). It also comprises of an abundance of α-helices with the β-structure accounting for only 6% of all residues. The two proteins do not exhibit any amino acid sequence similarity (close to random score), yet when the two structures are optimally superimposed (using DALI server), there is noticeable match with an r.m.s. deviation of 4.0 Å for 143 Cα atoms. It appears that the core structure for the two proteins are highly similar with significant differences in loops on the outer surface in the case of neurolysin (FIG. 3a,b). The striking similarity also extends to the active site region in neurolysin consisting of a deep narrow channel that divides the molecule into two halves. It has been speculated that using the flexible secondary structure elements in the active site cavity, the neuropeptidase can effectively cleave a variety of small peptides. Likewise in ACE, the geometry of the active site groove clearly accounts for ACE's inability to hydrolyse large, folded substrates. Furthermore, the enzyme's preference for oligopeptide substrates of about thirteen residues or less suggests that the substrate does not have the same freedom to extend outside of the channel during catalysis.
Example 9
Substrate Specificity
The geometry of the active site channel clearly accounts for ACE's inability to hydrolyse large, folded substrates. Furthermore, the enzyme's preference for oligopeptide substrates of about thirteen residues or less suggests that the substrate does not have the same freedom to extend outside of the channel during catalysis.
Example 10
Crystallization of ACE Mutants
tACEΔ36-g1234 and tACEΔ36-g1,3 mutants are successfully crystallised under similar conditions as tACEΔ36NJ protein (FIG. 5). Preliminary diffraction experiments show that tACEΔ36-g1234 crystals diffract to at least 2.8 Å and tACEΔ36-g1,3 crystals diffract to 3.0 Å respectively and these crystals are isomorphous with tACEΔ36 crystals.
CONCLUSIONS
The minimal glycosylation requirements for the expression and processing of enzymatically-active human tACE are determined by progressive deglycosylation. To investigate which sugars are vital for tACE expression, a series of mutants are constructed that contain a limited number of sites for N-linked glycosylation. N-glycan recognition sequons within the protein sequence are disrupted by mutagenesis of the Asn to a Gln within the recognition sequon.
The removal of a large percentage of glycans does not hamper the expression of enzymatically-active tACEΔ36 and the presence of glycans at two of the three N-terminal sites is sufficient to produce protein that retain the kinetic properties of the native enzyme. Furthermore, the minimum N-linked glycosylation that allowed for enzymatically-active tACE to be expressed is the presence of glycans at the first or third site. Glycosylation at either of these sites appears to be sufficient for protein folding, whereas glycosylation of the second site only, results in rapid intracellular degradation. This is in agreement with the glycosylation requirements of active rabbit ACE expressed in mammalian cells and yeast which also has a minimal requirement of at least one of the three N-terminal sites (3a).
In the construction of the tACEΔ36 glycosylation mutants, the seventh site which is not present in rabbit tACE is not targeted as it has been shown to be unglycosylated (7a). With the removal of the glycosylated sequons, it is possible that this site may be glycosylated in order to compensate for the loss of oligosaccharide chains. However, this is not the case and that even when there is only one N-linked oligosccharide, this does not occur.
There is a preference for oligosaccharides to be attached to sequons containing threonine residues rather than serine residues. This is observed in human tACE, where all sequons with a serine in the third position are partially glycosylated and those with threonine are fully glycosylated, except for the seventh site, which has a threonine in the third position (7a).
The fact that glycosylation at the seventh site appears to be occluded by the presence of the tryptophan, rather than the structure of the juxtamembrane region, is supported by the findings that a tACE deletion mutant, tACEΔ6, which generates a novel Asn-Arg-Ser sequon adjacent to the wild-type cleavage site, is glycosylated (14a). The extended conformation of oligosaccharides may prevent access of the secretase at this point resulting in displacement of the wild-type cleavage site 13 residues towards the C-terminus (14a).
CHO cells expressing wild-type tACE (tACE-wt) are exposed to tunicamycin, which inhibits N-linked glycosylation, to determine the effect of complete deglycosylation on the expression and activity of tACE over time. Cellular tACE-wt activity in cells treated with tunicamycin is approximately three-fold lower than that of untreated cells (data not shown) and a smaller immature form of the protein is observed by Western blot analysis. These results are consistent with the interpretation that the smaller 85 kDa-protein is the deglycosylated form and the 105 kDa-protein, the mature glycosylated form (7a), (9a), (14a). Thus, tunicamycin inhibits the formation of mature glycosylated tACE-wt, to a certain degree, resulting in the accumulation of unglycosylated tACE-wt in the cell, without a significant decrease in the total amount of protein compared to untreated cells. Our data suggest that unglycosylated tACE-wt is not solubilised and that it requires the presence of N-glycans for proper expression, maturation and processing.
The enzymatically-active tACE-wt present in cells treated with tunicamycin is most likely the product of a pool of glycosylated tACE-wt, which is either produced prior to tunicamycin treatment or is resistant to tunicamycin. Tunicamycin may therefore not be completely effective in CHO cells, whereas in HeLa cells, Kasturi et al. found that tunicamycin-treatment resulted in the generation of deglycosylated protein that is degraded intracellularly within three-hours, with no soluble tACE being detected (5a). Thus, it appears that the effect of tunicamycin on tACE glycosylation appears to be cell-specific.
Enzymatic removal of N-linked glycans is used to produce crystals of CD2 glycoprotein that diffracted to 2.5 Å (15a). However, crystallisation trials with deglycosylated tACEΔ36NJ that has a single GlcNAc residue attached to the asparagine residue of the N-linked site only produced needle-like crystals that are not suitable for further diffraction studies. Surprisingly, tACEΔ36NJ expressed in the presence of NB-DNJ, but retaining the simple high mannose oligosaccharides (Glc3Man7GlcNAc2) yielded the best crystals for X-ray diffraction studies and subsequent successful 3D structure determination at 2.0 Å resolution
Interestingly, the presence of the membrane anchor increased the extent of human CD59 glycan processing (16a). Possible reasons for this difference are, that the ectodomain is held closer to the glycan-processing enzymes and/or the longer exposure to the glycosyltransferases. The oligosaccharide processing of soluble tACEΔ36NJ protein may also differ from the membrane-bound form however, expressing the protein in the presence of a glucosidase inhibitor would prevent the production of complex oligosaccharides.
Furthermore, the kinetic properties of this mutant are not influenced by NB-DNJ treatment. Similarly, Yu et al. reported identical Km values for glycosylated and deglycosylated forms of tACEΔ36NJ, in agreement with that of tACE-wt, using furanacryloyl-Phe-Gly-Gly as a substrate (7a). Glucosidase inhibitors, at concentrations required to block trimming of the terminal glucose residues and subsequent complex oligosaccharide formation, can affect cell maturation and apoptosis (Misago M, Tsukada J, Fukuda M N, Eto S (2000) Biochem Biophys Res Commun. 269, 219-225). This treatment also results in a decrease in protein expression (unpublished data). Thus, mutants lacking some of the C-terminal N-linked glycans are used with the objective of producing protein with a minimal number of oligosaccharides that would crystallise in a reproducible fashion.
Crystals of glycosylation mutants g13 and g1234 have been grown under similar condition as in the case of tACEΔ36NJ. The glycosylation mutant crystals seem to grow faster than tACEΔ36NJ crystals. However, they are smaller in size in the first instance, but have been proven to be suitable for diffraction work.
The determination of the 3D structure of ACE and ACE-lisinopril complex may be effectively used for the development of novel, highly selective ACE modulators targeted, for example, to either the N or the C domain, by structure-based rational drug design. This may produce a new generation of ACE inhibitors with the potential for greater efficacy, fewer side effects and treatment of new indications (e.g. polycythemia). In addition, the unanticipated similarity with neurolysin has shown the structural conservation amongst an emerging family of peptidases with a common evolutionary origin.
In a further aspect, the present invention relates to a composition comprising ACE in a crystalline form.
In a further aspect, the present invention relates to a scalable 3D model of ACE having at least a portion of the structure co-ordinates shown in Table A or Table B.
All publications mentioned in the above specification are herein incorporated by reference. Various modifications and variations of the described methods and system of the invention will be apparent to those skilled in the art without departing from the scope and spirit of the invention. Although the invention has been described in connection with specific preferred embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the invention which are obvious to those skilled in molecular biology or related fields are intended to be within the scope of the following claims.
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    Shapiro, R., Holmquist, B. & Riordan, J. F. Anion activation of angiotensin converting enzyme: dependence of nature of substrate. Biochem. 22, 3850-3857 (1983).
    Waller, C. L. & Marshall, G. R. Three-dimensional quantitative structure-activity relationship of angiotesin-converting enzyme and thermolysin inhibitors. II. A comparison of CoMFA models incorporating molecular orbital fields and desolvation free energies based on active-analog and complementary-receptor-field alignment rules. J. Med Chem. 36, 2390-2403 (1993).
    Wei, L., Alhenc-Gelas, F., Corvol, P. & Clauser, E. The two homologous domains of human angiotensin-1 converting enzyme are both catalytically active. J. Biol. Chem. 266, 9002-9008 (1991).
    Williams, T. A., Corvol, O. & Soubrier, F. Identification of two active site residues in human angiotensin I-converting enzyme. J. Biol. Chem. 269,29430-29434 (1994).









TABLE 1







ACE-Lisinopril Contact Residues (hydrogen bonds at the active site)











Ligand atoms





Lisinopril



atom
Interacting atoms
Distance (Å)







O1
His 384 NE2
2.76



N1
His 384 NE2
3.24



N1
Ala 385 O
2.92



O4
Lys 542 NZ
2.93



O4
Tyr 551 OH
2.56



O3
Tyr 554 OH
2.77



O2
Wat
2.82



O5
Wat
2.68



N3
Wat
3.01



N3
Wat
3.26



O5
Wat
2.77



N3
Wat
3.11



O2
Glu 415 OE2
2.70



O1
His 544 NE2
3.11











Zinc Coordination-ACE-Lisinopril Complex












Coordination
Distance (Å)







Zn
His 414 NE2
2.04



Zn
His 418 NE2
2.07



Zn
Glu 442 OE1
2.00



Zn
Lis O3
2.14







Lis = Lisinopril













TABLE 2







Data Collection














Resolution rangea
%

Rmergeab


Crystal
Wavelength(Å)
(Å)
completenessa
<I>/<σ>a
(%)





MAD Phasing
Zn Peak 1.2825
50-2.00(2.07-2.00)
94.7(63.2)
11.54(1.93)
5.4(22.3)


data.
Zn infl. 1.2832
50-2.01(2.08-2.01)
95.9(72.1)
11.55(1.98)
5.8(23.8)



Zn rem. 0.9537
50-1.98(2.05-1.98)
94.1(65.8)
15.48(2.63)
4.8(14.9)



Long Wavelength
50-2.66(2.76-2.66)
99.6(97.0)
22.92(4.94)
8.3(21.8)



1.7712


MIRAS


Phasing data


Pt
0.87
20-2.80(2.9-2.8)
90.2(83.6)
 9.94(4.52)
11.2(27.1) 


Pt25
0.87
20-2.60(2.69-2.6)
89.9(75.9)
 13.6(4.17)
8.8(27.8)


Pd
0.978
50-2.18(2.26-2.18)
89.4(81.2)
26.14(6.73)
5.8(25.8)


Pd2
0.978
30-2.60(2.69-2.6)
95.2(86.7)
16.95(5.46)
9.5(35.7)


Oscl
1.488
50-2.80(2.9-2.8)
96.6(91.4)
18.51(6.16)
13.1(40.4) 


Native Data
1.488
50-2.00(2.07-2.0)
98.8(95.7)
22.46(4.44)
8.1(43.2)










Refinement









B factor Rmsd (Å2)











Rms deviations

Bonded




















Bond
Bond
Bonded
Side



Resolution
Reflections
Rcrystc
Rfreed
length
angle
Main Chain
Chain


Model
(Å)
working/test
(%)
(%)
(Å)
(°)
Atoms
Atoms





Native
47.14-2.0
39727/1675
18.29
22.08
0.005 
1.22
1.281
2.126


(ACE)


Lisinopril
47.14-2.0
76164/3094
18.14
21.88
0.0055
1.24
1.174
2.048


complex(ACE-


LIS)





aValues in parentheses are for the outer resolution shell.


bRmerge = Σ|I − <I>|/Σ I, where I is the observed intensity and <I> is the average intensity obtained from multiple observations of symmetry related reflections.


cRcryst = Σ|Fo| − |Fc|/Σ|Fo| where Fo and Fc are observed and calculated structure factors respectively.


dRfree is obtained for a test set of reflections, consisting of a randomly selected ~4% of reflections.













TABLE 3







Kinetic parameters for the hydrolysis of Hip-His-Leu by


various tACE glycoforms











Km (mM)
kcat (sec−1)
kcat/Km (sec−1mM−1)





tACE-wt
2.7
193
72


tACEΔ36-g1
1.6
128
79


tACEΔ36-g3
2.5
111
44


tACEΔ36-g13
2.7
170
63


tACEΔ36-g2
inactive
inactive
inactive


tACEΔ36-g12
2.1
195
94


tACEΔ36-g123
2.7
189
71


tACEΔ36-g1234
1.5
 85
56


tACEΔ36-NJ1
2.6
253
99


tACEΔ36-NJ2
4.1
289
70





1Expressed in CHO cells treated with NB-DNJ.


2Expressed in NB-DNJ-untreated CHO cells.













TABLE 4







Mass Spectral Analysis of C-Terminal Endoproteinase Lys-C Peptidesa











Peptide






(residue no.b)
tACEΔ36-g1
tACEΔ36g-1
tACEΔ36-g1234
tACEΔ36NJ





598-613c
1951.6 (1951.2)
1950.6 (1951.2)
1950.2 (1951.2)
1951.5 (1951.2)


614-627d
1689.7 (1690.8)
1690.5 (1690.8)
1690.9 (1690.5)


614-625d



1463.1 (1463.5)





aSoluble (shed) ACE proteins were purified from conditioned medium of transfected cells, digested with endoproteinase Lys-C and analyzed by MALDI-TOF mass spectrometry.


bAmino acid residue numbering refers to wild type tACE (Ehlers et al 1989). Shown are the masses of the penultimate c and ultimate d C-terminal peptides. All values are calculated for protonated isotopically averaged molecular masses m/z. In parentheses are expected masses.













TABLE A





Co-ordinates of underglycosylated tACEΔ36NJ ACE















REMARK coordinates from minimization refinement


REMARK refinement resolution: 47.14-2.0 A


REMARK starting r= 0.1829 free_r= 0.2206


REMARK final  r= 0.1829 free_r= 0.2208


REMARK rmsd bonds= 0.005706 rmsd angles= 1.22440


REMARK wa= 0.837519


REMARK target= mlf cycles= 1 steps= 20


REMARK sg= P2(1)2(1)2(1) a= 56.621 b= 85.062 c= 133.791 alpha= 90


beta= 90 gamma= 90


REMARK ncs= none


REMARK B-correction resolution: 6.0-2.0


REMARK initial B-factor correction applied to fobs:


REMARK  B11=  2.826 B22= −1.896 B33= −0.930


REMARK  B12=  0.000 B13=  0.000 B23=  0.000


REMARK B-factor correction applied to coordinate array B:  0.207


REMARK bulk solvent: density level= 0.355826 e/A{circumflex over ( )}3, B-factor= 50.0907


A{circumflex over ( )}2


REMARK reflections with |Fobs|/sigma_F < 0.0 rejected


REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected


REMARK theoretical total number of refl. in resol. range: 44472


(100.0%)


REMARK number of unobserved reflections (no entry or |F|=0): 3070


(6.9%)








REMARK number of reflections rejected:
  0 (  0.0% )


REMARK total number of reflections used:
41402 ( 93.1% )


REMARK number of reflections in working set:
39727 ( 89.3% )


REMARK number of reflections in test set:
 1675 (  3.8% )







CRYST1  56.621  85.062 133.791 90.00 90.00 90.00 P 21 21 21


REMARK VERSION: 1.1
















ATOM
1
CB
ALA
71
34.205
71.662
65.620
1.00
47.11


ATOM
2
C
ALA
71
36.244
70.263
65.985
1.00
47.34


ATOM
3
O
ALA
71
36.117
69.044
65.862
1.00
47.51


ATOM
4
N
ALA
71
35.784
72.211
67.437
1.00
47.96


ATOM
5
CA
ALA
71
35.164
71.098
66.663
1.00
47.50


ATOM
6
N
GLU
72
37.307
70.929
65.547
1.00
46.68


ATOM
7
CA
GLU
72
38.419
70.260
64.882
1.00
46.09


ATOM
8
CB
GLU
72
39.315
71.298
64.200
1.00
46.87


ATOM
9
CG
GLU
72
40.370
70.727
63.262
1.00
47.65


ATOM
10
CD
GLU
72
39.776
70.111
62.005
1.00
48.95


ATOM
11
OE1
GLU
72
38.997
70.801
61.309
1.00
48.20


ATOM
12
OE2
GLU
72
40.096
68.939
61.708
1.00
49.03


ATOM
13
C
GLU
72
39.223
69.474
65.916
1.00
45.81


ATOM
14
O
GLU
72
39.862
68.466
65.594
1.00
45.67


ATOM
15
N
ALA
73
39.184
69.941
67.161
1.00
43.82


ATOM
16
CA
ALA
73
39.905
69.292
68.249
1.00
42.35


ATOM
17
CB
ALA
73
39.995
70.229
69.446
1.00
42.98


ATOM
18
C
ALA
73
39.210
67.996
68.646
1.00
40.96


ATOM
19
O
ALA
73
39.863
66.990
68.926
1.00
39.62


ATOM
20
N
GLU
74
37.881
68.028
68.680
1.00
40.60


ATOM
21
CA
GLU
74
37.104
66.844
69.025
1.00
40.79


ATOM
22
CB
GLU
74
35.620
67.190
69.157
1.00
42.97


ATOM
23
CG
GLU
74
35.138
67.389
70.581
1.00
48.05


ATOM
24
CD
GLU
74
33.642
67.644
70.649
1.00
51.91


ATOM
25
OE1
GLU
74
32.869
66.798
70.142
1.00
53.53


ATOM
26
OE2
GLU
74
33.239
68.687
71.210
1.00
53.71


ATOM
27
C
GLU
74
37.272
65.799
67.931
1.00
38.90


ATOM
28
O
GLU
74
37.217
64.597
68.192
1.00
38.20


ATOM
29
N
ALA
75
37.482
66.273
66.706
1.00
37.33


ATOM
30
CA
ALA
75
37.643
65.395
65.552
1.00
35.44


ATOM
31
CB
ALA
75
37.619
66.217
64.268
1.00
34.80


ATOM
32
C
ALA
75
38.917
64.558
65.613
1.00
33.72


ATOM
33
O
ALA
75
38.871
63.343
65.434
1.00
34.25


ATOM
34
N
SER
76
40.053
65.204
65.856
1.00
32.28


ATOM
35
CA
SER
76
41.319
64.486
65.932
1.00
32.11


ATOM
36
CB
SER
76
42.486
65.468
66.012
1.00
33.65


ATOM
37
OG
SER
76
42.391
66.266
67.175
1.00
40.00


ATOM
38
C
SER
76
41.326
63.562
67.148
1.00
30.77


ATOM
39
O
SER
76
41.948
62.501
67.126
1.00
30.49


ATOM
40
N
LYS
77
40.631
63.974
68.204
1.00
29.20


ATOM
41
CA
LYS
77
40.534
63.179
69.424
1.00
29.11


ATOM
42
CB
LYS
77
39.924
64.021
70.547
1.00
32.76


ATOM
43
CG
LYS
77
39.438
63.219
71.745
1.00
35.84


ATOM
44
CD
LYS
77
38.889
64.135
72.830
1.00
42.05


ATOM
45
CE
LYS
77
38.072
63.355
73.847
1.00
44.16


ATOM
46
NZ
LYS
77
36.868
62.741
73.208
1.00
47.21


ATOM
47
C
LYS
77
39.662
61.952
69.160
1.00
28.16


ATOM
48
O
LYS
77
39.966
60.844
69.613
1.00
25.92


ATOM
49
N
PHE
78
38.573
62.163
68.427
1.00
26.59


ATOM
50
CA
PHE
78
37.661
61.079
68.083
1.00
26.14


ATOM
51
CB
PHE
78
36.495
61.610
67.250
1.00
26.37


ATOM
52
CG
PHE
78
35.634
60.527
66.657
1.00
28.09


ATOM
53
CD1
PHE
78
34.772
59.788
67.459
1.00
27.07


ATOM
54
CD2
PHE
78
35.700
60.238
65.297
1.00
27.78


ATOM
55
CE1
PHE
78
33.983
58.776
66.916
1.00
28.93


ATOM
56
CE2
PHE
78
34.914
59.224
64.745
1.00
29.96


ATOM
57
CZ
PHE
78
34.055
58.493
65.558
1.00
27.46


ATOM
58
C
PHE
78
38.407
60.018
67.281
1.00
24.51


ATOM
59
O
PHE
78
38.293
58.825
67.555
1.00
25.03


ATOM
60
N
VAL
79
39.174
60.460
66.290
1.00
24.17


ATOM
61
CA
VAL
79
39.928
59.539
65.448
1.00
25.75


ATOM
62
CB
VAL
79
40.647
60.296
64.315
1.00
27.26


ATOM
63
CG1
VAL
79
41.588
59.362
63.574
1.00
29.96


ATOM
64
CG2
VAL
79
39.618
60.868
63.352
1.00
26.11


ATOM
65
C
VAL
79
40.944
58.732
66.255
1.00
26.10


ATOM
66
O
VAL
79
41.109
57.527
66.030
1.00
26.21


ATOM
67
N
GLU
80
41.624
59.390
67.191
1.00
25.41


ATOM
68
CA
GLU
80
42.605
58.707
68.031
1.00
26.15


ATOM
69
CB
GLU
80
43.302
59.699
68.974
1.00
30.36


ATOM
70
CG
GLU
80
44.036
60.832
68.267
1.00
34.75


ATOM
71
CD
GLU
80
44.759
61.760
69.233
1.00
39.99


ATOM
72
OE1
GLU
80
44.149
62.161
70.251
1.00
41.71


ATOM
73
OE2
GLU
80
45.934
62.096
68.971
1.00
40.92


ATOM
74
C
GLU
80
41.910
57.627
68.858
1.00
23.94


ATOM
75
O
GLU
80
42.408
56.504
68.979
1.00
22.22


ATOM
76
N
GLU
81
40.759
57.969
69.431
1.00
22.01


ATOM
77
CA
GLU
81
40.011
57.013
70.237
1.00
22.46


ATOM
78
CB
GLU
81
38.831
57.706
70.927
1.00
25.23


ATOM
79
CG
GLU
81
39.227
58.391
72.231
1.00
29.28


ATOM
80
CD
GLU
81
38.161
59.326
72.773
1.00
32.89


ATOM
81
OE1
GLU
81
36.960
58.986
72.693
1.00
34.63


ATOM
82
OE2
GLU
81
38.531
60.399
73.298
1.00
35.89


ATOM
83
C
GLU
81
39.524
55.860
69.369
1.00
21.38


ATOM
84
O
GLU
81
39.678
54.686
69.725
1.00
19.63


ATOM
85
N
TYR
82
38.948
56.197
68.220
1.00
19.43


ATOM
86
CA
TYR
82
38.461
55.179
67.303
1.00
19.72


ATOM
87
CB
TYR
82
37.927
55.832
66.024
1.00
19.77


ATOM
88
CG
TYR
82
37.545
54.837
64.951
1.00
20.35


ATOM
89
CD1
TYR
82
36.376
54.078
65.054
1.00
19.98


ATOM
90
CE1
TYR
82
36.033
53.145
64.074
1.00
20.16


ATOM
91
CD2
TYR
82
38.363
54.638
63.842
1.00
20.13


ATOM
92
CE2
TYR
82
38.033
53.708
62.858
1.00
21.53


ATOM
93
CZ
TYR
82
36.866
52.967
62.980
1.00
20.57


ATOM
94
OH
TYR
82
36.538
52.053
62.011
1.00
19.33


ATOM
95
C
TYR
82
39.581
54.201
66.940
1.00
18.48


ATOM
96
O
TYR
82
39.382
52.987
66.944
1.00
19.79


ATOM
97
N
ASP
83
40.760
54.734
66.637
1.00
20.94


ATOM
98
CA
ASP
83
41.889
53.897
66.236
1.00
23.21


ATOM
99
CB
ASP
83
43.052
54.766
65.748
1.00
25.46


ATOM
100
CG
ASP
83
44.149
53.945
65.092
1.00
31.10


ATOM
101
OD1
ASP
83
43.862
53.293
64.065
1.00
33.90


ATOM
102
OD2
ASP
83
45.293
53.941
65.597
1.00
31.88


ATOM
103
C
ASP
83
42.398
52.937
67.307
1.00
23.85


ATOM
104
O
ASP
83
42.600
51.751
67.037
1.00
23.74


ATOM
105
N
ARG
84
42.617
53.431
68.521
1.00
23.48


ATOM
106
CA
ARG
84
43.117
52.548
69.565
1.00
24.21


ATOM
107
CB
ARG
84
43.576
53.351
70.792
1.00
25.95


ATOM
108
CG
ARG
84
42.574
54.331
71.350
1.00
28.39


ATOM
109
CD
ARG
84
43.155
55.060
72.557
1.00
29.91


ATOM
110
NE
ARG
84
44.269
55.945
72.220
1.00
28.71


ATOM
111
CZ
ARG
84
44.211
57.273
72.280
1.00
29.24


ATOM
112
NH1
ARG
84
43.093
57.877
72.660
1.00
28.18


ATOM
113
NH2
ARG
84
45.278
58.001
71.982
1.00
30.94


ATOM
114
C
ARG
84
42.107
51.474
69.959
1.00
22.21


ATOM
115
O
ARG
84
42.489
50.332
70.192
1.00
20.72


ATOM
116
N
THR
85
40.824
51.823
70.010
1.00
20.97


ATOM
117
CA
THR
85
39.796
50.845
70.365
1.00
21.86


ATOM
118
CB
THR
85
38.457
51.528
70.752
1.00
22.90


ATOM
119
OG1
THR
85
37.996
52.349
69.673
1.00
24.14


ATOM
120
CG2
THR
85
38.637
52.389
72.006
1.00
22.66


ATOM
121
C
THR
85
39.531
49.853
69.227
1.00
22.63


ATOM
122
O
THR
85
39.271
48.671
69.468
1.00
23.06


ATOM
123
N
SER
86
39.597
50.331
67.988
1.00
22.84


ATOM
124
CA
SER
86
39.364
49.467
66.833
1.00
23.43


ATOM
125
CB
SER
86
39.358
50.290
65.542
1.00
20.63


ATOM
126
OG
SER
86
38.201
51.101
65.469
1.00
22.91


ATOM
127
C
SER
86
40.420
48.375
66.737
1.00
23.93


ATOM
128
O
SER
86
40.107
47.224
66.431
1.00
26.22


ATOM
129
N
GLN
87
41.671
48.739
66.996
1.00
25.11


ATOM
130
CA
GLN
87
42.764
47.777
66.934
1.00
27.65


ATOM
131
CB
GLN
87
44.076
48.441
67.349
1.00
29.31


ATOM
132
CG
GLN
87
44.611
49.434
66.340
1.00
34.89


ATOM
133
CD
GLN
87
45.901
50.079
66.797
1.00
38.51


ATOM
134
OE1
GLN
87
46.854
49.392
67.170
1.00
39.63


ATOM
135
NE2
GLN
87
45.942
51.407
66.766
1.00
40.39


ATOM
136
C
GLN
87
42.494
46.575
67.832
1.00
27.47


ATOM
137
O
GLN
87
42.700
45.430
67.430
1.00
27.09


ATOM
138
N
VAL
88
42.027
46.843
69.049
1.00
27.70


ATOM
139
CA
VAL
88
41.732
45.784
70.009
1.00
27.09


ATOM
140
CB
VAL
88
41.457
46.363
71.418
1.00
28.38


ATOM
141
CG1
VAL
88
41.137
45.231
72.392
1.00
28.68


ATOM
142
CG2
VAL
88
42.666
47.156
71.902
1.00
28.04


ATOM
143
C
VAL
88
40.531
44.933
69.597
1.00
26.88


ATOM
144
O
VAL
88
40.628
43.711
69.537
1.00
26.76


ATOM
145
N
VAL
89
39.403
45.577
69.318
1.00
25.88


ATOM
146
CA
VAL
89
38.199
44.852
68.928
1.00
26.99


ATOM
147
CB
VAL
89
36.985
45.813
68.803
1.00
27.18


ATOM
148
CG1
VAL
89
37.315
46.950
67.862
1.00
32.87


ATOM
149
CG2
VAL
89
35.765
45.060
68.306
1.00
31.36


ATOM
150
C
VAL
89
38.375
44.071
67.616
1.00
27.29


ATOM
151
O
VAL
89
37.906
42.937
67.497
1.00
25.50


ATOM
152
N
TRP
90
39.048
44.674
66.637
1.00
26.45


ATOM
153
CA
TRP
90
39.273
44.010
65.354
1.00
27.47


ATOM
154
CB
TRP
90
39.817
45.003
64.325
1.00
29.71


ATOM
155
CG
TRP
90
38.809
46.020
63.873
1.00
33.63


ATOM
156
CD2
TRP
90
38.891
46.847
62.707
1.00
35.80


ATOM
157
CE2
TRP
90
37.752
47.684
62.707
1.00
37.41


ATOM
158
CE3
TRP
90
39.817
46.965
61.663
1.00
37.42


ATOM
159
CD1
TRP
90
37.656
46.375
64.513
1.00
34.94


ATOM
160
NE1
TRP
90
37.015
47.373
63.819
1.00
36.40


ATOM
161
CZ2
TRP
90
37.514
48.629
61.700
1.00
38.33


ATOM
162
CZ3
TRP
90
39.582
47.906
60.661
1.00
39.67


ATOM
163
CH2
TRP
90
38.437
48.726
60.690
1.00
40.02


ATOM
164
C
TRP
90
40.243
42.846
65.510
1.00
27.07


ATOM
165
O
TRP
90
40.121
41.831
64.824
1.00
27.40


ATOM
166
N
ASN
91
41.210
42.991
66.409
1.00
25.74


ATOM
167
CA
ASN
91
42.167
41.920
66.634
1.00
26.47


ATOM
168
CB
ASN
91
43.271
42.364
67.597
1.00
26.15


ATOM
169
CG
ASN
91
44.156
41.212
68.033
1.00
29.44


ATOM
170
OD1
ASN
91
43.840
40.502
68.987
1.00
30.76


ATOM
171
ND2
ASN
91
45.261
41.005
67.319
1.00
28.75


ATOM
172
C
ASN
91
41.442
40.705
67.196
1.00
27.08


ATOM
173
O
ASN
91
41.697
39.574
66.780
1.00
26.40


ATOM
174
N
GLU
92
40.533
40.942
68.138
1.00
26.14


ATOM
175
CA
GLU
92
39.768
39.858
68.734
1.00
27.35


ATOM
176
CB
GLU
92
38.906
40.378
69.888
1.00
30.98


ATOM
177
CG
GLU
92
39.643
40.460
71.214
1.00
37.75


ATOM
178
CD
GLU
92
38.847
41.182
72.288
1.00
40.97


ATOM
179
OE1
GLU
92
37.654
40.855
72.466
1.00
43.05


ATOM
180
OE2
GLU
92
39.421
42.070
72.955
1.00
41.95


ATOM
181
C
GLU
92
38.881
39.174
67.705
1.00
25.71


ATOM
182
O
GLU
92
38.777
37.952
67.689
1.00
25.50


ATOM
183
N
TYR
93
38.238
39.961
66.849
1.00
25.38


ATOM
184
CA
TYR
93
37.367
39.396
65.825
1.00
25.52


ATOM
185
CB
TYR
93
36.693
40.503
65.012
1.00
25.32


ATOM
186
CG
TYR
93
35.790
39.961
63.929
1.00
28.08


ATOM
187
CD1
TYR
93
34.578
39.348
64.248
1.00
28.32


ATOM
188
CE1
TYR
93
33.761
38.804
63.260
1.00
31.75


ATOM
189
CD2
TYR
93
36.165
40.021
62.588
1.00
29.39


ATOM
190
CE2
TYR
93
35.355
39.477
61.589
1.00
33.01


ATOM
191
CZ
TYR
93
34.155
38.872
61.933
1.00
33.10


ATOM
192
OH
TYR
93
33.354
38.334
60.952
1.00
36.34


ATOM
193
C
TYR
93
38.161
38.501
64.878
1.00
23.80


ATOM
194
O
TYR
93
37.725
37.404
64.528
1.00
24.56


ATOM
195
N
ALA
94
39.325
38.984
64.461
1.00
23.33


ATOM
196
CA
ALA
94
40.184
38.241
63.552
1.00
24.84


ATOM
197
CB
ALA
94
41.461
39.034
63.274
1.00
22.84


ATOM
198
C
ALA
94
40.526
36.876
64.143
1.00
24.40


ATOM
199
O
ALA
94
40.589
35.876
63.427
1.00
23.49


ATOM
200
N
ALA
95
40.739
36.840
65.454
1.00
25.55


ATOM
201
CA
ALA
95
41.069
35.593
66.136
1.00
25.36


ATOM
202
CB
ALA
95
41.361
35.864
67.609
1.00
30.67


ATOM
203
C
ALA
95
39.928
34.593
66.007
1.00
24.83


ATOM
204
O
ALA
95
40.138
33.440
65.630
1.00
26.02


ATOM
205
N
ALA
96
38.718
35.038
66.326
1.00
23.74


ATOM
206
CA
ALA
96
37.547
34.177
66.244
1.00
23.43


ATOM
207
CB
ALA
96
36.329
34.904
66.794
1.00
22.21


ATOM
208
C
ALA
96
37.284
33.742
64.803
1.00
23.35


ATOM
209
O
ALA
96
36.934
32.589
64.545
1.00
22.60


ATOM
210
N
ASN
97
37.451
34.673
63.870
1.00
21.81


ATOM
211
CA
ASN
97
37.224
34.389
62.456
1.00
22.42


ATOM
212
CB
ASN
97
37.308
35.695
61.651
1.00
21.62


ATOM
213
CG
ASN
97
36.768
35.553
60.241
1.00
22.75


ATOM
214
OD1
ASN
97
35.968
34.660
59.955
1.00
22.10


ATOM
215
ND2
ASN
97
37.186
36.450
59.356
1.00
21.12


ATOM
216
C
ASN
97
38.257
33.373
61.965
1.00
21.42


ATOM
217
O
ASN
97
37.941
32.480
61.183
1.00
22.56


ATOM
218
N
TRP
98
39.490
33.502
62.447
1.00
22.34


ATOM
219
CA
TRP
98
40.552
32.585
62.059
1.00
22.66


ATOM
220
CB
TRP
98
41.901
33.085
62.583
1.00
22.16


ATOM
221
CG
TRP
98
43.016
32.098
62.384
1.00
23.43


ATOM
222
CD2
TRP
98
43.883
32.003
61.246
1.00
22.99


ATOM
223
CE2
TRP
98
44.749
30.907
61.470
1.00
24.37


ATOM
224
CE3
TRP
98
44.010
32.735
60.055
1.00
21.19


ATOM
225
CD1
TRP
98
43.381
31.086
63.229
1.00
25.02


ATOM
226
NE1
TRP
98
44.421
30.365
62.686
1.00
25.09


ATOM
227
CZ2
TRP
98
45.733
30.526
60.547
1.00
23.12


ATOM
228
CZ3
TRP
98
44.989
32.354
59.134
1.00
21.49


ATOM
229
CH2
TRP
98
45.837
31.258
59.389
1.00
20.86


ATOM
230
C
TRP
98
40.286
31.170
62.578
1.00
23.96


ATOM
231
O
TRP
98
40.444
30.190
61.840
1.00
22.16


ATOM
232
N
ASN
99
39.876
31.071
63.841
1.00
24.47


ATOM
233
CA
ASN
99
39.596
29.770
64.455
1.00
26.36


ATOM
234
CB
ASN
99
39.230
29.936
65.937
1.00
27.31


ATOM
235
CG
ASN
99
40.368
30.524
66.760
1.00
29.77


ATOM
236
OD1
ASN
99
41.537
30.432
66.382
1.00
28.77


ATOM
237
ND2
ASN
99
40.028
31.119
67.899
1.00
30.82


ATOM
238
C
ASN
99
38.480
29.026
63.724
1.00
25.35


ATOM
239
O
ASN
99
38.523
27.802
63.588
1.00
23.96


ATOM
240
N
TYR
100
37.477
29.762
63.258
1.00
24.11


ATOM
241
CA
TYR
100
36.380
29.145
62.518
1.00
24.41


ATOM
242
CB
TYR
100
35.242
30.153
62.308
1.00
27.59


ATOM
243
CG
TYR
100
34.348
29.829
61.127
1.00
28.29


ATOM
244
CD1
TYR
100
33.375
28.834
61.209
1.00
30.33


ATOM
245
CE1
TYR
100
32.581
28.505
60.101
1.00
29.75


ATOM
246
CD2
TYR
100
34.508
30.494
59.912
1.00
31.13


ATOM
247
CE2
TYR
100
33.725
30.174
58.800
1.00
31.87


ATOM
248
CZ
TYR
100
32.765
29.180
58.902
1.00
32.09


ATOM
249
OH
TYR
100
31.995
28.868
57.799
1.00
31.48


ATOM
250
C
TYR
100
36.892
28.674
61.157
1.00
24.55


ATOM
251
O
TYR
100
36.698
27.521
60.770
1.00
23.28


ATOM
252
N
ASN
101
37.538
29.588
60.436
1.00
22.98


ATOM
253
CA
ASN
101
38.083
29.312
59.111
1.00
21.52


ATOM
254
CB
ASN
101
38.799
30.555
58.573
1.00
22.42


ATOM
255
CG
ASN
101
37.883
31.452
57.766
1.00
20.70


ATOM
256
OD1
ASN
101
37.843
31.369
56.541
1.00
20.36


ATOM
257
ND2
ASN
101
37.131
32.307
58.452
1.00
20.18


ATOM
258
C
ASN
101
39.048
28.130
59.074
1.00
22.49


ATOM
259
O
ASN
101
39.092
27.398
58.085
1.00
22.22


ATOM
260
N
THR
102
39.821
27.953
60.144
1.00
21.87


ATOM
261
CA
THR
102
40.799
26.866
60.209
1.00
23.29


ATOM
262
CB
THR
102
42.153
27.364
60.773
1.00
22.46


ATOM
263
OG1
THR
102
41.985
27.779
62.132
1.00
21.26


ATOM
264
CG2
THR
102
42.675
28.544
59.956
1.00
22.88


ATOM
265
C
THR
102
40.332
25.682
61.055
1.00
25.33


ATOM
266
O
THR
102
41.100
24.755
61.312
1.00
26.63


ATOM
267
N
ASN
103
39.073
25.709
61.478
1.00
26.22


ATOM
268
CA
ASN
103
38.513
24.633
62.293
1.00
27.70


ATOM
269
CB
ASN
103
39.154
24.648
63.691
1.00
28.15


ATOM
270
CG
ASN
103
38.674
23.499
64.576
1.00
31.04


ATOM
271
OD1
ASN
103
38.244
22.457
64.074
1.00
29.17


ATOM
272
ND2
ASN
103
38.761
23.701
65.892
1.00
32.86


ATOM
273
C
ASN
103
37.005
24.834
62.382
1.00
26.39


ATOM
274
O
ASN
103
36.486
25.297
63.395
1.00
28.11


ATOM
275
N
ILE
104
36.312
24.487
61.304
1.00
27.62


ATOM
276
CA
ILE
104
34.864
24.640
61.225
1.00
28.58


ATOM
277
CB
ILE
104
34.370
24.456
59.770
1.00
28.41


ATOM
278
CG2
ILE
104
32.849
24.581
59.710
1.00
29.27


ATOM
279
CG1
ILE
104
35.032
25.498
58.861
1.00
28.67


ATOM
280
CD1
ILE
104
34.674
25.359
57.387
1.00
27.85


ATOM
281
C
ILE
104
34.128
23.655
62.127
1.00
30.90


ATOM
282
O
ILE
104
34.063
22.460
61.839
1.00
31.19


ATOM
283
N
THR
105
33.579
24.171
63.222
1.00
32.51


ATOM
284
CA
THR
105
32.831
23.360
64.177
1.00
33.92


ATOM
285
CB
THR
105
33.688
22.982
65.399
1.00
34.56


ATOM
286
OG1
THR
105
34.015
24.169
66.133
1.00
35.94


ATOM
287
CG2
THR
105
34.972
22.284
64.965
1.00
33.74


ATOM
288
C
THR
105
31.649
24.176
64.677
1.00
34.62


ATOM
289
O
THR
105
31.575
25.384
64.450
1.00
34.35


ATOM
290
N
THR
106
30.722
23.518
65.360
1.00
34.69


ATOM
291
CA
THR
106
29.564
24.220
65.889
1.00
35.91


ATOM
292
CB
THR
106
28.546
23.229
66.510
1.00
36.94


ATOM
293
OG1
THR
106
27.453
23.956
67.085
1.00
40.00


ATOM
294
CG2
THR
106
29.205
22.386
67.582
1.00
36.78


ATOM
295
C
THR
106
30.041
25.219
66.945
1.00
35.21


ATOM
296
O
THR
106
29.499
26.318
67.069
1.00
34.43


ATOM
297
N
GLU
107
31.084
24.840
67.679
1.00
35.12


ATOM
298
CA
GLU
107
31.638
25.692
68.725
1.00
35.53


ATOM
299
CB
GLU
107
32.640
24.905
69.576
1.00
38.54


ATOM
300
CG
GLU
107
32.084
23.613
70.185
1.00
44.28


ATOM
301
CD
GLU
107
32.317
22.385
69.310
1.00
47.02


ATOM
302
OE1
GLU
107
31.828
22.356
68.161
1.00
48.87


ATOM
303
OE2
GLU
107
32.998
21.444
69.775
1.00
50.21


ATOM
304
C
GLU
107
32.309
26.957
68.180
1.00
34.45


ATOM
305
O
GLU
107
32.003
28.066
68.623
1.00
32.19


ATOM
306
N
THR
108
33.227
26.796
67.229
1.00
33.18


ATOM
307
CA
THR
108
33.913
27.949
66.651
1.00
32.17


ATOM
308
CB
THR
108
35.048
27.527
65.687
1.00
31.68


ATOM
309
OG1
THR
108
34.528
26.660
64.673
1.00
31.48


ATOM
310
CG2
THR
108
36.157
26.818
66.452
1.00
31.84


ATOM
311
C
THR
108
32.925
28.834
65.897
1.00
31.26


ATOM
312
O
THR
108
33.107
30.045
65.815
1.00
30.78


ATOM
313
N
SER
109
31.878
28.228
65.347
1.00
31.59


ATOM
314
CA
SER
109
30.865
28.989
64.623
1.00
32.27


ATOM
315
CB
SER
109
29.888
28.054
63.905
1.00
32.03


ATOM
316
OG
SER
109
30.511
27.388
62.819
1.00
33.62


ATOM
317
C
SER
109
30.094
29.863
65.602
1.00
33.27


ATOM
318
O
SER
109
29.871
31.046
65.352
1.00
31.52


ATOM
319
N
LYS
110
29.695
29.268
66.722
1.00
34.58


ATOM
320
CA
LYS
110
28.943
29.985
67.741
1.00
36.62


ATOM
321
CB
LYS
110
28.570
29.031
68.880
1.00
39.13


ATOM
322
CG
LYS
110
27.494
29.561
69.819
1.00
43.25


ATOM
323
CD
LYS
110
27.052
28.487
70.807
1.00
46.60


ATOM
324
CE
LYS
110
25.859
28.943
71.639
1.00
48.32


ATOM
325
NZ
LYS
110
25.369
27.861
72.547
1.00
49.35


ATOM
326
C
LYS
110
29.755
31.162
68.279
1.00
35.77


ATOM
327
O
LYS
110
29.234
32.264
68.449
1.00
36.40


ATOM
328
N
ILE
111
31.037
30.927
68.535
1.00
34.36


ATOM
329
CA
ILE
111
31.909
31.974
69.054
1.00
33.18


ATOM
330
CB
ILE
111
33.296
31.410
69.408
1.00
33.61


ATOM
331
CG2
ILE
111
34.226
32.537
69.837
1.00
33.24


ATOM
332
CG1
ILE
111
33.154
30.364
70.517
1.00
34.16


ATOM
333
CD1
ILE
111
34.458
29.696
70.907
1.00
33.43


ATOM
334
C
ILE
111
32.073
33.107
68.044
1.00
32.41


ATOM
335
O
ILE
111
32.075
34.284
68.410
1.00
32.05


ATOM
336
N
LEU
112
32.212
32.749
66.772
1.00
30.05


ATOM
337
CA
LEU
112
32.364
33.752
65.731
1.00
28.87


ATOM
338
CB
LEU
112
32.591
33.084
64.371
1.00
28.19


ATOM
339
CG
LEU
112
32.709
34.015
63.157
1.00
28.67


ATOM
340
CD1
LEU
112
33.778
35.063
63.405
1.00
28.05


ATOM
341
CD2
LEU
112
33.035
33.198
61.918
1.00
27.39


ATOM
342
C
LEU
112
31.127
34.645
65.672
1.00
28.87


ATOM
343
O
LEU
112
31.243
35.867
65.612
1.00
27.96


ATOM
344
N
LEU
113
29.942
34.040
65.700
1.00
28.83


ATOM
345
CA
LEU
113
28.710
34.821
65.641
1.00
29.55


ATOM
346
CB
LEU
113
27.488
33.897
65.581
1.00
28.66


ATOM
347
CG
LEU
113
27.358
33.047
64.313
1.00
27.25


ATOM
348
CD1
LEU
113
26.146
32.144
64.423
1.00
28.60


ATOM
349
CD2
LEU
113
27.238
33.955
63.090
1.00
29.42


ATOM
350
C
LEU
113
28.595
35.772
66.827
1.00
30.99


ATOM
351
O
LEU
113
28.035
36.861
66.703
1.00
30.68


ATOM
352
N
GLN
114
29.134
35.364
67.973
1.00
32.59


ATOM
353
CA
GLN
114
29.096
36.205
69.164
1.00
34.05


ATOM
354
CB
GLN
114
29.461
35.393
70.414
1.00
35.86


ATOM
355
CG
GLN
114
28.397
34.363
70.797
1.00
41.83


ATOM
356
CD
GLN
114
28.802
33.483
71.970
1.00
44.71


ATOM
357
OE1
GLN
114
29.028
33.966
73.080
1.00
47.69


ATOM
358
NE2
GLN
114
28.892
32.180
71.726
1.00
47.51


ATOM
359
C
GLN
114
30.056
37.375
68.992
1.00
33.41


ATOM
360
O
GLN
114
29.746
38.500
69.380
1.00
33.15


ATOM
361
N
LYS
115
31.222
37.114
68.409
1.00
33.19


ATOM
362
CA
LYS
115
32.194
38.177
68.185
1.00
33.34


ATOM
363
CB
LYS
115
33.527
37.604
67.695
1.00
35.03


ATOM
364
CG
LYS
115
34.397
37.022
68.802
1.00
39.16


ATOM
365
CD
LYS
115
34.872
38.111
69.757
1.00
41.08


ATOM
366
CE
LYS
115
35.682
37.534
70.912
1.00
43.92


ATOM
367
NZ
LYS
115
36.142
38.597
71.855
1.00
43.32


ATOM
368
C
LYS
115
31.655
39.180
67.172
1.00
32.53


ATOM
369
O
LYS
115
32.033
40.351
67.192
1.00
30.99


ATOM
370
N
ASN
116
30.779
38.717
66.283
1.00
33.42


ATOM
371
CA
ASN
116
30.180
39.597
65.279
1.00
34.57


ATOM
372
CB
ASN
116
29.219
38.820
64.368
1.00
36.23


ATOM
373
CG
ASN
116
29.938
37.996
63.314
1.00
37.73


ATOM
374
OD1
ASN
116
30.671
38.530
62.479
1.00
37.42


ATOM
375
ND2
ASN
116
29.719
36.685
63.340
1.00
41.84


ATOM
376
C
ASN
116
29.404
40.694
66.001
1.00
34.49


ATOM
377
O
ASN
116
29.531
41.874
65.683
1.00
33.34


ATOM
378
N
MET
117
28.597
40.286
66.975
1.00
34.71


ATOM
379
CA
MET
117
27.794
41.217
67.757
1.00
36.39


ATOM
380
CB
MET
117
26.943
40.448
68.772
1.00
39.17


ATOM
381
CG
MET
117
25.518
40.138
68.319
1.00
43.08


ATOM
382
SD
MET
117
25.294
40.020
66.531
1.00
49.27


ATOM
383
CE
MET
117
23.829
41.035
66.302
1.00
47.42


ATOM
384
C
MET
117
28.670
42.228
68.488
1.00
35.39


ATOM
385
O
MET
117
28.320
43.402
68.590
1.00
34.85


ATOM
386
N
GLN
118
29.814
41.772
68.989
1.00
34.91


ATOM
387
CA
GLN
118
30.722
42.648
69.719
1.00
35.11


ATOM
388
CB
GLN
118
31.818
41.826
70.405
1.00
38.55


ATOM
389
CG
GLN
118
31.278
40.731
71.319
1.00
44.24


ATOM
390
CD
GLN
118
32.340
40.138
72.229
1.00
47.30


ATOM
391
OE1
GLN
118
33.397
39.702
71.771
1.00
49.53


ATOM
392
NE2
GLN
118
32.060
40.115
73.528
1.00
47.80


ATOM
393
C
GLN
118
31.352
43.714
68.831
1.00
32.85


ATOM
394
O
GLN
118
31.371
44.895
69.188
1.00
31.35


ATOM
395
N
ILE
119
31.869
43.308
67.676
1.00
29.57


ATOM
396
CA
ILE
119
32.492
44.269
66.776
1.00
28.83


ATOM
397
CB
ILE
119
33.274
43.563
65.644
1.00
29.00


ATOM
398
CG2
ILE
119
32.319
42.794
64.742
1.00
29.58


ATOM
399
CG1
ILE
119
34.063
44.599
64.844
1.00
31.09


ATOM
400
CD1
ILE
119
35.045
43.992
63.864
1.00
33.97


ATOM
401
C
ILE
119
31.435
45.195
66.179
1.00
26.91


ATOM
402
O
ILE
119
31.709
46.358
65.872
1.00
25.48


ATOM
403
N
ALA
120
30.220
44.683
66.024
1.00
25.38


ATOM
404
CA
ALA
120
29.135
45.492
65.482
1.00
26.14


ATOM
405
CB
ALA
120
27.918
44.623
65.202
1.00
24.25


ATOM
406
C
ALA
120
28.790
46.568
66.509
1.00
25.83


ATOM
407
O
ALA
120
28.566
47.727
66.165
1.00
25.53


ATOM
408
N
ASN
121
28.755
46.178
67.778
1.00
25.13


ATOM
409
CA
ASN
121
28.443
47.131
68.834
1.00
25.64


ATOM
410
CB
ASN
121
28.407
46.426
70.191
1.00
28.05


ATOM
411
CG
ASN
121
27.945
47.341
71.304
1.00
33.48


ATOM
412
OD1
ASN
121
28.666
48.256
71.704
1.00
37.03


ATOM
413
ND2
ASN
121
26.732
47.107
71.797
1.00
35.02


ATOM
414
C
ASN
121
29.474
48.256
68.843
1.00
23.48


ATOM
415
O
ASN
121
29.131
49.421
69.052
1.00
24.86


ATOM
416
N
HIS
122
30.735
47.910
68.603
1.00
21.49


ATOM
417
CA
HIS
122
31.799
48.908
68.565
1.00
21.72


ATOM
418
CB
HIS
122
33.171
48.227
68.499
1.00
21.96


ATOM
419
CG
HIS
122
34.297
49.165
68.190
1.00
23.78


ATOM
420
CD2
HIS
122
35.094
49.902
69.002
1.00
22.69


ATOM
421
ND1
HIS
122
34.694
49.456
66.901
1.00
25.06


ATOM
422
CE1
HIS
122
35.684
50.330
66.934
1.00
24.61


ATOM
423
NE2
HIS
122
35.946
50.618
68.197
1.00
22.29


ATOM
424
C
HIS
122
31.624
49.822
67.354
1.00
22.77


ATOM
425
O
HIS
122
31.801
51.041
67.445
1.00
21.87


ATOM
426
N
THR
123
31.278
49.224
66.218
1.00
20.58


ATOM
427
CA
THR
123
31.083
49.979
64.987
1.00
21.80


ATOM
428
CB
THR
123
30.823
49.034
63.795
1.00
22.75


ATOM
429
OG1
THR
123
31.945
48.155
63.632
1.00
22.95


ATOM
430
CG2
THR
123
30.618
49.832
62.509
1.00
23.24


ATOM
431
C
THR
123
29.905
50.940
65.128
1.00
21.91


ATOM
432
O
THR
123
29.972
52.085
64.692
1.00
21.95


ATOM
433
N
LEU
124
28.829
50.468
65.747
1.00
23.43


ATOM
434
CA
LEU
124
27.643
51.291
65.945
1.00
24.99


ATOM
435
CB
LEU
124
26.538
50.458
66.590
1.00
27.24


ATOM
436
CG
LEU
124
25.215
51.170
66.870
1.00
29.20


ATOM
437
CD1
LEU
124
24.575
51.621
65.556
1.00
31.28


ATOM
438
CD2
LEU
124
24.294
50.228
67.622
1.00
30.06


ATOM
439
C
LEU
124
27.953
52.501
66.830
1.00
25.57


ATOM
440
O
LEU
124
27.559
53.628
66.526
1.00
23.70


ATOM
441
N
LYS
125
28.664
52.256
67.924
1.00
24.93


ATOM
442
CA
LYS
125
29.018
53.316
68.855
1.00
26.17


ATOM
443
CB
LYS
125
29.818
52.747
70.026
1.00
27.56


ATOM
444
CG
LYS
125
30.174
53.788
71.072
1.00
32.44


ATOM
445
CD
LYS
125
31.157
53.249
72.093
1.00
34.92


ATOM
446
CE
LYS
125
31.464
54.302
73.144
1.00
38.23


ATOM
447
NZ
LYS
125
31.907
55.587
72.522
1.00
40.02


ATOM
448
C
LYS
125
29.830
54.422
68.192
1.00
25.74


ATOM
449
O
LYS
125
29.455
55.593
68.244
1.00
25.50


ATOM
450
N
TYR
126
30.948
54.053
67.575
1.00
23.64


ATOM
451
CA
TYR
126
31.793
55.044
66.930
1.00
23.63


ATOM
452
CB
TYR
126
33.193
54.477
66.688
1.00
23.98


ATOM
453
CG
TYR
126
34.005
54.436
67.961
1.00
24.33


ATOM
454
CD1
TYR
126
33.877
53.380
68.865
1.00
24.10


ATOM
455
CE1
TYR
126
34.539
53.401
70.094
1.00
24.70


ATOM
456
CD2
TYR
126
34.822
55.509
68.314
1.00
25.19


ATOM
457
CE2
TYR
126
35.484
55.540
69.534
1.00
25.45


ATOM
458
CZ
TYR
126
35.337
54.489
70.420
1.00
24.76


ATOM
459
OH
TYR
126
35.971
54.545
71.640
1.00
26.84


ATOM
460
C
TYR
126
31.199
55.594
65.644
1.00
23.81


ATOM
461
O
TYR
126
31.426
56.756
65.303
1.00
24.01


ATOM
462
N
GLY
127
30.426
54.764
64.945
1.00
23.08


ATOM
463
CA
GLY
127
29.791
55.198
63.713
1.00
22.50


ATOM
464
C
GLY
127
28.741
56.255
63.994
1.00
23.32


ATOM
465
O
GLY
127
28.616
57.237
63.259
1.00
21.48


ATOM
466
N
THR
128
27.981
56.050
65.066
1.00
24.15


ATOM
467
CA
THR
128
26.945
56.996
65.468
1.00
25.03


ATOM
468
CB
THR
128
26.166
56.474
66.687
1.00
24.73


ATOM
469
OG1
THR
128
25.558
55.221
66.357
1.00
25.50


ATOM
470
CG2
THR
128
25.088
57.468
67.103
1.00
23.72


ATOM
471
C
THR
128
27.601
58.332
65.821
1.00
25.94


ATOM
472
O
THR
128
27.138
59.390
65.397
1.00
26.44


ATOM
473
N
GLN
129
28.680
58.275
66.597
1.00
27.23


ATOM
474
CA
GLN
129
29.408
59.481
66.980
1.00
28.25


ATOM
475
CB
GLN
129
30.587
59.138
67.901
1.00
32.26


ATOM
476
CG
GLN
129
30.285
59.178
69.396
1.00
38.49


ATOM
477
CD
GLN
129
31.487
58.779
70.249
1.00
42.52


ATOM
478
OE1
GLN
129
31.786
57.594
70.412
1.00
44.86


ATOM
479
NE2
GLN
129
32.187
59.772
70.787
1.00
45.22


ATOM
480
C
GLN
129
29.943
60.182
65.737
1.00
27.53


ATOM
481
O
GLN
129
29.824
61.399
65.601
1.00
26.41


ATOM
482
N
ALA
130
30.531
59.405
64.831
1.00
25.80


ATOM
483
CA
ALA
130
31.104
59.944
63.600
1.00
24.69


ATOM
484
CB
ALA
130
31.699
58.810
62.766
1.00
25.45


ATOM
485
C
ALA
130
30.100
60.729
62.757
1.00
25.28


ATOM
486
O
ALA
130
30.448
61.739
62.141
1.00
24.63


ATOM
487
N
ARG
131
28.860
60.256
62.723
1.00
24.09


ATOM
488
CA
ARG
131
27.819
60.908
61.945
1.00
26.32


ATOM
489
CB
ARG
131
26.600
59.994
61.836
1.00
25.28


ATOM
490
CG
ARG
131
26.859
58.750
61.015
1.00
26.20


ATOM
491
CD
ARG
131
25.613
57.904
60.897
1.00
26.32


ATOM
492
NE
ARG
131
25.805
56.792
59.972
1.00
25.16


ATOM
493
CZ
ARG
131
24.853
55.925
59.648
1.00
26.49


ATOM
494
NH1
ARG
131
23.640
56.041
60.180
1.00
25.08


ATOM
495
NH2
ARG
131
25.108
54.953
58.780
1.00
27.31


ATOM
496
C
ARG
131
27.398
62.254
62.519
1.00
27.69


ATOM
497
O
ARG
131
26.722
63.033
61.848
1.00
27.22


ATOM
498
N
LYS
132
27.792
62.524
63.758
1.00
28.78


ATOM
499
CA
LYS
132
27.444
63.785
64.397
1.00
31.07


ATOM
500
CB
LYS
132
27.480
63.629
65.920
1.00
32.98


ATOM
501
CG
LYS
132
26.404
62.682
66.437
1.00
37.31


ATOM
502
CD
LYS
132
26.517
62.422
67.931
1.00
40.01


ATOM
503
CE
LYS
132
25.419
61.469
68.386
1.00
42.18


ATOM
504
NZ
LYS
132
25.551
61.088
69.821
1.00
44.23


ATOM
505
C
LYS
132
28.371
64.906
63.946
1.00
30.99


ATOM
506
O
LYS
132
28.104
66.082
64.194
1.00
30.45


ATOM
507
N
PHE
133
29.461
64.543
63.278
1.00
31.38


ATOM
508
CA
PHE
133
30.401
65.542
62.776
1.00
32.92


ATOM
509
CB
PHE
133
31.825
64.980
62.665
1.00
32.55


ATOM
510
CG
PHE
133
32.531
64.825
63.977
1.00
32.74


ATOM
511
CD1
PHE
133
32.357
63.682
64.746
1.00
33.65


ATOM
512
CD2
PHE
133
33.376
65.828
64.444
1.00
34.44


ATOM
513
CE1
PHE
133
33.017
63.535
65.965
1.00
35.01


ATOM
514
CE2
PHE
133
34.041
65.695
65.664
1.00
34.23


ATOM
515
CZ
PHE
133
33.861
64.546
66.425
1.00
35.80


ATOM
516
C
PHE
133
29.970
65.978
61.390
1.00
33.66


ATOM
517
O
PHE
133
29.487
65.165
60.601
1.00
33.46


ATOM
518
N
ASP
134
30.136
67.262
61.095
1.00
34.13


ATOM
519
CA
ASP
134
29.804
67.769
59.772
1.00
34.82


ATOM
520
CB
ASP
134
29.286
69.209
59.836
1.00
35.44


ATOM
521
CG
ASP
134
28.831
69.724
58.477
1.00
35.56


ATOM
522
OD1
ASP
134
29.439
69.336
57.459
1.00
36.13


ATOM
523
OD2
ASP
134
27.873
70.522
58.425
1.00
36.65


ATOM
524
C
ASP
134
31.121
67.737
59.014
1.00
34.27


ATOM
525
O
ASP
134
31.909
68.677
59.089
1.00
34.87


ATOM
526
N
VAL
135
31.361
66.644
58.298
1.00
35.15


ATOM
527
CA
VAL
135
32.595
66.478
57.540
1.00
35.95


ATOM
528
CB
VAL
135
32.530
65.218
56.657
1.00
36.58


ATOM
529
CG1
VAL
135
33.794
65.095
55.833
1.00
37.87


ATOM
530
CG2
VAL
135
32.355
63.988
57.530
1.00
36.85


ATOM
531
C
VAL
135
32.915
67.682
56.660
1.00
36.83


ATOM
532
O
VAL
135
34.084
67.983
56.415
1.00
36.31


ATOM
533
N
ASN
136
31.880
68.371
56.189
1.00
37.34


ATOM
534
CA
ASN
136
32.077
69.540
55.340
1.00
39.98


ATOM
535
CB
ASN
136
30.729
70.105
54.873
1.00
39.64


ATOM
536
CG
ASN
136
29.961
69.138
53.996
1.00
40.40


ATOM
537
OD1
ASN
136
30.488
68.633
53.004
1.00
39.43


ATOM
538
ND2
ASN
136
28.703
68.879
54.354
1.00
39.64


ATOM
539
C
ASN
136
32.851
70.639
56.061
1.00
41.21


ATOM
540
O
ASN
136
33.593
71.396
55.437
1.00
42.44


ATOM
541
N
GLN
137
32.684
70.716
57.377
1.00
42.26


ATOM
542
CA
GLN
137
33.354
71.741
58.173
1.00
43.46


ATOM
543
CB
GLN
137
32.486
72.104
59.381
1.00
44.53


ATOM
544
CG
GLN
137
31.077
72.557
59.023
1.00
47.29


ATOM
545
CD
GLN
137
31.064
73.786
58.130
1.00
49.81


ATOM
546
OE1
GLN
137
31.620
74.830
58.480
1.00
51.43


ATOM
547
NE2
GLN
137
30.424
73.668
56.971
1.00
50.55


ATOM
548
C
GLN
137
34.755
71.355
58.648
1.00
43.13


ATOM
549
O
GLN
137
35.518
72.209
59.101
1.00
42.91


ATOM
550
N
LEU
138
35.096
70.074
58.549
1.00
43.61


ATOM
551
CA
LEU
138
36.411
69.608
58.983
1.00
43.43


ATOM
552
CB
LEU
138
36.432
68.078
59.043
1.00
43.64


ATOM
553
CG
LEU
138
36.358
67.475
60.451
1.00
44.21


ATOM
554
CD1
LEU
138
35.308
68.189
61.286
1.00
44.64


ATOM
555
CD2
LEU
138
36.049
65.994
60.349
1.00
44.83


ATOM
556
C
LEU
138
37.530
70.124
58.087
1.00
43.49


ATOM
557
O
LEU
138
37.443
70.055
56.862
1.00
43.96


ATOM
558
N
GLN
139
38.585
70.635
58.716
1.00
43.92


ATOM
559
CA
GLN
139
39.729
71.199
58.005
1.00
44.02


ATOM
560
CB
GLN
139
40.392
72.275
58.867
1.00
46.53


ATOM
561
CG
GLN
139
40.683
73.572
58.137
1.00
49.82


ATOM
562
CD
GLN
139
39.418
74.318
57.762
1.00
52.02


ATOM
563
OE1
GLN
139
38.581
73.813
57.012
1.00
53.40


ATOM
564
NE2
GLN
139
39.269
75.530
58.288
1.00
53.64


ATOM
565
C
GLN
139
40.778
70.167
57.603
1.00
43.28


ATOM
566
O
GLN
139
41.149
70.075
56.434
1.00
44.53


ATOM
567
N
ASN
140
41.268
69.403
58.575
1.00
41.60


ATOM
568
CA
ASN
140
42.280
68.385
58.307
1.00
39.70


ATOM
569
CB
ASN
140
42.721
67.719
59.614
1.00
38.65


ATOM
570
CG
ASN
140
43.904
66.782
59.425
1.00
38.74


ATOM
571
OD1
ASN
140
43.860
65.877
58.587
1.00
39.03


ATOM
572
ND2
ASN
140
44.959
67.007
60.208
1.00
38.01


ATOM
573
C
ASN
140
41.715
67.336
57.353
1.00
39.03


ATOM
574
O
ASN
140
40.752
66.640
57.682
1.00
37.85


ATOM
575
N
THR
141
42.319
67.222
56.175
1.00
38.84


ATOM
576
CA
THR
141
41.862
66.265
55.175
1.00
39.36


ATOM
577
CB
THR
141
42.689
66.377
53.878
1.00
40.12


ATOM
578
OG1
THR
141
44.072
66.148
54.168
1.00
42.67


ATOM
579
CG2
THR
141
42.527
67.761
53.263
1.00
40.55


ATOM
580
C
THR
141
41.910
64.820
55.673
1.00
38.70


ATOM
581
O
THR
141
40.965
64.060
55.469
1.00
39.63


ATOM
582
N
THR
142
43.003
64.442
56.327
1.00
37.88


ATOM
583
CA
THR
142
43.141
63.082
56.843
1.00
36.04


ATOM
584
CB
THR
142
44.516
62.870
57.509
1.00
36.83


ATOM
585
OG1
THR
142
45.547
63.012
56.524
1.00
36.96


ATOM
586
CG2
THR
142
44.605
61.481
58.126
1.00
37.59


ATOM
587
C
THR
142
42.045
62.770
57.857
1.00
35.01


ATOM
588
O
THR
142
41.465
61.686
57.836
1.00
34.20


ATOM
589
N
ILE
143
41.770
63.719
58.747
1.00
33.02


ATOM
590
CA
ILE
143
40.728
63.538
59.754
1.00
32.35


ATOM
591
CB
ILE
143
40.706
64.721
60.754
1.00
33.52


ATOM
592
CG2
ILE
143
39.488
64.620
61.664
1.00
31.47


ATOM
593
CG1
ILE
143
42.000
64.736
61.573
1.00
33.85


ATOM
594
CD1
ILE
143
42.192
63.512
62.442
1.00
36.23


ATOM
595
C
ILE
143
39.379
63.467
59.048
1.00
31.17


ATOM
596
O
ILE
143
38.503
62.679
59.413
1.00
29.34


ATOM
597
N
LYS
144
39.231
64.306
58.028
1.00
30.98


ATOM
598
CA
LYS
144
38.016
64.386
57.228
1.00
30.73


ATOM
599
CB
LYS
144
38.208
65.462
56.153
1.00
33.49


ATOM
600
CG
LYS
144
36.993
65.776
55.306
1.00
37.03


ATOM
601
CD
LYS
144
37.360
66.779
54.219
1.00
40.12


ATOM
602
CE
LYS
144
36.174
67.118
53.325
1.00
42.45


ATOM
603
NZ
LYS
144
35.112
67.865
54.051
1.00
43.36


ATOM
604
C
LYS
144
37.712
63.034
56.574
1.00
28.35


ATOM
605
O
LYS
144
36.590
62.526
56.645
1.00
27.74


ATOM
606
N
ARG
145
38.734
62.459
55.951
1.00
26.86


ATOM
607
CA
ARG
145
38.631
61.179
55.254
1.00
24.41


ATOM
608
CB
ARG
145
39.943
60.913
54.512
1.00
24.91


ATOM
609
CG
ARG
145
39.934
59.733
53.549
1.00
23.83


ATOM
610
CD
ARG
145
41.194
59.763
52.692
1.00
24.48


ATOM
611
NE
ARG
145
41.334
58.608
51.806
1.00
23.26


ATOM
612
CZ
ARG
145
40.576
58.376
50.738
1.00
25.83


ATOM
613
NH1
ARG
145
39.606
59.221
50.410
1.00
23.61


ATOM
614
NH2
ARG
145
40.796
57.300
49.988
1.00
23.06


ATOM
615
C
ARG
145
38.302
60.009
56.187
1.00
24.55


ATOM
616
O
ARG
145
37.457
59.168
55.871
1.00
22.27


ATOM
617
N
ILE
146
38.971
59.949
57.333
1.00
23.82


ATOM
618
CA
ILE
146
38.720
58.876
58.288
1.00
24.41


ATOM
619
CB
ILE
146
39.720
58.935
59.468
1.00
25.21


ATOM
620
CG2
ILE
146
39.251
58.033
60.600
1.00
22.70


ATOM
621
CG1
ILE
146
41.113
58.519
58.979
1.00
25.19


ATOM
622
CD1
ILE
146
42.202
58.625
60.028
1.00
26.27


ATOM
623
C
ILE
146
37.296
58.932
58.838
1.00
24.39


ATOM
624
O
ILE
146
36.591
57.922
58.858
1.00
24.78


ATOM
625
N
ILE
147
36.874
60.116
59.274
1.00
23.99


ATOM
626
CA
ILE
147
35.539
60.283
59.832
1.00
24.23


ATOM
627
CB
ILE
147
35.337
61.724
60.381
1.00
24.80


ATOM
628
CG2
ILE
147
33.871
61.960
60.733
1.00
25.96


ATOM
629
CG1
ILE
147
36.219
61.924
61.622
1.00
25.41


ATOM
630
CD1
ILE
147
36.029
63.261
62.324
1.00
25.15


ATOM
631
C
ILE
147
34.441
59.947
58.822
1.00
23.88


ATOM
632
O
ILE
147
33.459
59.293
59.168
1.00
22.19


ATOM
633
N
ALA
148
34.603
60.392
57.579
1.00
25.35


ATOM
634
CA
ALA
148
33.610
60.099
56.549
1.00
26.35


ATOM
635
CB
ALA
148
34.041
60.704
55.206
1.00
26.72


ATOM
636
C
ALA
148
33.470
58.584
56.424
1.00
26.20


ATOM
637
O
ALA
148
32.366
58.055
56.296
1.00
26.64


ATOM
638
N
LYS
149
34.604
57.892
56.476
1.00
26.33


ATOM
639
CA
LYS
149
34.632
56.439
56.372
1.00
25.57


ATOM
640
CB
LYS
149
36.080
55.970
56.205
1.00
28.20


ATOM
641
CG
LYS
149
36.244
54.497
55.885
1.00
32.16


ATOM
642
CD
LYS
149
37.640
54.228
55.333
1.00
36.26


ATOM
643
CE
LYS
149
37.815
52.773
54.930
1.00
37.26


ATOM
644
NZ
LYS
149
37.763
51.868
56.105
1.00
39.38


ATOM
645
C
LYS
149
33.989
55.754
57.581
1.00
24.69


ATOM
646
O
LYS
149
33.302
54.739
57.435
1.00
24.36


ATOM
647
N
VAL
150
34.205
56.307
58.772
1.00
22.37


ATOM
648
CA
VAL
150
33.632
55.727
59.981
1.00
22.59


ATOM
649
CB
VAL
150
34.270
56.341
61.254
1.00
23.63


ATOM
650
CG1
VAL
150
33.651
55.723
62.502
1.00
20.79


ATOM
651
CG2
VAL
150
35.776
56.099
61.243
1.00
22.23


ATOM
652
C
VAL
150
32.111
55.899
60.035
1.00
21.68


ATOM
653
O
VAL
150
31.426
55.151
60.730
1.00
21.12


ATOM
654
N
GLN
151
31.581
56.871
59.294
1.00
20.83


ATOM
655
CA
GLN
151
30.133
57.097
59.267
1.00
21.36


ATOM
656
CB
GLN
151
29.804
58.423
58.566
1.00
21.83


ATOM
657
CG
GLN
151
30.424
59.658
59.216
1.00
22.21


ATOM
658
CD
GLN
151
30.025
60.949
58.514
1.00
26.18


ATOM
659
OE1
GLN
151
29.786
60.960
57.306
1.00
26.64


ATOM
660
NE2
GLN
151
29.969
62.046
59.266
1.00
23.87


ATOM
661
C
GLN
151
29.405
55.948
58.555
1.00
21.63


ATOM
662
O
GLN
151
28.178
55.831
58.637
1.00
21.51


ATOM
663
N
ASP
152
30.162
55.111
57.848
1.00
19.66


ATOM
664
CA
ASP
152
29.596
53.958
57.141
1.00
21.29


ATOM
665
CB
ASP
152
30.413
53.657
55.875
1.00
19.46


ATOM
666
CG
ASP
152
29.783
52.574
55.004
1.00
21.81


ATOM
667
OD1
ASP
152
29.034
51.724
55.528
1.00
21.84


ATOM
668
OD2
ASP
152
30.056
52.563
53.784
1.00
22.86


ATOM
669
C
ASP
152
29.690
52.781
58.109
1.00
20.99


ATOM
670
O
ASP
152
30.772
52.240
58.323
1.00
20.95


ATOM
671
N
LEU
153
28.558
52.386
58.688
1.00
22.58


ATOM
672
CA
LEU
153
28.535
51.292
59.661
1.00
22.39


ATOM
673
CB
LEU
153
27.330
51.433
60.593
1.00
22.04


ATOM
674
CG
LEU
153
26.824
52.837
60.927
1.00
25.61


ATOM
675
CD1
LEU
153
25.697
52.735
61.951
1.00
25.99


ATOM
676
CD2
LEU
153
27.956
53.680
61.460
1.00
22.76


ATOM
677
C
LEU
153
28.460
49.919
59.013
1.00
22.78


ATOM
678
O
LEU
153
28.512
48.902
59.704
1.00
21.91


ATOM
679
N
GLU
154
28.341
49.894
57.691
1.00
22.03


ATOM
680
CA
GLU
154
28.202
48.644
56.965
1.00
23.75


ATOM
681
CB
GLU
154
29.540
47.902
56.894
1.00
26.94


ATOM
682
CG
GLU
154
30.179
48.049
55.508
1.00
34.66


ATOM
683
CD
GLU
154
31.604
48.553
55.547
1.00
38.29


ATOM
684
OE1
GLU
154
32.505
47.776
55.938
1.00
41.36


ATOM
685
OE2
GLU
154
31.825
49.729
55.185
1.00
42.09


ATOM
686
C
GLU
154
27.103
47.792
57.603
1.00
21.61


ATOM
687
O
GLU
154
26.055
48.324
57.952
1.00
22.87


ATOM
688
N
ARG
155
27.323
46.493
57.773
1.00
20.09


ATOM
689
CA
ARG
155
26.275
45.646
58.340
1.00
21.46


ATOM
690
CB
ARG
155
26.742
44.192
58.430
1.00
20.77


ATOM
691
CG
ARG
155
27.718
43.918
59.551
1.00
19.96


ATOM
692
CD
ARG
155
28.186
42.480
59.509
1.00
23.32


ATOM
693
NE
ARG
155
28.950
42.205
58.299
1.00
25.43


ATOM
694
CZ
ARG
155
29.456
41.017
57.994
1.00
29.86


ATOM
695
NH1
ARG
155
29.274
39.987
58.814
1.00
28.71


ATOM
696
NH2
ARG
155
30.152
40.858
56.873
1.00
31.49


ATOM
697
C
ARG
155
25.784
46.105
59.712
1.00
21.73


ATOM
698
O
ARG
155
24.638
45.846
60.084
1.00
21.61


ATOM
699
N
ALA
156
26.645
46.787
60.461
1.00
21.87


ATOM
700
CA
ALA
156
26.270
47.264
61.789
1.00
24.11


ATOM
701
CB
ALA
156
27.478
47.878
62.490
1.00
24.00


ATOM
702
C
ALA
156
25.117
48.270
61.749
1.00
24.29


ATOM
703
O
ALA
156
24.566
48.620
62.788
1.00
24.68


ATOM
704
N
ALA
157
24.748
48.735
60.557
1.00
22.56


ATOM
705
CA
ALA
157
23.642
49.684
60.447
1.00
22.76


ATOM
706
CB
ALA
157
23.721
50.438
59.125
1.00
21.66


ATOM
707
C
ALA
157
22.297
48.966
60.554
1.00
22.55


ATOM
708
O
ALA
157
21.258
49.598
60.749
1.00
23.01


ATOM
709
N
LEU
158
22.322
47.642
60.429
1.00
22.24


ATOM
710
CA
LEU
158
21.103
46.834
60.490
1.00
21.40


ATOM
711
CB
LEU
158
21.365
45.441
59.912
1.00
19.45


ATOM
712
CG
LEU
158
21.629
45.249
58.418
1.00
16.15


ATOM
713
CD1
LEU
158
22.085
43.821
58.168
1.00
18.41


ATOM
714
CD2
LEU
158
20.357
45.554
57.632
1.00
14.90


ATOM
715
C
LEU
158
20.542
46.655
61.900
1.00
22.60


ATOM
716
O
LEU
158
21.296
46.550
62.861
1.00
21.61


ATOM
717
N
PRO
159
19.202
46.616
62.033
1.00
23.33


ATOM
718
CD
PRO
159
18.180
46.863
60.999
1.00
22.87


ATOM
719
CA
PRO
159
18.582
46.430
63.348
1.00
24.44


ATOM
720
CB
PRO
159
17.096
46.342
63.017
1.00
23.93


ATOM
721
CG
PRO
159
16.970
47.241
61.824
1.00
24.99


ATOM
722
C
PRO
159
19.122
45.111
63.897
1.00
25.67


ATOM
723
O
PRO
159
19.384
44.182
63.128
1.00
24.90


ATOM
724
N
ALA
160
19.289
45.035
65.213
1.00
25.35


ATOM
725
CA
ALA
160
19.818
43.841
65.866
1.00
26.14


ATOM
726
CB
ALA
160
19.536
43.909
67.366
1.00
26.95


ATOM
727
C
ALA
160
19.296
42.516
65.303
1.00
26.55


ATOM
728
O
ALA
160
20.071
41.584
65.078
1.00
23.79


ATOM
729
N
GLN
161
17.989
42.431
65.077
1.00
26.32


ATOM
730
CA
GLN
161
17.397
41.201
64.563
1.00
29.37


ATOM
731
CB
GLN
161
15.871
41.313
64.542
1.00
31.38


ATOM
732
CG
GLN
161
15.167
40.022
64.158
1.00
37.44


ATOM
733
CD
GLN
161
13.656
40.124
64.267
1.00
41.02


ATOM
734
OE1
GLN
161
13.114
40.363
65.349
1.00
43.87


ATOM
735
NE2
GLN
161
12.967
39.947
63.144
1.00
43.01


ATOM
736
C
GLN
161
17.909
40.844
63.169
1.00
28.25


ATOM
737
O
GLN
161
18.313
39.705
62.922
1.00
27.07


ATOM
738
N
GLU
162
17.884
41.815
62.262
1.00
27.58


ATOM
739
CA
GLU
162
18.353
41.595
60.898
1.00
28.12


ATOM
740
CB
GLU
162
18.056
42.812
60.014
1.00
30.05


ATOM
741
CG
GLU
162
16.648
42.872
59.439
1.00
36.16


ATOM
742
CD
GLU
162
15.596
43.218
60.474
1.00
40.46


ATOM
743
OE1
GLU
162
15.349
42.396
61.383
1.00
43.71


ATOM
744
OE2
GLU
162
15.015
44.320
60.376
1.00
42.20


ATOM
745
C
GLU
162
19.852
41.319
60.875
1.00
25.64


ATOM
746
O
GLU
162
20.338
40.564
60.036
1.00
24.67


ATOM
747
N
LEU
163
20.583
41.933
61.798
1.00
23.77


ATOM
748
CA
LEU
163
22.027
41.741
61.856
1.00
23.77


ATOM
749
CB
LEU
163
22.658
42.686
62.886
1.00
23.27


ATOM
750
CG
LEU
163
24.167
42.535
63.139
1.00
22.82


ATOM
751
CD1
LEU
163
24.947
42.725
61.843
1.00
24.01


ATOM
752
CD2
LEU
163
24.614
43.548
64.179
1.00
23.32


ATOM
753
C
LEU
163
22.382
40.299
62.192
1.00
24.03


ATOM
754
O
LEU
163
23.248
39.700
61.546
1.00
23.44


ATOM
755
N
GLU
164
21.717
39.728
63.192
1.00
23.75


ATOM
756
CA
GLU
164
22.031
38.356
63.562
1.00
25.00


ATOM
757
CB
GLU
164
21.362
37.974
64.893
1.00
28.77


ATOM
758
CG
GLU
164
19.950
37.445
64.807
1.00
35.39


ATOM
759
CD
GLU
164
19.405
37.035
66.171
1.00
40.22


ATOM
760
OE1
GLU
164
18.302
36.450
66.224
1.00
41.83


ATOM
761
OE2
GLU
164
20.080
37.303
67.193
1.00
41.78


ATOM
762
C
GLU
164
21.628
37.401
62.445
1.00
23.01


ATOM
763
O
GLU
164
22.319
36.414
62.185
1.00
22.51


ATOM
764
N
GLU
165
20.524
37.703
61.768
1.00
22.62


ATOM
765
CA
GLU
165
20.073
36.857
60.670
1.00
24.34


ATOM
766
CB
GLU
165
18.669
37.265
60.209
1.00
24.26


ATOM
767
CG
GLU
165
18.195
36.512
58.973
1.00
26.97


ATOM
768
CD
GLU
165
16.781
36.876
58.560
1.00
28.34


ATOM
769
OE1
GLU
165
16.329
37.996
58.886
1.00
28.72


ATOM
770
OE2
GLU
165
16.127
36.045
57.893
1.00
28.15


ATOM
771
C
GLU
165
21.065
36.968
59.509
1.00
24.93


ATOM
772
O
GLU
165
21.395
35.967
58.865
1.00
24.77


ATOM
773
N
TYR
166
21.552
38.181
59.260
1.00
23.07


ATOM
774
CA
TYR
166
22.514
38.402
58.188
1.00
23.12


ATOM
775
CB
TYR
166
22.764
39.903
57.993
1.00
21.91


ATOM
776
CG
TYR
166
23.736
40.235
56.875
1.00
21.83


ATOM
777
CD1
TYR
166
23.502
39.807
55.568
1.00
22.95


ATOM
778
CE1
TYR
166
24.390
40.119
54.532
1.00
22.34


ATOM
779
CD2
TYR
166
24.886
40.985
57.125
1.00
21.46


ATOM
780
CE2
TYR
166
25.780
41.301
56.102
1.00
22.52


ATOM
781
CZ
TYR
166
25.526
40.865
54.808
1.00
23.28


ATOM
782
OH
TYR
166
26.403
41.176
53.795
1.00
23.78


ATOM
783
C
TYR
166
23.831
37.687
58.503
1.00
23.03


ATOM
784
O
TYR
166
24.412
37.040
57.633
1.00
23.00


ATOM
785
N
ASN
167
24.302
37.794
59.743
1.00
22.34


ATOM
786
CA
ASN
167
25.551
37.129
60.112
1.00
22.66


ATOM
787
CB
ASN
167
25.979
37.493
61.539
1.00
23.67


ATOM
788
CG
ASN
167
26.499
38.915
61.649
1.00
24.93


ATOM
789
OD1
ASN
167
27.226
39.393
60.777
1.00
26.06


ATOM
790
ND2
ASN
167
26.140
39.594
62.731
1.00
25.88


ATOM
791
C
ASN
167
25.430
35.616
59.994
1.00
22.26


ATOM
792
O
ASN
167
26.363
34.950
59.552
1.00
21.60


ATOM
793
N
LYS
168
24.280
35.073
60.382
1.00
20.98


ATOM
794
CA
LYS
168
24.079
33.632
60.307
1.00
21.98


ATOM
795
CB
LYS
168
22.809
33.214
61.055
1.00
23.33


ATOM
796
CG
LYS
168
22.528
31.729
60.936
1.00
27.37


ATOM
797
CD
LYS
168
21.405
31.270
61.844
1.00
32.52


ATOM
798
CE
LYS
168
21.082
29.808
61.567
1.00
35.29


ATOM
799
NZ
LYS
168
22.320
28.969
61.554
1.00
35.98


ATOM
800
C
LYS
168
24.006
33.159
58.860
1.00
20.98


ATOM
801
O
LYS
168
24.509
32.085
58.525
1.00
20.06


ATOM
802
N
ILE
169
23.374
33.959
58.007
1.00
19.85


ATOM
803
CA
ILE
169
23.260
33.615
56.595
1.00
21.24


ATOM
804
CB
ILE
169
22.368
34.631
55.846
1.00
21.43


ATOM
805
CG2
ILE
169
22.611
34.554
54.338
1.00
23.74


ATOM
806
CG1
ILE
169
20.900
34.340
56.159
1.00
24.06


ATOM
807
CD1
ILE
169
19.930
35.302
55.515
1.00
24.63


ATOM
808
C
ILE
169
24.643
33.554
55.944
1.00
19.54


ATOM
809
O
ILE
169
24.936
32.632
55.188
1.00
21.81


ATOM
810
N
LEU
170
25.491
34.530
56.244
1.00
19.05


ATOM
811
CA
LEU
170
26.837
34.562
55.687
1.00
19.74


ATOM
812
CB
LEU
170
27.565
35.834
56.131
1.00
19.37


ATOM
813
CG
LEU
170
27.041
37.157
55.559
1.00
21.50


ATOM
814
CD1
LEU
170
27.810
38.328
56.170
1.00
20.18


ATOM
815
CD2
LEU
170
27.188
37.151
54.044
1.00
19.99


ATOM
816
C
LEU
170
27.620
33.332
56.140
1.00
21.61


ATOM
817
O
LEU
170
28.300
32.682
55.344
1.00
21.28


ATOM
818
N
LEU
171
27.511
33.009
57.423
1.00
21.65


ATOM
819
CA
LEU
171
28.217
31.862
57.969
1.00
23.32


ATOM
820
CB
LEU
171
28.042
31.811
59.490
1.00
25.33


ATOM
821
CG
LEU
171
28.968
30.869
60.262
1.00
28.92


ATOM
822
CD1
LEU
171
30.414
31.241
59.990
1.00
30.99


ATOM
823
CD2
LEU
171
28.681
30.977
61.756
1.00
32.45


ATOM
824
C
LEU
171
27.714
30.569
57.337
1.00
22.19


ATOM
825
O
LEU
171
28.511
29.705
56.975
1.00
22.62


ATOM
826
N
ASP
172
26.396
30.439
57.202
1.00
20.90


ATOM
827
CA
ASP
172
25.817
29.237
56.615
1.00
21.82


ATOM
828
CB
ASP
172
24.283
29.261
56.698
1.00
22.55


ATOM
829
CG
ASP
172
23.766
29.076
58.121
1.00
24.93


ATOM
830
OD1
ASP
172
24.489
28.493
58.952
1.00
24.24


ATOM
831
OD2
ASP
172
22.625
29.502
58.404
1.00
26.64


ATOM
832
C
ASP
172
26.244
29.060
55.161
1.00
22.04


ATOM
833
O
ASP
172
26.501
27.940
54.720
1.00
21.02


ATOM
834
N
MET
173
26.315
30.156
54.411
1.00
20.30


ATOM
835
CA
MET
173
26.731
30.057
53.014
1.00
20.02


ATOM
836
CB
MET
173
26.524
31.389
52.277
1.00
16.36


ATOM
837
CG
MET
173
25.055
31.743
52.047
1.00
14.73


ATOM
838
SD
MET
173
24.812
32.982
50.748
1.00
18.57


ATOM
839
CE
MET
173
25.587
34.426
51.501
1.00
15.06


ATOM
840
C
MET
173
28.195
29.639
52.925
1.00
19.90


ATOM
841
O
MET
173
28.560
28.773
52.129
1.00
18.15


ATOM
842
N
GLU
174
29.033
30.251
53.751
1.00
21.27


ATOM
843
CA
GLU
174
30.452
29.931
53.745
1.00
24.34


ATOM
844
CB
GLU
174
31.209
30.830
54.719
1.00
26.33


ATOM
845
CG
GLU
174
32.700
30.567
54.706
1.00
31.24


ATOM
846
CD
GLU
174
33.296
30.741
53.321
1.00
34.04


ATOM
847
OE1
GLU
174
33.424
31.900
52.874
1.00
33.83


ATOM
848
OE2
GLU
174
33.624
29.716
52.678
1.00
34.64


ATOM
849
C
GLU
174
30.686
28.477
54.122
1.00
23.73


ATOM
850
O
GLU
174
31.454
27.768
53.464
1.00
23.77


ATOM
851
N
THR
175
30.024
28.037
55.187
1.00
22.79


ATOM
852
CA
THR
175
30.166
26.664
55.650
1.00
23.63


ATOM
853
CB
THR
175
29.363
26.425
56.941
1.00
23.79


ATOM
854
OG1
THR
175
29.850
27.294
57.971
1.00
23.95


ATOM
855
CG2
THR
175
29.502
24.973
57.391
1.00
23.49


ATOM
856
C
THR
175
29.693
25.671
54.593
1.00
22.90


ATOM
857
O
THR
175
30.391
24.701
54.279
1.00
24.74


ATOM
858
N
THR
176
28.507
25.917
54.050
1.00
19.50


ATOM
859
CA
THR
176
27.937
25.052
53.025
1.00
21.93


ATOM
860
CB
THR
176
26.605
25.616
52.494
1.00
21.32


ATOM
861
OG1
THR
176
25.646
25.661
53.559
1.00
22.38


ATOM
862
CG2
THR
176
26.068
24.740
51.358
1.00
20.84


ATOM
863
C
THR
176
28.884
24.870
51.842
1.00
21.08


ATOM
864
O
THR
176
29.060
23.761
51.342
1.00
22.40


ATOM
865
N
TYR
177
29.492
25.963
51.395
1.00
20.72


ATOM
866
CA
TYR
177
30.406
25.906
50.260
1.00
19.26


ATOM
867
CB
TYR
177
30.784
27.327
49.816
1.00
18.41


ATOM
868
CG
TYR
177
31.707
27.374
48.610
1.00
18.79


ATOM
869
CD1
TYR
177
31.196
27.356
47.311
1.00
16.82


ATOM
870
CE1
TYR
177
32.044
27.376
46.197
1.00
16.82


ATOM
871
CD2
TYR
177
33.094
27.410
48.770
1.00
17.18


ATOM
872
CE2
TYR
177
33.954
27.424
47.662
1.00
17.14


ATOM
873
CZ
TYR
177
33.418
27.406
46.382
1.00
18.38


ATOM
874
OH
TYR
177
34.256
27.403
45.289
1.00
18.18


ATOM
875
C
TYR
177
31.682
25.126
50.581
1.00
19.83


ATOM
876
O
TYR
177
32.089
24.244
49.826
1.00
19.73


ATOM
877
N
SER
178
32.298
25.448
51.712
1.00
19.67


ATOM
878
CA
SER
178
33.555
24.828
52.117
1.00
22.76


ATOM
879
CB
SER
178
34.208
25.678
53.211
1.00
23.75


ATOM
880
OG
SER
178
34.560
26.953
52.702
1.00
28.52


ATOM
881
C
SER
178
33.543
23.363
52.556
1.00
22.80


ATOM
882
O
SER
178
34.606
22.752
52.672
1.00
22.47


ATOM
883
N
VAL
179
32.368
22.796
52.803
1.00
22.17


ATOM
884
CA
VAL
179
32.309
21.401
53.219
1.00
23.76


ATOM
885
CB
VAL
179
31.676
21.255
54.631
1.00
24.20


ATOM
886
CG1
VAL
179
32.400
22.160
55.617
1.00
23.61


ATOM
887
CG2
VAL
179
30.189
21.584
54.588
1.00
23.11


ATOM
888
C
VAL
179
31.527
20.541
52.231
1.00
23.17


ATOM
889
O
VAL
179
31.277
19.366
52.482
1.00
24.77


ATOM
890
N
ALA
180
31.153
21.122
51.098
1.00
22.77


ATOM
891
CA
ALA
180
30.395
20.384
50.093
1.00
21.75


ATOM
892
CB
ALA
180
29.810
21.352
49.064
1.00
19.82


ATOM
893
C
ALA
180
31.247
19.329
49.391
1.00
21.47


ATOM
894
O
ALA
180
32.429
19.549
49.121
1.00
20.99


ATOM
895
N
THR
181
30.644
18.179
49.106
1.00
21.38


ATOM
896
CA
THR
181
31.354
17.111
48.411
1.00
22.06


ATOM
897
CB
THR
181
31.768
15.957
49.371
1.00
23.05


ATOM
898
OG1
THR
181
30.598
15.325
49.901
1.00
25.28


ATOM
899
CG2
THR
181
32.615
16.487
50.520
1.00
22.65


ATOM
900
C
THR
181
30.491
16.527
47.298
1.00
22.17


ATOM
901
O
THR
181
29.266
16.673
47.294
1.00
22.75


ATOM
902
N
VAL
182
31.145
15.881
46.343
1.00
22.72


ATOM
903
CA
VAL
182
30.459
15.244
45.228
1.00
24.25


ATOM
904
CB
VAL
182
30.941
15.813
43.884
1.00
23.11


ATOM
905
CG1
VAL
182
30.204
15.133
42.738
1.00
23.43


ATOM
906
CG2
VAL
182
30.707
17.324
43.852
1.00
22.55


ATOM
907
C
VAL
182
30.819
13.767
45.329
1.00
26.05


ATOM
908
O
VAL
182
31.990
13.404
45.239
1.00
26.03


ATOM
909
N
CYS
183
29.813
12.920
45.522
1.00
30.03


ATOM
910
CA
CYS
183
30.051
11.489
45.689
1.00
34.00


ATOM
911
C
CYS
183
29.670
10.596
44.514
1.00
36.77


ATOM
912
O
CYS
183
28.800
10.927
43.711
1.00
37.04


ATOM
913
CB
CYS
183
29.301
10.976
46.916
1.00
33.01


ATOM
914
SG
CYS
183
29.491
11.922
48.460
1.00
34.26


ATOM
915
N
HIS
184
30.333
9.443
44.450
1.00
40.51


ATOM
916
CA
HIS
184
30.085
8.433
43.427
1.00
43.09


ATOM
917
CB
HIS
184
31.392
7.748
43.028
1.00
43.26


ATOM
918
CG
HIS
184
32.240
8.552
42.097
1.00
44.35


ATOM
919
CD2
HIS
184
33.423
9.183
42.287
1.00
44.78


ATOM
920
ND1
HIS
184
31.902
8.761
40.777
1.00
45.33


ATOM
921
CE1
HIS
184
32.842
9.483
40.194
1.00
45.93


ATOM
922
NE2
HIS
184
33.777
9.752
41.088
1.00
46.19


ATOM
923
C
HIS
184
29.141
7.394
44.027
1.00
45.42


ATOM
924
O
HIS
184
28.935
7.360
45.243
1.00
45.31


ATOM
925
N
PRO
185
28.554
6.531
43.181
1.00
47.60


ATOM
926
CD
PRO
185
28.637
6.523
41.709
1.00
48.72


ATOM
927
CA
PRO
185
27.632
5.493
43.654
1.00
48.59


ATOM
928
CB
PRO
185
27.370
4.674
42.394
1.00
48.70


ATOM
929
CG
PRO
185
27.411
5.721
41.320
1.00
48.86


ATOM
930
C
PRO
185
28.231
4.651
44.780
1.00
49.38


ATOM
931
O
PRO
185
27.577
4.403
45.795
1.00
49.51


ATOM
932
N
ASN
186
29.478
4.220
44.597
1.00
49.61


ATOM
933
CA
ASN
186
30.154
3.407
45.602
1.00
50.29


ATOM
934
CB
ASN
186
31.594
3.082
45.168
1.00
49.31


ATOM
935
CG
ASN
186
32.299
4.260
44.507
1.00
47.77


ATOM
936
OD1
ASN
186
32.262
5.384
45.012
1.00
47.20


ATOM
937
ND2
ASN
186
32.955
3.993
43.377
1.00
45.72


ATOM
938
C
ASN
186
30.164
4.072
46.974
1.00
50.98


ATOM
939
O
ASN
186
29.525
3.592
47.913
1.00
53.09


ATOM
940
N
GLY
187
30.885
5.180
47.086
1.00
50.22


ATOM
941
CA
GLY
187
30.964
5.881
48.353
1.00
47.28


ATOM
942
C
GLY
187
32.148
6.822
48.369
1.00
45.22


ATOM
943
O
GLY
187
32.458
7.432
49.392
1.00
46.04


ATOM
944
N
SER
188
32.824
6.927
47.232
1.00
42.88


ATOM
945
CA
SER
188
33.965
7.821
47.122
1.00
41.34


ATOM
946
CB
SER
188
34.855
7.415
45.948
1.00
41.68


ATOM
947
OG
SER
188
35.413
6.130
46.160
1.00
45.75


ATOM
948
C
SER
188
33.431
9.230
46.904
1.00
38.80


ATOM
949
O
SER
188
32.807
9.517
45.884
1.00
37.31


ATOM
950
N
CYS
189
33.655
10.096
47.883
1.00
36.07


ATOM
951
CA
CYS
189
33.202
11.472
47.793
1.00
33.90


ATOM
952
C
CYS
189
34.416
12.358
47.579
1.00
32.06


ATOM
953
O
CYS
189
35.459
12.159
48.202
1.00
33.88


ATOM
954
CB
CYS
189
32.479
11.883
49.070
1.00
34.32


ATOM
955
SG
CYS
189
30.963
10.949
49.464
1.00
35.61


ATOM
956
N
LEU
190
34.280
13.331
46.689
1.00
28.75


ATOM
957
CA
LEU
190
35.377
14.237
46.387
1.00
26.04


ATOM
958
CB
LEU
190
35.644
14.252
44.875
1.00
26.05


ATOM
959
CG
LEU
190
36.265
13.013
44.216
1.00
27.11


ATOM
960
CD1
LEU
190
35.318
11.828
44.314
1.00
28.50


ATOM
961
CD2
LEU
190
36.569
13.323
42.753
1.00
27.77


ATOM
962
C
LEU
190
35.107
15.659
46.866
1.00
24.84


ATOM
963
O
LEU
190
33.988
16.159
46.765
1.00
23.97


ATOM
964
N
GLN
191
36.138
16.297
47.405
1.00
24.09


ATOM
965
CA
GLN
191
36.028
17.677
47.857
1.00
25.37


ATOM
966
CB
GLN
191
36.881
17.902
49.109
1.00
27.00


ATOM
967
CG
GLN
191
36.405
17.122
50.329
1.00
31.92


ATOM
968
CD
GLN
191
37.279
17.348
51.546
1.00
34.94


ATOM
969
OE1
GLN
191
38.476
17.061
51.527
1.00
38.38


ATOM
970
NE2
GLN
191
36.684
17.862
52.614
1.00
37.18


ATOM
971
C
GLN
191
36.550
18.534
46.704
1.00
23.81


ATOM
972
O
GLN
191
37.239
18.024
45.818
1.00
21.41


ATOM
973
N
LEU
192
36.222
19.824
46.705
1.00
23.17


ATOM
974
CA
LEU
192
36.680
20.709
45.639
1.00
22.33


ATOM
975
CB
LEU
192
36.151
22.131
45.856
1.00
21.16


ATOM
976
CG
LEU
192
36.586
23.161
44.808
1.00
19.56


ATOM
977
CD1
LEU
192
36.115
22.726
43.425
1.00
19.50


ATOM
978
CD2
LEU
192
36.015
24.527
45.166
1.00
21.09


ATOM
979
C
LEU
192
38.206
20.719
45.582
1.00
23.46


ATOM
980
O
LEU
192
38.801
20.494
44.533
1.00
23.60


ATOM
981
N
GLU
193
38.844
20.973
46.716
1.00
25.17


ATOM
982
CA
GLU
193
40.297
20.989
46.751
1.00
27.25


ATOM
983
CB
GLU
193
40.796
22.297
47.367
1.00
31.24


ATOM
984
CG
GLU
193
40.244
23.527
46.662
1.00
37.45


ATOM
985
CD
GLU
193
41.081
24.769
46.892
1.00
43.41


ATOM
986
OE1
GLU
193
41.256
25.170
48.060
1.00
46.60


ATOM
987
OE2
GLU
193
41.564
25.348
45.896
1.00
48.13


ATOM
988
C
GLU
193
40.789
19.794
47.558
1.00
27.24


ATOM
989
O
GLU
193
40.398
19.614
48.710
1.00
28.55


ATOM
990
N
PRO
194
41.663
18.964
46.965
1.00
26.18


ATOM
991
CD
PRO
194
42.458
17.987
47.737
1.00
26.80


ATOM
992
CA
PRO
194
42.200
19.094
45.607
1.00
24.97


ATOM
993
CB
PRO
194
43.662
18.750
45.806
1.00
26.63


ATOM
994
CG
PRO
194
43.547
17.564
46.737
1.00
25.86


ATOM
995
C
PRO
194
41.558
18.143
44.595
1.00
23.91


ATOM
996
O
PRO
194
41.868
18.203
43.404
1.00
22.16


ATOM
997
N
ASP
195
40.672
17.273
45.072
1.00
22.30


ATOM
998
CA
ASP
195
40.037
16.269
44.225
1.00
21.76


ATOM
999
CB
ASP
195
39.029
15.452
45.036
1.00
22.60


ATOM
1000
CG
ASP
195
39.608
14.946
46.341
1.00
26.35


ATOM
1001
OD1
ASP
195
40.763
14.474
46.339
1.00
26.43


ATOM
1002
OD2
ASP
195
38.902
15.018
47.369
1.00
29.80


ATOM
1003
C
ASP
195
39.365
16.754
42.945
1.00
21.71


ATOM
1004
O
ASP
195
39.793
16.392
41.850
1.00
23.10


ATOM
1005
N
LEU
196
38.308
17.551
43.068
1.00
19.29


ATOM
1006
CA
LEU
196
37.604
18.027
41.875
1.00
19.93


ATOM
1007
CB
LEU
196
36.316
18.753
42.273
1.00
19.22


ATOM
1008
CG
LEU
196
35.288
17.859
42.971
1.00
21.05


ATOM
1009
CD1
LEU
196
34.177
18.719
43.553
1.00
21.19


ATOM
1010
CD2
LEU
196
34.726
16.834
41.978
1.00
18.71


ATOM
1011
C
LEU
196
38.473
18.933
41.020
1.00
18.92


ATOM
1012
O
LEU
196
38.405
18.887
39.794
1.00
19.13


ATOM
1013
N
THR
197
39.287
19.757
41.673
1.00
19.32


ATOM
1014
CA
THR
197
40.179
20.667
40.968
1.00
20.23


ATOM
1015
CB
THR
197
40.994
21.530
41.962
1.00
21.09


ATOM
1016
OG1
THR
197
40.098
22.333
42.739
1.00
23.68


ATOM
1017
CG2
THR
197
41.962
22.444
41.212
1.00
23.82


ATOM
1018
C
THR
197
41.138
19.855
40.103
1.00
20.96


ATOM
1019
O
THR
197
41.408
20.203
38.950
1.00
18.55


ATOM
1020
N
ASN
198
41.649
18.762
40.660
1.00
20.33


ATOM
1021
CA
ASN
198
42.566
17.916
39.910
1.00
21.82


ATOM
1022
CB
ASN
198
43.144
16.820
40.800
1.00
24.76


ATOM
1023
CG
ASN
198
44.158
15.971
40.068
1.00
29.65


ATOM
1024
OD1
ASN
198
45.283
16.409
39.812
1.00
31.73


ATOM
1025
ND2
ASN
198
43.759
14.757
39.701
1.00
31.98


ATOM
1026
C
ASN
198
41.876
17.272
38.706
1.00
19.19


ATOM
1027
O
ASN
198
42.457
17.200
37.624
1.00
21.70


ATOM
1028
N
VAL
199
40.645
16.800
38.893
1.00
18.96


ATOM
1029
CA
VAL
199
39.907
16.180
37.795
1.00
18.37


ATOM
1030
CB
VAL
199
38.516
15.666
38.257
1.00
19.57


ATOM
1031
CG1
VAL
199
37.680
15.275
37.048
1.00
18.46


ATOM
1032
CG2
VAL
199
38.682
14.451
39.187
1.00
20.39


ATOM
1033
C
VAL
199
39.715
17.182
36.650
1.00
18.73


ATOM
1034
O
VAL
199
39.965
16.869
35.485
1.00
15.90


ATOM
1035
N
MET
200
39.279
18.392
36.988
1.00
18.95


ATOM
1036
CA
MET
200
39.063
19.423
35.980
1.00
17.76


ATOM
1037
CB
MET
200
38.475
20.680
36.630
1.00
18.24


ATOM
1038
CG
MET
200
37.084
20.494
37.227
1.00
16.87


ATOM
1039
SD
MET
200
35.914
19.807
36.056
1.00
20.02


ATOM
1040
CE
MET
200
35.798
21.162
34.832
1.00
21.44


ATOM
1041
C
MET
200
40.353
19.794
35.244
1.00
16.67


ATOM
1042
O
MET
200
40.328
20.125
34.060
1.00
17.29


ATOM
1043
N
ALA
201
41.478
19.724
35.944
1.00
15.31


ATOM
1044
CA
ALA
201
42.764
20.088
35.356
1.00
16.45


ATOM
1045
CB
ALA
201
43.708
20.570
36.458
1.00
14.53


ATOM
1046
C
ALA
201
43.473
19.014
34.530
1.00
17.34


ATOM
1047
O
ALA
201
44.191
19.336
33.580
1.00
18.65


ATOM
1048
N
THR
202
43.263
17.750
34.875
1.00
14.75


ATOM
1049
CA
THR
202
43.963
16.665
34.199
1.00
15.77


ATOM
1050
CB
THR
202
44.717
15.818
35.230
1.00
16.12


ATOM
1051
OG1
THR
202
43.773
15.222
36.124
1.00
17.60


ATOM
1052
CG2
THR
202
45.669
16.694
36.042
1.00
16.30


ATOM
1053
C
THR
202
43.151
15.721
33.322
1.00
17.01


ATOM
1054
O
THR
202
43.680
15.157
32.364
1.00
17.58


ATOM
1055
N
SER
203
41.876
15.531
33.634
1.00
16.36


ATOM
1056
CA
SER
203
41.070
14.635
32.816
1.00
16.62


ATOM
1057
CB
SER
203
39.717
14.379
33.471
1.00
17.45


ATOM
1058
OG
SER
203
38.883
13.637
32.592
1.00
17.94


ATOM
1059
C
SER
203
40.841
15.190
31.411
1.00
17.76


ATOM
1060
O
SER
203
40.627
16.390
31.231
1.00
16.09


ATOM
1061
N
ARG
204
40.894
14.305
30.420
1.00
17.37


ATOM
1062
CA
ARG
204
40.656
14.675
29.029
1.00
18.83


ATOM
1063
CB
ARG
204
41.899
14.394
28.175
1.00
21.32


ATOM
1064
CG
ARG
204
42.806
15.601
27.910
1.00
25.72


ATOM
1065
CD
ARG
204
42.784
16.603
29.041
1.00
24.96


ATOM
1066
NE
ARG
204
44.009
17.391
29.117
1.00
25.28


ATOM
1067
CZ
ARG
204
44.224
18.329
30.035
1.00
25.48


ATOM
1068
NH1
ARG
204
45.366
18.998
30.055
1.00
27.49


ATOM
1069
NH2
ARG
204
43.287
18.610
30.928
1.00
26.72


ATOM
1070
C
ARG
204
39.473
13.859
28.510
1.00
18.41


ATOM
1071
O
ARG
204
39.333
13.648
27.306
1.00
18.06


ATOM
1072
N
LYS
205
38.629
13.394
29.427
1.00
19.07


ATOM
1073
CA
LYS
205
37.449
12.614
29.058
1.00
19.70


ATOM
1074
CB
LYS
205
37.396
11.320
29.876
1.00
20.49


ATOM
1075
CG
LYS
205
38.655
10.464
29.712
1.00
25.63


ATOM
1076
CD
LYS
205
38.499
9.071
30.304
1.00
27.27


ATOM
1077
CE
LYS
205
37.450
8.267
29.552
1.00
32.01


ATOM
1078
NZ
LYS
205
37.428
6.847
30.001
1.00
36.31


ATOM
1079
C
LYS
205
36.181
13.441
29.276
1.00
18.76


ATOM
1080
O
LYS
205
35.836
13.786
30.412
1.00
16.76


ATOM
1081
N
TYR
206
35.499
13.750
28.175
1.00
17.94


ATOM
1082
CA
TYR
206
34.280
14.564
28.187
1.00
18.82


ATOM
1083
CB
TYR
206
33.561
14.456
26.834
1.00
17.41


ATOM
1084
CG
TYR
206
32.581
15.582
26.551
1.00
17.19


ATOM
1085
CD1
TYR
206
32.960
16.682
25.782
1.00
17.56


ATOM
1086
CE1
TYR
206
32.068
17.718
25.509
1.00
17.54


ATOM
1087
CD2
TYR
206
31.276
15.546
27.049
1.00
18.96


ATOM
1088
CE2
TYR
206
30.373
16.581
26.787
1.00
19.27


ATOM
1089
CZ
TYR
206
30.778
17.666
26.015
1.00
20.83


ATOM
1090
OH
TYR
206
29.908
18.711
25.768
1.00
21.81


ATOM
1091
C
TYR
206
33.298
14.209
29.303
1.00
18.43


ATOM
1092
O
TYR
206
32.820
15.092
30.016
1.00
18.33


ATOM
1093
N
GLU
207
32.996
12.922
29.454
1.00
17.90


ATOM
1094
CA
GLU
207
32.049
12.492
30.479
1.00
18.16


ATOM
1095
CB
GLU
207
31.598
11.046
30.224
1.00
20.18


ATOM
1096
CG
GLU
207
30.791
10.830
28.943
1.00
20.70


ATOM
1097
CD
GLU
207
29.494
11.633
28.895
1.00
23.77


ATOM
1098
OE1
GLU
207
28.760
11.661
29.907
1.00
22.24


ATOM
1099
OE2
GLU
207
29.202
12.226
27.833
1.00
24.84


ATOM
1100
C
GLU
207
32.548
12.619
31.917
1.00
17.41


ATOM
1101
O
GLU
207
31.752
12.866
32.821
1.00
16.71


ATOM
1102
N
ASP
208
33.848
12.443
32.145
1.00
16.59


ATOM
1103
CA
ASP
208
34.373
12.560
33.506
1.00
17.48


ATOM
1104
CB
ASP
208
35.774
11.944
33.617
1.00
19.01


ATOM
1105
CG
ASP
208
35.779
10.440
33.362
1.00
24.16


ATOM
1106
OD1
ASP
208
34.689
9.830
33.331
1.00
26.06


ATOM
1107
OD2
ASP
208
36.875
9.865
33.201
1.00
23.40


ATOM
1108
C
ASP
208
34.416
14.033
33.906
1.00
16.55


ATOM
1109
O
ASP
208
34.133
14.389
35.052
1.00
13.04


ATOM
1110
N
LEU
209
34.769
14.885
32.951
1.00
15.38


ATOM
1111
CA
LEU
209
34.822
16.319
33.200
1.00
16.48


ATOM
1112
CB
LEU
209
35.386
17.048
31.974
1.00
14.57


ATOM
1113
CG
LEU
209
36.893
16.869
31.731
1.00
14.85


ATOM
1114
CD1
LEU
209
37.298
17.512
30.412
1.00
14.52


ATOM
1115
CD2
LEU
209
37.668
17.501
32.880
1.00
14.67


ATOM
1116
C
LEU
209
33.404
16.803
33.499
1.00
16.80


ATOM
1117
O
LEU
209
33.192
17.636
34.385
1.00
17.09


ATOM
1118
N
LEU
210
32.434
16.258
32.768
1.00
15.84


ATOM
1119
CA
LEU
210
31.037
16.631
32.955
1.00
15.80


ATOM
1120
CB
LEU
210
30.160
15.971
31.881
1.00
18.19


ATOM
1121
CG
LEU
210
28.670
16.336
31.924
1.00
18.57


ATOM
1122
CD1
LEU
210
28.524
17.850
31.917
1.00
23.32


ATOM
1123
CD2
LEU
210
27.942
15.731
30.735
1.00
22.22


ATOM
1124
C
LEU
210
30.530
16.250
34.342
1.00
16.05


ATOM
1125
O
LEU
210
29.840
17.037
34.998
1.00
16.25


ATOM
1126
N
TRP
211
30.869
15.042
34.784
1.00
15.85


ATOM
1127
CA
TRP
211
30.452
14.556
36.099
1.00
16.79


ATOM
1128
CB
TRP
211
31.033
13.159
36.362
1.00
19.10


ATOM
1129
CG
TRP
211
30.687
12.625
37.721
1.00
22.86


ATOM
1130
CD2
TRP
211
31.472
12.746
38.916
1.00
24.67


ATOM
1131
CE2
TRP
211
30.727
12.167
39.967
1.00
26.17


ATOM
1132
CE3
TRP
211
32.731
13.290
39.199
1.00
25.03


ATOM
1133
CD1
TRP
211
29.531
11.991
38.086
1.00
25.13


ATOM
1134
NE1
TRP
211
29.549
11.714
39.436
1.00
25.08


ATOM
1135
CZ2
TRP
211
31.202
12.119
41.284
1.00
27.62


ATOM
1136
CZ3
TRP
211
33.203
13.241
40.509
1.00
26.84


ATOM
1137
CH2
TRP
211
32.439
12.659
41.533
1.00
27.01


ATOM
1138
C
TRP
211
30.914
15.505
37.208
1.00
15.76


ATOM
1139
O
TRP
211
30.139
15.871
38.091
1.00
15.00


ATOM
1140
N
ALA
212
32.181
15.899
37.158
1.00
16.39


ATOM
1141
CA
ALA
212
32.739
16.796
38.162
1.00
15.16


ATOM
1142
CB
ALA
212
34.256
16.863
38.010
1.00
14.42


ATOM
1143
C
ALA
212
32.142
18.200
38.063
1.00
15.48


ATOM
1144
O
ALA
212
31.839
18.826
39.080
1.00
16.14


ATOM
1145
N
TRP
213
31.982
18.684
36.835
1.00
15.80


ATOM
1146
CA
TRP
213
31.436
20.019
36.581
1.00
16.29


ATOM
1147
CB
TRP
213
31.506
20.331
35.082
1.00
15.34


ATOM
1148
CG
TRP
213
31.110
21.741
34.725
1.00
15.79


ATOM
1149
CD2
TRP
213
29.792
22.209
34.413
1.00
15.16


ATOM
1150
CE2
TRP
213
29.885
23.601
34.179
1.00
16.51


ATOM
1151
CE3
TRP
213
28.538
21.588
34.312
1.00
16.54


ATOM
1152
CD1
TRP
213
31.929
22.837
34.666
1.00
16.30


ATOM
1153
NE1
TRP
213
31.199
23.958
34.338
1.00
15.53


ATOM
1154
CZ2
TRP
213
28.771
24.382
33.849
1.00
14.24


ATOM
1155
CZ3
TRP
213
27.432
22.366
33.985
1.00
16.40


ATOM
1156
CH2
TRP
213
27.558
23.748
33.756
1.00
15.28


ATOM
1157
C
TRP
213
29.985
20.138
37.057
1.00
15.56


ATOM
1158
O
TRP
213
29.634
21.070
37.779
1.00
13.86


ATOM
1159
N
GLU
214
29.149
19.192
36.639
1.00
15.67


ATOM
1160
CA
GLU
214
27.741
19.178
37.019
1.00
15.17


ATOM
1161
CB
GLU
214
26.982
18.139
36.187
1.00
17.45


ATOM
1162
CG
GLU
214
25.473
18.101
36.444
1.00
19.85


ATOM
1163
CD
GLU
214
24.785
19.410
36.087
1.00
23.48


ATOM
1164
OE1
GLU
214
25.012
19.911
34.968
1.00
25.84


ATOM
1165
OE2
GLU
214
24.012
19.938
36.918
1.00
26.74


ATOM
1166
C
GLU
214
27.576
18.857
38.499
1.00
16.13


ATOM
1167
O
GLU
214
26.791
19.497
39.206
1.00
15.22


ATOM
1168
N
GLY
215
28.321
17.858
38.962
1.00
17.03


ATOM
1169
CA
GLY
215
28.244
17.452
40.352
1.00
17.32


ATOM
1170
C
GLY
215
28.530
18.576
41.328
1.00
18.14


ATOM
1171
O
GLY
215
27.812
18.750
42.312
1.00
18.29


ATOM
1172
N
TRP
216
29.584
19.340
41.067
1.00
17.32


ATOM
1173
CA
TRP
216
29.940
20.440
41.952
1.00
16.83


ATOM
1174
CB
TRP
216
31.209
21.145
41.459
1.00
15.21


ATOM
1175
CG
TRP
216
31.605
22.288
42.345
1.00
16.54


ATOM
1176
CD2
TRP
216
31.879
22.226
43.751
1.00
17.16


ATOM
1177
CE2
TRP
216
32.141
23.544
44.185
1.00
16.95


ATOM
1178
CE3
TRP
216
31.924
21.182
44.689
1.00
17.45


ATOM
1179
CD1
TRP
216
31.716
23.603
41.991
1.00
14.98


ATOM
1180
NE1
TRP
216
32.036
24.364
43.092
1.00
17.71


ATOM
1181
CZ2
TRP
216
32.444
23.849
45.518
1.00
16.83


ATOM
1182
CZ3
TRP
216
32.225
21.487
46.016
1.00
17.47


ATOM
1183
CH2
TRP
216
32.480
22.811
46.415
1.00
18.90


ATOM
1184
C
TRP
216
28.796
21.441
42.028
1.00
15.17


ATOM
1185
O
TRP
216
28.422
21.900
43.105
1.00
17.84


ATOM
1186
N
ARG
217
28.234
21.779
40.878
1.00
15.34


ATOM
1187
CA
ARG
217
27.136
22.724
40.854
1.00
16.45


ATOM
1188
CB
ARG
217
26.868
23.142
39.407
1.00
13.86


ATOM
1189
CG
ARG
217
27.981
24.074
38.923
1.00
16.46


ATOM
1190
CD
ARG
217
28.079
24.265
37.416
1.00
15.80


ATOM
1191
NE
ARG
217
29.144
25.230
37.139
1.00
15.22


ATOM
1192
CZ
ARG
217
30.444
24.974
37.269
1.00
15.55


ATOM
1193
NH1
ARG
217
31.333
25.920
37.009
1.00
16.82


ATOM
1194
NH2
ARG
217
30.860
23.766
37.632
1.00
15.71


ATOM
1195
C
ARG
217
25.903
22.145
41.547
1.00
17.65


ATOM
1196
O
ARG
217
25.202
22.858
42.263
1.00
17.39


ATOM
1197
N
ASP
218
25.661
20.848
41.374
1.00
18.73


ATOM
1198
CA
ASP
218
24.513
20.215
42.021
1.00
20.64


ATOM
1199
CB
ASP
218
24.388
18.745
41.612
1.00
22.06


ATOM
1200
CG
ASP
218
24.011
18.570
40.161
1.00
24.98


ATOM
1201
OD1
ASP
218
23.555
19.550
39.537
1.00
24.48


ATOM
1202
OD2
ASP
218
24.158
17.437
39.648
1.00
26.98


ATOM
1203
C
ASP
218
24.610
20.272
43.545
1.00
19.56


ATOM
1204
O
ASP
218
23.619
20.520
44.227
1.00
19.81


ATOM
1205
N
LYS
219
25.807
20.043
44.077
1.00
20.45


ATOM
1206
CA
LYS
219
26.003
20.031
45.525
1.00
21.29


ATOM
1207
CB
LYS
219
27.121
19.051
45.890
1.00
21.65


ATOM
1208
CG
LYS
219
26.895
17.629
45.373
1.00
25.13


ATOM
1209
CD
LYS
219
25.543
17.058
45.813
1.00
28.05


ATOM
1210
CE
LYS
219
25.447
16.918
47.328
1.00
29.00


ATOM
1211
NZ
LYS
219
26.538
16.060
47.868
1.00
30.61


ATOM
1212
C
LYS
219
26.279
21.378
46.183
1.00
21.42


ATOM
1213
O
LYS
219
25.719
21.678
47.236
1.00
24.45


ATOM
1214
N
ALA
220
27.143
22.188
45.579
1.00
21.30


ATOM
1215
CA
ALA
220
27.468
23.492
46.153
1.00
20.70


ATOM
1216
CB
ALA
220
28.902
23.878
45.799
1.00
20.00


ATOM
1217
C
ALA
220
26.504
24.578
45.685
1.00
19.99


ATOM
1218
O
ALA
220
25.902
25.276
46.501
1.00
21.16


ATOM
1219
N
GLY
221
26.358
24.711
44.370
1.00
18.26


ATOM
1220
CA
GLY
221
25.476
25.722
43.819
1.00
18.25


ATOM
1221
C
GLY
221
24.028
25.653
44.275
1.00
19.99


ATOM
1222
O
GLY
221
23.496
26.628
44.808
1.00
19.79


ATOM
1223
N
ARG
222
23.378
24.512
44.067
1.00
17.04


ATOM
1224
CA
ARG
222
21.982
24.377
44.467
1.00
19.12


ATOM
1225
CB
ARG
222
21.443
22.989
44.091
1.00
17.89


ATOM
1226
CG
ARG
222
21.397
22.730
42.592
1.00
19.59


ATOM
1227
CD
ARG
222
20.767
21.367
42.283
1.00
24.35


ATOM
1228
NE
ARG
222
20.643
21.152
40.845
1.00
30.28


ATOM
1229
CZ
ARG
222
20.353
19.984
40.276
1.00
33.18


ATOM
1230
NH1
ARG
222
20.150
18.901
41.021
1.00
31.51


ATOM
1231
NH2
ARG
222
20.281
19.896
38.954
1.00
33.98


ATOM
1232
C
ARG
222
21.800
24.611
45.965
1.00
18.43


ATOM
1233
O
ARG
222
20.803
25.193
46.385
1.00
19.58


ATOM
1234
N
ALA
223
22.771
24.171
46.757
1.00
16.28


ATOM
1235
CA
ALA
223
22.715
24.317
48.210
1.00
19.92


ATOM
1236
CB
ALA
223
23.824
23.483
48.859
1.00
19.14


ATOM
1237
C
ALA
223
22.815
25.767
48.681
1.00
19.46


ATOM
1238
O
ALA
223
22.435
26.089
49.806
1.00
22.30


ATOM
1239
N
ILE
224
23.329
26.646
47.833
1.00
18.66


ATOM
1240
CA
ILE
224
23.457
28.045
48.222
1.00
17.34


ATOM
1241
CB
ILE
224
24.679
28.705
47.522
1.00
16.89


ATOM
1242
CG2
ILE
224
24.729
30.202
47.819
1.00
15.15


ATOM
1243
CG1
ILE
224
25.966
28.023
47.993
1.00
14.94


ATOM
1244
CD1
ILE
224
26.218
28.141
49.488
1.00
15.97


ATOM
1245
C
ILE
224
22.187
28.830
47.897
1.00
17.43


ATOM
1246
O
ILE
224
21.883
29.825
48.550
1.00
18.29


ATOM
1247
N
LEU
225
21.435
28.360
46.907
1.00
16.61


ATOM
1248
CA
LEU
225
20.217
29.044
46.480
1.00
18.87


ATOM
1249
CB
LEU
225
19.511
28.233
45.386
1.00
17.28


ATOM
1250
CG
LEU
225
28.251
28.880
44.803
1.00
17.62


ATOM
1251
CD1
LEU
225
18.591
30.250
44.247
1.00
15.98


ATOM
1252
CD2
LEU
225
17.664
27.993
43.712
1.00
17.36


ATOM
1253
C
LEU
225
19.208
29.387
47.582
1.00
20.30


ATOM
1254
O
LEU
225
18.573
30.440
47.529
1.00
21.05


ATOM
1255
N
GLN
226
19.054
28.522
48.582
1.00
20.59


ATOM
1256
CA
GLN
226
18.086
28.812
49.635
1.00
20.98


ATOM
1257
CB
GLN
226
17.887
27.602
50.554
1.00
22.39


ATOM
1258
CG
GLN
226
19.098
27.206
51.373
1.00
22.59


ATOM
1259
CD
GLN
226
18.743
26.255
52.506
1.00
28.86


ATOM
1260
OE1
GLN
226
19.401
25.236
52.708
1.00
29.99


ATOM
1261
NE2
GLN
226
17.702
26.594
53.259
1.00
30.07


ATOM
1262
C
GLN
226
18.460
30.027
50.476
1.00
20.99


ATOM
1263
O
GLN
226
17.594
30.624
51.113
1.00
20.68


ATOM
1264
N
PHE
227
19.738
30.402
50.472
1.00
17.78


ATOM
1265
CA
PHE
227
20.188
31.548
51.261
1.00
18.81


ATOM
1266
CE
PHE
227
21.555
31.278
51.901
1.00
18.57


ATOM
1267
CG
PHE
227
21.626
30.016
52.709
1.00
20.93


ATOM
1268
CD1
PHE
227
22.241
28.881
52.191
1.00
19.23


ATOM
1269
CD2
PHE
227
21.106
29.970
53.998
1.00
19.89


ATOM
1270
CE1
PHE
227
22.340
27.720
52.945
1.00
20.37


ATOM
1271
CE2
PHE
227
21.198
28.812
54.763
1.00
20.86


ATOM
1272
CZ
PHE
227
21.818
27.683
54.236
1.00
21.52


ATOM
1273
C
PHE
227
20.320
32.875
50.515
1.00
18.52


ATOM
1274
O
PHE
227
20.150
33.936
51.116
1.00
18.03


ATOM
1275
N
TYR
228
20.631
32.824
49.220
1.00
17.84


ATOM
1276
CA
TYR
228
20.870
34.046
48.458
1.00
15.89


ATOM
1277
CB
TYR
228
21.267
33.716
47.013
1.00
14.37


ATOM
1278
CG
TYR
228
22.396
34.599
46.526
1.00
13.39


ATOM
1279
CD1
TYR
228
23.678
34.485
47.068
1.00
11.77


ATOM
1280
CE1
TYR
228
24.720
35.322
46.653
1.00
12.65


ATOM
1281
CD2
TYR
228
22.178
35.573
45.555
1.00
14.08


ATOM
1282
CE2
TYR
228
23.207
36.420
45.134
1.00
13.53


ATOM
1283
CZ
TYR
228
24.472
36.289
45.685
1.00
24.24


ATOM
1284
OH
TYR
228
25.484
37.127
45.274
1.00
15.11


ATOM
1285
C
TYR
228
19.817
35.146
48.437
1.00
16.77


ATOM
1286
O
TYR
228
20.143
36.313
48.645
1.00
16.17


ATOM
1287
N
PRO
229
18.546
34.805
48.173
1.00
16.14


ATOM
1288
CD
PRO
229
17.939
33.525
47.766
1.00
16.20


ATOM
1289
CA
PRO
229
17.556
35.887
48.156
1.00
16.22


ATOM
1290
CB
PRO
229
16.240
35.150
47.888
1.00
16.46


ATOM
1291
CG
PRO
229
16.688
33.982
47.027
1.00
16.36


ATOM
1292
C
PRO
229
17.525
36.702
49.451
1.00
16.67


ATOM
1293
O
PRO
229
17.395
37.924
49.414
1.00
18.90


ATOM
1294
N
LYS
230
17.655
36.030
50.590
1.00
17.12


ATOM
1295
CA
LYS
230
17.629
36.717
51.881
1.00
18.28


ATOM
1296
CB
LYS
230
17.459
35.711
53.019
1.00
20.03


ATOM
1297
CG
LYS
230
16.968
36.337
54.314
1.00
24.93


ATOM
1298
CD
LYS
230
15.626
37.010
54.076
1.00
29.71


ATOM
1299
CE
LYS
230
14.991
37.481
55.356
1.00
33.08


ATOM
1300
NZ
LYS
230
13.687
38.138
55.078
1.00
33.19


ATOM
1301
C
LYS
230
18.909
37.525
52.090
1.00
17.96


ATOM
1302
O
LYS
230
18.886
38.617
52.662
1.00
15.33


ATOM
1303
N
TYR
231
20.022
36.971
51.627
1.00
16.71


ATOM
1304
CA
TYR
231
21.314
37.638
51.715
1.00
16.94


ATOM
1305
CB
TYR
231
22.383
36.730
51.107
1.00
14.95


ATOM
1306
CG
TYR
231
23.567
37.445
50.490
1.00
13.63


ATOM
1307
CD1
TYR
231
24.576
37.988
51.286
1.00
13.32


ATOM
1308
CE1
TYR
231
25.693
38.608
50.715
1.00
14.67


ATOM
1309
CD2
TYR
231
23.694
37.543
49.101
1.00
14.54


ATOM
1310
CE2
TYR
231
24.802
38.162
48.518
1.00
13.31


ATOM
1311
CZ
TYR
231
25.797
38.688
49.329
1.00
12.39


ATOM
1312
OH
TYR
231
26.899
39.279
48.764
1.00
13.70


ATOM
1313
C
TYR
231
21.251
38.961
50.949
1.00
14.98


ATOM
1314
O
TYR
231
21.702
39.997
51.434
1.00
14.92


ATOM
1315
N
VAL
232
20.695
38.910
49.742
1.00
16.25


ATOM
1316
CA
VAL
232
20.568
40.091
48.888
1.00
15.73


ATOM
1317
CB
VAL
232
19.978
39.693
47.511
1.00
16.32


ATOM
1318
CG1
VAL
232
19.518
40.922
46.744
1.00
14.95


ATOM
1319
CG2
VAL
232
21.041
38.931
46.706
1.00
14.49


ATOM
1320
C
VAL
232
19.705
41.168
49.546
1.00
17.00


ATOM
1321
O
VAL
232
20.044
42.359
49.532
1.00
14.95


ATOM
1322
N
GLU
233
18.596
40.742
50.136
1.00
16.77


ATOM
1323
CA
GLU
233
17.695
41.670
50.802
1.00
18.55


ATOM
1324
CB
GLU
233
16.459
40.919
51.315
1.00
20.59


ATOM
1325
CG
GLU
233
15.554
41.728
52.234
1.00
27.30


ATOM
1326
CD
GLU
233
14.310
40.956
52.658
1.00
32.53


ATOM
1327
OE1
GLU
233
14.424
39.751
52.977
1.00
32.64


ATOM
1328
OE2
GLU
233
13.217
41.561
52.679
1.00
38.43


ATOM
1329
C
GLU
233
18.413
42.355
51.959
1.00
17.80


ATOM
1330
O
GLU
233
18.380
43.576
52.081
1.00
17.11


ATOM
1331
N
LEU
234
19.084
41.566
52.791
1.00
17.72


ATOM
1332
CA
LEU
234
19.782
42.107
53.951
1.00
17.47


ATOM
1333
CB
LEU
234
20.161
40.971
54.906
1.00
17.40


ATOM
1334
CG
LEU
234
18.941
40.262
55.503
1.00
22.59


ATOM
1335
CD1
LEU
234
19.386
39.093
56.366
1.00
22.34


ATOM
1336
CD2
LEU
234
18.119
41.256
56.319
1.00
22.15


ATOM
1337
C
LEU
234
21.006
42.963
53.638
1.00
17.17


ATOM
1338
O
LEU
234
21.205
43.995
54.273
1.00
16.30


ATOM
1339
N
ILE
235
21.823
42.560
52.666
1.00
14.58


ATOM
1340
CA
ILE
235
23.000
43.363
52.355
1.00
14.01


ATOM
1341
CB
ILE
235
24.023
42.592
51.472
1.00
13.57


ATOM
1342
CG2
ILE
235
23.462
42.349
50.074
1.00
12.52


ATOM
1343
CG1
ILE
235
25.331
43.389
51.395
1.00
11.74


ATOM
1344
CD1
ILE
235
26.469
42.632
50.735
1.00
11.93


ATOM
1345
C
ILE
235
22.563
44.661
51.679
1.00
14.36


ATOM
1346
O
ILE
235
23.193
45.705
51.857
1.00
13.51


ATOM
1347
N
ASN
236
21.474
44.600
50.916
1.00
14.39


ATOM
1348
CA
ASN
236
20.951
45.798
50.261
1.00
15.23


ATOM
1349
CB
ASN
236
19.837
45.448
49.264
1.00
15.19


ATOM
1350
CG
ASN
236
20.365
45.201
47.862
1.00
15.72


ATOM
1351
OD1
ASN
236
21.519
45.501
47.560
1.00
15.27


ATOM
1352
ND2
ASN
236
19.512
44.667
46.992
1.00
18.17


ATOM
1353
C
ASN
236
20.394
46.751
51.322
1.00
15.66


ATOM
1354
O
ASN
236
20.570
47.964
51.231
1.00
16.15


ATOM
1355
N
GLN
237
19.721
46.190
52.322
1.00
17.57


ATOM
1356
CA
GLN
237
19.146
46.989
53.404
1.00
18.43


ATOM
1357
CB
GLN
237
18.391
46.090
54.391
1.00
19.68


ATOM
1358
CG
GLN
237
17.537
46.858
55.391
1.00
22.74


ATOM
1359
CD
GLN
237
16.845
45.947
56.397
1.00
25.62


ATOM
1360
OE1
GLN
237
16.460
44.821
56.073
1.00
25.13


ATOM
1361
NE2
GLN
237
16.667
46.441
57.620
1.00
25.08


ATOM
1362
C
GLN
237
20.261
47.727
54.139
1.00
17.44


ATOM
1363
O
GLN
237
20.158
48.924
54.402
1.00
17.22


ATOM
1364
N
ALA
238
21.323
47.003
54.478
1.00
15.64


ATOM
1365
CA
ALA
238
22.460
47.604
55.162
1.00
16.63


ATOM
1366
CB
ALA
238
23.530
46.549
55.436
1.00
14.09


ATOM
1367
C
ALA
238
23.038
48.727
54.303
1.00
16.39


ATOM
1368
O
ALA
238
23.385
49.790
54.813
1.00
18.77


ATOM
1369
N
ALA
239
23.142
48.484
52.998
1.00
15.79


ATOM
1370
CA
ALA
239
23.672
49.482
52.076
1.00
16.70


ATOM
1371
CB
ALA
239
23.725
48.921
50.650
1.00
14.56


ATOM
1372
C
ALA
239
22.827
50.758
52.102
1.00
17.22


ATOM
1373
O
ALA
239
23.369
51.866
52.172
1.00
14.26


ATOM
1374
N
ARG
240
21.505
50.606
52.043
1.00
15.36


ATOM
1375
CA
ARG
240
20.622
51.774
52.064
1.00
17.46


ATOM
1376
CB
ARG
240
19.162
51.376
51.793
1.00
15.33


ATOM
1377
CG
ARG
240
18.893
50.824
50.388
1.00
17.28


ATOM
1378
CD
ARG
240
17.393
50.778
50.080
1.00
16.93


ATOM
1379
NE
ARG
240
16.638
50.067
51.108
1.00
19.77


ATOM
1380
CZ
ARG
240
16.521
48.744
51.180
1.00
22.01


ATOM
1381
NH1
ARG
240
17.107
47.966
50.271
1.00
19.52


ATOM
1382
NH2
ARG
240
15.823
48.197
52.169
1.00
18.66


ATOM
1383
C
ARG
240
20.701
52.506
53.404
1.00
17.66


ATOM
1384
O
ARG
240
20.569
53.729
53.460
1.00
16.54


ATOM
1385
N
LEU
241
20.916
51.759
54.482
1.00
17.65


ATOM
1386
CA
LEU
241
21.005
52.374
55.800
1.00
19.55


ATOM
1387
CB
LEU
241
20.827
51.315
56.898
1.00
19.64


ATOM
1388
CG
LEU
241
19.413
50.726
57.017
1.00
19.83


ATOM
1389
CD1
LEU
241
19.416
49.573
57.999
1.00
20.06


ATOM
1390
CD2
LEU
241
18.434
51.804
57.470
1.00
22.50


ATOM
1391
C
LEU
241
22.326
53.117
55.973
1.00
19.27


ATOM
1392
O
LEU
241
22.548
53.783
56.986
1.00
20.50


ATOM
1393
N
ASN
242
23.202
53.001
54.980
1.00
16.73


ATOM
1394
CA
ASN
242
24.481
53.693
55.021
1.00
16.25


ATOM
1395
CB
ASN
242
25.636
52.697
54.897
1.00
15.12


ATOM
1396
CG
ASN
242
25.891
51.952
56.195
1.00
19.42


ATOM
1397
OD1
ASN
242
26.139
52.571
57.234
1.00
19.98


ATOM
1398
ND2
ASN
242
25.825
50.622
56.148
1.00
18.09


ATOM
1399
C
ASN
242
24.572
54.763
53.934
1.00
17.24


ATOM
1400
O
ASN
242
25.652
55.290
53.655
1.00
17.37


ATOM
1401
N
GLY
243
23.429
55.066
53.321
1.00
15.75


ATOM
1402
CA
GLY
243
23.373
56.099
52.299
1.00
16.87


ATOM
1403
C
GLY
243
23.543
55.696
50.844
1.00
15.89


ATOM
1404
O
GLY
243
23.626
56.565
49.978
1.00
15.97


ATOM
1405
N
TYR
244
23.608
54.398
50.565
1.00
16.21


ATOM
1406
CA
TYR
244
23.764
53.922
49.189
1.00
14.57


ATOM
1407
CB
TYR
244
24.761
52.757
49.135
1.00
14.48


ATOM
1408
CG
TYR
244
26.167
53.146
49.521
1.00
15.74


ATOM
1409
CD1
TYR
244
26.665
52.860
50.787
1.00
14.52


ATOM
1410
CE1
TYR
244
27.951
53.250
51.158
1.00
16.68


ATOM
1411
CD2
TYR
244
26.989
53.833
48.627
1.00
16.81


ATOM
1412
CE2
TYR
244
28.274
54.231
48.988
1.00
16.81


ATOM
1413
CZ
TYR
244
28.747
53.935
50.255
1.00
16.66


ATOM
1414
OH
TYR
244
30.013
54.329
50.619
1.00
20.02


ATOM
1415
C
TYR
244
22.423
53.462
48.628
1.00
15.50


ATOM
1416
O
TYR
244
21.483
53.254
49.385
1.00
17.45


ATOM
1417
N
VAL
245
22.325
53.308
47.307
1.00
15.80


ATOM
1418
CA
VAL
245
21.069
52.854
46.713
1.00
15.94


ATOM
1419
CB
VAL
245
20.945
53.283
45.227
1.00
19.25


ATOM
1420
CG1
VAL
245
20.843
54.804
45.137
1.00
21.35


ATOM
1421
CG2
VAL
245
22.133
52.795
44.436
1.00
19.37


ATOM
1422
C
VAL
245
20.926
51.335
46.830
1.00
15.52


ATOM
1423
O
VAL
245
19.810
50.817
46.890
1.00
16.08


ATOM
1424
N
ASP
246
22.057
50.630
46.871
1.00
12.67


ATOM
1425
CA
ASP
246
22.077
49.169
47.017
1.00
12.71


ATOM
1426
CB
ASP
246
21.487
48.477
45.776
1.00
10.13


ATOM
1427
CG
ASP
246
22.273
48.765
44.509
1.00
12.08


ATOM
1428
OD1
ASP
246
23.483
48.446
44.453
1.00
15.10


ATOM
1429
OD2
ASP
246
21.676
49.312
43.561
1.00
15.37


ATOM
1430
C
ASP
246
23.507
48.677
47.273
1.00
11.44


ATOM
1431
O
ASP
246
24.450
49.463
47.236
1.00
12.92


ATOM
1432
N
ALA
247
23.666
47.381
47.537
1.00
12.55


ATOM
1433
CA
ALA
247
24.986
46.813
47.819
1.00
12.99


ATOM
1434
CB
ALA
247
24.855
45.318
48.148
1.00
12.30


ATOM
1435
C
ALA
247
26.016
47.011
46.704
1.00
11.82


ATOM
1436
O
ALA
247
27.204
47.218
46.975
1.00
12.97


ATOM
1437
N
GLY
248
25.570
46.935
45.453
1.00
10.87


ATOM
1438
CA
GLY
248
26.484
47.116
44.335
1.00
10.26


ATOM
1439
C
GLY
248
27.077
48.512
44.352
1.00
13.13


ATOM
1440
O
GLY
248
28.277
48.708
44.134
1.00
13.09


ATOM
1441
N
ASP
249
26.214
49.490
44.606
1.00
14.71


ATOM
1442
CA
ASP
249
26.615
50.894
44.685
1.00
15.46


ATOM
1443
CB
ASP
249
25.369
51.744
44.977
1.00
15.97


ATOM
1444
CG
ASP
249
25.671
53.226
45.132
1.00
17.81


ATOM
1445
OD1
ASP
249
26.503
53.765
44.373
1.00
16.36


ATOM
1446
OD2
ASP
249
25.040
53.856
46.005
1.00
18.13


ATOM
1447
C
ASP
249
27.652
51.008
45.804
1.00
15.19


ATOM
1448
O
ASP
249
28.718
51.598
45.626
1.00
14.88


ATOM
1449
N
SER
250
27.346
50.418
46.954
1.00
15.48


ATOM
1450
CA
SER
250
28.267
50.448
48.083
1.00
15.85


ATOM
1451
CB
SER
250
27.669
49.667
49.257
1.00
18.56


ATOM
1452
OG
SER
250
28.534
49.703
50.376
1.00
19.16


ATOM
1453
C
SER
250
29.650
49.877
47.723
1.00
15.52


ATOM
1454
O
SER
250
30.680
50.479
48.036
1.00
13.65


ATOM
1455
N
TRP
251
29.676
48.718
47.065
1.00
14.06


ATOM
1456
CA
TRP
251
30.945
48.093
46.672
1.00
14.44


ATOM
1457
CB
TRP
251
30.700
46.698
46.082
1.00
13.11


ATOM
1458
CG
TRP
251
30.248
45.674
47.075
1.00
14.95


ATOM
1459
CD2
TRP
251
30.022
44.282
46.820
1.00
15.48


ATOM
1460
CE2
TRP
251
29.626
43.691
48.041
1.00
17.39


ATOM
1461
CE3
TRP
251
30.117
43.477
45.676
1.00
12.92


ATOM
1462
CD1
TRP
251
29.985
45.868
48.405
1.00
16.16


ATOM
1463
NE1
TRP
251
29.612
44.680
48.992
1.00
16.30


ATOM
1464
CZ2
TRP
251
29.323
42.323
48.151
1.00
16.20


ATOM
1465
CZ3
TRP
251
29.817
42.120
45.784
1.00
15.52


ATOM
1466
CH2
TRP
251
29.425
41.558
47.014
1.00
15.29


ATOM
1467
C
TRP
251
31.735
48.923
45.662
1.00
14.40


ATOM
1468
O
TRP
251
32.956
49.057
45.776
1.00
11.76


ATOM
1469
N
ARG
252
31.043
49.471
44.665
1.00
14.90


ATOM
1470
CA
ARG
252
31.714
50.272
43.655
1.00
13.31


ATOM
1471
CB
ARG
252
30.740
50.668
42.528
1.00
14.60


ATOM
1472
CG
ARG
252
30.243
49.494
41.672
1.00
14.42


ATOM
1473
CD
ARG
252
29.472
49.970
40.447
1.00
12.08


ATOM
1474
NE
ARG
252
28.233
50.687
40.771
1.00
13.50


ATOM
1475
CZ
ARG
252
27.063
50.107
41.037
1.00
14.82


ATOM
1476
NH1
ARG
252
26.002
50.854
41.319
1.00
13.27


ATOM
1477
NH2
ARG
252
26.942
48.783
41.011
1.00
13.16


ATOM
1478
C
ARG
252
32.337
51.527
44.267
1.00
16.12


ATOM
1479
O
ARG
252
33.361
52.004
43.787
1.00
14.85


ATOM
1480
N
SER
253
31.730
52.050
45.332
1.00
15.54


ATOM
1481
CA
SER
253
32.239
53.260
45.977
1.00
16.04


ATOM
1482
CB
SER
253
31.309
53.703
47.112
1.00
16.20


ATOM
1483
OG
SER
253
31.590
52.997
48.309
1.00
20.61


ATOM
1484
C
SER
253
33.652
53.086
46.527
1.00
14.43


ATOM
1485
O
SER
253
34.339
54.069
46.789
1.00
14.48


ATOM
1486
N
MET
254
34.085
51.840
46.697
1.00
14.27


ATOM
1487
CA
MET
254
35.429
51.562
47.209
1.00
16.48


ATOM
1488
CB
MET
254
35.657
50.051
47.360
1.00
17.80


ATOM
1489
CG
MET
254
34.740
49.358
48.359
1.00
21.06


ATOM
1490
SD
MET
254
35.187
47.614
48.574
1.00
31.02


ATOM
1491
CE
MET
254
34.226
46.857
47.338
1.00
27.13


ATOM
1492
C
MET
254
36.517
52.121
46.298
1.00
15.51


ATOM
1493
O
MET
254
37.666
52.265
46.714
1.00
16.06


ATOM
1494
N
TYR
255
36.163
52.423
45.053
1.00
14.88


ATOM
1495
CA
TYR
255
37.135
52.956
44.105
1.00
15.20


ATOM
1496
CB
TYR
255
36.904
52.360
42.704
1.00
15.30


ATOM
1497
CG
TYR
255
37.206
50.880
42.631
1.00
13.36


ATOM
1498
CD1
TYR
255
36.245
49.935
42.986
1.00
12.66


ATOM
1499
CE1
TYR
255
36.544
48.568
43.000
1.00
13.69


ATOM
1500
CD2
TYR
255
38.479
50.427
42.281
1.00
12.94


ATOM
1501
CE2
TYR
255
38.792
49.064
42.293
1.00
14.05


ATOM
1502
CZ
TYR
255
37.818
48.143
42.659
1.00
13.41


ATOM
1503
OH
TYR
255
38.129
46.806
42.721
1.00
13.11


ATOM
1504
C
TYR
255
37.126
54.479
44.023
1.00
14.46


ATOM
1505
O
TYR
255
38.000
55.068
43.393
1.00
14.81


ATOM
1506
N
GLU
256
36.139
55.111
44.654
1.00
15.24


ATOM
1507
CA
GLU
256
36.028
56.574
44.642
1.00
16.61


ATOM
1508
CB
GLU
256
37.103
57.195
45.539
1.00
17.37


ATOM
1509
CG
GLU
256
37.109
56.665
46.966
1.00
22.10


ATOM
1510
CD
GLU
256
38.044
57.453
47.878
1.00
23.83


ATOM
1511
OE1
GLU
256
39.253
57.535
47.579
1.00
26.54


ATOM
1512
OE2
GLU
256
37.565
57.988
48.894
1.00
26.05


ATOM
1513
C
GLU
256
36.191
57.103
43.222
1.00
15.97


ATOM
1514
O
GLU
256
36.852
58.114
42.991
1.00
16.36


ATOM
1515
N
THR
257
35.575
56.413
42.273
1.00
16.18


ATOM
1516
CA
THR
257
35.678
56.786
40.872
1.00
17.13


ATOM
1517
CB
THR
257
36.628
55.824
40.144
1.00
18.70


ATOM
1518
OG1
THR
257
37.905
55.848
40.796
1.00
17.37


ATOM
1519
CG2
THR
257
36.789
56.226
38.679
1.00
17.93


ATOM
1520
C
THR
257
34.309
56.761
40.201
1.00
16.00


ATOM
1521
O
THR
257
33.818
55.707
39.797
1.00
15.27


ATOM
1522
N
PRO
258
33.673
57.936
40.077
1.00
15.23


ATOM
1523
CD
PRO
258
34.141
59.242
40.584
1.00
15.95


ATOM
1524
CA
PRO
258
32.349
58.057
39.456
1.00
15.97


ATOM
1525
CB
PRO
258
32.120
59.569
39.426
1.00
16.42


ATOM
1526
CG
PRO
258
32.851
60.041
40.663
1.00
16.92


ATOM
1527
C
PRO
258
32.254
57.434
38.064
1.00
15.58


ATOM
1528
O
PRO
258
31.208
56.909
37.683
1.00
16.29


ATOM
1529
N
SER
259
33.348
57.487
37.310
1.00
15.31


ATOM
1530
CA
SER
259
33.355
56.939
35.953
1.00
15.70


ATOM
1531
CB
SER
259
34.330
57.740
35.085
1.00
17.61


ATOM
1532
OG
SER
259
35.657
57.612
35.573
1.00
18.28


ATOM
1533
C
SER
259
33.728
55.452
35.884
1.00
14.57


ATOM
1534
O
SER
259
33.917
54.913
34.798
1.00
13.39


ATOM
1535
N
LEU
260
33.810
54.790
37.036
1.00
13.86


ATOM
1536
CA
LEU
260
34.200
53.376
37.094
1.00
14.52


ATOM
1537
CB
LEU
260
33.936
52.806
38.497
1.00
14.33


ATOM
1538
CG
LEU
260
34.446
51.379
38.763
1.00
17.84


ATOM
1539
CD1
LEU
260
35.965
51.348
38.632
1.00
17.38


ATOM
1540
CD2
LEU
260
34.033
50.922
40.161
1.00
17.16


ATOM
1541
C
LEU
260
33.577
52.437
36.056
1.00
13.87


ATOM
1542
O
LEU
260
34.299
51.777
35.311
1.00
9.84


ATOM
1543
N
GLU
261
32.248
52.363
36.003
1.00
13.07


ATOM
1544
CA
GLU
261
31.607
51.448
35.061
1.00
14.77


ATOM
1545
CB
GLU
261
30.079
51.514
35.191
1.00
12.37


ATOM
1546
CG
GLU
261
29.591
51.176
36.596
1.00
15.59


ATOM
1547
CD
GLU
261
28.174
50.633
36.623
1.00
17.28


ATOM
1548
OE1
GLU
261
27.524
50.604
35.560
1.00
21.19


ATOM
1549
OE2
GLU
261
27.714
50.234
37.712
1.00
18.05


ATOM
1550
C
GLU
261
32.030
51.664
33.618
1.00
14.11


ATOM
1551
O
GLU
261
32.295
50.704
32.895
1.00
14.05


ATOM
1552
N
GLN
262
32.108
52.919
33.200
1.00
15.79


ATOM
1553
CA
GLN
262
32.522
53.232
31.839
1.00
16.53


ATOM
1554
CB
GLN
262
32.280
54.712
31.547
1.00
21.41


ATOM
1555
CG
GLN
262
30.809
55.095
31.459
1.00
27.97


ATOM
1556
CD
GLN
262
30.587
56.587
31.641
1.00
32.44


ATOM
1557
OE1
GLN
262
29.655
57.162
31.077
1.00
34.42


ATOM
1558
NE2
GLN
262
31.439
57.220
32.447
1.00
33.41


ATOM
1559
C
GLN
262
34.001
52.901
31.642
1.00
17.20


ATOM
1560
O
GLN
262
34.382
52.314
30.625
1.00
15.46


ATOM
1561
N
ASP
263
34.830
53.280
32.612
1.00
16.67


ATOM
1562
CA
ASP
263
36.263
53.011
32.524
1.00
15.94


ATOM
1563
CB
ASP
263
36.998
53.485
33.781
1.00
19.14


ATOM
1564
CG
ASP
263
37.032
54.998
33.914
1.00
22.47


ATOM
1565
OD1
ASP
263
37.016
55.698
32.878
1.00
21.52


ATOM
1566
OD2
ASP
263
37.097
55.486
35.060
1.00
22.10


ATOM
1567
C
ASP
263
36.535
51.519
32.346
1.00
16.31


ATOM
1568
O
ASP
263
37.341
51.121
31.507
1.00
17.06


ATOM
1569
N
LEU
264
35.866
50.696
33.146
1.00
15.79


ATOM
1570
CA
LEU
264
36.056
49.251
33.082
1.00
16.11


ATOM
1571
CB
LEU
264
35.334
48.585
34.258
1.00
17.87


ATOM
1572
CG
LEU
264
35.807
49.044
35.641
1.00
18.11


ATOM
1573
CD1
LEU
264
35.050
48.285
36.717
1.00
19.50


ATOM
1574
CD2
LEU
264
37.303
48.819
35.781
1.00
19.36


ATOM
1575
C
LEU
264
35.567
48.667
31.757
1.00
16.10


ATOM
1576
O
LEU
264
36.175
47.746
31.215
1.00
14.50


ATOM
1577
N
GLU
265
34.468
49.206
31.240
1.00
17.12


ATOM
1578
CA
GLU
265
33.911
48.745
29.970
1.00
18.85


ATOM
1579
CB
GLU
265
32.571
49.440
29.708
1.00
21.26


ATOM
1580
CG
GLU
265
31.924
49.123
28.364
1.00
27.69


ATOM
1581
CD
GLU
265
31.617
47.648
28.189
1.00
34.09


ATOM
1582
OE1
GLU
265
31.001
47.050
29.100
1.00
36.70


ATOM
1583
OE2
GLU
265
31.984
47.087
27.134
1.00
37.08


ATOM
1584
C
GLU
265
34.890
49.034
28.830
1.00
19.85


ATOM
1585
O
GLU
265
35.077
48.207
27.935
1.00
19.78


ATOM
1586
N
ARG
266
35.515
50.210
28.859
1.00
17.74


ATOM
1587
CA
ARG
266
36.475
50.567
27.822
1.00
17.75


ATOM
1588
CB
ARG
266
36.920
52.026
27.970
1.00
20.40


ATOM
1589
CG
ARG
266
35.885
53.041
27.507
1.00
25.02


ATOM
1590
CD
ARG
266
36.506
54.424
27.397
1.00
28.27


ATOM
1591
NE
ARG
266
36.724
55.042
28.701
1.00
34.44


ATOM
1592
CZ
ARG
266
35.776
55.660
29.401
1.00
36.31


ATOM
1593
NH1
ARG
266
34.541
55.747
28.920
1.00
36.59


ATOM
1594
NH2
ARG
266
36.061
56.191
30.582
1.00
36.92


ATOM
1595
C
ARG
266
37.686
49.645
27.894
1.00
16.78


ATOM
1596
O
ARG
266
38.203
49.206
26.867
1.00
15.67


ATOM
1597
N
LEU
267
38.140
49.352
29.108
1.00
15.01


ATOM
1598
CA
LEU
267
39.280
48.459
29.289
1.00
14.82


ATOM
1599
CB
LEU
267
39.646
48.362
30.773
1.00
16.36


ATOM
1600
CG
LEU
267
40.160
49.672
31.381
1.00
16.60


ATOM
1601
CD1
LEU
267
40.344
49.515
32.884
1.00
16.07


ATOM
1602
CD2
LEU
267
41.486
50.064
30.709
1.00
15.87


ATOM
1603
C
LEU
267
38.932
47.076
28.743
1.00
17.23


ATOM
1604
O
LEU
267
39.737
46.439
28.054
1.00
15.82


ATOM
1605
N
PHE
268
37.723
46.616
29.046
1.00
15.48


ATOM
1606
CA
PHE
268
37.286
45.314
28.569
1.00
16.55


ATOM
1607
CB
PHE
268
35.879
44.994
29.062
1.00
18.24


ATOM
1608
CG
PHE
268
35.345
43.707
28.512
1.00
21.70


ATOM
1609
CD1
PHE
268
35.826
42.488
28.981
1.00
22.36


ATOM
1610
CD2
PHE
268
34.425
43.711
27.468
1.00
21.62


ATOM
1611
CE1
PHE
268
35.403
41.292
28.415
1.00
24.19


ATOM
1612
CE2
PHE
268
33.996
42.517
26.894
1.00
23.63


ATOM
1613
CZ
PHE
268
34.489
41.306
27.371
1.00
22.93


ATOM
1614
C
PHE
268
37.291
45.258
27.043
1.00
17.17


ATOM
1615
O
PHE
268
37.776
44.295
26.445
1.00
15.21


ATOM
1616
N
GLN
269
36.739
46.292
26.416
1.00
16.96


ATOM
1617
CA
GLN
269
36.677
46.361
24.962
1.00
17.31


ATOM
1618
CB
GLN
269
35.905
47.606
24.517
1.00
19.68


ATOM
1619
CG
GLN
269
34.408
47.569
24.831
1.00
24.90


ATOM
1620
CD
GLN
269
33.706
46.381
24.198
1.00
28.78


ATOM
1621
OE1
GLN
269
33.938
46.057
23.032
1.00
31.92


ATOM
1622
NE2
GLN
269
32.832
45.732
24.960
1.00
30.59


ATOM
1623
C
GLN
269
38.048
46.354
24.292
1.00
16.49


ATOM
1624
O
GLN
269
38.197
45.811
23.207
1.00
15.38


ATOM
1625
N
GLU
270
39.046
46.960
24.926
1.00
16.98


ATOM
1626
CA
GLU
270
40.386
46.992
24.345
1.00
20.14


ATOM
1627
CB
GLU
270
41.288
47.941
25.129
1.00
23.65


ATOM
1628
CG
GLU
270
40.839
49.382
25.073
1.00
30.06


ATOM
1629
CD
GLU
270
41.821
50.306
25.743
1.00
35.93


ATOM
1630
OE1
GLU
270
42.956
50.432
25.234
1.00
40.83


ATOM
1631
OE2
GLU
270
41.465
50.903
26.779
1.00
39.30


ATOM
1632
C
GLU
270
41.032
45.614
24.291
1.00
19.09


ATOM
1633
O
GLU
270
41.861
45.344
23.420
1.00
17.60


ATOM
1634
N
LEU
271
40.652
44.745
25.222
1.00
17.35


ATOM
1635
CA
LEU
271
41.197
43.393
25.269
1.00
18.44


ATOM
1636
CB
LEU
271
41.356
42.961
26.726
1.00
20.14


ATOM
1637
CG
LEU
271
42.655
43.506
27.322
1.00
24.11


ATOM
1638
CD1
LEU
271
42.449
43.927
28.754
1.00
26.75


ATOM
1639
CD2
LEU
271
43.731
42.429
27.210
1.00
25.08


ATOM
1640
C
LEU
271
40.366
42.366
24.495
1.00
18.59


ATOM
1641
O
LEU
271
40.722
41.188
24.434
1.00
17.40


ATOM
1642
N
GLN
272
39.270
42.818
23.894
1.00
18.72


ATOM
1643
CA
GLN
272
38.395
41.941
23.117
1.00
21.08


ATOM
1644
CB
GLN
272
37.207
42.734
22.565
1.00
22.80


ATOM
1645
CG
GLN
272
35.993
42.745
23.461
1.00
24.90


ATOM
1646
CD
GLN
272
35.383
41.367
23.607
1.00
27.57


ATOM
1647
OE1
GLN
272
35.940
40.495
24.274
1.00
28.36


ATOM
1648
NE2
GLN
272
34.235
41.161
22.973
1.00
28.83


ATOM
1649
C
GLN
272
39.098
41.233
21.960
1.00
21.24


ATOM
1650
O
GLN
272
39.024
40.010
22.835
1.00
23.38


ATOM
1651
N
PRO
273
39.783
41.992
21.091
1.00
21.84


ATOM
1652
CD
PRO
273
39.893
43.462
21.019
1.00
22.66


ATOM
1653
CA
PRO
273
40.476
41.364
19.961
1.00
22.92


ATOM
1654
CB
PRO
273
41.237
42.531
19.336
1.00
23.77


ATOM
1655
CG
PRO
273
40.304
43.685
19.570
1.00
21.85


ATOM
1656
C
PRO
273
41.398
40.223
20.381
1.00
22.91


ATOM
1657
O
PRO
273
41.432
39.162
19.745
1.00
23.26


ATOM
1658
N
LEU
274
42.142
40.442
21.457
1.00
22.09


ATOM
1659
CA
LEU
274
43.062
39.433
21.951
1.00
19.44


ATOM
1660
CB
LEU
274
43.971
40.044
23.017
1.00
21.98


ATOM
1661
CG
LEU
274
45.175
39.249
23.520
1.00
26.32


ATOM
1662
CD1
LEU
274
45.869
38.537
22.366
1.00
25.68


ATOM
1663
CD2
LEU
274
46.138
40.216
24.215
1.00
26.73


ATOM
1664
C
LEU
274
42.294
38.234
22.511
1.00
18.52


ATOM
1665
O
LEU
274
42.607
37.087
22.186
1.00
16.12


ATOM
1666
N
TYR
275
41.286
38.487
23.345
1.00
15.05


ATOM
1667
CA
TYR
275
40.520
37.376
23.897
1.00
16.26


ATOM
1668
CB
TYR
275
39.462
37.844
24.898
1.00
14.51


ATOM
1669
CG
TYR
275
38.655
36.674
25.425
1.00
15.81


ATOM
1670
CD1
TYR
275
39.259
35.687
26.205
1.00
14.55


ATOM
1671
CE1
TYR
275
38.550
34.567
26.627
1.00
15.08


ATOM
1672
CD2
TYR
275
37.313
36.512
25.082
1.00
15.17


ATOM
1673
CE2
TYR
275
36.592
35.394
25.499
1.00
14.87


ATOM
1674
CZ
TYR
275
37.217
34.427
26.271
1.00
13.90


ATOM
1675
OH
TYR
275
36.513
33.326
26.697
1.00
13.75


ATOM
1676
C
TYR
275
39.816
36.576
22.801
1.00
14.63


ATOM
1677
O
TYR
275
39.852
35.346
22.803
1.00
13.73


ATOM
1678
N
LEU
276
39.174
37.268
21.865
1.00
14.03


ATOM
1679
CA
LEU
276
38.458
36.567
20.799
1.00
15.37


ATOM
1680
CB
LEU
276
37.718
37.563
19.906
1.00
15.87


ATOM
1681
CG
LEU
276
36.570
38.318
20.588
1.00
18.77


ATOM
1682
CD1
LEU
276
35.991
39.340
19.620
1.00
17.96


ATOM
1683
CD2
LEU
276
35.494
37.336
21.039
1.00
19.76


ATOM
1684
C
LEU
276
39.381
35.691
19.960
1.00
15.77


ATOM
1685
O
LEU
276
38.986
34.612
19.513
1.00
15.97


ATOM
1686
N
ASN
277
40.609
36.151
19.740
1.00
13.92


ATOM
1687
CA
ASN
277
41.558
35.367
18.965
1.00
14.44


ATOM
1688
CB
ASN
277
42.734
36.239
18.528
1.00
14.75


ATOM
1689
CG
ASN
277
42.463
36.954
17.219
1.00
17.20


ATOM
1690
OD1
ASN
277
42.442
36.330
16.157
1.00
16.39


ATOM
1691
ND2
ASN
277
42.239
38.266
17.288
1.00
16.71


ATOM
1692
C
ASN
277
42.044
34.158
19.760
1.00
14.54


ATOM
1693
O
ASN
277
42.272
33.090
19.199
1.00
12.53


ATOM
1694
N
LEU
278
42.192
34.319
21.071
1.00
12.24


ATOM
1695
CA
LEU
278
42.635
33.204
21.900
1.00
13.24


ATOM
1696
CB
LEU
278
42.986
33.691
23.311
1.00
12.96


ATOM
1697
CG
LEU
278
43.378
32.597
24.310
1.00
12.38


ATOM
1698
CD1
LEU
278
44.717
31.969
23.898
1.00
12.63


ATOM
1699
CD2
LEU
278
43.484
33.201
25.713
1.00
14.10


ATOM
1700
C
LEU
278
41.507
32.173
21.972
1.00
12.49


ATOM
1701
O
LEU
278
41.747
30.969
21.906
1.00
10.75


ATOM
1702
N
HIS
279
40.280
32.669
22.111
1.00
12.22


ATOM
1703
CA
HIS
279
39.080
31.837
22.190
1.00
13.07


ATOM
1704
CB
HIS
279
37.847
32.740
22.333
1.00
11.98


ATOM
1705
CG
HIS
279
36.539
32.007
22.308
1.00
12.16


ATOM
1706
CD2
HIS
279
35.775
31.586
21.273
1.00
9.43


ATOM
1707
ND1
HIS
279
35.844
31.678
23.454
1.00
14.66


ATOM
1708
CE1
HIS
279
34.707
31.091
23.126
1.00
10.50


ATOM
1709
NE2
HIS
279
34.641
31.022
21.808
1.00
16.46


ATOM
1710
C
HIS
279
38.946
30.972
20.936
1.00
13.49


ATOM
1711
O
HIS
279
38.766
29.759
21.026
1.00
14.71


ATOM
1712
N
ALA
280
39.037
31.603
19.769
1.00
11.17


ATOM
1713
CA
ALA
280
38.918
30.891
18.501
1.00
12.70


ATOM
1714
CB
ALA
280
38.966
31.887
17.342
1.00
11.01


ATOM
1715
C
ALA
280
40.010
29.828
18.328
1.00
13.11


ATOM
1716
O
ALA
280
39.752
28.728
17.828
1.00
14.49


ATOM
1717
N
TYR
281
41.231
30.161
18.734
1.00
14.23


ATOM
1718
CA
TYR
281
42.349
29.230
18.624
1.00
14.13


ATOM
1719
CB
TYR
281
43.658
29.942
18.979
1.00
13.18


ATOM
1720
CG
TYR
281
44.863
29.030
19.022
1.00
15.59


ATOM
1721
CD1
TYR
281
45.465
28.571
17.849
1.00
16.24


ATOM
1722
CE1
TYR
281
46.565
27.709
17.889
1.00
16.63


ATOM
1723
CD2
TYR
281
45.390
28.609
20.239
1.00
14.46


ATOM
1724
CE2
TYR
281
46.482
27.753
20.291
1.00
19.39


ATOM
1725
CZ
TYR
281
47.065
27.305
19.114
1.00
18.64


ATOM
1726
OH
TYR
281
48.143
26.448
19.182
1.00
19.16


ATOM
1727
C
TYR
281
42.142
28.025
19.544
1.00
14.20


ATOM
1728
O
TYR
281
42.339
26.876
19.140
1.00
12.95


ATOM
1729
N
VAL
282
41.747
28.291
20.785
1.00
13.42


ATOM
1730
CA
VAL
282
41.514
27.217
21.744
1.00
13.04


ATOM
1731
CB
VAL
282
41.263
27.790
23.156
1.00
12.69


ATOM
1732
CG1
VAL
282
40.806
26.681
24.113
1.00
10.82


ATOM
1733
CG2
VAL
282
42.544
28.439
23.674
1.00
11.44


ATOM
1734
C
VAL
282
40.328
26.351
21.309
1.00
13.40


ATOM
1735
O
VAL
282
40.356
25.129
21.451
1.00
12.76


ATOM
1736
N
ARG
283
39.294
26.989
20.770
1.00
12.27


ATOM
1737
CA
ARG
283
38.112
26.276
20.301
1.00
12.41


ATOM
1738
CB
ARG
283
37.073
27.280
19.788
1.00
10.58


ATOM
1739
CG
ARG
283
35.801
26.655
19.227
1.00
10.97


ATOM
1740
CD
ARG
283
34.793
27.732
18.829
1.00
11.14


ATOM
1741
NE
ARG
283
35.374
28.708
17.911
1.00
12.22


ATOM
1742
CZ
ARG
283
34.815
29.873
17.593
1.00
14.58


ATOM
1743
NH1
ARG
283
33.647
30.225
18.119
1.00
12.82


ATOM
1744
NH2
ARG
283
35.431
30.691
16.744
1.00
13.94


ATOM
1745
C
ARG
283
38.497
25.290
19.189
1.00
15.02


ATOM
1746
O
ARG
283
37.973
24.174
19.121
1.00
14.50


ATOM
1747
N
ARG
284
39.415
25.705
18.320
1.00
15.37


ATOM
1748
CA
ARG
284
39.865
24.842
17.231
1.00
16.53


ATOM
1749
CB
ARG
284
40.791
25.619
16.289
1.00
15.14


ATOM
1750
CG
ARG
284
41.532
24.771
15.262
1.00
17.18


ATOM
1751
CD
ARG
284
40.608
24.186
14.201
1.00
17.98


ATOM
1752
NE
ARG
284
39.899
25.226
13.458
1.00
17.50


ATOM
1753
CZ
ARG
284
39.121
24.987
12.406
1.00
20.20


ATOM
1754
NH1
ARG
284
38.505
25.989
11.789
1.00
17.52


ATOM
1755
NH2
ARG
284
38.967
23.742
11.963
1.00
18.66


ATOM
1756
C
ARG
284
40.592
23.615
17.793
1.00
17.62


ATOM
1757
O
ARG
284
40.369
22.490
17.340
1.00
16.82


ATOM
1758
N
ALA
285
41.456
23.838
18.782
1.00
16.05


ATOM
1759
CA
ALA
285
42.213
22.751
19.400
1.00
16.40


ATOM
1760
CB
ALA
285
43.247
23.312
20.369
1.00
15.81


ATOM
1761
C
ALA
285
41.288
21.770
20.122
1.00
17.14


ATOM
1762
O
ALA
285
41.527
20.560
20.111
1.00
15.20


ATOM
1763
N
LEU
286
40.237
22.289
20.748
1.00
14.27


ATOM
1764
CA
LEU
286
39.285
21.428
21.449
1.00
16.86


ATOM
1765
CB
LEU
286
38.331
22.266
22.301
1.00
15.32


ATOM
1766
CG
LEU
286
38.945
22.925
23.542
1.00
17.90


ATOM
1767
CD1
LEU
286
37.887
23.785
24.230
1.00
15.75


ATOM
1768
CD2
LEU
286
39.470
21.850
24.505
1.00
13.91


ATOM
1769
C
LEU
286
38.502
20.615
20.422
1.00
17.67


ATOM
1770
O
LEU
286
38.172
19.452
20.651
1.00
17.19


ATOM
1771
N
HIS
287
38.212
21.245
19.286
1.00
16.68


ATOM
1772
CA
HIS
287
37.494
20.601
18.196
1.00
18.26


ATOM
1773
CB
HIS
287
37.292
21.621
17.062
1.00
18.41


ATOM
1774
CG
HIS
287
36.648
21.061
15.831
1.00
18.72


ATOM
1775
CD2
HIS
287
35.373
21.137
15.380
1.00
17.00


ATOM
1776
ND1
HIS
287
37.351
20.359
14.875
1.00
18.34


ATOM
1777
CE1
HIS
287
36.537
20.031
13.887
1.00
14.90


ATOM
1778
NE2
HIS
287
35.332
20.492
14.169
1.00
16.90


ATOM
1779
C
HIS
287
38.361
19.421
17.740
1.00
19.03


ATOM
1780
O
HIS
287
37.866
18.327
17.471
1.00
17.36


ATOM
1781
N
ARG
288
39.666
19.659
17.700
1.00
18.55


ATOM
1782
CA
ARG
288
40.649
18.662
17.295
1.00
20.61


ATOM
1783
CB
ARG
288
42.028
19.320
17.254
1.00
23.74


ATOM
1784
CG
ARG
288
42.870
19.014
16.032
1.00
30.47


ATOM
1785
CD
ARG
288
43.922
20.102
15.857
1.00
33.76


ATOM
1786
NE
ARG
288
44.686
20.306
17.083
1.00
33.81


ATOM
1787
CZ
ARG
288
45.113
21.487
17.514
1.00
35.70


ATOM
1788
NH1
ARG
288
44.852
22.587
16.817
1.00
35.23


ATOM
1789
NH2
ARG
288
45.800
21.569
18.646
1.00
36.87


ATOM
1790
C
ARG
288
40.679
17.468
18.253
1.00
20.35


ATOM
1791
O
ARG
288
40.773
16.314
17.825
1.00
19.01


ATOM
1792
N
HIS
289
40.586
17.747
19.550
1.00
19.12


ATOM
1793
CA
HIS
289
40.641
16.692
20.559
1.00
20.16


ATOM
1794
CB
HIS
289
41.247
17.230
21.858
1.00
21.21


ATOM
1795
CG
HIS
289
41.407
16.184
22.916
1.00
23.81


ATOM
1796
CD2
HIS
289
40.632
15.866
23.980
1.00
24.22


ATOM
1797
ND1
HIS
289
42.440
15.270
22.909
1.00
26.00


ATOM
1798
CE1
HIS
289
42.292
14.433
23.921
1.00
24.08


ATOM
1799
NE2
HIS
289
41.202
14.772
24.585
1.00
27.58


ATOM
1800
C
HIS
289
39.327
15.997
20.903
1.00
20.43


ATOM
1801
O
HIS
289
39.276
14.768
20.978
1.00
20.43


ATOM
1802
N
TYR
290
38.270
16.772
21.123
1.00
19.15


ATOM
1803
CA
TYR
290
36.990
16.194
21.503
1.00
18.20


ATOM
1804
CB
TYR
290
36.298
17.098
22.527
1.00
17.79


ATOM
1805
CG
TYR
290
37.025
17.158
23.859
1.00
17.11


ATOM
1806
CD1
TYR
290
37.840
18.242
24.188
1.00
14.34


ATOM
1807
CE1
TYR
290
38.538
18.284
25.403
1.00
15.63


ATOM
1808
CD2
TYR
290
36.922
16.111
24.778
1.00
17.43


ATOM
1809
CE2
TYR
290
37.616
16.140
25.990
1.00
16.23


ATOM
1810
CZ
TYR
290
38.421
17.227
26.296
1.00
17.84


ATOM
1811
OH
TYR
290
39.117
17.242
27.485
1.00
16.73


ATOM
1812
C
TYR
290
36.026
15.842
20.375
1.00
19.53


ATOM
1813
O
TYR
290
34.985
15.235
20.624
1.00
19.64


ATOM
1814
N
GLY
291
36.359
16.224
19.145
1.00
19.76


ATOM
1815
CA
GLY
291
35.503
15.890
18.017
1.00
19.38


ATOM
1816
C
GLY
291
34.552
16.967
17.537
1.00
17.77


ATOM
1817
O
GLY
291
34.058
17.772
18.317
1.00
16.36


ATOM
1818
N
ALA
292
34.279
16.958
16.237
1.00
18.00


ATOM
1819
CA
ALA
292
33.392
17.939
15.620
1.00
17.85


ATOM
1820
CB
ALA
292
33.401
17.757
14.094
1.00
18.60


ATOM
1821
C
ALA
292
31.961
17.871
16.142
1.00
17.75


ATOM
1822
O
ALA
292
31.235
18.859
16.095
1.00
17.45


ATOM
1823
N
GLN
293
31.548
16.705
16.631
1.00
17.76


ATOM
1824
CA
GLN
293
30.194
16.544
17.149
1.00
17.65


ATOM
1825
CB
GLN
293
29.845
15.053
17.276
1.00
19.36


ATOM
1826
CG
GLN
293
29.784
14.287
15.947
1.00
18.52


ATOM
1827
CD
GLN
293
28.512
14.554
15.153
1.00
19.88


ATOM
1828
OE1
GLN
293
27.616
15.264
15.606
1.00
19.17


ATOM
1829
NE2
GLN
293
28.428
13.973
13.959
1.00
18.08


ATOM
1830
C
GLN
293
30.005
17.229
18.503
1.00
18.04


ATOM
1831
O
GLN
293
28.873
17.405
18.960
1.00
17.48


ATOM
1832
N
HIS
294
31.105
17.630
19.137
1.00
16.33


ATOM
1833
CA
HIS
294
31.021
18.277
20.446
1.00
17.25


ATOM
1834
CB
HIS
294
31.784
17.445
21.478
1.00
18.66


ATOM
1835
CG
HIS
294
31.345
16.014
21.532
1.00
21.25


ATOM
1836
CD2
HIS
294
31.954
14.879
21.111
1.00
21.69


ATOM
1837
ND1
HIS
294
30.114
15.631
22.021
1.00
22.71


ATOM
1838
CE1
HIS
294
29.982
14.322
21.894
1.00
23.73


ATOM
1839
NE2
HIS
294
31.084
13.842
21.344
1.00
24.62


ATOM
1840
C
HIS
294
31.519
19.720
20.480
1.00
18.08


ATOM
1841
O
HIS
294
31.356
20.409
21.488
1.00
19.39


ATOM
1842
N
ILE
295
32.122
20.180
19.387
1.00
17.59


ATOM
1843
CA
ILE
295
32.625
21.552
19.323
1.00
17.39


ATOM
1844
CB
ILE
295
34.177
21.600
19.335
1.00
18.25


ATOM
1845
CG2
ILE
295
34.650
23.050
19.161
1.00
19.44


ATOM
1846
CG1
ILE
295
34.724
20.998
20.634
1.00
19.74


ATOM
1847
CD1
ILE
295
34.452
21.827
21.889
1.00
19.50


ATOM
1848
C
ILE
295
32.150
22.259
18.060
1.00
15.69


ATOM
1849
O
ILE
295
32.467
21.836
16.948
1.00
16.28


ATOM
1850
N
ASN
296
31.381
23.328
18.234
1.00
14.98


ATOM
1851
CA
ASN
296
30.896
24.112
17.105
1.00
17.48


ATOM
1852
CB
ASN
296
29.559
24.766
17.450
1.00
18.21


ATOM
1853
CG
ASN
296
28.995
25.586
16.304
1.00
20.95


ATOM
1854
OD1
ASN
296
29.639
25.764
15.271
1.00
18.66


ATOM
1855
ND2
ASN
296
27.786
26.096
16.487
1.00
24.30


ATOM
1856
C
ASN
296
31.946
25.194
16.840
1.00
17.45


ATOM
1857
O
ASN
296
32.135
26.091
17.662
1.00
17.17


ATOM
1858
N
LEU
297
32.621
25.105
15.697
1.00
15.65


ATOM
1859
CA
LEU
297
33.670
26.060
15.333
1.00
17.18


ATOM
1860
CB
LEU
297
34.357
25.613
14.042
1.00
15.85


ATOM
1861
CG
LEU
297
35.202
24.338
14.136
1.00
15.74


ATOM
1862
CD1
LEU
297
35.632
23.934
12.741
1.00
17.98


ATOM
1863
CD2
LEU
297
36.415
24.565
15.032
1.00
15.34


ATOM
1864
C
LEU
297
33.192
27.502
15.182
1.00
17.65


ATOM
1865
O
LEU
297
34.006
28.418
15.037
1.00
15.95


ATOM
1866
N
GLU
298
31.877
27.702
15.214
1.00
17.41


ATOM
1867
CA
GLU
298
31.311
29.041
15.101
1.00
19.65


ATOM
1868
CB
GLU
298
30.460
29.158
13.830
1.00
22.80


ATOM
1869
CG
GLU
298
31.163
28.684
12.570
1.00
27.54


ATOM
1870
CD
GLU
298
30.365
28.977
11.309
1.00
31.19


ATOM
1871
OE1
GLU
298
29.148
28.692
11.282
1.00
32.45


ATOM
1872
OE2
GLU
298
30.961
29.488
10.342
1.00
32.93


ATOM
1873
C
GLU
298
30.445
29.366
16.317
1.00
18.22


ATOM
1874
O
GLU
298
29.660
30.318
16.294
1.00
20.41


ATOM
1875
N
GLY
299
30.588
28.581
17.381
1.00
14.98


ATOM
1876
CA
GLY
299
29.785
28.818
18.567
1.00
12.99


ATOM
1877
C
GLY
299
30.562
28.885
19.867
1.00
13.29


ATOM
1878
O
GLY
299
31.793
28.909
19.858
1.00
13.77


ATOM
1879
N
PRO
300
29.864
28.918
21.014
1.00
14.38


ATOM
1880
CD
PRO
300
28.397
28.934
21.180
1.00
14.36


ATOM
1881
CA
PRO
300
30.539
28.982
22.311
1.00
15.04


ATOM
1882
CB
PRO
300
29.411
29.353
23.263
1.00
15.56


ATOM
1883
CG
PRO
300
28.232
28.651
22.661
1.00
16.94


ATOM
1884
C
PRO
300
31.217
27.660
22.676
1.00
15.92


ATOM
1885
O
PRO
300
30.914
26.614
22.100
1.00
14.68


ATOM
1886
N
ILE
301
32.131
27.724
23.639
1.00
14.52


ATOM
1887
CA
ILE
301
32.885
26.560
24.090
1.00
13.49


ATOM
1888
CB
ILE
301
34.345
26.958
24.416
1.00
14.98


ATOM
1889
CG2
ILE
301
35.104
25.763
25.013
1.00
13.64


ATOM
1890
CG1
ILE
301
35.033
27.492
23.158
1.00
15.50


ATOM
1891
CD1
ILE
301
36.413
28.053
23.409
1.00
14.09


ATOM
1892
C
ILE
301
32.275
25.957
25.351
1.00
13.55


ATOM
1893
O
ILE
301
31.946
26.681
26.288
1.00
9.28


ATOM
1894
N
PRO
302
32.097
24.623
25.380
1.00
12.22


ATOM
1895
CD
PRO
302
32.236
23.667
24.271
1.00
12.83


ATOM
1896
CA
PRO
302
31.528
23.966
26.562
1.00
13.66


ATOM
1897
CB
PRO
302
31.608
22.487
26.200
1.00
12.81


ATOM
1898
CG
PRO
302
31.360
22.510
24.733
1.00
13.21


ATOM
1899
C
PRO
302
32.387
24.325
27.777
1.00
12.95


ATOM
1900
O
PRO
302
33.606
24.133
27.772
1.00
10.63


ATOM
1901
N
ALA
303
31.731
24.835
28.814
1.00
13.88


ATOM
1902
CA
ALA
303
32.386
25.304
30.033
1.00
13.20


ATOM
1903
CB
ALA
303
31.348
25.984
30.917
1.00
12.25


ATOM
1904
C
ALA
303
33.197
24.326
30.876
1.00
14.39


ATOM
1905
O
ALA
303
33.897
24.752
31.798
1.00
14.70


ATOM
1906
N
HIS
304
33.125
23.032
30.583
1.00
13.10


ATOM
1907
CA
HIS
304
33.861
22.065
31.391
1.00
15.86


ATOM
1908
CB
HIS
304
32.972
20.847
31.673
1.00
14.23


ATOM
1909
CG
HIS
304
32.622
20.057
30.448
1.00
16.26


ATOM
1910
CD2
HIS
304
32.663
18.725
30.202
1.00
14.69


ATOM
1911
ND1
HIS
304
32.138
20.644
29.297
1.00
16.27


ATOM
1912
CE1
HIS
304
31.896
19.708
28.396
1.00
16.80


ATOM
1913
NE2
HIS
304
32.205
18.534
28.920
1.00
16.57


ATOM
1914
C
HIS
304
35.175
21.596
30.772
1.00
15.34


ATOM
1915
O
HIS
304
35.876
20.776
31.362
1.00
13.95


ATOM
1916
N
LEU
305
35.519
22.136
29.605
1.00
14.97


ATOM
1917
CA
LEU
305
36.725
21.716
28.891
1.00
14.04


ATOM
1918
CB
LEU
305
36.383
21.531
27.405
1.00
12.83


ATOM
1919
CG
LEU
305
35.144
20.690
27.076
1.00
12.75


ATOM
1920
CD1
LEU
305
34.877
20.727
25.564
1.00
9.86


ATOM
1921
CD2
LEU
305
35.367
19.260
27.559
1.00
10.56


ATOM
1922
C
LEU
305
37.947
22.624
28.991
1.00
15.10


ATOM
1923
O
LEU
305
38.921
22.424
28.262
1.00
16.46


ATOM
1924
N
LEU
306
37.925
23.602
29.889
1.00
14.31


ATOM
1925
CA
LEU
306
39.047
24.527
29.972
1.00
15.42


ATOM
1926
CB
LEU
306
38.524
25.972
30.053
1.00
13.51


ATOM
1927
CG
LEU
306
37.764
26.550
28.848
1.00
14.73


ATOM
1928
CD1
LEU
306
38.592
26.362
27.577
1.00
14.30


ATOM
1929
CD2
LEU
306
36.410
25.870
28.694
1.00
15.38


ATOM
1930
C
LEU
306
40.080
24.275
31.070
1.00
15.84


ATOM
1931
O
LEU
306
40.937
25.124
31.313
1.00
15.82


ATOM
1932
N
GLY
307
39.997
23.120
31.728
1.00
16.01


ATOM
1933
CA
GLY
307
40.967
22.766
32.758
1.00
15.85


ATOM
1934
C
GLY
307
40.780
23.392
34.126
1.00
16.19


ATOM
1935
O
GLY
307
41.595
23.195
35.035
1.00
14.81


ATOM
1936
N
ASN
308
39.692
24.137
34.275
1.00
15.62


ATOM
1937
CA
ASN
308
39.381
24.815
35.522
1.00
15.37


ATOM
1938
CB
ASN
308
39.878
26.265
35.430
1.00
14.32


ATOM
1939
CG
ASN
308
39.391
27.132
36.570
1.00
15.28


ATOM
1940
OD1
ASN
308
38.277
27.654
36.530
1.00
15.45


ATOM
1941
ND2
ASN
308
40.226
27.292
37.598
1.00
13.64


ATOM
1942
C
ASN
308
37.869
24.734
35.769
1.00
14.00


ATOM
1943
O
ASN
308
37.072
24.858
34.842
1.00
12.08


ATOM
1944
N
MET
309
37.486
24.519
37.023
1.00
13.86


ATOM
1945
CA
MET
309
36.077
24.368
37.390
1.00
14.00


ATOM
1946
CB
MET
309
35.951
24.234
38.916
1.00
14.12


ATOM
1947
CG
MET
309
34.527
24.008
39.414
1.00
15.15


ATOM
1948
SD
MET
309
33.787
22.492
38.767
1.00
16.63


ATOM
1949
CE
MET
309
34.428
21.288
39.947
1.00
16.22


ATOM
1950
C
MET
309
35.155
25.478
36.884
1.00
14.78


ATOM
1951
O
MET
309
33.996
25.220
36.548
1.00
13.18


ATOM
1952
N
TRP
310
35.671
26.703
36.812
1.00
11.51


ATOM
1953
CA
TRP
310
34.872
27.843
36.366
1.00
14.25


ATOM
1954
CB
TRP
310
34.970
28.968
37.403
1.00
12.20


ATOM
1955
CG
TRP
310
34.625
28.480
38.772
1.00
12.52


ATOM
1956
CD2
TRP
310
35.538
27.959
39.745
1.00
12.82


ATOM
1957
CE2
TRP
310
34.764
27.461
40.817
1.00
13.24


ATOM
1958
CE3
TRP
310
36.937
27.855
39.810
1.00
13.78


ATOM
1959
CD1
TRP
310
33.373
28.295
39.283
1.00
11.84


ATOM
1960
NE1
TRP
310
33.447
27.681
40.509
1.00
12.66


ATOM
1961
CZ2
TRP
310
35.340
26.866
41.948
1.00
12.55


ATOM
1962
CZ3
TRP
310
37.513
27.260
40.934
1.00
13.31


ATOM
1963
CH2
TRP
310
36.708
26.773
41.990
1.00
12.52


ATOM
1964
C
TRP
310
35.309
28.360
35.001
1.00
13.97


ATOM
1965
O
TRP
310
34.772
29.348
34.508
1.00
12.98


ATOM
1966
N
ALA
311
36.269
27.670
34.388
1.00
14.15


ATOM
1967
CA
ALA
311
36.799
28.086
33.096
1.00
13.77


ATOM
1968
CB
ALA
311
35.719
27.964
32.021
1.00
14.05


ATOM
1969
C
ALA
311
37.297
29.534
33.179
1.00
13.58


ATOM
1970
O
ALA
311
37.249
30.263
32.189
1.00
13.90


ATOM
1971
N
GLN
312
37.761
29.952
34.358
1.00
13.19


ATOM
1972
CA
GLN
312
38.247
31.325
34.541
1.00
13.69


ATOM
1973
CB
GLN
312
38.088
31.770
36.000
1.00
12.28


ATOM
1974
CG
GLN
312
38.917
30.995
36.999
1.00
14.52


ATOM
1975
CD
GLN
312
38.542
31.318
38.433
1.00
17.57


ATOM
1976
OE1
GLN
312
37.382
31.187
38.828
1.00
15.61


ATOM
1977
NE2
GLN
312
39.522
31.739
39.220
1.00
19.96


ATOM
1978
C
GLN
312
39.700
31.485
34.102
1.00
13.47


ATOM
1979
O
GLN
312
40.137
32.587
33.771
1.00
11.19


ATOM
1980
N
THR
313
40.442
30.382
34.124
1.00
12.33


ATOM
1981
CA
THR
313
41.835
30.354
33.687
1.00
13.83


ATOM
1982
CB
THR
313
42.826
30.403
34.875
1.00
16.20


ATOM
1983
OG1
THR
313
42.468
29.425
35.858
1.00
16.40


ATOM
1984
CG2
THR
313
42.819
31.789
35.511
1.00
17.20


ATOM
1985
C
THR
313
41.964
29.040
32.918
1.00
16.52


ATOM
1986
O
THR
313
41.415
28.021
33.335
1.00
14.73


ATOM
1987
N
TRP
314
42.675
29.065
31.795
1.00
14.06


ATOM
1988
CA
TRP
314
42.788
27.881
30.948
1.00
15.86


ATOM
1989
CB
TRP
314
42.318
28.216
29.529
1.00
15.32


ATOM
1990
CG
TRP
314
40.991
28.934
29.408
1.00
13.99


ATOM
1991
CD2
TRP
314
40.457
29.529
28.219
1.00
13.70


ATOM
1992
CE2
TRP
314
39.164
30.012
28.534
1.00
14.95


ATOM
1993
CE3
TRP
314
40.943
29.698
26.915
1.00
12.93


ATOM
1994
CD1
TRP
314
40.032
29.079
30.372
1.00
14.30


ATOM
1995
NE1
TRP
314
38.929
29.725
29.854
1.00
13.72


ATOM
1996
CZ2
TRP
314
38.355
30.650
27.592
1.00
13.70


ATOM
1997
CZ3
TRP
314
40.137
30.332
25.979
1.00
16.03


ATOM
1998
CH2
TRP
314
38.853
30.800
26.325
1.00
16.16


ATOM
1999
C
TRP
314
44.171
27.255
30.816
1.00
17.18


ATOM
2000
O
TRP
314
44.363
26.402
29.950
1.00
16.26


ATOM
2001
N
SER
315
45.125
27.655
31.648
1.00
16.81


ATOM
2002
CA
SER
315
46.482
27.131
31.514
1.00
18.73


ATOM
2003
CB
SER
315
47.429
27.840
32.493
1.00
19.48


ATOM
2004
OG
SER
315
47.078
27.573
33.834
1.00
23.23


ATOM
2005
C
SER
315
46.628
25.618
31.658
1.00
17.43


ATOM
2006
O
SER
315
47.599
25.043
31.165
1.00
16.20


ATOM
2007
N
ASN
316
45.669
24.967
32.309
1.00
16.52


ATOM
2008
CA
ASN
316
45.758
23.526
32.487
1.00
16.72


ATOM
2009
CB
ASN
316
44.827
23.068
33.617
1.00
16.47


ATOM
2010
CG
ASN
316
45.342
23.494
34.991
1.00
18.32


ATOM
2011
OD1
ASN
316
46.504
23.262
35.323
1.00
19.09


ATOM
2012
ND2
ASN
316
44.484
24.116
35.788
1.00
15.86


ATOM
2013
C
ASN
316
45.540
22.700
31.219
1.00
17.50


ATOM
2014
O
ASN
316
45.834
21.508
31.210
1.00
17.87


ATOM
2015
N
ILE
317
45.028
23.311
30.150
1.00
17.39


ATOM
2016
CA
ILE
317
44.869
22.568
28.901
1.00
17.13


ATOM
2017
CB
ILE
317
43.479
22.759
28.246
1.00
16.82


ATOM
2018
CG2
ILE
317
42.394
22.220
29.170
1.00
16.53


ATOM
2019
CG1
ILE
317
43.242
24.230
27.902
1.00
17.65


ATOM
2020
CD1
ILE
317
42.036
24.444
27.019
1.00
18.86


ATOM
2021
C
ILE
317
45.947
23.014
27.915
1.00
18.07


ATOM
2022
O
ILE
317
45.793
22.892
26.697
1.00
16.69


ATOM
2023
N
TYR
318
47.047
23.536
28.454
1.00
18.93


ATOM
2024
CA
TYR
318
48.155
23.983
27.618
1.00
20.39


ATOM
2025
CB
TYR
318
49.337
24.421
28.479
1.00
21.07


ATOM
2026
CG
TYP
318
50.567
24.757
27.667
1.00
23.88


ATOM
2027
CD1
TYR
318
50.635
25.931
26.917
1.00
22.79


ATOM
2028
CE1
TYR
318
51.749
26.225
26.138
1.00
25.90


ATOM
2029
CD2
TYR
318
51.652
23.879
27.618
1.00
25.81


ATOM
2030
CE2
TYR
318
52.774
24.163
26.841
1.00
26.76


ATOM
2031
CZ
TYR
318
52.815
25.335
26.105
1.00
27.14


ATOM
2032
OH
TYR
318
53.919
25.616
25.338
1.00
27.90


ATOM
2033
C
TYR
318
48.609
22.861
26.682
1.00
20.54


ATOM
2034
O
TYR
318
48.933
23.108
25.525
1.00
19.56


ATOM
2035
N
ASP
319
48.624
21.634
27.194
1.00
21.68


ATOM
2036
CA
ASP
319
49.041
20.468
26.415
1.00
24.93


ATOM
2037
CB
ASP
319
48.942
19.205
27.273
1.00
27.75


ATOM
2038
CG
ASP
319
47.532
18.947
27.770
1.00
33.89


ATOM
2039
OD1
ASP
319
46.943
19.866
28.377
1.00
37.33


ATOM
2040
OD2
ASP
319
47.009
17.829
27.560
1.00
36.71


ATOM
2041
C
ASP
319
48.214
20.275
25.144
1.00
24.42


ATOM
2042
O
ASP
319
48.721
19.790
24.133
1.00
24.30


ATOM
2043
N
LEU
320
46.940
20.648
25.200
1.00
22.05


ATOM
2044
CA
LEU
320
46.057
20.502
24.048
1.00
21.65


ATOM
2045
CB
LEU
320
44.594
20.431
24.503
1.00
21.37


ATOM
2046
CG
LEU
320
44.138
19.298
25.429
1.00
20.50


ATOM
2047
CD1
LEU
320
42.647
19.458
25.712
1.00
20.57


ATOM
2048
CD2
LEU
320
44.414
17.946
24.780
1.00
20.05


ATOM
2049
C
LEU
320
46.190
21.626
23.023
1.00
20.30


ATOM
2050
O
LEU
320
45.750
21.476
21.884
1.00
20.89


ATOM
2051
N
VAL
321
46.803
22.743
23.411
1.00
18.20


ATOM
2052
CA
VAL
321
46.911
23.878
22.497
1.00
17.14


ATOM
2053
CB
VAL
321
46.014
25.051
22.986
1.00
15.95


ATOM
2054
CG1
VAL
321
44.637
24.529
23.358
1.00
16.89


ATOM
2055
CG2
VAL
321
46.648
25.737
24.182
1.00
13.25


ATOM
2056
C
VAL
321
48.319
24.420
22.267
1.00
18.07


ATOM
2057
O
VAL
321
48.477
25.496
21.697
1.00
19.68


ATOM
2058
N
VAL
322
49.342
23.689
22.699
1.00
20.47


ATOM
2059
CA
VAL
322
50.715
24.154
22.516
1.00
23.25


ATOM
2060
CB
VAL
322
51.735
23.050
22.893
1.00
25.43


ATOM
2061
CG1
VAL
322
51.487
21.801
22.069
1.00
27.69


ATOM
2062
CG2
VAL
322
53.156
23.561
22.680
1.00
27.11


ATOM
2063
C
VAL
322
50.975
24.620
21.077
1.00
22.80


ATOM
2064
O
VAL
322
50.758
23.875
20.123
1.00
23.34


ATOM
2065
N
PRO
323
51.432
25.874
20.904
1.00
23.14


ATOM
2066
CD
PRO
323
51.589
26.917
21.934
1.00
21.86


ATOM
2067
CA
PRO
323
51.712
26.414
19.566
1.00
24.47


ATOM
2068
CB
PRO
323
52.152
27.848
19.855
1.00
23.04


ATOM
2069
CG
PRO
323
51.422
28.181
21.134
1.00
22.71


ATOM
2070
C
PRO
323
52.790
25.620
18.821
1.00
26.42


ATOM
2071
O
PRO
323
52.615
25.255
17.658
1.00
26.23


ATOM
2072
N
PHE
324
53.905
25.359
19.494
1.00
27.57


ATOM
2073
CA
PHE
324
54.996
24.606
18.885
1.00
28.92


ATOM
2074
CB
PHE
324
56.232
25.494
18.707
1.00
29.24


ATOM
2075
CG
PHE
324
56.003
26.667
17.801
1.00
28.40


ATOM
2076
CD1
PHE
324
55.591
27.890
18.314
1.00
28.05


ATOM
2077
CD2
PHE
324
56.159
26.538
16.426
1.00
30.34


ATOM
2078
CE1
PHE
324
55.333
28.964
17.473
1.00
28.58


ATOM
2079
CE2
PHE
324
55.903
27.605
15.575
1.00
28.99


ATOM
2080
CZ
PHE
324
55.490
28.823
16.099
1.00
29.77


ATOM
2081
C
PHE
324
55.339
23.400
19.738
1.00
29.62


ATOM
2082
O
PHE
324
56.221
23.460
20.596
1.00
27.80


ATOM
2083
N
PRO
325
54.633
22.280
19.514
1.00
31.43


ATOM
2084
CD
PRO
325
53.589
22.095
18.491
1.00
32.36


ATOM
2085
CA
PRO
325
54.855
21.042
20.263
1.00
34.46


ATOM
2086
CB
PRO
325
53.756
20.118
19.737
1.00
33.87


ATOM
2087
CG
PRO
325
53.560
20.595
18.336
1.00
33.40


ATOM
2088
C
PRO
325
56.257
20.463
20.083
1.00
36.18


ATOM
2089
O
PRO
325
56.677
19.593
20.849
1.00
37.18


ATOM
2090
N
SER
326
56.980
20.947
19.077
1.00
37.49


ATOM
2091
CA
SER
326
58.337
20.473
18.832
1.00
41.11


ATOM
2092
CB
SER
326
58.858
20.989
17.490
1.00
42.68


ATOM
2093
OG
SER
326
58.218
20.326
16.416
1.00
46.06


ATOM
2094
C
SER
326
59.259
20.936
19.949
1.00
41.74


ATOM
2095
O
SER
326
60.210
20.246
20.300
1.00
42.06


ATOM
2096
N
ALA
327
58.974
22.113
20.498
1.00
42.81


ATOM
2097
CA
ALA
327
59.767
22.663
21.591
1.00
44.30


ATOM
2098
CB
ALA
327
59.778
24.183
21.516
1.00
44.00


ATOM
2099
C
ALA
327
59.138
22.200
22.903
1.00
45.75


ATOM
2100
O
ALA
327
58.246
22.857
23.440
1.00
45.98


ATOM
2101
N
PRO
328
59.601
21.059
23.439
1.00
46.83


ATOM
2102
CD
PRO
328
60.768
20.265
23.013
1.00
47.01


ATOM
2103
CA
PRO
328
59.051
20.539
24.692
1.00
48.00


ATOM
2104
CB
PRO
328
59.746
19.189
24.834
1.00
48.21


ATOM
2105
CG
PRO
328
61.100
19.469
24.262
1.00
48.04


ATOM
2106
C
PRO
328
59.297
21.448
25.890
1.00
48.18


ATOM
2107
O
PRO
328
60.282
22.187
25.940
1.00
46.83


ATOM
2108
N
ALA
329
58.381
21.388
26.849
1.00
49.04


ATOM
2109
CA
ALA
329
58.484
22.185
28.063
1.00
50.15


ATOM
2110
CB
ALA
329
57.284
23.123
28.183
1.00
50.22


ATOM
2111
C
ALA
329
58.521
21.222
29.240
1.00
49.64


ATOM
2112
O
ALA
329
57.741
20.270
29.293
1.00
49.91


ATOM
2113
N
MET
330
59.432
21.462
30.177
1.00
49.53


ATOM
2114
CA
MET
330
59.547
20.599
31.340
1.00
49.53


ATOM
2115
CB
MET
330
60.673
21.070
32.257
1.00
51.15


ATOM
2116
CG
MET
330
62.029
20.527
31.884
1.00
53.03


ATOM
2117
SD
MET
330
63.171
20.647
33.253
1.00
57.37


ATOM
2118
CE
MET
330
62.679
19.231
34.226
1.00
55.84


ATOM
2119
C
MET
330
58.262
20.525
32.144
1.00
48.79


ATOM
2120
O
MET
330
57.481
21.475
32.183
1.00
49.29


ATOM
2121
N
ASP
331
58.048
19.381
32.781
1.00
47.29


ATOM
2122
CA
ASP
331
56.874
19.182
33.615
1.00
45.73


ATOM
2123
CB
ASP
331
56.656
17.689
33.862
1.00
47.61


ATOM
2124
CG
ASP
331
55.342
17.400
34.557
1.00
48.84


ATOM
2125
OD1
ASP
331
54.962
18.178
35.459
1.00
49.28


ATOM
2126
OD2
ASP
331
54.698
16.388
34.211
1.00
49.53


ATOM
2127
C
ASP
331
57.190
19.889
34.932
1.00
43.86


ATOM
2128
O
ASP
331
57.723
19.279
35.860
1.00
42.31


ATOM
2129
N
THR
332
56.872
21.178
34.999
1.00
41.74


ATOM
2130
CA
THR
332
57.140
21.978
36.191
1.00
40.58


ATOM
2131
CB
THR
332
56.484
23.371
36.090
1.00
41.27


ATOM
2132
OG1
THR
332
56.908
24.016
34.881
1.00
42.14


ATOM
2133
CG2
THR
332
56.896
24.236
37.275
1.00
42.66


ATOM
2134
C
THR
332
56.669
21.307
37.476
1.00
39.17


ATOM
2135
O
THR
332
57.411
21.245
38.457
1.00
37.70


ATOM
2136
N
THR
333
55.437
20.807
37.472
1.00
37.74


ATOM
2137
CA
THR
333
54.890
20.144
38.648
1.00
36.86


ATOM
2138
CB
THR
333
53.427
19.719
38.418
1.00
37.40


ATOM
2139
OG1
THR
333
52.628
20.882
38.169
1.00
36.62


ATOM
2140
CG2
THR
333
52.886
18.984
39.635
1.00
37.24


ATOM
2141
C
THR
333
55.722
18.914
38.981
1.00
36.88


ATOM
2142
O
THR
333
56.088
18.692
40.137
1.00
36.19


ATOM
2143
N
ALA
334
56.023
18.116
37.960
1.00
36.39


ATOM
2144
CA
ALA
334
56.826
16.917
38.153
1.00
35.82


ATOM
2145
CB
ALA
334
57.017
16.187
36.828
1.00
36.09


ATOM
2146
C
ALA
334
58.176
17.327
38.725
1.00
35.55


ATOM
2147
O
ALA
334
58.707
16.666
39.618
1.00
36.24


ATOM
2148
N
ALA
335
58.723
18.424
38.209
1.00
34.21


ATOM
2149
CA
ALA
335
60.009
18.923
38.675
1.00
33.61


ATOM
2150
CB
ALA
335
60.436
20.128
37.846
1.00
33.15


ATOM
2151
C
ALA
335
59.901
19.304
40.146
1.00
33.27


ATOM
2152
O
ALA
335
60.704
18.866
40.965
1.00
31.41


ATOM
2153
N
MET
336
58.894
20.107
40.482
1.00
34.57


ATOM
2154
CA
MET
336
58.688
20.531
41.866
1.00
34.78


ATOM
2155
CB
MET
336
57.427
21.394
41.975
1.00
32.50


ATOM
2156
CG
MET
336
57.541
22.735
41.264
1.00
29.70


ATOM
2157
SD
MET
336
56.074
23.759
41.452
1.00
28.38


ATOM
2158
CE
MET
336
56.194
24.182
43.188
1.00
22.94


ATOM
2159
C
MET
336
58.578
19.323
42.795
1.00
35.93


ATOM
2160
O
MET
336
59.274
19.241
43.810
1.00
35.89


ATOM
2161
N
LEU
337
57.706
18.384
42.440
1.00
37.76


ATOM
2162
CA
LEU
337
57.524
17.178
43.239
1.00
40.14


ATOM
2163
CB
LEU
337
56.380
16.334
42.666
1.00
40.76


ATOM
2164
CG
LEU
337
54.971
16.932
42.725
1.00
41.59


ATOM
2165
CD1
LEU
337
54.024
16.102
41.871
1.00
41.83


ATOM
2166
CD2
LEU
337
54.491
16.982
44.171
1.00
41.58


ATOM
2167
C
LEU
337
58.817
16.365
43.241
1.00
41.26


ATOM
2168
O
LEU
337
59.253
15.871
44.283
1.00
41.87


ATOM
2169
N
ALA
338
59.430
16.242
42.067
1.00
41.93


ATOM
2170
CA
ALA
338
60.671
15.490
41.913
1.00
42.20


ATOM
2171
CB
ALA
338
61.200
15.641
40.495
1.00
43.26


ATOM
2172
C
ALA
338
61.736
15.922
42.909
1.00
42.52


ATOM
2173
O
ALA
338
62.386
15.081
43.530
1.00
42.44


ATOM
2174
N
GLN
339
61.926
17.230
43.062
1.00
42.25


ATOM
2175
CA
GLN
339
62.928
17.713
44.001
1.00
41.65


ATOM
2176
CB
GLN
339
63.734
18.859
43.394
1.00
42.74


ATOM
2177
CG
GLN
339
63.026
19.643
42.327
1.00
44.14


ATOM
2178
CD
GLN
339
63.993
20.157
41.285
1.00
45.56


ATOM
2179
OE1
GLN
339
64.984
20.807
41.613
1.00
47.00


ATOM
2180
NE2
GLN
339
63.715
19.862
40.019
1.00
45.62


ATOM
2181
C
GLN
339
62.357
18.113
45.350
1.00
40.44


ATOM
2182
O
GLN
339
62.847
19.031
46.004
1.00
41.27


ATOM
2183
N
GLY
340
61.312
17.399
45.752
1.00
39.31


ATOM
2184
CA
GLY
340
60.678
17.619
47.038
1.00
38.16


ATOM
2185
C
GLY
340
60.257
19.015
47.451
1.00
35.80


ATOM
2186
O
GLY
340
60.453
19.396
48.603
1.00
35.38


ATOM
2187
N
TRP
341
59.690
19.788
46.533
1.00
34.88


ATOM
2188
CA
TRP
341
59.229
21.119
46.900
1.00
33.70


ATOM
2189
CB
TRP
341
58.805
21.916
45.663
1.00
32.35


ATOM
2190
CG
TRP
341
59.926
22.667
45.025
1.00
32.45


ATOM
2191
CD2
TRP
341
59.992
24.080
44.792
1.00
33.12


ATOM
2192
CE2
TRP
341
61.228
24.341
44.163
1.00
33.53


ATOM
2193
CE3
TRP
341
59.125
25.151
45.053
1.00
33.17


ATOM
2194
CD1
TRP
341
61.089
22.146
44.544
1.00
33.26


ATOM
2195
NE1
TRP
341
61.877
23.143
44.024
1.00
33.74


ATOM
2196
CZ2
TRP
341
61.624
25.632
43.788
1.00
33.86


ATOM
2197
CZ3
TRP
341
59.517
26.435
44.681
1.00
33.83


ATOM
2198
CH2
TRP
341
60.758
26.663
44.054
1.00
33.79


ATOM
2199
C
TRP
341
58.035
20.916
47.822
1.00
32.71


ATOM
2200
O
TRP
341
57.268
19.968
47.650
1.00
32.15


ATOM
2201
N
THR
342
57.892
21.790
48.812
1.00
31.61


ATOM
2202
CA
THR
342
56.782
21.697
49.754
1.00
30.86


ATOM
2203
CB
THR
342
57.271
21.368
51.176
1.00
31.36


ATOM
2204
OG1
THR
342
58.015
22.481
51.687
1.00
30.07


ATOM
2205
CG2
THR
342
58.158
20.128
51.170
1.00
32.63


ATOM
2206
C
THR
342
56.072
23.042
49.825
1.00
29.61


ATOM
2207
O
THR
342
56.577
24.044
49.324
1.00
28.37


ATOM
2208
N
PRO
343
54.882
23.078
50.442
1.00
29.45


ATOM
2209
CD
PRO
343
54.024
21.946
50.843
1.00
27.29


ATOM
2210
CA
PRO
343
54.160
24.347
50.552
1.00
28.24


ATOM
2211
CB
PRO
343
52.937
23.969
51.378
1.00
27.42


ATOM
2212
CG
PRO
343
52.646
22.579
50.887
1.00
27.57


ATOM
2213
C
PRO
343
55.036
25.393
51.247
1.00
28.41


ATOM
2214
O
PRO
343
55.105
26.543
50.816
1.00
28.24


ATOM
2215
N
ARG
344
55.721
24.982
52.311
1.00
29.01


ATOM
2216
CA
ARG
344
56.588
25.896
53.052
1.00
30.23


ATOM
2217
CB
ARG
344
57.207
25.183
54.260
1.00
32.72


ATOM
2218
CG
ARG
344
57.690
26.117
55.376
1.00
38.15


ATOM
2219
CD
ARG
344
58.192
25.317
56.580
1.00
41.91


ATOM
2220
NE
ARG
344
58.217
26.096
57.821
1.00
46.21


ATOM
2221
CZ
ARG
344
59.095
27.056
58.100
1.00
46.40


ATOM
2222
NH1
ARG
344
59.026
27.700
59.258
1.00
46.37


ATOM
2223
NH2
ARG
344
60.046
27.368
57.232
1.00
48.36


ATOM
2224
C
ARG
344
57.689
26.436
52.140
1.00
29.35


ATOM
2225
O
ARG
344
58.016
27.620
52.183
1.00
28.16


ATOM
2226
N
ARG
345
58.248
25.565
51.304
1.00
28.94


ATOM
2227
CA
ARG
345
59.302
25.968
50.378
1.00
28.91


ATOM
2228
CB
ARG
345
59.793
24.764
49.567
1.00
32.39


ATOM
2229
CG
ARG
345
61.304
24.601
49.543
1.00
38.26


ATOM
2230
CD
ARG
345
62.016
25.852
49.048
1.00
41.91


ATOM
2231
NE
ARG
345
62.441
25.769
47.650
1.00
47.14


ATOM
2232
CZ
ARG
345
63.250
24.830
47.163
1.00
48.30


ATOM
2233
NH1
ARG
345
63.724
23.877
47.955
1.00
50.47


ATOM
2234
NH2
ARG
345
63.609
24.858
45.888
1.00
48.82


ATOM
2235
C
ARG
345
58.771
27.020
49.414
1.00
26.66


ATOM
2236
O
ARG
345
59.443
28.008
49.117
1.00
25.29


ATOM
2237
N
MET
346
57.558
26.783
48.925
1.00
24.67


ATOM
2238
CA
MET
346
56.909
27.680
47.981
1.00
23.82


ATOM
2239
CB
MET
346
55.538
27.115
47.593
1.00
22.88


ATOM
2240
CG
MET
346
55.631
25.817
46.789
1.00
22.60


ATOM
2241
SD
MET
346
54.099
24.884
46.702
1.00
23.12


ATOM
2242
CE
MET
346
53.193
25.800
45.456
1.00
22.77


ATOM
2243
C
MET
346
56.776
29.087
48.548
1.00
22.51


ATOM
2244
O
MET
346
57.111
30.061
47.877
1.00
22.36


ATOM
2245
N
PHE
347
56.299
29.198
49.783
1.00
22.71


ATOM
2246
CA
PHE
347
56.154
30.512
50.397
1.00
23.33


ATOM
2247
CB
PHE
347
55.272
30.431
51.650
1.00
21.23


ATOM
2248
CG
PHE
347
53.810
30.232
51.344
1.00
20.37


ATOM
2249
CD1
PHE
347
53.280
28.957
51.191
1.00
20.90


ATOM
2250
CD2
PHE
347
52.974
31.328
51.156
1.00
20.68


ATOM
2251
CE1
PHE
347
51.937
28.775
50.855
1.00
22.83


ATOM
2252
CE2
PHE
347
51.633
31.158
50.820
1.00
19.46


ATOM
2253
CZ
PHE
347
51.113
29.879
50.668
1.00
20.69


ATOM
2254
C
PHE
347
57.521
31.109
50.731
1.00
24.58


ATOM
2255
O
PHE
347
57.698
32.329
50.701
1.00
23.58


ATOM
2256
N
LYS
348
58.489
30.248
51.039
1.00
25.53


ATOM
2257
CA
LYS
348
59.838
30.708
51.349
1.00
25.95


ATOM
2258
CB
LYS
348
60.726
29.531
51.772
1.00
29.39


ATOM
2259
CG
LYS
348
60.529
29.067
53.209
1.00
32.76


ATOM
2260
CD
LYS
348
61.020
30.117
54.201
1.00
37.96


ATOM
2261
CE
LYS
348
60.995
29.590
55.633
1.00
38.41


ATOM
2262
NZ
LYS
348
61.587
30.556
56.606
1.00
38.93


ATOM
2263
C
LYS
348
60.428
31.383
50.115
1.00
25.86


ATOM
2264
O
LYS
348
61.081
32.418
50.223
1.00
26.39


ATOM
2265
N
GLU
349
60.197
30.796
48.941
1.00
25.73


ATOM
2266
CA
GLU
349
60.701
31.375
47.696
1.00
25.00


ATOM
2267
CB
GLU
349
60.425
30.445
46.510
1.00
27.57


ATOM
2268
CG
GLU
349
61.252
29.163
46.476
1.00
32.10


ATOM
2269
CD
GLU
349
62.754
29.418
46.536
1.00
34.82


ATOM
2270
OE1
GLU
349
63.207
30.487
46.066
1.00
35.04


ATOM
2271
OE2
GLU
349
63.484
28.538
47.041
1.00
36.16


ATOM
2272
C
GLU
349
60.031
32.727
47.446
1.00
24.44


ATOM
2273
O
GLU
349
60.679
33.684
47.018
1.00
23.97


ATOM
2274
N
ALA
350
58.727
32.797
47.702
1.00
23.38


ATOM
2275
CA
ALA
350
57.985
34.043
47.522
1.00
22.42


ATOM
2276
CB
ALA
350
56.511
33.829
47.857
1.00
22.54


ATOM
2277
C
ALA
350
58.579
35.104
48.444
1.00
21.24


ATOM
2278
O
ALA
350
58.844
36.233
48.027
1.00
21.74


ATOM
2279
N
ASP
351
58.787
34.732
49.702
1.00
20.72


ATOM
2280
CA
ASP
351
59.353
35.652
50.682
1.00
21.66


ATOM
2281
CB
ASP
351
59.499
34.949
52.037
1.00
23.19


ATOM
2282
CG
ASP
351
59.901
35.900
53.150
1.00
26.89


ATOM
2283
OD1
ASP
351
59.198
36.914
53.364
1.00
26.58


ATOM
2284
OD2
ASP
351
60.921
35.633
53.818
1.00
26.96


ATOM
2285
C
ASP
351
60.708
36.163
50.198
1.00
22.19


ATOM
2286
O
ASP
351
61.051
37.330
50.392
1.00
22.86


ATOM
2287
N
ASP
352
61.472
35.289
49.548
1.00
23.64


ATOM
2288
CA
ASP
352
62.787
35.667
49.041
1.00
23.82


ATOM
2289
CB
ASP
352
63.553
34.430
48.548
1.00
23.91


ATOM
2290
CG
ASP
352
64.921
34.780
47.988
1.00
26.32


ATOM
2291
OD1
ASP
352
65.096
34.724
46.753
1.00
25.02


ATOM
2292
OD2
ASP
352
65.821
35.124
48.786
1.00
28.34


ATOM
2293
C
ASP
352
62.680
36.688
47.916
1.00
23.50


ATOM
2294
O
ASP
352
63.486
37.612
47.836
1.00
22.72


ATOM
2295
N
PHE
353
61.681
36.534
47.051
1.00
23.52


ATOM
2296
CA
PHE
353
61.522
37.475
45.953
1.00
22.24


ATOM
2297
CB
PHE
353
60.397
37.045
45.001
1.00
21.06


ATOM
2298
CG
PHE
353
60.542
37.609
43.607
1.00
19.58


ATOM
2299
CD1
PHE
353
60.744
36.767
42.516
1.00
21.35


ATOM
2300
CD2
PHE
353
60.528
38.984
43.392
1.00
19.63


ATOM
2301
CE1
PHE
353
60.935
37.288
41.230
1.00
19.63


ATOM
2302
CE2
PHE
353
60.718
39.513
42.115
1.00
19.63


ATOM
2303
CZ
PHE
353
60.923
38.660
41.029
1.00
29.46


ATOM
2304
C
PHE
353
61.237
38.870
46.504
1.00
20.90


ATOM
2305
O
PHE
353
61.837
39.849
46.059
1.00
22.16


ATOM
2306
N
PHE
354
60.329
38.968
47.471
1.00
20.76


ATOM
2307
CA
PHE
354
60.019
40.269
48.057
1.00
20.13


ATOM
2308
CB
PHE
354
58.915
40.143
49.115
1.00
20.30


ATOM
2309
CG
PHE
354
57.526
40.045
48.535
1.00
18.25


ATOM
2310
CD1
PHE
354
56.932
38.805
48.306
1.00
17.88


ATOM
2311
CD2
PHE
354
56.826
41.200
48.187
1.00
19.40


ATOM
2312
CE1
PHE
354
55.662
38.713
47.738
1.00
17.04


ATOM
2313
CE2
PHE
354
55.548
41.123
47.612
1.00
18.88


ATOM
2314
CZ
PHE
354
54.968
39.875
47.388
1.00
19.24


ATOM
2315
C
PHE
354
61.258
40.935
48.671
1.00
21.10


ATOM
2316
O
PHE
354
61.517
42.120
48.427
1.00
19.45


ATOM
2317
N
THR
355
62.028
40.184
49.456
1.00
22.06


ATOM
2318
CA
THR
355
63.224
40.748
50.081
1.00
24.14


ATOM
2319
CB
THR
355
63.849
39.787
51.126
1.00
24.56


ATOM
2320
OG1
THR
355
64.083
38.505
50.533
1.00
26.60


ATOM
2321
CG2
THR
355
62.926
39.633
52.326
1.00
25.22


ATOM
2322
C
THR
355
64.289
41.118
49.055
1.00
23.51


ATOM
2323
O
THR
355
65.042
42.070
49.257
1.00
25.42


ATOM
2324
N
SER
356
64.342
40.386
47.948
1.00
23.09


ATOM
2325
CA
SER
356
65.332
40.676
46.913
1.00
22.30


ATOM
2326
CB
SER
356
65.256
39.642
45.784
1.00
23.31


ATOM
2327
OG
SER
356
64.163
39.901
44.915
1.00
25.00


ATOM
2328
C
SER
356
65.088
42.068
46.345
1.00
22.33


ATOM
2329
O
SER
356
66.005
42.707
45.824
1.00
22.15


ATOM
2330
N
LEU
357
63.846
42.535
46.452
1.00
20.54


ATOM
2331
CA
LEU
357
63.477
43.855
45.951
1.00
21.18


ATOM
2332
CB
LEU
357
62.007
43.874
45.515
1.00
20.21


ATOM
2333
CG
LEU
357
61.567
42.939
44.386
1.00
22.18


ATOM
2334
CD1
LEU
357
60.089
43.169
44.092
1.00
20.93


ATOM
2335
CD2
LEU
357
62.391
43.197
43.140
1.00
19.15


ATOM
2336
C
LEU
357
63.687
44.929
47.015
1.00
21.10


ATOM
2337
O
LEU
357
63.448
46.113
46.769
1.00
21.69


ATOM
2338
N
GLY
358
64.133
44.513
48.193
1.00
20.78


ATOM
2339
CA
GLY
358
64.340
45.465
49.269
1.00
22.52


ATOM
2340
C
GLY
358
63.086
45.581
50.120
1.00
23.30


ATOM
2341
O
GLY
358
63.053
46.339
51.091
1.00
23.76


ATOM
2342
N
LEU
359
62.051
44.826
49.754
1.00
20.72


ATOM
2343
CA
LEU
359
60.792
44.844
50.487
1.00
21.07


ATOM
2344
CB
LEU
359
59.667
44.293
49.604
1.00
17.66


ATOM
2345
CG
LEU
359
59.417
45.174
48.371
1.00
19.03


ATOM
2346
CD1
LEU
359
58.362
44.551
47.459
1.00
16.52


ATOM
2347
CD2
LEU
359
58.977
46.563
48.829
1.00
16.74


ATOM
2348
C
LEU
359
60.909
44.062
51.797
1.00
21.60


ATOM
2349
O
LEU
359
61.932
43.424
52.058
1.00
21.13


ATOM
2350
N
LEU
360
59.863
44.112
52.616
1.00
21.11


ATOM
2351
CA
LEU
360
59.869
43.451
53.921
1.00
22.96


ATOM
2352
CB
LEU
360
58.815
44.093
54.830
1.00
23.88


ATOM
2353
CG
LEU
360
58.982
45.575
55.274
1.00
27.26


ATOM
2354
CD1
LEU
360
57.692
46.100
55.788
1.00
27.98


ATOM
2355
CD2
LEU
360
60.162
45.756
56.131
1.00
25.65


ATOM
2356
C
LEU
360
59.654
41.942
53.937
1.00
23.76


ATOM
2357
O
LEU
360
58.870
41.401
53.163
1.00
24.22


ATOM
2358
N
PRO
361
60.355
41.241
54.840
1.00
25.33


ATOM
2359
CD
PRO
361
61.465
41.730
55.683
1.00
26.75


ATOM
2360
CA
PRO
361
60.217
39.791
54.953
1.00
25.45


ATOM
2361
CB
PRO
361
61.562
39.373
55.529
1.00
27.39


ATOM
2362
CG
PRO
361
61.851
40.492
56.480
1.00
27.59


ATOM
2363
C
PRO
361
59.071
39.538
55.926
1.00
25.74


ATOM
2364
O
PRO
361
58.773
40.394
56.759
1.00
26.40


ATOM
2365
N
VAL
362
58.412
38.390
55.827
1.00
25.30


ATOM
2366
CA
VAL
362
57.323
38.115
56.757
1.00
25.65


ATOM
2367
CB
VAL
362
56.462
36.916
56.303
1.00
24.53


ATOM
2368
CG1
VAL
362
55.770
37.249
54.980
1.00
23.68


ATOM
2369
CG2
VAL
362
57.327
35.674
56.167
1.00
23.66


ATOM
2370
C
VAL
362
57.926
37.820
58.127
1.00
27.19


ATOM
2371
O
VAL
362
59.013
37.247
58.221
1.00
27.05


ATOM
2372
N
PRO
363
57.235
38.226
59.207
1.00
26.80


ATOM
2373
CD
PRO
363
56.022
39.063
59.229
1.00
26.99


ATOM
2374
CA
PRO
363
57.726
37.995
60.570
1.00
27.57


ATOM
2375
CB
PRO
363
56.685
38.706
61.441
1.00
26.11


ATOM
2376
CG
PRO
363
56.169
39.793
60.545
1.00
27.52


ATOM
2377
C
PRO
363
57.826
36.513
60.911
1.00
27.67


ATOM
2378
O
PRO
363
57.114
35.684
60.340
1.00
27.28


ATOM
2379
N
PRO
364
58.722
36.160
61.847
1.00
28.91


ATOM
2380
CD
PRO
364
59.688
37.033
62.542
1.00
30.07


ATOM
2381
CA
PRO
364
58.888
34.761
62.252
1.00
27.66


ATOM
2382
CB
PRO
364
59.844
34.864
63.437
1.00
30.48


ATOM
2383
CG
PRO
364
60.707
36.037
63.061
1.00
31.62


ATOM
2384
C
PRO
364
57.537
34.165
62.650
1.00
27.12


ATOM
2385
O
PRO
364
57.245
33.003
62.369
1.00
25.49


ATOM
2386
N
GLU
365
56.715
34.985
63.297
1.00
28.48


ATOM
2387
CA
GLU
365
55.387
34.578
63.755
1.00
29.40


ATOM
2388
CB
GLU
365
54.705
35.769
64.439
1.00
31.16


ATOM
2389
CG
GLU
365
53.287
35.524
64.907
1.00
34.46


ATOM
2390
CD
GLU
365
52.757
36.659
65.770
1.00
37.66


ATOM
2391
OE1
GLU
365
53.118
37.831
65.518
1.00
38.25


ATOM
2392
OE2
GLU
365
51.967
36.381
66.696
1.00
38.79


ATOM
2393
C
GLU
365
54.511
34.039
62.617
1.00
29.17


ATOM
2394
O
GLU
365
53.653
33.178
62.832
1.00
29.47


ATOM
2395
N
PHE
366
54.736
34.549
61.409
1.00
28.47


ATOM
2396
CA
PHE
366
53.990
34.128
60.222
1.00
26.31


ATOM
2397
CB
PHE
366
54.487
34.904
58.997
1.00
25.09


ATOM
2398
CG
PHE
366
53.986
34.361
57.680
1.00
23.73


ATOM
2399
CD1
PHE
366
52.829
34.865
57.096
1.00
22.77


ATOM
2400
CD2
PHE
366
54.681
33.348
57.023
1.00
24.15


ATOM
2401
CE1
PHE
366
52.368
34.371
55.873
1.00
21.92


ATOM
2402
CE2
PHE
366
54.228
32.845
55.799
1.00
22.88


ATOM
2403
CZ
PHE
366
53.071
33.358
55.225
1.00
22.34


ATOM
2404
C
PHE
366
54.162
32.632
59.965
1.00
25.92


ATOM
2405
O
PHE
366
53.190
31.899
59.774
1.00
24.62


ATOM
2406
N
TRP
367
55.414
32.189
59.948
1.00
26.49


ATOM
2407
CA
TRP
367
55.724
30.788
59.699
1.00
28.05


ATOM
2408
CB
TRP
367
57.242
30.605
59.640
1.00
27.25


ATOM
2409
CG
TRP
367
57.869
31.421
58.559
1.00
26.72


ATOM
2410
CD2
TRP
367
57.708
31.235
57.148
1.00
24.28


ATOM
2411
CE2
TRP
367
58.450
32.249
56.508
1.00
24.53


ATOM
2412
CE3
TRP
367
57.007
30.308
56.363
1.00
25.77


ATOM
2413
CD1
TRP
367
58.678
32.507
58.713
1.00
26.27


ATOM
2414
NE1
TRP
367
59.032
33.011
57.486
1.00
24.78


ATOM
2415
CZ2
TRP
367
58.515
32.367
55.115
1.00
25.59


ATOM
2416
CZ3
TRP
367
57.070
30.423
54.975
1.00
25.39


ATOM
2417
CH2
TRP
367
57.820
31.446
54.368
1.00
26.81


ATOM
2418
C
TRP
367
55.128
29.845
60.737
1.00
28.77


ATOM
2419
O
TRP
367
54.818
28.693
60.436
1.00
29.68


ATOM
2420
N
ASN
368
54.948
30.341
61.955
1.00
29.29


ATOM
2421
CA
ASN
368
54.407
29.517
63.023
1.00
30.04


ATOM
2422
CB
ASN
368
54.955
29.999
64.369
1.00
33.90


ATOM
2423
CG
ASN
368
54.405
29.197
65.545
1.00
37.17


ATOM
2424
OD1
ASN
368
53.214
29.307
65.846
1.00
41.44


ATOM
2425
ND2
ASN
368
55.233
28.397
66.223
1.00
37.16


ATOM
2426
C
ASN
368
52.882
29.448
63.097
1.00
30.01


ATOM
2427
O
ASN
368
52.323
28.404
63.431
1.00
27.10


ATOM
2428
N
LYS
369
52.206
30.547
62.780
1.00
28.47


ATOM
2429
CA
LYS
369
50.753
30.567
62.870
1.00
29.06


ATOM
2430
CB
LYS
369
50.308
31.882
63.513
1.00
30.23


ATOM
2431
CG
LYS
369
50.848
32.067
64.931
1.00
32.99


ATOM
2432
CD
LYS
369
50.314
33.335
65.573
1.00
38.01


ATOM
2433
CE
LYS
369
50.831
33.502
66.996
1.00
40.47


ATOM
2434
NZ
LYS
369
50.244
34.711
67.648
1.00
43.23


ATOM
2435
C
LYS
369
49.964
30.320
61.584
1.00
28.08


ATOM
2436
O
LYS
369
48.788
29.961
61.645
1.00
29.11


ATOM
2437
N
SER
370
50.594
30.498
60.426
1.00
27.36


ATOM
2438
CA
SER
370
49.904
30.288
59.151
1.00
26.35


ATOM
2439
CB
SER
370
50.774
30.764
57.977
1.00
24.78


ATOM
2440
OG
SER
370
50.954
32.171
57.991
1.00
22.65


ATOM
2441
C
SER
370
49.524
28.830
58.908
1.00
27.44


ATOM
2442
O
SER
370
50.158
27.911
59.430
1.00
27.46


ATOM
2443
N
MET
371
48.475
28.628
58.117
1.00
27.03


ATOM
2444
CA
MET
371
48.029
27.288
57.749
1.00
27.37


ATOM
2445
CB
MET
371
46.524
27.117
57.973
1.00
25.87


ATOM
2446
CG
MET
371
46.028
25.700
57.695
1.00
23.55


ATOM
2447
SD
MET
371
44.257
25.591
57.365
1.00
24.62


ATOM
2448
CE
MET
371
44.241
25.865
55.602
1.00
23.28


ATOM
2449
C
MET
371
48.336
27.186
56.259
1.00
28.01


ATOM
2450
O
MET
371
47.493
27.511
55.419
1.00
27.83


ATOM
2451
N
LEU
372
49.547
26.742
55.935
1.00
28.67


ATOM
2452
CA
LEU
372
49.976
26.636
54.544
1.00
27.98


ATOM
2453
CB
LEU
372
51.488
26.849
54.463
1.00
26.09


ATOM
2454
CG
LEU
372
52.000
28.142
55.109
1.00
26.99


ATOM
2455
CD1
LEU
372
53.516
28.186
55.014
1.00
25.50


ATOM
2456
CD2
LEU
372
51.382
29.362
54.421
1.00
25.38


ATOM
2457
C
LEU
372
49.597
25.325
53.861
1.00
29.45


ATOM
2458
O
LEU
372
49.835
25.154
52.664
1.00
29.43


ATOM
2459
N
GLU
373
49.002
24.407
54.618
1.00
30.71


ATOM
2460
CA
GLU
373
48.589
23.115
54.074
1.00
33.88


ATOM
2461
CB
GLU
373
49.576
22.012
54.460
1.00
36.25


ATOM
2462
CG
GLU
373
51.022
22.277
54.127
1.00
43.43


ATOM
2463
CD
GLU
373
51.929
21.197
54.686
1.00
46.04


ATOM
2464
OE1
GLU
373
51.953
21.025
55.924
1.00
49.71


ATOM
2465
OE2
GLU
373
52.609
20.515
53.892
1.00
48.87


ATOM
2466
C
GLU
373
47.230
22.718
54.622
1.00
33.50


ATOM
2467
O
GLU
373
46.854
23.115
55.726
1.00
32.75


ATOM
2468
N
LYS
374
46.506
21.917
53.851
1.00
33.65


ATOM
2469
CA
LYS
374
45.200
21.429
54.271
1.00
35.26


ATOM
2470
CB
LYS
374
44.523
20.687
53.121
1.00
35.25


ATOM
2471
CG
LYS
374
43.155
20.120
53.456
1.00
35.45


ATOM
2472
CD
LYS
374
42.518
19.531
52.208
1.00
35.40


ATOM
2473
CE
LYS
374
41.132
18.994
52.483
1.00
36.09


ATOM
2474
NZ
LYS
374
40.514
18.496
51.224
1.00
36.76


ATOM
2475
C
LYS
374
45.432
20.474
55.435
1.00
36.99


ATOM
2476
O
LYS
374
46.171
19.496
55.307
1.00
37.40


ATOM
2477
N
PRO
375
44.813
20.747
56.591
1.00
38.18


ATOM
2478
CD
PRO
375
44.031
21.941
56.951
1.00
38.24


ATOM
2479
CA
PRO
375
44.992
19.873
57.753
1.00
40.05


ATOM
2480
CB
PRO
375
44.133
20.545
58.822
1.00
39.71


ATOM
2481
CG
PRO
375
44.209
21.993
58.451
1.00
39.38


ATOM
2482
C
PRO
375
44.570
18.427
57.509
1.00
41.45


ATOM
2483
O
PRO
375
43.595
18.159
56.808
1.00
40.45


ATOM
2484
N
THR
376
45.330
17.502
58.084
1.00
43.87


ATOM
2485
CA
THR
376
45.042
16.077
57.989
1.00
46.82


ATOM
2486
CB
THR
376
46.331
15.268
57.766
1.00
47.11


ATOM
2487
OG1
THR
376
47.272
15.569
58.804
1.00
48.76


ATOM
2488
CG2
THR
376
46.946
15.622
56.425
1.00
46.74


ATOM
2489
C
THR
376
44.450
15.750
59.355
1.00
48.06


ATOM
2490
O
THR
376
44.102
14.612
59.664
1.00
49.50


ATOM
2491
N
ASP
377
44.345
16.808
60.151
1.00
49.79


ATOM
2492
CA
ASP
377
43.821
16.801
61.510
1.00
50.68


ATOM
2493
CB
ASP
377
43.722
18.252
61.991
1.00
51.52


ATOM
2494
CG
ASP
377
44.084
18.416
63.445
1.00
53.90


ATOM
2495
OD1
ASP
377
43.505
17.705
64.293
1.00
56.14


ATOM
2496
OD2
ASP
377
44.950
19.267
63.737
1.00
54.87


ATOM
2497
C
ASP
377
42.439
16.162
61.607
1.00
50.48


ATOM
2498
O
ASP
377
41.919
15.965
62.705
1.00
50.57


ATOM
2499
N
GLY
378
41.845
15.831
60.465
1.00
50.81


ATOM
2500
CA
GLY
378
40.504
15.280
60.486
1.00
50.66


ATOM
2501
C
GLY
378
39.635
16.487
60.795
1.00
50.28


ATOM
2502
O
GLY
378
38.488
16.379
61.230
1.00
51.71


ATOM
2503
N
ARG
379
40.231
17.653
60.560
1.00
48.17


ATOM
2504
CA
ARG
379
39.613
18.954
60.788
1.00
45.10


ATOM
2505
CB
ARG
379
40.688
19.934
61.261
1.00
45.50


ATOM
2506
CG
ARG
379
40.269
20.913
62.332
1.00
44.65


ATOM
2507
CD
ARG
379
41.270
22.052
62.408
1.00
44.87


ATOM
2508
NE
ARG
379
42.651
21.577
62.397
1.00
44.55


ATOM
2509
CZ
ARG
379
43.705
22.356
62.170
1.00
44.28


ATOM
2510
NH1
ARG
379
43.540
23.651
61.933
1.00
42.73


ATOM
2511
NH2
ARG
379
44.927
21.841
62.174
1.00
44.56


ATOM
2512
C
ARG
379
39.013
19.464
59.477
1.00
41.98


ATOM
2513
O
ARG
379
39.522
19.167
58.398
1.00
42.26


ATOM
2514
N
GLU
380
37.932
20.227
59.573
1.00
38.86


ATOM
2515
CA
GLU
380
37.286
20.788
58.390
1.00
35.74


ATOM
2516
CB
GLU
380
35.767
20.654
58.508
1.00
37.72


ATOM
2517
CG
GLU
380
35.008
20.940
57.225
1.00
41.39


ATOM
2518
CD
GLU
380
34.671
19.679
56.439
1.00
44.40


ATOM
2519
OE1
GLU
380
33.991
18.792
57.003
1.00
45.17


ATOM
2520
OE2
GLU
380
35.075
19.577
55.260
1.00
43.36


ATOM
2521
C
GLU
380
37.681
22.266
58.330
1.00
31.68


ATOM
2522
O
GLU
380
37.643
22.958
59.346
1.00
28.60


ATOM
2523
N
VAL
381
38.066
22.749
57.150
1.00
29.12


ATOM
2524
CA
VAL
381
38.480
24.145
57.013
1.00
25.82


ATOM
2525
CB
VAL
381
40.022
24.281
57.096
1.00
26.30


ATOM
2526
CG1
VAL
381
40.546
23.600
58.347
1.00
26.29


ATOM
2527
CG2
VAL
381
40.669
23.673
55.855
1.00
26.07


ATOM
2528
C
VAL
381
38.041
24.806
55.708
1.00
25.16


ATOM
2529
O
VAL
381
37.528
24.150
54.799
1.00
24.70


ATOM
2530
N
VAL
382
38.238
26.120
55.637
1.00
22.13


ATOM
2531
CA
VAL
382
37.929
26.879
54.433
1.00
22.57


ATOM
2532
CB
VAL
382
37.533
28.341
54.764
1.00
23.19


ATOM
2533
CG1
VAL
382
37.289
29.122
53.479
1.00
22.36


ATOM
2534
CG2
VAL
382
36.279
28.355
55.636
1.00
21.95


ATOM
2535
C
VAL
382
39.254
26.864
53.679
1.00
22.05


ATOM
2536
O
VAL
382
40.199
27.551
54.056
1.00
22.15


ATOM
2537
N
CYS
383
39.331
26.059
52.626
1.00
22.87


ATOM
2538
CA
CYS
383
40.561
25.937
51.857
1.00
22.31


ATOM
2539
C
CYS
383
40.946
27.106
50.957
1.00
22.33


ATOM
2540
O
CYS
383
42.134
27.335
50.723
1.00
22.41


ATOM
2541
CB
CYS
383
40.521
24.664
51.018
1.00
23.58


ATOM
2542
SG
CYS
383
41.168
23.197
51.879
1.00
25.88


ATOM
2543
N
HIS
384
39.958
27.841
50.456
1.00
21.14


ATOM
2544
CA
HIS
384
40.231
28.961
49.558
1.00
19.98


ATOM
2545
CB
HIS
384
38.954
29.761
49.286
1.00
17.69


ATOM
2546
CG
HIS
384
39.075
30.695
48.123
1.00
16.80


ATOM
2547
CD2
HIS
384
39.392
32.009
48.067
1.00
16.85


ATOM
2548
ND1
HIS
384
38.954
30.273
46.816
1.00
17.45


ATOM
2549
CE1
HIS
384
39.196
31.287
46.004
1.00
17.61


ATOM
2550
NE2
HIS
384
39.466
32.352
46.737
1.00
20.78


ATOM
2551
C
HIS
384
41.309
29.884
50.124
1.00
19.92


ATOM
2552
O
HIS
384
41.173
30.412
51.226
1.00
19.94


ATOM
2553
N
ALA
385
42.376
30.080
49.355
1.00
19.69


ATOM
2554
CA
ALA
385
43.497
30.917
49.779
1.00
18.75


ATOM
2555
CB
ALA
385
44.529
31.007
48.657
1.00
16.28


ATOM
2556
C
ALA
385
43.110
32.322
50.228
1.00
17.94


ATOM
2557
O
ALA
385
42.298
32.990
49.589
1.00
16.36


ATOM
2558
N
SER
386
43.708
32.769
51.328
1.00
19.03


ATOM
2559
CA
SER
386
43.450
34.110
51.847
1.00
19.74


ATOM
2560
CB
SER
386
42.098
34.163
52.581
1.00
20.01


ATOM
2561
OG
SER
386
42.041
33.244
53.656
1.00
24.98


ATOM
2562
C
SER
386
44.576
34.584
52.767
1.00
19.49


ATOM
2563
O
SER
386
45.305
33.775
53.355
1.00
20.16


ATOM
2564
N
ALA
387
44.721
35.903
52.860
1.00
19.32


ATOM
2565
CA
ALA
387
45.744
36.541
53.682
1.00
18.05


ATOM
2566
CB
ALA
387
46.571
37.502
52.840
1.00
18.53


ATOM
2567
C
ALA
387
45.048
37.292
54.804
1.00
19.41


ATOM
2568
O
ALA
387
44.006
37.922
54.594
1.00
18.50


ATOM
2569
N
TRP
388
45.641
37.243
55.988
1.00
18.57


ATOM
2570
CA
TRP
388
45.043
37.862
57.157
1.00
20.63


ATOM
2571
CB
TRP
388
44.672
36.764
58.158
1.00
20.94


ATOM
2572
CG
TRP
388
43.693
35.759
57.626
1.00
20.63


ATOM
2573
CD2
TRP
388
42.423
35.424
58.195
1.00
20.38


ATOM
2574
CE2
TRP
388
41.847
34.427
57.374
1.00
20.45


ATOM
2575
CE3
TRP
388
41.715
35.872
59.321
1.00
20.78


ATOM
2576
CD1
TRP
388
43.834
34.974
56.513
1.00
21.13


ATOM
2577
NE1
TRP
388
42.728
34.171
56.356
1.00
19.97


ATOM
2578
CZ2
TRP
388
40.591
33.867
57.645
1.00
21.53


ATOM
2579
CZ3
TRP
388
40.464
35.315
59.590
1.00
22.62


ATOM
2580
CH2
TRP
388
39.917
34.323
58.754
1.00
22.52


ATOM
2581
C
TRP
388
45.873
38.923
57.877
1.00
21.09


ATOM
2582
O
TRP
388
47.062
38.734
58.148
1.00
20.91


ATOM
2583
N
ASP
389
45.222
40.040
58.183
1.00
20.21


ATOM
2584
CA
ASP
389
45.845
41.127
58.922
1.00
20.18


ATOM
2585
CB
ASP
389
45.577
42.472
58.241
1.00
18.75


ATOM
2586
CG
ASP
389
46.327
43.615
58.900
1.00
19.53


ATOM
2587
OD1
ASP
389
46.749
43.451
60.065
1.00
19.53


ATOM
2588
OD2
ASP
389
46.492
44.676
58.261
1.00
18.57


ATOM
2589
C
ASP
389
45.140
41.091
60.283
1.00
21.39


ATOM
2590
O
ASP
389
43.913
41.234
60.350
1.00
19.21


ATOM
2591
N
PHE
390
45.894
40.875
61.358
1.00
21.15


ATOM
2592
CA
PHE
390
45.286
40.819
62.687
1.00
23.78


ATOM
2593
CB
PHE
390
45.959
39.741
63.546
1.00
22.15


ATOM
2594
CG
PHE
390
45.567
38.341
63.165
1.00
23.26


ATOM
2595
CD1
PHE
390
46.029
37.771
61.983
1.00
21.17


ATOM
2596
CD2
PHE
390
44.707
37.604
63.974
1.00
23.14


ATOM
2597
CE1
PHE
390
45.640
36.490
61.608
1.00
22.67


ATOM
2598
CE2
PHE
390
44.310
36.321
63.610
1.00
25.19


ATOM
2599
CZ
PHE
390
44.780
35.761
62.420
1.00
24.11


ATOM
2600
C
PHE
390
45.289
42.159
63.414
1.00
24.86


ATOM
2601
O
PHE
390
45.079
42.226
64.627
1.00
26.08


ATOM
2602
N
TYR
391
45.529
43.218
62.649
1.00
26.25


ATOM
2603
CA
TYR
391
45.535
44.597
63.133
1.00
29.34


ATOM
2604
CB
TYR
391
44.097
45.083
63.329
1.00
32.35


ATOM
2605
CG
TYR
391
43.174
44.734
62.188
1.00
36.14


ATOM
2606
CD1
TYR
391
42.490
43.521
62.172
1.00
38.33


ATOM
2607
CE1
TYR
391
41.645
43.185
61.126
1.00
41.84


ATOM
2608
CD2
TYR
391
42.992
45.609
61.118
1.00
39.05


ATOM
2609
CE2
TYR
391
42.148
45.281
60.059
1.00
42.44


ATOM
2610
CZ
TYR
391
41.477
44.068
60.074
1.00
42.85


ATOM
2611
OH
TYR
391
40.630
43.737
59.042
1.00
48.25


ATOM
2612
C
TYR
391
46.334
44.960
64.382
1.00
29.54


ATOM
2613
O
TYR
391
45.897
45.802
65.166
1.00
30.88


ATOM
2614
N
ASN
392
47.492
44.342
64.583
1.00
28.09


ATOM
2615
CA
ASN
392
48.317
44.697
65.732
1.00
26.46


ATOM
2616
CB
ASN
392
48.375
43.554
66.762
1.00
25.72


ATOM
2617
CG
ASN
392
49.069
42.311
66.238
1.00
24.13


ATOM
2618
OD1
ASN
392
49.450
42.234
65.074
1.00
19.92


ATOM
2619
ND2
ASN
392
49.232
41.324
67.110
1.00
24.99


ATOM
2620
C
ASN
392
49.703
45.042
65.208
1.00
26.86


ATOM
2621
O
ASN
392
50.630
45.301
65.974
1.00
26.07


ATOM
2622
N
GLY
393
49.820
45.051
63.880
1.00
26.09


ATOM
2623
CA
GLY
393
51.075
45.371
63.225
1.00
24.15


ATOM
2624
C
GLY
393
52.155
44.325
63.404
1.00
24.36


ATOM
2625
O
GLY
393
53.313
44.560
63.061
1.00
25.32


ATOM
2626
N
LYS
394
51.784
43.159
63.916
1.00
23.94


ATOM
2627
CA
LYS
394
52.763
42.107
64.147
1.00
26.37


ATOM
2628
CB
LYS
394
53.069
42.017
65.645
1.00
29.65


ATOM
2629
CG
LYS
394
54.522
42.251
65.990
1.00
35.63


ATOM
2630
CD
LYS
394
54.954
43.660
65.631
1.00
38.94


ATOM
2631
CE
LYS
394
54.438
44.665
66.640
1.00
42.85


ATOM
2632
NZ
LYS
394
55.031
44.415
67.988
1.00
44.66


ATOM
2633
C
LYS
394
52.336
40.732
63.647
1.00
25.74


ATOM
2634
O
LYS
394
53.145
39.984
63.097
1.00
26.30


ATOM
2635
N
ASP
395
51.062
40.413
63.839
1.00
24.66


ATOM
2636
CA
ASP
395
50.514
39.117
63.461
1.00
24.69


ATOM
2637
CB
ASP
395
49.529
38.674
64.549
1.00
22.82


ATOM
2638
CG
ASP
395
49.088
37.237
64.402
1.00
24.52


ATOM
2639
OD1
ASP
395
49.389
36.602
63.368
1.00
24.94


ATOM
2640
OD2
ASP
395
48.424
36.738
65.333
1.00
27.00


ATOM
2641
C
ASP
395
49.830
39.102
62.086
1.00
25.11


ATOM
2642
O
ASP
395
48.725
39.631
61.919
1.00
23.47


ATOM
2643
N
PHE
396
50.498
38.498
61.106
1.00
24.32


ATOM
2644
CA
PHE
396
49.955
38.383
59.750
1.00
23.41


ATOM
2645
CB
PHE
396
50.783
39.188
58.743
1.00
23.60


ATOM
2646
CG
PHE
396
51.136
40.571
59.203
1.00
24.38


ATOM
2647
CD1
PHE
396
52.341
40.813
59.858
1.00
25.69


ATOM
2648
CD2
PHE
396
50.274
41.641
58.965
1.00
25.33


ATOM
2649
CE1
PHE
396
52.687
42.104
60.267
1.00
23.83


ATOM
2650
CE2
PHE
396
50.611
42.934
59.371
1.00
23.41


ATOM
2651
CZ
PHE
396
51.821
43.164
60.023
1.00
23.93


ATOM
2652
C
PHE
396
50.027
36.910
59.379
1.00
23.79


ATOM
2653
O
PHE
396
51.023
36.246
59.670
1.00
24.61


ATOM
2654
N
ARG
397
48.984
36.394
58.736
1.00
23.34


ATOM
2655
CA
ARG
397
48.973
34.984
58.371
1.00
21.97


ATOM
2656
CB
ARG
397
48.245
34.166
59.443
1.00
22.90


ATOM
2657
CG
ARG
397
48.555
34.552
60.881
1.00
23.65


ATOM
2658
CD
ARG
397
47.710
33.717
61.832
1.00
24.02


ATOM
2659
NE
ARG
397
47.685
34.268
63.183
1.00
24.58


ATOM
2660
CZ
ARG
397
46.977
33.755
64.184
1.00
25.68


ATOM
2661
NH1
ARG
397
46.235
32.672
63.988
1.00
24.67


ATOM
2662
NH2
ARG
397
46.998
34.333
65.377
1.00
25.68


ATOM
2663
C
ARG
397
48.312
34.679
57.035
1.00
22.32


ATOM
2664
O
ARG
397
47.522
35.468
56.507
1.00
20.61


ATOM
2665
N
ILE
398
48.636
33.504
56.505
1.00
22.29


ATOM
2666
CA
ILE
398
48.057
33.029
55.260
1.00
20.95


ATOM
2667
CB
ILE
398
49.137
32.891
54.154
1.00
20.55


ATOM
2668
CG2
ILE
398
48.629
32.009
53.016
1.00
21.09


ATOM
2669
CG1
ILE
398
49.502
34.282
53.625
1.00
18.02


ATOM
2670
CD1
ILE
398
50.575
34.283
52.548
1.00
17.26


ATOM
2671
C
ILE
398
47.400
31.679
55.544
1.00
21.59


ATOM
2672
O
ILE
398
47.938
30.862
56.300
1.00
21.62


ATOM
2673
N
LYS
399
46.214
31.478
54.971
1.00
20.68


ATOM
2674
CA
LYS
399
45.453
30.239
55.115
1.00
19.59


ATOM
2675
CB
LYS
399
44.115
30.495
55.818
1.00
19.25


ATOM
2676
CG
LYS
399
43.236
29.248
55.912
1.00
20.50


ATOM
2677
CD
LYS
399
41.796
29.585
56.296
1.00
20.84


ATOM
2678
CE
LYS
399
41.143
30.517
55.274
1.00
19.03


ATOM
2679
NZ
LYS
399
41.207
29.974
53.882
1.00
17.95


ATOM
2680
C
LYS
399
45.188
29.723
53.704
1.00
20.32


ATOM
2681
O
LYS
399
44.379
30.291
52.966
1.00
17.80


ATOM
2682
N
GLN
400
45.857
28.638
53.335
1.00
19.73


ATOM
2683
CA
GLN
400
45.716
28.092
51.993
1.00
19.81


ATOM
2684
CB
GLN
400
46.701
28.819
51.074
1.00
20.96


ATOM
2685
CG
GLN
400
46.652
28.439
49.606
1.00
22.65


ATOM
2686
CD
GLN
400
47.679
29.200
48.788
1.00
23.34


ATOM
2687
OE1
GLN
400
47.979
30.360
49.073
1.00
23.98


ATOM
2688
NE2
GLN
400
48.213
28.556
47.757
1.00
25.85


ATOM
2689
C
GLN
400
46.013
26.601
51.986
1.00
20.97


ATOM
2690
O
GLN
400
47.011
26.173
52.559
1.00
19.21


ATOM
2691
N
CYS
401
45.148
25.810
51.356
1.00
22.51


ATOM
2692
CA
CYS
401
45.389
24.372
51.268
1.00
24.18


ATOM
2693
C
CYS
401
46.241
24.204
50.017
1.00
24.54


ATOM
2694
O
CYS
401
45.795
23.703
48.982
1.00
24.83


ATOM
2695
CB
CYS
401
44.077
23.602
51.144
1.00
24.18


ATOM
2696
SG
CYS
401
42.962
23.853
52.560
1.00
26.68


ATOM
2697
N
THR
402
47.481
24.653
50.145
1.00
23.39


ATOM
2698
CA
THR
402
48.455
24.649
49.072
1.00
23.83


ATOM
2699
CB
THR
402
49.761
25.296
49.553
1.00
24.60


ATOM
2700
OG1
THR
402
49.458
26.532
50.214
1.00
24.98


ATOM
2701
CG2
THR
402
50.694
25.564
48.377
1.00
24.72


ATOM
2702
C
THR
402
48.789
23.295
48.468
1.00
23.55


ATOM
2703
O
THR
402
49.037
22.323
49.178
1.00
22.36


ATOM
2704
N
THR
403
48.790
23.250
47.142
1.00
24.22


ATOM
2705
CA
THR
403
49.142
22.044
46.407
1.00
25.66


ATOM
2706
CB
THR
403
48.096
21.716
45.323
1.00
26.94


ATOM
2707
OG1
THR
403
46.879
21.298
45.953
1.00
31.08


ATOM
2708
CG2
THR
403
48.589
20.597
44.421
1.00
30.68


ATOM
2709
C
THR
403
50.482
22.350
45.752
1.00
24.67


ATOM
2710
O
THR
403
50.747
23.494
45.377
1.00
24.35


ATOM
2711
N
VAL
404
51.329
21.337
45.618
1.00
25.92


ATOM
2712
CA
VAL
404
52.644
21.533
45.021
1.00
25.04


ATOM
2713
CB
VAL
404
53.648
20.485
45.549
1.00
25.96


ATOM
2714
CG1
VAL
404
55.024
20.725
44.949
1.00
24.79


ATOM
2715
CG2
VAL
404
53.716
20.557
47.068
1.00
24.67


ATOM
2716
C
VAL
404
52.632
21.494
43.493
1.00
25.52


ATOM
2717
O
VAL
404
52.737
20.429
42.881
1.00
26.04


ATOM
2718
N
ASN
405
52.491
22.671
42.893
1.00
24.32


ATOM
2719
CA
ASN
405
52.490
22.835
41.440
1.00
24.14


ATOM
2720
CB
ASN
405
51.176
22.345
40.818
1.00
24.83


ATOM
2721
CG
ASN
405
49.954
22.969
41.456
1.00
27.35


ATOM
2722
OD1
ASN
405
49.858
24.187
41.591
1.00
29.21


ATOM
2723
ND2
ASN
405
49.004
22.132
41.842
1.00
28.69


ATOM
2724
C
ASN
405
52.702
24.311
41.133
1.00
24.79


ATOM
2725
O
ASN
405
52.667
25.150
42.041
1.00
22.13


ATOM
2726
N
LEU
406
52.922
24.629
39.862
1.00
22.38


ATOM
2727
CA
LEU
406
53.167
26.005
39.459
1.00
24.32


ATOM
2728
CB
LEU
406
53.582
26.056
37.986
1.00
24.24


ATOM
2729
CG
LEU
406
53.912
27.439
37.417
1.00
26.51


ATOM
2730
CD1
LEU
406
54.969
28.127
38.280
1.00
25.09


ATOM
2731
CD2
LEU
406
54.403
27.288
35.980
1.00
27.04


ATOM
2732
C
LEU
406
51.978
26.931
39.691
1.00
24.77


ATOM
2733
O
LEU
406
52.152
28.082
40.082
1.00
24.88


ATOM
2734
N
GLU
407
50.773
26.428
39.452
1.00
24.97


ATOM
2735
CA
GLU
407
49.571
27.231
39.635
1.00
27.47


ATOM
2736
CB
GLU
407
48.334
26.392
39.285
1.00
29.90


ATOM
2737
CG
GLU
407
47.011
27.143
39.341
1.00
33.59


ATOM
2738
CD
GLU
407
45.921
26.457
38.527
1.00
36.42


ATOM
2739
OE1
GLU
407
45.788
25.218
38.627
1.00
36.53


ATOM
2740
OE2
GLU
407
45.193
27.159
37.791
1.00
37.68


ATOM
2741
C
GLU
407
49.482
27.767
41.066
1.00
26.40


ATOM
2742
O
GLU
407
49.209
28.948
41.278
1.00
27.12


ATOM
2743
N
ASP
408
49.729
26.901
42.043
1.00
25.56


ATOM
2744
CA
ASP
408
49.683
27.303
43.448
1.00
26.24


ATOM
2745
CB
ASP
408
49.567
26.070
44.345
1.00
28.50


ATOM
2746
CG
ASP
408
48.160
25.857
44.850
1.00
32.70


ATOM
2747
OD1
ASP
408
47.216
26.002
44.047
1.00
38.19


ATOM
2748
OD2
ASP
408
47.992
25.541
46.046
1.00
36.12


ATOM
2749
C
ASP
408
50.895
28.132
43.866
1.00
25.11


ATOM
2750
O
ASP
408
50.853
28.837
44.873
1.00
23.90


ATOM
2751
N
LEU
409
51.980
28.039
43.103
1.00
22.82


ATOM
2752
CA
LEU
409
53.170
28.819
43.416
1.00
22.42


ATOM
2753
CB
LEU
409
54.349
28.401
42.532
1.00
23.11


ATOM
2754
CG
LEU
409
55.660
29.142
42.815
1.00
23.64


ATOM
2755
CD1
LEU
409
56.084
28.889
44.253
1.00
23.67


ATOM
2756
CD2
LEU
409
56.739
28.674
41.855
1.00
23.00


ATOM
2757
C
LEU
409
52.811
30.274
43.140
1.00
21.63


ATOM
2758
O
LEU
409
53.165
31.175
43.906
1.00
19.27


ATOM
2759
N
VAL
410
52.100
30.491
42.037
1.00
19.69


ATOM
2760
CA
VAL
410
51.664
31.829
41.666
1.00
20.55


ATOM
2761
CB
VAL
410
50.977
31.834
40.282
1.00
21.61


ATOM
2762
CG1
VAL
410
50.409
33.215
39.983
1.00
20.73


ATOM
2763
CG2
VAL
410
51.981
31.433
39.209
1.00
24.65


ATOM
2764
C
VAL
410
50.678
32.332
42.717
1.00
19.32


ATOM
2765
O
VAL
410
50.747
33.485
43.138
1.00
20.39


ATOM
2766
N
VAL
411
49.766
31.465
43.150
1.00
19.65


ATOM
2767
CA
VAL
411
48.790
31.858
44.163
1.00
20.22


ATOM
2768
CB
VAL
411
47.767
30.730
44.439
1.00
20.61


ATOM
2769
CG1
VAL
411
46.824
31.137
45.578
1.00
19.72


ATOM
2770
CG2
VAL
411
46.957
30.447
43.174
1.00
18.85


ATOM
2771
C
VAL
411
49.497
32.226
45.466
1.00
21.47


ATOM
2772
O
VAL
411
49.085
33.150
46.171
1.00
20.05


ATOM
2773
N
ALA
412
50.572
31.510
45.776
1.00
20.65


ATOM
2774
CA
ALA
412
51.332
31.781
46.989
1.00
20.54


ATOM
2775
CB
ALA
412
52.448
30.755
47.145
1.00
20.33


ATOM
2776
C
ALA
412
51.912
33.196
46.935
1.00
20.50


ATOM
2777
O
ALA
412
51.902
33.915
47.934
1.00
20.25


ATOM
2778
N
HIS
413
52.422
33.591
45.769
1.00
19.01


ATOM
2779
CA
HIS
413
52.979
34.931
45.605
1.00
18.24


ATOM
2780
CB
HIS
413
53.653
35.084
44.236
1.00
18.06


ATOM
2781
CG
HIS
413
55.006
34.452
44.161
1.00
17.97


ATOM
2782
CD2
HIS
413
56.243
35.001
44.109
1.00
17.44


ATOM
2783
ND1
HIS
413
55.193
33.087
44.199
1.00
18.68


ATOM
2784
CE1
HIS
413
56.488
32.822
44.176
1.00
17.45


ATOM
2785
NE2
HIS
413
57.146
33.965
44.123
1.00
17.19


ATOM
2786
C
HIS
413
51.861
35.950
45.736
1.00
16.58


ATOM
2787
O
HIS
413
52.041
37.005
46.339
1.00
15.66


ATOM
2788
N
HIS
414
50.708
35.623
45.158
1.00
16.88


ATOM
2789
CA
HIS
414
49.534
36.492
45.212
1.00
16.63


ATOM
2790
CB
HIS
414
48.320
35.785
44.596
1.00
17.03


ATOM
2791
CG
HIS
414
47.034
36.539
44.760
1.00
17.66


ATOM
2792
CD2
HIS
414
46.091
36.491
45.732
1.00
16.85


ATOM
2793
ND1
HIS
414
46.612
37.497
43.863
1.00
17.56


ATOM
2794
CE1
HIS
414
45.463
38.005
44.275
1.00
17.61


ATOM
2795
NE2
HIS
414
45.125
37.411
45.406
1.00
17.08


ATOM
2796
C
HIS
414
49.218
36.835
46.662
1.00
16.06


ATOM
2797
O
HIS
414
49.070
38.006
47.017
1.00
17.09


ATOM
2798
N
GLU
415
49.118
35.799
47.493
1.00
15.07


ATOM
2799
CA
GLU
415
48.807
35.964
48.910
1.00
16.06


ATOM
2800
CB
GLU
415
48.527
34.600
49.553
1.00
16.75


ATOM
2801
CG
GLU
415
47.327
33.845
48.972
1.00
16.11


ATOM
2802
CD
GLU
415
46.013
34.599
49.145
1.00
16.59


ATOM
2803
OE1
GLU
415
45.878
35.334
50.142
1.00
17.28


ATOM
2804
OE2
GLU
415
45.109
34.444
48.292
1.00
15.42


ATOM
2805
C
GLU
415
49.920
36.679
49.676
1.00
17.92


ATOM
2806
O
GLU
415
49.642
37.486
50.570
1.00
18.35


ATOM
2807
N
MET
416
51.174
36.383
49.338
1.00
16.54


ATOM
2808
CA
MET
416
52.295
37.034
50.008
1.00
17.95


ATOM
2809
CB
MET
416
53.619
36.392
49.583
1.00
17.54


ATOM
2810
CG
MET
416
53.855
35.041
50.243
1.00
19.19


ATOM
2811
SD
MET
416
54.175
35.197
52.034
1.00
21.75


ATOM
2812
CE
MET
416
55.966
35.333
52.015
1.00
20.55


ATOM
2813
C
MET
416
52.280
38.522
49.670
1.00
18.12


ATOM
2814
O
MET
416
52.789
39.356
50.427
1.00
15.13


ATOM
2815
N
GLY
417
51.680
38.840
48.526
1.00
17.95


ATOM
2816
CA
GLY
417
51.561
40.222
48.109
1.00
15.72


ATOM
2817
C
GLY
417
50.621
40.942
49.066
1.00
15.92


ATOM
2818
O
GLY
417
50.856
42.094
49.413
1.00
14.01


ATOM
2819
N
HIS
418
49.551
40.268
49.487
1.00
16.50


ATOM
2820
CA
HIS
418
48.603
40.861
50.434
1.00
17.17


ATOM
2821
CB
HIS
418
47.415
39.931
50.697
1.00
15.51


ATOM
2822
CG
HIS
418
46.421
39.866
49.578
1.00
17.03


ATOM
2823
CD2
HIS
418
45.843
38.807
48.963
1.00
15.43


ATOM
2824
ND1
HIS
418
45.848
40.991
49.022
1.00
19.32


ATOM
2825
CE1
HIS
418
44.958
40.626
48.115
1.00
17.79


ATOM
2826
NE2
HIS
418
44.935
39.306
48.060
1.00
17.55


ATOM
2827
C
HIS
418
49.320
41.110
51.758
1.00
17.69


ATOM
2828
O
HIS
418
49.163
42.167
52.370
1.00
16.65


ATOM
2829
N
ILE
419
50.100
40.126
52.199
1.00
16.39


ATOM
2830
CA
ILE
419
50.848
40.239
53.450
1.00
18.31


ATOM
2831
CB
ILE
419
51.640
38.941
53.745
1.00
17.86


ATOM
2832
CG2
ILE
419
52.498
39.115
54.995
1.00
17.98


ATOM
2833
CG1
ILE
419
50.668
37.767
53.910
1.00
17.08


ATOM
2834
CD1
ILE
419
49.723
37.907
55.078
1.00
16.70


ATOM
2835
C
ILE
419
51.821
41.417
53.410
1.00
17.09


ATOM
2836
O
ILE
419
51.988
42.127
54.403
1.00
18.17


ATOM
2837
N
GLN
420
52.457
41.628
52.260
1.00
17.68


ATOM
2838
CA
GLN
420
53.404
42.728
52.115
1.00
16.85


ATOM
2839
CB
GLN
420
54.093
42.677
50.746
1.00
17.05


ATOM
2840
CG
GLN
420
55.148
43.766
50.562
1.00
17.55


ATOM
2841
CD
GLN
420
56.380
43.547
51.428
1.00
18.80


ATOM
2842
OE1
GLN
420
57.049
44.501
51.824
1.00
17.97


ATOM
2843
NE2
GLN
420
56.694
42.286
51.710
1.00
18.82


ATOM
2844
C
GLN
420
52.671
44.054
52.274
1.00
17.71


ATOM
2845
O
GLN
420
53.171
44.985
52.909
1.00
17.12


ATOM
2846
N
TYR
421
51.479
44.138
51.695
1.00
18.42


ATOM
2847
CA
TYR
421
50.688
45.356
51.792
1.00
18.42


ATOM
2848
CB
TYR
421
49.418
45.217
50.943
1.00
16.41


ATOM
2849
CG
TYR
421
49.113
46.419
50.075
1.00
15.65


ATOM
2850
CD1
TYR
421
48.661
46.257
48.764
1.00
14.49


ATOM
2851
CE1
TYR
421
48.335
47.352
47.973
1.00
14.23


ATOM
2852
CD2
TYR
421
49.237
47.717
50.570
1.00
16.14


ATOM
2853
CE2
TYR
421
48.913
48.825
49.783
1.00
15.24


ATOM
2854
CZ
TYR
421
48.459
48.633
48.486
1.00
16.86


ATOM
2855
OH
TYR
421
48.108
49.718
47.703
1.00
14.61


ATOM
2856
C
TYR
421
50.344
45.619
53.266
1.00
19.47


ATOM
2857
O
TYR
421
50.473
46.746
53.744
1.00
19.23


ATOM
2858
N
PHE
422
49.928
44.577
53.986
1.00
19.13


ATOM
2859
CA
PHE
422
49.591
44.716
55.407
1.00
20.97


ATOM
2860
CB
PHE
422
49.260
43.353
56.029
1.00
19.61


ATOM
2861
CG
PHE
422
48.029
42.690
55.463
1.00
19.85


ATOM
2862
CD1
PHE
422
47.863
41.309
55.574
1.00
20.06


ATOM
2863
CD2
PHE
422
47.038
43.434
54.829
1.00
18.91


ATOM
2864
CE1
PHE
422
46.731
40.675
55.058
1.00
19.40


ATOM
2865
CE2
PHE
422
45.898
42.807
54.312
1.00
18.30


ATOM
2866
CZ
PHE
422
45.748
41.425
54.427
1.00
18.76


ATOM
2867
C
PHE
422
50.771
45.314
56.170
1.00
21.67


ATOM
2868
O
PHE
422
50.619
46.274
56.923
1.00
21.52


ATOM
2869
N
MET
423
51.950
44.737
55.964
1.00
21.08


ATOM
2870
CA
MET
423
53.153
45.196
56.644
1.00
21.47


ATOM
2871
CB
MET
423
54.316
44.237
56.373
1.00
21.55


ATOM
2872
CG
MET
423
54.057
42.811
56.820
1.00
23.09


ATOM
2873
SD
MET
423
55.572
41.828
56.883
1.00
26.45


ATOM
2874
CE
MET
423
55.812
41.441
55.121
1.00
20.52


ATOM
2875
C
MET
423
53.560
46.610
56.257
1.00
22.13


ATOM
2876
O
MET
423
54.024
47.375
57.104
1.00
21.14


ATOM
2877
N
GLN
424
53.381
46.957
54.985
1.00
21.08


ATOM
2878
CA
GLN
424
53.747
48.281
54.499
1.00
21.09


ATOM
2879
CB
GLN
424
53.668
48.326
52.967
1.00
21.81


ATOM
2880
CG
GLN
424
54.783
47.570
52.238
1.00
20.30


ATOM
2881
CD
GLN
424
56.145
48.214
52.419
1.00
21.34


ATOM
2882
OE1
GLN
424
56.248
49.415
52.677
1.00
21.87


ATOM
2883
NE2
GLN
424
57.200
47.422
52.262
1.00
20.74


ATOM
2884
C
GLN
424
52.921
49.431
55.082
1.00
22.17


ATOM
2885
O
GLN
424
53.460
50.514
55.319
1.00
21.22


ATOM
2886
N
TYR
425
51.624
49.219
55.308
1.00
21.31


ATOM
2887
CA
TYR
425
50.791
50.293
55.861
1.00
20.51


ATOM
2888
CB
TYR
425
49.551
50.538
54.975
1.00
18.49


ATOM
2889
CG
TYR
425
48.603
49.360
54.753
1.00
18.46


ATOM
2890
CD1
TYR
425
48.144
48.581
55.820
1.00
16.90


ATOM
2891
CE1
TYR
425
47.193
47.564
55.624
1.00
16.58


ATOM
2892
CD2
TYR
425
48.091
49.089
53.478
1.00
16.81


ATOM
2893
CE2
TYR
425
47.139
48.083
53.272
1.00
16.87


ATOM
2894
CZ
TYR
425
46.694
47.324
54.349
1.00
18.42


ATOM
2895
OH
TYR
425
45.744
46.342
54.150
1.00
17.95


ATOM
2896
C
TYR
425
50.354
50.082
57.310
1.00
21.09


ATOM
2897
O
TYR
425
49.447
50.758
57.795
1.00
21.46


ATOM
2898
N
LYS
426
51.018
49.162
58.003
1.00
21.85


ATOM
2899
CA
LYS
426
50.678
48.840
59.391
1.00
24.15


ATOM
2900
CB
LYS
426
51.593
47.727
59.912
1.00
23.65


ATOM
2901
CG
LYS
426
53.048
48.138
60.077
1.00
27.12


ATOM
2902
CD
LYS
426
53.883
46.986
60.636
1.00
29.68


ATOM
2903
CE
LYS
426
55.337
47.396
60.853
1.00
32.06


ATOM
2904
NZ
LYS
426
55.457
48.484
61.862
1.00
35.07


ATOM
2905
C
LYS
426
50.708
50.007
60.383
1.00
24.45


ATOM
2906
O
LYS
426
50.117
49.914
61.460
1.00
24.16


ATOM
2907
N
ASP
427
51.385
51.098
60.033
1.00
25.44


ATOM
2908
CA
ASP
427
51.473
52.238
60.941
1.00
27.31


ATOM
2909
CB
ASP
427
52.888
52.816
60.921
1.00
29.17


ATOM
2910
CG
ASP
427
53.919
51.824
61.410
1.00
32.66


ATOM
2911
OD1
ASP
427
53.697
51.226
62.484
1.00
34.11


ATOM
2912
OD2
ASP
427
54.948
51.644
60.727
1.00
35.93


ATOM
2913
C
ASP
427
50.466
53.354
60.686
1.00
27.40


ATOM
2914
O
ASP
427
50.487
54.382
61.362
1.00
27.53


ATOM
2915
N
LEU
428
49.586
53.163
59.711
1.00
26.71


ATOM
2916
CA
LEU
428
48.581
54.175
59.417
1.00
25.14


ATOM
2917
CB
LEU
428
48.159
54.110
57.946
1.00
25.72


ATOM
2918
CG
LEU
428
49.169
54.334
56.819
1.00
24.48


ATOM
2919
CD1
LEU
428
48.466
54.097
55.487
1.00
23.73


ATOM
2920
CD2
LEU
428
49.731
55.743
56.878
1.00
24.31


ATOM
2921
C
LEU
428
47.356
53.897
60.271
1.00
23.90


ATOM
2922
O
LEU
428
47.199
52.798
60.801
1.00
23.96


ATOM
2923
N
PRO
429
46.477
54.897
60.433
1.00
23.83


ATOM
2924
CD
PRO
429
46.585
56.303
60.003
1.00
22.86


ATOM
2925
CA
PRO
429
45.267
54.676
61.232
1.00
24.74


ATOM
2926
CB
PRO
429
44.497
55.977
61.046
1.00
22.89


ATOM
2927
CG
PRO
429
45.593
56.993
60.911
1.00
23.44


ATOM
2928
C
PRO
429
44.555
53.484
60.584
1.00
25.64


ATOM
2929
O
PRO
429
44.529
53.380
59.356
1.00
25.40


ATOM
2930
N
VAL
430
43.986
52.590
61.390
1.00
26.24


ATOM
2931
CA
VAL
430
43.320
51.404
60.854
1.00
26.47


ATOM
2932
CB
VAL
430
42.621
50.590
61.972
1.00
29.13


ATOM
2933
CG1
VAL
430
43.660
50.035
62.933
1.00
28.70


ATOM
2934
CG2
VAL
430
41.620
51.467
62.708
1.00
30.53


ATOM
2935
C
VAL
430
42.307
51.672
59.743
1.00
25.82


ATOM
2936
O
VAL
430
42.148
50.856
58.837
1.00
24.60


ATOM
2937
N
ALA
431
41.629
52.812
59.802
1.00
24.76


ATOM
2938
CA
ALA
431
40.639
53.143
58.786
1.00
24.41


ATOM
2939
CB
ALA
431
39.898
54.419
59.171
1.00
26.53


ATOM
2940
C
ALA
431
41.286
53.313
57.419
1.00
23.48


ATOM
2941
O
ALA
431
40.623
53.198
56.391
1.00
23.10


ATOM
2942
N
LEU
432
42.587
53.583
57.407
1.00
23.44


ATOM
2943
CA
LEU
432
43.297
53.785
56.153
1.00
22.88


ATOM
2944
CB
LEU
432
44.143
55.059
56.236
1.00
23.01


ATOM
2945
CG
LEU
432
43.365
56.321
56.628
1.00
22.58


ATOM
2946
CD1
LEU
432
44.321
57.500
56.716
1.00
21.61


ATOM
2947
CD2
LEU
432
42.267
56.597
55.606
1.00
24.25


ATOM
2948
C
LEU
432
44.178
52.595
55.787
1.00
23.45


ATOM
2949
O
LEU
432
44.974
52.666
54.844
1.00
23.80


ATOM
2950
N
ARG
433
44.030
51.501
56.529
1.00
22.08


ATOM
2951
CA
ARG
433
44.815
50.303
56.260
1.00
22.75


ATOM
2952
CB
ARG
433
45.026
49.497
57.546
1.00
23.50


ATOM
2953
CG
ARG
433
45.849
50.225
58.607
1.00
26.73


ATOM
2954
CD
ARG
433
46.193
49.307
59.779
1.00
29.04


ATOM
2955
NE
ARG
433
46.793
50.044
60.888
1.00
32.42


ATOM
2956
CZ
ARG
433
47.191
49.492
62.031
1.00
33.50


ATOM
2957
NH1
ARG
433
47.061
48.187
62.229
1.00
33.63


ATOM
2958
NH2
ARG
433
47.710
50.252
62.986
1.00
35.11


ATOM
2959
C
ARG
433
44.162
49.424
55.188
1.00
21.02


ATOM
2960
O
ARG
433
43.635
48.347
55.474
1.00
19.37


ATOM
2961
N
GLU
434
44.188
49.914
53.954
1.00
20.40


ATOM
2962
CA
GLU
434
43.644
49.196
52.803
1.00
21.33


ATOM
2963
CB
GLU
434
42.172
49.560
52.567
1.00
24.12


ATOM
2964
CG
GLU
434
41.226
49.009
53.624
1.00
34.46


ATOM
2965
CD
GLU
434
40.542
50.099
54.420
1.00
38.95


ATOM
2966
OE1
GLU
434
41.253
50.975
54.958
1.00
42.61


ATOM
2967
OE2
GLU
434
39.295
50.078
54.515
1.00
42.67


ATOM
2968
C
GLU
434
44.476
49.606
51.604
1.00
18.30


ATOM
2969
O
GLU
434
45.303
50.507
51.713
1.00
16.88


ATOM
2970
N
GLY
435
44.271
48.945
50.466
1.00
19.36


ATOM
2971
CA
GLY
435
45.031
49.296
49.276
1.00
18.55


ATOM
2972
C
GLY
435
44.491
50.578
48.679
1.00
18.67


ATOM
2973
O
GLY
435
43.400
51.005
49.055
1.00
17.09


ATOM
2974
N
ALA
436
45.246
51.204
47.775
1.00
19.08


ATOM
2975
CA
ALA
436
44.799
52.442
47.123
1.00
17.26


ATOM
2976
CB
ALA
436
45.667
52.731
45.906
1.00
17.85


ATOM
2977
C
ALA
436
43.336
52.215
46.722
1.00
16.59


ATOM
2978
O
ALA
436
42.493
53.097
46.842
1.00
16.06


ATOM
2979
N
ASN
437
43.066
51.020
46.212
1.00
16.87


ATOM
2980
CA
ASN
437
41.712
50.570
45.889
1.00
16.03


ATOM
2981
CB
ASN
437
41.185
51.088
44.526
1.00
14.52


ATOM
2982
CG
ASN
437
41.872
50.474
43.324
1.00
14.43


ATOM
2983
OD1
ASN
437
42.105
49.269
43.261
1.00
15.44


ATOM
2984
ND2
ASN
437
42.162
51.311
42.335
1.00
13.55


ATOM
2985
C
ASN
437
41.865
49.054
45.948
1.00
16.39


ATOM
2986
O
ASN
437
42.988
48.551
45.956
1.00
15.77


ATOM
2987
N
PRO
438
40.756
48.306
46.030
1.00
15.87


ATOM
2988
CD
PRO
438
39.350
48.730
46.157
1.00
14.94


ATOM
2989
CA
PRO
438
40.869
46.846
46.105
1.00
13.68


ATOM
2990
CB
PRO
438
39.413
46.391
46.059
1.00
14.60


ATOM
2991
CG
PRO
438
38.712
47.508
46.793
1.00
16.23


ATOM
2992
C
PRO
438
41.737
46.185
45.039
1.00
14.27


ATOM
2993
O
PRO
438
42.379
45.170
45.306
1.00
14.30


ATOM
2994
N
GLY
439
41.760
46.760
43.840
1.00
13.68


ATOM
2995
CA
GLY
439
42.563
46.201
42.766
1.00
13.77


ATOM
2996
C
GLY
439
44.051
46.182
43.070
1.00
14.65


ATOM
2997
O
GLY
439
44.741
45.203
42.776
1.00
12.71


ATOM
2998
N
PHE
440
44.553
47.269
43.649
1.00
14.29


ATOM
2999
CA
PHE
440
45.968
47.364
44.006
1.00
14.09


ATOM
3000
CB
PHE
440
46.262
48.708
44.691
1.00
14.69


ATOM
3001
CG
PHE
440
46.467
49.856
43.736
1.00
17.06


ATOM
3002
CD1
PHE
440
45.474
50.226
42.836
1.00
16.87


ATOM
3003
CD2
PHE
440
47.658
50.580
43.753
1.00
16.76


ATOM
3004
CE1
PHE
440
45.663
51.307
41.962
1.00
16.34


ATOM
3005
CE2
PHE
440
47.856
51.655
42.890
1.00
16.34


ATOM
3006
CZ
PHE
440
46.857
52.019
41.993
1.00
16.50


ATOM
3007
C
PHE
440
46.369
46.235
44.954
1.00
13.76


ATOM
3008
O
PHE
440
47.432
45.629
44.807
1.00
12.46


ATOM
3009
N
HIS
441
45.521
45.962
45.940
1.00
14.94


ATOM
3010
CA
HIS
441
45.813
44.911
46.910
1.00
15.78


ATOM
3011
CB
HIS
441
44.703
44.833
47.964
1.00
17.07


ATOM
3012
CG
HIS
441
45.209
44.750
49.374
1.00
15.66


ATOM
3013
CD2
HIS
441
44.960
45.526
50.456
1.00
15.15


ATOM
3014
ND1
HIS
441
46.073
43.763
49.802
1.00
16.88


ATOM
3015
CE1
HIS
441
46.332
43.935
51.087
1.00
14.94


ATOM
3016
NE2
HIS
441
45.669
44.998
51.508
1.00
15.07


ATOM
3017
C
HIS
441
45.958
43.555
46.220
1.00
16.92


ATOM
3018
O
HIS
441
46.813
42.747
46.592
1.00
15.31


ATOM
3019
N
GLU
442
45.122
43.311
45.214
1.00
16.74


ATOM
3020
CA
GLU
442
45.162
42.049
44.482
1.00
15.92


ATOM
3021
CB
GLU
442
43.861
41.851
43.701
1.00
15.02


ATOM
3022
CG
GLU
442
42.590
41.822
44.542
1.00
11.10


ATOM
3023
CD
GLU
442
42.635
40.757
45.617
1.00
11.15


ATOM
3024
OE1
GLU
442
43.250
39.697
45.371
1.00
14.00


ATOM
3025
OE2
GLU
442
42.055
40.975
46.699
1.00
11.81


ATOM
3026
C
GLU
442
46.329
41.955
43.497
1.00
17.24


ATOM
3027
O
GLU
442
46.778
40.859
43.162
1.00
16.84


ATOM
3028
N
ALA
443
46.826
43.100
43.039
1.00
15.95


ATOM
3029
CA
ALA
443
47.894
43.114
42.041
1.00
17.36


ATOM
3030
CB
ALA
443
47.799
44.404
41.221
1.00
15.87


ATOM
3031
C
ALA
443
49.343
42.907
42.491
1.00
16.95


ATOM
3032
O
ALA
443
50.135
42.328
41.750
1.00
17.94


ATOM
3033
N
ILE
444
49.692
43.374
43.686
1.00
16.73


ATOM
3034
CA
ILE
444
51.070
43.264
44.176
1.00
15.92


ATOM
3035
CB
ILE
444
51.166
43.630
45.671
1.00
15.04


ATOM
3036
CG2
ILE
444
52.631
43.664
46.095
1.00
16.89


ATOM
3037
CG1
ILE
444
50.502
44.990
45.927
1.00
14.90


ATOM
3038
CD1
ILE
444
51.112
46.139
45.153
1.00
15.89


ATOM
3039
C
ILE
444
51.744
41.902
43.980
1.00
16.43


ATOM
3040
O
ILE
444
52.792
41.807
43.332
1.00
15.13


ATOM
3041
N
GLY
445
51.155
40.858
44.554
1.00
15.53


ATOM
3042
CA
GLY
445
51.724
39.528
44.427
1.00
16.88


ATOM
3043
C
GLY
445
51.844
39.072
42.985
1.00
18.50


ATOM
3044
O
GLY
445
52.866
38.512
42.581
1.00
17.19


ATOM
3045
N
ASP
446
50.796
39.317
42.205
1.00
16.96


ATOM
3046
CA
ASP
446
50.775
38.935
40.795
1.00
17.24


ATOM
3047
CB
ASP
446
49.438
39.334
40.157
1.00
15.35


ATOM
3048
CG
ASP
446
48.291
38.426
40.579
1.00
17.38


ATOM
3049
OD1
ASP
446
48.298
37.936
41.728
1.00
14.96


ATOM
3050
OD2
ASP
446
47.370
38.212
39.761
1.00
16.72


ATOM
3051
C
ASP
446
51.919
39.572
40.016
1.00
18.31


ATOM
3052
O
ASP
446
52.503
38.939
39.132
1.00
16.77


ATOM
3053
N
VAL
447
52.234
40.829
40.328
1.00
18.18


ATOM
3054
CA
VAL
447
53.314
41.508
39.629
1.00
18.02


ATOM
3055
CB
VAL
447
53.542
42.935
40.158
1.00
17.59


ATOM
3056
CG1
VAL
447
54.795
43.520
39.514
1.00
20.25


ATOM
3057
CG2
VAL
447
52.330
43.816
39.831
1.00
15.79


ATOM
3058
C
VAL
447
54.611
40.716
39.765
1.00
18.36


ATOM
3059
O
VAL
447
55.293
40.471
38.773
1.00
17.66


ATOM
3060
N
LEU
448
54.948
40.312
40.986
1.00
18.09


ATOM
3061
CA
LEU
448
56.167
39.543
41.194
1.00
18.49


ATOM
3062
CB
LEU
448
56.464
39.378
42.691
1.00
17.75


ATOM
3063
CG
LEU
448
57.233
40.500
43.405
1.00
18.33


ATOM
3064
CD1
LEU
448
56.458
41.811
43.359
1.00
17.13


ATOM
3065
CD2
LEU
448
57.487
40.082
44.848
1.00
18.72


ATOM
3066
C
LEU
448
56.053
38.170
40.529
1.00
19.50


ATOM
3067
O
LEU
448
57.011
37.682
39.930
1.00
20.72


ATOM
3068
N
ALA
449
54.879
37.551
40.627
1.00
18.48


ATOM
3069
CA
ALA
449
54.671
36.240
40.028
1.00
18.81


ATOM
3070
CB
ALA
449
53.260
35.731
40.337
1.00
18.00


ATOM
3071
C
ALA
449
54.905
36.272
38.518
1.00
17.58


ATOM
3072
O
ALA
449
55.285
35.261
37.925
1.00
17.76


ATOM
3073
N
LEU
450
54.677
37.424
37.890
1.00
16.49


ATOM
3074
CA
LEU
450
54.898
37.536
36.449
1.00
16.51


ATOM
3075
CB
LEU
450
54.516
38.933
35.935
1.00
15.69


ATOM
3076
CG
LEU
450
53.027
39.294
35.797
1.00
14.12


ATOM
3077
CD1
LEU
450
52.887
40.749
35.374
1.00
12.95


ATOM
3078
CD2
LEU
450
52.356
38.385
34.770
1.00
15.02


ATOM
3079
C
LEU
450
56.376
37.262
36.150
1.00
18.30


ATOM
3080
O
LEU
450
56.702
36.552
35.196
1.00
17.45


ATOM
3081
N
SER
451
57.266
37.824
36.966
1.00
18.19


ATOM
3082
CA
SER
451
58.701
37.617
36.777
1.00
18.99


ATOM
3083
CB
SER
451
59.507
38.572
37.663
1.00
16.95


ATOM
3084
OG
SER
451
59.480
39.890
37.141
1.00
17.53


ATOM
3085
C
SER
451
59.092
36.178
37.092
1.00
19.71


ATOM
3086
O
SER
451
59.896
35.575
36.383
1.00
20.72


ATOM
3087
N
VAL
452
58.520
35.635
38.160
1.00
21.54


ATOM
3088
CA
VAL
452
58.798
34.263
38.574
1.00
22.76


ATOM
3089
CB
VAL
452
57.997
33.893
39.843
1.00
22.77


ATOM
3090
CG1
VAL
452
58.217
32.428
40.195
1.00
25.58


ATOM
3091
CG2
VAL
452
58.419
34.781
40.997
1.00
25.93


ATOM
3092
C
VAL
452
58.435
33.259
37.482
1.00
24.01


ATOM
3093
O
VAL
452
59.112
32.243
37.307
1.00
23.13


ATOM
3094
N
SER
453
57.358
33.552
36.757
1.00
22.60


ATOM
3095
CA
SER
453
56.870
32.678
35.693
1.00
23.40


ATOM
3096
CB
SER
453
55.434
33.067
35.317
1.00
21.89


ATOM
3097
OG
SER
453
54.546
32.810
36.393
1.00
20.22


ATOM
3098
C
SER
453
57.715
32.622
34.424
1.00
22.87


ATOM
3099
O
SER
453
57.563
31.697
33.631
1.00
22.16


ATOM
3100
N
THR
454
58.592
33.602
34.219
1.00
23.18


ATOM
3101
CA
THR
454
59.420
33.601
33.016
1.00
24.33


ATOM
3102
CB
THR
454
60.373
34.817
32.972
1.00
23.24


ATOM
3103
OG1
THR
454
61.199
34.827
34.143
1.00
24.32


ATOM
3104
CG2
THR
454
59.576
36.115
32.894
1.00
24.49


ATOM
3105
C
THR
454
60.240
32.313
32.940
1.00
25.55


ATOM
3106
O
THR
454
60.749
31.827
33.949
1.00
25.28


ATOM
3107
N
PRO
455
60.368
31.738
31.734
1.00
25.92


ATOM
3108
CD
PRO
455
59.860
32.211
30.433
1.00
26.48


ATOM
3109
CA
PRO
455
61.134
30.499
31.574
1.00
27.37


ATOM
3110
CB
PRO
455
61.238
30.351
30.058
1.00
27.14


ATOM
3111
CG
PRO
455
59.949
30.959
29.578
1.00
25.75


ATOM
3112
C
PRO
455
62.499
30.573
32.245
1.00
27.20


ATOM
3113
O
PRO
455
62.909
29.646
32.946
1.00
26.66


ATOM
3114
N
LYS
456
63.193
31.688
32.045
1.00
28.50


ATOM
3115
CA
LYS
456
64.513
31.851
32.626
1.00
29.18


ATOM
3116
CB
LYS
456
65.150
33.161
32.164
1.00
31.89


ATOM
3117
CG
LYS
456
66.669
33.142
32.280
1.00
36.40


ATOM
3118
CD
LYS
456
67.296
34.487
31.959
1.00
39.36


ATOM
3119
CE
LYS
456
68.815
34.374
31.932
1.00
40.98


ATOM
3120
NZ
LYS
456
69.335
33.657
33.129
1.00
43.02


ATOM
3121
C
LYS
456
64.501
31.795
34.151
1.00
29.42


ATOM
3122
O
LYS
456
65.366
31.151
34.753
1.00
28.75


ATOM
3123
N
HIS
457
63.534
32.458
34.785
1.00
24.85


ATOM
3124
CA
HIS
457
63.486
32.427
36.242
1.00
23.20


ATOM
3125
CB
HIS
457
62.439
33.397
36.791
1.00
23.95


ATOM
3126
CG
HIS
457
62.503
33.558
38.278
1.00
23.17


ATOM
3127
CD2
HIS
457
61.930
32.846
39.277
1.00
23.50


ATOM
3128
ND1
HIS
457
63.300
34.501
38.892
1.00
24.07


ATOM
3129
CE1
HIS
457
63.218
34.360
40.203
1.00
25.29


ATOM
3130
NE2
HIS
457
62.393
33.361
40.463
1.00
25.90


ATOM
3131
C
HIS
457
63.167
31.019
36.738
1.00
23.20


ATOM
3132
O
HIS
457
63.768
30.541
37.701
1.00
21.36


ATOM
3133
N
LEU
458
62.208
30.362
36.089
1.00
24.06


ATOM
3134
CA
LEU
458
61.835
29.010
36.481
1.00
25.22


ATOM
3135
CB
LEU
458
60.694
28.486
35.600
1.00
25.32


ATOM
3136
CG
LEU
458
59.302
29.096
35.812
1.00
24.79


ATOM
3137
CD1
LEU
458
58.314
28.482
34.827
1.00
24.94


ATOM
3138
CD2
LEU
458
58.848
28.852
37.249
1.00
24.07


ATOM
3139
C
LEU
458
63.058
28.105
36.350
1.00
26.11


ATOM
3140
O
LEU
458
63.265
27.204
37.157
1.00
24.93


ATOM
3141
N
HIS
459
63.875
28.356
35.334
1.00
28.43


ATOM
3142
CA
HIS
459
65.070
27.548
35.140
1.00
31.28


ATOM
3143
CB
HIS
459
65.731
27.872
33.799
1.00
33.71


ATOM
3144
CG
HIS
459
66.959
27.060
33.521
1.00
39.54


ATOM
3145
CD2
HIS
459
67.152
25.977
32.730
1.00
40.92


ATOM
3146
ND1
HIS
459
68.174
27.316
34.120
1.00
42.70


ATOM
3147
CE1
HIS
459
69.062
26.427
33.711
1.00
42.68


ATOM
3148
NE2
HIS
459
68.467
25.603
32.867
1.00
43.45


ATOM
3149
C
HIS
459
66.053
27.782
36.283
1.00
30.04


ATOM
3150
O
HIS
459
66.755
26.861
36.699
1.00
29.57


ATOM
3151
N
SER
460
66.087
29.008
36.803
1.00
28.70


ATOM
3152
CA
SER
460
66.997
29.335
37.897
1.00
27.62


ATOM
3153
CB
SER
460
67.034
30.850
38.142
1.00
27.69


ATOM
3154
OG
SER
460
65.945
31.283
38.942
1.00
27.73


ATOM
3155
C
SER
460
66.579
28.613
39.174
1.00
27.55


ATOM
3156
O
SER
460
67.380
28.446
40.091
1.00
26.24


ATOM
3157
N
LEU
461
65.321
28.186
39.228
1.00
26.91


ATOM
3158
CA
LEU
461
64.808
27.463
40.388
1.00
29.43


ATOM
3159
CB
LEU
461
63.337
27.813
40.641
1.00
27.64


ATOM
3160
CG
LEU
461
63.027
29.239
41.101
1.00
28.24


ATOM
3161
CD1
LEU
461
61.523
29.462
41.111
1.00
28.05


ATOM
3162
CD2
LEU
461
63.611
29.461
42.488
1.00
27.97


ATOM
3163
C
LEU
461
64.931
25.971
40.119
1.00
30.51


ATOM
3164
O
LEU
461
64.528
25.142
40.938
1.00
31.19


ATOM
3165
N
ASN
462
65.491
25.649
38.957
1.00
32.47


ATOM
3166
CA
ASN
462
65.684
24.272
38.523
1.00
34.80


ATOM
3167
CB
ASN
462
66.447
23.484
39.594
1.00
35.75


ATOM
3168
CG
ASN
462
67.114
22.241
39.036
1.00
38.55


ATOM
3169
OD1
ASN
462
67.732
22.283
37.973
1.00
38.16


ATOM
3170
ND2
ASN
462
67.006
21.132
39.758
1.00
39.43


ATOM
3171
C
ASN
462
64.337
23.607
38.222
1.00
36.15


ATOM
3172
O
ASN
462
64.154
22.414
38.466
1.00
35.72


ATOM
3173
N
LEU
463
63.402
24.391
37.689
1.00
36.82


ATOM
3174
CA
LEU
463
62.074
23.886
37.345
1.00
39.43


ATOM
3175
CB
LEU
463
60.987
24.713
38.038
1.00
37.66


ATOM
3176
CG
LEU
463
60.997
24.667
39.569
1.00
37.31


ATOM
3177
CD1
LEU
463
59.836
25.492
40.111
1.00
36.51


ATOM
3178
CD2
LEU
463
60.898
23.227
40.046
1.00
36.47


ATOM
3179
C
LEU
463
61.851
23.900
35.839
1.00
41.12


ATOM
3180
O
LEU
463
60.771
23.568
35.355
1.00
42.26


ATOM
3181
N
LEU
464
62.880
24.307
35.105
1.00
43.53


ATOM
3182
CA
LEU
464
62.832
24.341
33.647
1.00
46.78


ATOM
3183
CB
LEU
464
62.358
25.707
33.131
1.00
47.15


ATOM
3184
CG
LEU
464
60.846
25.963
33.126
1.00
47.86


ATOM
3185
CD1
LEU
464
60.553
27.253
32.374
1.00
48.43


ATOM
3186
CD2
LEU
464
60.122
24.801
32.457
1.00
48.04


ATOM
3187
C
LEU
464
64.217
24.032
33.097
1.00
47.91


ATOM
3188
O
LEU
464
65.208
24.081
33.830
1.00
48.74


ATOM
3189
N
SER
465
64.282
23.702
31.812
1.00
49.72


ATOM
3190
CA
SER
465
65.552
23.375
31.173
1.00
51.10


ATOM
3191
CB
SER
465
65.619
21.873
30.887
1.00
51.49


ATOM
3192
OG
SER
465
64.505
21.452
30.117
1.00
52.92


ATOM
3193
C
SER
465
65.745
24.157
29.879
1.00
51.56


ATOM
3194
O
SER
465
66.428
25.182
29.860
1.00
52.18


ATOM
3195
N
GLY
470
64.653
32.326
21.785
1.00
48.10


ATOM
3196
CA
GLY
470
63.950
31.478
20.839
1.00
48.51


ATOM
3197
C
GLY
470
62.522
31.928
20.591
1.00
47.84


ATOM
3198
O
GLY
470
61.718
31.998
21.520
1.00
48.31


ATOM
3199
N
ALA
471
62.202
32.229
19.336
1.00
46.54


ATOM
3200
CA
ALA
471
60.864
32.681
18.976
1.00
45.12


ATOM
3201
CB
ALA
471
60.799
32.979
17.485
1.00
46.24


ATOM
3202
C
ALA
471
59.799
31.654
19.351
1.00
44.20


ATOM
3203
O
ALA
471
58.843
31.976
20.056
1.00
44.05


ATOM
3204
N
GLU
472
59.965
30.420
18.883
1.00
41.85


ATOM
3205
CA
GLU
472
59.002
29.367
19.178
1.00
40.72


ATOM
3206
CB
GLU
472
59.411
28.062
18.492
1.00
40.77


ATOM
3207
CG
GLU
472
59.039
28.041
17.019
1.00
43.32


ATOM
3208
CD
GLU
472
59.363
26.728
16.336
1.00
44.64


ATOM
3209
OE1
GLU
472
59.319
25.675
17.008
1.00
44.66


ATOM
3210
OE2
GLU
472
59.641
26.753
15.117
1.00
46.17


ATOM
3211
C
GLU
472
58.810
29.146
20.672
1.00
39.99


ATOM
3212
O
GLU
472
57.724
28.762
21.111
1.00
37.39


ATOM
3213
N
HIS
473
59.859
29.380
21.454
1.00
39.00


ATOM
3214
CA
HIS
473
59.746
29.226
22.896
1.00
38.09


ATOM
3215
CB
HIS
473
61.121
29.080
23.551
1.00
40.74


ATOM
3216
CG
HIS
473
61.664
27.684
23.510
1.00
43.40


ATOM
3217
CD2
HIS
473
61.475
26.632
24.341
1.00
44.06


ATOM
3218
ND1
HIS
473
62.501
27.236
22.510
1.00
45.60


ATOM
3219
CE1
HIS
473
62.805
25.969
22.729
1.00
45.16


ATOM
3220
NE2
HIS
473
62.195
25.578
23.833
1.00
45.60


ATOM
3221
C
HIS
473
59.032
30.449
23.453
1.00
36.31


ATOM
3222
O
HIS
473
58.367
30.368
24.482
1.00
36.98


ATOM
3223
N
ASP
474
59.172
31.581
22.766
1.00
34.37


ATOM
3224
CA
ASP
474
58.516
32.810
23.187
1.00
34.17


ATOM
3225
CB
ASP
474
59.000
34.009
22.365
1.00
38.03


ATOM
3226
CG
ASP
474
60.243
34.647
22.937
1.00
41.09


ATOM
3227
OD1
ASP
474
60.257
34.930
24.154
1.00
42.53


ATOM
3228
OD2
ASP
474
61.202
34.878
22.169
1.00
43.99


ATOM
3229
C
ASP
474
57.007
32.692
23.021
1.00
32.16


ATOM
3230
O
ASP
474
56.248
33.095
23.903
1.00
30.43


ATOM
3231
N
ILE
475
56.580
32.153
21.880
1.00
28.89


ATOM
3232
CA
ILE
475
55.159
31.996
21.595
1.00
25.76


ATOM
3233
CB
ILE
475
54.922
31.577
20.122
1.00
26.10


ATOM
3234
CG2
ILE
475
53.425
31.456
19.838
1.00
22.06


ATOM
3235
CG1
ILE
475
55.544
32.613
19.183
1.00
23.79


ATOM
3236
CD1
ILE
475
54.998
34.015
19.363
1.00
25.45


ATOM
3237
C
ILE
475
54.539
30.962
22.526
1.00
24.56


ATOM
3238
O
ILE
475
53.422
31.150
23.009
1.00
23.51


ATOM
3239
N
ASN
476
55.258
29.869
22.775
1.00
22.07


ATOM
3240
CA
ASN
476
54.749
28.843
23.673
1.00
22.59


ATOM
3241
CB
ASN
476
55.718
27.658
23.777
1.00
22.82


ATOM
3242
CG
ASN
476
55.557
26.656
22.640
1.00
23.84


ATOM
3243
OD1
ASN
476
54.640
26.756
21.822
1.00
23.67


ATOM
3244
ND2
ASN
476
56.451
25.674
22.595
1.00
22.00


ATOM
3245
C
ASN
476
54.564
29.465
25.057
1.00
22.14


ATOM
3246
O
ASN
476
53.554
29.231
25.721
1.00
20.32


ATOM
3247
N
PHE
477
55.544
30.258
25.487
1.00
19.74


ATOM
3248
CA
PHE
477
55.473
30.907
26.795
1.00
20.07


ATOM
3249
CB
PHE
477
56.779
31.630
27.118
1.00
19.28


ATOM
3250
CG
PHE
477
56.697
32.491
28.348
1.00
19.26


ATOM
3251
CD1
PHE
477
56.387
31.930
29.582
1.00
19.77


ATOM
3252
CD2
PHE
477
56.908
33.861
28.270
1.00
18.99


ATOM
3253
CE1
PHE
477
56.288
32.721
30.723
1.00
20.49


ATOM
3254
CE2
PHE
477
56.811
34.664
29.404
1.00
21.68


ATOM
3255
CZ
PHE
477
56.501
34.091
30.634
1.00
20.79


ATOM
3256
C
PHE
477
54.327
31.910
26.879
1.00
18.41


ATOM
3257
O
PHE
477
53.558
31.907
27.840
1.00
17.57


ATOM
3258
N
LEU
478
54.230
32.782
25.882
1.00
16.70


ATOM
3259
CA
LEU
478
53.171
33.778
25.858
1.00
17.73


ATOM
3260
CB
LEU
478
53.315
34.692
24.634
1.00
18.54


ATOM
3261
CG
LEU
478
54.441
35.733
24.725
1.00
18.88


ATOM
3262
CD1
LEU
478
54.594
36.453
23.399
1.00
20.51


ATOM
3263
CD2
LEU
478
54.133
36.732
25.835
1.00
21.13


ATOM
3264
C
LEU
478
51.808
33.094
25.857
1.00
17.77


ATOM
3265
O
LEU
478
50.859
33.602
26.454
1.00
16.81


ATOM
3266
N
MET
479
51.710
31.943
25.192
1.00
16.85


ATOM
3267
CA
MET
479
50.447
31.207
25.155
1.00
16.42


ATOM
3268
CB
MET
479
50.523
30.020
24.187
1.00
16.54


ATOM
3269
CG
MET
479
49.265
29.145
24.170
1.00
15.90


ATOM
3270
SD
MET
479
47.741
30.068
23.800
1.00
20.51


ATOM
3271
CE
MET
479
47.978
30.453
22.101
1.00
14.74


ATOM
3272
C
MET
479
50.112
30.697
26.552
1.00
18.16


ATOM
3273
O
MET
479
48.965
30.772
26.987
1.00
16.49


ATOM
3274
N
LYS
480
51.108
30.169
27.257
1.00
17.20


ATOM
3275
CA
LYS
480
50.852
29.673
28.600
1.00
19.57


ATOM
3276
CB
LYS
480
52.117
29.038
29.191
1.00
22.36


ATOM
3277
CG
LYS
480
51.837
28.140
30.387
1.00
27.80


ATOM
3278
CD
LYS
480
53.012
27.221
30.741
1.00
33.74


ATOM
3279
CE
LYS
480
54.250
28.002
31.184
1.00
37.33


ATOM
3280
NZ
LYS
480
55.332
27.126
31.746
1.00
39.64


ATOM
3281
C
LYS
480
50.368
30.835
29.478
1.00
17.85


ATOM
3282
O
LYS
480
49.420
30.689
30.247
1.00
18.61


ATOM
3283
N
MET
481
51.006
31.992
29.343
1.00
15.91


ATOM
3284
CA
MET
481
50.619
33.165
30.123
1.00
16.21


ATOM
3285
CB
MET
481
51.627
34.302
29.925
1.00
15.78


ATOM
3286
CG
MET
481
53.019
34.045
30.504
1.00
17.36


ATOM
3287
SD
MET
481
53.024
33.719
32.288
1.00
23.53


ATOM
3288
CE
MET
481
52.210
35.205
32.913
1.00
14.65


ATOM
3289
C
MET
481
49.224
33.662
29.740
1.00
14.73


ATOM
3290
O
MET
481
48.430
34.029
30.605
1.00
15.28


ATOM
3291
N
ALA
482
48.930
33.672
28.444
1.00
12.83


ATOM
3292
CA
ALA
482
47.635
34.144
27.966
1.00
14.42


ATOM
3293
CB
ALA
482
47.640
34.229
26.440
1.00
12.60


ATOM
3294
C
ALA
482
46.485
33.254
28.432
1.00
13.98


ATOM
3295
O
ALA
482
45.404
33.737
28.742
1.00
12.54


ATOM
3296
N
LEU
483
46.721
31.950
28.469
1.00
12.96


ATOM
3297
CA
LEU
483
45.687
31.019
28.889
1.00
15.49


ATOM
3298
CB
LEU
483
46.221
29.581
28.845
1.00
13.86


ATOM
3299
CG
LEU
483
46.433
29.004
27.438
1.00
12.19


ATOM
3300
CD1
LEU
483
47.119
27.645
27.522
1.00
12.00


ATOM
3301
CD2
LEU
483
45.099
28.868
26.744
1.00
11.05


ATOM
3302
C
LEU
483
45.172
31.377
30.286
1.00
15.60


ATOM
3303
O
LEU
483
44.029
31.076
30.633
1.00
13.79


ATOM
3304
N
ASP
484
46.011
32.026
31.088
1.00
17.99


ATOM
3305
CA
ASP
484
45.579
32.432
32.421
1.00
19.85


ATOM
3306
CB
ASP
484
46.675
32.186
33.457
1.00
23.35


ATOM
3307
CG
ASP
484
46.697
30.752
33.950
1.00
31.47


ATOM
3308
OD1
ASP
484
45.708
30.017
33.703
1.00
32.89


ATOM
3309
OD2
ASP
484
47.692
30.358
34.590
1.00
35.68


ATOM
3310
C
ASP
484
45.159
33.900
32.469
1.00
19.15


ATOM
3311
O
ASP
484
44.016
34.205
32.801
1.00
19.40


ATOM
3312
N
LYS
485
46.074
34.797
32.106
1.00
15.90


ATOM
3313
CA
LYS
485
45.809
36.233
32.153
1.00
15.26


ATOM
3314
CB
LYS
485
47.115
37.013
31.937
1.00
16.44


ATOM
3315
CG
LYS
485
48.221
36.683
32.935
1.00
17.03


ATOM
3316
CD
LYS
485
47.780
36.925
34.376
1.00
16.07


ATOM
3317
CE
LYS
485
48.914
36.634
35.355
1.00
16.43


ATOM
3318
NZ
LYS
485
48.526
36.873
36.774
1.00
15.12


ATOM
3319
C
LYS
485
44.743
36.792
31.207
1.00
15.09


ATOM
3320
O
LYS
485
43.963
37.655
31.608
1.00
14.86


ATOM
3321
N
ILE
486
44.720
36.338
29.954
1.00
12.89


ATOM
3322
CA
ILE
486
43.738
36.845
28.997
1.00
12.96


ATOM
3323
CB
ILE
486
44.206
36.634
27.534
1.00
12.31


ATOM
3324
CG2
ILE
486
43.111
37.083
26.564
1.00
11.47


ATOM
3325
CG1
ILE
486
45.492
37.431
27.269
1.00
14.69


ATOM
3326
CD1
ILE
486
45.378
38.921
27.561
1.00
14.14


ATOM
3327
C
ILE
486
42.370
36.185
29.177
1.00
13.40


ATOM
3328
O
ILE
486
41.339
36.856
29.155
1.00
13.09


ATOM
3329
N
ALA
487
42.363
34.868
29.343
1.00
13.68


ATOM
3330
CA
ALA
487
41.108
34.143
29.523
1.00
13.77


ATOM
3331
CB
ALA
487
41.381
32.640
29.672
1.00
13.45


ATOM
3332
C
ALA
487
40.356
34.655
30.746
1.00
12.99


ATOM
3333
O
ALA
487
39.130
34.653
30.773
1.00
14.04


ATOM
3334
N
PHE
488
41.095
35.111
31.750
1.00
11.52


ATOM
3335
CA
PHE
488
40.488
35.595
32.984
1.00
12.47


ATOM
3336
CB
PHE
488
41.548
35.663
34.079
1.00
10.72


ATOM
3337
CG
PHE
488
41.002
35.979
35.445
1.00
13.51


ATOM
3338
CD1
PHE
488
40.295
35.019
36.172
1.00
11.90


ATOM
3339
CD2
PHE
488
41.245
37.216
36.031
1.00
12.70


ATOM
3340
CE1
PHE
488
39.850
35.286
37.467
1.00
12.84


ATOM
3341
CE2
PHE
488
40.803
37.492
37.324
1.00
12.47


ATOM
3342
CZ
PHE
488
40.106
36.524
38.043
1.00
11.48


ATOM
3343
C
PHE
488
39.806
36.957
32.858
1.00
12.87


ATOM
3344
O
PHE
488
38.944
37.290
33.669
1.00
14.49


ATOM
3345
N
ILE
489
40.190
37.738
31.851
1.00
13.59


ATOM
3346
CA
ILE
489
39.616
39.064
31.661
1.00
12.89


ATOM
3347
CB
ILE
489
40.200
39.758
30.404
1.00
14.05


ATOM
3348
CG2
ILE
489
39.399
41.024
30.076
1.00
11.51


ATOM
3349
CG1
ILE
489
41.677
40.100
30.636
1.00
15.42


ATOM
3350
CD1
ILE
489
41.931
41.022
31.840
1.00
16.62


ATOM
3351
C
ILE
489
38.083
39.080
31.581
1.00
14.01


ATOM
3352
O
ILE
489
37.433
39.771
32.361
1.00
13.07


ATOM
3353
N
PRO
490
37.486
38.340
30.630
1.00
11.60


ATOM
3354
CD
PRO
490
38.036
37.616
29.470
1.00
12.38


ATOM
3355
CA
PRO
490
36.022
38.377
30.580
1.00
12.27


ATOM
3356
CB
PRO
490
35.694
37.643
29.276
1.00
12.12


ATOM
3357
CG
PRO
490
36.876
36.749
29.062
1.00
14.13


ATOM
3358
C
PRO
490
35.339
37.767
31.802
1.00
11.71


ATOM
3359
O
PRO
490
34.267
38.218
32.202
1.00
11.51


ATOM
3360
N
PHE
491
35.950
36.747
32.401
1.00
10.88


ATOM
3361
CA
PHE
491
35.346
36.126
33.581
1.00
10.74


ATOM
3362
CB
PHE
491
36.113
34.871
34.017
1.00
9.32


ATOM
3363
CG
PHE
491
35.556
34.230
35.269
1.00
9.41


ATOM
3364
CD1
PHE
491
34.443
33.396
35.206
1.00
10.06


ATOM
3365
CD2
PHE
491
36.121
34.492
36.511
1.00
9.76


ATOM
3366
CE1
PHE
491
33.901
32.834
36.365
1.00
12.14


ATOM
3367
CE2
PHE
491
35.589
33.937
37.679
1.00
11.37


ATOM
3368
CZ
PHE
491
34.476
33.104
37.606
1.00
11.49


ATOM
3369
C
PHE
491
35.337
37.110
34.745
1.00
10.49


ATOM
3370
O
PHE
491
34.308
37.310
35.390
1.00
11.46


ATOM
3371
N
SER
492
36.482
37.732
35.005
1.00
10.88


ATOM
3372
CA
SER
492
36.584
38.673
36.117
1.00
12.32


ATOM
3373
CB
SER
492
38.031
39.125
36.308
1.00
11.29


ATOM
3374
OG
SER
492
38.510
39.836
35.181
1.00
11.99


ATOM
3375
C
SER
492
35.679
39.888
35.940
1.00
13.79


ATOM
3376
O
SER
492
35.297
40.533
36.919
1.00
15.69


ATOM
3377
N
TYR
493
35.340
40.190
34.693
1.00
12.01


ATOM
3378
CA
TYR
493
34.468
41.320
34.374
1.00
12.81


ATOM
3379
CB
TYR
493
34.633
41.700
32.897
1.00
14.65


ATOM
3380
CG
TYR
493
33.937
42.983
32.493
1.00
16.68


ATOM
3381
CD1
TYR
493
34.362
44.214
32.989
1.00
18.71


ATOM
3382
CE1
TYR
493
33.724
45.398
32.624
1.00
20.68


ATOM
3383
CD2
TYR
493
32.852
42.966
31.617
1.00
17.79


ATOM
3384
CE2
TYR
493
32.207
44.147
31.245
1.00
20.59


ATOM
3385
CZ
TYR
493
32.649
45.357
31.753
1.00
19.58


ATOM
3386
OH
TYR
493
32.014
46.526
31.400
1.00
18.46


ATOM
3387
C
TYR
493
33.010
40.948
34.621
1.00
13.40


ATOM
3388
O
TYR
493
32.227
41.727
35.162
1.00
13.85


ATOM
3389
N
LEU
494
32.666
39.733
34.217
1.00
12.33


ATOM
3390
CA
LEU
494
31.313
39.197
34.311
1.00
13.77


ATOM
3391
CB
LEU
494
31.293
37.864
33.551
1.00
16.44


ATOM
3392
CG
LEU
494
30.246
36.756
33.614
1.00
23.07


ATOM
3393
CD1
LEU
494
30.665
35.692
32.600
1.00
23.72


ATOM
3394
CD2
LEU
494
30.142
36.150
34.994
1.00
18.70


ATOM
3395
C
LEU
494
30.713
39.016
35.704
1.00
11.84


ATOM
3396
O
LEU
494
29.542
39.330
35.925
1.00
13.02


ATOM
3397
N
VAL
495
31.505
38.516
36.643
1.00
10.62


ATOM
3398
CA
VAL
495
30.990
38.236
37.979
1.00
11.98


ATOM
3399
CB
VAL
495
32.112
37.768
38.922
1.00
11.36


ATOM
3400
CG1
VAL
495
31.552
37.498
40.309
1.00
9.21


ATOM
3401
CG2
VAL
495
32.751
36.504
38.362
1.00
13.56


ATOM
3402
C
VAL
495
30.207
39.360
38.642
1.00
12.05


ATOM
3403
O
VAL
495
29.064
39.150
39.050
1.00
8.92


ATOM
3404
N
ASP
496
30.802
40.543
38.760
1.00
11.08


ATOM
3405
CA
ASP
496
30.086
41.641
39.391
1.00
11.99


ATOM
3406
CB
ASP
496
31.056
42.624
40.061
1.00
11.20


ATOM
3407
CG
ASP
496
31.579
42.096
41.400
1.00
12.07


ATOM
3408
OD1
ASP
496
31.048
41.069
41.881
1.00
13.72


ATOM
3409
OD2
ASP
496
32.507
42.695
41.980
1.00
10.70


ATOM
3410
C
ASP
496
29.120
42.358
38.453
1.00
13.14


ATOM
3411
O
ASP
496
28.297
43.151
38.906
1.00
12.97


ATOM
3412
N
GLN
497
29.207
42.096
37.151
1.00
12.75


ATOM
3413
CA
GLN
497
28.234
42.711
36.255
1.00
12.19


ATOM
3414
CB
GLN
497
28.561
42.447
34.781
1.00
14.86


ATOM
3415
CG
GLN
497
29.789
43.181
34.232
1.00
15.25


ATOM
3416
CD
GLN
497
29.717
44.698
34.383
1.00
19.00


ATOM
3417
OE1
GLN
497
28.641
45.290
34.356
1.00
17.62


ATOM
3418
NE2
GLN
497
30.875
45.330
34.526
1.00
19.82


ATOM
3419
C
GLN
497
26.926
42.008
36.633
1.00
14.20


ATOM
3420
O
GLN
497
25.857
42.615
36.640
1.00
12.70


ATOM
3421
N
TRP
498
27.033
40.720
36.964
1.00
12.15


ATOM
3422
CA
TRP
498
25.876
39.927
37.371
1.00
13.21


ATOM
3423
CB
TRP
498
26.230
38.435
37.414
1.00
12.05


ATOM
3424
CG
TRP
498
25.081
37.551
37.820
1.00
12.38


ATOM
3425
CD2
TRP
498
24.828
37.025
39.124
1.00
11.96


ATOM
3426
CE2
TRP
498
23.647
36.251
39.043
1.00
14.37


ATOM
3427
CE3
TRP
498
25.487
37.129
40.357
1.00
12.53


ATOM
3428
CD1
TRP
498
24.068
37.091
37.018
1.00
13.82


ATOM
3429
NE1
TRP
498
23.204
36.309
37.747
1.00
13.23


ATOM
3430
CZ2
TRP
498
23.111
35.584
40.150
1.00
12.76


ATOM
3431
CZ3
TRP
498
24.953
36.463
41.458
1.00
14.42


ATOM
3432
CH2
TRP
498
23.777
35.702
41.345
1.00
12.98


ATOM
3433
C
TRP
498
25.388
40.363
38.757
1.00
12.74


ATOM
3434
O
TRP
498
24.202
40.609
38.945
1.00
12.76


ATOM
3435
N
ARG
499
26.297
40.458
39.726
1.00
14.02


ATOM
3436
CA
ARG
499
25.907
40.862
41.080
1.00
14.05


ATOM
3437
CB
ARG
499
27.069
40.693
42.066
1.00
13.99


ATOM
3438
CG
ARG
499
27.111
39.317
42.732
1.00
15.24


ATOM
3439
CD
ARG
499
28.018
39.283
43.967
1.00
14.11


ATOM
3440
NE
ARG
499
29.427
39.442
43.618
1.00
12.25


ATOM
3441
CZ
ARG
499
30.435
38.959
44.333
1.00
14.41


ATOM
3442
NH1
ARG
499
30.195
38.280
45.453
1.00
13.25


ATOM
3443
NH2
ARG
499
31.686
39.137
43.917
1.00
12.95


ATOM
3444
C
ARG
499
25.362
42.289
41.177
1.00
15.06


ATOM
3445
O
ARG
499
24.423
42.539
41.936
1.00
13.96


ATOM
3446
N
TRP
500
25.942
43.223
40.427
1.00
12.32


ATOM
3447
CA
TRP
500
25.454
44.600
40.469
1.00
14.74


ATOM
3448
CB
TRP
500
26.277
45.529
39.561
1.00
11.23


ATOM
3449
CG
TRP
500
27.692
45.753
39.989
1.00
12.02


ATOM
3450
CD2
TRP
500
28.757
46.277
39.181
1.00
11.01


ATOM
3451
CE2
TRP
500
29.916
46.302
39.984
1.00
10.87


ATOM
3452
CE3
TRP
500
28.841
46.728
37.855
1.00
13.39


ATOM
3453
CD1
TRP
500
28.233
45.495
41.214
1.00
10.03


ATOM
3454
NE1
TRP
500
29.567
45.819
41.218
1.00
10.74


ATOM
3455
CZ2
TRP
500
31.153
46.759
39.508
1.00
8.74


ATOM
3456
CZ3
TRP
500
30.073
47.186
37.378
1.00
11.68


ATOM
3457
CH2
TRP
500
31.210
47.195
38.205
1.00
11.27


ATOM
3458
C
TRP
500
23.997
44.651
40.015
1.00
15.43


ATOM
3459
O
TRP
500
23.213
45.457
40.513
1.00
14.95


ATOM
3460
N
ARG
501
23.643
43.799
39.056
1.00
15.05


ATOM
3461
CA
ARG
501
22.275
43.769
38.551
1.00
15.13


ATOM
3462
CB
ARG
501
22.249
43.170
37.142
1.00
17.81


ATOM
3463
CG
ARG
501
22.833
44.107
36.088
1.00
22.48


ATOM
3464
CD
ARG
501
22.988
43.403
34.751
1.00
29.90


ATOM
3465
NE
ARG
501
21.713
42.901
34.245
1.00
35.03


ATOM
3466
CZ
ARG
501
21.596
41.864
33.422
1.00
37.06


ATOM
3467
NH1
ARG
501
22.678
41.213
33.012
1.00
37.13


ATOM
3468
NH2
ARG
501
20.397
41.481
33.004
1.00
36.72


ATOM
3469
C
ARG
501
21.346
43.006
39.493
1.00
15.12


ATOM
3470
O
ARG
501
20.129
43.222
39.497
1.00
13.20


ATOM
3471
N
VAL
502
21.917
42.102
40.284
1.00
13.23


ATOM
3472
CA
VAL
502
21.126
41.367
41.262
1.00
14.21


ATOM
3473
CB
VAL
502
21.910
40.175
41.854
1.00
10.98


ATOM
3474
CG1
VAL
502
21.207
39.660
43.102
1.00
11.32


ATOM
3475
CG2
VAL
502
22.003
39.052
40.816
1.00
14.99


ATOM
3476
C
VAL
502
20.820
42.369
42.373
1.00
14.19


ATOM
3477
O
VAL
502
19.678
42.513
42.813
1.00
14.12


ATOM
3478
N
PHE
503
21.862
43.072
42.802
1.00
14.50


ATOM
3479
CA
PHE
503
21.749
44.070
43.856
1.00
15.39


ATOM
3480
CB
PHE
503
23.139
44.614
44.197
1.00
14.83


ATOM
3481
CG
PHE
503
23.999
43.647
44.971
1.00
14.46


ATOM
3482
CD1
PHE
503
25.383
43.722
44.901
1.00
14.93


ATOM
3483
CD2
PHE
503
23.422
42.677
45.793
1.00
16.22


ATOM
3484
CE1
PHE
503
26.186
42.848
45.640
1.00
14.36


ATOM
3485
CE2
PHE
503
24.218
41.797
46.537
1.00
12.05


ATOM
3486
CZ
PHE
503
25.598
41.886
46.459
1.00
15.10


ATOM
3487
C
PHE
503
20.802
45.221
43.509
1.00
15.02


ATOM
3488
O
PHE
503
20.022
45.650
44.359
1.00
14.79


ATOM
3489
N
ASP
504
20.853
45.722
42.274
1.00
14.97


ATOM
3490
CA
ASP
504
19.963
46.820
41.916
1.00
15.11


ATOM
3491
CB
ASP
504
20.575
47.716
40.819
1.00
15.57


ATOM
3492
CG
ASP
504
20.520
47.100
39.426
1.00
16.33


ATOM
3493
OD1
ASP
504
19.860
46.057
39.220
1.00
17.34


ATOM
3494
OD2
ASP
504
21.144
47.689
38.522
1.00
17.52


ATOM
3495
C
ASP
504
18.565
46.356
41.516
1.00
16.58


ATOM
3496
O
ASP
504
17.756
47.153
41.044
1.00
17.20


ATOM
3497
N
GLY
505
18.287
45.067
41.708
1.00
16.74


ATOM
3498
CA
GLY
505
16.971
44.527
41.400
1.00
17.30


ATOM
3499
C
GLY
505
16.636
44.167
39.961
1.00
17.93


ATOM
3500
O
GLY
505
15.520
43.732
39.693
1.00
18.99


ATOM
3501
N
SER
506
17.578
44.341
39.039
1.00
17.16


ATOM
3502
CA
SER
506
17.350
44.013
37.630
1.00
18.82


ATOM
3503
CB
SER
506
18.514
44.514
36.771
1.00
19.99


ATOM
3504
OG
SER
506
18.605
45.920
36.805
1.00
25.35


ATOM
3505
C
SER
506
17.185
42.509
37.401
1.00
18.71


ATOM
3506
O
SER
506
16.500
42.089
36.470
1.00
19.68


ATOM
3507
N
ILE
507
17.837
41.709
38.241
1.00
17.20


ATOM
3508
CA
ILE
507
17.767
40.253
38.147
1.00
17.19


ATOM
3509
CB
ILE
507
19.184
39.630
38.004
1.00
16.86


ATOM
3510
CG2
ILE
507
19.076
38.112
37.912
1.00
15.71


ATOM
3511
CG1
ILE
507
19.890
40.193
36.767
1.00
17.34


ATOM
3512
CD1
ILE
507
21.357
39.746
36.640
1.00
15.06


ATOM
3513
C
ILE
507
17.123
39.695
39.420
1.00
17.07


ATOM
3514
O
ILE
507
17.689
39.807
40.509
1.00
16.98


ATOM
3515
N
THR
508
15.940
39.105
39.281
1.00
17.01


ATOM
3516
CA
THR
508
15.227
38.531
40.421
1.00
18.33


ATOM
3517
CB
THR
508
13.710
38.551
40.196
1.00
18.44


ATOM
3518
OG1
THR
508
13.365
37.586
39.191
1.00
20.70


ATOM
3519
CG2
THR
508
13.263
39.931
39.734
1.00
20.95


ATOM
3520
C
THR
508
15.671
37.088
40.581
1.00
18.12


ATOM
3521
O
THR
508
16.318
36.540
39.689
1.00
17.12


ATOM
3522
N
LYS
509
15.312
36.469
41.703
1.00
20.57


ATOM
3523
CA
LYS
509
15.702
35.087
41.961
1.00
23.09


ATOM
3524
CB
LYS
509
15.240
34.637
43.352
1.00
24.96


ATOM
3525
CG
LYS
509
13.763
34.281
43.465
1.00
29.41


ATOM
3526
CD
LYS
509
13.455
33.746
44.859
1.00
32.03


ATOM
3527
CE
LYS
509
12.017
33.278
44.988
1.00
33.33


ATOM
3528
NZ
LYS
509
11.724
32.824
46.378
1.00
34.91


ATOM
3529
C
LYS
509
15.142
34.148
40.909
1.00
24.36


ATOM
3530
O
LYS
509
15.601
33.018
40.769
1.00
25.76


ATOM
3531
N
GLU
510
14.146
34.619
40.169
1.00
25.33


ATOM
3532
CA
GLU
510
13.534
33.819
39.116
1.00
26.94


ATOM
3533
CB
GLU
510
12.240
34.481
38.649
1.00
31.14


ATOM
3534
CG
GLU
510
11.420
35.078
39.776
1.00
39.75


ATOM
3535
CD
GLU
510
10.187
34.265
40.094
1.00
42.36


ATOM
3536
OE1
GLU
510
9.312
34.169
39.212
1.00
46.25


ATOM
3537
OE2
GLU
510
10.094
33.725
41.217
1.00
45.33


ATOM
3538
C
GLU
510
14.489
33.726
37.927
1.00
26.01


ATOM
3539
O
GLU
510
14.458
32.758
37.163
1.00
25.45


ATOM
3540
N
ASN
511
15.343
34.736
37.780
1.00
22.90


ATOM
3541
CA
ASN
511
16.271
34.785
36.657
1.00
21.40


ATOM
3542
CB
ASN
511
15.973
36.028
35.811
1.00
23.82


ATOM
3543
CG
ASN
511
14.538
36.057
35.315
1.00
29.85


ATOM
3544
OD1
ASN
511
14.086
35.126
34.646
1.00
30.15


ATOM
3545
ND2
ASN
511
13.811
37.122
35.647
1.00
28.53


ATOM
3546
C
ASN
511
17.759
34.747
37.000
1.00
18.64


ATOM
3547
O
ASN
511
18.593
34.993
36.131
1.00
16.50


ATOM
3548
N
TYR
512
18.089
34.441
38.251
1.00
15.85


ATOM
3549
CA
TYR
512
19.487
34.360
38.681
1.00
15.32


ATOM
3550
CB
TYR
512
19.604
33.604
40.007
1.00
14.72


ATOM
3551
CG
TYR
512
19.244
34.359
41.266
1.00
14.45


ATOM
3552
CD1
TYR
512
19.008
33.667
42.450
1.00
14.67


ATOM
3553
CE1
TYR
512
18.736
34.335
43.637
1.00
16.30


ATOM
3554
CD2
TYR
512
19.194
35.753
41.295
1.00
14.34


ATOM
3555
CE2
TYR
512
18.920
36.435
42.484
1.00
17.16


ATOM
3556
CZ
TYR
512
18.695
35.714
43.648
1.00
18.10


ATOM
3557
OH
TYR
512
18.451
36.361
44.837
1.00
21.96


ATOM
3558
C
TYR
512
20.378
33.613
37.688
1.00
16.40


ATOM
3559
O
TYR
512
21.318
34.171
37.108
1.00
13.43


ATOM
3560
N
ASN
513
20.077
32.328
37.521
1.00
15.11


ATOM
3561
CA
ASN
513
20.877
31.461
36.673
1.00
14.44


ATOM
3562
CB
ASN
513
20.478
29.999
36.894
1.00
14.83


ATOM
3563
CG
ASN
513
21.677
29.073
36.872
1.00
13.79


ATOM
3564
OD1
ASN
513
22.620
29.261
37.634
1.00
15.96


ATOM
3565
ND2
ASN
513
21.652
28.078
35.993
1.00
13.24


ATOM
3566
C
ASN
513
20.840
31.778
35.198
1.00
14.91


ATOM
3567
O
ASN
513
21.865
31.701
34.517
1.00
12.27


ATOM
3568
N
GLN
514
19.664
32.133
34.697
1.00
13.28


ATOM
3569
CA
GLN
514
19.539
32.441
33.285
1.00
16.41


ATOM
3570
CB
GLN
514
18.062
32.642
32.924
1.00
18.43


ATOM
3571
CG
GLN
514
17.219
31.363
33.087
1.00
25.86


ATOM
3572
CD
GLN
514
16.628
31.163
34.492
1.00
27.97


ATOM
3573
OE1
GLN
514
17.184
31.606
35.501
1.00
22.77


ATOM
3574
NE2
GLN
514
15.493
30.468
34.551
1.00
32.36


ATOM
3575
C
GLN
514
20.378
33.660
32.900
1.00
16.35


ATOM
3576
O
GLN
514
21.004
33.682
31.830
1.00
14.47


ATOM
3577
N
GLU
515
20.406
34.668
33.769
1.00
14.45


ATOM
3578
CA
GLU
515
21.188
35.872
33.486
1.00
15.60


ATOM
3579
CB
GLU
515
20.762
37.023
34.398
1.00
17.63


ATOM
3580
CG
GLU
515
19.361
37.553
34.107
1.00
23.50


ATOM
3581
CD
GLU
515
19.200
37.998
32.663
1.00
29.39


ATOM
3582
OE1
GLU
515
20.051
38.776
32.177
1.00
29.30


ATOM
3583
OE2
GLU
515
18.220
37.570
32.016
1.00
31.22


ATOM
3584
C
GLU
515
22.680
35.591
33.656
1.00
13.08


ATOM
3585
O
GLU
515
23.512
36.209
32.992
1.00
14.72


ATOM
3586
N
TRP
516
23.018
34.671
34.555
1.00
11.64


ATOM
3587
CA
TRP
516
24.423
34.303
34.752
1.00
12.26


ATOM
3588
CB
TRP
516
24.559
33.298
35.901
1.00
10.60


ATOM
3589
CG
TRP
516
25.924
32.648
36.038
1.00
13.26


ATOM
3590
CD2
TRP
516
27.086
33.201
36.671
1.00
13.09


ATOM
3591
CE2
TRP
516
28.110
32.228
36.593
1.00
14.57


ATOM
3592
CE3
TRP
516
27.362
34.423
37.300
1.00
14.40


ATOM
3593
CD1
TRP
516
26.281
31.402
35.612
1.00
15.30


ATOM
3594
NE1
TRP
516
27.593
31.140
35.943
1.00
14.97


ATOM
3595
CZ2
TRP
516
29.392
32.438
37.119
1.00
14.78


ATOM
3596
CZ3
TRP
516
28.640
34.632
37.827
1.00
15.38


ATOM
3597
CH2
TRP
516
29.636
33.642
37.731
1.00
16.29


ATOM
3598
C
TRP
516
24.945
33.701
33.450
1.00
12.53


ATOM
3599
O
TRP
516
26.014
34.081
32.967
1.00
15.24


ATOM
3600
N
TRP
517
24.186
32.778
32.864
1.00
11.64


ATOM
3601
CA
TRP
517
24.631
32.169
31.618
1.00
12.88


ATOM
3602
CB
TRP
517
23.892
30.850
31.371
1.00
11.74


ATOM
3603
CG
TRP
517
24.494
29.780
32.238
1.00
11.07


ATOM
3604
CD2
TRP
517
25.768
29.150
32.047
1.00
10.34


ATOM
3605
CE2
TRP
517
26.014
28.349
33.182
1.00
11.07


ATOM
3606
CE3
TRP
517
26.730
29.193
31.028
1.00
13.21


ATOM
3607
CD1
TRP
517
24.028
29.338
33.442
1.00
10.52


ATOM
3608
NE1
TRP
517
24.937
28.480
34.019
1.00
12.71


ATOM
3609
CZ2
TRP
517
27.185
27.596
33.328
1.00
11.38


ATOM
3610
CZ3
TRP
517
27.899
28.441
31.174
1.00
13.92


ATOM
3611
CH2
TRP
517
28.112
27.657
32.315
1.00
11.19


ATOM
3612
C
TRP
517
24.571
33.092
30.402
1.00
13.68


ATOM
3613
O
TRP
517
25.360
32.937
29.473
1.00
13.23


ATOM
3614
N
SER
518
23.662
34.063
30.403
1.00
13.61


ATOM
3615
CA
SER
518
23.606
35.001
29.289
1.00
13.77


ATOM
3616
CB
SER
518
22.406
35.938
29.429
1.00
16.27


ATOM
3617
OG
SER
518
21.198
35.215
29.273
1.00
25.55


ATOM
3618
C
SER
518
24.908
35.812
29.306
1.00
13.80


ATOM
3619
O
SER
518
25.438
36.174
28.261
1.00
11.73


ATOM
3620
N
LEU
519
25.420
36.085
30.503
1.00
12.48


ATOM
3621
CA
LEU
519
26.664
36.835
30.642
1.00
13.86


ATOM
3622
CB
LEU
519
26.792
37.386
32.065
1.00
13.18


ATOM
3623
CG
LEU
519
25.820
38.521
32.408
1.00
17.32


ATOM
3624
CD1
LEU
519
25.996
38.936
33.869
1.00
15.81


ATOM
3625
CD2
LEU
519
26.082
39.706
31.497
1.00
18.32


ATOM
3626
C
LEU
519
27.854
35.936
30.315
1.00
14.53


ATOM
3627
O
LEU
519
28.833
36.374
29.701
1.00
13.21


ATOM
3628
N
ARG
520
27.763
34.680
30.740
1.00
12.53


ATOM
3629
CA
ARG
520
28.811
33.698
30.483
1.00
14.43


ATOM
3630
CB
ARG
520
28.415
32.342
31.080
1.00
12.24


ATOM
3631
CG
ARG
520
28.505
32.295
32.602
1.00
10.71


ATOM
3632
CD
ARG
520
29.933
32.016
33.047
1.00
11.25


ATOM
3633
NE
ARG
520
30.126
30.601
33.360
1.00
11.37


ATOM
3634
CZ
ARG
520
31.309
30.021
33.547
1.00
14.25


ATOM
3635
NH1
ARG
520
31.364
28.728
33.843
1.00
11.46


ATOM
3636
NH2
ARG
520
32.435
30.722
33.418
1.00
8.82


ATOM
3637
C
ARG
520
29.018
33.581
28.975
1.00
15.32


ATOM
3638
O
ARG
520
30.154
33.479
28.499
1.00
14.29


ATOM
3639
N
LEU
521
27.914
33.602
28.232
1.00
14.48


ATOM
3640
CA
LEU
521
27.964
33.534
26.775
1.00
15.03


ATOM
3641
CB
LEU
521
26.570
33.237
26.197
1.00
14.34


ATOM
3642
CG
LEU
521
26.464
33.320
24.663
1.00
17.99


ATOM
3643
CD1
LEU
521
27.277
32.193
24.036
1.00
14.70


ATOM
3644
CD2
LEU
521
25.003
33.225
24.221
1.00
19.69


ATOM
3645
C
LEU
521
28.463
34.862
26.195
1.00
15.14


ATOM
3646
O
LEU
521
29.426
34.901
25.433
1.00
16.02


ATOM
3647
N
LYS
522
27.800
35.952
26.564
1.00
15.84


ATOM
3648
CA
LYS
522
28.156
37.273
26.053
1.00
16.80


ATOM
3649
CB
LYS
522
27.257
38.340
26.691
1.00
20.30


ATOM
3650
CG
LYS
522
27.614
39.767
26.290
1.00
25.17


ATOM
3651
CD
LYS
522
26.641
40.777
26.885
1.00
25.79


ATOM
3652
CE
LYS
522
27.035
42.197
26.505
1.00
27.00


ATOM
3653
NZ
LYS
522
26.061
43.202
27.014
1.00
29.07


ATOM
3654
C
LYS
522
29.618
37.664
26.245
1.00
15.29


ATOM
3655
O
LYS
522
30.254
38.159
25.322
1.00
15.94


ATOM
3656
N
TYR
523
30.159
37.446
27.437
1.00
14.11


ATOM
3657
CA
TYR
523
31.545
37.823
27.689
1.00
14.39


ATOM
3658
CB
TYR
523
31.672
38.370
29.115
1.00
16.01


ATOM
3659
CG
TYR
523
30.969
39.699
29.274
1.00
19.66


ATOM
3660
CD1
TYR
523
29.842
39.833
30.085
1.00
22.54


ATOM
3661
CE1
TYR
523
29.159
41.054
30.173
1.00
24.34


ATOM
3662
CD2
TYR
523
31.400
40.816
28.560
1.00
21.80


ATOM
3663
CE2
TYR
523
30.730
42.029
28.641
1.00
24.56


ATOM
3664
CZ
TYR
523
29.611
42.142
29.444
1.00
24.26


ATOM
3665
OH
TYR
523
28.946
43.346
29.493
1.00
30.82


ATOM
3666
C
TYR
523
32.605
36.752
27.437
1.00
14.99


ATOM
3667
O
TYR
523
33.610
37.023
26.781
1.00
12.52


ATOM
3668
N
GLN
524
32.389
35.537
27.935
1.00
13.32


ATOM
3669
CA
GLN
524
33.382
34.470
27.751
1.00
12.95


ATOM
3670
CB
GLN
524
33.425
33.566
28.980
1.00
11.02


ATOM
3671
CG
GLN
524
33.970
34.205
30.230
1.00
12.37


ATOM
3672
CD
GLN
524
34.033
33.207
31.356
1.00
10.81


ATOM
3673
OE1
GLN
524
33.043
32.974
32.049
1.00
12.38


ATOM
3674
NE2
GLN
524
35.191
32.577
31.520
1.00
10.48


ATOM
3675
C
GLN
524
33.162
33.584
26.534
1.00
11.74


ATOM
3676
O
GLN
524
34.059
32.845
26.137
1.00
12.11


ATOM
3677
N
GLY
525
31.973
33.637
25.949
1.00
12.72


ATOM
3678
CA
GLY
525
31.709
32.785
24.804
1.00
13.19


ATOM
3679
C
GLY
525
31.674
31.328
25.237
1.00
13.82


ATOM
3680
O
GLY
525
32.180
30.444
24.540
1.00
12.99


ATOM
3681
N
LEU
526
31.087
31.074
26.403
1.00
12.01


ATOM
3682
CA
LEU
526
30.975
29.710
26.913
1.00
11.37


ATOM
3683
CB
LEU
526
31.581
29.598
28.317
1.00
11.79


ATOM
3684
CG
LEU
526
33.052
29.983
28.498
1.00
11.39


ATOM
3685
CD1
LEU
526
33.439
29.852
29.978
1.00
12.76


ATOM
3686
CD2
LEU
526
33.926
29.084
27.625
1.00
9.67


ATOM
3687
C
LEU
526
29.515
29.289
26.989
1.00
14.13


ATOM
3688
O
LEU
526
28.617
30.134
27.059
1.00
14.75


ATOM
3689
N
CYS
527
29.284
27.978
26.963
1.00
13.45


ATOM
3690
CA
CYS
527
27.939
27.429
27.078
1.00
15.05


ATOM
3691
CB
CYS
527
27.424
26.919
25.722
1.00
15.05


ATOM
3692
SG
CYS
527
28.474
25.702
24.876
1.00
19.74


ATOM
3693
C
CYS
527
27.978
26.287
28.091
1.00
15.94


ATOM
3694
O
CYS
527
29.019
25.653
28.289
1.00
15.05


ATOM
3695
N
PRO
528
26.854
26.034
28.773
1.00
15.16


ATOM
3696
CD
PRO
528
25.587
26.794
28.757
1.00
16.64


ATOM
3697
CA
PRO
528
26.816
24.952
29.761
1.00
15.93


ATOM
3698
CB
PRO
528
25.579
25.291
30.588
1.00
15.52


ATOM
3699
CG
PRO
528
24.653
25.904
29.560
1.00
17.39


ATOM
3700
C
PRO
528
26.706
23.606
29.040
1.00
16.28


ATOM
3701
O
PRO
528
25.832
23.426
28.195
1.00
16.69


ATOM
3702
N
PRO
529
27.602
22.650
29.359
1.00
15.89


ATOM
3703
CD
PRO
529
28.620
22.713
30.423
1.00
17.16


ATOM
3704
CA
PRO
529
27.595
21.325
28.728
1.00
16.53


ATOM
3705
CB
PRO
529
28.813
20.646
29.347
1.00
16.86


ATOM
3706
CG
PRO
529
28.864
21.250
30.719
1.00
17.60


ATOM
3707
C
PRO
529
26.299
20.564
28.979
1.00
16.93


ATOM
3708
O
PRO
529
25.929
19.675
28.214
1.00
19.21


ATOM
3709
N
VAL
530
25.620
20.919
30.064
1.00
15.31


ATOM
3710
CA
VAL
530
24.345
20.309
30.421
1.00
18.95


ATOM
3711
CB
VAL
530
24.447
19.514
31.747
1.00
18.21


ATOM
3712
CG1
VAL
530
23.057
19.197
32.277
1.00
20.68


ATOM
3713
CG2
VAL
530
25.221
18.216
31.516
1.00
20.27


ATOM
3714
C
VAL
530
23.331
21.439
30.591
1.00
18.93


ATOM
3715
O
VAL
530
23.586
22.402
31.320
1.00
17.96


ATOM
3716
N
PRO
531
22.179
21.351
29.908
1.00
19.85


ATOM
3717
CD
PRO
531
21.701
20.311
28.982
1.00
21.08


ATOM
3718
CA
PRO
531
21.186
22.422
30.055
1.00
20.04


ATOM
3719
CB
PRO
531
20.019
21.940
29.186
1.00
23.88


ATOM
3720
CG
PRO
531
20.207
20.436
29.134
1.00
24.49


ATOM
3721
C
PRO
531
20.806
22.624
31.519
1.00
20.47


ATOM
3722
O
PRO
531
20.590
21.660
32.258
1.00
19.22


ATOM
3723
N
ARG
532
20.748
23.880
31.946
1.00
17.94


ATOM
3724
CA
ARG
532
20.408
24.173
33.331
1.00
19.58


ATOM
3725
CB
ARG
532
20.850
25.597
33.698
1.00
17.12


ATOM
3726
CG
ARG
532
22.203
26.006
33.109
1.00
17.15


ATOM
3727
CD
ARG
532
23.261
24.916
33.259
1.00
14.33


ATOM
3728
NE
ARG
532
23.625
24.670
34.650
1.00
16.72


ATOM
3729
CZ
ARG
532
23.756
23.457
35.175
1.00
18.54


ATOM
3730
NH1
ARG
532
23.548
22.382
34.418
1.00
18.00


ATOM
3731
NH2
ARG
532
24.100
23.316
36.447
1.00
16.39


ATOM
3732
C
ARG
532
18.903
24.018
33.538
1.00
20.97


ATOM
3733
O
ARG
532
18.125
24.148
32.593
1.00
21.91


ATOM
3734
N
THR
533
18.502
23.735
34.773
1.00
21.56


ATOM
3735
CA
THR
533
17.089
23.560
35.099
1.00
23.91


ATOM
3736
CB
THR
533
16.743
22.075
35.337
1.00
24.39


ATOM
3737
OG1
THR
533
17.593
21.542
36.363
1.00
26.32


ATOM
3738
CG2
THR
533
16.930
21.273
34.054
1.00
26.00


ATOM
3739
C
THR
533
16.734
24.342
36.354
1.00
24.49


ATOM
3740
O
THR
533
17.622
24.792
37.088
1.00
22.75


ATOM
3741
N
GLN
534
15.436
24.494
36.601
1.00
25.56


ATOM
3742
CA
GLN
534
14.963
25.227
37.769
1.00
27.46


ATOM
3743
CB
GLN
534
13.429
25.173
37.845
1.00
29.98


ATOM
3744
CG
GLN
534
12.834
26.077
38.917
1.00
34.85


ATOM
3745
CD
GLN
534
12.498
25.332
40.196
1.00
38.40


ATOM
3746
OE1
GLN
534
13.144
24.341
40.542
1.00
39.55


ATOM
3747
NE2
GLN
534
11.487
25.815
40.914
1.00
40.66


ATOM
3748
C
GLN
534
15.589
24.628
39.023
1.00
26.85


ATOM
3749
O
GLN
534
15.630
23.410
39.195
1.00
28.91


ATOM
3750
N
GLY
535
16.088
25.486
39.900
1.00
26.04


ATOM
3751
CA
GLY
535
16.722
24.988
41.103
1.00
22.99


ATOM
3752
C
GLY
535
18.230
25.145
41.032
1.00
20.56


ATOM
3753
O
GLY
535
18.893
25.172
42.062
1.00
21.12


ATOM
3754
N
ASP
536
18.783
25.236
39.824
1.00
19.34


ATOM
3755
CA
ASP
536
20.229
25.412
39.690
1.00
18.42


ATOM
3756
CB
ASP
536
20.710
25.126
38.262
1.00
18.23


ATOM
3757
CG
ASP
536
20.693
23.647
37.917
1.00
17.73


ATOM
3758
OD1
ASP
536
20.885
22.814
38.829
1.00
16.38


ATOM
3759
OD2
ASP
536
20.509
23.326
36.726
1.00
18.51


ATOM
3760
C
ASP
536
20.617
26.845
40.039
1.00
17.25


ATOM
3761
O
ASP
536
19.893
27.786
39.722
1.00
17.90


ATOM
3762
N
PHE
537
21.761
26.996
40.694
1.00
15.41


ATOM
3763
CA
PHE
537
22.285
28.309
41.069
1.00
15.10


ATOM
3764
CB
PHE
537
21.914
28.654
42.511
1.00
13.69


ATOM
3765
CG
PHE
537
22.344
30.031
42.934
1.00
14.67


ATOM
3766
CD1
PHE
537
21.970
31.150
42.190
1.00
14.51


ATOM
3767
CD2
PHE
537
23.127
30.211
44.073
1.00
14.42


ATOM
3768
CE1
PHE
537
22.372
32.434
42.576
1.00
16.76


ATOM
3769
CE2
PHE
537
23.535
31.490
44.469
1.00
16.13


ATOM
3770
CZ
PHE
537
23.155
32.602
43.717
1.00
16.55


ATOM
3771
C
PHE
537
23.798
28.188
40.929
1.00
14.34


ATOM
3772
O
PHE
537
24.534
28.107
41.910
1.00
11.59


ATOM
3773
N
ASP
538
24.246
28.160
39.683
1.00
13.08


ATOM
3774
CA
ASP
538
25.656
28.013
39.380
1.00
12.91


ATOM
3775
CB
ASP
538
25.812
27.915
37.858
1.00
14.42


ATOM
3776
CG
ASP
538
24.984
26.761
37.275
1.00
13.98


ATOM
3777
OD1
ASP
538
24.869
25.725
37.959
1.00
15.77


ATOM
3778
OD2
ASP
538
24.456
26.875
36.148
1.00
16.17


ATOM
3779
C
ASP
538
26.546
29.093
40.005
1.00
13.57


ATOM
3780
O
ASP
538
27.680
28.814
40.391
1.00
14.25


ATOM
3781
N
PRO
539
26.049
30.336
40.125
1.00
12.45


ATOM
3782
CD
PRO
539
24.833
30.944
39.554
1.00
12.63


ATOM
3783
CA
PRO
539
26.903
31.362
40.738
1.00
14.07


ATOM
3784
CB
PRO
539
25.998
32.596
40.760
1.00
13.43


ATOM
3785
CG
PRO
539
25.203
32.428
39.495
1.00
14.83


ATOM
3786
C
PRO
539
27.318
30.945
42.149
1.00
14.32


ATOM
3787
O
PRO
539
28.405
31.290
42.620
1.00
15.96


ATOM
3788
N
GLY
540
26.443
30.201
42.818
1.00
13.56


ATOM
3789
CA
GLY
540
26.726
29.759
44.173
1.00
13.06


ATOM
3790
C
GLY
540
27.880
28.779
44.262
1.00
14.35


ATOM
3791
O
GLY
540
28.410
28.530
45.350
1.00
14.78


ATOM
3792
N
ALA
541
28.278
28.233
43.116
1.00
13.27


ATOM
3793
CA
ALA
541
29.374
27.268
43.057
1.00
13.82


ATOM
3794
CB
ALA
541
29.142
26.282
41.908
1.00
13.95


ATOM
3795
C
ALA
541
30.736
27.948
42.899
1.00
14.23


ATOM
3796
O
ALA
541
31.755
27.277
42.723
1.00
14.48


ATOM
3797
N
LYS
542
30.744
29.278
42.950
1.00
13.31


ATOM
3798
CA
LYS
542
31.981
30.051
42.845
1.00
13.43


ATOM
3799
CB
LYS
542
31.854
31.131
41.758
1.00
11.46


ATOM
3800
CG
LYS
542
33.080
32.052
41.629
1.00
11.83


ATOM
3801
CD
LYS
542
34.363
31.258
41.356
1.00
11.07


ATOM
3802
CE
LYS
542
35.594
32.152
41.434
1.00
13.88


ATOM
3803
NZ
LYS
542
36.866
31.380
41.387
1.00
13.39


ATOM
3804
C
LYS
542
32.195
30.690
44.215
1.00
14.23


ATOM
3805
O
LYS
542
31.363
31.472
44.678
1.00
13.83


ATOM
3806
N
PHE
543
33.309
30.346
44.857
1.00
14.52


ATOM
3807
CA
PHE
543
33.640
30.842
46.197
1.00
15.65


ATOM
3808
CB
PHE
543
35.156
30.803
46.422
1.00
16.34


ATOM
3809
CG
PHE
543
35.581
31.353
47.760
1.00
16.35


ATOM
3810
CD1
PHE
543
35.489
30.574
48.909
1.00
18.40


ATOM
3811
CD2
PHE
543
36.047
32.661
47.875
1.00
19.53


ATOM
3812
CE1
PHE
543
35.858
31.090
50.161
1.00
18.32


ATOM
3813
CE2
PHE
543
36.418
33.188
49.120
1.00
18.19


ATOM
3814
CZ
PHE
543
36.323
32.399
50.263
1.00
18.52


ATOM
3815
C
PHE
543
33.159
32.242
46.577
1.00
16.50


ATOM
3816
O
PHE
543
32.411
32.411
47.540
1.00
17.35


ATOM
3817
N
HIS
544
33.603
33.242
45.822
1.00
13.72


ATOM
3818
CA
HIS
544
33.284
34.635
46.119
1.00
14.78


ATOM
3819
CB
HIS
544
34.006
35.543
45.116
1.00
13.88


ATOM
3820
CG
HIS
544
35.484
35.298
45.050
1.00
13.02


ATOM
3821
CD2
HIS
544
36.536
36.070
45.408
1.00
10.61


ATOM
3822
ND1
HIS
544
36.017
34.106
44.606
1.00
14.71


ATOM
3823
CE1
HIS
544
37.335
34.155
44.693
1.00
13.70


ATOM
3824
NE2
HIS
544
37.678
35.335
45.176
1.00
13.80


ATOM
3825
C
HIS
544
31.808
35.016
46.213
1.00
14.84


ATOM
3826
O
HIS
544
31.470
36.034
46.826
1.00
14.80


ATOM
3827
N
ILE
545
30.930
34.212
45.622
1.00
14.32


ATOM
3828
CA
ILE
545
29.504
34.511
45.670
1.00
13.72


ATOM
3829
CB
ILE
545
28.733
33.701
44.598
1.00
14.44


ATOM
3830
CG2
ILE
545
27.234
33.908
44.749
1.00
12.67


ATOM
3831
CG1
ILE
545
29.190
34.138
43.199
1.00
16.16


ATOM
3832
CD1
ILE
545
29.032
35.621
42.922
1.00
16.96


ATOM
3833
C
ILE
545
28.954
34.249
47.079
1.00
14.60


ATOM
3834
O
ILE
545
28.518
35.182
47.757
1.00
13.03


ATOM
3835
N
PRO
546
28.976
32.986
47.549
1.00
15.66


ATOM
3836
CD
PRO
546
29.355
31.713
46.909
1.00
13.25


ATOM
3837
CA
PRO
546
28.457
32.750
48.903
1.00
15.17


ATOM
3838
CB
PRO
546
28.453
31.222
49.014
1.00
16.53


ATOM
3839
CG
PRO
546
29.579
30.812
48.111
1.00
17.51


ATOM
3840
C
PRO
546
29.305
33.419
49.990
1.00
16.68


ATOM
3841
O
PRO
546
28.799
33.732
51.074
1.00
15.08


ATOM
3842
N
SER
547
30.589
33.641
49.701
1.00
13.81


ATOM
3843
CA
SER
547
31.488
34.284
50.659
1.00
15.60


ATOM
3844
CB
SER
547
32.947
33.918
50.362
1.00
18.79


ATOM
3845
OG
SER
547
33.183
32.536
50.565
1.00
22.02


ATOM
3846
C
SER
547
31.342
35.803
50.646
1.00
13.58


ATOM
3847
O
SER
547
31.965
36.499
51.443
1.00
13.34


ATOM
3848
N
SER
548
30.529
36.312
49.727
1.00
13.46


ATOM
3849
CA
SER
548
30.288
37.751
49.617
1.00
13.96


ATOM
3850
CB
SER
548
29.427
38.231
50.791
1.00
14.80


ATOM
3851
OG
SER
548
28.929
39.544
50.566
1.00
14.76


ATOM
3852
C
SER
548
31.571
38.587
49.542
1.00
15.62


ATOM
3853
O
SER
548
31.743
39.553
50.288
1.00
15.61


ATOM
3854
N
VAL
549
32.464
38.201
48.637
1.00
14.22


ATOM
3855
CA
VAL
549
33.718
38.914
48.413
1.00
14.31


ATOM
3856
CB
VAL
549
34.936
37.957
48.426
1.00
14.24


ATOM
3857
CG1
VAL
549
36.200
38.716
48.029
1.00
15.66


ATOM
3858
CG2
VAL
549
35.105
37.337
49.813
1.00
15.47


ATOM
3859
C
VAL
549
33.611
39.538
47.023
1.00
13.23


ATOM
3860
O
VAL
549
33.448
38.826
46.034
1.00
14.20


ATOM
3861
N
PRO
550
33.680
40.877
46.931
1.00
13.00


ATOM
3862
CD
PRO
550
33.789
41.840
48.040
1.00
12.51


ATOM
3863
CA
PRO
550
33.588
41.572
45.637
1.00
13.72


ATOM
3864
CB
PRO
550
33.870
43.026
46.007
1.00
12.92


ATOM
3865
CG
PRO
550
33.282
43.120
47.399
1.00
13.93


ATOM
3866
C
PRO
550
34.597
41.006
44.640
1.00
13.40


ATOM
3867
O
PRO
550
35.694
40.602
45.027
1.00
12.68


ATOM
3868
N
TYR
551
34.238
40.996
43.357
1.00
12.51


ATOM
3869
CA
TYR
551
35.111
40.419
42.337
1.00
11.74


ATOM
3870
CB
TYR
551
34.343
39.339
41.565
1.00
12.26


ATOM
3871
CG
TYR
551
35.216
38.181
41.146
1.00
11.10


ATOM
3872
CD1
TYR
551
35.589
37.201
42.069
1.00
12.21


ATOM
3873
CE1
TYR
551
36.445
36.163
41.716
1.00
11.38


ATOM
3874
CD2
TYR
551
35.717
38.092
39.849
1.00
10.70


ATOM
3875
CE2
TYR
551
36.578
37.052
39.479
1.00
11.88


ATOM
3876
CZ
TYR
551
36.936
36.095
40.422
1.00
12.73


ATOM
3877
OH
TYR
551
37.789
35.078
40.077
1.00
12.21


ATOM
3878
C
TYR
551
35.758
41.362
41.316
1.00
12.92


ATOM
3879
O
TYR
551
36.772
41.009
40.713
1.00
12.28


ATOM
3880
N
ILE
552
35.182
42.543
41.106
1.00
10.57


ATOM
3881
CA
ILE
552
35.729
43.474
40.123
1.00
10.70


ATOM
3882
CB
ILE
552
34.866
44.760
40.042
1.00
10.46


ATOM
3883
CG2
ILE
552
35.175
45.681
41.219
1.00
10.81


ATOM
3884
CG1
ILE
552
35.111
45.464
38.706
1.00
11.02


ATOM
3885
CD1
ILE
552
34.654
44.656
37.494
1.00
11.29


ATOM
3886
C
ILE
552
37.195
43.826
40.404
1.00
11.68


ATOM
3887
O
ILE
552
37.940
44.198
39.499
1.00
12.19


ATOM
3888
N
ARG
553
37.607
43.692
41.660
1.00
11.17


ATOM
3889
CA
ARG
553
38.989
43.952
42.055
1.00
10.89


ATOM
3890
CB
ARG
553
39.156
43.668
43.549
1.00
11.30


ATOM
3891
CG
ARG
553
38.686
42.265
43.958
1.00
13.00


ATOM
3892
CD
ARG
553
38.704
42.074
45.474
1.00
13.72


ATOM
3893
NE
ARG
553
37.886
43.088
46.134
1.00
10.87


ATOM
3894
CZ
ARG
553
37.634
43.123
47.439
1.00
13.84


ATOM
3895
NH1
ARG
553
38.132
42.196
48.247
1.00
11.15


ATOM
3896
NH2
ARG
553
36.889
44.100
47.941
1.00
13.85


ATOM
3897
C
ARG
553
39.971
43.071
41.260
1.00
12.16


ATOM
3898
O
ARG
553
41.105
43.478
40.990
1.00
11.49


ATOM
3899
N
TYR
554
39.539
41.871
40.881
1.00
10.69


ATOM
3900
CA
TYR
554
40.408
40.965
40.130
1.00
12.89


ATOM
3901
CB
TYR
554
39.882
39.525
40.215
1.00
10.20


ATOM
3902
CG
TYR
554
39.814
39.009
41.640
1.00
12.03


ATOM
3903
CD1
TYR
554
38.586
38.818
42.274
1.00
14.17


ATOM
3904
CE1
TYR
554
38.515
38.381
43.599
1.00
13.54


ATOM
3905
CD2
TYR
554
40.978
38.750
42.367
1.00
12.66


ATOM
3906
CE2
TYR
554
40.920
38.317
43.695
1.00
13.05


ATOM
3907
CZ
TYR
554
39.683
38.133
44.302
1.00
13.70


ATOM
3908
OH
TYR
554
39.603
37.697
45.610
1.00
13.05


ATOM
3909
C
TYR
554
40.558
41.394
38.672
1.00
12.72


ATOM
3910
O
TYR
554
41.599
41.152
38.051
1.00
12.24


ATOM
3911
N
PHE
555
39.515
42.016
38.128
1.00
10.68


ATOM
3912
CA
PHE
555
39.550
42.509
36.750
1.00
11.93


ATOM
3913
CB
PHE
555
38.154
42.980
36.317
1.00
11.21


ATOM
3914
CG
PHE
555
38.125
43.646
34.968
1.00
14.00


ATOM
3915
CD1
PHE
555
38.050
42.892
33.801
1.00
14.57


ATOM
3916
CD2
PHE
555
38.193
45.031
34.867
1.00
15.09


ATOM
3917
CE1
PHE
555
38.043
43.510
32.549
1.00
16.67


ATOM
3918
CE2
PHE
555
38.189
45.660
33.619
1.00
17.16


ATOM
3919
CZ
PHE
555
38.113
44.899
32.458
1.00
17.19


ATOM
3920
C
PHE
555
40.527
43.689
36.735
1.00
13.11


ATOM
3921
O
PHE
555
41.400
43.779
35.872
1.00
13.19


ATOM
3922
N
VAL
556
40.366
44.592
37.698
1.00
10.88


ATOM
3923
CA
VAL
556
41.239
45.753
37.809
1.00
11.92


ATOM
3924
CB
VAL
556
40.830
46.642
39.004
1.00
11.44


ATOM
3925
CG1
VAL
556
41.847
47.767
39.202
1.00
13.68


ATOM
3926
CG2
VAL
556
39.433
47.226
38.757
1.00
12.64


ATOM
3927
C
VAL
556
42.683
45.276
37.989
1.00
12.43


ATOM
3928
O
VAL
556
43.590
45.746
37.308
1.00
12.45


ATOM
3929
N
SER
557
42.882
44.325
38.895
1.00
12.83


ATOM
3930
CA
SER
557
44.211
43.781
39.156
1.00
13.38


ATOM
3931
CB
SER
557
44.124
42.658
40.195
1.00
14.45


ATOM
3932
OG
SER
557
45.366
41.981
40.321
1.00
15.47


ATOM
3933
C
SER
557
44.915
43.252
37.908
1.00
14.80


ATOM
3934
O
SER
557
46.080
43.567
37.659
1.00
13.56


ATOM
3935
N
PHE
558
44.220
42.438
37.123
1.00
13.85


ATOM
3936
CA
PHE
558
44.843
41.878
35.936
1.00
16.13


ATOM
3937
CB
PHE
558
43.930
40.813
35.311
1.00
14.35


ATOM
3938
CG
PHE
558
44.109
39.446
35.921
1.00
12.86


ATOM
3939
CD1
PHE
558
44.081
39.279
37.304
1.00
14.64


ATOM
3940
CD2
PHE
558
44.352
38.336
35.116
1.00
12.97


ATOM
3941
CE1
PHE
558
44.301
38.021
37.881
1.00
14.77


ATOM
3942
CE2
PHE
558
44.570
37.081
35.674
1.00
14.28


ATOM
3943
CZ
PHE
558
44.546
36.921
37.061
1.00
14.43


ATOM
3944
C
PHE
558
45.265
42.937
34.923
1.00
17.21


ATOM
3945
O
PHE
558
46.248
42.757
34.210
1.00
18.29


ATOM
3946
N
ILE
559
44.545
44.052
34.875
1.00
17.72


ATOM
3947
CA
ILE
559
44.907
45.124
33.956
1.00
17.85


ATOM
3948
CB
ILE
559
43.754
46.148
33.780
1.00
19.20


ATOM
3949
CG2
ILE
559
44.260
47.363
33.011
1.00
19.44


ATOM
3950
CG1
ILE
559
42.564
45.502
33.064
1.00
21.05


ATOM
3951
CD1
ILE
559
42.807
45.211
31.605
1.00
22.66


ATOM
3952
C
ILE
559
46.120
45.891
34.491
1.00
16.91


ATOM
3953
O
ILE
559
47.155
45.991
33.826
1.00
18.09


ATOM
3954
N
ILE
560
45.991
46.417
35.704
1.00
15.99


ATOM
3955
CA
ILE
560
47.056
47.221
36.294
1.00
14.87


ATOM
3956
CB
ILE
560
46.560
47.971
37.563
1.00
15.25


ATOM
3957
CG2
ILE
560
45.253
48.708
37.249
1.00
13.63


ATOM
3958
CG1
ILE
560
46.366
46.996
38.725
1.00
14.28


ATOM
3959
CD1
ILE
560
45.970
47.678
40.039
1.00
14.84


ATOM
3960
C
ILE
560
48.337
46.467
36.639
1.00
16.49


ATOM
3961
O
ILE
560
49.415
47.060
36.666
1.00
14.18


ATOM
3962
N
GLN
561
48.245
45.167
36.900
1.00
15.61


ATOM
3963
CA
GLN
561
49.461
44.443
37.233
1.00
16.41


ATOM
3964
CB
GLN
561
49.152
43.001
37.663
1.00
15.73


ATOM
3965
CG
GLN
561
48.557
42.090
36.604
1.00
14.21


ATOM
3966
CD
GLN
561
48.239
40.715
37.171
1.00
17.73


ATOM
3967
OE1
GLN
561
48.834
39.715
36.771
1.00
16.09


ATOM
3968
NE2
GLN
561
47.300
40.664
38.121
1.00
14.54


ATOM
3969
C
GLN
561
50.450
44.476
36.064
1.00
16.86


ATOM
3970
O
GLN
561
51.664
44.434
36.273
1.00
16.40


ATOM
3971
N
PHE
562
49.939
44.565
34.836
1.00
15.77


ATOM
3972
CA
PHE
562
50.824
44.631
33.684
1.00
16.79


ATOM
3973
CB
PHE
562
50.096
44.217
32.399
1.00
15.11


ATOM
3974
CG
PHE
562
49.994
42.729
32.236
1.00
16.63


ATOM
3975
CD1
PHE
562
48.911
42.029
32.757
1.00
14.63


ATOM
3976
CD2
PHE
562
51.037
42.012
31.648
1.00
18.81


ATOM
3977
CE1
PHE
562
48.865
40.637
32.705
1.00
18.62


ATOM
3978
CE2
PHE
562
51.006
40.615
31.589
1.00
18.29


ATOM
3979
CZ
PHE
562
49.915
39.927
32.121
1.00
17.80


ATOM
3980
C
PHE
562
51.385
46.042
33.579
1.00
17.19


ATOM
3981
O
PHE
562
52.517
46.238
33.143
1.00
15.79


ATOM
3982
N
GLN
563
50.592
47.022
33.998
1.00
16.85


ATOM
3983
CA
GLN
563
51.043
48.407
34.001
1.00
18.71


ATOM
3984
CB
GLN
563
49.909
49.347
34.418
1.00
18.72


ATOM
3985
CG
GLN
563
48.890
49.651
33.335
1.00
16.23


ATOM
3986
CD
GLN
563
47.819
50.607
33.825
1.00
18.40


ATOM
3987
OE1
GLN
563
46.777
50.188
34.326
1.00
16.56


ATOM
3988
NE2
GLN
563
48.084
51.908
33.700
1.00
15.19


ATOM
3989
C
GLN
563
52.184
48.528
35.011
1.00
18.91


ATOM
3990
O
GLN
563
53.159
49.237
34.773
1.00
21.62


ATOM
3991
N
PHE
564
52.048
47.846
36.148
1.00
17.60


ATOM
3992
CA
PHE
564
53.082
47.879
37.179
1.00
17.70


ATOM
3993
CB
PHE
564
52.576
47.237
38.479
1.00
16.56


ATOM
3994
CG
PHE
564
51.412
47.961
39.114
1.00
16.88


ATOM
3995
CD1
PHE
564
51.009
49.216
38.655
1.00
17.26


ATOM
3996
CD2
PHE
564
50.732
47.393
40.193
1.00
17.51


ATOM
3997
CE1
PHE
564
49.948
49.896
39.262
1.00
17.30


ATOM
3998
CE2
PHE
564
49.668
48.065
40.811
1.00
16.87


ATOM
3999
CZ
PHE
564
49.275
49.316
40.346
1.00
17.82


ATOM
4000
C
PHE
564
54.320
47.132
36.682
1.00
18.19


ATOM
4001
O
PHE
564
55.448
47.583
36.866
1.00
16.35


ATOM
4002
N
HIS
565
54.103
45.980
36.058
1.00
18.26


ATOM
4003
CA
HIS
565
55.201
45.191
35.523
1.00
17.93


ATOM
4004
CB
HIS
565
54.652
43.948
34.813
1.00
16.92


ATOM
4005
CG
HIS
565
55.712
43.026
34.290
1.00
19.54


ATOM
4006
CD2
HIS
565
55.963
42.577
33.036
1.00
18.23


ATOM
4007
ND1
HIS
565
56.645
42.424
35.106
1.00
19.14


ATOM
4008
CE1
HIS
565
57.423
41.641
34.379
1.00
19.86


ATOM
4009
NE2
HIS
565
57.030
41.716
33.120
1.00
18.37


ATOM
4010
C
HIS
565
56.001
46.053
34.536
1.00
19.62


ATOM
4011
O
HIS
565
57.224
46.140
34.623
1.00
19.79


ATOM
4012
N
GLU
566
55.299
46.692
33.605
1.00
19.55


ATOM
4013
CA
GLU
566
55.938
47.546
32.607
1.00
21.41


ATOM
4014
CB
GLU
566
54.874
48.175
31.702
1.00
21.29


ATOM
4015
CG
GLU
566
55.420
49.067
30.595
1.00
22.84


ATOM
4016
CD
GLU
566
54.320
49.736
29.798
1.00
23.16


ATOM
4017
OE1
GLU
566
53.587
50.571
30.370
1.00
25.71


ATOM
4018
OE2
GLU
566
54.180
49.423
28.599
1.00
24.72


ATOM
4019
C
GLU
566
56.781
48.645
33.259
1.00
22.27


ATOM
4020
O
GLU
566
57.954
48.823
32.920
1.00
22.02


ATOM
4021
N
ALA
567
56.185
49.375
34.199
1.00
22.14


ATOM
4022
CA
ALA
567
56.884
50.457
34.887
1.00
22.62


ATOM
4023
CB
ALA
567
55.918
51.206
35.794
1.00
21.46


ATOM
4024
C
ALA
567
58.081
49.966
35.698
1.00
23.23


ATOM
4025
O
ALA
567
59.165
50.544
35.633
1.00
21.96


ATOM
4026
N
LEU
568
57.884
48.898
36.463
1.00
23.52


ATOM
4027
CA
LEU
568
58.953
48.353
37.287
1.00
24.49


ATOM
4028
CB
LEU
568
58.427
47.204
38.149
1.00
23.80


ATOM
4029
CG
LEU
568
57.319
47.563
39.146
1.00
25.68


ATOM
4030
CD1
LEU
568
56.974
46.337
39.976
1.00
24.01


ATOM
4031
CD2
LEU
568
57.770
48.705
40.047
1.00
24.11


ATOM
4032
C
LEU
568
60.129
47.874
36.444
1.00
26.12


ATOM
4033
O
LEU
568
61.287
48.041
36.835
1.00
25.53


ATOM
4034
N
CYS
569
59.829
47.277
35.293
1.00
26.09


ATOM
4035
CA
CYS
569
60.866
46.785
34.394
1.00
26.84


ATOM
4036
C
CYS
569
61.662
47.954
33.833
1.00
29.17


ATOM
4037
O
CYS
569
62.888
47.891
33.735
1.00
29.21


ATOM
4038
CB
CYS
569
60.245
45.983
33.251
1.00
24.41


ATOM
4039
SG
CYS
569
59.479
44.440
33.829
1.00
23.54


ATOM
4040
N
GLN
570
60.958
49.018
33.461
1.00
30.60


ATOM
4041
CA
GLN
570
61.609
50.205
32.929
1.00
33.85


ATOM
4042
CB
GLN
570
60.560
51.241
32.508
1.00
36.01


ATOM
4043
CG
GLN
570
61.123
52.471
31.797
1.00
40.86


ATOM
4044
CD
GLN
570
61.634
53.535
32.755
1.00
44.93


ATOM
4045
OE1
GLN
570
62.251
54.518
32.338
1.00
47.36


ATOM
4046
NE2
GLN
570
61.370
53.349
34.044
1.00
46.77


ATOM
4047
C
GLN
570
62.518
50.774
34.018
1.00
34.13


ATOM
4048
O
GLN
570
63.651
51.168
33.750
1.00
35.84


ATOM
4049
N
ALA
571
62.023
50.793
35.252
1.00
33.88


ATOM
4050
CA
ALA
571
62.798
51.308
36.376
1.00
33.88


ATOM
4051
CB
ALA
571
61.922
51.397
37.616
1.00
33.43


ATOM
4052
C
ALA
571
64.008
50.421
36.655
1.00
34.68


ATOM
4053
O
ALA
571
65.025
50.891
37.168
1.00
33.79


ATOM
4054
N
ALA
572
63.894
49.140
36.314
1.00
34.10


ATOM
4055
CA
ALA
572
64.979
48.187
36.529
1.00
34.04


ATOM
4056
CB
ALA
572
64.414
46.781
36.698
1.00
31.78


ATOM
4057
C
ALA
572
65.987
48.209
35.381
1.00
34.28


ATOM
4058
O
ALA
572
66.963
47.456
35.387
1.00
33.48


ATOM
4059
N
GLY
573
65.740
49.067
34.396
1.00
35.90


ATOM
4060
CA
GLY
573
66.639
49.173
33.261
1.00
36.02


ATOM
4061
C
GLY
573
66.486
48.083
32.214
1.00
36.88


ATOM
4062
O
GLY
573
67.380
47.876
31.391
1.00
36.25


ATOM
4063
N
HIS
574
65.357
47.381
32.232
1.00
36.48


ATOM
4064
CA
HIS
574
65.124
46.320
31.262
1.00
34.33


ATOM
4065
CB
HIS
574
63.916
45.472
31.661
1.00
35.35


ATOM
4066
CG
HIS
574
63.584
44.400
30.670
1.00
36.05


ATOM
4067
CD2
HIS
574
62.614
44.325
29.727
1.00
36.62


ATOM
4068
ND1
HIS
574
64.327
43.245
30.547
1.00
36.78


ATOM
4069
CE1
HIS
574
63.829
42.506
29.571
1.00
36.45


ATOM
4070
NE2
HIS
574
62.790
43.138
29.057
1.00
35.54


ATOM
4071
C
HIS
574
64.874
46.906
29.881
1.00
33.60


ATOM
4072
O
HIS
574
64.237
47.946
29.743
1.00
33.03


ATOM
4073
N
THR
575
65.380
46.227
28.859
1.00
32.54


ATOM
4074
CA
THR
575
65.192
46.671
27.488
1.00
33.83


ATOM
4075
CB
THR
575
66.501
47.234
26.889
1.00
34.38


ATOM
4076
OG1
THR
575
67.435
46.166
26.684
1.00
35.54


ATOM
4077
CG2
THR
575
67.115
48.261
27.831
1.00
35.04


ATOM
4078
C
THR
575
64.751
45.462
26.676
1.00
33.06


ATOM
4079
O
THR
575
65.060
44.322
27.030
1.00
33.26


ATOM
4080
N
GLY
576
64.023
45.711
25.594
1.00
32.96


ATOM
4081
CA
GLY
576
63.554
44.618
24.764
1.00
32.46


ATOM
4082
C
GLY
576
62.144
44.192
25.125
1.00
32.04


ATOM
4083
O
GLY
576
61.479
44.862
25.915
1.00
32.23


ATOM
4084
N
PRO
577
61.663
43.068
24.571
1.00
31.90


ATOM
4085
CD
PRO
577
62.410
42.136
23.709
1.00
30.59


ATOM
4086
CA
PRO
577
60.314
42.558
24.841
1.00
29.53


ATOM
4087
CB
PRO
577
60.351
41.158
24.235
1.00
30.83


ATOM
4088
CG
PRO
577
61.297
41.321
23.087
1.00
32.27


ATOM
4089
C
PRO
577
59.972
42.538
26.329
1.00
28.72


ATOM
4090
O
PRO
577
60.709
41.981
27.143
1.00
28.66


ATOM
4091
N
LEU
578
58.842
43.146
26.672
1.00
27.32


ATOM
4092
CA
LEU
578
58.393
43.211
28.055
1.00
25.47


ATOM
4093
CB
LEU
578
57.073
43.990
28.135
1.00
24.84


ATOM
4094
CG
LEU
578
56.462
44.208
29.523
1.00
23.79


ATOM
4095
CD1
LEU
578
57.435
44.990
30.395
1.00
23.05


ATOM
4096
CD2
LEU
578
55.141
44.962
29.390
1.00
24.13


ATOM
4097
C
LEU
578
58.224
41.831
28.695
1.00
24.37


ATOM
4098
O
LEU
578
58.540
41.646
29.874
1.00
25.18


ATOM
4099
N
HIS
579
57.743
40.855
27.927
1.00
22.93


ATOM
4100
CA
HIS
579
57.533
39.521
28.482
1.00
22.45


ATOM
4101
CB
HIS
579
56.736
38.635
27.511
1.00
22.24


ATOM
4102
CG
HIS
579
57.512
38.181
26.313
1.00
22.10


ATOM
4103
CD2
HIS
579
58.201
37.038
26.080
1.00
23.76


ATOM
4104
ND1
HIS
579
57.627
38.938
25.166
1.00
24.64


ATOM
4105
CE1
HIS
579
58.350
38.279
24.277
1.00
25.23


ATOM
4106
NE2
HIS
579
58.711
37.123
24.807
1.00
25.73


ATOM
4107
C
HIS
579
58.810
38.796
28.900
1.00
23.53


ATOM
4108
O
HIS
579
58.744
37.743
29.535
1.00
24.05


ATOM
4109
N
LYS
580
59.968
39.348
28.547
1.00
23.73


ATOM
4110
CA
LYS
580
61.244
38.734
28.919
1.00
26.19


ATOM
4111
CB
LYS
580
62.272
38.902
27.794
1.00
27.71


ATOM
4112
CG
LYS
580
61.993
38.075
26.553
1.00
31.25


ATOM
4113
CD
LYS
580
63.043
38.351
25.481
1.00
34.78


ATOM
4114
CE
LYS
580
62.733
37.611
24.191
1.00
37.22


ATOM
4115
NZ
LYS
580
63.671
37.995
23.096
1.00
40.53


ATOM
4116
C
LYS
580
61.811
39.340
30.206
1.00
26.16


ATOM
4117
O
LYS
580
62.850
38.903
30.706
1.00
23.22


ATOM
4118
N
CYS
581
61.124
40.344
30.739
1.00
24.41


ATOM
4119
CA
CYS
581
61.569
41.006
31.959
1.00
23.52


ATOM
4120
C
CYS
581
61.407
40.186
33.240
1.00
24.04


ATOM
4121
O
CYS
581
60.418
39.469
33.419
1.00
21.53


ATOM
4122
CB
CYS
581
60.838
42.342
32.119
1.00
23.29


ATOM
4123
SG
CYS
581
61.004
43.098
33.770
1.00
24.70


ATOM
4124
N
ASP
582
62.400
40.306
34.121
1.00
21.19


ATOM
4125
CA
ASP
582
62.419
39.637
35.421
1.00
22.50


ATOM
4126
CB
ASP
582
63.317
38.394
35.392
1.00
22.61


ATOM
4127
CG
ASP
582
63.390
37.685
36.742
1.00
23.83


ATOM
4128
OD1
ASP
582
62.906
38.239
37.758
1.00
24.26


ATOM
4129
OD2
ASP
582
63.947
36.567
36.793
1.00
23.11


ATOM
4130
C
ASP
582
63.010
40.680
36.360
1.00
24.44


ATOM
4131
O
ASP
582
64.211
40.968
36.302
1.00
24.08


ATOM
4132
N
ILE
583
62.165
41.253
37.213
1.00
22.22


ATOM
4133
CA
ILE
583
62.601
42.294
38.138
1.00
21.09


ATOM
4134
CB
ILE
583
61.413
43.184
38.568
1.00
19.80


ATOM
4135
CG2
ILE
583
60.751
43.796
37.340
1.00
18.47


ATOM
4136
CG1
ILE
583
60.408
42.355
39.369
1.00
19.27


ATOM
4137
CD1
ILE
583
59.301
43.181
40.010
1.00
21.03


ATOM
4138
C
ILE
583
63.279
41.779
39.401
1.00
21.02


ATOM
4139
O
ILE
583
63.533
42.552
40.325
1.00
21.75


ATOM
4140
N
TYR
584
63.575
40.484
39.445
1.00
21.19


ATOM
4141
CA
TYR
584
64.220
39.906
40.620
1.00
22.52


ATOM
4142
CB
TYR
584
64.660
38.466
40.346
1.00
23.63


ATOM
4143
CG
TYR
584
65.245
37.787
41.565
1.00
25.38


ATOM
4144
CD1
TYR
584
64.420
37.304
42.576
1.00
24.65


ATOM
4145
CE1
TYR
584
64.951
36.724
43.725
1.00
26.30


ATOM
4146
CD2
TYR
584
66.625
37.672
41.731
1.00
25.96


ATOM
4147
CE2
TYR
584
67.167
37.095
42.878
1.00
27.41


ATOM
4148
CZ
TYR
584
66.325
36.624
43.869
1.00
27.35


ATOM
4149
OH
TYR
584
66.852
36.048
45.003
1.00
29.28


ATOM
4150
C
TYR
584
65.434
40.721
41.068
1.00
22.10


ATOM
4151
O
TYR
584
66.273
41.102
40.252
1.00
19.45


ATOM
4152
N
GLN
585
65.501
40.980
42.373
1.00
24.34


ATOM
4153
CA
GLN
585
66.581
41.736
43.014
1.00
25.79


ATOM
4154
CB
GLN
585
67.937
41.063
42.740
1.00
27.46


ATOM
4155
CG
GLN
585
69.106
41.754
43.433
1.00
30.44


ATOM
4156
CD
GLN
585
70.383
40.939
43.418
1.00
32.54


ATOM
4157
OE1
GLN
585
71.474
41.474
43.621
1.00
33.54


ATOM
4158
NE2
GLN
585
70.253
39.636
43.194
1.00
31.30


ATOM
4159
C
GLN
585
66.666
43.231
42.687
1.00
25.96


ATOM
4160
O
GLN
585
67.585
43.919
43.139
1.00
27.28


ATOM
4161
N
SER
586
65.707
43.747
41.924
1.00
24.70


ATOM
4162
CA
SER
586
65.716
45.165
41.577
1.00
25.28


ATOM
4163
CB
SER
586
64.829
45.436
40.365
1.00
24.97


ATOM
4164
OG
SER
586
64.667
46.834
40.178
1.00
25.13


ATOM
4165
C
SER
586
65.247
46.047
42.728
1.00
26.57


ATOM
4166
O
SER
586
64.072
46.026
43.103
1.00
26.45


ATOM
4167
N
LYS
587
66.167
46.832
43.277
1.00
25.12


ATOM
4168
CA
LYS
587
65.843
47.724
44.378
1.00
26.77


ATOM
4169
CB
LYS
587
67.126
48.207
45.067
1.00
26.74


ATOM
4170
CG
LYS
587
67.944
47.087
45.702
1.00
27.54


ATOM
4171
CD
LYS
587
67.119
46.297
46.712
1.00
27.45


ATOM
4172
CE
LYS
587
67.925
45.161
47.332
1.00
26.21


ATOM
4173
NZ
LYS
587
68.401
44.190
46.311
1.00
25.90


ATOM
4174
C
LYS
587
65.022
48.918
43.897
1.00
25.59


ATOM
4175
O
LYS
587
64.201
49.448
44.642
1.00
26.97


ATOM
4176
N
GLU
588
65.245
49.344
42.657
1.00
24.23


ATOM
4177
CA
GLU
588
64.496
50.467
42.104
1.00
25.34


ATOM
4178
CB
GLU
588
65.025
50.849
40.718
1.00
29.07


ATOM
4179
CG
GLU
588
66.440
51.417
40.693
1.00
34.67


ATOM
4180
CD
GLU
588
67.496
50.393
41.060
1.00
38.21


ATOM
4181
OE1
GLU
588
67.482
49.283
40.480
1.00
38.94


ATOM
4182
OE2
GLU
588
68.348
50.704
41.921
1.00
41.97


ATOM
4183
C
GLU
588
63.021
50.071
41.987
1.00
25.42


ATOM
4184
O
GLU
588
62.125
50.880
42.238
1.00
22.32


ATOM
4185
N
ALA
589
62.783
48.822
41.596
1.00
24.18


ATOM
4186
CA
ALA
589
61.426
48.306
41.452
1.00
24.57


ATOM
4187
CB
ALA
589
61.455
46.903
40.851
1.00
24.39


ATOM
4188
C
ALA
589
60.761
48.271
42.822
1.00
24.55


ATOM
4189
O
ALA
589
59.665
48.801
43.009
1.00
24.25


ATOM
4190
N
GLY
590
61.439
47.646
43.778
1.00
23.98


ATOM
4191
CA
GLY
590
60.902
47.551
45.121
1.00
26.42


ATOM
4192
C
GLY
590
60.582
48.897
45.746
1.00
27.69


ATOM
4193
O
GLY
590
59.577
49.039
46.442
1.00
28.18


ATOM
4194
N
GLN
591
61.429
49.890
45.500
1.00
27.79


ATOM
4195
CA
GLN
591
61.214
51.214
46.066
1.00
29.11


ATOM
4196
CB
GLN
591
62.376
52.143
45.715
1.00
31.76


ATOM
4197
CG
GLN
591
62.271
53.502
46.384
1.00
36.94


ATOM
4198
CD
GLN
591
62.181
53.386
47.896
1.00
41.21


ATOM
4199
OE1
GLN
591
63.116
52.925
48.554
1.00
44.17


ATOM
4200
NE2
GLN
591
61.048
53.795
48.454
1.00
43.27


ATOM
4201
C
GLN
591
59.904
51.843
45.600
1.00
28.84


ATOM
4202
O
GLN
591
59.228
52.522
46.371
1.00
26.01


ATOM
4203
N
ARG
592
59.547
51.625
44.340
1.00
28.52


ATOM
4204
CA
ARG
592
58.307
52.191
43.823
1.00
29.49


ATOM
4205
CB
ARG
592
58.258
52.089
42.298
1.00
30.74


ATOM
4206
CG
ARG
592
59.232
53.022
41.610
1.00
33.59


ATOM
4207
CD
ARG
592
58.864
53.215
40.162
1.00
34.84


ATOM
4208
NE
ARG
592
59.817
54.071
39.469
1.00
36.89


ATOM
4209
CZ
ARG
592
59.720
54.401
38.187
1.00
39.66


ATOM
4210
NH1
ARG
592
58.706
53.948
37.460
1.00
40.17


ATOM
4211
NH2
ARG
592
60.641
55.173
37.628
1.00
40.49


ATOM
4212
C
ARG
592
57.086
51.515
44.428
1.00
28.08


ATOM
4213
O
ARG
592
56.103
52.177
44.758
1.00
30.13


ATOM
4214
N
LEU
593
57.144
50.197
44.576
1.00
25.72


ATOM
4215
CA
LEU
593
56.028
49.468
45.162
1.00
24.31


ATOM
4216
CB
LEU
593
56.257
47.960
45.061
1.00
23.41


ATOM
4217
CG
LEU
593
56.003
47.293
43.710
1.00
24.09


ATOM
4218
CD1
LEU
593
56.340
45.814
43.814
1.00
22.31


ATOM
4219
CD2
LEU
593
54.541
47.482
43.309
1.00
24.13


ATOM
4220
C
LEU
593
55.856
49.851
46.630
1.00
24.61


ATOM
4221
O
LEU
593
54.734
50.014
47.113
1.00
22.28


ATOM
4222
N
ALA
594
56.979
49.994
47.327
1.00
22.88


ATOM
4223
CA
ALA
594
56.975
50.342
48.743
1.00
24.40


ATOM
4224
CB
ALA
594
58.400
50.304
49.299
1.00
23.81


ATOM
4225
C
ALA
594
56.350
51.704
49.016
1.00
23.79


ATOM
4226
O
ALA
594
55.480
51.824
49.878
1.00
24.99


ATOM
4227
N
THR
595
56.784
52.729
48.288
1.00
23.07


ATOM
4228
CA
THR
595
56.244
54.065
48.506
1.00
26.20


ATOM
4229
CB
THR
595
56.956
55.126
47.627
1.00
28.03


ATOM
4230
OG1
THR
595
56.705
54.861
46.242
1.00
35.56


ATOM
4231
CG2
THR
595
58.457
55.094
47.873
1.00
28.43


ATOM
4232
C
THR
595
54.745
54.092
48.218
1.00
25.47


ATOM
4233
O
THR
595
53.983
54.780
48.901
1.00
24.49


ATOM
4234
N
ALA
596
54.326
53.331
47.211
1.00
23.19


ATOM
4235
CA
ALA
596
52.918
53.265
46.846
1.00
22.32


ATOM
4236
CB
ALA
596
52.756
52.563
45.496
1.00
22.20


ATOM
4237
C
ALA
596
52.123
52.530
47.919
1.00
20.86


ATOM
4238
O
ALA
596
51.067
52.993
48.347
1.00
21.03


ATOM
4239
N
MET
597
52.631
51.385
48.362
1.00
20.23


ATOM
4240
CA
MET
597
51.930
50.608
49.376
1.00
20.17


ATOM
4241
CB
MET
597
52.610
49.249
49.581
1.00
18.97


ATOM
4242
CG
MET
597
52.435
48.280
48.412
1.00
18.62


ATOM
4243
SD
MET
597
53.001
46.611
48.797
1.00
20.81


ATOM
4244
CE
MET
597
54.714
46.755
48.344
1.00
18.21


ATOM
4245
C
MET
597
51.824
51.338
50.710
1.00
21.22


ATOM
4246
O
MET
597
50.834
51.194
51.426
1.00
19.46


ATOM
4247
N
LYS
598
52.839
52.128
51.039
1.00
22.34


ATOM
4248
CA
LYS
598
52.845
52.863
52.298
1.00
23.65


ATOM
4249
CB
LYS
598
54.194
53.565
52.492
1.00
23.93


ATOM
4250
CG
LYS
598
55.328
52.609
52.830
1.00
28.85


ATOM
4251
CD
LYS
598
56.610
53.354
53.162
1.00
31.84


ATOM
4252
CE
LYS
598
57.625
52.428
53.822
1.00
35.46


ATOM
4253
NZ
LYS
598
58.006
51.266
52.967
1.00
38.87


ATOM
4254
C
LYS
598
51.706
53.875
52.417
1.00
22.67


ATOM
4255
O
LYS
598
51.337
54.267
53.522
1.00
23.02


ATOM
4256
N
LEU
599
51.154
54.299
51.284
1.00
20.77


ATOM
4257
CA
LEU
599
50.050
55.257
51.290
1.00
20.03


ATOM
4258
CB
LEU
599
49.807
55.812
49.883
1.00
21.69


ATOM
4259
CG
LEU
599
50.838
56.754
49.260
1.00
22.59


ATOM
4260
CD1
LEU
599
50.420
57.074
47.835
1.00
22.70


ATOM
4261
CD2
LEU
599
50.947
58.026
50.085
1.00
22.77


ATOM
4262
C
LEU
599
48.757
54.614
51.784
1.00
20.21


ATOM
4263
O
LEU
599
47.834
55.306
52.219
1.00
19.40


ATOM
4264
N
GLY
600
48.690
53.290
51.717
1.00
20.15


ATOM
4265
CA
GLY
600
47.478
52.611
52.134
1.00
20.16


ATOM
4266
C
GLY
600
46.297
53.228
51.402
1.00
20.63


ATOM
4267
O
GLY
600
46.347
53.438
50.185
1.00
20.76


ATOM
4268
N
PHE
601
45.245
53.544
52.150
1.00
20.86


ATOM
4269
CA
PHE
601
44.031
54.143
51.593
1.00
21.23


ATOM
4270
CB
PHE
601
42.807
53.406
52.161
1.00
20.65


ATOM
4271
CG
PHE
601
41.509
53.733
51.470
1.00
24.23


ATOM
4272
CD1
PHE
601
41.340
53.471
50.115
1.00
25.84


ATOM
4273
CD2
PHE
601
40.449
54.283
52.183
1.00
24.34


ATOM
4274
CE1
PHE
601
40.130
53.751
49.479
1.00
28.01


ATOM
4275
CE2
PHE
601
39.233
54.568
51.557
1.00
27.29


ATOM
4276
CZ
PHE
601
39.075
54.300
50.202
1.00
26.47


ATOM
4277
C
PHE
601
43.972
55.632
51.961
1.00
20.30


ATOM
4278
O
PHE
601
42.899
56.230
51.999
1.00
21.85


ATOM
4279
N
SER
602
45.133
56.231
52.209
1.00
21.00


ATOM
4280
CA
SER
602
45.208
57.641
52.609
1.00
22.21


ATOM
4281
CB
SER
602
46.560
57.918
53.270
1.00
22.60


ATOM
4282
OG
SER
602
47.619
57.789
52.338
1.00
20.98


ATOM
4283
C
SER
602
44.982
58.679
51.506
1.00
23.68


ATOM
4284
O
SER
602
44.636
59.827
51.795
1.00
23.46


ATOM
4285
N
ARG
603
45.177
58.285
50.252
1.00
22.88


ATOM
4286
CA
ARG
603
45.005
59.207
49.130
1.00
25.54


ATOM
4287
CB
ARG
603
46.380
59.662
48.620
1.00
27.34


ATOM
4288
CG
ARG
603
47.247
60.373
49.654
1.00
31.36


ATOM
4289
CD
ARG
603
46.692
61.748
49.980
1.00
35.45


ATOM
4290
NE
ARG
603
46.606
62.585
48.784
1.00
40.01


ATOM
4291
CZ
ARG
603
46.063
63.799
48.754
1.00
42.24


ATOM
4292
NH1
ARG
603
45.552
64.329
49.857
1.00
44.20


ATOM
4293
NH2
ARG
603
46.029
64.483
47.618
1.00
41.85


ATOM
4294
C
ARG
603
44.243
58.549
47.981
1.00
23.92


ATOM
4295
O
ARG
603
44.199
57.330
47.884
1.00
24.89


ATOM
4296
N
PRO
604
43.623
59.353
47.101
1.00
24.43


ATOM
4297
CD
PRO
604
43.538
60.825
47.105
1.00
24.47


ATOM
4298
CA
PRO
604
42.881
58.785
45.967
1.00
23.43


ATOM
4299
CB
PRO
604
42.495
60.021
45.161
1.00
24.04


ATOM
4300
CG
PRO
604
42.327
61.076
46.235
1.00
24.67


ATOM
4301
C
PRO
604
43.856
57.874
45.217
1.00
22.52


ATOM
4302
O
PRO
604
45.017
58.241
45.026
1.00
19.66


ATOM
4303
N
TRP
605
43.397
56.702
44.784
1.00
21.06


ATOM
4304
CA
TRP
605
44.295
55.761
44.115
1.00
19.74


ATOM
4305
CB
TRP
605
43.547
54.478
43.719
1.00
17.20


ATOM
4306
CG
TRP
605
42.556
54.624
42.617
1.00
16.80


ATOM
4307
CD2
TRP
605
42.839
54.662
41.218
1.00
13.73


ATOM
4308
CE2
TRP
605
41.604
54.771
40.545
1.00
13.99


ATOM
4309
CE3
TRP
605
44.019
54.611
40.465
1.00
14.13


ATOM
4310
CD1
TRP
605
41.198
54.716
42.736
1.00
16.73


ATOM
4311
NE1
TRP
605
40.619
54.802
41.496
1.00
15.70


ATOM
4312
CZ2
TRP
605
41.514
54.835
39.153
1.00
12.90


ATOM
4313
CZ3
TRP
605
43.929
54.674
39.083
1.00
15.39


ATOM
4314
CH2
TRP
605
42.684
54.783
38.442
1.00
15.57


ATOM
4315
C
TRP
605
45.110
56.278
42.928
1.00
18.46


ATOM
4316
O
TRP
605
46.203
55.777
42.671
1.00
19.34


ATOM
4317
N
PRO
606
44.599
57.271
42.179
1.00
19.18


ATOM
4318
CD
PRO
606
43.257
57.880
42.148
1.00
18.96


ATOM
4319
CA
PRO
606
45.409
57.748
41.052
1.00
20.80


ATOM
4320
CB
PRO
606
44.583
58.910
40.507
1.00
20.75


ATOM
4321
CG
PRO
606
43.184
58.426
40.733
1.00
20.74


ATOM
4322
C
PRO
606
46.813
58.182
41.485
1.00
21.70


ATOM
4323
O
PRO
606
47.751
58.138
40.697
1.00
20.53


ATOM
4324
N
GLU
607
46.951
58.596
42.742
1.00
22.05


ATOM
4325
CA
GLU
607
48.250
59.020
43.250
1.00
23.78


ATOM
4326
CB
GLU
607
48.102
59.712
44.606
1.00
24.14


ATOM
4327
CG
GLU
607
47.576
61.128
44.482
1.00
30.40


ATOM
4328
CD
GLU
607
47.542
61.858
45.811
1.00
32.85


ATOM
4329
OE1
GLU
607
48.566
61.837
46.530
1.00
33.25


ATOM
4330
OE2
GLU
607
46.493
62.457
46.127
1.00
34.78


ATOM
4331
C
GLU
607
49.197
57.838
43.367
1.00
23.11


ATOM
4332
O
GLU
607
50.370
57.949
43.017
1.00
22.68


ATOM
4333
N
ALA
608
48.691
56.711
43.861
1.00
20.59


ATOM
4334
CA
ALA
608
49.514
55.513
43.984
1.00
21.79


ATOM
4335
CB
ALA
608
48.766
54.431
44.770
1.00
19.65


ATOM
4336
C
ALA
608
49.854
55.014
42.575
1.00
20.36


ATOM
4337
O
ALA
608
50.941
54.484
42.341
1.00
20.96


ATOM
4338
N
MET
609
48.922
55.191
41.641
1.00
19.66


ATOM
4339
CA
MET
609
49.139
54.772
40.257
1.00
19.69


ATOM
4340
CB
MET
609
47.873
54.978
39.425
1.00
19.14


ATOM
4341
CG
MET
609
48.052
54.689
37.933
1.00
17.12


ATOM
4342
SD
MET
609
48.510
52.964
37.574
1.00
19.73


ATOM
4343
CE
MET
609
46.861
52.188
37.611
1.00
15.34


ATOM
4344
C
MET
609
50.266
55.601
39.658
1.00
21.29


ATOM
4345
O
MET
609
51.131
55.080
38.956
1.00
21.89


ATOM
4346
N
GLN
610
50.244
56.899
39.945
1.00
22.60


ATOM
4347
CA
GLN
610
51.254
57.820
39.444
1.00
24.68


ATOM
4348
CB
GLN
610
50.880
59.253
39.810
1.00
28.02


ATOM
4349
CG
GLN
610
51.680
60.294
39.059
1.00
32.26


ATOM
4350
CD
GLN
610
50.791
61.215
38.261
1.00
34.82


ATOM
4351
OE1
GLN
610
50.166
62.126
38.805
1.00
37.92


ATOM
4352
NE2
GLN
610
50.709
60.969
36.962
1.00
39.74


ATOM
4353
C
GLN
610
52.628
57.493
40.018
1.00
25.43


ATOM
4354
O
GLN
610
53.626
57.492
39.297
1.00
26.39


ATOM
4355
N
LEU
611
52.677
57.221
41.318
1.00
25.09


ATOM
4356
CA
LEU
611
53.936
56.889
41.976
1.00
26.89


ATOM
4357
CB
LEU
611
53.704
56.624
43.466
1.00
28.27


ATOM
4358
CG
LEU
611
53.394
57.852
44.319
1.00
30.25


ATOM
4359
CD1
LEU
611
53.105
57.417
45.742
1.00
30.76


ATOM
4360
CD2
LEU
611
54.577
58.818
44.279
1.00
30.95


ATOM
4361
C
LEU
611
54.624
55.677
41.357
1.00
25.11


ATOM
4362
O
LEU
611
55.850
55.622
41.271
1.00
25.06


ATOM
4363
N
ILE
612
53.834
54.703
40.928
1.00
23.32


ATOM
4364
CA
ILE
612
54.394
53.497
40.339
1.00
22.85


ATOM
4365
CB
ILE
612
53.449
52.286
40.530
1.00
23.45


ATOM
4366
CG2
ILE
612
54.042
51.054
39.856
1.00
24.69


ATOM
4367
CG1
ILE
612
53.216
52.018
42.017
1.00
24.83


ATOM
4368
CD1
ILE
612
52.078
51.033
42.285
1.00
23.21


ATOM
4369
C
ILE
612
54.678
53.607
38.844
1.00
22.85


ATOM
4370
O
ILE
612
55.739
53.187
38.380
1.00
23.82


ATOM
4371
N
THR
613
53.736
54.179
38.099
1.00
22.01


ATOM
4372
CA
THR
613
53.846
54.262
36.642
1.00
22.05


ATOM
4373
CB
THR
613
52.552
53.740
35.993
1.00
20.57


ATOM
4374
OG1
THR
613
51.498
54.680
36.225
1.00
19.96


ATOM
4375
CG2
THR
613
52.151
52.397
36.600
1.00
17.72


ATOM
4376
C
THR
613
54.164
55.608
35.989
1.00
22.43


ATOM
4377
O
THR
613
54.456
55.660
34.796
1.00
22.71


ATOM
4378
N
GLY
614
54.095
56.696
36.743
1.00
24.21


ATOM
4379
CA
GLY
614
54.392
57.987
36.150
1.00
22.90


ATOM
4380
C
GLY
614
53.188
58.640
35.501
1.00
22.97


ATOM
4381
O
GLY
614
53.294
59.729
34.937
1.00
21.49


ATOM
4382
N
GLN
615
52.046
57.962
35.554
1.00
23.88


ATOM
4383
CA
GLN
615
50.802
58.502
35.012
1.00
21.95


ATOM
4384
CB
GLN
615
50.581
58.015
33.574
1.00
22.47


ATOM
4385
CG
GLN
615
50.505
56.523
33.379
1.00
22.03


ATOM
4386
CD
GLN
615
49.156
55.988
33.763
1.00
19.05


ATOM
4387
OE1
GLN
615
48.129
56.540
33.362
1.00
19.51


ATOM
4388
NE2
GLN
615
49.141
54.908
34.537
1.00
16.18


ATOM
4389
C
GLN
615
49.689
58.095
35.989
1.00
20.81


ATOM
4390
O
GLN
615
49.891
57.215
36.825
1.00
20.69


ATOM
4391
N
PRO
616
48.502
58.716
35.897
1.00
19.66


ATOM
4392
CD
PRO
616
48.157
59.932
35.138
1.00
21.70


ATOM
4393
CA
PRO
616
47.427
58.379
36.836
1.00
20.55


ATOM
4394
CB
PRO
616
46.908
59.751
37.209
1.00
20.89


ATOM
4395
CG
PRO
616
46.873
60.418
35.835
1.00
20.78


ATOM
4396
C
PRO
616
46.267
57.457
36.457
1.00
19.89


ATOM
4397
O
PRO
616
45.445
57.136
37.314
1.00
19.50


ATOM
4398
N
ASN
617
46.183
57.029
35.206
1.00
18.92


ATOM
4399
CA
ASN
617
45.051
56.199
34.799
1.00
20.34


ATOM
4400
CB
ASN
617
44.498
56.699
33.462
1.00
23.41


ATOM
4401
CG
ASN
617
44.426
58.205
33.391
1.00
26.99


ATOM
4402
OD1
ASN
617
44.083
58.855
34.377
1.00
31.32


ATOM
4403
ND2
ASN
617
44.732
58.761
32.219
1.00
31.42


ATOM
4404
C
ASN
617
45.303
54.708
34.664
1.00
17.45


ATOM
4405
O
ASN
617
46.445
54.250
34.621
1.00
17.50


ATOM
4406
N
MET
618
44.208
53.957
34.603
1.00
16.22


ATOM
4407
CA
MET
618
44.279
52.520
34.387
1.00
17.60


ATOM
4408
CB
MET
618
42.982
51.821
34.807
1.00
14.99


ATOM
4409
CG
MET
618
42.792
51.646
36.305
1.00
15.84


ATOM
4410
SD
MET
618
41.282
50.709
36.700
1.00
17.39


ATOM
4411
CE
MET
618
40.045
51.984
36.543
1.00
20.05


ATOM
4412
C
MET
618
44.402
52.465
32.872
1.00
16.95


ATOM
4413
O
MET
618
43.843
53.315
32.178
1.00
16.75


ATOM
4414
N
SER
619
45.117
51.480
32.351
1.00
16.04


ATOM
4415
CA
SER
619
45.286
51.385
30.904
1.00
16.02


ATOM
4416
CB
SER
619
46.420
52.314
30.449
1.00
16.02


ATOM
4417
OG
SER
619
46.691
52.155
29.067
1.00
19.66


ATOM
4418
C
SER
619
45.617
49.965
30.495
1.00
15.40


ATOM
4419
O
SER
619
46.400
49.297
31.161
1.00
14.10


ATOM
4420
N
ALA
620
45.024
49.516
29.392
1.00
15.67


ATOM
4421
CA
ALA
620
45.265
48.173
28.880
1.00
17.19


ATOM
4422
CB
ALA
620
44.053
47.695
28.092
1.00
15.24


ATOM
4423
C
ALA
620
46.509
48.124
27.991
1.00
17.50


ATOM
4424
O
ALA
620
46.909
47.052
27.533
1.00
16.59


ATOM
4425
N
SER
621
47.124
49.282
27.755
1.00
19.02


ATOM
4426
CA
SER
621
48.310
49.356
26.896
1.00
20.17


ATOM
4427
CB
SER
621
48.839
50.791
26.838
1.00
19.94


ATOM
4428
OG
SER
621
47.940
51.611
26.112
1.00
28.11


ATOM
4429
C
SER
621
49.443
48.420
27.296
1.00
18.71


ATOM
4430
O
SER
621
50.023
47.752
26.448
1.00
19.01


ATOM
4431
N
ALA
622
49.761
48.373
28.584
1.00
18.30


ATOM
4432
CA
ALA
622
50.841
47.513
29.060
1.00
17.71


ATOM
4433
CB
ALA
622
51.067
47.741
30.557
1.00
17.13


ATOM
4434
C
ALA
622
50.554
46.034
28.784
1.00
16.19


ATOM
4435
O
ALA
622
51.410
45.305
28.271
1.00
16.07


ATOM
4436
N
MET
623
49.350
45.591
29.122
1.00
15.56


ATOM
4437
CA
MET
623
48.974
44.202
28.899
1.00
15.10


ATOM
4438
CB
MET
623
47.580
43.931
29.475
1.00
15.03


ATOM
4439
CG
MET
623
47.133
42.489
29.348
1.00
18.59


ATOM
4440
SD
MET
623
45.530
42.188
30.123
1.00
19.23


ATOM
4441
CE
MET
623
45.854
40.606
30.925
1.00
19.84


ATOM
4442
C
MET
623
49.008
43.868
27.402
1.00
16.05


ATOM
4443
O
MET
623
49.480
42.802
27.012
1.00
17.32


ATOM
4444
N
LEU
624
48.508
44.774
26.566
1.00
15.21


ATOM
4445
CA
LEU
624
48.515
44.543
25.120
1.00
18.46


ATOM
4446
CB
LEU
624
47.735
45.649
24.396
1.00
19.41


ATOM
4447
CG
LEU
624
46.220
45.664
24.628
1.00
22.76


ATOM
4448
CD1
LEU
624
45.576
46.786
23.827
1.00
21.15


ATOM
4449
CD2
LEU
624
45.634
44.315
24.214
1.00
24.62


ATOM
4450
C
LEU
624
49.956
44.487
24.598
1.00
19.43


ATOM
4451
O
LEU
624
50.295
43.655
23.751
1.00
18.79


ATOM
4452
N
SER
625
50.802
45.375
25.112
1.00
19.19


ATOM
4453
CA
SER
625
52.208
45.418
24.717
1.00
19.92


ATOM
4454
CB
SER
625
52.891
46.612
25.402
1.00
22.10


ATOM
4455
OG
SER
625
54.286
46.618
25.176
1.00
27.80


ATOM
4456
C
SER
625
52.892
44.100
25.113
1.00
18.98


ATOM
4457
O
SER
625
53.667
43.525
24.345
1.00
19.48


ATOM
4458
N
TYR
626
52.600
43.623
26.316
1.00
17.23


ATOM
4459
CA
TYR
626
53.169
42.370
26.803
1.00
17.45


ATOM
4460
CB
TYR
626
52.626
42.070
28.203
1.00
17.03


ATOM
4461
CG
TYR
626
53.131
40.783
28.824
1.00
16.24


ATOM
4462
CD1
TYR
626
54.122
40.798
29.806
1.00
18.36


ATOM
4463
CE1
TYR
626
54.560
39.612
30.412
1.00
16.21


ATOM
4464
CD2
TYR
626
52.590
39.551
28.454
1.00
16.60


ATOM
4465
CE2
TYR
626
53.018
38.367
29.046
1.00
15.67


ATOM
4466
CZ
TYR
626
53.998
38.402
30.026
1.00
17.59


ATOM
4467
OH
TYR
626
54.385
37.225
30.630
1.00
17.16


ATOM
4468
C
TYR
626
52.820
41.206
25.858
1.00
18.35


ATOM
4469
O
TYR
626
53.676
40.379
25.534
1.00
17.96


ATOM
4470
N
PHE
627
51.564
41.151
25.416
1.00
17.36


ATOM
4471
CA
PHE
627
51.108
40.071
24.538
1.00
18.59


ATOM
4472
CB
PHE
627
49.679
39.657
24.914
1.00
15.88


ATOM
4473
CG
PHE
627
49.585
38.913
26.208
1.00
15.40


ATOM
4474
CD1
PHE
627
49.150
39.552
27.366
1.00
15.71


ATOM
4475
CD2
PHE
627
49.952
37.573
26.278
1.00
15.04


ATOM
4476
CE1
PHE
627
49.081
38.864
28.579
1.00
14.00


ATOM
4477
CE2
PHE
627
49.889
36.874
27.483
1.00
15.01


ATOM
4478
CZ
PHE
627
49.453
37.519
28.636
1.00
14.97


ATOM
4479
C
PHE
627
51.151
40.323
23.030
1.00
18.84


ATOM
4480
O
PHE
627
50.741
39.464
22.254
1.00
19.04


ATOM
4481
N
LYS
628
51.644
41.484
22.612
1.00
19.54


ATOM
4482
CA
LYS
628
51.705
41.819
21.190
1.00
19.75


ATOM
4483
CB
LYS
628
52.556
43.079
20.989
1.00
22.03


ATOM
4484
CG
LYS
628
52.868
43.419
19.532
1.00
23.91


ATOM
4485
CD
LYS
628
51.621
43.760
18.727
1.00
27.23


ATOM
4486
CE
LYS
628
52.002
44.196
17.306
1.00
30.31


ATOM
4487
NZ
LYS
628
50.817
44.449
16.440
1.00
30.49


ATOM
4488
C
LYS
628
52.217
40.692
20.283
1.00
20.01


ATOM
4489
O
LYS
628
51.584
40.365
19.281
1.00
21.94


ATOM
4490
N
PRO
629
53.369
40.087
20.611
1.00
20.55


ATOM
4491
CD
PRO
629
54.306
40.351
21.717
1.00
22.46


ATOM
4492
CA
PRO
629
53.867
39.008
19.749
1.00
21.49


ATOM
4493
CB
PRO
629
55.151
38.566
20.450
1.00
21.82


ATOM
4494
CG
PRO
629
55.607
39.818
21.155
1.00
23.13


ATOM
4495
C
PRO
629
52.857
37.867
19.613
1.00
20.35


ATOM
4496
O
PRO
629
52.732
37.256
18.553
1.00
19.97


ATOM
4497
N
LEU
630
52.131
37.583
20.687
1.00
19.10


ATOM
4498
CA
LEU
630
51.150
36.510
20.649
1.00
18.86


ATOM
4499
CB
LEU
630
50.695
36.135
22.059
1.00
17.73


ATOM
4500
CG
LEU
630
49.725
34.946
22.116
1.00
18.16


ATOM
4501
CD1
LEU
630
50.447
33.682
21.698
1.00
17.06


ATOM
4502
CD2
LEU
630
49.167
34.789
23.525
1.00
17.08


ATOM
4503
C
LEU
630
49.945
36.906
19.807
1.00
18.76


ATOM
4504
O
LEU
630
49.448
36.106
19.016
1.00
20.28


ATOM
4505
N
LEU
631
49.480
38.140
19.972
1.00
18.81


ATOM
4506
CA
LEU
631
48.332
38.617
19.207
1.00
19.95


ATOM
4507
CB
LEU
631
48.025
40.079
19.543
1.00
18.70


ATOM
4508
CG
LEU
631
46.896
40.731
18.735
1.00
21.74


ATOM
4509
CD1
LEU
631
45.584
40.002
18.990
1.00
23.52


ATOM
4510
CD2
LEU
631
46.766
42.196
19.119
1.00
22.39


ATOM
4511
C
LEU
631
48.599
38.482
17.709
1.00
21.61


ATOM
4512
O
LEU
631
47.725
38.048
16.955
1.00
18.83


ATOM
4513
N
ASP
632
49.804
38.855
17.281
1.00
21.33


ATOM
4514
CA
ASP
632
50.160
38.756
15.869
1.00
21.95


ATOM
4515
CB
ASP
632
51.525
39.405
15.604
1.00
23.60


ATOM
4516
CG
ASP
632
51.516
40.903
15.839
1.00
24.22


ATOM
4517
OD1
ASP
632
50.469
41.541
15.604
1.00
26.63


ATOM
4518
OD2
ASP
632
52.562
41.447
16.243
1.00
26.55


ATOM
4519
C
ASP
632
50.197
37.293
15.425
1.00
21.32


ATOM
4520
O
ASP
632
49.742
36.964
14.330
1.00
20.49


ATOM
4521
N
TRP
633
50.736
36.418
16.271
1.00
19.81


ATOM
4522
CA
TRP
633
50.808
34.998
15.929
1.00
20.07


ATOM
4523
CB
TRP
633
51.595
34.213
16.987
1.00
19.94


ATOM
4524
CG
TRP
633
51.761
32.756
16.632
1.00
21.13


ATOM
4525
CD2
TRP
633
50.902
31.674
17.019
1.00
21.92


ATOM
4526
CE2
TRP
633
51.389
30.505
16.388
1.00
22.13


ATOM
4527
CE3
TRP
633
49.766
31.578
17.836
1.00
22.40


ATOM
4528
CD1
TRP
633
52.712
32.211
15.807
1.00
22.30


ATOM
4529
NE1
TRP
633
52.492
30.860
15.656
1.00
21.61


ATOM
4530
CZ2
TRP
633
50.779
29.255
16.549
1.00
22.73


ATOM
4531
CZ3
TRP
633
49.158
30.333
17.996
1.00
23.58


ATOM
4532
CH2
TRP
633
49.669
29.189
17.354
1.00
24.12


ATOM
4533
C
TRP
633
49.402
34.407
15.817
1.00
20.16


ATOM
4534
O
TRP
633
49.120
33.624
14.908
1.00
20.21


ATOM
4535
N
LEU
634
48.528
34.788
16.745
1.00
18.10


ATOM
4536
CA
LEU
634
47.152
34.291
16.767
1.00
17.96


ATOM
4537
CB
LEU
634
46.433
34.766
18.033
1.00
13.19


ATOM
4538
CG
LEU
634
46.823
34.058
19.331
1.00
15.98


ATOM
4539
CD1
LEU
634
46.121
34.731
20.512
1.00
15.76


ATOM
4540
CD2
LEU
634
46.433
32.585
19.242
1.00
17.65


ATOM
4541
C
LEU
634
46.358
34.720
15.543
1.00
17.44


ATOM
4542
O
LEU
634
45.597
33.934
14.982
1.00
18.04


ATOM
4543
N
ARG
635
46.522
35.971
15.135
1.00
19.17


ATOM
4544
CA
ARG
635
45.809
36.459
13.965
1.00
20.10


ATOM
4545
CB
ARG
635
46.057
37.955
13.776
1.00
21.85


ATOM
4546
CG
ARG
635
45.154
38.812
14.644
1.00
25.01


ATOM
4547
CD
ARG
635
45.529
40.272
14.572
1.00
29.62


ATOM
4548
NE
ARG
635
44.548
41.106
15.260
1.00
33.26


ATOM
4549
CZ
ARG
635
44.745
42.381
15.571
1.00
34.54


ATOM
4550
NH1
ARG
635
45.895
42.969
15.259
1.00
35.00


ATOM
4551
NH2
ARG
635
43.791
43.069
16.185
1.00
36.75


ATOM
4552
C
ARG
635
46.240
35.688
12.728
1.00
19.78


ATOM
4553
O
ARG
635
45.404
35.275
11.930
1.00
19.55


ATOM
4554
N
THR
636
47.544
35.485
12.577
1.00
20.54


ATOM
4555
CA
THR
636
48.067
34.745
11.431
1.00
21.78


ATOM
4556
CB
THR
636
49.604
34.749
11.430
1.00
22.60


ATOM
4557
OG1
THR
636
50.072
36.101
11.362
1.00
26.06


ATOM
4558
CG2
THR
636
50.142
33.960
10.241
1.00
23.85


ATOM
4559
C
THR
636
47.579
33.296
11.463
1.00
20.62


ATOM
4560
O
THR
636
47.170
32.747
10.439
1.00
19.63


ATOM
4561
N
GLU
637
47.619
32.684
12.643
1.00
19.42


ATOM
4562
CA
GLU
637
47.176
31.299
12.804
1.00
18.86


ATOM
4563
CB
GLU
637
47.517
30.791
14.211
1.00
19.68


ATOM
4564
CG
GLU
637
46.993
29.385
14.533
1.00
20.95


ATOM
4565
CD
GLU
637
47.704
28.278
13.757
1.00
24.76


ATOM
4566
OE1
GLU
637
48.584
28.589
12.924
1.00
25.29


ATOM
4567
OE2
GLU
637
47.379
27.091
13.984
1.00
25.20


ATOM
4568
C
GLU
637
45.676
31.152
12.553
1.00
17.40


ATOM
4569
O
GLU
637
45.258
30.279
11.794
1.00
18.84


ATOM
4570
N
ASN
638
44.867
32.001
13.183
1.00
17.45


ATOM
4571
CA
ASN
638
43.416
31.928
13.006
1.00
17.49


ATOM
4572
CB
ASN
638
42.691
32.889
13.962
1.00
15.50


ATOM
4573
CG
ASN
638
42.730
32.411
15.408
1.00
16.54


ATOM
4574
OD1
ASN
638
42.820
31.209
15.674
1.00
15.31


ATOM
4575
ND2
ASN
638
42.652
33.348
16.348
1.00
12.94


ATOM
4576
C
ASN
638
43.015
32.235
11.571
1.00
18.74


ATOM
4577
O
ASN
638
42.067
31.655
11.039
1.00
16.61


ATOM
4578
N
GLU
639
43.748
33.147
10.944
1.00
20.32


ATOM
4579
CA
GLU
639
43.468
33.530
9.566
1.00
22.55


ATOM
4580
CB
GLU
639
44.335
34.729
9.178
1.00
23.65


ATOM
4581
CG
GLU
639
44.290
35.079
7.704
1.00
30.44


ATOM
4582
CD
GLU
639
45.149
36.284
7.386
1.00
33.49


ATOM
4583
OE1
GLU
639
44.809
37.389
7.863
1.00
34.20


ATOM
4584
OE2
GLU
639
46.166
36.122
6.675
1.00
33.48


ATOM
4585
C
GLU
639
43.703
32.382
8.581
1.00
22.09


ATOM
4586
O
GLU
639
42.873
32.118
7.712
1.00
21.43


ATOM
4587
N
LEU
640
44.825
31.688
8.722
1.00
22.49


ATOM
4588
CA
LEU
640
45.118
30.600
7.801
1.00
24.32


ATOM
4589
CB
LEU
640
46.576
30.150
7.956
1.00
25.56


ATOM
4590
CG
LEU
640
47.046
29.348
9.162
1.00
26.95


ATOM
4591
CD1
LEU
640
46.720
27.878
8.949
1.00
27.03


ATOM
4592
CD2
LEU
640
48.555
29.519
9.316
1.00
29.34


ATOM
4593
C
LEU
640
44.149
29.426
7.953
1.00
23.29


ATOM
4594
O
LEU
640
43.985
28.631
7.027
1.00
22.55


ATOM
4595
N
HIS
641
43.495
29.327
9.110
1.00
21.91


ATOM
4596
CA
HIS
641
42.524
28.263
9.339
1.00
22.74


ATOM
4597
CB
HIS
641
42.622
27.728
10.772
1.00
23.20


ATOM
4598
CG
HIS
641
43.812
26.856
11.000
1.00
24.45


ATOM
4599
CD2
HIS
641
44.112
25.623
10.530
1.00
25.66


ATOM
4600
ND1
HIS
641
44.894
27.252
11.756
1.00
28.28


ATOM
4601
CE1
HIS
641
45.810
26.301
11.742
1.00
26.29


ATOM
4602
NE2
HIS
641
45.360
25.302
11.005
1.00
29.81


ATOM
4603
C
HIS
641
41.106
28.747
9.071
1.00
23.10


ATOM
4604
O
HIS
641
40.145
27.988
9.217
1.00
22.01


ATOM
4605
N
GLY
642
40.986
30.012
8.678
1.00
22.53


ATOM
4606
CA
GLY
642
39.683
30.582
8.381
1.00
22.30


ATOM
4607
C
GLY
642
38.729
30.590
9.561
1.00
23.68


ATOM
4608
O
GLY
642
37.544
30.277
9.416
1.00
22.74


ATOM
4609
N
GLU
643
39.233
30.950
10.735
1.00
21.41


ATOM
4610
CA
GLU
643
38.386
30.981
11.919
1.00
21.09


ATOM
4611
CB
GLU
643
39.235
31.103
13.188
1.00
18.57


ATOM
4612
CG
GLU
643
40.322
30.051
13.336
1.00
18.36


ATOM
4613
CD
GLU
643
39.780
28.639
13.541
1.00
16.54


ATOM
4614
OE1
GLU
643
38.545
28.441
13.509
1.00
16.76


ATOM
4615
OE2
GLU
643
40.604
27.724
13.733
1.00
18.63


ATOM
4616
C
GLU
643
37.407
32.147
11.872
1.00
22.46


ATOM
4617
O
GLU
643
37.727
33.230
11.371
1.00
23.79


ATOM
4618
N
LYS
644
36.207
31.910
12.386
1.00
21.56


ATOM
4619
CA
LYS
644
35.180
32.938
12.472
1.00
22.52


ATOM
4620
CB
LYS
644
33.816
32.367
12.090
1.00
25.95


ATOM
4621
CG
LYS
644
32.662
33.335
12.296
1.00
32.66


ATOM
4622
CD
LYS
644
31.336
32.666
11.974
1.00
37.37


ATOM
4623
CE
LYS
644
30.164
33.603
12.192
1.00
38.64


ATOM
4624
NZ
LYS
644
28.883
32.959
11.777
1.00
42.06


ATOM
4625
C
LYS
644
35.170
33.347
13.940
1.00
22.34


ATOM
4626
O
LYS
644
34.633
32.626
14.779
1.00
22.63


ATOM
4627
N
LEU
645
35.777
34.490
14.250
1.00
21.01


ATOM
4628
CA
LEU
645
35.846
34.965
15.630
1.00
21.37


ATOM
4629
CB
LEU
645
36.662
36.251
15.721
1.00
19.95


ATOM
4630
CG
LEU
645
38.110
36.202
15.233
1.00
21.57


ATOM
4631
CD1
LEU
645
38.774
37.542
15.513
1.00
22.47


ATOM
4632
CD2
LEU
645
38.859
35.084
15.927
1.00
19.75


ATOM
4633
C
LEU
645
34.470
35.217
16.215
1.00
21.96


ATOM
4634
O
LEU
645
33.546
35.613
15.508
1.00
20.21


ATOM
4635
N
GLY
646
34.339
34.987
17.517
1.00
21.25


ATOM
4636
CA
GLY
646
33.065
35.214
18.167
1.00
20.02


ATOM
4637
C
GLY
646
32.117
34.037
18.080
1.00
21.85


ATOM
4638
O
GLY
646
32.516
32.919
17.748
1.00
19.09


ATOM
4639
N
TRP
647
30.850
34.302
18.369
1.00
22.45


ATOM
4640
CA
TRP
647
29.828
33.268
18.356
1.00
28.97


ATOM
4641
CB
TRP
647
29.778
32.601
19.734
1.00
23.61


ATOM
4642
CG
TRP
647
29.902
33.584
20.866
1.00
21.96


ATOM
4643
CD2
TRP
647
31.119
34.062
21.459
1.00
19.96


ATOM
4644
CE2
TRP
647
30.761
35.004
22.452
1.00
19.26


ATOM
4645
CE3
TRP
647
32.480
33.787
21.247
1.00
18.03


ATOM
4646
CD1
TRP
647
28.883
34.238
21.507
1.00
20.08


ATOM
4647
NE1
TRP
647
29.392
35.089
22.460
1.00
19.39


ATOM
4648
CZ2
TRP
647
31.713
35.675
23.231
1.00
17.35


ATOM
4649
CZ3
TRP
647
33.428
34.453
22.022
1.00
19.00


ATOM
4650
CH2
TRP
647
33.037
35.389
23.005
1.00
18.89


ATOM
4651
C
TRP
647
28.462
33.843
17.983
1.00
34.48


ATOM
4652
O
TRP
647
27.676
34.217
18.849
1.00
35.78


ATOM
4653
N
PRO
648
28.166
33.914
16.675
1.00
41.48


ATOM
4654
CD
PRO
648
28.952
33.316
15.580
1.00
42.76


ATOM
4655
CA
PRO
648
26.895
34.443
16.166
1.00
44.45


ATOM
4656
CB
PRO
648
27.033
34.263
14.656
1.00
45.15


ATOM
4657
CG
PRO
648
27.883
33.024
14.556
1.00
44.87


ATOM
4658
C
PRO
648
25.679
33.707
16.726
1.00
46.65


ATOM
4659
O
PRO
648
24.898
34.348
17.458
1.00
48.64


ATOM
4660
OXT
PRO
648
25.526
32.501
16.429
1.00
48.70


ATOM
4661
OH2
WAT
705
33.725
46.851
44.246
1.00
15.53


ATOM
4662
OH2
WAT
706
32.992
26.241
34.112
1.00
12.73


ATOM
4663
OH2
WAT
707
24.332
47.645
41.904
1.00
11.04


ATOM
4664
OH2
WAT
708
41.493
22.764
37.711
1.00
14.46


ATOM
4665
OH2
WAT
709
57.554
41.574
37.486
1.00
16.47


ATOM
4666
OH2
WAT
710
39.385
24.084
39.045
1.00
16.57


ATOM
4667
OH2
WAT
711
51.141
36.659
37.992
1.00
13.96


ATOM
4668
OH2
WAT
712
53.148
51.275
33.059
1.00
23.13


ATOM
4669
OH2
WAT
713
52.416
34.580
36.566
1.00
18.04


ATOM
4670
OH2
WAT
714
16.540
45.049
50.781
1.00
15.93


ATOM
4671
OH2
WAT
715
47.597
46.867
31.105
1.00
15.09


ATOM
4672
OH2
WAT
716
33.726
54.353
42.506
1.00
17.24


ATOM
4673
OH2
WAT
717
33.205
41.739
37.987
1.00
14.76


ATOM
4674
OH2
WAT
718
37.109
27.771
45.829
1.00
18.94


ATOM
4675
OH2
WAT
719
17.460
40.837
43.030
1.00
16.41


ATOM
4676
OH2
WAT
720
40.996
49.596
48.874
1.00
12.40


ATOM
4677
OH2
WAT
721
37.232
33.021
29.678
1.00
13.93


ATOM
4678
OH2
WAT
722
48.355
52.277
48.594
1.00
16.39


ATOM
4679
OH2
WAT
723
44.253
25.373
17.456
1.00
17.05


ATOM
4680
OH2
WAT
724
37.616
28.428
16.196
1.00
14.22


ATOM
4681
OH2
WAT
725
31.807
45.250
42.894
1.00
12.95


ATOM
4682
OH2
WAT
726
48.929
40.765
46.120
1.00
16.42


ATOM
4683
OH2
WAT
727
43.001
28.525
14.577
1.00
19.16


ATOM
4684
OH2
WAT
728
36.297
33.649
19.024
1.00
16.26


ATOM
4685
OH2
WAT
729
45.223
39.419
41.235
1.00
17.97


ATOM
4686
OH2
WAT
730
19.069
49.921
43.313
1.00
22.26


ATOM
4687
OH2
WAT
731
18.652
48.396
47.732
1.00
19.58


ATOM
4688
OH2
WAT
732
16.355
39.332
47.441
1.00
16.61


ATOM
4689
OH2
WAT
734
27.725
37.511
46.838
1.00
11.65


ATOM
4690
OH2
WAT
735
43.139
43.055
22.306
1.00
14.35


ATOM
4691
OH2
WAT
736
23.288
50.618
41.612
1.00
18.93


ATOM
4692
OH2
WAT
737
40.575
28.769
39.893
1.00
24.17


ATOM
4693
OH2
WAT
738
44.624
45.246
56.395
1.00
17.22


ATOM
4694
OH2
WAT
739
42.886
25.680
33.406
1.00
14.64


ATOM
4695
OH2
WAT
740
36.434
24.093
32.323
1.00
12.11


ATOM
4696
OH2
WAT
741
39.736
39.843
47.740
1.00
17.61


ATOM
4697
OH2
WAT
742
47.972
45.541
61.312
1.00
27.55


ATOM
4698
OH2
WAT
743
48.595
42.613
62.331
1.00
19.33


ATOM
4699
OH2
WAT
744
16.756
44.276
47.836
1.00
17.52


ATOM
4700
OH2
WAT
745
50.833
52.475
32.781
1.00
22.48


ATOM
4701
OH2
WAT
746
43.086
51.380
39.452
1.00
19.50


ATOM
4702
OH2
WAT
747
43.065
37.312
51.242
1.00
19.15


ATOM
4703
OH2
WAT
748
36.377
29.551
43.539
1.00
26.33


ATOM
4704
OH2
WAT
749
31.749
23.341
13.589
1.00
21.93


ATOM
4705
OH2
WAT
750
51.017
32.405
13.102
1.00
23.70


ATOM
4706
OH2
WAT
751
23.902
25.063
40.491
1.00
17.23


ATOM
4707
OH2
WAT
752
46.245
55.817
48.913
1.00
17.11


ATOM
4708
OH2
WAT
753
17.325
38.625
44.796
1.00
17.92


ATOM
4709
OH2
WAT
754
30.477
54.512
37.203
1.00
19.17


ATOM
4710
OH2
WAT
755
30.153
29.098
39.015
1.00
13.90


ATOM
4711
OH2
WAT
756
40.602
56.391
45.574
1.00
29.30


ATOM
4712
OH2
WAT
757
48.469
46.405
58.796
1.00
20.34


ATOM
4713
OH2
WAT
758
23.341
22.303
39.374
1.00
19.80


ATOM
4714
OH2
WAT
759
39.109
29.949
42.113
1.00
17.81


ATOM
4715
OH2
WAT
760
41.617
55.292
34.623
1.00
19.28


ATOM
4716
OH2
WAT
761
50.433
32.980
35.395
1.00
27.78


ATOM
4717
OH2
WAT
762
55.349
39.853
51.988
1.00
21.56


ATOM
4718
OH2
WAT
763
17.829
47.302
45.052
1.00
19.63


ATOM
4719
OH2
WAT
764
41.437
43.591
47.417
1.00
17.87


ATOM
4720
OH2
WAT
765
31.453
48.234
33.459
1.00
20.09


ATOM
4721
OH2
WAT
766
35.895
29.226
13.339
1.00
19.08


ATOM
4722
OH2
WAT
767
42.129
47.247
49.577
1.00
21.96


ATOM
4723
OH2
WAT
768
39.938
19.646
28.365
1.00
16.90


ATOM
4724
OH2
WAT
770
53.052
28.858
13.534
1.00
29.07


ATOM
4725
OH2
WAT
771
39.487
58.074
40.481
1.00
19.31


ATOM
4726
OH2
WAT
772
34.677
20.856
49.093
1.00
29.57


ATOM
4727
OH2
WAT
773
17.419
31.215
38.280
1.00
27.38


ATOM
4728
OH2
WAT
774
44.543
23.939
14.013
1.00
24.17


ATOM
4729
OH2
WAT
775
31.307
56.780
49.243
1.00
27.95


ATOM
4730
OH2
WAT
776
46.870
56.616
46.429
1.00
26.71


ATOM
4731
OH2
WAT
777
43.022
58.359
37.108
1.00
24.23


ATOM
4732
OH2
WAT
778
40.838
33.568
7.092
1.00
29.87


ATOM
4733
OH2
WAT
779
35.280
52.569
73.408
1.00
30.56


ATOM
4734
OH2
WAT
780
14.847
39.443
36.394
1.00
22.09


ATOM
4735
OH2
WAT
781
39.543
32.050
52.976
1.00
16.43


ATOM
4736
OH2
WAT
782
27.658
50.202
53.322
1.00
36.66


ATOM
4737
OH2
WAT
783
49.665
26.157
11.610
1.00
31.59


ATOM
4738
OH2
WAT
784
44.790
26.439
15.055
1.00
18.95


ATOM
4739
OH2
WAT
785
57.915
38.932
52.077
1.00
23.38


ATOM
4740
OH2
WAT
786
34.219
51.188
61.855
1.00
27.39


ATOM
4741
OH2
WAT
788
43.520
51.469
28.053
1.00
23.51


ATOM
4742
OH2
WAT
789
20.741
25.871
29.764
1.00
25.31


ATOM
4743
OH2
WAT
790
31.996
32.524
15.060
1.00
27.33


ATOM
4744
OH2
WAT
791
50.065
48.521
23.797
1.00
22.69


ATOM
4745
OH2
WAT
793
40.065
53.867
45.877
1.00
28.99


ATOM
4746
OH2
WAT
794
27.500
14.226
27.489
1.00
25.41


ATOM
4747
OH2
WAT
795
40.088
34.807
11.689
1.00
31.73


ATOM
4748
OH2
WAT
796
39.102
11.125
33.545
1.00
21.19


ATOM
4749
OH2
WAT
797
27.472
21.519
51.557
1.00
21.90


ATOM
4750
OH2
WAT
798
66.482
40.320
37.672
1.00
26.30


ATOM
4751
OH2
WAT
799
22.957
49.917
38.951
1.00
28.18


ATOM
4752
OH2
WAT
800
26.175
37.519
64.945
1.00
35.81


ATOM
4753
OH2
WAT
801
34.181
10.599
28.257
1.00
20.76


ATOM
4754
OH2
WAT
802
59.869
33.554
44.206
1.00
24.54


ATOM
4755
OH2
WAT
803
38.591
20.686
31.734
1.00
19.19


ATOM
4756
OH2
WAT
804
40.781
21.352
12.247
1.00
34.63


ATOM
4757
OH2
WAT
805
56.133
41.425
25.091
1.00
22.31


ATOM
4758
OH2
WAT
806
37.118
27.351
50.493
1.00
21.88


ATOM
4759
OH2
WAT
807
42.654
46.736
21.378
1.00
21.89


ATOM
4760
OH2
WAT
808
35.150
28.150
10.834
1.00
28.45


ATOM
4761
OH2
WAT
809
29.291
19.889
23.346
1.00
24.18


ATOM
4762
OH2
WAT
810
52.883
51.977
57.763
1.00
29.06


ATOM
4763
OH2
WAT
811
53.403
37.618
61.414
1.00
27.12


ATOM
4764
OH2
WAT
812
11.989
35.114
47.917
1.00
33.35


ATOM
4765
OH2
WAT
813
25.177
49.091
37.779
1.00
23.88


ATOM
4766
OH2
WAT
814
43.929
19.517
20.685
1.00
25.16


ATOM
4767
OH2
WAT
815
36.157
15.297
14.633
1.00
24.52


ATOM
4768
OH2
WAT
816
35.907
12.552
25.672
1.00
25.39


ATOM
4769
OH2
WAT
817
39.592
55.524
36.450
1.00
25.79


ATOM
4770
OH2
WAT
818
62.649
34.290
30.290
1.00
24.83


ATOM
4771
OH2
WAT
819
19.911
55.424
50.600
1.00
37.80


ATOM
4772
OH2
WAT
820
50.799
29.874
12.353
1.00
25.54


ATOM
4773
OH2
WAT
821
27.864
56.624
70.138
1.00
27.58


ATOM
4774
OH2
WAT
823
27.817
17.957
50.119
1.00
32.04


ATOM
4775
OH2
WAT
824
56.121
37.459
32.732
1.00
21.41


ATOM
4776
OH2
WAT
825
9.453
31.180
47.871
1.00
51.79


ATOM
4777
OH2
WAT
826
41.647
54.559
62.566
1.00
39.79


ATOM
4778
OH2
WAT
827
50.893
18.450
23.970
1.00
27.60


ATOM
4779
OH2
WAT
828
26.079
14.620
12.464
1.00
24.55


ATOM
4780
OH2
WAT
829
69.963
44.562
41.439
1.00
32.79


ATOM
4781
OH2
WAT
830
56.486
22.481
16.758
1.00
35.62


ATOM
4782
OH2
WAT
831
26.101
20.243
49.585
1.00
24.90


ATOM
4783
OH2
WAT
832
16.729
33.274
50.986
1.00
24.98


ATOM
4784
OH2
WAT
833
21.501
54.137
59.417
1.00
23.27


ATOM
4785
OH2
WAT
834
47.542
53.259
64.127
1.00
45.51


ATOM
4786
OH2
WAT
836
49.479
39.080
12.500
1.00
30.28


ATOM
4787
OH2
WAT
838
42.825
25.879
37.780
1.00
23.21


ATOM
4788
OH2
WAT
839
50.943
24.947
57.867
1.00
32.14


ATOM
4789
OH2
WAT
840
54.743
56.961
50.478
1.00
26.75


ATOM
4790
OH2
WAT
841
40.544
53.741
32.431
1.00
34.46


ATOM
4791
OH2
WAT
842
26.547
47.649
53.571
1.00
39.97


ATOM
4792
OH2
WAT
843
37.195
32.835
54.383
1.00
28.68


ATOM
4793
OH2
WAT
844
58.053
39.110
31.973
1.00
18.62


ATOM
4794
OH2
WAT
845
18.264
24.599
44.498
1.00
27.65


ATOM
4795
OH2
WAT
847
13.854
29.610
37.456
1.00
44.84


ATOM
4796
OH2
WAT
849
22.552
38.833
31.917
1.00
48.29


ATOM
4797
OH2
WAT
850
35.645
59.479
37.510
1.00
31.45


ATOM
4798
OH2
WAT
851
24.548
59.962
64.794
1.00
38.37


ATOM
4799
OH2
WAT
852
30.633
55.275
34.413
1.00
26.28


ATOM
4800
OH2
WAT
853
39.272
27.243
44.281
1.00
44.92


ATOM
4801
OH2
WAT
854
32.053
46.154
71.549
1.00
34.74


ATOM
4802
OH2
WAT
855
48.612
24.905
14.847
1.00
36.12


ATOM
4803
OH2
WAT
857
18.696
30.214
40.372
1.00
32.39


ATOM
4804
OH2
WAT
858
67.928
43.317
39.467
1.00
25.41


ATOM
4805
OH2
WAT
859
29.220
64.769
57.769
1.00
33.69


ATOM
4806
OH2
WAT
860
50.268
24.002
37.829
1.00
31.48


ATOM
4807
OH2
WAT
861
50.197
23.766
16.468
1.00
47.21


ATOM
4808
OH2
WAT
862
50.752
18.550
46.573
1.00
33.31


ATOM
4809
OH2
WAT
863
54.737
36.999
16.598
1.00
28.84


ATOM
4810
OH2
WAT
864
23.466
24.199
53.649
1.00
29.72


ATOM
4811
OH2
WAT
865
33.404
55.021
25.847
1.00
52.41


ATOM
4812
OH2
WAT
866
42.687
31.048
44.149
1.00
40.21


ATOM
4813
OH2
WAT
867
28.448
42.954
54.380
1.00
36.53


ATOM
4814
OH2
WAT
868
14.997
43.707
34.454
1.00
43.03


ATOM
4815
OH2
WAT
869
14.328
39.153
57.579
1.00
40.69


ATOM
4816
OH2
WAT
870
57.378
37.209
64.736
1.00
28.61


ATOM
4817
OH2
WAT
871
20.536
32.124
29.526
1.00
31.13


ATOM
4818
OH2
WAT
872
52.129
50.355
27.209
1.00
31.95


ATOM
4819
OH2
WAT
873
51.809
35.631
62.337
1.00
31.87


ATOM
4820
OH2
WAT
874
47.029
21.316
50.899
1.00
28.63


ATOM
4821
OH2
WAT
875
29.328
44.418
56.243
1.00
29.76


ATOM
4822
OH2
WAT
876
40.553
19.067
31.054
1.00
31.19


ATOM
4823
OH2
WAT
877
56.608
42.974
23.109
1.00
36.47


ATOM
4824
OH2
WAT
878
33.944
18.283
53.032
1.00
48.79


ATOM
4825
OH2
WAT
879
27.295
18.819
26.051
1.00
23.88


ATOM
4826
OH2
WAT
880
62.721
54.186
39.777
1.00
38.87


ATOM
4827
OH2
WAT
881
35.611
9.588
50.038
1.00
41.90


ATOM
4828
OH2
WAT
882
38.082
58.167
33.104
1.00
35.67


ATOM
4829
OH2
WAT
883
20.479
20.811
35.650
1.00
28.10


ATOM
4830
OH2
WAT
884
64.071
48.661
47.710
1.00
36.23


ATOM
4831
OH2
WAT
885
62.169
33.114
54.016
1.00
38.38


ATOM
4832
OH2
WAT
886
46.247
15.458
31.504
1.00
29.44


ATOM
4833
OH2
WAT
887
15.161
50.744
53.893
1.00
46.81


ATOM
4834
OH2
WAT
888
21.461
24.555
51.822
1.00
33.72


ATOM
4835
OH2
WAT
889
39.805
19.953
14.067
1.00
34.19


ATOM
4836
OH2
WAT
890
44.630
68.730
56.107
1.00
44.36


ATOM
4837
OH2
WAT
891
47.554
30.392
39.434
1.00
32.91


ATOM
4838
OH2
WAT
892
32.135
20.873
14.262
1.00
29.57


ATOM
4839
OH2
WAT
893
69.474
42.046
47.848
1.00
40.45


ATOM
4840
OH2
WAT
894
23.764
15.417
41.216
1.00
45.57


ATOM
4841
OH2
WAT
895
30.804
11.274
25.353
1.00
36.15


ATOM
4842
OH2
WAT
896
42.686
40.690
57.070
1.00
26.52


ATOM
4843
OH2
WAT
898
41.447
36.486
13.521
1.00
40.39


ATOM
4844
OH2
WAT
899
38.960
38.628
60.048
1.00
40.06


ATOM
4845
OH2
WAT
900
41.026
24.976
9.369
1.00
38.69


ATOM
4846
OH2
WAT
902
55.833
48.047
27.058
1.00
38.88


ATOM
4847
OH2
WAT
903
33.909
34.365
58.131
1.00
39.46


ATOM
4848
OH2
WAT
904
56.604
58.656
39.499
1.00
34.67


ATOM
4849
OH2
WAT
905
57.413
45.071
24.624
1.00
33.81


ATOM
4850
OH2
WAT
906
68.047
30.945
34.093
1.00
36.91


ATOM
4851
OH2
WAT
907
17.540
52.182
46.933
1.00
26.43


ATOM
4852
OH2
WAT
908
35.513
31.206
66.336
1.00
25.73


ATOM
4853
OH2
WAT
910
62.045
46.674
53.517
1.00
33.21


ATOM
4854
OH2
WAT
911
46.903
38.348
67.243
1.00
32.49


ATOM
4855
OH2
WAT
912
60.188
33.756
26.674
1.00
37.96


ATOM
4856
OH2
WAT
913
17.538
36.873
63.382
1.00
49.19


ATOM
4857
OH2
WAT
914
23.983
36.615
25.955
1.00
28.20


ATOM
4858
OH2
WAT
915
15.876
30.521
47.253
1.00
31.86


ATOM
4859
OH2
WAT
916
23.539
62.135
63.215
1.00
37.75


ATOM
4860
OH2
WAT
917
50.546
48.552
64.034
1.00
38.09


ATOM
4861
OH2
WAT
918
64.968
41.202
32.910
1.00
30.16


ATOM
4862
OH2
WAT
919
47.342
55.129
71.525
1.00
41.35


ATOM
4863
OH2
WAT
920
15.582
44.034
65.703
1.00
31.07


ATOM
4864
OH2
WAT
921
37.858
50.757
24.526
1.00
31.62


ATOM
4865
OH2
WAT
922
37.372
23.617
9.556
1.00
39.44


ATOM
4866
OH2
WAT
924
24.489
15.323
15.117
1.00
46.62


ATOM
4867
OH2
WAT
925
22.412
16.803
37.659
1.00
43.70


ATOM
4868
OH2
WAT
926
29.507
54.047
43.644
1.00
35.52


ATOM
4869
OH2
WAT
927
60.554
35.356
56.976
1.00
42.99


ATOM
4870
OH2
WAT
929
20.021
33.589
59.004
1.00
30.36


ATOM
4871
OH2
WAT
930
19.473
19.176
31.910
1.00
31.54


ATOM
4872
OH2
WAT
931
48.046
22.565
58.100
1.00
30.58


ATOM
4873
OH2
WAT
932
43.806
63.606
53.022
1.00
40.90


ATOM
4874
OH2
WAT
933
33.913
20.122
11.496
1.00
24.77


ATOM
4875
OH2
WAT
934
49.430
59.955
52.495
1.00
37.32


ATOM
4876
OH2
WAT
935
63.827
32.863
45.133
1.00
49.52


ATOM
4877
OH2
WAT
936
37.964
21.411
49.414
1.00
30.06


ATOM
4878
OH2
WAT
937
27.725
14.522
39.223
1.00
39.88


ATOM
4879
OH2
WAT
938
15.164
38.822
61.336
1.00
46.35


ATOM
4880
OH2
WAT
939
59.040
42.353
59.062
1.00
33.96


ATOM
4881
OH2
WAT
940
47.109
42.149
69.895
1.00
45.88


ATOM
4882
OH2
WAT
941
26.653
32.630
69.093
1.00
36.31


ATOM
4883
OH2
WAT
942
28.206
17.559
22.902
1.00
32.76


ATOM
4884
OH2
WAT
943
26.970
50.327
70.960
1.00
48.12


ATOM
4885
OH2
WAT
944
64.060
23.004
42.589
1.00
32.90


ATOM
4886
OH2
WAT
945
47.727
33.598
7.895
1.00
35.65


ATOM
4887
OH2
WAT
946
34.742
23.791
49.020
1.00
25.74


ATOM
4888
OH2
WAT
947
47.101
46.897
68.781
1.00
45.45


ATOM
4889
OH2
WAT
948
41.870
11.724
30.722
1.00
27.02


ATOM
4890
OH2
WAT
949
34.529
49.050
63.729
1.00
32.80


ATOM
4891
OH2
WAT
950
38.408
61.853
51.628
1.00
49.43


ATOM
4892
OH2
WAT
951
44.952
50.165
71.454
1.00
36.16


ATOM
4893
OH2
WAT
952
46.362
23.481
42.021
1.00
38.59


ATOM
4894
OH2
WAT
953
22.997
57.578
62.984
1.00
48.56


ATOM
4895
OH2
WAT
954
53.705
20.324
34.584
1.00
46.72


ATOM
4896
OH2
WAT
955
39.632
64.246
53.049
1.00
38.41


ATOM
4897
OH2
WAT
956
20.296
21.770
47.578
1.00
38.44


ATOM
4898
OH2
WAT
957
70.708
44.445
44.502
1.00
35.87


ATOM
4899
OH2
WAT
958
13.567
22.992
35.251
1.00
36.22


ATOM
4900
OH2
WAT
959
61.462
37.840
59.404
1.00
32.38


ATOM
4901
OH2
WAT
960
70.605
49.268
42.736
1.00
49.49


ATOM
4902
OH2
WAT
961
27.001
13.873
45.582
1.00
34.49


ATOM
4903
OH2
WAT
962
40.837
53.265
28.588
1.00
34.92


ATOM
4904
OH2
WAT
963
41.440
40.204
15.200
1.00
25.63


ATOM
4905
OH2
WAT
964
47.029
18.253
59.807
1.00
47.20


ATOM
4906
OH2
WAT
965
30.122
45.125
27.224
1.00
41.19


ATOM
4907
OH2
WAT
966
70.354
22.884
32.301
1.00
45.44


ATOM
4908
OH2
WAT
967
54.548
57.173
32.638
1.00
33.64


ATOM
4909
OH2
WAT
968
47.786
18.173
53.594
1.00
33.24


ATOM
4910
OH2
WAT
969
38.400
16.790
14.876
1.00
37.75


ATOM
4911
OH2
WAT
970
28.970
12.153
32.723
1.00
24.55


ATOM
4912
OH2
WAT
971
28.874
35.834
60.109
1.00
39.03


ATOM
4913
OH2
WAT
972
47.546
23.630
12.714
1.00
51.51


ATOM
4914
OH2
WAT
973
40.454
49.523
57.495
1.00
35.41


ATOM
4915
OH2
WAT
974
48.210
48.061
65.137
1.00
47.07


ATOM
4916
OH2
WAT
975
37.958
26.212
47.790
1.00
44.98


ATOM
4917
OH2
WAT
977
37.233
24.170
51.843
1.00
33.85


ATOM
4918
OH2
WAT
978
33.749
56.149
48.597
1.00
30.36


ATOM
4919
OH2
WAT
979
48.361
43.396
21.748
1.00
40.73


ATOM
4920
OH2
WAT
980
47.355
49.826
23.205
1.00
38.07


ATOM
4921
OH2
WAT
982
37.732
7.064
33.535
1.00
48.68


ATOM
4922
OH2
WAT
984
67.639
44.821
28.942
1.00
56.38


ATOM
4923
OH2
WAT
985
65.770
35.555
35.108
1.00
50.64


ATOM
4924
OH2
WAT
986
30.693
20.715
65.019
1.00
32.06


ATOM
4925
OH2
WAT
987
27.053
36.974
22.607
1.00
38.10


ATOM
4926
OH2
WAT
988
19.163
25.611
48.320
1.00
25.80


ATOM
4927
OH2
WAT
989
48.005
58.792
30.965
1.00
45.93


ATOM
4928
OH2
WAT
990
33.951
58.019
31.506
1.00
26.89


ATOM
4929
OH2
WAT
991
60.149
48.327
52.415
1.00
42.30


ATOM
4930
OH2
WAT
993
64.162
36.713
52.481
1.00
35.08


ATOM
4931
OH2
WAT
996
36.217
29.075
7.223
1.00
43.08


ATOM
4932
OH2
WAT
997
49.801
51.068
30.170
1.00
33.40


ATOM
4933
OH2
WAT
998
11.053
37.371
34.418
1.00
31.32


ATOM
4934
OH2
WAT
999
44.601
23.087
39.455
1.00
47.23


ATOM
4935
OH2
WAT
1000
50.726
38.377
68.058
1.00
47.19


ATOM
4936
OH2
WAT
1002
60.312
35.422
29.042
1.00
30.62


ATOM
4937
OH2
WAT
1003
20.479
31.153
57.519
1.00
37.20


ATOM
4938
OH2
WAT
1004
20.277
29.204
31.044
1.00
31.69


ATOM
4939
OH2
WAT
1005
20.943
52.359
61.162
1.00
36.05


ATOM
4940
OH2
WAT
1006
44.819
20.699
43.312
1.00
49.10


ATOM
4941
OH2
WAT
1008
34.011
36.177
53.463
1.00
33.13


ATOM
4942
OH2
WAT
1010
55.158
53.328
33.223
1.00
28.59


ATOM
4943
OH2
WAT
1012
55.826
39.714
64.610
1.00
34.66


ATOM
4944
OH2
WAT
1014
66.327
38.147
49.052
1.00
26.67


ATOM
4945
OH2
WAT
1017
30.997
50.156
52.375
1.00
35.44


ATOM
4946
OH2
WAT
1020
13.998
44.255
63.276
1.00
37.79


ATOM
4947
OH2
WAT
1021
54.863
22.503
53.859
1.00
37.14


ATOM
4948
OH2
WAT
1022
17.119
28.668
38.825
1.00
36.01


ATOM
4949
OH2
WAT
1024
36.501
20.637
51.705
1.00
45.60


ATOM
4950
OH2
WAT
1025
48.817
20.944
30.325
1.00
27.83


ATOM
4951
OH2
WAT
1027
14.381
45.600
52.809
1.00
44.10


ATOM
4952
OH2
WAT
1032
35.525
5.074
31.109
1.00
41.37


ATOM
4953
OH2
WAT
1033
29.779
34.319
53.582
1.00
28.70


ATOM
4954
OH2
WAT
1034
47.328
38.726
9.716
1.00
49.35


ATOM
4955
OH2
WAT
1035
44.854
34.535
67.215
1.00
48.50


ATOM
4956
OH2
WAT
1037
26.055
45.081
34.982
1.00
35.09


ATOM
4957
OH2
WAT
1040
11.141
37.010
54.220
1.00
43.27


ATOM
4958
OH2
WAT
1041
29.634
41.348
52.346
1.00
40.29


ATOM
4959
OH2
WAT
1042
36.989
26.821
9.501
1.00
47.61


ATOM
4960
OH2
WAT
1043
57.297
28.427
29.996
1.00
42.70


ATOM
4961
OH2
WAT
1044
15.339
49.780
56.964
1.00
42.68


ATOM
4962
OH2
WAT
1045
46.946
51.783
70.089
1.00
52.87


ATOM
4963
OH2
WAT
1047
43.735
26.720
48.439
1.00
32.56


ATOM
4964
OH2
WAT
1049
59.084
48.736
30.360
1.00
45.92


ATOM
4965
OH2
WAT
1051
47.217
61.277
55.003
1.00
50.60


ATOM
4966
OH2
WAT
1052
42.854
26.577
64.396
1.00
40.89


ATOM
4967
OH2
WAT
1053
56.373
17.507
47.814
1.00
44.29


ATOM
4968
OH2
WAT
1056
58.449
30.554
63.214
1.00
46.73


ATOM
4969
OH2
WAT
1057
25.498
11.492
25.912
1.00
40.95


ATOM
4970
OH2
WAT
1058
44.975
29.368
39.403
1.00
43.65


ATOM
4971
OH2
WAT
1059
25.317
25.265
57.780
1.00
47.77


ATOM
4972
OH2
WAT
1061
28.989
59.107
55.188
1.00
46.96


ATOM
4973
OH2
WAT
1062
62.109
32.898
43.133
1.00
29.76


ATOM
4974
OH2
WAT
1063
68.950
47.081
42.243
1.00
32.59


ATOM
4975
OH2
WAT
1066
53.065
54.350
56.726
1.00
53.35


ATOM
4976
OH2
WAT
1068
44.519
16.873
20.860
1.00
43.15


ATOM
4977
OH2
WAT
1070
45.839
26.154
61.550
1.00
36.80


ATOM
4978
OH2
WAT
1072
36.197
36.508
12.204
1.00
33.71


ATOM
4979
OH2
WAT
1073
35.351
41.501
68.026
1.00
45.11


ATOM
4980
OH2
WAT
1074
65.633
34.803
51.451
1.00
38.53


ATOM
4981
OH2
WAT
1078
41.335
38.420
54.710
0.50
29.72


ATOM
4982
OH2
WAT
1079
29.512
38.685
22.833
1.00
39.63


ATOM
4983
OH2
WAT
1080
14.118
37.523
50.894
1.00
39.63


ATOM
4984
OH2
WAT
1081
48.556
54.366
25.635
1.00
42.49


ATOM
4985
OH2
WAT
1082
40.975
25.862
40.806
1.00
24.48


ATOM
4986
OH2
WAT
1083
40.345
57.934
37.750
1.00
22.44


ATOM
4987
OH2
WAT
1084
54.691
59.362
48.731
1.00
33.75


ATOM
4988
OH2
WAT
1085
53.736
57.789
52.852
1.00
40.58


ATOM
4989
OH2
WAT
1086
15.708
33.122
54.732
1.00
44.11


ATOM
4990
OH2
WAT
1087
22.243
32.265
27.402
1.00
38.80


ATOM
4991
OH2
WAT
1088
47.611
17.171
32.905
1.00
43.63


ATOM
4992
OH2
WAT
1089
58.379
48.121
27.949
1.00
43.58


ATOM
4993
OH2
WAT
1092
57.488
59.756
41.894
1.00
54.98


ATOM
4994
OH2
WAT
1093
37.216
31.175
68.418
1.00
28.64


ATOM
4995
OH2
WAT
1094
37.762
33.656
69.811
1.00
40.47


ATOM
4996
OH2
WAT
1095
65.445
43.712
34.681
1.00
47.01


ATOM
4997
OH2
WAT
1097
28.164
21.093
19.000
1.00
34.17


ATOM
4998
OH2
WAT
1098
18.673
33.165
61.660
1.00
40.84


ATOM
4999
OH2
WAT
1100
51.193
61.127
51.030
1.00
39.94


ATOM
5000
OH2
WAT
1101
56.432
43.982
59.555
1.00
39.42


ATOM
5001
OH2
WAT
1102
56.968
41.831
63.701
1.00
42.73


ATOM
5002
OH2
WAT
1103
34.405
49.957
71.786
1.00
35.15


ATOM
5003
OH2
WAT
1104
41.241
9.964
32.536
1.00
31.00


ATOM
5004
OH2
WAT
1105
21.105
21.857
50.569
1.00
43.38


ATOM
5005
OH2
WAT
1106
23.670
20.267
50.750
1.00
41.28


ATOM
5006
OH2
WAT
1108
29.571
9.657
34.297
1.00
39.24


ATOM
5007
OH2
WAT
1109
27.460
9.067
36.007
1.00
35.51


ATOM
5008
OH2
WAT
1111
24.692
47.272
35.502
1.00
33.10


ATOM
5009
OH2
WAT
1113
29.462
58.167
41.963
1.00
39.41


ATOM
5010
OH2
WAT
1115
26.304
58.757
54.952
1.00
54.54


ATOM
5011
OH2
WAT
1116
22.934
60.561
60.251
1.00
49.35


ATOM
5012
OH2
WAT
1117
39.244
37.381
55.807
1.00
42.76


ATOM
5013
OH2
WAT
1119
37.428
43.614
61.340
1.00
41.53


ATOM
5014
OH2
WAT
1121
17.907
30.515
55.600
1.00
52.02


ATOM
5015
OH2
WAT
1122
33.636
10.725
25.760
1.00
26.11


ATOM
5016
OH2
WAT
1123
37.687
60.192
39.575
1.00
27.92


ATOM
5017
OH2
WAT
1124
40.750
44.964
49.691
1.00
25.17


ATOM
5018
OH2
WAT
1125
70.584
38.077
47.755
1.00
37.02


ATOM
5019
OH2
WAT
1126
15.603
41.927
47.692
1.00
28.52


ATOM
5020
OH2
WAT
1127
25.206
43.505
32.164
1.00
33.23


ATOM
5021
OH2
WAT
1128
26.442
21.223
54.177
1.00
26.91


ATOM
5022
OH2
WAT
1130
42.766
41.142
51.475
1.00
46.99


ATOM
5023
OH2
WAT
1131
43.109
61.103
37.679
1.00
41.65


ATOM
5024
OH2
WAT
1132
14.570
30.169
45.086
1.00
42.30


ATOM
5025
OH2
WAT
1133
34.157
38.583
24.573
1.00
28.21


ATOM
5026
OH2
WAT
1135
35.943
44.155
50.435
1.00
35.21


ATOM
5027
OH2
WAT
1137
15.347
36.178
62.387
1.00
48.01


ATOM
5028
OH2
WAT
1142
30.780
45.800
61.426
1.00
46.24


ATOM
5029
OH2
WAT
1144
56.000
49.811
57.192
1.00
33.19


ATOM
5030
OH2
WAT
1145
50.931
47.015
21.718
1.00
41.76


ATOM
5031
OH2
WAT
1148
41.181
13.664
41.675
1.00
36.85


ATOM
5032
OH2
WAT
1149
26.829
13.900
42.000
1.00
51.60


ATOM
5033
OH2
WAT
1150
38.428
50.689
49.680
1.00
38.37


ATOM
5034
OH2
WAT
1151
13.307
43.102
37.676
1.00
40.57


ATOM
5035
OH2
WAT
1153
32.376
39.513
22.416
1.00
42.97


ATOM
5036
OH2
WAT
1155
14.863
50.906
47.090
1.00
49.79


ATOM
5037
OH2
WAT
1156
39.040
11.571
36.195
1.00
42.49


ATOM
5038
OH2
WAT
1157
55.760
18.990
54.253
1.00
46.82


ATOM
5039
OH2
WAT
1159
29.811
44.316
51.775
1.00
29.84


ATOM
5040
OH2
WAT
1160
26.254
30.191
18.160
1.00
47.30


ATOM
5041
OH2
WAT
1163
50.589
53.935
30.727
1.00
41.87


ATOM
5042
OH2
WAT
1164
26.778
17.598
17.107
1.00
39.40


ATOM
5043
OH2
WAT
1166
57.293
56.491
51.361
1.00
36.42


ATOM
5044
OH2
WAT
1167
55.900
43.483
62.013
1.00
33.17


ATOM
5045
OH2
WAT
1170
45.416
56.601
68.328
1.00
39.64


ATOM
5046
OH2
WAT
1171
45.090
53.796
27.563
1.00
44.12


ATOM
5047
OH2
WAT
1172
25.950
27.760
17.747
1.00
47.76


ATOM
5048
OH2
WAT
1174
21.716
34.736
25.915
1.00
39.70


ATOM
5049
OH2
WAT
1177
28.580
48.024
33.877
1.00
34.88


ATOM
5050
OH2
WAT
1178
45.395
19.823
49.333
1.00
48.96


ATOM
5051
OH2
WAT
1180
66.122
32.218
43.068
1.00
46.26


ATOM
5052
OH2
WAT
1181
61.892
29.586
16.389
1.00
40.21


ATOM
5053
OH2
WAT
1183
15.358
27.450
47.492
1.00
49.59


ATOM
5054
OH2
WAT
1184
13.556
47.284
49.126
1.00
53.43


ATOM
5055
OH2
WAT
1185
47.096
19.628
33.301
1.00
39.63


ATOM
5056
OH2
WAT
1186
15.740
33.792
31.449
1.00
55.70


ATOM
5057
OH2
WAT
1189
28.976
26.719
60.440
1.00
42.03


ATOM
5058
OH2
WAT
1190
18.223
23.257
49.730
1.00
49.11


ATOM
5059
OH2
WAT
1191
51.509
56.989
54.192
1.00
38.61


ATOM
5060
OH2
WAT
1193
43.560
45.405
17.563
1.00
36.62


ATOM
5061
OH2
WAT
1204
30.518
43.634
25.079
1.00
47.04


ATOM
5062
OH2
WAT
1208
21.476
24.864
27.340
1.00
34.36


ATOM
5063
OH2
WAT
1209
17.760
41.993
33.261
1.00
55.66


ATOM
5064
OH2
WAT
1212
46.798
63.405
52.749
1.00
51.44


ATOM
5065
OH2
WAT
1219
34.617
51.206
58.460
1.00
49.36


ATOM
5066
OH2
WAT
1220
24.104
41.582
29.552
1.00
45.40


ATOM
5067
OH2
WAT
1223
23.863
21.524
53.424
1.00
45.78


ATOM
5068
OH2
WAT
1224
50.956
18.524
42.578
1.00
40.01


ATOM
5069
OH2
WAT
1226
49.969
19.920
49.613
1.00
44.84


ATOM
5070
OH2
WAT
1229
49.709
30.628
33.104
1.00
41.21


ATOM
5071
OH2
WAT
1230
31.240
38.559
20.375
1.00
47.94


ATOM
5072
OH2
WAT
1232
23.399
22.619
27.338
1.00
34.56


ATOM
5073
OH2
WAT
1233
48.110
31.839
37.064
1.00
42.29


ATOM
5074
OH2
WAT
1236
47.248
45.427
20.268
1.00
40.26


ATOM
5075
OH2
WAT
1237
19.590
16.455
39.634
1.00
45.25


ATOM
5076
OH2
WAT
1239
40.962
60.463
74.404
1.00
45.01


ATOM
5077
OH2
WAT
1243
46.981
33.979
68.748
1.00
49.24


ATOM
5078
OH2
WAT
1244
61.241
43.880
58.980
1.00
42.97


ATOM
5079
OH2
WAT
1250
35.115
51.055
23.889
1.00
51.05


ATOM
5080
OH2
WAT
1255
12.571
50.793
52.116
0.50
33.17


ATOM
5081
OH2
WAT
1266
25.841
9.552
44.564
1.00
55.17


ATOM
5082
OH2
WAT
1268
61.336
50.541
51.337
1.00
45.61


ATOM
5083
OH2
WAT
1273
23.939
29.659
26.509
1.00
42.88


ATOM
5084
OH2
WAT
1275
59.410
55.437
44.599
1.00
42.16


ATOM
5085
OH2
WAT
1278
64.290
43.553
53.436
1.00
38.01


ATOM
5086
OH2
WAT
1279
36.463
61.861
41.741
1.00
31.97


ATOM
5087
OH2
WAT
1282
37.884
28.719
70.368
1.00
50.75


ATOM
5088
OH2
WAT
1286
21.758
53.622
63.516
1.00
46.95


ATOM
5089
OH2
WAT
1288
49.866
23.754
32.094
1.00
47.08


ATOM
5090
OH2
WAT
1289
46.816
19.829
38.612
1.00
41.12


ATOM
5091
OH2
WAT
1294
41.690
12.743
36.520
1.00
45.23


ATOM
5092
OH2
WAT
1302
47.382
23.700
60.586
1.00
42.72


ATOM
5093
OH2
WAT
1303
65.406
53.318
38.129
1.00
42.46


ATOM
5094
OH2
WAT
1304
16.963
19.384
30.420
1.00
49.48


ATOM
5095
OH2
WAT
1308
63.085
28.921
19.779
1.00
53.97


ATOM
5096
OH2
WAT
1309
23.293
21.221
25.162
1.00
40.04


ATOM
5097
OH2
WAT
1312
47.167
34.527
37.872
1.00
27.27


ATOM
5098
OH2
WAT
1314
10.864
37.430
37.980
1.00
28.15


ATOM
5099
OH2
WAT
1315
44.856
27.880
46.189
1.00
30.95


ATOM
5100
OH2
WAT
1317
58.272
25.539
24.981
1.00
32.58


ATOM
5101
OH2
WAT
1318
18.820
50.334
62.005
1.00
36.58


ATOM
5102
OH2
WAT
1319
30.841
37.131
59.111
1.00
46.56


ATOM
5103
OH2
WAT
1320
29.617
62.035
68.933
1.00
44.43


ATOM
5104
OH2
WAT
1321
46.544
35.226
40.439
1.00
40.06


ATOM
5105
OH2
WAT
1322
28.073
10.853
25.663
1.00
40.56


ATOM
5106
OH2
WAT
1323
42.441
29.122
46.515
1.00
39.18


ATOM
5107
OH2
WAT
1324
32.503
25.207
20.281
1.00
30.43


ATOM
5108
OH2
WAT
1325
45.433
45.115
68.057
1.00
34.28


ATOM
5109
OH2
WAT
1326
60.152
17.493
35.180
1.00
31.13


ATOM
5110
OH2
WAT
1327
18.398
27.449
35.882
1.00
37.64


ATOM
5111
OH2
WAT
1328
25.504
31.112
20.438
1.00
38.34


ATOM
5112
OH2
WAT
1329
30.779
47.918
51.067
1.00
35.49


ATOM
5113
OH2
WAT
1330
19.913
28.817
33.764
1.00
31.28


ATOM
5114
OH2
WAT
1331
41.767
10.738
28.096
1.00
41.34


ATOM
5115
OH2
WAT
1332
26.547
23.240
56.068
1.00
41.06


ATOM
5116
OH2
WAT
1333
33.925
58.939
47.024
1.00
34.77


ATOM
5117
OH2
WAT
1334
22.602
51.105
36.733
1.00
43.04


ATOM
5118
OH2
WAT
1335
22.996
38.949
26.371
1.00
38.28


ATOM
5119
OH2
WAT
1336
29.162
20.497
16.594
1.00
43.76


ATOM
5120
OH2
WAT
1337
20.274
17.838
34.214
1.00
44.34


ATOM
5121
OH2
WAT
1338
39.624
36.468
69.824
1.00
40.01


ATOM
5122
OH2
WAT
1339
37.483
51.842
59.120
1.00
44.97


ATOM
5123
OH2
WAT
1340
24.717
29.196
23.868
1.00
34.46


ATOM
5124
OH2
WAT
1341
44.042
21.496
47.701
1.00
33.63


ATOM
5125
OH2
WAT
1342
13.466
35.511
57.867
1.00
42.68


ATOM
5126
OH2
WAT
1343
55.772
29.777
32.992
1.00
44.58


ATOM
5127
OH2
WAT
1344
14.280
32.060
49.325
1.00
38.28


ATOM
5128
OH2
WAT
1345
45.443
50.731
25.094
1.00
46.95


ATOM
5129
OH2
WAT
1346
68.409
39.510
47.837
1.00
41.69


ATOM
5130
OH2
WAT
1347
39.778
58.278
43.142
1.00
32.41


ATOM
5131
OH2
WAT
1348
29.470
22.597
20.692
1.00
48.08


ATOM
5132
OH2
WAT
1349
24.093
35.444
64.264
1.00
35.01


ATOM
5133
OH2
WAT
1351
26.090
30.612
28.125
1.00
36.91


ATOM
5134
OH2
WAT
1352
17.332
33.459
57.443
1.00
41.72


ATOM
5135
OH2
WAT
1353
56.042
23.489
25.469
1.00
43.75


ATOM
5136
OH2
WAT
1354
42.787
43.334
56.083
1.00
40.09


ATOM
5137
OH2
WAT
1355
50.830
26.069
35.611
1.00
40.02


ATOM
5138
OH2
WAT
1356
38.381
12.374
24.731
1.00
44.11


ATOM
5139
OH2
WAT
1357
44.282
44.869
20.284
1.00
42.34


ATOM
5140
OH2
WAT
1359
34.183
42.608
20.745
1.00
46.91


ATOM
5141
OH2
WAT
1360
31.973
57.138
43.492
1.00
43.69


ATOM
5142
OH2
WAT
1361
47.127
28.967
63.758
1.00
39.75


ATOM
5143
OH2
WAT
1362
16.760
48.273
38.728
1.00
43.33


ATOM
5144
OH2
WAT
1363
31.959
52.844
61.725
1.00
48.88


ATOM
5145
OH2
WAT
1364
48.548
41.547
13.592
1.00
46.21


ATOM
5146
OH2
WAT
1365
28.676
25.375
20.616
1.00
37.11


ATOM
5147
OH2
WAT
1366
29.885
56.396
44.858
1.00
36.90


ATOM
5148
OH2
WAT
1367
40.319
47.450
20.023
1.00
43.96


ATOM
5149
OH2
WAT
1368
38.503
60.152
44.332
1.00
32.68


ATOM
5150
OH2
WAT
1369
44.801
17.250
50.502
1.00
43.13


ATOM
5151
OH2
WAT
1370
37.328
23.957
49.049
1.00
45.36


ATOM
5152
OH2
WAT
1371
24.009
57.807
55.904
1.00
42.44


ATOM
5153
OH2
WAT
1372
28.513
45.956
53.486
1.00
46.34


ATOM
5154
OH2
WAT
1373
49.030
36.730
6.520
1.00
45.48


ATOM
5155
OH2
WAT
1374
38.498
35.628
50.765
1.00
26.69


ATOM
5156
OH2
WAT
1375
39.668
33.298
50.610
1.00
33.61


ATOM
5157
OH2
WAT
1376
52.375
26.835
60.266
1.00
44.32


ATOM
5158
OH2
WAT
1377
55.500
25.818
58.095
1.00
44.59


ATOM
5159
OH2
WAT
1378
30.116
36.834
19.045
1.00
39.93


ATOM
5160
OH2
WAT
1381
43.493
27.126
35.565
1.00
48.96


ATOM
5161
OH2
WAT
1382
33.586
58.999
44.339
1.00
41.52


ATOM
5162
OH2
WAT
1383
35.232
41.723
71.023
1.00
46.74


ATOM
5163
OH2
WAT
1384
71.095
37.535
44.165
1.00
41.47


ATOM
5164
OH2
WAT
1386
48.253
57.473
71.974
1.00
43.72


ATOM
5165
C1
NAG
691
38.666
22.463
66.650
0.50
29.58


ATOM
5166
C2
NAG
691
39.962
22.246
67.525
0.50
29.55


ATOM
5167
C3
NAG
691
39.524
21.408
68.772
0.50
29.52


ATOM
5168
C4
NAG
691
38.496
22.259
69.550
0.50
29.70


ATOM
5169
C5
NAG
691
37.241
22.504
68.605
0.50
30.07


ATOM
5170
C6
NAG
691
36.157
23.293
69.219
0.50
28.97


ATOM
5171
C7
NAG
691
42.209
21.838
66.543
0.50
29.68


ATOM
5172
C8
NAG
691
43.027
20.911
65.781
0.50
29.38


ATOM
5173
N2
NAG
691
40.925
21.438
66.776
0.50
28.28


ATOM
5174
O3
NAG
691
40.679
21.179
69.596
0.50
29.08


ATOM
5175
O4
NAG
691
38.067
21.525
70.710
0.50
31.81


ATOM
5176
O5
NAG
691
37.742
23.245
67.408
0.50
28.44


ATOM
5177
O6
NAG
691
34.965
23.182
68.486
0.50
29.28


ATOM
5178
O7
NAG
691
42.632
22.844
66.920
0.50
30.40


ATOM
5179
C1
NAG
692
26.823
46.501
73.110
0.25
30.78


ATOM
5180
C2
NAG
692
26.060
47.367
74.194
0.25
29.79


ATOM
5181
C3
NAG
692
26.339
46.684
75.578
0.25
28.68


ATOM
5182
C4
NAG
692
25.778
45.248
75.517
0.25
28.12


ATOM
5183
C5
NAG
692
26.546
44.463
74.365
0.25
28.47


ATOM
5184
C6
NAG
692
26.141
43.054
74.189
0.25
27.89


ATOM
5185
C7
NAG
692
27.924
49.127
74.485
0.25
29.38


ATOM
5186
C8
NAG
692
28.176
50.560
74.479
0.25
29.34


ATOM
5187
N2
NAG
692
26.610
48.755
74.247
0.25
29.38


ATOM
5188
O3
NAG
692
25.663
47.437
76.598
0.25
28.79


ATOM
5189
O4
NAG
692
26.031
44.601
76.779
0.25
26.69


ATOM
5190
O5
NAG
692
26.263
45.191
73.097
0.25
29.85


ATOM
5191
O6
NAG
692
26.884
42.425
73.176
0.25
25.82


ATOM
5192
O7
NAG
692
28.778
48.376
74.677
0.25
28.91


ATOM
5193
C1
NAG
693
45.844
65.857
60.275
0.50
34.64


ATOM
5194
C2
NAG
693
47.343
66.335
60.338
0.50
33.61


ATOM
5195
C3
NAG
693
48.225
65.046
60.320
0.50
33.54


ATOM
5196
C4
NAG
693
47.874
64.228
61.582
0.50
33.12


ATOM
5197
C5
NAG
693
46.335
63.825
61.490
0.50
32.64


ATOM
5198
C6
NAG
693
45.829
63.006
62.614
0.50
32.29


ATOM
5199
C7
NAG
693
47.847
68.449
59.114
0.50
33.80


ATOM
5200
C8
NAG
693
48.147
69.026
57.814
0.50
33.51


ATOM
5201
N2
NAG
693
47.658
67.096
59.127
0.50
33.78


ATOM
5202
O3
NAG
693
49.604
65.442
60.373
0.50
34.37


ATOM
5203
O4
NAG
693
48.672
63.030
61.597
0.50
32.73


ATOM
5204
O5
NAG
693
45.563
65.105
61.455
0.50
32.95


ATOM
5205
O6
NAG
693
46.059
63.613
63.861
0.50
33.79


ATOM
5206
O7
NAG
693
47.775
69.104
60.061
0.50
34.69


ATOM
5207
C1
NAG
694
34.333
4.445
43.451
0.50
42.09


ATOM
5208
C2
NAG
694
35.344
3.237
43.321
0.50
40.59


ATOM
5209
C3
NAG
694
36.776
3.873
43.266
0.50
40.44


ATOM
5210
C4
NAG
694
36.837
4.763
42.008
0.50
39.57


ATOM
5211
C5
NAG
694
35.747
5.912
42.160
0.50
40.19


ATOM
5212
C6
NAG
694
35.697
6.867
41.038
0.50
39.67


ATOM
5213
C7
NAG
694
35.390
1.041
44.522
0.50
38.40


ATOM
5214
C8
NAG
694
35.318
0.390
45.820
0.50
37.85


ATOM
5215
N2
NAG
694
35.289
2.407
44.534
0.50
39.83


ATOM
5216
O3
NAG
694
37.745
2.817
43.151
0.50
41.14


ATOM
5217
O4
NAG
694
38.143
5.361
41.930
0.50
39.45


ATOM
5218
O5
NAG
694
34.422
5.231
42.261
0.50
40.94


ATOM
5219
O6
NAG
694
36.230
8.118
41.399
0.50
40.94


ATOM
5220
O7
NAG
694
35.527
0.432
43.553
0.50
39.01


ATOM
5221
C1
NAG
695
56.458
28.072
65.509
0.25
31.56


ATOM
5222
C2
NAG
695
56.666
26.508
65.432
0.25
30.72


ATOM
5223
C3
NAG
695
56.499
25.969
66.893
0.25
29.54


ATOM
5224
C4
NAG
695
57.609
26.616
67.754
0.25
29.02


ATOM
5225
C5
NAG
695
57.392
28.194
67.738
0.25
28.93


ATOM
5226
C6
NAG
695
58.361
28.972
68.535
0.25
29.26


ATOM
5227
C7
NAG
695
55.782
25.465
63.341
0.25
29.26


ATOM
5228
C8
NAG
695
54.608
24.896
62.697
0.25
29.00


ATOM
5229
N2
NAG
695
55.599
25.907
64.623
0.25
29.43


ATOM
5230
O3
NAG
695
56.674
24.544
66.875
0.25
30.87


ATOM
5231
O4
NAG
695
57.485
26.137
69.107
0.25
27.69


ATOM
5232
O5
NAG
695
57.504
28.627
66.310
0.25
30.15


ATOM
5233
O6
NAG
695
57.844
30.233
68.885
0.25
30.07


ATOM
5234
O7
NAG
695
56.794
25.529
62.791
0.25
29.27


ATOM
5235
C1
NAG
696
43.763
59.783
31.843
0.50
32.65


ATOM
5236
C2
NAG
696
43.513
59.801
30.283
0.50
33.89


ATOM
5237
C3
NAG
696
42.464
60.933
30.025
0.50
34.52


ATOM
5238
C4
NAG
696
41.169
60.556
30.774
0.50
34.29


ATOM
5239
C5
NAG
696
41.517
60.476
32.322
0.50
33.83


ATOM
5240
C6
NAG
696
40.400
60.153
33.216
0.50
33.87


ATOM
5241
C7
NAG
696
45.496
59.327
28.856
0.50
33.72


ATOM
5242
C8
NAG
696
46.660
59.906
28.211
0.50
33.27


ATOM
5243
N2
NAG
696
44.730
60.198
29.572
0.50
33.67


ATOM
5244
O3
NAG
696
42.197
61.001
28.614
0.50
36.84


ATOM
5245
O4
NAG
696
40.196
61.589
30.553
0.50
36.06


ATOM
5246
O5
NAG
696
42.537
59.408
32.458
0.50
34.67


ATOM
5247
O6
NAG
696
40.731
60.434
34.555
0.50
33.99


ATOM
5248
O7
NAG
696
45.250
58.204
28.755
0.50
33.63


ATOM
5249
C
ACY
700
42.190
36.698
47.868
1.00
17.87


ATOM
5250
O
ACY
700
43.358
36.429
48.383
1.00
17.41


ATOM
5251
OXT
ACY
700
41.942
37.484
46.891
1.00
16.00


ATOM
5252
CH3
ACY
700
41.037
35.966
48.550
1.00
16.17


ATOM
5253
O1
MSA
702
40.494
34.478
45.311
1.00
21.85


ATOM
5254
O2
MSA
702
42.778
34.136
45.475
1.00
27.34


ATOM
5255
C1
MSA
702
41.675
34.389
44.805
1.00
25.81


ATOM
5256
N1
MSA
702
41.988
34.537
43.491
1.00
23.47


ATOM
5257
C2
MSA
702
40.825
34.645
42.578
1.00
24.59


ATOM
5258
C3
MSA
702
41.603
34.810
41.280
1.00
26.22


ATOM
5259
C4
MSA
702
39.846
33.467
42.340
1.00
22.86


ATOM
5260
O3
MSA
702
38.793
33.259
41.647
1.00
21.49


ATOM
5261
O4
MSA
702
40.179
32.410
43.024
1.00
21.93


ATOM
5262
ZN + 2
ZN2
701
43.817
38.308
46.652
1.00
16.34


ATOM
5263
CL
CL
703
29.185
28.250
36.073
1.00
16.51


ATOM
5264
CL
CL
704
36.287
45.320
44.617
1.00
16.56


END
















TABLE B





Co-ordinates of an underglycosylated tACEΔ36NJ ACE-lisinopril complex















REMARK coordinates from minimization refinement


REMARK refinement resolution: 47.14-2.0 A








REMARK starting
r = 0.1816 free_r = 0.2186


REMARK final
r = 0.1814 free_r = 0.2188







REMARK rmsd bonds = 0.005621 rmsd angles = 1.23822


REMARK wa = 0.450786


REMARK target = mlf cycles = 1 steps = 10


REMARK sg = P2(1)2(1)2(1) a = 56.472 b = 84.899 c = 133.990 alpha = 90


beta = 90 gamma = 90


REMARK anomalous f′ f′′ library: CNS_XRAYLIB: anom_cu.lib


REMARK reflection file = ../dm10_2A.cv


REMARK ncs = none


REMARK B-correction resolution: 6.0-2.0


REMARK initial B-factor correction applied to fobs:


REMARK  B11 =  1.410 B22 =  0.301 B33 =  −1.711


REMARK  B12 =  0.000 B13 =  0.000 B23 =    0.000


REMARK B-factor correction applied to coordinate array B: 0.605


REMARK bulk solvent: density level = 0.336734 e/A{circumflex over ( )}3, B-factor = 42.5542


A{circumflex over ( )}2


REMARK reflections with |Fobs|/sigma_F < 0.0 rejected


REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected


REMARK anomalous diffraction data was input


REMARK theoretical total number of refl. in resol. range: 84079


(100.0%)


REMARK number of unobserved reflections (no entry or |F| = 0): 821


(5.7%)








REMARK number of reflections rejected:
  0 ( 0.0% )


REMARK total number of reflections used:
79258 ( 94.3% )


REMARK number of reflections in working set:
76164 ( 90.6% )


REMARK number of reflections in test set:
 3094 ( 3.7% )














CRYST1
56.472
84.899
133.990
90.00
90.00
90.00
P 21 21 21








REMARK
VERSION: 1.1
















ATOM
1
CB
ALA
71
34.080
71.619
65.828
1.00
37.03


ATOM
2
C
ALA
71
36.046
70.116
66.197
1.00
37.52


ATOM
3
O
ALA
71
35.940
68.889
66.147
1.00
37.50


ATOM
4
N
ALA
71
35.606
72.021
67.727
1.00
37.87


ATOM
5
CA
ALA
71
34.977
70.970
66.876
1.00
37.06


ATOM
6
N
GLU
72
37.077
70.776
65.680
1.00
36.64


ATOM
7
CA
GLU
72
38.178
70.092
65.008
1.00
37.31


ATOM
8
CB
GLU
72
39.088
71.119
64.323
1.00
37.75


ATOM
9
CG
GLU
72
40.071
70.565
63.292
1.00
41.00


ATOM
10
CD
GLU
72
39.421
70.271
61.945
1.00
42.37


ATOM
11
OE1
GLU
72
38.580
71.081
61.495
1.00
42.32


ATOM
12
OE2
GLU
72
39.764
69.237
61.329
1.00
44.26


ATOM
13
C
GLU
72
38.973
69.307
66.051
1.00
37.09


ATOM
14
O
GLU
72
39.518
68.241
65.758
1.00
36.65


ATOM
15
N
ALA
73
39.030
69.841
67.270
1.00
35.26


ATOM
16
CA
ALA
73
39.751
69.193
68.361
1.00
33.85


ATOM
17
CB
ALA
73
39.874
70.140
69.549
1.00
34.20


ATOM
18
C
ALA
73
39.018
67.921
68.779
1.00
32.78


ATOM
19
O
ALA
73
39.640
66.900
69.076
1.00
32.36


ATOM
20
N
GLU
74
37.692
67.996
68.807
1.00
31.76


ATOM
21
CA
GLU
74
36.867
66.849
69.169
1.00
32.74


ATOM
22
CB
GLU
74
35.393
67.257
69.234
1.00
34.51


ATOM
23
CG
GLU
74
34.783
67.216
70.619
1.00
39.69


ATOM
24
CD
GLU
74
33.360
67.750
70.636
1.00
43.24


ATOM
25
OE1
GLU
74
32.467
67.110
70.032
1.00
44.62


ATOM
26
OE2
GLU
74
33.139
68.819
71.249
1.00
44.03


ATOM
27
C
GLU
74
37.036
65.758
68.118
1.00
31.08


ATOM
28
O
GLU
74
36.987
64.568
68.422
1.00
30.67


ATOM
29
N
ALA
75
37.242
66.185
66.877
1.00
29.99


ATOM
30
CA
ALA
75
37.399
65.267
65.754
1.00
28.87


ATOM
31
CB
ALA
75
37.351
66.043
64.442
1.00
27.23


ATOM
32
C
ALA
75
38.669
64.421
65.814
1.00
27.10


ATOM
33
O
ALA
75
38.608
63.201
65.663
1.00
26.57


ATOM
34
N
SER
76
39.817
65.060
66.027
1.00
26.04


ATOM
35
CA
SER
76
41.078
64.326
66.089
1.00
25.45


ATOM
36
CB
SER
76
42.268
65.290
66.137
1.00
26.93


ATOM
37
OG
SER
76
42.278
66.033
67.338
1.00
32.77


ATOM
38
C
SER
76
41.101
63.404
67.302
1.00
23.44


ATOM
39
O
SER
76
41.710
62.337
67.265
1.00
25.13


ATOM
40
N
LYS
77
40.438
63.823
68.373
1.00
22.27


ATOM
41
CA
LYS
77
40.354
63.024
69.589
1.00
21.77


ATOM
42
CB
LYS
77
39.744
63.856
70.717
1.00
25.02


ATOM
43
CG
LYS
77
39.406
63.069
71.974
1.00
28.89


ATOM
44
CD
LYS
77
38.810
63.983
73.038
1.00
34.02


ATOM
45
CE
LYS
77
37.827
63.235
73.916
1.00
36.45


ATOM
46
NZ
LYS
77
36.683
62.717
73.107
1.00
39.31


ATOM
47
C
LYS
77
39.484
61.798
69.315
1.00
20.85


ATOM
48
O
LYS
77
39.791
60.691
69.758
1.00
19.15


ATOM
49
N
PHE
78
38.395
62.005
68.582
1.00
20.00


ATOM
50
CA
PHE
78
37.497
60.912
68.232
1.00
20.44


ATOM
51
CB
PHE
78
36.323
61.433
67.399
1.00
20.72


ATOM
52
CG
PHE
78
35.490
60.344
66.779
1.00
22.38


ATOM
53
CD1
PHE
78
34.602
59.605
67.550
1.00
21.45


ATOM
54
CD2
PHE
78
35.612
60.045
65.427
1.00
21.21


ATOM
55
CE1
PHE
78
33.845
58.580
66.985
1.00
23.63


ATOM
56
CE2
PHE
78
34.860
59.021
64.853
1.00
24.14


ATOM
57
CZ
PHE
78
33.976
58.288
65.632
1.00
21.01


ATOM
58
C
PHE
78
38.274
59.878
67.421
1.00
19.50


ATOM
59
O
PHE
78
38.222
58.680
67.702
1.00
19.55


ATOM
60
N
VAL
79
39.004
60.358
66.418
1.00
20.22


ATOM
61
CA
VAL
79
39.790
59.484
65.556
1.00
21.86


ATOM
62
CB
VAL
79
40.528
60.312
64.473
1.00
23.18


ATOM
63
CG1
VAL
79
41.695
59.532
63.902
1.00
27.20


ATOM
64
CG2
VAL
79
39.555
60.661
63.355
1.00
23.07


ATOM
65
C
VAL
79
40.782
58.648
66.365
1.00
22.62


ATOM
66
O
VAL
79
40.920
57.445
66.132
1.00
22.22


ATOM
67
N
GLU
80
41.459
59.280
67.320
1.00
22.66


ATOM
68
CA
GLU
80
42.418
58.570
68.165
1.00
22.34


ATOM
69
CB
GLU
80
43.117
59.544
69.122
1.00
25.90


ATOM
70
CG
GLU
80
43.893
60.652
68.424
1.00
31.05


ATOM
71
CD
GLU
80
44.564
61.606
69.399
1.00
35.35


ATOM
72
OE1
GLU
80
43.881
62.088
70.333
1.00
36.66


ATOM
73
OE2
GLU
80
45.772
61.880
69.225
1.00
37.98


ATOM
74
C
GLU
80
41.726
57.475
68.977
1.00
20.25


ATOM
75
O
GLU
80
42.209
56.345
69.046
1.00
18.55


ATOM
76
N
GLU
81
40.595
57.811
69.595
1.00
18.66


ATOM
77
CA
GLU
81
39.863
56.836
70.399
1.00
19.96


ATOM
78
CB
GLU
81
38.702
57.512
71.134
1.00
21.24


ATOM
79
CG
GLU
81
39.168
58.560
72.135
1.00
23.95


ATOM
80
CD
GLU
81
38.027
59.258
72.845
1.00
26.18


ATOM
81
OE1
GLU
81
36.854
58.937
72.564
1.00
27.70


ATOM
82
OE2
GLU
81
38.311
60.133
73.691
1.00
28.83


ATOM
83
C
GLU
81
39.352
55.704
69.514
1.00
18.59


ATOM
84
O
GLU
81
39.428
54.529
69.881
1.00
16.88


ATOM
85
N
TYR
82
38.839
56.060
68.341
1.00
17.35


ATOM
86
CA
TYR
82
38.345
55.059
67.410
1.00
17.12


ATOM
87
CB
TYR
82
37.807
55.726
66.143
1.00
15.74


ATOM
88
CG
TYR
82
37.428
54.730
65.071
1.00
15.18


ATOM
89
CD1
TYR
82
36.303
53.918
65.217
1.00
13.96


ATOM
90
CE1
TYR
82
35.957
52.986
64.244
1.00
13.99


ATOM
91
CD2
TYR
82
38.204
54.583
63.924
1.00
14.71


ATOM
92
CE2
TYR
82
37.871
53.652
62.942
1.00
16.19


ATOM
93
CZ
TYR
82
36.744
52.862
63.108
1.00
15.36


ATOM
94
OH
TYR
82
36.388
51.969
62.131
1.00
14.06


ATOM
95
C
TYR
82
39.469
54.089
67.027
1.00
16.14


ATOM
96
O
TYR
82
39.279
52.876
67.018
1.00
15.38


ATOM
97
N
ASP
83
40.642
54.630
66.719
1.00
17.88


ATOM
98
CA
ASP
83
41.770
53.798
66.315
1.00
19.78


ATOM
99
CB
ASP
83
42.938
54.670
65.855
1.00
21.25


ATOM
100
CG
ASP
83
44.049
53.855
65.214
1.00
27.73


ATOM
101
OD1
ASP
83
43.791
53.214
64.168
1.00
30.70


ATOM
102
OD2
ASP
83
45.178
53.846
65.752
1.00
28.73


ATOM
103
C
ASP
83
42.267
52.835
67.394
1.00
20.18


ATOM
104
O
ASP
83
42.446
51.645
67.132
1.00
19.78


ATOM
105
N
ARG
84
42.497
53.338
68.604
1.00
19.30


ATOM
106
CA
ARG
84
42.994
52.461
69.656
1.00
21.26


ATOM
107
CB
ARG
84
43.473
53.271
70.871
1.00
22.61


ATOM
108
CG
ARG
84
42.506
54.308
71.400
1.00
24.22


ATOM
109
CD
ARG
84
43.054
54.955
72.673
1.00
24.57


ATOM
110
NE
ARG
84
44.153
55.891
72.435
1.00
24.09


ATOM
111
CZ
ARG
84
44.020
57.216
72.424
1.00
22.92


ATOM
112
NH1
ARG
84
42.833
57.772
72.633
1.00
23.01


ATOM
113
NH2
ARG
84
45.078
57.990
72.228
1.00
22.71


ATOM
114
C
ARG
84
41.987
51.395
70.075
1.00
19.10


ATOM
115
O
ARG
84
42.372
50.264
70.352
1.00
17.70


ATOM
116
N
THR
85
40.702
51.739
70.101
1.00
18.78


ATOM
117
CA
THR
85
39.685
50.762
70.482
1.00
18.36


ATOM
118
CB
THR
85
38.350
51.447
70.903
1.00
18.42


ATOM
119
OG1
THR
85
37.846
52.253
69.829
1.00
18.84


ATOM
120
CG2
THR
85
38.565
52.321
72.135
1.00
19.44


ATOM
121
C
THR
85
39.406
49.762
69.353
1.00
18.86


ATOM
122
O
THR
85
39.099
48.597
69.610
1.00
18.81


ATOM
123
N
SER
86
39.516
50.214
68.107
1.00
19.00


ATOM
124
CA
SER
86
39.269
49.338
66.962
1.00
19.38


ATOM
125
CB
SER
86
39.279
50.142
65.660
1.00
17.79


ATOM
126
OG
SER
86
38.175
51.031
65.605
1.00
18.69


ATOM
127
C
SER
86
40.305
48.219
66.885
1.00
20.96


ATOM
128
O
SER
86
39.966
47.060
66.630
1.00
21.64


ATOM
129
N
GLN
87
41.566
48.569
67.109
1.00
21.67


ATOM
130
CA
GLN
87
42.647
47.593
67.068
1.00
23.50


ATOM
131
CB
GLN
87
43.958
48.246
67.494
1.00
25.78


ATOM
132
CG
GLN
87
44.498
49.257
66.514
1.00
30.26


ATOM
133
CD
GLN
87
45.770
49.899
67.014
1.00
33.27


ATOM
134
OE1
GLN
87
46.693
49.212
67.453
1.00
35.56


ATOM
135
NE2
GLN
87
45.831
51.225
66.947
1.00
35.59


ATOM
136
C
GLN
87
42.370
46.401
67.978
1.00
23.44


ATOM
137
O
GLN
87
42.576
45.252
67.593
1.00
23.72


ATOM
138
N
VAL
88
41.908
46.684
69.190
1.00
23.72


ATOM
139
CA
VAL
88
41.616
45.635
70.154
1.00
22.98


ATOM
140
CB
VAL
88
41.316
46.234
71.546
1.00
24.62


ATOM
141
CG1
VAL
88
41.060
45.114
72.549
1.00
24.67


ATOM
142
CG2
VAL
88
42.486
47.102
72.004
1.00
23.17


ATOM
143
C
VAL
88
40.432
44.769
69.725
1.00
23.12


ATOM
144
O
VAL
88
40.536
43.543
69.672
1.00
21.83


ATOM
145
N
VAL
89
39.306
45.406
69.417
1.00
21.91


ATOM
146
CA
VAL
89
38.114
44.673
69.010
1.00
22.14


ATOM
147
CB
VAL
89
36.889
45.623
68.873
1.00
22.30


ATOM
148
CG1
VAL
89
37.197
46.738
67.901
1.00
25.90


ATOM
149
CG2
VAL
89
35.675
44.844
68.406
1.00
25.67


ATOM
150
C
VAL
89
38.317
43.904
67.700
1.00
21.76


ATOM
151
O
VAL
89
37.875
42.762
67.576
1.00
20.11


ATOM
152
N
TRP
90
38.980
44.526
66.728
1.00
21.83


ATOM
153
CA
TRP
90
39.224
43.868
65.448
1.00
22.98


ATOM
154
CB
TRP
90
39.759
44.873
64.419
1.00
24.28


ATOM
155
CG
TRP
90
38.739
45.905
63.988
1.00
28.97


ATOM
156
CD2
TRP
90
38.805
46.752
62.832
1.00
30.58


ATOM
157
CE2
TRP
90
37.665
47.586
62.859
1.00
31.50


ATOM
158
CE3
TRP
90
39.717
46.890
61.777
1.00
31.93


ATOM
159
CD1
TRP
90
37.593
46.250
64.645
1.00
30.90


ATOM
160
NE1
TRP
90
36.943
47.257
63.975
1.00
30.56


ATOM
161
CZ2
TRP
90
37.411
48.546
61.871
1.00
32.79


ATOM
162
CZ3
TRP
90
39.464
47.847
60.792
1.00
33.43


ATOM
163
CH2
TRP
90
38.319
48.662
60.850
1.00
32.95


ATOM
164
C
TRP
90
40.207
42.714
65.622
1.00
21.98


ATOM
165
O
TRP
90
40.089
41.692
64.957
1.00
22.45


ATOM
166
N
ASN
91
41.175
42.870
66.518
1.00
22.59


ATOM
167
CA
ASN
91
42.137
41.799
66.744
1.00
23.45


ATOM
168
CB
ASN
91
43.253
42.245
67.690
1.00
22.82


ATOM
169
CG
ASN
91
44.153
41.091
68.103
1.00
25.02


ATOM
170
OD1
ASN
91
43.810
40.313
68.993
1.00
26.35


ATOM
171
ND2
ASN
91
45.301
40.961
67.442
1.00
25.21


ATOM
172
C
ASN
91
41.434
40.577
67.321
1.00
24.29


ATOM
173
O
ASN
91
41.721
39.443
66.929
1.00
24.22


ATOM
174
N
GLU
92
40.511
40.813
68.249
1.00
23.78


ATOM
175
CA
GLU
92
39.767
39.726
68.863
1.00
24.44


ATOM
176
CB
GLU
92
38.940
40.242
70.046
1.00
27.98


ATOM
177
CG
GLU
92
39.655
40.108
71.386
1.00
32.87


ATOM
178
CD
GLU
92
38.998
40.903
72.502
1.00
33.99


ATOM
179
OE1
GLU
92
37.797
40.691
72.771
1.00
36.12


ATOM
180
OE2
GLU
92
39.690
41.740
73.116
1.00
35.60


ATOM
181
C
GLU
92
38.859
39.041
67.857
1.00
24.09


ATOM
182
O
GLU
92
38.731
37.817
67.867
1.00
25.43


ATOM
183
N
TYR
93
38.230
39.824
66.987
1.00
22.66


ATOM
184
CA
TYR
93
37.343
39.253
65.982
1.00
22.78


ATOM
185
CB
TYR
93
36.609
40.346
65.202
1.00
23.71


ATOM
186
CG
TYR
93
35.739
39.782
64.102
1.00
24.71


ATOM
187
CD1
TYR
93
34.533
39.149
64.398
1.00
25.73


ATOM
188
CE1
TYR
93
33.759
38.563
63.398
1.00
27.34


ATOM
189
CD2
TYR
93
36.152
39.820
62.771
1.00
27.78


ATOM
190
CE2
TYR
93
35.389
39.235
61.761
1.00
28.66


ATOM
191
CZ
TYR
93
34.194
38.608
62.083
1.00
28.76


ATOM
192
OH
TYR
93
33.441
38.020
61.093
1.00
30.77


ATOM
193
C
TYR
93
38.140
38.401
65.002
1.00
21.84


ATOM
194
O
TYR
93
37.705
37.319
64.608
1.00
20.79


ATOM
195
N
ALA
94
39.304
38.902
64.605
1.00
21.93


ATOM
196
CA
ALA
94
40.160
38.185
63.669
1.00
23.19


ATOM
197
CB
ALA
94
41.438
38.984
63.415
1.00
21.92


ATOM
198
C
ALA
94
40.501
36.803
64.223
1.00
22.67


ATOM
199
O
ALA
94
40.570
35.824
63.480
1.00
23.01


ATOM
200
N
ALA
95
40.701
36.733
65.536
1.00
24.22


ATOM
201
CA
ALA
95
41.041
35.482
66.210
1.00
24.36


ATOM
202
CB
ALA
95
41.354
35.757
67.676
1.00
28.15


ATOM
203
C
ALA
95
39.922
34.455
66.105
1.00
24.75


ATOM
204
O
ALA
95
40.147
33.311
65.707
1.00
25.33


ATOM
205
N
ALA
96
38.715
34.867
66.474
1.00
24.39


ATOM
206
CA
ALA
96
37.563
33.978
66.421
1.00
24.27


ATOM
207
CB
ALA
96
36.350
34.670
67.026
1.00
23.28


ATOM
208
C
ALA
96
37.266
33.552
64.984
1.00
23.78


ATOM
209
O
ALA
96
36.898
32.403
64.724
1.00
23.70


ATOM
210
N
ASN
97
37.426
34.483
64.051
1.00
21.38


ATOM
211
CA
ASN
97
37.162
34.200
62.647
1.00
22.12


ATOM
212
CB
ASN
97
37.224
35.506
61.845
1.00
20.92


ATOM
213
CG
ASN
97
36.706
35.353
60.433
1.00
22.34


ATOM
214
OD1
ASN
97
35.908
34.459
60.140
1.00
20.62


ATOM
215
ND2
ASN
97
37.144
36.243
59.548
1.00
20.25


ATOM
216
C
ASN
97
38.192
33.189
62.142
1.00
21.72


ATOM
217
O
ASN
97
37.863
32.270
61.393
1.00
21.75


ATOM
218
N
TRP
98
39.437
33.353
62.576
1.00
21.37


ATOM
219
CA
TRP
98
40.502
32.449
62.172
1.00
23.30


ATOM
220
CB
TRP
98
41.856
32.963
62.676
1.00
21.74


ATOM
221
CG
TRP
98
42.995
32.002
62.444
1.00
23.76


ATOM
222
CD2
TRP
98
43.871
31.960
61.305
1.00
22.12


ATOM
223
CE2
TRP
98
44.772
30.891
61.510
1.00
23.47


ATOM
224
CE3
TRP
98
43.979
32.720
60.131
1.00
21.74


ATOM
225
CD1
TRP
98
43.390
30.985
63.266
1.00
23.18


ATOM
226
NE1
TRP
98
44.456
30.314
62.712
1.00
24.63


ATOM
227
CZ2
TRP
98
45.772
30.562
60.584
1.00
21.94


ATOM
228
CZ3
TRP
98
44.973
32.392
59.209
1.00
20.39


ATOM
229
CH2
TRP
98
45.856
31.320
59.444
1.00
20.85


ATOM
230
C
TRP
98
40.251
31.041
62.702
1.00
23.90


ATOM
231
O
TRP
98
40.306
30.061
61.953
1.00
21.48


ATOM
232
N
ASN
99
39.963
30.945
63.997
1.00
25.31


ATOM
233
CA
ASN
99
39.716
29.648
64.619
1.00
24.92


ATOM
234
CB
ASN
99
39.393
29.820
66.103
1.00
24.71


ATOM
235
CG
ASN
99
40.545
30.430
66.874
1.00
25.68


ATOM
236
OD1
ASN
99
41.690
30.397
66.423
1.00
26.00


ATOM
237
ND2
ASN
99
40.252
30.980
68.046
1.00
25.62


ATOM
238
C
ASN
99
38.594
28.901
63.922
1.00
24.14


ATOM
239
O
ASN
99
38.627
27.674
63.820
1.00
24.01


ATOM
240
N
TYR
100
37.600
29.633
63.433
1.00
23.70


ATOM
241
CA
TYR
100
36.504
28.978
62.738
1.00
23.65


ATOM
242
CB
TYR
100
35.312
29.912
62.567
1.00
27.83


ATOM
243
CG
TYR
100
34.175
29.198
61.890
1.00
30.19


ATOM
244
CD1
TYR
100
33.577
28.097
62.496
1.00
31.92


ATOM
245
CE1
TYR
100
32.587
27.378
61.856
1.00
35.09


ATOM
246
CD2
TYR
100
33.746
29.567
60.617
1.00
32.59


ATOM
247
CE2
TYR
100
32.746
28.848
59.961
1.00
33.60


ATOM
248
CZ
TYR
100
32.173
27.755
60.591
1.00
34.32


ATOM
249
OH
TYR
100
31.182
27.031
59.973
1.00
36.77


ATOM
250
C
TYR
100
36.943
28.492
61.360
1.00
22.55


ATOM
251
O
TYR
100
36.656
27.362
60.971
1.00
20.86


ATOM
252
N
ASN
101
37.628
29.360
60.622
1.00
21.15


ATOM
253
CA
ASN
101
38.114
29.029
59.286
1.00
20.76


ATOM
254
CB
ASN
101
38.798
30.251
58.655
1.00
19.09


ATOM
255
CG
ASN
101
37.838
31.110
57.853
1.00
18.55


ATOM
256
OD1
ASN
101
37.829
31.067
56.624
1.00
19.63


ATOM
257
ND2
ASN
101
37.018
31.892
58.546
1.00
18.23


ATOM
258
C
ASN
101
39.089
27.852
59.295
1.00
20.96


ATOM
259
O
ASN
101
39.149
27.084
58.332
1.00
21.16


ATOM
260
N
THR
102
39.851
27.714
60.378
1.00
19.64


ATOM
261
CA
THR
102
40.826
26.635
60.488
1.00
19.80


ATOM
262
CB
THR
102
42.158
27.152
61.056
1.00
18.90


ATOM
263
OG1
THR
102
41.937
27.725
62.347
1.00
19.19


ATOM
264
CG2
THR
102
42.756
28.207
60.137
1.00
21.98


ATOM
265
C
THR
102
40.356
25.450
61.339
1.00
21.84


ATOM
266
O
THR
102
41.139
24.549
61.642
1.00
21.38


ATOM
267
N
ASN
103
39.084
25.454
61.724
1.00
22.72


ATOM
268
CA
ASN
103
38.514
24.365
62.518
1.00
24.63


ATOM
269
CB
ASN
103
39.149
24.313
63.919
1.00
26.53


ATOM
270
CG
ASN
103
38.705
23.085
64.720
1.00
29.25


ATOM
271
OD1
ASN
103
38.126
22.147
64.171
1.00
29.00


ATOM
272
ND2
ASN
103
38.989
23.088
66.020
1.00
31.72


ATOM
273
C
ASN
103
37.012
24.567
62.626
1.00
23.73


ATOM
274
O
ASN
103
36.502
25.032
63.643
1.00
24.12


ATOM
275
N
ILE
104
36.313
24.224
61.551
1.00
25.67


ATOM
276
CA
ILE
104
34.867
24.367
61.489
1.00
27.61


ATOM
277
CB
ILE
104
34.338
24.109
60.059
1.00
28.22


ATOM
278
CG2
ILE
104
32.821
24.281
60.027
1.00
29.99


ATOM
279
CG1
ILE
104
35.005
25.069
59.072
1.00
29.22


ATOM
280
CD1
ILE
104
34.560
24.879
57.626
1.00
29.37


ATOM
281
C
ILE
104
34.169
23.403
62.439
1.00
28.58


ATOM
282
O
ILE
104
34.079
22.207
62.168
1.00
28.13


ATOM
283
N
THR
105
33.683
23.936
63.555
1.00
30.58


ATOM
284
CA
THR
105
32.968
23.143
64.549
1.00
31.89


ATOM
285
CB
THR
105
33.843
22.821
65.775
1.00
31.98


ATOM
286
OG1
THR
105
34.107
24.026
66.506
1.00
33.11


ATOM
287
CG2
THR
105
35.162
22.194
65.341
1.00
32.86


ATOM
288
C
THR
105
31.783
23.971
65.017
1.00
32.44


ATOM
289
O
THR
105
31.752
25.188
64.827
1.00
32.52


ATOM
290
N
THR
106
30.803
23.319
65.623
1.00
33.00


ATOM
291
CA
THR
106
29.640
24.044
66.109
1.00
33.81


ATOM
292
CB
THR
106
28.570
23.072
66.662
1.00
34.97


ATOM
293
OG1
THR
106
27.463
23.818
67.184
1.00
37.98


ATOM
294
CG2
THR
106
29.155
22.199
67.752
1.00
34.76


ATOM
295
C
THR
106
30.093
25.020
67.198
1.00
32.47


ATOM
296
O
THR
106
29.512
26.094
67.361
1.00
31.96


ATOM
297
N
GLU
107
31.153
24.655
67.917
1.00
31.54


ATOM
298
CA
GLU
107
31.687
25.501
68.985
1.00
32.42


ATOM
299
CB
GLU
107
32.731
24.740
69.809
1.00
34.68


ATOM
300
CG
GLU
107
32.272
23.390
70.349
1.00
40.20


ATOM
301
CD
GLU
107
32.542
22.243
69.385
1.00
42.52


ATOM
302
OE1
GLU
107
31.917
22.202
68.304
1.00
44.41


ATOM
303
OE2
GLU
107
33.390
21.383
69.710
1.00
44.47


ATOM
304
C
GLU
107
32.327
26.783
68.445
1.00
31.96


ATOM
305
O
GLU
107
31.980
27.883
68.875
1.00
31.54


ATOM
306
N
THR
108
33.272
26.641
67.516
1.00
30.47


ATOM
307
CA
THR
108
33.935
27.807
66.939
1.00
29.64


ATOM
308
CB
THR
108
35.056
27.402
65.946
1.00
29.18


ATOM
309
OG1
THR
108
34.534
26.500
64.964
1.00
30.34


ATOM
310
CG2
THR
108
36.210
26.741
66.683
1.00
26.97


ATOM
311
C
THR
108
32.916
28.689
66.219
1.00
29.12


ATOM
312
O
THR
108
33.050
29.911
66.201
1.00
29.17


ATOM
313
N
SER
109
31.895
28.069
65.631
1.00
28.85


ATOM
314
CA
SER
109
30.851
28.822
64.937
1.00
29.69


ATOM
315
CB
SER
109
29.809
27.885
64.321
1.00
29.41


ATOM
316
OG
SER
109
30.254
27.336
63.098
1.00
31.41


ATOM
317
C
SER
109
30.144
29.737
65.923
1.00
30.53


ATOM
318
O
SER
109
29.992
30.936
65.679
1.00
27.87


ATOM
319
N
LYS
110
29.715
29.150
67.036
1.00
31.92


ATOM
320
CA
LYS
110
29.002
29.876
68.077
1.00
33.73


ATOM
321
CB
LYS
110
28.653
28.927
69.229
1.00
35.14


ATOM
322
CG
LYS
110
27.472
29.384
70.080
1.00
38.08


ATOM
323
CD
LYS
110
27.054
28.310
71.080
1.00
39.49


ATOM
324
CE
LYS
110
25.706
28.637
71.707
1.00
40.76


ATOM
325
NZ
LYS
110
25.254
27.575
72.650
1.00
40.35


ATOM
326
C
LYS
110
29.820
31.053
68.595
1.00
32.96


ATOM
327
O
LYS
110
29.301
32.157
68.747
1.00
33.66


ATOM
328
N
ILE
111
31.101
30.820
68.858
1.00
32.50


ATOM
329
CA
ILE
111
31.972
31.876
69.357
1.00
31.17


ATOM
330
CB
ILE
111
33.354
31.318
69.722
1.00
30.98


ATOM
331
CG2
ILE
111
34.278
32.448
70.166
1.00
29.81


ATOM
332
CG1
ILE
111
33.205
30.271
70.828
1.00
31.92


ATOM
333
CD1
ILE
111
34.494
29.560
71.183
1.00
31.87


ATOM
334
C
ILE
111
32.138
33.002
68.334
1.00
30.85


ATOM
335
O
ILE
111
32.164
34.180
68.693
1.00
31.16


ATOM
336
N
LEU
112
32.247
32.635
67.061
1.00
29.75


ATOM
337
CA
LEU
112
32.404
33.629
66.007
1.00
28.55


ATOM
338
CB
LEU
112
32.644
32.948
64.656
1.00
27.63


ATOM
339
CG
LEU
112
32.720
33.872
63.430
1.00
26.14


ATOM
340
CD1
LEU
112
33.789
34.938
63.643
1.00
22.46


ATOM
341
CD2
LEU
112
33.021
33.046
62.187
1.00
24.13


ATOM
342
C
LEU
112
31.178
34.529
65.917
1.00
29.28


ATOM
343
O
LEU
112
31.303
35.754
65.907
1.00
29.00


ATOM
344
N
LEU
113
29.997
33.921
65.853
1.00
29.16


ATOM
345
CA
LEU
113
28.754
34.680
65.761
1.00
29.91


ATOM
346
CB
LEU
113
27.552
33.730
65.669
1.00
29.27


ATOM
347
CG
LEU
113
27.451
32.874
64.397
1.00
29.32


ATOM
348
CD1
LEU
113
26.281
31.905
64.514
1.00
30.07


ATOM
349
CD2
LEU
113
27.279
33.777
63.179
1.00
29.18


ATOM
350
C
LEU
113
28.590
35.624
66.950
1.00
31.04


ATOM
351
O
LEU
113
27.976
36.685
66.831
1.00
30.89


ATOM
352
N
GLN
114
29.143
35.234
68.095
1.00
32.01


ATOM
353
CA
GLN
114
29.074
36.057
69.297
1.00
33.69


ATOM
354
CB
GLN
114
29.403
35.218
70.537
1.00
35.55


ATOM
355
CG
GLN
114
28.383
34.113
70.801
1.00
40.14


ATOM
356
CD
GLN
114
28.764
33.207
71.960
1.00
43.52


ATOM
357
OE1
GLN
114
28.850
33.644
73.110
1.00
44.43


ATOM
358
NE2
GLN
114
28.996
31.932
71.658
1.00
44.83


ATOM
359
C
GLN
114
30.060
37.208
69.157
1.00
33.40


ATOM
360
O
GLN
114
29.773
38.336
69.555
1.00
32.65


ATOM
361
N
LYS
115
31.224
36.918
68.587
1.00
33.87


ATOM
362
CA
LYS
115
32.235
37.944
68.369
1.00
33.82


ATOM
363
CB
LYS
115
33.547
37.318
67.889
1.00
36.05


ATOM
364
CG
LYS
115
34.622
37.276
68.960
1.00
39.80


ATOM
365
CD
LYS
115
34.924
38.684
69.443
1.00
42.99


ATOM
366
CE
LYS
115
35.903
38.699
70.598
1.00
45.69


ATOM
367
NZ
LYS
115
36.078
40.092
71.099
1.00
48.43


ATOM
368
C
LYS
115
31.718
38.937
67.335
1.00
32.81


ATOM
369
O
LYS
115
32.132
40.094
67.310
1.00
30.93


ATOM
370
N
ASN
116
30.813
38.472
66.480
1.00
32.71


ATOM
371
CA
ASN
116
30.215
39.325
65.458
1.00
33.77


ATOM
372
CB
ASN
116
29.223
38.530
64.602
1.00
34.22


ATOM
373
CG
ASN
116
29.855
37.950
63.356
1.00
35.11


ATOM
374
OD1
ASN
116
30.356
38.683
62.502
1.00
35.08


ATOM
375
ND2
ASN
116
29.827
36.627
63.239
1.00
37.76


ATOM
376
C
ASN
116
29.465
40.459
66.146
1.00
33.07


ATOM
377
O
ASN
116
29.675
41.632
65.847
1.00
32.40


ATOM
378
N
MET
117
28.586
40.086
67.070
1.00
33.09


ATOM
379
CA
MET
117
27.783
41.044
67.812
1.00
32.98


ATOM
380
CB
MET
117
26.843
40.299
68.764
1.00
34.71


ATOM
381
CG
MET
117
25.382
40.289
68.317
1.00
39.02


ATOM
382
SD
MET
117
25.127
39.995
66.544
1.00
41.96


ATOM
383
CE
MET
117
23.347
40.015
66.451
1.00
41.75


ATOM
384
C
MET
117
28.638
42.039
68.585
1.00
31.36


ATOM
385
O
MET
117
28.287
43.212
68.697
1.00
29.55


ATOM
386
N
GLN
118
29.768
41.576
69.106
1.00
31.05


ATOM
387
CA
GLN
118
30.653
42.447
69.868
1.00
31.16


ATOM
388
CB
GLN
118
31.741
41.625
70.563
1.00
34.52


ATOM
389
CG
GLN
118
31.195
40.567
71.509
1.00
38.71


ATOM
390
CD
GLN
118
32.270
39.974
72.402
1.00
41.62


ATOM
391
OE1
GLN
118
33.294
39.485
71.922
1.00
43.74


ATOM
392
NE2
GLN
118
32.039
40.013
73.711
1.00
42.41


ATOM
393
C
GLN
118
31.298
43.519
68.999
1.00
29.23


ATOM
394
O
GLN
118
31.318
44.698
69.365
1.00
28.92


ATOM
395
N
ILE
119
31.822
43.120
67.846
1.00
25.46


ATOM
396
CA
ILE
119
32.457
44.081
66.957
1.00
24.61


ATOM
397
CB
ILE
119
33.281
43.365
65.853
1.00
25.09


ATOM
398
CG2
ILE
119
32.362
42.581
64.923
1.00
24.21


ATOM
399
CG1
ILE
119
34.096
44.392
65.071
1.00
25.85


ATOM
400
CD1
ILE
119
35.175
43.779
64.208
1.00
26.22


ATOM
401
C
ILE
119
31.401
44.995
66.329
1.00
22.47


ATOM
402
O
ILE
119
31.674
46.153
66.003
1.00
22.00


ATOM
403
N
ALA
120
30.187
44.481
66.171
1.00
21.10


ATOM
404
CA
ALA
120
29.109
45.283
65.599
1.00
22.02


ATOM
405
CB
ALA
120
27.902
44.401
65.294
1.00
20.08


ATOM
406
C
ALA
120
28.734
46.359
66.616
1.00
22.84


ATOM
407
O
ALA
120
28.410
47.490
66.264
1.00
22.93


ATOM
408
N
ASN
121
28.790
45.987
67.888
1.00
21.65


ATOM
409
CA
ASN
121
28.468
46.901
68.970
1.00
23.13


ATOM
410
CB
ASN
121
28.572
46.166
70.300
1.00
27.59


ATOM
411
CG
ASN
121
27.649
46.732
71.342
1.00
34.63


ATOM
412
OD1
ASN
121
28.016
47.635
72.096
1.00
39.08


ATOM
413
ND2
ASN
121
26.427
46.206
71.389
1.00
38.10


ATOM
414
C
ASN
121
29.428
48.086
68.951
1.00
21.02


ATOM
415
O
ASN
121
29.020
49.241
69.101
1.00
20.93


ATOM
416
N
HIS
122
30.710
47.789
68.776
1.00
17.91


ATOM
417
CA
HIS
122
31.739
48.817
68.716
1.00
17.11


ATOM
418
CB
HIS
122
33.122
48.152
68.661
1.00
15.18


ATOM
419
CG
HIS
122
34.235
49.093
68.327
1.00
16.93


ATOM
420
CD2
HIS
122
35.035
49.844
69.119
1.00
15.16


ATOM
421
ND1
HIS
122
34.617
49.363
67.031
1.00
18.07


ATOM
422
CE1
HIS
122
35.606
50.240
67.041
1.00
18.19


ATOM
423
NE2
HIS
122
35.879
50.547
68.296
1.00
15.55


ATOM
424
C
HIS
122
31.520
49.698
67.487
1.00
17.81


ATOM
425
O
HIS
122
31.628
50.925
67.556
1.00
18.93


ATOM
426
N
THR
123
31.213
49.066
66.360
1.00
17.71


ATOM
427
CA
THR
123
30.983
49.794
65.117
1.00
18.02


ATOM
428
CB
THR
123
30.700
48.823
63.956
1.00
17.98


ATOM
429
OG1
THR
123
31.807
47.926
63.810
1.00
16.69


ATOM
430
CG2
THR
123
30.494
49.591
62.646
1.00
18.45


ATOM
431
C
THR
123
29.808
50.758
65.260
1.00
18.44


ATOM
432
O
THR
123
29.872
51.903
64.817
1.00
18.36


ATOM
433
N
LEU
124
28.737
50.292
65.886
1.00
19.48


ATOM
434
CA
LEU
124
27.556
51.123
66.083
1.00
21.69


ATOM
435
CB
LEU
124
26.407
50.264
66.625
1.00
22.76


ATOM
436
CG
LEU
124
25.009
50.870
66.792
1.00
25.84


ATOM
437
CD1
LEU
124
24.634
51.743
65.596
1.00
26.67


ATOM
438
CD2
LEU
124
24.015
49.731
66.952
1.00
28.14


ATOM
439
C
LEU
124
27.849
52.293
67.028
1.00
22.10


ATOM
440
O
LEU
124
27.395
53.414
66.805
1.00
22.48


ATOM
441
N
LYS
125
28.619
52.029
68.077
1.00
21.30


ATOM
442
CA
LYS
125
28.968
53.061
69.044
1.00
21.15


ATOM
443
CB
LYS
125
29.826
52.468
70.165
1.00
22.88


ATOM
444
CG
LYS
125
30.218
53.462
71.247
1.00
24.84


ATOM
445
CD
LYS
125
31.157
52.829
72.267
1.00
27.95


ATOM
446
CE
LYS
125
31.480
53.799
73.392
1.00
30.77


ATOM
447
NZ
LYS
125
31.992
55.102
72.875
1.00
33.91


ATOM
448
C
LYS
125
29.727
54.203
68.377
1.00
20.96


ATOM
449
O
LYS
125
29.344
55.367
68.492
1.00
20.95


ATOM
450
N
TYR
126
30.805
53.869
67.675
1.00
18.64


ATOM
451
CA
TYR
126
31.598
54.893
67.020
1.00
17.79


ATOM
452
CB
TYR
126
33.026
54.388
66.782
1.00
18.37


ATOM
453
CG
TYR
126
33.817
54.315
68.071
1.00
20.45


ATOM
454
CD1
TYR
126
33.687
53.226
68.934
1.00
20.37


ATOM
455
CE1
TYR
126
34.326
53.209
70.171
1.00
21.90


ATOM
456
CD2
TYR
126
34.618
55.383
68.476
1.00
20.13


ATOM
457
CE2
TYR
126
35.260
55.376
69.710
1.00
21.70


ATOM
458
CZ
TYR
126
35.107
54.290
70.552
1.00
21.90


ATOM
459
OH
TYR
126
35.717
54.301
71.783
1.00
22.74


ATOM
460
C
TYR
126
30.983
55.411
65.733
1.00
16.79


ATOM
461
O
TYR
126
31.168
56.573
65.383
1.00
17.06


ATOM
462
N
GLY
127
30.239
54.554
65.038
1.00
17.21


ATOM
463
CA
GLY
127
29.596
54.977
63.806
1.00
16.33


ATOM
464
C
GLY
127
28.534
56.020
64.099
1.00
17.87


ATOM
465
O
GLY
127
28.366
56.984
63.351
1.00
17.27


ATOM
466
N
THR
128
27.815
55.825
65.199
1.00
17.84


ATOM
467
CA
THR
128
26.774
56.759
65.607
1.00
19.72


ATOM
468
CB
THR
128
25.997
56.216
66.826
1.00
19.70


ATOM
469
OG1
THR
128
25.413
54.951
66.487
1.00
21.12


ATOM
470
CG2
THR
128
24.896
57.188
67.244
1.00
20.40


ATOM
471
C
THR
128
27.409
58.107
65.958
1.00
20.53


ATOM
472
O
THR
128
26.887
59.161
65.599
1.00
20.68


ATOM
473
N
GLN
129
28.542
58.064
66.655
1.00
21.83


ATOM
474
CA
GLN
129
29.262
59.280
67.038
1.00
21.59


ATOM
475
CB
GLN
129
30.455
58.939
67.938
1.00
26.47


ATOM
476
CG
GLN
129
30.215
59.095
69.432
1.00
31.89


ATOM
477
CD
GLN
129
31.440
58.719
70.262
1.00
34.85


ATOM
478
OE1
GLN
129
31.608
57.567
70.666
1.00
35.57


ATOM
479
NE2
GLN
129
32.310
59.693
70.504
1.00
36.98


ATOM
480
C
GLN
129
29.781
60.020
65.810
1.00
20.77


ATOM
481
O
GLN
129
29.638
61.238
65.698
1.00
19.33


ATOM
482
N
ALA
130
30.389
59.270
64.896
1.00
18.52


ATOM
483
CA
ALA
130
30.956
59.831
63.673
1.00
17.79


ATOM
484
CB
ALA
130
31.622
58.722
62.858
1.00
17.56


ATOM
485
C
ALA
130
29.927
60.561
62.815
1.00
16.56


ATOM
486
O
ALA
130
30.245
61.547
62.156
1.00
16.12


ATOM
487
N
ARG
131
28.697
60.066
62.817
1.00
17.47


ATOM
488
CA
ARG
131
27.634
60.680
62.036
1.00
19.03


ATOM
489
CB
ARG
131
26.436
59.736
61.952
1.00
18.10


ATOM
490
CG
ARG
131
26.676
58.528
61.066
1.00
18.60


ATOM
491
CD
ARG
131
25.435
57.669
60.979
1.00
20.30


ATOM
492
NE
ARG
131
25.604
56.546
60.062
1.00
17.51


ATOM
493
CZ
ARG
131
24.642
55.679
59.766
1.00
19.71


ATOM
494
NH1
ARG
131
23.441
55.803
60.317
1.00
17.67


ATOM
495
NH2
ARG
131
24.877
54.692
58.910
1.00
19.33


ATOM
496
C
ARG
131
27.188
62.030
62.599
1.00
21.80


ATOM
497
O
ARG
131
26.512
62.801
61.913
1.00
20.73


ATOM
498
N
LYS
132
27.562
62.309
63.844
1.00
22.02


ATOM
499
CA
LYS
132
27.195
63.569
64.479
1.00
24.28


ATOM
500
CB
LYS
132
27.232
63.425
66.002
1.00
25.70


ATOM
501
CG
LYS
132
26.128
62.535
66.553
1.00
31.41


ATOM
502
CD
LYS
132
26.278
62.309
68.048
1.00
33.41


ATOM
503
CE
LYS
132
25.149
61.442
68.580
1.00
36.75


ATOM
504
NZ
LYS
132
25.398
60.989
69.977
1.00
38.85


ATOM
505
C
LYS
132
28.113
64.698
64.036
1.00
24.23


ATOM
506
O
LYS
132
27.815
65.872
64.255
1.00
24.28


ATOM
507
N
PHE
133
29.235
64.344
63.417
1.00
25.03


ATOM
508
CA
PHE
133
30.178
65.347
62.928
1.00
26.68


ATOM
509
CB
PHE
133
31.606
64.786
62.822
1.00
26.18


ATOM
510
CG
PHE
133
32.297
64.597
64.140
1.00
26.01


ATOM
511
CD1
PHE
133
32.189
63.396
64.833
1.00
26.90


ATOM
512
CD2
PHE
133
33.063
65.625
64.686
1.00
27.15


ATOM
513
CE1
PHE
133
32.837
63.218
66.057
1.00
28.34


ATOM
514
CE2
PHE
133
33.714
65.461
65.909
1.00
26.84


ATOM
515
CZ
PHE
133
33.602
64.256
66.595
1.00
27.99


ATOM
516
C
PHE
133
29.766
65.801
61.540
1.00
27.95


ATOM
517
O
PHE
133
29.350
64.989
60.714
1.00
28.75


ATOM
518
N
ASP
134
29.876
67.099
61.281
1.00
29.55


ATOM
519
CA
ASP
134
29.561
67.611
59.957
1.00
30.26


ATOM
520
CB
ASP
134
29.048
69.051
60.007
1.00
32.19


ATOM
521
CG
ASP
134
28.560
69.538
58.648
1.00
32.97


ATOM
522
OD1
ASP
134
29.035
69.008
57.620
1.00
33.76


ATOM
523
OD2
ASP
134
27.710
70.450
58.602
1.00
35.71


ATOM
524
C
ASP
134
30.896
67.577
59.231
1.00
30.16


ATOM
525
O
ASP
134
31.721
68.478
59.381
1.00
30.39


ATOM
526
N
VAL
135
31.110
66.522
58.457
1.00
31.36


ATOM
527
CA
VAL
135
32.353
66.354
57.722
1.00
31.74


ATOM
528
CB
VAL
135
32.308
65.059
56.880
1.00
32.36


ATOM
529
CG1
VAL
135
33.587
64.904
56.083
1.00
33.06


ATOM
530
CG2
VAL
135
32.113
63.864
57.794
1.00
31.68


ATOM
531
C
VAL
135
32.660
67.549
56.820
1.00
32.14


ATOM
532
O
VAL
135
33.824
67.884
56.599
1.00
32.77


ATOM
533
N
ASN
136
31.615
68.194
56.310
1.00
32.14


ATOM
534
CA
ASN
136
31.790
69.346
55.432
1.00
34.09


ATOM
535
CB
ASN
136
30.430
69.871
54.961
1.00
34.55


ATOM
536
CG
ASN
136
29.697
68.881
54.079
1.00
36.54


ATOM
537
OD1
ASN
136
30.246
68.397
53.089
1.00
34.66


ATOM
538
ND2
ASN
136
28.449
68.575
54.433
1.00
35.78


ATOM
539
C
ASN
136
32.555
70.478
56.103
1.00
34.86


ATOM
540
O
ASN
136
33.238
71.251
55.436
1.00
34.66


ATOM
541
N
GLN
137
32.445
70.568
57.424
1.00
36.37


ATOM
542
CA
GLN
137
33.114
71.628
58.171
1.00
37.67


ATOM
543
CB
GLN
137
32.192
72.122
59.290
1.00
40.06


ATOM
544
CG
GLN
137
30.886
72.738
58.797
1.00
43.99


ATOM
545
CD
GLN
137
31.108
73.973
57.939
1.00
47.20


ATOM
546
OE1
GLN
137
31.777
74.922
58.355
1.00
49.72


ATOM
547
NE2
GLN
137
30.540
73.970
56.736
1.00
49.42


ATOM
548
C
GLN
137
34.471
71.237
58.756
1.00
36.89


ATOM
549
O
GLN
137
35.136
72.057
59.389
1.00
36.28


ATOM
550
N
LEU
138
34.886
69.992
58.539
1.00
36.72


ATOM
551
CA
LEU
138
36.162
69.516
59.061
1.00
35.87


ATOM
552
CB
LEU
138
36.140
67.991
59.166
1.00
36.10


ATOM
553
CG
LEU
138
36.216
67.413
60.585
1.00
36.93


ATOM
554
CD1
LEU
138
35.438
68.279
61.565
1.00
36.66


ATOM
555
CD2
LEU
138
35.678
65.994
60.576
1.00
37.81


ATOM
556
C
LEU
138
37.330
69.980
58.198
1.00
36.49


ATOM
557
O
LEU
138
37.350
69.764
56.987
1.00
37.24


ATOM
558
N
GLN
139
38.310
70.612
58.837
1.00
36.86


ATOM
559
CA
GLN
139
39.476
71.144
58.140
1.00
37.44


ATOM
560
CB
GLN
139
40.141
72.224
58.995
1.00
39.57


ATOM
561
CG
GLN
139
40.513
73.479
58.225
1.00
43.68


ATOM
562
CD
GLN
139
39.295
74.262
57.761
1.00
46.04


ATOM
563
OE1
GLN
139
38.423
73.729
57.070
1.00
48.18


ATOM
564
NE2
GLN
139
39.230
75.535
58.138
1.00
46.25


ATOM
565
C
GLN
139
40.516
70.094
57.755
1.00
36.44


ATOM
566
O
GLN
139
40.868
69.970
56.583
1.00
37.59


ATOM
567
N
ASN
140
41.016
69.353
58.739
1.00
35.34


ATOM
568
CA
ASN
140
42.018
68.320
58.486
1.00
34.29


ATOM
569
CB
ASN
140
42.428
67.659
59.807
1.00
35.01


ATOM
570
CG
ASN
140
43.640
66.763
59.660
1.00
36.54


ATOM
571
OD1
ASN
140
43.676
65.880
58.801
1.00
37.38


ATOM
572
ND2
ASN
140
44.643
66.982
60.504
1.00
38.59


ATOM
573
C
ASN
140
41.443
67.273
57.529
1.00
33.04


ATOM
574
O
ASN
140
40.438
66.632
57.838
1.00
32.86


ATOM
575
N
THR
141
42.082
67.094
56.376
1.00
31.07


ATOM
576
CA
THR
141
41.599
66.135
55.386
1.00
30.83


ATOM
577
CB
THR
141
42.347
66.287
54.038
1.00
31.28


ATOM
578
OG1
THR
141
43.753
66.108
54.238
1.00
31.57


ATOM
579
CG2
THR
141
42.089
67.668
53.438
1.00
31.26


ATOM
580
C
THR
141
41.681
64.674
55.835
1.00
30.16


ATOM
581
O
THR
141
40.809
63.875
55.504
1.00
30.19


ATOM
582
N
THR
142
42.722
64.323
56.582
1.00
29.65


ATOM
583
CA
THR
142
42.866
62.951
57.061
1.00
28.87


ATOM
584
CB
THR
142
44.242
62.733
57.722
1.00
30.00


ATOM
585
OG1
THR
142
45.266
62.851
56.726
1.00
31.45


ATOM
586
CG2
THR
142
44.324
61.354
58.366
1.00
29.44


ATOM
587
C
THR
142
41.760
62.627
58.064
1.00
27.94


ATOM
588
O
THR
142
41.151
61.558
58.005
1.00
27.97


ATOM
589
N
ILE
143
41.499
63.555
58.979
1.00
25.97


ATOM
590
CA
ILE
143
40.451
63.367
59.979
1.00
25.63


ATOM
591
CB
ILE
143
40.415
64.552
60.975
1.00
26.33


ATOM
592
CG2
ILE
143
39.202
64.438
61.888
1.00
24.81


ATOM
593
CG1
ILE
143
41.709
64.584
61.792
1.00
27.36


ATOM
594
CD1
ILE
143
41.941
63.340
62.619
1.00
29.54


ATOM
595
C
ILE
143
39.101
63.283
59.273
1.00
25.21


ATOM
596
O
ILE
143
38.248
62.463
59.612
1.00
24.06


ATOM
597
N
LYS
144
38.930
64.153
58.285
1.00
24.13


ATOM
598
CA
LYS
144
37.716
64.237
57.489
1.00
23.56


ATOM
599
CB
LYS
144
37.868
65.405
56.502
1.00
25.02


ATOM
600
CG
LYS
144
36.692
65.695
55.598
1.00
27.86


ATOM
601
CD
LYS
144
36.894
67.050
54.915
1.00
31.18


ATOM
602
CE
LYS
144
35.905
67.295
53.782
1.00
32.81


ATOM
603
NZ
LYS
144
34.486
67.288
54.224
1.00
35.78


ATOM
604
C
LYS
144
37.468
62.918
56.752
1.00
22.05


ATOM
605
O
LYS
144
36.349
62.402
56.734
1.00
22.03


ATOM
606
N
ARG
145
38.524
62.371
56.164
1.00
21.34


ATOM
607
CA
ARG
145
38.435
61.118
55.421
1.00
20.58


ATOM
608
CB
ARG
145
39.750
60.871
54.676
1.00
20.47


ATOM
609
CG
ARG
145
39.747
59.672
53.734
1.00
19.28


ATOM
610
CD
ARG
145
41.005
59.671
52.875
1.00
17.58


ATOM
611
NE
ARG
145
41.122
58.488
52.023
1.00
16.82


ATOM
612
CZ
ARG
145
40.350
58.238
50.969
1.00
18.88


ATOM
613
NH1
ARG
145
39.391
59.092
50.627
1.00
18.08


ATOM
614
NH2
ARG
145
40.541
57.133
50.252
1.00
15.35


ATOM
615
C
ARG
145
38.119
59.933
56.337
1.00
21.54


ATOM
616
O
ARG
145
37.294
59.081
56.002
1.00
19.52


ATOM
617
N
ILE
146
38.775
59.880
57.493
1.00
20.89


ATOM
618
CA
ILE
146
38.543
58.793
58.436
1.00
20.61


ATOM
619
CB
ILE
146
39.550
58.843
59.611
1.00
20.86


ATOM
620
CG2
ILE
146
39.105
57.904
60.729
1.00
18.26


ATOM
621
CG1
ILE
146
40.942
58.445
59.109
1.00
21.92


ATOM
622
CD1
ILE
146
42.034
58.531
60.163
1.00
23.09


ATOM
623
C
ILE
146
37.124
58.833
58.991
1.00
20.19


ATOM
624
O
ILE
146
36.433
57.814
59.024
1.00
20.23


ATOM
625
N
ILE
147
36.687
60.013
59.416
1.00
19.22


ATOM
626
CA
ILE
147
35.352
60.161
59.973
1.00
19.37


ATOM
627
CB
ILE
147
35.132
61.590
60.536
1.00
19.10


ATOM
628
CG2
ILE
147
33.657
61.806
60.859
1.00
19.65


ATOM
629
CG1
ILE
147
35.991
61.780
61.794
1.00
18.67


ATOM
630
CD1
ILE
147
35.771
63.090
62.519
1.00
20.74


ATOM
631
C
ILE
147
34.259
59.820
58.960
1.00
18.50


ATOM
632
O
ILE
147
33.278
59.166
59.305
1.00
16.03


ATOM
633
N
ALA
148
34.426
60.259
57.716
1.00
19.76


ATOM
634
CA
ALA
148
33.432
59.961
56.685
1.00
20.41


ATOM
635
CB
ALA
148
33.838
60.592
55.348
1.00
19.63


ATOM
636
C
ALA
148
33.305
58.447
56.535
1.00
19.95


ATOM
637
O
ALA
148
32.203
57.917
56.406
1.00
21.03


ATOM
638
N
LYS
149
34.438
57.752
56.566
1.00
19.67


ATOM
639
CA
LYS
149
34.446
56.300
56.435
1.00
19.12


ATOM
640
CB
LYS
149
35.886
55.802
56.246
1.00
21.29


ATOM
641
CG
LYS
149
36.016
54.302
55.997
1.00
25.45


ATOM
642
CD
LYS
149
37.389
53.971
55.418
1.00
29.29


ATOM
643
CE
LYS
149
37.511
52.506
55.013
1.00
29.09


ATOM
644
NZ
LYS
149
37.592
51.592
56.184
1.00
31.55


ATOM
645
C
LYS
149
33.802
55.601
57.633
1.00
18.43


ATOM
646
O
LYS
149
33.088
54.606
57.469
1.00
18.62


ATOM
647
N
VAL
150
34.042
56.122
58.835
1.00
17.00


ATOM
648
CA
VAL
150
33.475
55.528
60.041
1.00
16.77


ATOM
649
CB
VAL
150
34.145
56.106
61.316
1.00
18.58


ATOM
650
CG1
VAL
150
33.532
55.480
62.573
1.00
17.11


ATOM
651
CG2
VAL
150
35.641
55.825
61.276
1.00
17.68


ATOM
652
C
VAL
150
31.956
55.701
60.127
1.00
15.66


ATOM
653
O
VAL
150
31.291
54.974
60.861
1.00
14.92


ATOM
654
N
GLN
151
31.407
56.656
59.379
1.00
15.58


ATOM
655
CA
GLN
151
29.958
56.875
59.371
1.00
16.33


ATOM
656
CB
GLN
151
29.608
58.196
58.674
1.00
17.28


ATOM
657
CG
GLN
151
30.272
59.437
59.263
1.00
19.28


ATOM
658
CD
GLN
151
29.802
60.723
58.597
1.00
22.98


ATOM
659
OE1
GLN
151
29.570
60.758
57.388
1.00
24.55


ATOM
660
NE2
GLN
151
29.677
61.790
59.381
1.00
23.47


ATOM
661
C
GLN
151
29.237
55.719
58.656
1.00
16.52


ATOM
662
O
GLN
151
28.014
55.595
58.732
1.00
16.41


ATOM
663
N
ASP
152
29.997
54.887
57.950
1.00
14.56


ATOM
664
CA
ASP
152
29.436
53.732
57.242
1.00
16.29


ATOM
665
CB
ASP
152
30.237
53.457
55.965
1.00
15.31


ATOM
666
CG
ASP
152
29.661
52.317
55.131
1.00
17.15


ATOM
667
OD1
ASP
152
28.797
51.560
55.623
1.00
16.35


ATOM
668
OD2
ASP
152
30.095
52.172
53.970
1.00
18.62


ATOM
669
C
ASP
152
29.552
52.545
58.198
1.00
16.49


ATOM
670
O
ASP
152
30.641
52.022
58.408
1.00
16.64


ATOM
671
N
LEU
153
28.429
52.126
58.772
1.00
17.15


ATOM
672
CA
LEU
153
28.423
51.023
59.731
1.00
18.78


ATOM
673
CB
LEU
153
27.197
51.122
60.640
1.00
19.19


ATOM
674
CG
LEU
153
26.729
52.501
61.112
1.00
22.36


ATOM
675
CD1
LEU
153
25.611
52.330
62.137
1.00
22.96


ATOM
676
CD2
LEU
153
27.881
53.260
61.715
1.00
20.38


ATOM
677
C
LEU
153
28.417
49.650
59.080
1.00
18.93


ATOM
678
O
LEU
153
28.600
48.635
59.756
1.00
18.52


ATOM
679
N
GLU
154
28.207
49.617
57.769
1.00
19.03


ATOM
680
CA
GLU
154
28.133
48.360
57.049
1.00
19.00


ATOM
681
CB
GLU
154
29.505
47.674
57.033
1.00
23.48


ATOM
682
CG
GLU
154
30.375
48.165
55.867
1.00
32.92


ATOM
683
CD
GLU
154
31.838
47.766
55.981
1.00
38.33


ATOM
684
OE1
GLU
154
32.122
46.597
56.317
1.00
44.51


ATOM
685
OE2
GLU
154
32.709
48.622
55.720
1.00
42.26


ATOM
686
C
GLU
154
27.046
47.508
57.704
1.00
16.46


ATOM
687
O
GLU
154
25.984
48.038
58.020
1.00
16.75


ATOM
688
N
ARG
155
27.285
46.220
57.939
1.00
14.21


ATOM
689
CA
ARG
155
26.238
45.381
58.525
1.00
15.38


ATOM
690
CB
ARG
155
26.698
43.921
58.607
1.00
16.09


ATOM
691
CG
ARG
155
27.670
43.615
59.735
1.00
14.62


ATOM
692
CD
ARG
155
28.101
42.156
59.685
1.00
16.01


ATOM
693
NE
ARG
155
28.976
41.887
58.550
1.00
18.81


ATOM
694
CZ
ARG
155
29.461
40.686
58.244
1.00
21.66


ATOM
695
NH1
ARG
155
29.150
39.629
58.989
1.00
20.13


ATOM
696
NH2
ARG
155
30.274
40.547
57.204
1.00
22.28


ATOM
697
C
ARG
155
25.728
45.838
59.896
1.00
16.17


ATOM
698
O
ARG
155
24.567
45.602
60.246
1.00
15.50


ATOM
699
N
ALA
156
26.586
46.496
60.668
1.00
17.02


ATOM
700
CA
ALA
156
26.185
46.963
61.994
1.00
18.35


ATOM
701
CB
ALA
156
27.380
47.563
62.722
1.00
17.23


ATOM
702
C
ALA
156
25.031
47.969
61.954
1.00
19.07


ATOM
703
O
ALA
156
24.495
48.341
62.997
1.00
19.97


ATOM
704
N
ALA
157
24.645
48.409
60.759
1.00
17.62


ATOM
705
CA
ALA
157
23.534
49.354
60.635
1.00
17.85


ATOM
706
CB
ALA
157
23.620
50.104
59.311
1.00
15.36


ATOM
707
C
ALA
157
22.186
48.647
60.739
1.00
17.21


ATOM
708
O
ALA
157
21.155
49.286
60.946
1.00
18.26


ATOM
709
N
LEU
158
22.197
47.327
60.591
1.00
17.55


ATOM
710
CA
LEU
158
20.970
46.536
60.656
1.00
17.62


ATOM
711
CB
LEU
158
21.209
45.132
60.090
1.00
16.43


ATOM
712
CG
LEU
158
21.510
44.911
58.609
1.00
15.07


ATOM
713
CD1
LEU
158
21.931
43.465
58.404
1.00
15.08


ATOM
714
CD2
LEU
158
20.282
45.243
57.777
1.00
13.17


ATOM
715
C
LEU
158
20.430
46.377
62.073
1.00
17.49


ATOM
716
O
LEU
158
21.196
46.258
63.020
1.00
18.06


ATOM
717
N
PRO
159
19.096
46.374
62.229
1.00
18.66


ATOM
718
CD
PRO
159
18.053
46.623
61.215
1.00
18.39


ATOM
719
CA
PRO
159
18.508
46.207
63.561
1.00
18.87


ATOM
720
CB
PRO
159
17.014
46.153
63.273
1.00
19.07


ATOM
721
CG
PRO
159
16.873
47.046
62.062
1.00
20.37


ATOM
722
C
PRO
159
19.038
44.877
64.098
1.00
20.43


ATOM
723
O
PRO
159
19.318
43.966
63.317
1.00
20.96


ATOM
724
N
ALA
160
19.183
44.770
65.415
1.00
20.67


ATOM
725
CA
ALA
160
19.698
43.560
66.052
1.00
21.14


ATOM
726
CB
ALA
160
19.397
43.600
67.554
1.00
20.94


ATOM
727
C
ALA
160
19.183
42.246
65.459
1.00
21.41


ATOM
728
O
ALA
160
19.958
41.329
65.193
1.00
20.22


ATOM
729
N
GLN
161
17.873
42.154
65.261
1.00
22.76


ATOM
730
CA
GLN
161
17.268
40.941
64.724
1.00
24.75


ATOM
731
CB
GLN
161
15.749
41.106
64.668
1.00
27.09


ATOM
732
CG
GLN
161
14.993
39.854
64.268
1.00
34.37


ATOM
733
CD
GLN
161
13.498
39.986
64.496
1.00
38.16


ATOM
734
OE1
GLN
161
13.044
40.152
65.631
1.00
40.84


ATOM
735
NE2
GLN
161
12.724
39.914
63.417
1.00
39.81


ATOM
736
C
GLN
161
17.813
40.579
63.340
1.00
24.20


ATOM
737
O
GLN
161
18.220
39.437
63.105
1.00
22.98


ATOM
738
N
GLU
162
17.822
41.550
62.432
1.00
22.26


ATOM
739
CA
GLU
162
18.323
41.330
61.079
1.00
23.01


ATOM
740
CB
GLU
162
18.034
42.545
60.187
1.00
25.38


ATOM
741
CG
GLU
162
16.629
42.608
59.583
1.00
30.24


ATOM
742
CD
GLU
162
15.545
42.908
60.604
1.00
33.50


ATOM
743
OE1
GLU
162
15.246
42.031
61.441
1.00
37.24


ATOM
744
OE2
GLU
162
14.989
44.025
60.564
1.00
35.02


ATOM
745
C
GLU
162
19.827
41.053
61.066
1.00
20.41


ATOM
746
O
GLU
162
20.311
40.262
60.262
1.00
19.24


ATOM
747
N
LEU
163
20.567
41.705
61.956
1.00
20.49


ATOM
748
CA
LEU
163
22.008
41.504
62.001
1.00
19.77


ATOM
749
CB
LEU
163
22.655
42.455
63.013
1.00
19.73


ATOM
750
CG
LEU
163
24.177
42.335
63.191
1.00
20.15


ATOM
751
CD1
LEU
163
24.890
42.506
61.856
1.00
20.35


ATOM
752
CD2
LEU
163
24.651
43.385
64.183
1.00
20.52


ATOM
753
C
LEU
163
22.373
40.062
62.336
1.00
20.22


ATOM
754
O
LEU
163
23.242
39.469
61.690
1.00
18.49


ATOM
755
N
GLU
164
21.715
39.487
63.338
1.00
21.24


ATOM
756
CA
GLU
164
22.033
38.114
63.702
1.00
22.56


ATOM
757
CB
GLU
164
21.368
37.715
65.031
1.00
25.63


ATOM
758
CG
GLU
164
19.931
37.253
64.946
1.00
32.73


ATOM
759
CD
GLU
164
19.410
36.719
66.280
1.00
36.98


ATOM
760
OE1
GLU
164
18.266
36.215
66.315
1.00
39.72


ATOM
761
OE2
GLU
164
20.141
36.805
67.292
1.00
37.47


ATOM
762
C
GLU
164
21.629
37.159
62.583
1.00
19.87


ATOM
763
O
GLU
164
22.330
36.191
62.309
1.00
19.06


ATOM
764
N
GLU
165
20.511
37.436
61.923
1.00
18.96


ATOM
765
CA
GLU
165
20.076
36.575
60.829
1.00
19.42


ATOM
766
CB
GLU
165
18.677
36.962
60.354
1.00
19.49


ATOM
767
CG
GLU
165
18.230
36.176
59.138
1.00
22.13


ATOM
768
CD
GLU
165
16.817
36.502
58.721
1.00
23.77


ATOM
769
OE1
GLU
165
16.368
37.642
58.976
1.00
25.48


ATOM
770
OE2
GLU
165
16.163
35.622
58.122
1.00
23.74


ATOM
771
C
GLU
165
21.069
36.659
59.664
1.00
19.62


ATOM
772
O
GLU
165
21.405
35.645
59.050
1.00
19.06


ATOM
773
N
TYR
166
21.536
37.869
59.372
1.00
18.74


ATOM
774
CA
TYR
166
22.499
38.083
58.298
1.00
19.37


ATOM
775
CB
TYR
166
22.767
39.579
58.117
1.00
18.92


ATOM
776
CG
TYR
166
23.762
39.899
57.021
1.00
18.54


ATOM
777
CD1
TYR
166
23.522
39.516
55.699
1.00
17.98


ATOM
778
CE1
TYR
166
24.431
39.816
54.685
1.00
18.12


ATOM
779
CD2
TYR
166
24.938
40.591
57.302
1.00
19.19


ATOM
780
CE2
TYR
166
25.853
40.898
56.296
1.00
19.67


ATOM
781
CZ
TYR
166
25.593
40.508
54.992
1.00
19.53


ATOM
782
OH
TYR
166
26.492
40.814
53.997
1.00
20.23


ATOM
783
C
TYR
166
23.815
37.365
58.603
1.00
19.45


ATOM
784
O
TYR
166
24.375
36.681
57.742
1.00
17.70


ATOM
785
N
ASN
167
24.313
37.524
59.827
1.00
19.79


ATOM
786
CA
ASN
167
25.563
36.874
60.197
1.00
19.29


ATOM
787
CB
ASN
167
25.980
37.248
61.623
1.00
20.64


ATOM
788
CG
ASN
167
26.480
38.678
61.729
1.00
21.06


ATOM
789
OD1
ASN
167
27.214
39.156
60.864
1.00
22.90


ATOM
790
ND2
ASN
167
26.096
39.361
62.798
1.00
20.86


ATOM
791
C
ASN
167
25.448
35.364
60.077
1.00
19.16


ATOM
792
O
ASN
167
26.378
34.706
59.619
1.00
19.57


ATOM
793
N
LYS
168
24.308
34.813
60.483
1.00
19.46


ATOM
794
CA
LYS
168
24.116
33.370
60.403
1.00
20.23


ATOM
795
CB
LYS
168
22.864
32.929
61.172
1.00
20.58


ATOM
796
CG
LYS
168
22.625
31.428
61.056
1.00
24.70


ATOM
797
CD
LYS
168
21.400
30.961
61.813
1.00
28.42


ATOM
798
CE
LYS
168
21.048
29.527
61.414
1.00
30.39


ATOM
799
NZ
LYS
168
22.235
28.626
61.471
1.00
30.19


ATOM
800
C
LYS
168
24.006
32.930
58.950
1.00
18.98


ATOM
801
O
LYS
168
24.485
31.859
58.580
1.00
17.60


ATOM
802
N
ILE
169
23.363
33.760
58.135
1.00
18.74


ATOM
803
CA
ILE
169
23.213
33.473
56.715
1.00
19.75


ATOM
804
CB
ILE
169
22.464
34.615
55.987
1.00
20.57


ATOM
805
CG2
ILE
169
22.651
34.489
54.480
1.00
22.22


ATOM
806
CG1
ILE
169
20.975
34.585
56.341
1.00
23.21


ATOM
807
CD1
ILE
169
20.236
33.385
55.798
1.00
23.57


ATOM
808
C
ILE
169
24.603
33.331
56.096
1.00
17.44


ATOM
809
O
ILE
169
24.903
32.337
55.443
1.00
17.43


ATOM
810
N
LEU
170
25.445
34.338
56.305
1.00
16.93


ATOM
811
CA
LEU
170
26.802
34.321
55.771
1.00
17.48


ATOM
812
CB
LEU
170
27.555
35.582
56.195
1.00
16.14


ATOM
813
CG
LEU
170
27.069
36.914
55.617
1.00
16.26


ATOM
814
CD1
LEU
170
27.899
38.051
56.203
1.00
15.60


ATOM
815
CD2
LEU
170
27.182
36.895
54.098
1.00
15.95


ATOM
816
C
LEU
170
27.561
33.091
56.257
1.00
19.23


ATOM
817
O
LEU
170
28.222
32.398
55.479
1.00
18.65


ATOM
818
N
LEU
171
27.464
32.827
57.553
1.00
19.55


ATOM
819
CA
LEU
171
28.135
31.687
58.150
1.00
20.58


ATOM
820
CB
LEU
171
27.824
31.621
59.647
1.00
23.73


ATOM
821
CG
LEU
171
28.435
30.447
60.413
1.00
27.50


ATOM
822
CD1
LEU
171
29.939
30.625
60.513
1.00
27.87


ATOM
823
CD2
LEU
171
27.812
30.371
61.801
1.00
30.52


ATOM
824
C
LEU
171
27.698
30.386
57.481
1.00
20.07


ATOM
825
O
LEU
171
28.537
29.561
57.109
1.00
20.05


ATOM
826
N
ASP
172
26.389
30.206
57.328
1.00
17.76


ATOM
827
CA
ASP
172
25.864
28.988
56.723
1.00
18.58


ATOM
828
CB
ASP
172
24.336
28.926
56.843
1.00
19.17


ATOM
829
CG
ASP
172
23.859
28.732
58.280
1.00
20.25


ATOM
830
OD1
ASP
172
24.644
28.263
59.129
1.00
20.96


ATOM
831
OD2
ASP
172
22.680
29.035
58.554
1.00
22.31


ATOM
832
C
ASP
172
26.267
28.823
55.260
1.00
18.13


ATOM
833
O
ASP
172
26.537
27.709
54.819
1.00
18.79


ATOM
834
N
MET
173
26.301
29.915
54.501
1.00
17.04


ATOM
835
CA
MET
173
26.695
29.810
53.098
1.00
16.32


ATOM
836
CB
MET
173
26.486
31.141
52.354
1.00
13.73


ATOM
837
CG
MET
173
25.021
31.532
52.178
1.00
13.28


ATOM
838
SD
MET
173
24.730
32.777
50.896
1.00
14.85


ATOM
839
CE
MET
173
25.634
34.204
51.591
1.00
10.81


ATOM
840
C
MET
173
28.159
29.388
52.998
1.00
16.03


ATOM
841
O
MET
173
28.510
28.516
52.205
1.00
15.12


ATOM
842
N
GLU
174
29.008
30.003
53.812
1.00
16.72


ATOM
843
CA
GLU
174
30.430
29.686
53.796
1.00
20.27


ATOM
844
CB
GLU
174
31.197
30.594
54.757
1.00
22.24


ATOM
845
CG
GLU
174
32.675
30.254
54.819
1.00
28.10


ATOM
846
CD
GLU
174
33.359
30.397
53.470
1.00
31.42


ATOM
847
OE1
GLU
174
33.614
31.552
53.059
1.00
33.86


ATOM
848
OE2
GLU
174
33.631
29.361
52.817
1.00
30.70


ATOM
849
C
GLU
174
30.692
28.233
54.171
1.00
19.72


ATOM
850
O
GLU
174
31.497
27.551
53.533
1.00
19.19


ATOM
851
N
THR
175
30.016
27.770
55.216
1.00
19.54


ATOM
852
CA
THR
175
30.176
26.401
55.686
1.00
19.81


ATOM
853
CB
THR
175
29.389
26.174
56.991
1.00
20.87


ATOM
854
OG1
THR
175
29.833
27.111
57.978
1.00
22.15


ATOM
855
CG2
THR
175
29.613
24.761
57.513
1.00
23.20


ATOM
856
C
THR
175
29.694
25.414
54.635
1.00
19.62


ATOM
857
O
THR
175
30.392
24.447
54.315
1.00
21.27


ATOM
858
N
THR
176
28.501
25.660
54.101
1.00
16.70


ATOM
859
CA
THR
176
27.923
24.794
53.076
1.00
16.77


ATOM
860
CB
THR
176
26.594
25.375
52.546
1.00
17.25


ATOM
861
OG1
THR
176
25.646
25.467
53.620
1.00
16.27


ATOM
862
CG2
THR
176
26.028
24.488
51.428
1.00
13.62


ATOM
863
C
THR
176
28.882
24.620
51.895
1.00
16.32


ATOM
864
O
THR
176
29.088
23.512
51.408
1.00
17.12


ATOM
865
N
TYR
177
29.467
25.720
51.439
1.00
16.42


ATOM
866
CA
TYR
177
30.396
25.675
50.316
1.00
17.56


ATOM
867
CB
TYR
177
30.773
27.103
49.885
1.00
15.76


ATOM
868
CG
TYR
177
31.734
27.166
48.708
1.00
15.72


ATOM
869
CD1
TYR
177
31.265
27.155
47.392
1.00
14.57


ATOM
870
CE1
TYR
177
32.152
27.198
46.301
1.00
14.15


ATOM
871
CD2
TYR
177
33.114
27.220
48.912
1.00
15.54


ATOM
872
CE2
TYR
177
34.009
27.259
47.834
1.00
12.96


ATOM
873
CZ
TYR
177
33.521
27.248
46.534
1.00
15.16


ATOM
874
OH
TYR
177
34.402
27.283
45.477
1.00
14.20


ATOM
875
C
TYR
177
31.673
24.897
50.651
1.00
18.31


ATOM
876
O
TYR
177
32.072
23.998
49.913
1.00
18.88


ATOM
877
N
SER
178
32.304
25.251
51.768
1.00
18.65


ATOM
878
CA
SER
178
33.555
24.628
52.188
1.00
20.78


ATOM
879
CB
SER
178
34.201
25.451
53.306
1.00
21.43


ATOM
880
OG
SER
178
34.760
26.650
52.796
1.00
24.23


ATOM
881
C
SER
178
33.522
23.163
52.613
1.00
21.32


ATOM
882
O
SER
178
34.577
22.541
52.739
1.00
21.59


ATOM
883
N
VAL
179
32.338
22.604
52.835
1.00
20.55


ATOM
884
CA
VAL
179
32.253
21.206
53.242
1.00
21.42


ATOM
885
CB
VAL
179
31.541
21.049
54.616
1.00
23.05


ATOM
886
CG1
VAL
179
32.268
21.866
55.672
1.00
21.20


ATOM
887
CG2
VAL
179
30.085
21.474
54.509
1.00
22.91


ATOM
888
C
VAL
179
31.527
20.337
52.218
1.00
21.32


ATOM
889
O
VAL
179
31.367
19.135
52.421
1.00
21.62


ATOM
890
N
ALA
180
31.106
20.941
51.113
1.00
20.29


ATOM
891
CA
ALA
180
30.393
20.203
50.081
1.00
19.37


ATOM
892
CB
ALA
180
29.855
21.169
49.026
1.00
18.54


ATOM
893
C
ALA
180
31.285
19.157
49.424
1.00
18.64


ATOM
894
O
ALA
180
32.479
19.384
49.224
1.00
19.38


ATOM
895
N
THR
181
30.692
18.013
49.095
1.00
19.37


ATOM
896
CA
THR
181
31.413
16.925
48.442
1.00
20.39


ATOM
897
CB
THR
181
31.749
15.781
49.434
1.00
21.11


ATOM
898
OG1
THR
181
30.534
15.211
49.931
1.00
24.35


ATOM
899
CG2
THR
181
32.576
16.301
50.603
1.00
21.45


ATOM
900
C
THR
181
30.579
16.334
47.309
1.00
19.99


ATOM
901
O
THR
181
29.353
16.463
47.288
1.00
18.79


ATOM
902
N
VAL
182
31.257
15.694
46.362
1.00
20.53


ATOM
903
CA
VAL
182
30.601
15.053
45.227
1.00
20.87


ATOM
904
CB
VAL
182
31.084
15.655
43.890
1.00
18.48


ATOM
905
CG1
VAL
182
30.321
15.021
42.724
1.00
18.85


ATOM
906
CG2
VAL
182
30.882
17.166
43.897
1.00
16.20


ATOM
907
C
VAL
182
30.987
13.584
45.307
1.00
22.10


ATOM
908
O
VAL
182
32.167
13.249
45.261
1.00
21.07


ATOM
909
N
CYS
183
29.989
12.714
45.435
1.00
26.01


ATOM
910
CA
CYS
183
30.247
11.285
45.580
1.00
29.42


ATOM
911
C
CYS
183
29.855
10.406
44.398
1.00
31.72


ATOM
912
O
CYS
183
28.976
10.755
43.607
1.00
31.89


ATOM
913
CB
CYS
183
29.514
10.743
46.811
1.00
28.21


ATOM
914
SG
CYS
183
29.634
11.717
48.345
1.00
30.87


ATOM
915
N
HIS
184
30.518
9.252
44.310
1.00
35.55


ATOM
916
CA
HIS
184
30.247
8.250
43.284
1.00
37.73


ATOM
917
CB
HIS
184
31.542
7.526
42.894
1.00
38.32


ATOM
918
CG
HIS
184
32.423
8.311
41.970
1.00
39.50


ATOM
919
CD2
HIS
184
33.641
8.871
42.163
1.00
40.09


ATOM
920
ND1
HIS
184
32.082
8.580
40.661
1.00
39.50


ATOM
921
CE1
HIS
184
33.053
9.267
40.087
1.00
40.74


ATOM
922
NE2
HIS
184
34.012
9.456
40.977
1.00
41.17


ATOM
923
C
HIS
184
29.267
7.251
43.896
1.00
39.60


ATOM
924
O
HIS
184
29.012
7.282
45.095
1.00
38.09


ATOM
925
N
PRO
185
28.712
6.348
43.082
1.00
42.45


ATOM
926
CD
PRO
185
28.759
6.347
41.608
1.00
43.76


ATOM
927
CA
PRO
185
27.762
5.347
43.588
1.00
43.42


ATOM
928
CB
PRO
185
27.433
4.539
42.341
1.00
44.10


ATOM
929
CG
PRO
185
27.503
5.614
41.253
1.00
44.49


ATOM
930
C
PRO
185
28.305
4.467
44.722
1.00
44.53


ATOM
931
O
PRO
185
27.545
3.951
45.540
1.00
44.42


ATOM
932
N
ASN
186
29.617
4.276
44.744
1.00
46.05


ATOM
933
CA
ASN
186
30.217
3.474
45.795
1.00
47.57


ATOM
934
CB
ASN
186
31.688
3.146
45.466
1.00
48.59


ATOM
935
CG
ASN
186
32.413
4.289
44.776
1.00
49.30


ATOM
936
OD1
ASN
186
32.309
5.433
45.193
1.00
50.36


ATOM
937
ND2
ASN
186
33.142
3.979
43.698
1.00
49.33


ATOM
938
C
ASN
186
30.140
4.201
47.144
1.00
47.63


ATOM
939
O
ASN
186
29.211
4.005
47.946
1.00
49.72


ATOM
940
N
GLY
187
31.125
5.059
47.377
1.00
46.81


ATOM
941
CA
GLY
187
31.186
5.818
48.609
1.00
43.76


ATOM
942
C
GLY
187
32.326
6.797
48.480
1.00
41.12


ATOM
943
O
GLY
187
32.640
7.519
49.421
1.00
42.63


ATOM
944
N
SER
188
32.951
6.800
47.306
1.00
38.37


ATOM
945
CA
SER
188
34.065
7.691
47.030
1.00
36.56


ATOM
946
CB
SER
188
34.804
7.249
45.768
1.00
37.67


ATOM
947
OG
SER
188
35.648
6.153
46.049
1.00
42.41


ATOM
948
C
SER
188
33.530
9.100
46.839
1.00
33.64


ATOM
949
O
SER
188
32.904
9.408
45.824
1.00
31.94


ATOM
950
N
CYS
189
33.757
9.946
47.835
1.00
31.40


ATOM
951
CA
CYS
189
33.320
11.329
47.768
1.00
29.46


ATOM
952
C
CYS
189
34.555
12.190
47.586
1.00
27.90


ATOM
953
O
CYS
189
35.591
11.948
48.202
1.00
28.50


ATOM
954
CB
CYS
189
32.598
11.731
49.051
1.00
29.56


ATOM
955
SG
CYS
189
31.084
10.792
49.428
1.00
31.98


ATOM
956
N
LEU
190
34.445
13.191
46.726
1.00
24.76


ATOM
957
CA
LEU
190
35.563
14.079
46.472
1.00
22.68


ATOM
958
CB
LEU
190
35.873
14.143
44.970
1.00
22.93


ATOM
959
CG
LEU
190
36.414
12.907
44.247
1.00
22.92


ATOM
960
CD1
LEU
190
35.367
11.804
44.233
1.00
23.79


ATOM
961
CD2
LEU
190
36.794
13.293
42.820
1.00
23.49


ATOM
962
C
LEU
190
35.263
15.481
46.971
1.00
21.66


ATOM
963
O
LEU
190
34.128
15.954
46.880
1.00
18.61


ATOM
964
N
GLN
191
36.285
16.133
47.508
1.00
20.57


ATOM
965
CA
GLN
191
36.157
17.502
47.976
1.00
21.68


ATOM
966
CB
GLN
191
37.052
17.737
49.193
1.00
22.65


ATOM
967
CG
GLN
191
36.635
16.951
50.422
1.00
27.39


ATOM
968
CD
GLN
191
37.541
17.213
51.609
1.00
28.93


ATOM
969
OE1
GLN
191
38.750
16.992
51.543
1.00
31.20


ATOM
970
NE2
GLN
191
36.958
17.685
52.703
1.00
31.79


ATOM
971
C
GLN
191
36.629
18.361
46.804
1.00
20.53


ATOM
972
O
GLN
191
37.304
17.857
45.902
1.00
17.89


ATOM
973
N
LEU
192
36.279
19.646
46.814
1.00
18.80


ATOM
974
CA
LEU
192
36.683
20.538
45.736
1.00
17.83


ATOM
975
CB
LEU
192
36.197
21.964
46.004
1.00
17.41


ATOM
976
CG
LEU
192
36.569
22.988
44.926
1.00
15.82


ATOM
977
CD1
LEU
192
35.877
22.630
43.615
1.00
18.76


ATOM
978
CD2
LEU
192
36.164
24.377
45.378
1.00
17.28


ATOM
979
C
LEU
192
38.199
20.540
45.568
1.00
19.20


ATOM
980
O
LEU
192
38.713
20.284
44.483
1.00
19.52


ATOM
981
N
GLU
193
38.914
20.837
46.644
1.00
20.67


ATOM
982
CA
GLU
193
40.366
20.860
46.590
1.00
24.08


ATOM
983
CB
GLU
193
40.894
22.208
47.099
1.00
25.06


ATOM
984
CG
GLU
193
40.261
23.400
46.387
1.00
30.04


ATOM
985
CD
GLU
193
41.009
24.704
46.605
1.00
32.48


ATOM
986
OE1
GLU
193
41.103
25.165
47.764
1.00
34.10


ATOM
987
OE2
GLU
193
41.504
25.270
45.606
1.00
34.77


ATOM
988
C
GLU
193
40.916
19.718
47.441
1.00
24.65


ATOM
989
O
GLU
193
40.514
19.542
48.590
1.00
24.48


ATOM
990
N
PRO
194
41.831
18.914
46.877
1.00
24.86


ATOM
991
CD
PRO
194
42.651
17.967
47.659
1.00
24.60


ATOM
992
CA
PRO
194
42.361
19.042
45.516
1.00
23.62


ATOM
993
CB
PRO
194
43.821
18.693
45.705
1.00
24.03


ATOM
994
CG
PRO
194
43.704
17.508
46.641
1.00
24.48


ATOM
995
C
PRO
194
41.694
18.072
44.539
1.00
22.86


ATOM
996
O
PRO
194
41.957
18.116
43.337
1.00
21.75


ATOM
997
N
ASP
195
40.840
17.201
45.067
1.00
21.42


ATOM
998
CA
ASP
195
40.176
16.177
44.267
1.00
22.19


ATOM
999
CB
ASP
195
39.183
15.395
45.130
1.00
21.92


ATOM
1000
CG
ASP
195
39.844
14.746
46.330
1.00
27.22


ATOM
1001
OD1
ASP
195
40.997
14.287
46.197
1.00
27.92


ATOM
1002
OD2
ASP
195
39.208
14.687
47.402
1.00
30.18


ATOM
1003
C
ASP
195
39.488
16.623
42.985
1.00
21.21


ATOM
1004
O
ASP
195
39.953
16.301
41.893
1.00
23.11


ATOM
1005
N
LEU
196
38.383
17.351
43.107
1.00
19.29


ATOM
1006
CA
LEU
196
37.662
17.793
41.921
1.00
18.52


ATOM
1007
CB
LEU
196
36.360
18.487
42.324
1.00
16.88


ATOM
1008
CG
LEU
196
35.342
17.535
42.964
1.00
19.05


ATOM
1009
CD1
LEU
196
34.224
18.325
43.620
1.00
19.51


ATOM
1010
CD2
LEU
196
34.793
16.583
41.901
1.00
19.00


ATOM
1011
C
LEU
196
38.519
18.708
41.061
1.00
17.36


ATOM
1012
O
LEU
196
38.435
18.675
39.837
1.00
16.52


ATOM
1013
N
THR
197
39.346
19.517
41.713
1.00
17.60


ATOM
1014
CA
THR
197
40.231
20.440
41.016
1.00
17.78


ATOM
1015
CB
THR
197
41.020
21.316
42.023
1.00
18.34


ATOM
1016
OG1
THR
197
40.137
22.295
42.592
1.00
22.95


ATOM
1017
CG2
THR
197
42.172
22.032
41.334
1.00
22.61


ATOM
1018
C
THR
197
41.205
19.679
40.120
1.00
18.14


ATOM
1019
O
THR
197
41.460
20.089
38.987
1.00
15.11


ATOM
1020
N
ASN
198
41.747
18.575
40.633
1.00
18.47


ATOM
1021
CA
ASN
198
42.679
17.760
39.860
1.00
19.73


ATOM
1022
CB
ASN
198
43.298
16.648
40.721
1.00
24.67


ATOM
1023
CG
ASN
198
44.208
17.185
41.815
1.00
30.01


ATOM
1024
OD1
ASN
198
44.853
18.223
41.655
1.00
32.67


ATOM
1025
ND2
ASN
198
44.282
16.460
42.930
1.00
33.72


ATOM
1026
C
ASN
198
41.968
17.128
38.669
1.00
16.49


ATOM
1027
O
ASN
198
42.514
17.091
37.569
1.00
17.40


ATOM
1028
N
VAL
199
40.754
16.626
38.889
1.00
15.82


ATOM
1029
CA
VAL
199
39.988
16.013
37.806
1.00
14.87


ATOM
1030
CB
VAL
199
38.605
15.504
38.290
1.00
15.42


ATOM
1031
CG1
VAL
199
37.766
15.069
37.091
1.00
15.86


ATOM
1032
CG2
VAL
199
38.776
14.317
39.255
1.00
14.36


ATOM
1033
C
VAL
199
39.771
17.013
36.666
1.00
14.32


ATOM
1034
O
VAL
199
39.965
16.688
35.491
1.00
11.80


ATOM
1035
N
MET
200
39.366
18.231
37.016
1.00
14.83


ATOM
1036
CA
MET
200
39.123
19.259
36.008
1.00
14.38


ATOM
1037
CB
MET
200
38.524
20.517
36.650
1.00
12.52


ATOM
1038
CG
MET
200
37.128
20.328
37.233
1.00
12.28


ATOM
1039
SD
MET
200
35.935
19.690
36.045
1.00
14.88


ATOM
1040
CE
MET
200
35.797
21.097
34.903
1.00
12.30


ATOM
1041
C
MET
200
40.405
19.632
35.274
1.00
13.50


ATOM
1042
O
MET
200
40.375
19.989
34.099
1.00
13.68


ATOM
1043
N
ALA
201
41.533
19.535
35.966
1.00
12.51


ATOM
1044
CA
ALA
201
42.814
19.891
35.372
1.00
14.22


ATOM
1045
CB
ALA
201
43.762
20.372
36.465
1.00
12.68


ATOM
1046
C
ALA
201
43.501
18.794
34.556
1.00
14.13


ATOM
1047
O
ALA
201
44.239
19.092
33.619
1.00
13.71


ATOM
1048
N
THR
202
43.246
17.534
34.889
1.00
13.05


ATOM
1049
CA
THR
202
43.932
16.442
34.211
1.00
14.28


ATOM
1050
CB
THR
202
44.677
15.579
35.243
1.00
13.91


ATOM
1051
OG1
THR
202
43.734
15.052
36.182
1.00
16.38


ATOM
1052
CG2
THR
202
45.702
16.412
35.995
1.00
14.07


ATOM
1053
C
THR
202
43.105
15.512
33.329
1.00
14.85


ATOM
1054
O
THR
202
43.631
14.920
32.382
1.00
13.44


ATOM
1055
N
SER
203
41.824
15.356
33.637
1.00
14.42


ATOM
1056
CA
SER
203
40.993
14.482
32.821
1.00
15.37


ATOM
1057
CB
SER
203
39.620
14.296
33.458
1.00
15.43


ATOM
1058
OG
SER
203
38.771
13.571
32.585
1.00
16.22


ATOM
1059
C
SER
203
40.817
15.043
31.410
1.00
17.26


ATOM
1060
O
SER
203
40.718
16.258
31.216
1.00
15.56


ATOM
1061
N
ARG
204
40.788
14.143
30.431
1.00
17.39


ATOM
1062
CA
ARG
204
40.598
14.503
29.030
1.00
19.50


ATOM
1063
CB
ARG
204
41.869
14.206
28.224
1.00
21.26


ATOM
1064
CG
ARG
204
42.743
15.424
27.899
1.00
24.82


ATOM
1065
CD
ARG
204
42.745
16.460
29.009
1.00
25.90


ATOM
1066
NE
ARG
204
43.950
17.284
29.001
1.00
25.48


ATOM
1067
CZ
ARG
204
44.225
18.207
29.921
1.00
26.92


ATOM
1068
NH1
ARG
204
45.345
18.908
29.852
1.00
26.07


ATOM
1069
NH2
ARG
204
43.372
18.437
30.908
1.00
28.93


ATOM
1070
C
ARG
204
39.425
13.679
28.497
1.00
19.23


ATOM
1071
O
ARG
204
39.299
13.448
27.292
1.00
18.09


ATOM
1072
N
LYS
205
38.575
13.231
29.416
1.00
19.44


ATOM
1073
CA
LYS
205
37.397
12.444
29.069
1.00
20.20


ATOM
1074
CB
LYS
205
37.340
11.175
29.922
1.00
20.93


ATOM
1075
CG
LYS
205
38.602
10.323
29.803
1.00
26.30


ATOM
1076
CD
LYS
205
38.426
8.924
30.380
1.00
29.11


ATOM
1077
CE
LYS
205
37.499
8.077
29.518
1.00
32.25


ATOM
1078
NZ
LYS
205
37.474
6.652
29.959
1.00
35.02


ATOM
1079
C
LYS
205
36.160
13.304
29.303
1.00
18.71


ATOM
1080
O
LYS
205
35.854
13.680
30.440
1.00
17.01


ATOM
1081
N
TYR
206
35.457
13.608
28.215
1.00
16.75


ATOM
1082
CA
TYR
206
34.263
14.453
28.241
1.00
16.98


ATOM
1083
CB
TYR
206
33.550
14.383
26.884
1.00
16.42


ATOM
1084
CG
TYR
206
32.574
15.513
26.617
1.00
16.97


ATOM
1085
CD1
TYR
206
32.941
16.599
25.821
1.00
15.01


ATOM
1086
CE1
TYR
206
32.044
17.621
25.539
1.00
16.36


ATOM
1087
CD2
TYR
206
31.275
15.485
27.135
1.00
15.21


ATOM
1088
CE2
TYR
206
30.370
16.509
26.862
1.00
15.72


ATOM
1089
CZ
TYR
206
30.761
17.573
26.061
1.00
17.54


ATOM
1090
OH
TYR
206
29.874
18.590
25.772
1.00
19.58


ATOM
1091
C
TYR
206
33.273
14.106
29.350
1.00
16.80


ATOM
1092
O
TYR
206
32.772
14.990
30.039
1.00
16.60


ATOM
1093
N
GLU
207
32.980
12.819
29.514
1.00
16.66


ATOM
1094
CA
GLU
207
32.029
12.387
30.533
1.00
15.78


ATOM
1095
CB
GLU
207
31.584
10.941
30.268
1.00
16.34


ATOM
1096
CG
GLU
207
30.808
10.730
28.962
1.00
17.93


ATOM
1097
CD
GLU
207
29.479
11.488
28.917
1.00
21.81


ATOM
1098
OE1
GLU
207
28.742
11.475
29.925
1.00
20.91


ATOM
1099
OE2
GLU
207
29.166
12.089
27.863
1.00
22.78


ATOM
1100
C
GLU
207
32.565
12.511
31.960
1.00
14.53


ATOM
1101
O
GLU
207
31.798
12.773
32.886
1.00
15.02


ATOM
1102
N
ASP
208
33.867
12.312
32.147
1.00
13.86


ATOM
1103
CA
ASP
208
34.445
12.422
33.489
1.00
14.82


ATOM
1104
CB
ASP
208
35.870
11.854
33.531
1.00
16.21


ATOM
1105
CG
ASP
208
35.912
10.338
33.365
1.00
20.87


ATOM
1106
OD1
ASP
208
34.883
9.674
33.606
1.00
23.51


ATOM
1107
OD2
ASP
208
36.984
9.805
33.011
1.00
22.35


ATOM
1108
C
ASP
208
34.460
13.890
33.920
1.00
13.51


ATOM
1109
O
ASP
208
34.160
14.216
35.068
1.00
10.65


ATOM
1110
N
LEU
209
34.808
14.771
32.988
1.00
12.89


ATOM
1111
CA
LEU
209
34.838
16.200
33.269
1.00
12.10


ATOM
1112
CB
LEU
209
35.407
16.951
32.063
1.00
11.37


ATOM
1113
CG
LEU
209
36.907
16.746
31.811
1.00
10.29


ATOM
1114
CD1
LEU
209
37.298
17.353
30.474
1.00
9.40


ATOM
1115
CD2
LEU
209
37.705
17.380
32.950
1.00
9.04


ATOM
1116
C
LEU
209
33.421
16.684
33.575
1.00
13.60


ATOM
1117
O
LEU
209
33.210
17.517
34.460
1.00
12.24


ATOM
1118
N
LEU
210
32.452
16.145
32.843
1.00
12.89


ATOM
1119
CA
LEU
210
31.058
16.516
33.033
1.00
13.89


ATOM
1120
CB
LEU
210
30.193
15.862
31.951
1.00
16.04


ATOM
1121
CG
LEU
210
28.700
16.200
31.985
1.00
17.33


ATOM
1122
CD1
LEU
210
28.515
17.711
31.938
1.00
18.83


ATOM
1123
CD2
LEU
210
28.003
15.543
30.803
1.00
18.20


ATOM
1124
C
LEU
210
30.561
16.100
34.415
1.00
14.94


ATOM
1125
O
LEU
210
29.848
16.849
35.089
1.00
13.44


ATOM
1126
N
TRP
211
30.938
14.895
34.829
1.00
14.27


ATOM
1127
CA
TRP
211
30.543
14.377
36.133
1.00
14.75


ATOM
1128
CB
TRP
211
31.191
13.003
36.380
1.00
17.05


ATOM
1129
CG
TRP
211
30.897
12.452
37.745
1.00
19.27


ATOM
1130
CD2
TRP
211
31.702
12.600
38.925
1.00
19.31


ATOM
1131
CE2
TRP
211
30.996
12.007
39.991
1.00
20.70


ATOM
1132
CE3
TRP
211
32.950
13.183
39.183
1.00
20.90


ATOM
1133
CD1
TRP
211
29.772
11.788
38.133
1.00
21.04


ATOM
1134
NE1
TRP
211
29.822
11.517
39.482
1.00
21.92


ATOM
1135
CZ2
TRP
211
31.496
11.977
41.301
1.00
23.12


ATOM
1136
CZ3
TRP
211
33.448
13.154
40.485
1.00
21.37


ATOM
1137
CH2
TRP
211
32.720
12.556
41.526
1.00
21.61


ATOM
1138
C
TRP
211
30.977
15.350
37.236
1.00
13.96


ATOM
1139
O
TRP
211
30.183
15.722
38.096
1.00
11.98


ATOM
1140
N
ALA
212
32.244
15.753
37.200
1.00
13.24


ATOM
1141
CA
ALA
212
32.790
16.673
38.195
1.00
13.44


ATOM
1142
CB
ALA
212
34.313
16.743
38.057
1.00
12.36


ATOM
1143
C
ALA
212
32.194
18.076
38.081
1.00
13.04


ATOM
1144
O
ALA
212
31.875
18.707
39.091
1.00
13.12


ATOM
1145
N
TRP
213
32.050
18.560
36.851
1.00
13.51


ATOM
1146
CA
TRP
213
31.503
19.896
36.601
1.00
13.80


ATOM
1147
CB
TRP
213
31.554
20.212
35.099
1.00
13.04


ATOM
1148
CG
TRP
213
31.128
21.614
34.756
1.00
12.05


ATOM
1149
CD2
TRP
213
29.800
22.062
34.454
1.00
12.15


ATOM
1150
CE2
TRP
213
29.870
23.458
34.233
1.00
13.44


ATOM
1151
CE3
TRP
213
28.556
21.421
34.352
1.00
12.18


ATOM
1152
CD1
TRP
213
31.925
22.723
34.704
1.00
14.22


ATOM
1153
NE1
TRP
213
31.177
23.834
34.390
1.00
12.82


ATOM
1154
CZ2
TRP
213
28.741
24.227
33.915
1.00
12.19


ATOM
1155
CZ3
TRP
213
27.434
22.184
34.035
1.00
12.97


ATOM
1156
CH2
TRP
213
27.536
23.574
33.821
1.00
12.27


ATOM
1157
C
TRP
213
30.058
20.014
37.094
1.00
13.65


ATOM
1158
O
TRP
213
29.711
20.944
37.824
1.00
12.41


ATOM
1159
N
GLU
214
29.223
19.065
36.678
1.00
14.41


ATOM
1160
CA
GLU
214
27.815
19.043
37.055
1.00
15.02


ATOM
1161
CB
GLU
214
27.067
18.017
36.200
1.00
16.55


ATOM
1162
CG
GLU
214
25.569
17.945
36.459
1.00
19.62


ATOM
1163
CD
GLU
214
24.851
19.220
36.077
1.00
21.05


ATOM
1164
OE1
GLU
214
25.063
19.698
34.944
1.00
24.80


ATOM
1165
OE2
GLU
214
24.068
19.743
36.901
1.00
24.78


ATOM
1166
C
GLU
214
27.636
18.704
38.533
1.00
15.51


ATOM
1167
O
GLU
214
26.829
19.320
39.232
1.00
14.95


ATOM
1168
N
GLY
215
28.398
17.722
39.002
1.00
15.44


ATOM
1169
CA
GLY
215
28.302
17.307
40.389
1.00
15.35


ATOM
1170
C
GLY
215
28.587
18.422
41.373
1.00
15.21


ATOM
1171
O
GLY
215
27.857
18.604
42.345
1.00
15.46


ATOM
1172
N
TRP
216
29.650
19.176
41.121
1.00
15.46


ATOM
1173
CA
TRP
216
30.009
20.267
42.011
1.00
14.95


ATOM
1174
CB
TRP
216
31.285
20.965
41.528
1.00
14.52


ATOM
1175
CG
TRP
216
31.676
22.122
42.404
1.00
13.26


ATOM
1176
CD2
TRP
216
31.967
22.071
43.807
1.00
14.02


ATOM
1177
CE2
TRP
216
32.207
23.399
44.233
1.00
14.00


ATOM
1178
CE3
TRP
216
32.046
21.033
44.747
1.00
13.78


ATOM
1179
CD1
TRP
216
31.755
23.437
42.045
1.00
11.53


ATOM
1180
NE1
TRP
216
32.073
24.210
43.138
1.00
12.94


ATOM
1181
CZ2
TRP
216
32.519
23.717
45.558
1.00
13.90


ATOM
1182
CZ3
TRP
216
32.357
21.349
46.068
1.00
15.08


ATOM
1183
CH2
TRP
216
32.589
22.684
46.459
1.00
16.36


ATOM
1184
C
TRP
216
28.874
21.276
42.111
1.00
14.83


ATOM
1185
O
TRP
216
28.560
21.768
43.193
1.00
16.29


ATOM
1186
N
ARG
217
28.253
21.575
40.978
1.00
14.63


ATOM
1187
CA
ARG
217
27.159
22.528
40.959
1.00
14.60


ATOM
1188
CB
ARG
217
26.903
22.978
39.517
1.00
12.12


ATOM
1189
CG
ARG
217
28.042
23.875
39.021
1.00
13.34


ATOM
1190
CD
ARG
217
28.071
24.122
37.520
1.00
12.75


ATOM
1191
NE
ARG
217
29.163
25.043
37.206
1.00
12.99


ATOM
1192
CZ
ARG
217
30.458
24.750
37.326
1.00
11.14


ATOM
1193
NH1
ARG
217
31.373
25.658
37.033
1.00
12.84


ATOM
1194
NH2
ARG
217
30.844
23.544
37.714
1.00
12.36


ATOM
1195
C
ARG
217
25.905
21.958
41.622
1.00
15.54


ATOM
1196
O
ARG
217
25.174
22.680
42.293
1.00
15.86


ATOM
1197
N
ASP
218
25.672
20.657
41.459
1.00
16.94


ATOM
1198
CA
ASP
218
24.515
20.012
42.077
1.00
17.27


ATOM
1199
CB
ASP
218
24.403
18.543
41.652
1.00
16.71


ATOM
1200
CG
ASP
218
24.061
18.372
40.185
1.00
19.76


ATOM
1201
OD1
ASP
218
23.644
19.355
39.531
1.00
21.08


ATOM
1202
OD2
ASP
218
24.194
17.233
39.691
1.00
19.39


ATOM
1203
C
ASP
218
24.624
20.048
43.601
1.00
16.65


ATOM
1204
O
ASP
218
23.633
20.251
44.300
1.00
18.01


ATOM
1205
N
LYS
219
25.836
19.846
44.108
1.00
17.48


ATOM
1206
CA
LYS
219
26.068
19.814
45.550
1.00
18.13


ATOM
1207
CB
LYS
219
27.184
18.817
45.867
1.00
18.30


ATOM
1208
CG
LYS
219
26.905
17.403
45.361
1.00
20.52


ATOM
1209
CD
LYS
219
25.600
16.846
45.927
1.00
21.52


ATOM
1210
CE
LYS
219
25.657
16.721
47.445
1.00
23.83


ATOM
1211
NZ
LYS
219
26.779
15.849
47.890
1.00
24.81


ATOM
1212
C
LYS
219
26.376
21.151
46.221
1.00
18.56


ATOM
1213
O
LYS
219
25.864
21.430
47.302
1.00
19.73


ATOM
1214
N
ALA
220
27.221
21.972
45.607
1.00
18.09


ATOM
1215
CA
ALA
220
27.552
23.264
46.207
1.00
17.10


ATOM
1216
CB
ALA
220
28.988
23.656
45.867
1.00
16.84


ATOM
1217
C
ALA
220
26.585
24.350
45.739
1.00
15.48


ATOM
1218
O
ALA
220
25.976
25.038
46.553
1.00
16.35


ATOM
1219
N
GLY
221
26.444
24.486
44.425
1.00
14.00


ATOM
1220
CA
GLY
221
25.561
25.491
43.868
1.00
12.74


ATOM
1221
C
GLY
221
24.118
25.433
44.344
1.00
15.22


ATOM
1222
O
GLY
221
23.598
26.412
44.886
1.00
15.26


ATOM
1223
N
ARG
222
23.461
24.295
44.147
1.00
14.02


ATOM
1224
CA
ARG
222
22.068
24.157
44.556
1.00
15.84


ATOM
1225
CB
ARG
222
21.532
22.774
44.160
1.00
16.90


ATOM
1226
CG
ARG
222
21.412
22.572
42.655
1.00
16.24


ATOM
1227
CD
ARG
222
20.870
21.182
42.318
1.00
20.12


ATOM
1228
NE
ARG
222
20.609
21.044
40.888
1.00
23.09


ATOM
1229
CZ
ARG
222
20.399
19.884
40.269
1.00
25.88


ATOM
1230
NH1
ARG
222
20.417
18.746
40.952
1.00
24.84


ATOM
1231
NH2
ARG
222
20.182
19.860
38.960
1.00
26.85


ATOM
1232
C
ARG
222
21.846
24.385
46.050
1.00
14.53


ATOM
1233
O
ARG
222
20.813
24.918
46.452
1.00
15.21


ATOM
1234
N
ALA
223
22.821
23.991
46.861
1.00
13.97


ATOM
1235
CA
ALA
223
22.729
24.133
48.310
1.00
14.89


ATOM
1236
CB
ALA
223
23.818
23.284
48.980
1.00
14.97


ATOM
1237
C
ALA
223
22.822
25.581
48.794
1.00
15.26


ATOM
1238
O
ALA
223
22.443
25.891
49.923
1.00
15.20


ATOM
1239
N
ILE
224
23.328
26.470
47.949
1.00
14.59


ATOM
1240
CA
ILE
224
23.444
27.871
48.338
1.00
13.97


ATOM
1241
CB
ILE
224
24.651
28.545
47.629
1.00
13.29


ATOM
1242
CG2
ILE
224
24.713
30.027
47.970
1.00
11.18


ATOM
1243
CG1
ILE
224
25.950
27.852
48.051
1.00
15.89


ATOM
1244
CD1
ILE
224
26.228
27.904
49.550
1.00
14.70


ATOM
1245
C
ILE
224
22.163
28.644
48.007
1.00
13.79


ATOM
1246
O
ILE
224
21.842
29.638
48.655
1.00
14.26


ATOM
1247
N
LEU
225
21.422
28.167
47.014
1.00
13.03


ATOM
1248
CA
LEU
225
20.203
28.834
46.578
1.00
13.73


ATOM
1249
CB
LEU
225
19.521
28.011
45.481
1.00
13.73


ATOM
1250
CG
LEU
225
18.230
28.616
44.922
1.00
15.14


ATOM
1251
CD1
LEU
225
18.513
29.995
44.338
1.00
13.02


ATOM
1252
CD2
LEU
225
17.646
27.684
43.865
1.00
15.05


ATOM
1253
C
LEU
225
19.188
29.170
47.673
1.00
15.99


ATOM
1254
O
LEU
225
18.557
30.228
47.626
1.00
16.45


ATOM
1255
N
GLN
226
19.022
28.296
48.661
1.00
17.25


ATOM
1256
CA
GLN
226
18.053
28.578
49.717
1.00
17.93


ATOM
1257
CB
GLN
226
17.860
27.365
50.629
1.00
18.12


ATOM
1258
CG
GLN
226
19.093
26.934
51.392
1.00
21.07


ATOM
1259
CD
GLN
226
18.752
26.031
52.566
1.00
25.37


ATOM
1260
OE1
GLN
226
19.475
25.083
52.869
1.00
28.28


ATOM
1261
NE2
GLN
226
17.651
26.334
53.242
1.00
25.39


ATOM
1262
C
GLN
226
18.422
29.787
50.570
1.00
18.27


ATOM
1263
O
GLN
226
17.552
30.381
51.207
1.00
18.35


ATOM
1264
N
PHE
227
19.702
30.158
50.579
1.00
17.08


ATOM
1265
CA
PHE
227
20.156
31.298
51.376
1.00
17.03


ATOM
1266
CB
PHE
227
21.531
31.015
52.001
1.00
17.75


ATOM
1267
CG
PHE
227
21.594
29.756
52.820
1.00
19.66


ATOM
1268
CD1
PHE
227
22.214
28.617
52.315
1.00
18.54


ATOM
1269
CD2
PHE
227
21.058
29.715
54.102
1.00
19.80


ATOM
1270
CE1
PHE
227
22.303
27.457
53.077
1.00
20.33


ATOM
1271
CE2
PHE
227
21.138
28.560
54.874
1.00
20.11


ATOM
1272
CZ
PHE
227
21.763
27.428
54.362
1.00
21.23


ATOM
1273
C
PHE
227
20.277
32.631
50.635
1.00
15.96


ATOM
1274
O
PHE
227
20.123
33.686
51.243
1.00
14.83


ATOM
1275
N
TYR
228
20.552
32.588
49.332
1.00
14.81


ATOM
1276
CA
TYR
228
20.786
33.813
48.566
1.00
13.93


ATOM
1277
CB
TYR
228
21.163
33.484
47.114
1.00
12.40


ATOM
1278
CG
TYR
228
22.287
34.363
46.617
1.00
11.13


ATOM
1279
CD1
TYR
228
23.561
34.271
47.181
1.00
10.09


ATOM
1280
CE1
TYR
228
24.596
35.119
46.780
1.00
9.24


ATOM
1281
CD2
TYR
228
22.073
35.327
45.628
1.00
12.00


ATOM
1282
CE2
TYR
228
23.105
36.184
45.218
1.00
9.28


ATOM
1283
CZ
TYR
228
24.361
36.073
45.803
1.00
10.33


ATOM
1284
OH
TYR
228
25.380
36.927
45.447
1.00
9.24


ATOM
1285
C
TYR
228
19.750
34.930
48.561
1.00
14.20


ATOM
1286
O
TYR
228
20.095
36.092
48.787
1.00
13.92


ATOM
1287
N
PRO
229
18.476
34.615
48.287
1.00
15.32


ATOM
1288
CD
PRO
229
17.850
33.355
47.841
1.00
14.61


ATOM
1289
CA
PRO
229
17.504
35.713
48.288
1.00
14.32


ATOM
1290
CB
PRO
229
16.183
35.001
48.005
1.00
14.50


ATOM
1291
CG
PRO
229
16.612
33.854
47.114
1.00
14.48


ATOM
1292
C
PRO
229
17.487
36.503
49.603
1.00
15.12


ATOM
1293
O
PRO
229
17.378
37.731
49.592
1.00
14.15


ATOM
1294
N
LYS
230
17.612
35.803
50.730
1.00
15.42


ATOM
1295
CA
LYS
230
17.598
36.463
52.038
1.00
15.89


ATOM
1296
CB
LYS
230
17.459
35.441
53.166
1.00
16.82


ATOM
1297
CG
LYS
230
16.964
36.061
54.462
1.00
19.46


ATOM
1298
CD
LYS
230
15.624
36.737
54.200
1.00
24.16


ATOM
1299
CE
LYS
230
14.959
37.224
55.463
1.00
28.11


ATOM
1300
NZ
LYS
230
13.630
37.824
55.153
1.00
26.83


ATOM
1301
C
LYS
230
18.871
37.272
52.240
1.00
14.81


ATOM
1302
O
LYS
230
18.852
38.364
52.811
1.00
12.92


ATOM
1303
N
TYR
231
19.979
36.714
51.774
1.00
14.42


ATOM
1304
CA
TYR
231
21.270
37.375
51.848
1.00
11.87


ATOM
1305
CB
TYR
231
22.330
36.466
51.223
1.00
11.76


ATOM
1306
CG
TYR
231
23.525
37.197
50.660
1.00
10.89


ATOM
1307
CD1
TYR
231
24.499
37.736
51.500
1.00
9.98


ATOM
1308
CE1
TYR
231
25.612
38.397
50.976
1.00
12.44


ATOM
1309
CD2
TYR
231
23.683
37.341
49.279
1.00
11.71


ATOM
1310
CE2
TYR
231
24.788
38.004
48.745
1.00
12.56


ATOM
1311
CZ
TYR
231
25.750
38.523
49.597
1.00
11.83


ATOM
1312
OH
TYR
231
26.870
39.120
49.071
1.00
11.18


ATOM
1313
C
TYR
231
21.191
38.699
51.080
1.00
11.12


ATOM
1314
O
TYR
231
21.616
39.741
51.575
1.00
12.14


ATOM
1315
N
VAL
232
20.654
38.646
49.864
1.00
11.62


ATOM
1316
CA
VAL
232
20.516
39.833
49.019
1.00
10.85


ATOM
1317
CB
VAL
232
19.900
39.455
47.648
1.00
11.31


ATOM
1318
CG1
VAL
232
19.439
40.697
46.900
1.00
10.40


ATOM
1319
CG2
VAL
232
20.934
38.699
46.821
1.00
11.64


ATOM
1320
C
VAL
232
19.658
40.904
49.698
1.00
12.40


ATOM
1321
O
VAL
232
19.992
42.096
49.682
1.00
11.44


ATOM
1322
N
GLU
233
18.557
40.473
50.303
1.00
12.62


ATOM
1323
CA
GLU
233
17.661
41.389
50.995
1.00
14.05


ATOM
1324
CB
GLU
233
16.437
40.617
51.506
1.00
17.42


ATOM
1325
CG
GLU
233
15.557
41.381
52.487
1.00
22.94


ATOM
1326
CD
GLU
233
14.322
40.593
52.907
1.00
27.83


ATOM
1327
OE1
GLU
233
14.416
39.355
53.069
1.00
29.39


ATOM
1328
OE2
GLU
233
13.256
41.216
53.089
1.00
32.62


ATOM
1329
C
GLU
233
18.367
42.098
52.155
1.00
12.54


ATOM
1330
O
GLU
233
18.313
43.320
52.273
1.00
13.58


ATOM
1331
N
LEU
234
19.043
41.328
52.999
1.00
12.59


ATOM
1332
CA
LEU
234
19.738
41.885
54.153
1.00
12.98


ATOM
1333
CB
LEU
234
20.149
40.758
55.106
1.00
13.67


ATOM
1334
CG
LEU
234
18.968
40.015
55.738
1.00
16.89


ATOM
1335
CD1
LEU
234
19.464
38.803
56.512
1.00
16.48


ATOM
1336
CD2
LEU
234
18.200
40.964
56.650
1.00
16.76


ATOM
1337
C
LEU
234
20.952
42.750
53.820
1.00
12.60


ATOM
1338
O
LEU
234
21.145
43.801
54.430
1.00
11.00


ATOM
1339
N
ILE
235
21.774
42.328
52.862
1.00
10.69


ATOM
1340
CA
ILE
235
22.945
43.130
52.522
1.00
10.15


ATOM
1341
CB
ILE
235
23.963
42.341
51.654
1.00
11.30


ATOM
1342
CG2
ILE
235
23.383
42.074
50.252
1.00
8.24


ATOM
1343
CG1
ILE
235
25.283
43.124
51.589
1.00
9.63


ATOM
1344
CD1
ILE
235
26.426
42.355
50.948
1.00
9.83


ATOM
1345
C
ILE
235
22.525
44.422
51.820
1.00
9.51


ATOM
1346
O
ILE
235
23.177
45.456
51.970
1.00
9.55


ATOM
1347
N
ASN
236
21.430
44.372
51.066
1.00
9.09


ATOM
1348
CA
ASN
236
20.925
45.570
50.398
1.00
10.19


ATOM
1349
CB
ASN
236
19.825
45.225
49.385
1.00
10.23


ATOM
1350
CG
ASN
236
20.371
44.929
48.001
1.00
11.26


ATOM
1351
OD1
ASN
236
21.501
45.293
47.677
1.00
10.18


ATOM
1352
ND2
ASN
236
19.557
44.290
47.167
1.00
12.22


ATOM
1353
C
ASN
236
20.356
46.525
51.453
1.00
11.01


ATOM
1354
O
ASN
236
20.569
47.738
51.387
1.00
10.90


ATOM
1355
N
GLN
237
19.630
45.969
52.421
1.00
12.58


ATOM
1356
CA
GLN
237
19.038
46.769
53.489
1.00
12.11


ATOM
1357
CB
GLN
237
18.264
45.876
54.460
1.00
14.23


ATOM
1358
CG
GLN
237
17.428
46.638
55.483
1.00
14.79


ATOM
1359
CD
GLN
237
16.781
45.714
56.502
1.00
18.93


ATOM
1360
OE1
GLN
237
16.567
44.532
56.233
1.00
20.61


ATOM
1361
NE2
GLN
237
16.455
46.254
57.672
1.00
17.63


ATOM
1362
C
GLN
237
20.149
47.498
54.239
1.00
12.36


ATOM
1363
O
GLN
237
20.038
48.687
54.537
1.00
12.83


ATOM
1364
N
ALA
238
21.218
46.771
54.549
1.00
10.55


ATOM
1365
CA
ALA
238
22.353
47.361
55.245
1.00
10.94


ATOM
1366
CB
ALA
238
23.431
46.316
55.473
1.00
7.92


ATOM
1367
C
ALA
238
22.909
48.509
54.408
1.00
11.58


ATOM
1368
O
ALA
238
23.205
49.578
54.931
1.00
12.66


ATOM
1369
N
ALA
239
23.045
48.280
53.104
1.00
11.03


ATOM
1370
CA
ALA
239
23.569
49.302
52.207
1.00
12.87


ATOM
1371
CB
ALA
239
23.647
48.762
50.779
1.00
11.95


ATOM
1372
C
ALA
239
22.719
50.570
52.245
1.00
13.46


ATOM
1373
O
ALA
239
23.257
51.677
52.337
1.00
12.98


ATOM
1374
N
ARG
240
21.396
50.408
52.180
1.00
13.34


ATOM
1375
CA
ARG
240
20.491
51.556
52.204
1.00
13.67


ATOM
1376
CB
ARG
240
19.037
51.122
51.959
1.00
12.51


ATOM
1377
CG
ARG
240
18.763
50.570
50.559
1.00
14.85


ATOM
1378
CD
ARG
240
17.266
50.496
50.262
1.00
13.15


ATOM
1379
NE
ARG
240
16.531
49.731
51.269
1.00
15.23


ATOM
1380
CZ
ARG
240
16.450
48.405
51.307
1.00
17.70


ATOM
1381
NH1
ARG
240
17.060
47.665
50.380
1.00
15.68


ATOM
1382
NH2
ARG
240
15.759
47.814
52.278
1.00
16.05


ATOM
1383
C
ARG
240
20.583
52.299
53.533
1.00
13.93


ATOM
1384
O
ARG
240
20.502
53.526
53.571
1.00
13.67


ATOM
1385
N
LEU
241
20.753
51.553
54.619
1.00
14.68


ATOM
1386
CA
LEU
241
20.853
52.155
55.941
1.00
15.52


ATOM
1387
CB
LEU
241
20.731
51.075
57.025
1.00
14.97


ATOM
1388
CG
LEU
241
19.324
50.472
57.150
1.00
16.48


ATOM
1389
CD1
LEU
241
19.332
49.281
58.102
1.00
14.35


ATOM
1390
CD2
LEU
241
18.361
51.552
57.644
1.00
17.43


ATOM
1391
C
LEU
241
22.159
52.927
56.096
1.00
15.83


ATOM
1392
O
LEU
241
22.331
53.695
57.047
1.00
15.43


ATOM
1393
N
ASN
242
23.074
52.729
55.152
1.00
14.16


ATOM
1394
CA
ASN
242
24.350
53.426
55.185
1.00
13.59


ATOM
1395
CB
ASN
242
25.500
52.423
55.067
1.00
12.71


ATOM
1396
CG
ASN
242
25.778
51.711
56.384
1.00
15.20


ATOM
1397
OD1
ASN
242
26.069
52.354
57.395
1.00
14.44


ATOM
1398
ND2
ASN
242
25.678
50.385
56.382
1.00
13.74


ATOM
1399
C
ASN
242
24.463
54.516
54.120
1.00
13.25


ATOM
1400
O
ASN
242
25.540
55.063
53.894
1.00
13.69


ATOM
1401
N
GLY
243
23.346
54.820
53.462
1.00
13.09


ATOM
1402
CA
GLY
243
23.341
55.876
52.462
1.00
14.67


ATOM
1403
C
GLY
243
23.442
55.495
50.997
1.00
12.85


ATOM
1404
O
GLY
243
23.392
56.375
50.137
1.00
13.08


ATOM
1405
N
TYR
244
23.595
54.207
50.701
1.00
12.73


ATOM
1406
CA
TYR
244
23.697
53.752
49.312
1.00
12.34


ATOM
1407
CB
TYR
244
24.715
52.609
49.200
1.00
10.80


ATOM
1408
CG
TYR
244
26.115
52.990
49.633
1.00
12.14


ATOM
1409
CD1
TYR
244
26.589
52.660
50.901
1.00
11.88


ATOM
1410
CE1
TYR
244
27.870
53.038
51.316
1.00
10.81


ATOM
1411
CD2
TYR
244
26.956
53.711
48.783
1.00
9.56


ATOM
1412
CE2
TYR
244
28.237
54.096
49.189
1.00
10.67


ATOM
1413
CZ
TYR
244
28.684
53.757
50.455
1.00
10.80


ATOM
1414
OH
TYR
244
29.937
54.150
50.864
1.00
13.51


ATOM
1415
C
TYR
244
22.337
53.281
48.802
1.00
12.43


ATOM
1416
O
TYR
244
21.401
53.121
49.585
1.00
15.41


ATOM
1417
N
VAL
245
22.215
53.064
47.493
1.00
13.45


ATOM
1418
CA
VAL
245
20.945
52.596
46.937
1.00
13.11


ATOM
1419
CB
VAL
245
20.752
53.071
45.476
1.00
15.33


ATOM
1420
CG1
VAL
245
20.670
54.595
45.446
1.00
17.06


ATOM
1421
CG2
VAL
245
21.894
52.589
44.604
1.00
15.86


ATOM
1422
C
VAL
245
20.807
51.073
47.015
1.00
11.99


ATOM
1423
O
VAL
245
19.697
50.549
47.045
1.00
13.05


ATOM
1424
N
ASP
246
21.936
50.368
47.047
1.00
9.74


ATOM
1425
CA
ASP
246
21.946
48.907
47.163
1.00
10.63


ATOM
1426
CB
ASP
246
21.378
48.233
45.896
1.00
9.06


ATOM
1427
CG
ASP
246
22.202
48.520
44.644
1.00
11.98


ATOM
1428
OD1
ASP
246
23.385
48.125
44.586
1.00
10.98


ATOM
1429
OD2
ASP
246
21.658
49.140
43.708
1.00
10.66


ATOM
1430
C
ASP
246
23.373
48.424
47.444
1.00
9.60


ATOM
1431
O
ASP
246
24.308
49.219
47.429
1.00
11.47


ATOM
1432
N
ALA
247
23.538
47.130
47.706
1.00
9.86


ATOM
1433
CA
ALA
247
24.858
46.577
48.007
1.00
10.45


ATOM
1434
CB
ALA
247
24.738
45.084
48.336
1.00
9.21


ATOM
1435
C
ALA
247
25.895
46.787
46.894
1.00
9.94


ATOM
1436
O
ALA
247
27.072
47.006
47.177
1.00
10.23


ATOM
1437
N
GLY
248
25.465
46.701
45.638
1.00
9.68


ATOM
1438
CA
GLY
248
26.388
46.894
44.527
1.00
9.78


ATOM
1439
C
GLY
248
26.974
48.297
44.551
1.00
12.15


ATOM
1440
O
GLY
248
28.177
48.499
44.354
1.00
11.20


ATOM
1441
N
ASP
249
26.103
49.271
44.790
1.00
12.09


ATOM
1442
CA
ASP
249
26.494
50.674
44.873
1.00
12.50


ATOM
1443
CB
ASP
249
25.246
51.506
45.210
1.00
12.82


ATOM
1444
CG
ASP
249
25.528
52.995
45.337
1.00
13.95


ATOM
1445
OD1
ASP
249
26.395
53.521
44.610
1.00
13.98


ATOM
1446
OD2
ASP
249
24.851
53.647
46.159
1.00
13.82


ATOM
1447
C
ASP
249
27.562
50.795
45.961
1.00
12.92


ATOM
1448
O
ASP
249
28.640
51.350
45.741
1.00
11.95


ATOM
1449
N
SER
250
27.255
50.251
47.133
1.00
13.21


ATOM
1450
CA
SER
250
28.178
50.277
48.259
1.00
13.25


ATOM
1451
CB
SER
250
27.585
49.479
49.424
1.00
14.69


ATOM
1452
OG
SER
250
28.391
49.595
50.583
1.00
18.32


ATOM
1453
C
SER
250
29.557
49.705
47.876
1.00
12.60


ATOM
1454
O
SER
250
30.587
50.324
48.143
1.00
11.74


ATOM
1455
N
TRP
251
29.574
48.530
47.251
1.00
10.27


ATOM
1456
CA
TRP
251
30.840
47.908
46.847
1.00
11.25


ATOM
1457
CB
TRP
251
30.587
46.525
46.236
1.00
10.10


ATOM
1458
CG
TRP
251
30.163
45.479
47.223
1.00
10.89


ATOM
1459
CD2
TRP
251
29.970
44.084
46.957
1.00
10.95


ATOM
1460
CE2
TRP
251
29.587
43.475
48.174
1.00
12.43


ATOM
1461
CE3
TRP
251
30.086
43.288
45.808
1.00
9.38


ATOM
1462
CD1
TRP
251
29.895
45.657
48.554
1.00
10.57


ATOM
1463
NE1
TRP
251
29.549
44.457
49.129
1.00
12.56


ATOM
1464
CZ2
TRP
251
29.317
42.101
48.276
1.00
11.07


ATOM
1465
CZ3
TRP
251
29.817
41.923
45.909
1.00
10.48


ATOM
1466
CH2
TRP
251
29.437
41.345
47.135
1.00
9.03


ATOM
1467
C
TRP
251
31.641
48.751
45.852
1.00
10.66


ATOM
1468
O
TRP
251
32.847
48.926
46.009
1.00
11.21


ATOM
1469
N
ARG
252
30.972
49.266
44.824
1.00
10.93


ATOM
1470
CA
ARG
252
31.654
50.075
43.824
1.00
10.15


ATOM
1471
CB
ARG
252
30.691
50.462
42.686
1.00
10.20


ATOM
1472
CG
ARG
252
30.225
49.288
41.810
1.00
9.68


ATOM
1473
CD
ARG
252
29.435
49.763
40.580
1.00
10.48


ATOM
1474
NE
ARG
252
28.195
50.475
40.912
1.00
10.26


ATOM
1475
CZ
ARG
252
27.039
49.892
41.215
1.00
12.09


ATOM
1476
NH1
ARG
252
25.973
50.633
41.506
1.00
10.42


ATOM
1477
NH2
ARG
252
26.940
48.569
41.217
1.00
10.98


ATOM
1478
C
ARG
252
32.271
51.337
44.440
1.00
11.46


ATOM
1479
O
ARG
252
33.296
51.821
43.969
1.00
10.38


ATOM
1480
N
SER
253
31.657
51.852
45.505
1.00
13.01


ATOM
1481
CA
SER
253
32.147
53.065
46.157
1.00
13.62


ATOM
1482
CB
SER
253
31.224
53.465
47.309
1.00
12.96


ATOM
1483
OG
SER
253
31.473
52.676
48.460
1.00
16.21


ATOM
1484
C
SER
253
33.575
52.932
46.685
1.00
12.79


ATOM
1485
O
SER
253
34.253
53.935
46.893
1.00
12.73


ATOM
1486
N
MET
254
34.025
51.699
46.903
1.00
14.11


ATOM
1487
CA
MET
254
35.378
51.462
47.406
1.00
14.12


ATOM
1488
CB
MET
254
35.622
49.960
47.620
1.00
16.31


ATOM
1489
CG
MET
254
34.751
49.331
48.699
1.00
19.32


ATOM
1490
SD
MET
254
35.231
47.629
49.106
1.00
25.77


ATOM
1491
CE
MET
254
34.333
46.745
47.898
1.00
17.52


ATOM
1492
C
MET
254
36.440
52.013
46.457
1.00
12.73


ATOM
1493
O
MET
254
37.585
52.214
46.849
1.00
14.95


ATOM
1494
N
TYR
255
36.061
52.251
45.207
1.00
11.95


ATOM
1495
CA
TYR
255
37.001
52.782
44.227
1.00
10.96


ATOM
1496
CB
TYR
255
36.734
52.180
42.840
1.00
10.71


ATOM
1497
CG
TYR
255
37.055
50.711
42.767
1.00
10.53


ATOM
1498
CD1
TYR
255
36.120
49.755
43.159
1.00
10.46


ATOM
1499
CE1
TYR
255
36.441
48.401
43.183
1.00
10.93


ATOM
1500
CD2
TYR
255
38.326
50.276
42.389
1.00
11.13


ATOM
1501
CE2
TYR
255
38.661
48.915
42.415
1.00
11.62


ATOM
1502
CZ
TYR
255
37.711
47.987
42.817
1.00
11.67


ATOM
1503
OH
TYR
255
38.039
46.653
42.896
1.00
10.68


ATOM
1504
C
TYR
255
36.976
54.305
44.139
1.00
10.20


ATOM
1505
O
TYR
255
37.845
54.898
43.505
1.00
11.25


ATOM
1506
N
GLU
256
35.985
54.932
44.767
1.00
10.48


ATOM
1507
CA
GLU
256
35.874
56.396
44.750
1.00
11.92


ATOM
1508
CB
GLU
256
36.950
57.018
45.649
1.00
12.76


ATOM
1509
CG
GLU
256
36.925
56.528
47.097
1.00
16.04


ATOM
1510
CD
GLU
256
37.925
57.263
47.993
1.00
20.13


ATOM
1511
OE1
GLU
256
39.145
57.187
47.736
1.00
19.80


ATOM
1512
OE2
GLU
256
37.487
57.917
48.959
1.00
23.10


ATOM
1513
C
GLU
256
36.040
56.925
43.327
1.00
11.30


ATOM
1514
O
GLU
256
36.703
57.935
43.100
1.00
12.11


ATOM
1515
N
THR
257
35.430
56.236
42.371
1.00
11.67


ATOM
1516
CA
THR
257
35.537
56.607
40.965
1.00
11.88


ATOM
1517
CB
THR
257
36.511
55.649
40.239
1.00
13.99


ATOM
1518
OG1
THR
257
37.788
55.701
40.889
1.00
13.92


ATOM
1519
CG2
THR
257
36.679
56.043
38.775
1.00
13.03


ATOM
1520
C
THR
257
34.167
56.555
40.296
1.00
11.09


ATOM
1521
O
THR
257
33.691
55.490
39.918
1.00
10.49


ATOM
1522
N
PRO
258
33.514
57.719
40.154
1.00
11.64


ATOM
1523
CD
PRO
258
33.992
59.028
40.638
1.00
11.87


ATOM
1524
CA
PRO
258
32.186
57.842
39.539
1.00
12.51


ATOM
1525
CB
PRO
258
31.953
59.352
39.526
1.00
13.07


ATOM
1526
CG
PRO
258
32.703
59.817
40.754
1.00
13.28


ATOM
1527
C
PRO
258
32.072
57.226
38.143
1.00
12.84


ATOM
1528
O
PRO
258
31.014
56.719
37.762
1.00
13.80


ATOM
1529
N
SER
259
33.164
57.270
37.387
1.00
12.06


ATOM
1530
CA
SER
259
33.182
56.728
36.030
1.00
13.03


ATOM
1531
CB
SER
259
34.154
57.536
35.170
1.00
15.05


ATOM
1532
OG
SER
259
35.466
57.473
35.707
1.00
14.74


ATOM
1533
C
SER
259
33.588
55.254
35.987
1.00
12.40


ATOM
1534
O
SER
259
33.830
54.708
34.917
1.00
11.54


ATOM
1535
N
LEU
260
33.649
54.615
37.150
1.00
12.21


ATOM
1536
CA
LEU
260
34.060
53.214
37.243
1.00
12.51


ATOM
1537
CB
LEU
260
33.766
52.665
38.648
1.00
11.05


ATOM
1538
CG
LEU
260
34.282
51.236
38.891
1.00
13.73


ATOM
1539
CD1
LEU
260
35.808
51.214
38.751
1.00
10.71


ATOM
1540
CD2
LEU
260
33.870
50.751
40.275
1.00
12.15


ATOM
1541
C
LEU
260
33.465
52.256
36.207
1.00
13.15


ATOM
1542
O
LEU
260
34.205
51.578
35.485
1.00
9.99


ATOM
1543
N
GLU
261
32.138
52.187
36.131
1.00
11.55


ATOM
1544
CA
GLU
261
31.512
51.266
35.190
1.00
13.22


ATOM
1545
CB
GLU
261
29.985
51.292
35.353
1.00
12.14


ATOM
1546
CG
GLU
261
29.554
50.650
36.671
1.00
15.06


ATOM
1547
CD
GLU
261
28.065
50.396
36.774
1.00
16.56


ATOM
1548
OE1
GLU
261
27.388
50.379
35.727
1.00
20.06


ATOM
1549
OE2
GLU
261
27.574
50.197
37.906
1.00
17.33


ATOM
1550
C
GLU
261
31.923
51.495
33.740
1.00
13.12


ATOM
1551
O
GLU
261
32.193
50.538
33.011
1.00
11.67


ATOM
1552
N
GLN
262
31.988
52.752
33.320
1.00
11.67


ATOM
1553
CA
GLN
262
32.395
53.042
31.952
1.00
13.82


ATOM
1554
CB
GLN
262
32.128
54.508
31.607
1.00
15.74


ATOM
1555
CG
GLN
262
30.659
54.915
31.661
1.00
24.70


ATOM
1556
CD
GLN
262
30.455
56.378
31.298
1.00
29.02


ATOM
1557
OE1
GLN
262
30.558
56.762
30.132
1.00
35.05


ATOM
1558
NE2
GLN
262
30.183
57.205
32.300
1.00
32.50


ATOM
1559
C
GLN
262
33.883
52.733
31.760
1.00
12.94


ATOM
1560
O
GLN
262
34.285
52.213
30.715
1.00
11.76


ATOM
1561
N
ASP
263
34.696
53.059
32.764
1.00
11.79


ATOM
1562
CA
ASP
263
36.131
52.805
32.689
1.00
12.07


ATOM
1563
CB
ASP
263
36.845
53.238
33.975
1.00
12.41


ATOM
1564
CG
ASP
263
36.890
54.742
34.145
1.00
13.78


ATOM
1565
OD1
ASP
263
36.821
55.453
33.127
1.00
14.89


ATOM
1566
OD2
ASP
263
37.015
55.211
35.296
1.00
15.49


ATOM
1567
C
ASP
263
36.410
51.328
32.469
1.00
13.01


ATOM
1568
O
ASP
263
37.190
50.957
31.593
1.00
11.20


ATOM
1569
N
LEU
264
35.773
50.495
33.284
1.00
12.13


ATOM
1570
CA
LEU
264
35.958
49.055
33.207
1.00
13.22


ATOM
1571
CB
LEU
264
35.259
48.379
34.393
1.00
12.89


ATOM
1572
CG
LEU
264
35.758
48.893
35.750
1.00
17.46


ATOM
1573
CD1
LEU
264
35.091
48.124
36.883
1.00
15.64


ATOM
1574
CD2
LEU
264
37.281
48.756
35.826
1.00
18.10


ATOM
1575
C
LEU
264
35.449
48.498
31.884
1.00
13.15


ATOM
1576
O
LEU
264
36.049
47.591
31.318
1.00
12.41


ATOM
1577
N
GLU
265
34.348
49.051
31.387
1.00
15.01


ATOM
1578
CA
GLU
265
33.788
48.612
30.114
1.00
18.16


ATOM
1579
CB
GLU
265
32.457
49.326
29.856
1.00
20.13


ATOM
1580
CG
GLU
265
31.833
49.068
28.485
1.00
26.44


ATOM
1581
CD
GLU
265
31.578
47.599
28.209
1.00
31.50


ATOM
1582
OE1
GLU
265
31.057
46.900
29.108
1.00
33.66


ATOM
1583
OE2
GLU
265
31.886
47.145
27.085
1.00
34.88


ATOM
1584
C
GLU
265
34.773
48.889
28.966
1.00
18.71


ATOM
1585
O
GLU
265
34.969
48.038
28.094
1.00
17.84


ATOM
1586
N
ARG
266
35.389
50.072
28.971
1.00
16.94


ATOM
1587
CA
ARG
266
36.355
50.425
27.932
1.00
17.44


ATOM
1588
CB
ARG
266
36.840
51.873
28.101
1.00
20.53


ATOM
1589
CG
ARG
266
35.900
52.936
27.550
1.00
22.86


ATOM
1590
CD
ARG
266
36.534
54.323
27.645
1.00
23.46


ATOM
1591
NE
ARG
266
36.579
54.824
29.016
1.00
25.90


ATOM
1592
CZ
ARG
266
35.566
55.437
29.623
1.00
28.47


ATOM
1593
NH1
ARG
266
34.423
55.634
28.979
1.00
29.44


ATOM
1594
NH2
ARG
266
35.693
55.851
30.876
1.00
30.11


ATOM
1595
C
ARG
266
37.554
49.486
27.986
1.00
15.99


ATOM
1596
O
ARG
266
38.055
49.042
26.955
1.00
15.42


ATOM
1597
N
LEU
267
38.014
49.188
29.197
1.00
15.40


ATOM
1598
CA
LEU
267
39.154
48.299
29.372
1.00
13.76


ATOM
1599
CB
LEU
267
39.539
48.228
30.853
1.00
13.89


ATOM
1600
CG
LEU
267
40.091
49.539
31.438
1.00
13.95


ATOM
1601
CD1
LEU
267
40.200
49.433
32.952
1.00
12.21


ATOM
1602
CD2
LEU
267
41.462
49.849
30.815
1.00
12.02


ATOM
1603
C
LEU
267
38.836
46.907
28.830
1.00
15.08


ATOM
1604
O
LEU
267
39.655
46.296
28.135
1.00
13.11


ATOM
1605
N
PHE
268
37.642
46.412
29.136
1.00
14.37


ATOM
1606
CA
PHE
268
37.233
45.098
28.658
1.00
14.85


ATOM
1607
CB
PHE
268
35.841
44.735
29.172
1.00
15.58


ATOM
1608
CG
PHE
268
35.308
43.453
28.590
1.00
19.42


ATOM
1609
CD1
PHE
268
35.795
42.219
29.026
1.00
17.97


ATOM
1610
CD2
PHE
268
34.373
43.480
27.561
1.00
17.52


ATOM
1611
CE1
PHE
268
35.360
41.036
28.439
1.00
20.24


ATOM
1612
CE2
PHE
268
33.932
42.301
26.966
1.00
20.46


ATOM
1613
CZ
PHE
268
34.428
41.076
27.407
1.00
20.47


ATOM
1614
C
PHE
268
37.222
45.061
27.132
1.00
15.22


ATOM
1615
O
PHE
268
37.717
44.113
26.521
1.00
15.06


ATOM
1616
N
GLN
269
36.649
46.094
26.521
1.00
14.71


ATOM
1617
CA
GLN
269
36.570
46.174
25.066
1.00
15.04


ATOM
1618
CB
GLN
269
35.797
47.427
24.642
1.00
18.56


ATOM
1619
CG
GLN
269
34.296
47.359
24.893
1.00
23.06


ATOM
1620
CD
GLN
269
33.650
46.149
24.238
1.00
25.97


ATOM
1621
OE1
GLN
269
33.962
45.805
23.098
1.00
27.07


ATOM
1622
NE2
GLN
269
32.736
45.506
24.953
1.00
27.62


ATOM
1623
C
GLN
269
37.936
46.172
24.389
1.00
14.54


ATOM
1624
O
GLN
269
38.082
45.640
23.297
1.00
13.32


ATOM
1625
N
GLU
270
38.936
46.767
25.030
1.00
15.04


ATOM
1626
CA
GLU
270
40.269
46.802
24.445
1.00
17.22


ATOM
1627
CB
GLU
270
41.152
47.805
25.188
1.00
20.98


ATOM
1628
CG
GLU
270
40.700
49.238
25.008
1.00
27.35


ATOM
1629
CD
GLU
270
41.710
50.229
25.524
1.00
33.16


ATOM
1630
OE1
GLU
270
42.862
50.199
25.039
1.00
38.02


ATOM
1631
OE2
GLU
270
41.356
51.040
26.409
1.00
36.92


ATOM
1632
C
GLU
270
40.952
45.437
24.412
1.00
15.82


ATOM
1633
O
GLU
270
41.820
45.196
23.573
1.00
14.50


ATOM
1634
N
LEU
271
40.567
44.548
25.320
1.00
13.35


ATOM
1635
CA
LEU
271
41.156
43.214
25.356
1.00
15.36


ATOM
1636
CB
LEU
271
41.353
42.771
26.805
1.00
16.31


ATOM
1637
CG
LEU
271
42.710
43.258
27.322
1.00
19.74


ATOM
1638
CD1
LEU
271
42.552
44.028
28.610
1.00
19.63


ATOM
1639
CD2
LEU
271
43.631
42.059
27.493
1.00
19.25


ATOM
1640
C
LEU
271
40.340
42.177
24.583
1.00
15.26


ATOM
1641
O
LEU
271
40.684
40.993
24.545
1.00
15.34


ATOM
1642
N
GLN
272
39.267
42.637
23.951
1.00
15.74


ATOM
1643
CA
GLN
272
38.395
41.772
23.163
1.00
16.76


ATOM
1644
CB
GLN
272
37.193
42.572
22.663
1.00
18.77


ATOM
1645
CG
GLN
272
36.064
42.594
23.656
1.00
19.01


ATOM
1646
CD
GLN
272
35.339
41.272
23.691
1.00
20.95


ATOM
1647
OE1
GLN
272
34.458
41.017
22.869
1.00
24.44


ATOM
1648
NE2
GLN
272
35.717
40.412
24.627
1.00
20.60


ATOM
1649
C
GLN
272
39.099
41.109
21.986
1.00
18.21


ATOM
1650
O
GLN
272
38.980
39.899
21.780
1.00
19.85


ATOM
1651
N
PRO
273
39.831
41.892
21.181
1.00
19.01


ATOM
1652
CD
PRO
273
39.939
43.364
21.145
1.00
19.93


ATOM
1653
CA
PRO
273
40.525
41.290
20.042
1.00
18.86


ATOM
1654
CB
PRO
273
41.321
42.465
19.473
1.00
20.13


ATOM
1655
CG
PRO
273
40.387
43.624
19.711
1.00
18.58


ATOM
1656
C
PRO
273
41.418
40.135
20.480
1.00
19.29


ATOM
1657
O
PRO
273
41.425
39.067
19.864
1.00
20.36


ATOM
1658
N
LEU
274
42.161
40.351
21.558
1.00
17.91


ATOM
1659
CA
LEU
274
43.062
39.335
22.073
1.00
15.61


ATOM
1660
CB
LEU
274
43.958
39.950
23.148
1.00
19.23


ATOM
1661
CG
LEU
274
45.126
39.145
23.717
1.00
21.54


ATOM
1662
CD1
LEU
274
45.847
38.382
22.608
1.00
24.13


ATOM
1663
CD2
LEU
274
46.079
40.107
24.415
1.00
22.56


ATOM
1664
C
LEU
274
42.294
38.128
22.622
1.00
15.23


ATOM
1665
O
LEU
274
42.626
36.987
22.305
1.00
13.78


ATOM
1666
N
TYR
275
41.264
38.369
23.432
1.00
12.57


ATOM
1667
CA
TYR
275
40.494
37.255
23.977
1.00
12.75


ATOM
1668
CB
TYR
275
39.449
37.723
24.988
1.00
11.47


ATOM
1669
CG
TYR
275
38.643
36.554
25.512
1.00
11.88


ATOM
1670
CD1
TYR
275
39.245
35.574
26.298
1.00
9.65


ATOM
1671
CE1
TYR
275
38.544
34.449
26.711
1.00
11.95


ATOM
1672
CD2
TYR
275
37.306
36.382
25.151
1.00
10.41


ATOM
1673
CE2
TYR
275
36.591
35.258
25.556
1.00
10.77


ATOM
1674
CZ
TYR
275
37.216
34.299
26.335
1.00
11.79


ATOM
1675
OH
TYR
275
36.518
33.196
26.758
1.00
12.85


ATOM
1676
C
TYR
275
39.779
36.457
22.890
1.00
12.15


ATOM
1677
O
TYR
275
39.819
35.230
22.886
1.00
11.27


ATOM
1678
N
LEU
276
39.116
37.155
21.976
1.00
12.64


ATOM
1679
CA
LEU
276
38.400
36.478
20.903
1.00
12.64


ATOM
1680
CB
LEU
276
37.689
37.499
20.016
1.00
12.92


ATOM
1681
CG
LEU
276
36.589
38.299
20.719
1.00
15.08


ATOM
1682
CD1
LEU
276
35.965
39.298
19.744
1.00
13.79


ATOM
1683
CD2
LEU
276
35.534
37.338
21.267
1.00
16.31


ATOM
1684
C
LEU
276
39.316
35.601
20.057
1.00
12.23


ATOM
1685
O
LEU
276
38.913
34.530
19.608
1.00
13.24


ATOM
1686
N
ASN
277
40.544
36.054
19.834
1.00
10.74


ATOM
1687
CA
ASN
277
41.479
35.269
19.041
1.00
11.60


ATOM
1688
CB
ASN
277
42.654
36.139
18.593
1.00
11.61


ATOM
1689
CG
ASN
277
42.393
36.814
17.257
1.00
16.00


ATOM
1690
OD1
ASN
277
42.442
36.164
16.207
1.00
14.40


ATOM
1691
ND2
ASN
277
42.094
38.115
17.287
1.00
13.69


ATOM
1692
C
ASN
277
41.962
34.051
19.827
1.00
11.77


ATOM
1693
O
ASN
277
42.124
32.969
19.266
1.00
11.85


ATOM
1694
N
LEU
278
42.180
34.227
21.125
1.00
10.50


ATOM
1695
CA
LEU
278
42.624
33.116
21.958
1.00
10.97


ATOM
1696
CB
LEU
278
42.955
33.600
23.372
1.00
8.91


ATOM
1697
CG
LEU
278
43.363
32.498
24.359
1.00
11.30


ATOM
1698
CD1
LEU
278
44.732
31.924
23.970
1.00
9.95


ATOM
1699
CD2
LEU
278
43.404
33.067
25.770
1.00
9.64


ATOM
1700
C
LEU
278
41.496
32.089
22.023
1.00
9.88


ATOM
1701
O
LEU
278
41.733
30.886
21.922
1.00
9.70


ATOM
1702
N
HIS
279
40.274
32.589
22.193
1.00
9.53


ATOM
1703
CA
HIS
279
39.068
31.762
22.272
1.00
10.82


ATOM
1704
CB
HIS
279
37.836
32.667
22.421
1.00
10.16


ATOM
1705
CG
HIS
279
36.526
31.938
22.379
1.00
10.69


ATOM
1706
CD2
HIS
279
35.770
31.528
21.333
1.00
7.62


ATOM
1707
ND1
HIS
279
35.821
31.601
23.516
1.00
12.88


ATOM
1708
CE1
HIS
279
34.685
31.019
23.172
1.00
7.41


ATOM
1709
NE2
HIS
279
34.629
30.963
21.853
1.00
10.98


ATOM
1710
C
HIS
279
38.914
30.886
21.030
1.00
10.36


ATOM
1711
O
HIS
279
38.667
29.685
21.133
1.00
10.76


ATOM
1712
N
ALA
280
39.066
31.489
19.857
1.00
10.79


ATOM
1713
CA
ALA
280
38.931
30.752
18.601
1.00
11.15


ATOM
1714
CB
ALA
280
38.930
31.723
17.429
1.00
9.52


ATOM
1715
C
ALA
280
40.032
29.705
18.422
1.00
11.20


ATOM
1716
O
ALA
280
39.780
28.600
17.938
1.00
10.26


ATOM
1717
N
TYR
281
41.255
30.053
18.810
1.00
11.54


ATOM
1718
CA
TYR
281
42.373
29.120
18.692
1.00
11.98


ATOM
1719
CB
TYR
281
43.685
29.823
19.052
1.00
10.00


ATOM
1720
CG
TYR
281
44.895
28.914
19.065
1.00
12.10


ATOM
1721
CD1
TYR
281
45.461
28.446
17.879
1.00
13.19


ATOM
1722
CE1
TYR
281
46.567
27.594
17.895
1.00
11.96


ATOM
1723
CD2
TYR
281
45.465
28.507
20.271
1.00
10.46


ATOM
1724
CE2
TYR
281
46.564
27.660
20.299
1.00
12.98


ATOM
1725
CZ
TYR
281
47.112
27.205
19.109
1.00
14.87


ATOM
1726
OH
TYR
281
48.212
26.367
19.146
1.00
14.76


ATOM
1727
C
TYR
281
42.156
27.909
19.606
1.00
12.24


ATOM
1728
O
TYR
281
42.339
26.764
19.189
1.00
12.81


ATOM
1729
N
VAL
282
41.764
28.167
20.852
1.00
11.07


ATOM
1730
CA
VAL
282
41.517
27.093
21.809
1.00
10.51


ATOM
1731
CB
VAL
282
41.246
27.656
23.231
1.00
10.61


ATOM
1732
CG1
VAL
282
40.816
26.529
24.181
1.00
8.01


ATOM
1733
CG2
VAL
282
42.504
28.335
23.760
1.00
10.58


ATOM
1734
C
VAL
282
40.331
26.240
21.359
1.00
11.07


ATOM
1735
O
VAL
282
40.357
25.012
21.462
1.00
11.90


ATOM
1736
N
ARG
283
39.291
26.893
20.859
1.00
9.21


ATOM
1737
CA
ARG
283
38.113
26.179
20.379
1.00
10.93


ATOM
1738
CB
ARG
283
37.077
27.186
19.859
1.00
9.04


ATOM
1739
CG
ARG
283
35.802
26.566
19.293
1.00
7.71


ATOM
1740
CD
ARG
283
34.800
27.655
18.923
1.00
8.79


ATOM
1741
NE
ARG
283
35.371
28.597
17.966
1.00
8.59


ATOM
1742
CZ
ARG
283
34.837
29.773
17.651
1.00
12.17


ATOM
1743
NH1
ARG
283
33.702
30.174
18.219
1.00
8.02


ATOM
1744
NH2
ARG
283
35.445
30.552
16.763
1.00
9.21


ATOM
1745
C
ARG
283
38.520
25.191
19.268
1.00
11.88


ATOM
1746
O
ARG
283
38.026
24.065
19.210
1.00
11.57


ATOM
1747
N
ARG
284
39.432
25.615
18.396
1.00
12.83


ATOM
1748
CA
ARG
284
39.905
24.759
17.305
1.00
13.40


ATOM
1749
CB
ARG
284
40.815
25.557
16.362
1.00
12.91


ATOM
1750
CG
ARG
284
41.550
24.721
15.314
1.00
16.01


ATOM
1751
CD
ARG
284
40.608
24.122
14.274
1.00
14.55


ATOM
1752
NE
ARG
284
39.864
25.154
13.555
1.00
13.70


ATOM
1753
CZ
ARG
284
39.073
24.917
12.513
1.00
15.26


ATOM
1754
NH1
ARG
284
38.433
25.921
11.927
1.00
12.96


ATOM
1755
NH2
ARG
284
38.930
23.679
12.049
1.00
13.60


ATOM
1756
C
ARG
284
40.657
23.546
17.866
1.00
13.94


ATOM
1757
O
ARG
284
40.452
22.414
17.416
1.00
14.76


ATOM
1758
N
ALA
285
41.517
23.781
18.852
1.00
12.64


ATOM
1759
CA
ALA
285
42.277
22.698
19.468
1.00
12.04


ATOM
1760
CB
ALA
285
43.289
23.259
20.453
1.00
12.45


ATOM
1761
C
ALA
285
41.349
21.709
20.172
1.00
13.35


ATOM
1762
O
ALA
285
41.596
20.500
20.162
1.00
14.01


ATOM
1763
N
LEU
286
40.287
22.220
20.791
1.00
11.56


ATOM
1764
CA
LEU
286
39.330
21.356
21.478
1.00
12.33


ATOM
1765
CB
LEU
286
38.364
22.189
22.326
1.00
10.45


ATOM
1766
CG
LEU
286
38.952
22.846
23.583
1.00
13.14


ATOM
1767
CD1
LEU
286
37.884
23.713
24.255
1.00
11.79


ATOM
1768
CD2
LEU
286
39.452
21.767
24.548
1.00
9.81


ATOM
1769
C
LEU
286
38.553
20.529
20.453
1.00
11.97


ATOM
1770
O
LEU
286
38.225
19.368
20.693
1.00
12.10


ATOM
1771
N
HIS
287
38.257
21.146
19.315
1.00
12.58


ATOM
1772
CA
HIS
287
37.544
20.482
18.229
1.00
13.37


ATOM
1773
CB
HIS
287
37.351
21.476
17.073
1.00
13.36


ATOM
1774
CG
HIS
287
36.674
20.902
15.863
1.00
12.74


ATOM
1775
CD2
HIS
287
35.383
20.956
15.455
1.00
10.37


ATOM
1776
ND1
HIS
287
37.361
20.238
14.868
1.00
12.14


ATOM
1777
CE1
HIS
287
36.525
19.914
13.897
1.00
10.26


ATOM
1778
NE2
HIS
287
35.319
20.339
14.228
1.00
14.44


ATOM
1779
C
HIS
287
38.401
19.294
17.790
1.00
14.98


ATOM
1780
O
HIS
287
37.898
18.196
17.561
1.00
14.57


ATOM
1781
N
ARG
288
39.707
19.529
17.701
1.00
15.29


ATOM
1782
CA
ARG
288
40.666
18.506
17.305
1.00
17.69


ATOM
1783
CB
ARG
288
42.068
19.112
17.249
1.00
21.34


ATOM
1784
CG
ARG
288
42.685
19.208
15.862
1.00
27.31


ATOM
1785
CD
ARG
288
43.749
20.293
15.841
1.00
29.77


ATOM
1786
NE
ARG
288
44.569
20.250
17.048
1.00
29.56


ATOM
1787
CZ
ARG
288
45.157
21.311
17.586
1.00
29.93


ATOM
1788
NH1
ARG
288
45.019
22.505
17.021
1.00
30.44


ATOM
1789
NH2
ARG
288
45.874
21.183
18.696
1.00
31.11


ATOM
1790
C
ARG
288
40.674
17.329
18.276
1.00
17.37


ATOM
1791
O
ARG
288
40.713
16.169
17.861
1.00
16.21


ATOM
1792
N
HIS
289
40.629
17.629
19.571
1.00
17.16


ATOM
1793
CA
HIS
289
40.668
16.587
20.590
1.00
17.12


ATOM
1794
CB
HIS
289
41.281
17.132
21.882
1.00
18.15


ATOM
1795
CG
HIS
289
41.421
16.098
22.954
1.00
21.15


ATOM
1796
CD2
HIS
289
40.616
15.780
23.997
1.00
21.55


ATOM
1797
ND1
HIS
289
42.462
15.195
22.985
1.00
22.19


ATOM
1798
CE1
HIS
289
42.292
14.363
23.997
1.00
21.47


ATOM
1799
NE2
HIS
289
41.179
14.697
24.627
1.00
25.04


ATOM
1800
C
HIS
289
39.352
15.904
20.947
1.00
16.83


ATOM
1801
O
HIS
289
39.298
14.681
21.043
1.00
16.83


ATOM
1802
N
TYR
290
38.294
16.683
21.153
1.00
16.34


ATOM
1803
CA
TYR
290
37.016
16.110
21.549
1.00
15.13


ATOM
1804
CB
TYR
290
36.333
17.025
22.571
1.00
14.53


ATOM
1805
CG
TYR
290
37.073
17.093
23.894
1.00
14.22


ATOM
1806
CD1
TYR
290
37.842
18.208
24.237
1.00
12.56


ATOM
1807
CE1
TYR
290
38.547
18.255
25.445
1.00
12.09


ATOM
1808
CD2
TYR
290
37.025
16.026
24.791
1.00
13.17


ATOM
1809
CE2
TYR
290
37.721
16.062
25.995
1.00
13.22


ATOM
1810
CZ
TYR
290
38.480
17.175
26.316
1.00
14.11


ATOM
1811
OH
TYR
290
39.186
17.186
27.496
1.00
13.69


ATOM
1812
C
TYR
290
36.042
15.746
20.434
1.00
16.43


ATOM
1813
O
TYR
290
34.980
15.180
20.703
1.00
16.48


ATOM
1814
N
GLY
291
36.395
16.068
19.194
1.00
17.05


ATOM
1815
CA
GLY
291
35.535
15.730
18.072
1.00
15.48


ATOM
1816
C
GLY
291
34.611
16.813
17.552
1.00
13.32


ATOM
1817
O
GLY
291
34.111
17.647
18.305
1.00
11.67


ATOM
1818
N
ALA
292
34.369
16.781
16.248
1.00
13.25


ATOM
1819
CA
ALA
292
33.504
17.755
15.590
1.00
13.14


ATOM
1820
CB
ALA
292
33.530
17.532
14.077
1.00
15.01


ATOM
1821
C
ALA
292
32.065
17.708
16.099
1.00
13.40


ATOM
1822
O
ALA
292
31.362
18.713
16.056
1.00
12.55


ATOM
1823
N
GLN
293
31.625
16.545
16.575
1.00
12.64


ATOM
1824
CA
GLN
293
30.265
16.407
17.081
1.00
13.50


ATOM
1825
CB
GLN
293
29.888
14.919
17.199
1.00
13.51


ATOM
1826
CG
GLN
293
29.794
14.161
15.863
1.00
12.95


ATOM
1827
CD
GLN
293
28.496
14.423
15.109
1.00
14.29


ATOM
1828
OE1
GLN
293
27.607
15.121
15.597
1.00
13.82


ATOM
1829
NE2
GLN
293
28.382
13.853
13.909
1.00
12.74


ATOM
1830
C
GLN
293
30.071
17.091
18.436
1.00
14.40


ATOM
1831
O
GLN
293
28.938
17.278
18.879
1.00
15.91


ATOM
1832
N
HIS
294
31.168
17.487
19.081
1.00
13.64


ATOM
1833
CA
HIS
294
31.088
18.118
20.397
1.00
14.94


ATOM
1834
CB
HIS
294
31.831
17.248
21.413
1.00
14.73


ATOM
1835
CG
HIS
294
31.381
15.820
21.403
1.00
17.46


ATOM
1836
CD2
HIS
294
32.001
14.693
20.977
1.00
16.75


ATOM
1837
ND1
HIS
294
30.113
15.438
21.787
1.00
19.13


ATOM
1838
CE1
HIS
294
29.970
14.139
21.592
1.00
18.70


ATOM
1839
NE2
HIS
294
31.100
13.664
21.101
1.00
18.34


ATOM
1840
C
HIS
294
31.593
19.559
20.476
1.00
15.34


ATOM
1841
O
HIS
294
31.475
20.204
21.519
1.00
16.59


ATOM
1842
N
ILE
295
32.147
20.066
19.379
1.00
13.77


ATOM
1843
CA
ILE
295
32.654
21.435
19.352
1.00
13.59


ATOM
1844
CB
ILE
295
34.209
21.474
19.346
1.00
13.71


ATOM
1845
CG2
ILE
295
34.695
22.905
19.124
1.00
14.49


ATOM
1846
CG1
ILE
295
34.763
20.904
20.656
1.00
14.93


ATOM
1847
CD1
ILE
295
34.360
21.684
21.906
1.00
14.38


ATOM
1848
C
ILE
295
32.154
22.141
18.107
1.00
13.18


ATOM
1849
O
ILE
295
32.437
21.712
16.994
1.00
15.59


ATOM
1850
N
ASN
296
31.395
23.214
18.297
1.00
12.79


ATOM
1851
CA
ASN
296
30.878
23.992
17.175
1.00
13.84


ATOM
1852
CB
ASN
296
29.535
24.632
17.549
1.00
13.94


ATOM
1853
CG
ASN
296
28.943
25.462
16.419
1.00
17.67


ATOM
1854
OD1
ASN
296
29.597
25.724
15.408
1.00
16.28


ATOM
1855
ND2
ASN
296
27.700
25.890
16.595
1.00
20.03


ATOM
1856
C
ASN
296
31.917
25.076
16.897
1.00
13.19


ATOM
1857
O
ASN
296
32.123
25.966
17.724
1.00
13.14


ATOM
1858
N
LEU
297
32.570
25.001
15.742
1.00
12.09


ATOM
1859
CA
LEU
297
33.608
25.964
15.386
1.00
13.05


ATOM
1860
CB
LEU
297
34.308
25.528
14.097
1.00
14.01


ATOM
1861
CG
LEU
297
35.176
24.265
14.185
1.00
14.42


ATOM
1862
CD1
LEU
297
35.551
23.810
12.787
1.00
14.91


ATOM
1863
CD2
LEU
297
36.426
24.540
15.017
1.00
11.68


ATOM
1864
C
LEU
297
33.130
27.408
15.253
1.00
13.77


ATOM
1865
O
LEU
297
33.945
28.321
15.103
1.00
13.21


ATOM
1866
N
GLU
298
31.818
27.621
15.304
1.00
13.89


ATOM
1867
CA
GLU
298
31.275
28.975
15.210
1.00
16.15


ATOM
1868
CB
GLU
298
30.452
29.133
13.926
1.00
18.06


ATOM
1869
CG
GLU
298
31.227
28.791
12.659
1.00
23.45


ATOM
1870
CD
GLU
298
30.389
28.914
11.394
1.00
27.52


ATOM
1871
OE1
GLU
298
29.209
28.504
11.411
1.00
30.58


ATOM
1872
OE2
GLU
298
30.915
29.407
10.376
1.00
29.39


ATOM
1873
C
GLU
298
30.403
29.282
16.424
1.00
15.59


ATOM
1874
O
GLU
298
29.621
30.236
16.414
1.00
15.76


ATOM
1875
N
GLY
299
30.538
28.472
17.472
1.00
12.59


ATOM
1876
CA
GLY
299
29.732
28.683
18.659
1.00
11.43


ATOM
1877
C
GLY
299
30.514
28.756
19.956
1.00
12.49


ATOM
1878
O
GLY
299
31.749
28.812
19.945
1.00
12.02


ATOM
1879
N
PRO
300
29.815
28.762
21.104
1.00
11.77


ATOM
1880
CD
PRO
300
28.348
28.749
21.265
1.00
11.48


ATOM
1881
CA
PRO
300
30.484
28.829
22.406
1.00
12.78


ATOM
1882
CB
PRO
300
29.341
29.164
23.358
1.00
13.30


ATOM
1883
CG
PRO
300
28.183
28.440
22.741
1.00
13.51


ATOM
1884
C
PRO
300
31.176
27.513
22.761
1.00
13.23


ATOM
1885
O
PRO
300
30.857
26.465
22.204
1.00
11.48


ATOM
1886
N
ILE
301
32.118
27.581
23.693
1.00
12.03


ATOM
1887
CA
ILE
301
32.870
26.412
24.137
1.00
12.06


ATOM
1888
CB
ILE
301
34.329
26.807
24.481
1.00
12.23


ATOM
1889
CG2
ILE
301
35.087
25.601
25.038
1.00
11.68


ATOM
1890
CG1
ILE
301
35.017
27.390
23.241
1.00
11.62


ATOM
1891
CD1
ILE
301
36.392
27.983
23.521
1.00
9.44


ATOM
1892
C
ILE
301
32.236
25.807
25.388
1.00
12.04


ATOM
1893
O
ILE
301
31.880
26.535
26.318
1.00
10.31


ATOM
1894
N
PRO
302
32.066
24.469
25.421
1.00
11.07


ATOM
1895
CD
PRO
302
32.244
23.489
24.336
1.00
12.03


ATOM
1896
CA
PRO
302
31.472
23.833
26.602
1.00
11.31


ATOM
1897
CB
PRO
302
31.529
22.348
26.257
1.00
10.99


ATOM
1898
CG
PRO
302
31.324
22.358
24.774
1.00
12.05


ATOM
1899
C
PRO
302
32.319
24.201
27.826
1.00
9.53


ATOM
1900
O
PRO
302
33.537
24.067
27.809
1.00
9.50


ATOM
1901
N
ALA
303
31.655
24.657
28.879
1.00
10.56


ATOM
1902
CA
ALA
303
32.313
25.124
30.097
1.00
10.69


ATOM
1903
CB
ALA
303
31.274
25.775
31.005
1.00
8.77


ATOM
1904
C
ALA
303
33.164
24.162
30.914
1.00
11.62


ATOM
1905
O
ALA
303
33.903
24.603
31.792
1.00
10.65


ATOM
1906
N
HIS
304
33.084
22.863
30.644
1.00
12.09


ATOM
1907
CA
HIS
304
33.866
21.903
31.428
1.00
12.58


ATOM
1908
CB
HIS
304
33.017
20.657
31.721
1.00
11.82


ATOM
1909
CG
HIS
304
32.640
19.875
30.500
1.00
14.31


ATOM
1910
CD2
HIS
304
32.678
18.544
30.246
1.00
12.99


ATOM
1911
ND1
HIS
304
32.127
20.466
29.365
1.00
15.10


ATOM
1912
CE1
HIS
304
31.866
19.534
28.465
1.00
13.57


ATOM
1913
NE2
HIS
304
32.191
18.359
28.975
1.00
14.81


ATOM
1914
C
HIS
304
35.189
21.465
30.801
1.00
12.09


ATOM
1915
O
HIS
304
35.922
20.670
31.392
1.00
10.75


ATOM
1916
N
LEU
305
35.516
22.004
29.631
1.00
12.26


ATOM
1917
CA
LEU
305
36.728
21.590
28.924
1.00
11.26


ATOM
1918
CB
LEU
305
36.394
21.420
27.443
1.00
9.94


ATOM
1919
CG
LEU
305
35.159
20.564
27.149
1.00
10.57


ATOM
1920
CD1
LEU
305
34.896
20.538
25.642
1.00
10.40


ATOM
1921
CD2
LEU
305
35.377
19.153
27.697
1.00
9.11


ATOM
1922
C
LEU
305
37.968
22.466
29.043
1.00
12.64


ATOM
1923
O
LEU
305
38.973
22.197
28.380
1.00
12.19


ATOM
1924
N
LEU
306
37.922
23.490
29.889
1.00
13.29


ATOM
1925
CA
LEU
306
39.051
24.405
30.001
1.00
14.22


ATOM
1926
CB
LEU
306
38.537
25.846
30.141
1.00
11.93


ATOM
1927
CG
LEU
306
37.738
26.440
28.970
1.00
14.40


ATOM
1928
CD1
LEU
306
38.488
26.212
27.652
1.00
12.20


ATOM
1929
CD2
LEU
306
36.353
25.805
28.910
1.00
14.99


ATOM
1930
C
LEU
306
40.104
24.122
31.076
1.00
14.70


ATOM
1931
O
LEU
306
41.017
24.925
31.267
1.00
15.61


ATOM
1932
N
GLY
307
39.980
22.989
31.765
1.00
14.31


ATOM
1933
CA
GLY
307
40.955
22.613
32.777
1.00
12.37


ATOM
1934
C
GLY
307
40.767
23.242
34.145
1.00
14.30


ATOM
1935
O
GLY
307
41.596
23.064
35.045
1.00
12.62


ATOM
1936
N
ASN
308
39.668
23.967
34.307
1.00
11.75


ATOM
1937
CA
ASN
308
39.373
24.644
35.558
1.00
12.13


ATOM
1938
CB
ASN
308
39.906
26.086
35.480
1.00
10.17


ATOM
1939
CG
ASN
308
39.427
26.967
36.622
1.00
11.14


ATOM
1940
OD1
ASN
308
38.327
27.522
36.573
1.00
10.87


ATOM
1941
ND2
ASN
308
40.254
27.104
37.655
1.00
9.94


ATOM
1942
C
ASN
308
37.867
24.597
35.812
1.00
10.98


ATOM
1943
O
ASN
308
37.069
24.750
34.894
1.00
10.76


ATOM
1944
N
MET
309
37.493
24.369
37.066
1.00
10.81


ATOM
1945
CA
MET
309
36.094
24.255
37.453
1.00
11.22


ATOM
1946
CB
MET
309
35.984
24.189
38.984
1.00
12.08


ATOM
1947
CG
MET
309
34.568
23.932
39.491
1.00
12.10


ATOM
1948
SD
MET
309
33.855
22.420
38.792
1.00
12.04


ATOM
1949
CE
MET
309
34.496
21.188
39.955
1.00
12.99


ATOM
1950
C
MET
309
35.189
25.365
36.925
1.00
12.07


ATOM
1951
O
MET
309
34.038
25.110
36.562
1.00
11.18


ATOM
1952
N
TRP
310
35.709
26.588
36.877
1.00
10.53


ATOM
1953
CA
TRP
310
34.928
27.735
36.418
1.00
11.65


ATOM
1954
CB
TRP
310
35.020
28.856
37.456
1.00
10.85


ATOM
1955
CG
TRP
310
34.629
28.367
38.808
1.00
10.71


ATOM
1956
CD2
TRP
310
35.509
27.879
39.825
1.00
10.32


ATOM
1957
CE2
TRP
310
34.702
27.370
40.866
1.00
10.65


ATOM
1958
CE3
TRP
310
36.905
27.815
39.954
1.00
11.66


ATOM
1959
CD1
TRP
310
33.360
28.153
39.266
1.00
9.51


ATOM
1960
NE1
TRP
310
33.396
27.550
40.498
1.00
9.82


ATOM
1961
CZ2
TRP
310
35.243
26.805
42.028
1.00
10.04


ATOM
1962
CZ3
TRP
310
37.446
27.251
41.106
1.00
12.67


ATOM
1963
CH2
TRP
310
36.613
26.752
42.129
1.00
12.66


ATOM
1964
C
TRP
310
35.379
28.245
35.054
1.00
12.14


ATOM
1965
O
TRP
310
34.840
29.233
34.544
1.00
10.52


ATOM
1966
N
ALA
311
36.351
27.554
34.460
1.00
11.25


ATOM
1967
CA
ALA
311
36.890
27.949
33.166
1.00
11.45


ATOM
1968
CB
ALA
311
35.817
27.803
32.076
1.00
13.28


ATOM
1969
C
ALA
311
37.372
29.395
33.240
1.00
11.09


ATOM
1970
O
ALA
311
37.296
30.128
32.256
1.00
10.98


ATOM
1971
N
GLN
312
37.862
29.804
34.410
1.00
11.21


ATOM
1972
CA
GLN
312
38.346
31.168
34.594
1.00
10.89


ATOM
1973
CB
GLN
312
38.201
31.603
36.057
1.00
10.80


ATOM
1974
CG
GLN
312
39.053
30.838
37.052
1.00
11.00


ATOM
1975
CD
GLN
312
38.662
31.139
38.488
1.00
12.63


ATOM
1976
OE1
GLN
312
37.508
30.951
38.876
1.00
10.11


ATOM
1977
NE2
GLN
312
39.621
31.610
39.283
1.00
12.95


ATOM
1978
C
GLN
312
39.794
31.302
34.138
1.00
12.02


ATOM
1979
O
GLN
312
40.249
32.398
33.809
1.00
10.55


ATOM
1980
N
THR
313
40.510
30.182
34.141
1.00
12.20


ATOM
1981
CA
THR
313
41.898
30.117
33.687
1.00
13.97


ATOM
1982
CB
THR
313
42.914
30.108
34.859
1.00
15.24


ATOM
1983
OG1
THR
313
42.544
29.117
35.826
1.00
18.23


ATOM
1984
CG2
THR
313
42.951
31.468
35.527
1.00
19.92


ATOM
1985
C
THR
313
41.998
28.814
32.903
1.00
12.84


ATOM
1986
O
THR
313
41.464
27.790
33.328
1.00
11.11


ATOM
1987
N
TRP
314
42.660
28.864
31.751
1.00
12.37


ATOM
1988
CA
TRP
314
42.778
27.696
30.884
1.00
12.96


ATOM
1989
CB
TRP
314
42.357
28.060
29.464
1.00
12.27


ATOM
1990
CG
TRP
314
41.057
28.797
29.339
1.00
13.71


ATOM
1991
CD2
TRP
314
40.534
29.392
28.145
1.00
13.32


ATOM
1992
CE2
TRP
314
39.244
29.882
28.450
1.00
13.06


ATOM
1993
CE3
TRP
314
41.027
29.551
26.844
1.00
12.97


ATOM
1994
CD1
TRP
314
40.094
28.957
30.299
1.00
12.24


ATOM
1995
NE1
TRP
314
39.002
29.606
29.772
1.00
12.13


ATOM
1996
CZ2
TRP
314
38.442
30.519
27.502
1.00
12.07


ATOM
1997
CZ3
TRP
314
40.227
30.186
25.899
1.00
14.41


ATOM
1998
CH2
TRP
314
38.947
30.659
26.236
1.00
13.57


ATOM
1999
C
TRP
314
44.184
27.111
30.823
1.00
14.49


ATOM
2000
O
TRP
314
44.492
26.330
29.922
1.00
13.65


ATOM
2001
N
SER
315
45.029
27.489
31.775
1.00
15.57


ATOM
2002
CA
SER
315
46.414
27.021
31.818
1.00
16.96


ATOM
2003
CB
SER
315
47.093
27.539
33.091
1.00
18.01


ATOM
2004
OG
SER
315
46.977
28.947
33.186
1.00
26.11


ATOM
2005
C
SER
315
46.568
25.500
31.768
1.00
15.01


ATOM
2006
O
SER
315
47.487
24.980
31.135
1.00
12.81


ATOM
2007
N
ASN
316
45.663
24.794
32.434
1.00
15.19


ATOM
2008
CA
ASN
316
45.742
23.345
32.504
1.00
14.93


ATOM
2009
CB
ASN
316
44.837
22.849
33.632
1.00
16.81


ATOM
2010
CG
ASN
316
45.348
23.284
35.005
1.00
19.36


ATOM
2011
OD1
ASN
316
46.503
23.037
35.345
1.00
20.13


ATOM
2012
ND2
ASN
316
44.496
23.939
35.787
1.00
17.72


ATOM
2013
C
ASN
316
45.527
22.542
31.224
1.00
14.44


ATOM
2014
O
ASN
316
45.772
21.341
31.212
1.00
13.76


ATOM
2015
N
ILE
317
45.078
23.187
30.152
1.00
12.82


ATOM
2016
CA
ILE
317
44.925
22.476
28.883
1.00
13.82


ATOM
2017
CB
ILE
317
43.533
22.691
28.230
1.00
14.54


ATOM
2018
CG2
ILE
317
42.447
22.099
29.126
1.00
15.01


ATOM
2019
CG1
ILE
317
43.301
24.175
27.945
1.00
14.21


ATOM
2020
CD1
ILE
317
42.110
24.433
27.049
1.00
15.28


ATOM
2021
C
ILE
317
46.004
22.933
27.898
1.00
13.81


ATOM
2022
O
ILE
317
45.836
22.823
26.686
1.00
13.91


ATOM
2023
N
TYR
318
47.115
23.443
28.429
1.00
14.69


ATOM
2024
CA
TYR
318
48.228
23.899
27.595
1.00
16.96


ATOM
2025
CB
TYR
318
49.406
24.338
28.471
1.00
17.55


ATOM
2026
CG
TYR
318
50.637
24.733
27.682
1.00
20.39


ATOM
2027
CD1
TYR
318
50.690
25.942
26.995
1.00
19.75


ATOM
2028
CE1
TYR
318
51.802
26.290
26.233
1.00
22.32


ATOM
2029
CD2
TYR
318
51.734
23.875
27.590
1.00
21.99


ATOM
2030
CE2
TYR
318
52.850
24.212
26.831
1.00
23.31


ATOM
2031
CZ
TYR
318
52.878
25.421
26.157
1.00
23.13


ATOM
2032
OH
TYR
318
53.983
25.764
25.411
1.00
24.51


ATOM
2033
C
TYR
318
48.691
22.787
26.645
1.00
17.99


ATOM
2034
O
TYR
318
48.996
23.038
25.480
1.00
17.00


ATOM
2035
N
ASP
319
48.735
21.561
27.154
1.00
18.60


ATOM
2036
CA
ASP
319
49.157
20.403
26.369
1.00
21.85


ATOM
2037
CB
ASP
319
49.104
19.140
27.232
1.00
24.07


ATOM
2038
CG
ASP
319
47.724
18.888
27.806
1.00
29.24


ATOM
2039
OD1
ASP
319
47.207
19.781
28.507
1.00
34.33


ATOM
2040
OD2
ASP
319
47.149
17.805
27.558
1.00
33.51


ATOM
2041
C
ASP
319
48.298
20.192
25.122
1.00
21.74


ATOM
2042
O
ASP
319
48.768
19.645
24.124
1.00
20.42


ATOM
2043
N
LEU
320
47.041
20.622
25.180
1.00
19.73


ATOM
2044
CA
LEU
320
46.141
20.459
24.045
1.00
19.44


ATOM
2045
CB
LEU
320
44.684
20.371
24.523
1.00
19.37


ATOM
2046
CG
LEU
320
44.255
19.241
25.471
1.00
20.20


ATOM
2047
CD1
LEU
320
42.774
19.397
25.798
1.00
19.42


ATOM
2048
CD2
LEU
320
44.515
17.888
24.830
1.00
18.15


ATOM
2049
C
LEU
320
46.253
21.588
23.025
1.00
17.85


ATOM
2050
O
LEU
320
45.823
21.434
21.882
1.00
17.25


ATOM
2051
N
VAL
321
46.845
22.711
23.426
1.00
16.88


ATOM
2052
CA
VAL
321
46.944
23.864
22.531
1.00
17.25


ATOM
2053
CB
VAL
321
46.073
25.038
23.063
1.00
15.70


ATOM
2054
CG1
VAL
321
44.683
24.538
23.413
1.00
15.29


ATOM
2055
CG2
VAL
321
46.726
25.665
24.285
1.00
13.63


ATOM
2056
C
VAL
321
48.352
24.407
22.270
1.00
18.75


ATOM
2057
O
VAL
321
48.501
25.476
21.670
1.00
20.66


ATOM
2058
N
VAL
322
49.379
23.684
22.705
1.00
19.31


ATOM
2059
CA
VAL
322
50.752
24.145
22.514
1.00
20.26


ATOM
2060
CB
VAL
322
51.767
23.052
22.933
1.00
22.20


ATOM
2061
CG1
VAL
322
51.500
21.770
22.172
1.00
24.86


ATOM
2062
CG2
VAL
322
53.187
23.540
22.692
1.00
23.70


ATOM
2063
C
VAL
322
51.029
24.591
21.072
1.00
19.64


ATOM
2064
O
VAL
322
50.878
23.816
20.130
1.00
19.00


ATOM
2065
N
PRO
323
51.426
25.864
20.888
1.00
18.76


ATOM
2066
CD
PRO
323
51.505
26.903
21.931
1.00
17.26


ATOM
2067
CA
PRO
323
51.725
26.429
19.566
1.00
19.32


ATOM
2068
CB
PRO
323
52.142
27.863
19.890
1.00
19.18


ATOM
2069
CG
PRO
323
51.348
28.170
21.135
1.00
17.09


ATOM
2070
C
PRO
323
52.812
25.665
18.809
1.00
20.64


ATOM
2071
O
PRO
323
52.647
25.336
17.634
1.00
20.49


ATOM
2072
N
PHE
324
53.927
25.398
19.479
1.00
21.43


ATOM
2073
CA
PHE
324
55.019
24.660
18.854
1.00
22.71


ATOM
2074
CB
PHE
324
56.245
25.560
18.668
1.00
22.22


ATOM
2075
CG
PHE
324
55.991
26.751
17.789
1.00
20.95


ATOM
2076
CD1
PHE
324
55.631
27.977
18.339
1.00
20.89


ATOM
2077
CD2
PHE
324
56.088
26.642
16.408
1.00
20.89


ATOM
2078
CE1
PHE
324
55.371
29.073
17.526
1.00
21.44


ATOM
2079
CE2
PHE
324
55.829
27.734
15.586
1.00
20.48


ATOM
2080
CZ
PHE
324
55.471
28.951
16.144
1.00
20.58


ATOM
2081
C
PHE
324
55.376
23.458
19.712
1.00
23.69


ATOM
2082
O
PHE
324
56.267
23.526
20.557
1.00
21.84


ATOM
2083
N
PRO
325
54.670
22.334
19.505
1.00
26.08


ATOM
2084
CD
PRO
325
53.612
22.157
18.495
1.00
26.36


ATOM
2085
CA
PRO
325
54.888
21.091
20.251
1.00
28.73


ATOM
2086
CB
PRO
325
53.790
20.168
19.714
1.00
27.79


ATOM
2087
CG
PRO
325
53.588
20.660
18.319
1.00
27.78


ATOM
2088
C
PRO
325
56.290
20.500
20.110
1.00
30.60


ATOM
2089
O
PRO
325
56.732
19.732
20.968
1.00
30.52


ATOM
2090
N
SER
326
56.991
20.858
19.038
1.00
31.95


ATOM
2091
CA
SER
326
58.346
20.356
18.837
1.00
35.76


ATOM
2092
CB
SER
326
58.885
20.786
17.472
1.00
37.39


ATOM
2093
OG
SER
326
58.203
20.118
16.424
1.00
41.03


ATOM
2094
C
SER
326
59.261
20.883
19.940
1.00
36.95


ATOM
2095
O
SER
326
60.355
20.363
20.152
1.00
36.99


ATOM
2096
N
ALA
327
58.809
21.925
20.631
1.00
37.24


ATOM
2097
CA
ALA
327
59.575
22.517
21.720
1.00
38.79


ATOM
2098
CB
ALA
327
59.564
24.039
21.610
1.00
38.45


ATOM
2099
C
ALA
327
58.937
22.078
23.033
1.00
40.49


ATOM
2100
O
ALA
327
58.143
22.811
23.623
1.00
41.01


ATOM
2101
N
PRO
328
59.283
20.870
23.509
1.00
41.45


ATOM
2102
CD
PRO
328
60.341
19.988
22.982
1.00
41.86


ATOM
2103
CA
PRO
328
58.737
20.330
24.757
1.00
42.79


ATOM
2104
CB
PRO
328
59.317
18.919
24.799
1.00
42.30


ATOM
2105
CG
PRO
328
60.663
19.112
24.175
1.00
42.39


ATOM
2106
C
PRO
328
59.111
21.150
25.989
1.00
42.72


ATOM
2107
O
PRO
328
60.206
21.712
26.072
1.00
42.49


ATOM
2108
N
ALA
329
58.186
21.218
26.939
1.00
42.80


ATOM
2109
CA
ALA
329
58.410
21.954
28.173
1.00
43.32


ATOM
2110
CB
ALA
329
57.310
22.996
28.373
1.00
43.71


ATOM
2111
C
ALA
329
58.419
20.967
29.329
1.00
42.69


ATOM
2112
O
ALA
329
57.621
20.027
29.359
1.00
41.34


ATOM
2113
N
MET
330
59.325
21.173
30.278
1.00
42.76


ATOM
2114
CA
MET
330
59.417
20.288
31.425
1.00
42.98


ATOM
2115
CB
MET
330
60.525
20.743
32.372
1.00
44.14


ATOM
2116
CG
MET
330
61.873
20.155
32.054
1.00
45.52


ATOM
2117
SD
MET
330
63.030
20.380
33.396
1.00
50.91


ATOM
2118
CE
MET
330
62.368
19.255
34.608
1.00
49.99


ATOM
2119
C
MET
330
58.120
20.194
32.208
1.00
43.28


ATOM
2120
O
MET
330
57.295
21.109
32.194
1.00
44.37


ATOM
2121
N
ASP
331
57.951
19.068
32.889
1.00
42.06


ATOM
2122
CA
ASP
331
56.784
18.835
33.718
1.00
41.71


ATOM
2123
CB
ASP
331
56.652
17.339
34.010
1.00
43.19


ATOM
2124
CG
ASP
331
55.319
16.978
34.623
1.00
44.69


ATOM
2125
OD1
ASP
331
54.829
17.742
35.482
1.00
45.38


ATOM
2126
OD2
ASP
331
54.771
15.920
34.252
1.00
46.02


ATOM
2127
C
ASP
331
57.068
19.606
35.006
1.00
40.79


ATOM
2128
O
ASP
331
57.739
19.096
35.907
1.00
39.06


ATOM
2129
N
THR
332
56.581
20.842
35.077
1.00
39.46


ATOM
2130
CA
THR
332
56.817
21.678
36.247
1.00
39.60


ATOM
2131
CB
THR
332
56.132
23.054
36.106
1.00
40.44


ATOM
2132
OG1
THR
332
56.580
23.698
34.907
1.00
44.22


ATOM
2133
CG2
THR
332
56.497
23.963
37.287
1.00
43.44


ATOM
2134
C
THR
332
56.376
21.042
37.559
1.00
38.30


ATOM
2135
O
THR
332
57.120
21.075
38.537
1.00
37.12


ATOM
2136
N
THR
333
55.181
20.457
37.584
1.00
37.24


ATOM
2137
CA
THR
333
54.694
19.819
38.799
1.00
35.98


ATOM
2138
CB
THR
333
53.238
19.345
38.638
1.00
35.93


ATOM
2139
OG1
THR
333
52.384
20.485
38.467
1.00
35.53


ATOM
2140
CG2
THR
333
52.798
18.557
39.857
1.00
35.95


ATOM
2141
C
THR
333
55.584
18.628
39.139
1.00
35.83


ATOM
2142
O
THR
333
55.983
18.447
40.292
1.00
35.49


ATOM
2143
N
ALA
334
55.900
17.818
38.132
1.00
35.47


ATOM
2144
CA
ALA
334
56.753
16.652
38.338
1.00
34.53


ATOM
2145
CB
ALA
334
56.918
15.875
37.032
1.00
35.72


ATOM
2146
C
ALA
334
58.116
17.078
38.869
1.00
33.83


ATOM
2147
O
ALA
334
58.714
16.387
39.693
1.00
34.31


ATOM
2148
N
ALA
335
58.602
18.221
38.391
1.00
32.92


ATOM
2149
CA
ALA
335
59.897
18.745
38.818
1.00
31.60


ATOM
2150
CB
ALA
335
60.295
19.935
37.946
1.00
30.64


ATOM
2151
C
ALA
335
59.867
19.158
40.289
1.00
30.59


ATOM
2152
O
ALA
335
60.750
18.791
41.056
1.00
29.04


ATOM
2153
N
MET
336
58.848
19.919
40.680
1.00
31.65


ATOM
2154
CA
MET
336
58.720
20.361
42.069
1.00
33.03


ATOM
2155
CB
MET
336
57.454
21.205
42.242
1.00
31.27


ATOM
2156
CG
MET
336
57.523
22.564
41.568
1.00
29.31


ATOM
2157
SD
MET
336
55.990
23.505
41.708
1.00
26.33


ATOM
2158
CE
MET
336
56.044
23.993
43.446
1.00
23.57


ATOM
2159
C
MET
336
58.671
19.158
43.008
1.00
33.75


ATOM
2160
O
MET
336
59.380
19.104
44.015
1.00
32.69


ATOM
2161
N
LEU
337
57.828
18.190
42.665
1.00
36.37


ATOM
2162
CA
LEU
337
57.679
16.976
43.457
1.00
38.17


ATOM
2163
CB
LEU
337
56.509
16.148
42.921
1.00
38.76


ATOM
2164
CG
LEU
337
55.116
16.781
43.006
1.00
39.29


ATOM
2165
CD1
LEU
337
54.152
16.026
42.106
1.00
39.59


ATOM
2166
CD2
LEU
337
54.630
16.771
44.449
1.00
39.05


ATOM
2167
C
LEU
337
58.964
16.155
43.403
1.00
39.59


ATOM
2168
O
LEU
337
59.437
15.656
44.425
1.00
40.32


ATOM
2169
N
ALA
338
59.524
16.027
42.203
1.00
40.41


ATOM
2170
CA
ALA
338
60.750
15.267
41.994
1.00
41.35


ATOM
2171
CB
ALA
338
61.195
15.374
40.538
1.00
41.73


ATOM
2172
C
ALA
338
61.881
15.713
42.912
1.00
41.96


ATOM
2173
O
ALA
338
62.699
14.895
43.332
1.00
42.58


ATOM
2174
N
GLN
339
61.942
17.006
43.219
1.00
41.77


ATOM
2175
CA
GLN
339
63.000
17.490
44.094
1.00
40.98


ATOM
2176
CB
GLN
339
63.871
18.519
43.369
1.00
42.73


ATOM
2177
CG
GLN
339
63.134
19.520
42.516
1.00
44.71


ATOM
2178
CD
GLN
339
64.047
20.143
41.476
1.00
45.98


ATOM
2179
OE1
GLN
339
65.096
20.697
41.806
1.00
46.01


ATOM
2180
NE2
GLN
339
63.656
20.046
40.210
1.00
46.19


ATOM
2181
C
GLN
339
62.518
18.029
45.434
1.00
39.28


ATOM
2182
O
GLN
339
62.990
19.054
45.923
1.00
39.85


ATOM
2183
N
GLY
340
61.567
17.305
46.014
1.00
38.07


ATOM
2184
CA
GLY
340
61.023
17.625
47.322
1.00
35.18


ATOM
2185
C
GLY
340
60.537
19.011
47.696
1.00
33.08


ATOM
2186
O
GLY
340
60.742
19.433
48.834
1.00
32.07


ATOM
2187
N
TRP
341
59.905
19.731
46.775
1.00
31.21


ATOM
2188
CA
TRP
341
59.390
21.049
47.128
1.00
30.14


ATOM
2189
CB
TRP
341
58.899
21.808
45.887
1.00
29.67


ATOM
2190
CG
TRP
341
59.982
22.541
45.158
1.00
29.21


ATOM
2191
CD2
TRP
341
60.033
23.948
44.884
1.00
30.13


ATOM
2192
CE2
TRP
341
61.235
24.193
44.182
1.00
30.52


ATOM
2193
CE3
TRP
341
59.181
25.025
45.163
1.00
29.73


ATOM
2194
CD1
TRP
341
61.119
22.007
44.627
1.00
29.98


ATOM
2195
NE1
TRP
341
61.877
22.992
44.039
1.00
29.90


ATOM
2196
CZ2
TRP
341
61.608
25.474
43.754
1.00
29.27


ATOM
2197
CZ3
TRP
341
59.551
26.298
44.738
1.00
30.55


ATOM
2198
CH2
TRP
341
60.757
26.509
44.039
1.00
30.31


ATOM
2199
C
TRP
341
58.225
20.821
48.085
1.00
28.38


ATOM
2200
O
TRP
341
57.478
19.857
47.936
1.00
27.83


ATOM
2201
N
THR
342
58.086
21.695
49.075
1.00
27.38


ATOM
2202
CA
THR
342
57.001
21.583
50.045
1.00
26.99


ATOM
2203
CB
THR
342
57.527
21.284
51.463
1.00
26.84


ATOM
2204
OG1
THR
342
58.278
22.410
51.937
1.00
25.96


ATOM
2205
CG2
THR
342
58.416
20.046
51.458
1.00
27.25


ATOM
2206
C
THR
342
56.277
22.918
50.107
1.00
26.48


ATOM
2207
O
THR
342
56.784
23.926
49.622
1.00
25.97


ATOM
2208
N
PRO
343
55.075
22.942
50.702
1.00
25.99


ATOM
2209
CD
PRO
343
54.229
21.824
51.158
1.00
24.91


ATOM
2210
CA
PRO
343
54.352
24.211
50.787
1.00
25.66


ATOM
2211
CB
PRO
343
53.128
23.846
51.620
1.00
24.24


ATOM
2212
CG
PRO
343
52.849
22.444
51.163
1.00
23.75


ATOM
2213
C
PRO
343
55.214
25.287
51.446
1.00
25.07


ATOM
2214
O
PRO
343
55.196
26.446
51.036
1.00
24.95


ATOM
2215
N
ARG
344
55.981
24.897
52.460
1.00
25.30


ATOM
2216
CA
ARG
344
56.836
25.846
53.160
1.00
26.37


ATOM
2217
CB
ARG
344
57.483
25.189
54.383
1.00
29.20


ATOM
2218
CG
ARG
344
57.856
26.180
55.485
1.00
34.03


ATOM
2219
CD
ARG
344
58.585
25.495
56.634
1.00
38.59


ATOM
2220
NE
ARG
344
58.774
26.369
57.794
1.00
42.13


ATOM
2221
CZ
ARG
344
57.793
26.785
58.593
1.00
43.28


ATOM
2222
NH1
ARG
344
56.535
26.416
58.364
1.00
44.54


ATOM
2223
NH2
ARG
344
58.070
27.563
59.631
1.00
42.82


ATOM
2224
C
ARG
344
57.914
26.395
52.227
1.00
26.08


ATOM
2225
O
ARG
344
58.199
27.590
52.243
1.00
24.97


ATOM
2226
N
ARG
345
58.509
25.521
51.416
1.00
26.26


ATOM
2227
CA
ARG
345
59.542
25.944
50.468
1.00
26.55


ATOM
2228
CB
ARG
345
59.986
24.772
49.584
1.00
28.67


ATOM
2229
CG
ARG
345
61.485
24.491
49.595
1.00
35.65


ATOM
2230
CD
ARG
345
62.322
25.714
49.229
1.00
39.10


ATOM
2231
NE
ARG
345
62.669
25.799
47.808
1.00
43.47


ATOM
2232
CZ
ARG
345
63.388
24.894
47.149
1.00
43.78


ATOM
2233
NH1
ARG
345
63.840
23.814
47.771
1.00
45.20


ATOM
2234
NH2
ARG
345
63.681
25.079
45.870
1.00
45.37


ATOM
2235
C
ARG
345
58.948
27.020
49.573
1.00
24.15


ATOM
2236
O
ARG
345
59.558
28.063
49.330
1.00
23.46


ATOM
2237
N
MET
346
57.746
26.736
49.084
1.00
22.01


ATOM
2238
CA
MET
346
57.024
27.634
48.199
1.00
21.13


ATOM
2239
CB
MET
346
55.660
27.023
47.864
1.00
22.10


ATOM
2240
CG
MET
346
55.773
25.773
46.989
1.00
20.75


ATOM
2241
SD
MET
346
54.316
24.724
47.003
1.00
22.63


ATOM
2242
CE
MET
346
53.205
25.656
45.917
1.00
19.78


ATOM
2243
C
MET
346
56.869
29.039
48.775
1.00
19.41


ATOM
2244
O
MET
346
57.169
30.018
48.098
1.00
20.08


ATOM
2245
N
PHE
347
56.418
29.148
50.021
1.00
18.55


ATOM
2246
CA
PHE
347
56.260
30.469
50.621
1.00
19.25


ATOM
2247
CB
PHE
347
55.388
30.400
51.879
1.00
17.54


ATOM
2248
CG
PHE
347
53.931
30.168
51.587
1.00
16.26


ATOM
2249
CD1
PHE
347
53.434
28.882
51.430
1.00
14.65


ATOM
2250
CD2
PHE
347
53.064
31.244
51.421
1.00
16.74


ATOM
2251
CE1
PHE
347
52.091
28.669
51.109
1.00
17.04


ATOM
2252
CE2
PHE
347
51.721
31.041
51.100
1.00
15.45


ATOM
2253
CZ
PHE
347
51.236
29.754
50.942
1.00
13.62


ATOM
2254
C
PHE
347
57.607
31.109
50.938
1.00
19.50


ATOM
2255
O
PHE
347
57.733
32.334
50.931
1.00
19.74


ATOM
2256
N
LYS
348
58.612
30.281
51.212
1.00
19.37


ATOM
2257
CA
LYS
348
59.949
30.789
51.499
1.00
20.13


ATOM
2258
CB
LYS
348
60.871
29.653
51.964
1.00
23.49


ATOM
2259
CG
LYS
348
60.647
29.188
53.404
1.00
26.94


ATOM
2260
CD
LYS
348
61.173
30.215
54.405
1.00
30.04


ATOM
2261
CE
LYS
348
61.057
29.722
55.840
1.00
30.37


ATOM
2262
NZ
LYS
348
61.712
30.663
56.797
1.00
32.04


ATOM
2263
C
LYS
348
60.517
31.434
50.234
1.00
19.83


ATOM
2264
O
LYS
348
61.180
32.466
50.303
1.00
18.66


ATOM
2265
N
GLU
349
60.263
30.823
49.077
1.00
19.90


ATOM
2266
CA
GLU
349
60.746
31.383
47.817
1.00
19.84


ATOM
2267
CB
GLU
349
60.449
30.444
46.644
1.00
22.36


ATOM
2268
CG
GLU
349
61.320
29.196
46.568
1.00
26.40


ATOM
2269
CD
GLU
349
62.807
29.505
46.643
1.00
29.00


ATOM
2270
OE1
GLU
349
63.241
30.541
46.083
1.00
29.80


ATOM
2271
OE2
GLU
349
63.543
28.701
47.253
1.00
30.47


ATOM
2272
C
GLU
349
60.074
32.730
47.565
1.00
19.20


ATOM
2273
O
GLU
349
60.723
33.688
47.140
1.00
19.59


ATOM
2274
N
ALA
350
58.770
32.798
47.820
1.00
18.23


ATOM
2275
CA
ALA
350
58.016
34.035
47.633
1.00
17.72


ATOM
2276
CB
ALA
350
56.529
33.796
47.903
1.00
17.17


ATOM
2277
C
ALA
350
58.556
35.102
48.582
1.00
18.51


ATOM
2278
O
ALA
350
58.763
36.249
48.189
1.00
18.51


ATOM
2279
N
ASP
351
58.790
34.718
49.835
1.00
17.68


ATOM
2280
CA
ASP
351
59.316
35.653
50.823
1.00
17.98


ATOM
2281
CB
ASP
351
59.481
34.950
52.179
1.00
18.35


ATOM
2282
CG
ASP
351
59.841
35.912
53.306
1.00
21.38


ATOM
2283
OD1
ASP
351
59.094
36.886
53.542
1.00
21.06


ATOM
2284
OD2
ASP
351
60.871
35.688
53.972
1.00
23.40


ATOM
2285
C
ASP
351
60.658
36.193
50.322
1.00
17.98


ATOM
2286
O
ASP
351
60.945
37.386
50.449
1.00
16.96


ATOM
2287
N
ASP
352
61.468
35.312
49.733
1.00
17.61


ATOM
2288
CA
ASP
352
62.776
35.702
49.207
1.00
17.44


ATOM
2289
CB
ASP
352
63.544
34.464
48.718
1.00
16.88


ATOM
2290
CG
ASP
352
64.886
34.819
48.100
1.00
20.01


ATOM
2291
OD1
ASP
352
64.986
34.843
46.857
1.00
20.73


ATOM
2292
OD2
ASP
352
65.842
35.089
48.858
1.00
22.68


ATOM
2293
C
ASP
352
62.668
36.724
48.074
1.00
16.59


ATOM
2294
O
ASP
352
63.456
37.665
48.001
1.00
16.83


ATOM
2295
N
PHE
353
61.687
36.546
47.196
1.00
16.60


ATOM
2296
CA
PHE
353
61.516
37.481
46.094
1.00
15.67


ATOM
2297
CB
PHE
353
60.393
37.022
45.151
1.00
15.02


ATOM
2298
CG
PHE
353
60.498
37.599
43.760
1.00
13.85


ATOM
2299
CD1
PHE
353
60.633
36.766
42.655
1.00
15.98


ATOM
2300
CD2
PHE
353
60.491
38.977
43.558
1.00
14.55


ATOM
2301
CE1
PHE
353
60.763
37.292
41.363
1.00
13.57


ATOM
2302
CE2
PHE
353
60.622
39.515
42.272
1.00
15.24


ATOM
2303
CZ
PHE
353
60.759
38.668
41.173
1.00
14.14


ATOM
2304
C
PHE
353
61.212
38.874
46.647
1.00
14.39


ATOM
2305
O
PHE
353
61.808
39.863
46.212
1.00
15.75


ATOM
2306
N
PHE
354
60.301
38.964
47.612
1.00
14.89


ATOM
2307
CA
PHE
354
59.980
40.269
48.191
1.00
15.05


ATOM
2308
CB
PHE
354
58.864
40.149
49.238
1.00
14.19


ATOM
2309
CG
PHE
354
57.481
40.060
48.645
1.00
14.57


ATOM
2310
CD1
PHE
354
56.876
38.824
48.428
1.00
13.09


ATOM
2311
CD2
PHE
354
56.797
41.217
48.275
1.00
14.46


ATOM
2312
CE1
PHE
354
55.613
38.738
47.852
1.00
12.80


ATOM
2313
CE2
PHE
354
55.528
41.144
47.695
1.00
14.78


ATOM
2314
CZ
PHE
354
54.935
39.901
47.484
1.00
14.26


ATOM
2315
C
PHE
354
61.203
40.959
48.811
1.00
15.63


ATOM
2316
O
PHE
354
61.448
42.141
48.555
1.00
16.90


ATOM
2317
N
THR
355
61.973
40.233
49.620
1.00
17.16


ATOM
2318
CA
THR
355
63.155
40.824
50.243
1.00
17.44


ATOM
2319
CB
THR
355
63.798
39.887
51.306
1.00
19.33


ATOM
2320
OG1
THR
355
64.122
38.624
50.713
1.00
22.32


ATOM
2321
CG2
THR
355
62.845
39.675
52.476
1.00
19.21


ATOM
2322
C
THR
355
64.207
41.179
49.202
1.00
16.79


ATOM
2323
O
THR
355
64.968
42.130
49.387
1.00
17.18


ATOM
2324
N
SER
356
64.242
40.429
48.102
1.00
16.97


ATOM
2325
CA
SER
356
65.215
40.702
47.045
1.00
16.07


ATOM
2326
CB
SER
356
65.127
39.651
45.930
1.00
17.08


ATOM
2327
OG
SER
356
64.105
39.961
44.991
1.00
20.08


ATOM
2328
C
SER
356
64.942
42.087
46.471
1.00
17.25


ATOM
2329
O
SER
356
65.856
42.767
46.005
1.00
16.33


ATOM
2330
N
LEU
357
63.677
42.503
46.514
1.00
16.63


ATOM
2331
CA
LEU
357
63.282
43.817
46.013
1.00
17.17


ATOM
2332
CB
LEU
357
61.804
43.821
45.607
1.00
16.38


ATOM
2333
CG
LEU
357
61.378
42.907
44.458
1.00
16.10


ATOM
2334
CD1
LEU
357
59.897
43.117
44.185
1.00
16.24


ATOM
2335
CD2
LEU
357
62.202
43.212
43.211
1.00
13.65


ATOM
2336
C
LEU
357
63.496
44.875
47.087
1.00
16.00


ATOM
2337
O
LEU
357
63.228
46.057
46.872
1.00
16.89


ATOM
2338
N
GLY
358
63.978
44.445
48.246
1.00
15.89


ATOM
2339
CA
GLY
358
64.193
45.378
49.333
1.00
16.90


ATOM
2340
C
GLY
358
62.928
45.537
50.163
1.00
18.34


ATOM
2341
O
GLY
358
62.866
46.386
51.054
1.00
19.04


ATOM
2342
N
LEU
359
61.914
44.724
49.873
1.00
16.43


ATOM
2343
CA
LEU
359
60.663
44.790
50.618
1.00
17.52


ATOM
2344
CB
LEU
359
59.510
44.258
49.757
1.00
13.59


ATOM
2345
CG
LEU
359
59.299
45.099
48.487
1.00
14.94


ATOM
2346
CD1
LEU
359
58.221
44.490
47.588
1.00
12.02


ATOM
2347
CD2
LEU
359
58.928
46.518
48.893
1.00
13.39


ATOM
2348
C
LEU
359
60.786
44.014
51.938
1.00
18.75


ATOM
2349
O
LEU
359
61.807
43.369
52.194
1.00
18.11


ATOM
2350
N
LEU
360
59.744
44.078
52.763
1.00
17.60


ATOM
2351
CA
LEU
360
59.741
43.432
54.075
1.00
17.15


ATOM
2352
CB
LEU
360
58.661
44.064
54.958
1.00
16.43


ATOM
2353
CG
LEU
360
58.719
45.578
55.171
1.00
18.94


ATOM
2354
CD1
LEU
360
57.401
46.059
55.780
1.00
18.12


ATOM
2355
CD2
LEU
360
59.911
45.924
56.064
1.00
17.34


ATOM
2356
C
LEU
360
59.546
41.925
54.109
1.00
18.61


ATOM
2357
O
LEU
360
58.764
41.364
53.342
1.00
19.09


ATOM
2358
N
PRO
361
60.271
41.244
55.011
1.00
19.60


ATOM
2359
CD
PRO
361
61.405
41.728
55.824
1.00
19.10


ATOM
2360
CA
PRO
361
60.130
39.795
55.121
1.00
19.12


ATOM
2361
CB
PRO
361
61.461
39.368
55.730
1.00
20.18


ATOM
2362
CG
PRO
361
61.770
40.500
56.650
1.00
19.74


ATOM
2363
C
PRO
361
58.960
39.548
56.065
1.00
19.48


ATOM
2364
O
PRO
361
58.636
40.407
56.887
1.00
21.65


ATOM
2365
N
VAL
362
58.305
38.404
55.945
1.00
20.31


ATOM
2366
CA
VAL
362
57.202
38.123
56.855
1.00
21.83


ATOM
2367
CB
VAL
362
56.383
36.900
56.400
1.00
20.89


ATOM
2368
CG1
VAL
362
55.737
37.189
55.052
1.00
19.57


ATOM
2369
CG2
VAL
362
57.278
35.670
56.325
1.00
19.33


ATOM
2370
C
VAL
362
57.828
37.846
58.217
1.00
23.46


ATOM
2371
O
VAL
362
58.916
37.271
58.298
1.00
22.63


ATOM
2372
N
PRO
363
57.157
38.266
59.305
1.00
23.58


ATOM
2373
CD
PRO
363
55.924
39.073
59.315
1.00
23.83


ATOM
2374
CA
PRO
363
57.652
38.066
60.672
1.00
23.23


ATOM
2375
CB
PRO
363
56.602
38.777
61.529
1.00
23.92


ATOM
2376
CG
PRO
363
56.060
39.835
60.608
1.00
23.78


ATOM
2377
C
PRO
363
57.778
36.597
61.049
1.00
22.63


ATOM
2378
O
PRO
363
57.080
35.741
60.502
1.00
23.59


ATOM
2379
N
PRO
364
58.684
36.285
61.987
1.00
23.85


ATOM
2380
CD
PRO
364
59.645
37.186
62.654
1.00
23.46


ATOM
2381
CA
PRO
364
58.872
34.897
62.422
1.00
21.89


ATOM
2382
CB
PRO
364
59.831
35.039
63.603
1.00
23.26


ATOM
2383
CG
PRO
364
60.673
36.218
63.203
1.00
24.65


ATOM
2384
C
PRO
364
57.533
34.289
62.837
1.00
21.17


ATOM
2385
O
PRO
364
57.256
33.119
62.570
1.00
20.23


ATOM
2386
N
GLU
365
56.704
35.105
63.484
1.00
21.36


ATOM
2387
CA
GLU
365
55.388
34.681
63.957
1.00
22.68


ATOM
2388
CB
GLU
365
54.691
35.860
64.644
1.00
25.18


ATOM
2389
CG
GLU
365
53.265
35.599
65.084
1.00
27.55


ATOM
2390
CD
GLU
365
52.726
36.694
65.995
1.00
30.30


ATOM
2391
OE1
GLU
365
53.118
37.871
65.821
1.00
29.38


ATOM
2392
OE2
GLU
365
51.898
36.378
66.876
1.00
30.66


ATOM
2393
C
GLU
365
54.511
34.131
62.832
1.00
23.65


ATOM
2394
O
GLU
365
53.640
33.286
63.068
1.00
24.23


ATOM
2395
N
PHE
366
54.752
34.611
61.612
1.00
22.72


ATOM
2396
CA
PHE
366
54.007
34.179
60.428
1.00
20.44


ATOM
2397
CB
PHE
366
54.516
34.930
59.191
1.00
20.08


ATOM
2398
CG
PHE
366
53.982
34.397
57.880
1.00
19.61


ATOM
2399
CD1
PHE
366
52.811
34.911
57.326
1.00
19.02


ATOM
2400
CD2
PHE
366
54.665
33.395
57.192
1.00
18.91


ATOM
2401
CE1
PHE
366
52.327
34.438
56.106
1.00
17.67


ATOM
2402
CE2
PHE
366
54.191
32.913
55.968
1.00
19.81


ATOM
2403
CZ
PHE
366
53.020
33.436
55.424
1.00
18.45


ATOM
2404
C
PHE
366
54.161
32.681
60.196
1.00
20.36


ATOM
2405
O
PHE
366
53.182
31.968
59.962
1.00
20.59


ATOM
2406
N
TRP
367
55.398
32.207
60.252
1.00
21.17


ATOM
2407
CA
TRP
367
55.680
30.792
60.033
1.00
23.44


ATOM
2408
CB
TRP
367
57.193
30.571
59.936
1.00
23.71


ATOM
2409
CG
TRP
367
57.837
31.400
58.866
1.00
23.03


ATOM
2410
CD2
TRP
367
57.716
31.214
57.450
1.00
21.94


ATOM
2411
CE2
TRP
367
58.454
32.244
56.828
1.00
20.04


ATOM
2412
CE3
TRP
367
57.053
30.276
56.646
1.00
21.24


ATOM
2413
CD1
TRP
367
58.620
32.503
59.041
1.00
22.06


ATOM
2414
NE1
TRP
367
58.995
33.017
57.822
1.00
22.15


ATOM
2415
CZ2
TRP
367
58.552
32.364
55.437
1.00
21.91


ATOM
2416
CZ3
TRP
367
57.149
30.394
55.260
1.00
22.47


ATOM
2417
CH2
TRP
367
57.894
31.434
54.672
1.00
21.53


ATOM
2418
C
TRP
367
55.096
29.898
61.124
1.00
25.38


ATOM
2419
O
TRP
367
54.753
28.741
60.877
1.00
26.15


ATOM
2420
N
ASN
368
54.965
30.445
62.325
1.00
26.99


ATOM
2421
CA
ASN
368
54.439
29.683
63.446
1.00
29.40


ATOM
2422
CB
ASN
368
54.971
30.277
64.754
1.00
32.59


ATOM
2423
CG
ASN
368
54.447
29.558
65.979
1.00
36.43


ATOM
2424
OD1
ASN
368
53.351
29.842
66.458
1.00
38.69


ATOM
2425
ND2
ASN
368
55.229
28.610
66.489
1.00
39.13


ATOM
2426
C
ASN
368
52.911
29.593
63.493
1.00
29.33


ATOM
2427
O
ASN
368
52.361
28.559
63.878
1.00
28.62


ATOM
2428
N
LYS
369
52.224
30.655
63.082
1.00
27.34


ATOM
2429
CA
LYS
369
50.766
30.664
63.134
1.00
26.72


ATOM
2430
CB
LYS
369
50.286
31.988
63.734
1.00
28.17


ATOM
2431
CG
LYS
369
50.778
32.222
65.163
1.00
30.11


ATOM
2432
CD
LYS
369
50.173
33.486
65.756
1.00
33.96


ATOM
2433
CE
LYS
369
50.598
33.679
67.206
1.00
36.40


ATOM
2434
NZ
LYS
369
49.966
34.897
67.802
1.00
39.20


ATOM
2435
C
LYS
369
50.013
30.392
61.833
1.00
26.02


ATOM
2436
O
LYS
369
48.821
30.084
61.864
1.00
25.69


ATOM
2437
N
SER
370
50.689
30.503
60.696
1.00
23.45


ATOM
2438
CA
SER
370
50.021
30.262
59.421
1.00
23.37


ATOM
2439
CB
SER
370
50.897
30.732
58.249
1.00
21.85


ATOM
2440
OG
SER
370
51.005
32.143
58.202
1.00
19.18


ATOM
2441
C
SER
370
49.668
28.792
59.214
1.00
23.22


ATOM
2442
O
SER
370
50.301
27.901
59.777
1.00
23.81


ATOM
2443
N
MET
371
48.639
28.549
58.411
1.00
23.49


ATOM
2444
CA
MET
371
48.224
27.193
58.083
1.00
24.10


ATOM
2445
CB
MET
371
46.730
26.991
58.349
1.00
23.79


ATOM
2446
CG
MET
371
46.260
25.564
58.100
1.00
23.95


ATOM
2447
SD
MET
371
44.475
25.392
57.941
1.00
26.45


ATOM
2448
CE
MET
371
44.296
25.509
56.167
1.00
26.30


ATOM
2449
C
MET
371
48.506
27.061
56.588
1.00
24.40


ATOM
2450
O
MET
371
47.671
27.417
55.755
1.00
24.50


ATOM
2451
N
LEU
372
49.691
26.559
56.257
1.00
25.00


ATOM
2452
CA
LEU
372
50.099
26.409
54.865
1.00
25.46


ATOM
2453
CB
LEU
372
51.599
26.684
54.743
1.00
23.72


ATOM
2454
CG
LEU
372
52.070
27.996
55.382
1.00
24.19


ATOM
2455
CD1
LEU
372
53.581
28.097
55.296
1.00
23.40


ATOM
2456
CD2
LEU
372
51.408
29.184
54.688
1.00
22.75


ATOM
2457
C
LEU
372
49.770
25.044
54.267
1.00
26.72


ATOM
2458
O
LEU
372
49.995
24.815
53.080
1.00
27.70


ATOM
2459
N
GLU
373
49.238
24.141
55.086
1.00
27.93


ATOM
2460
CA
GLU
373
48.879
22.803
54.620
1.00
29.95


ATOM
2461
CB
GLU
373
49.850
21.750
55.164
1.00
32.89


ATOM
2462
CG
GLU
373
51.281
21.859
54.689
1.00
38.75


ATOM
2463
CD
GLU
373
52.099
20.640
55.086
1.00
42.30


ATOM
2464
OE1
GLU
373
52.259
20.397
56.302
1.00
44.27


ATOM
2465
OE2
GLU
373
52.573
19.918
54.181
1.00
43.48


ATOM
2466
C
GLU
373
47.483
22.425
55.084
1.00
29.73


ATOM
2467
O
GLU
373
47.011
22.899
56.115
1.00
30.00


ATOM
2468
N
LYS
374
46.824
21.562
54.324
1.00
29.28


ATOM
2469
CA
LYS
374
45.497
21.107
54.699
1.00
30.95


ATOM
2470
CB
LYS
374
44.889
20.253
53.586
1.00
31.28


ATOM
2471
CG
LYS
374
43.444
19.847
53.822
1.00
31.52


ATOM
2472
CD
LYS
374
42.926
19.049
52.631
1.00
33.34


ATOM
2473
CE
LYS
374
41.415
19.128
52.514
1.00
33.68


ATOM
2474
NZ
LYS
374
40.933
18.533
51.235
1.00
33.80


ATOM
2475
C
LYS
374
45.697
20.256
55.944
1.00
32.17


ATOM
2476
O
LYS
374
46.520
19.342
55.948
1.00
32.16


ATOM
2477
N
PRO
375
44.975
20.567
57.030
1.00
33.39


ATOM
2478
CD
PRO
375
44.183
21.784
57.276
1.00
33.07


ATOM
2479
CA
PRO
375
45.120
19.785
58.261
1.00
34.99


ATOM
2480
CB
PRO
375
44.196
20.512
59.236
1.00
34.90


ATOM
2481
CG
PRO
375
44.299
21.933
58.777
1.00
33.52


ATOM
2482
C
PRO
375
44.724
18.323
58.064
1.00
35.62


ATOM
2483
O
PRO
375
43.812
18.013
57.296
1.00
34.22


ATOM
2484
N
THR
376
45.421
17.428
58.755
1.00
37.71


ATOM
2485
CA
THR
376
45.138
16.000
58.665
1.00
39.65


ATOM
2486
CB
THR
376
46.308
15.233
58.009
1.00
39.07


ATOM
2487
OG1
THR
376
47.491
15.390
58.804
1.00
38.66


ATOM
2488
CG2
THR
376
46.575
15.762
56.608
1.00
39.31


ATOM
2489
C
THR
376
44.906
15.439
60.063
1.00
41.67


ATOM
2490
O
THR
376
45.345
14.333
60.379
1.00
42.78


ATOM
2491
N
ASP
377
44.221
16.211
60.900
1.00
42.52


ATOM
2492
CA
ASP
377
43.946
15.781
62.264
1.00
43.25


ATOM
2493
CB
ASP
377
44.579
16.748
63.272
1.00
44.11


ATOM
2494
CG
ASP
377
44.103
18.181
63.093
1.00
44.64


ATOM
2495
OD1
ASP
377
42.879
18.394
62.984
1.00
43.68


ATOM
2496
OD2
ASP
377
44.955
19.095
63.072
1.00
44.31


ATOM
2497
C
ASP
377
42.455
15.649
62.549
1.00
43.56


ATOM
2498
O
ASP
377
42.031
15.714
63.703
1.00
43.97


ATOM
2499
N
GLY
378
41.664
15.473
61.496
1.00
43.76


ATOM
2500
CA
GLY
378
40.234
15.313
61.674
1.00
45.10


ATOM
2501
C
GLY
378
39.389
16.574
61.613
1.00
45.20


ATOM
2502
O
GLY
378
38.160
16.480
61.553
1.00
46.83


ATOM
2503
N
ARG
379
40.018
17.747
61.629
1.00
43.58


ATOM
2504
CA
ARG
379
39.248
18.985
61.569
1.00
41.75


ATOM
2505
CB
ARG
379
39.902
20.086
62.417
1.00
41.40


ATOM
2506
CG
ARG
379
41.307
20.489
62.025
1.00
41.01


ATOM
2507
CD
ARG
379
41.892
21.409
63.091
1.00
40.32


ATOM
2508
NE
ARG
379
43.352
21.472
63.049
1.00
42.06


ATOM
2509
CZ
ARG
379
44.051
22.421
62.435
1.00
42.42


ATOM
2510
NH1
ARG
379
43.431
23.409
61.801
1.00
42.84


ATOM
2511
NH2
ARG
379
45.376
22.384
62.456
1.00
42.41


ATOM
2512
C
ARG
379
39.017
19.488
60.150
1.00
39.88


ATOM
2513
O
ARG
379
39.884
19.385
59.284
1.00
39.95


ATOM
2514
N
GLU
380
37.819
20.015
59.927
1.00
37.75


ATOM
2515
CA
GLU
380
37.424
20.552
58.635
1.00
35.59


ATOM
2516
CB
GLU
380
35.913
20.375
58.456
1.00
38.09


ATOM
2517
CG
GLU
380
35.383
20.691
57.068
1.00
42.10


ATOM
2518
CD
GLU
380
34.658
19.508
56.444
1.00
43.64


ATOM
2519
OE1
GLU
380
33.789
18.911
57.120
1.00
45.08


ATOM
2520
OE2
GLU
380
34.951
19.179
55.277
1.00
43.23


ATOM
2521
C
GLU
380
37.793
22.034
58.633
1.00
31.78


ATOM
2522
O
GLU
380
37.679
22.705
59.659
1.00
28.75


ATOM
2523
N
VAL
381
38.241
22.545
57.492
1.00
29.15


ATOM
2524
CA
VAL
381
38.630
23.950
57.404
1.00
26.32


ATOM
2525
CB
VAL
381
40.169
24.112
57.499
1.00
24.57


ATOM
2526
CG1
VAL
381
40.705
23.390
58.726
1.00
25.23


ATOM
2527
CG2
VAL
381
40.824
23.560
56.247
1.00
25.89


ATOM
2528
C
VAL
381
38.185
24.577
56.090
1.00
24.82


ATOM
2529
O
VAL
381
37.661
23.896
55.208
1.00
24.94


ATOM
2530
N
VAL
382
38.383
25.887
55.975
1.00
23.19


ATOM
2531
CA
VAL
382
38.070
26.602
54.744
1.00
21.67


ATOM
2532
CB
VAL
382
37.674
28.073
54.999
1.00
21.80


ATOM
2533
CG1
VAL
382
37.563
28.811
53.674
1.00
20.55


ATOM
2534
CG2
VAL
382
36.348
28.145
55.744
1.00
21.77


ATOM
2535
C
VAL
382
39.401
26.582
54.006
1.00
21.54


ATOM
2536
O
VAL
382
40.341
27.267
54.402
1.00
20.36


ATOM
2537
N
CYS
383
39.492
25.779
52.953
1.00
21.15


ATOM
2538
CA
CYS
383
40.734
25.676
52.203
1.00
21.33


ATOM
2539
C
CYS
383
41.071
26.872
51.324
1.00
20.79


ATOM
2540
O
CYS
383
42.241
27.238
51.206
1.00
21.41


ATOM
2541
CB
CYS
383
40.730
24.407
51.351
1.00
21.86


ATOM
2542
SG
CYS
383
41.329
22.923
52.225
1.00
23.08


ATOM
2543
N
HIS
384
40.055
27.482
50.716
1.00
19.24


ATOM
2544
CA
HIS
384
40.269
28.628
49.829
1.00
17.16


ATOM
2545
CB
HIS
384
38.957
29.376
49.584
1.00
13.14


ATOM
2546
CG
HIS
384
39.027
30.345
48.447
1.00
13.04


ATOM
2547
CD2
HIS
384
39.476
31.621
48.390
1.00
11.87


ATOM
2548
ND1
HIS
384
38.665
30.009
47.159
1.00
12.76


ATOM
2549
CE1
HIS
384
38.888
31.036
46.360
1.00
14.29


ATOM
2550
NE2
HIS
384
39.381
32.028
47.081
1.00
15.54


ATOM
2551
C
HIS
384
41.307
29.602
50.388
1.00
17.15


ATOM
2552
O
HIS
384
41.058
30.293
51.375
1.00
18.56


ATOM
2553
N
ALA
385
42.465
29.653
49.738
1.00
15.37


ATOM
2554
CA
ALA
385
43.573
30.514
50.152
1.00
15.12


ATOM
2555
CB
ALA
385
44.663
30.492
49.081
1.00
12.93


ATOM
2556
C
ALA
385
43.216
31.965
50.478
1.00
13.38


ATOM
2557
O
ALA
385
42.495
32.626
49.733
1.00
13.27


ATOM
2558
N
SER
386
43.739
32.456
51.596
1.00
12.79


ATOM
2559
CA
SER
386
43.508
33.837
52.003
1.00
13.42


ATOM
2560
CB
SER
386
42.123
33.988
52.651
1.00
12.99


ATOM
2561
OG
SER
386
41.970
33.130
53.765
1.00
14.28


ATOM
2562
C
SER
386
44.602
34.324
52.954
1.00
13.14


ATOM
2563
O
SER
386
45.263
33.525
53.629
1.00
12.93


ATOM
2564
N
ALA
387
44.800
35.640
52.979
1.00
13.15


ATOM
2565
CA
ALA
387
45.803
36.280
53.825
1.00
13.29


ATOM
2566
CB
ALA
387
46.653
37.239
53.003
1.00
13.06


ATOM
2567
C
ALA
387
45.064
37.033
54.920
1.00
14.39


ATOM
2568
O
ALA
387
44.017
37.637
54.672
1.00
15.15


ATOM
2569
N
TRP
388
45.621
37.014
56.124
1.00
14.45


ATOM
2570
CA
TRP
388
44.981
37.641
57.272
1.00
15.44


ATOM
2571
CB
TRP
388
44.559
36.547
58.263
1.00
15.81


ATOM
2572
CG
TRP
388
43.575
35.556
57.707
1.00
15.75


ATOM
2573
CD2
TRP
388
42.297
35.219
58.261
1.00
17.72


ATOM
2574
CE2
TRP
388
41.716
34.241
57.416
1.00
17.38


ATOM
2575
CE3
TRP
388
41.584
35.649
59.391
1.00
18.07


ATOM
2576
CD1
TRP
388
43.717
34.789
56.581
1.00
16.55


ATOM
2577
NE1
TRP
388
42.602
33.997
56.400
1.00
15.73


ATOM
2578
CZ2
TRP
388
40.454
33.687
57.668
1.00
18.71


ATOM
2579
CZ3
TRP
388
40.327
35.095
59.642
1.00
19.40


ATOM
2580
CH2
TRP
388
39.777
34.125
58.782
1.00
18.61


ATOM
2581
C
TRP
388
45.805
38.692
58.014
1.00
17.06


ATOM
2582
O
TRP
388
46.989
38.499
58.298
1.00
17.43


ATOM
2583
N
ASP
389
45.152
39.807
58.328
1.00
16.13


ATOM
2584
CA
ASP
389
45.764
40.900
59.073
1.00
17.75


ATOM
2585
CB
ASP
389
45.501
42.231
58.365
1.00
17.00


ATOM
2586
CG
ASP
389
46.187
43.399
59.041
1.00
16.49


ATOM
2587
OD1
ASP
389
46.524
43.285
60.239
1.00
18.76


ATOM
2588
OD2
ASP
389
46.382
44.436
58.376
1.00
14.01


ATOM
2589
C
ASP
389
45.054
40.888
60.433
1.00
19.06


ATOM
2590
O
ASP
389
43.828
41.011
60.488
1.00
19.40


ATOM
2591
N
PHE
390
45.805
40.726
61.520
1.00
18.93


ATOM
2592
CA
PHE
390
45.189
40.686
62.846
1.00
22.25


ATOM
2593
CB
PHE
390
45.850
39.603
63.709
1.00
21.51


ATOM
2594
CG
PHE
390
45.477
38.208
63.294
1.00
23.36


ATOM
2595
CD1
PHE
390
45.997
37.655
62.125
1.00
21.45


ATOM
2596
CD2
PHE
390
44.547
37.475
64.027
1.00
22.78


ATOM
2597
CE1
PHE
390
45.595
36.395
61.687
1.00
23.06


ATOM
2598
CE2
PHE
390
44.136
36.214
63.599
1.00
25.87


ATOM
2599
CZ
PHE
390
44.661
35.671
62.424
1.00
24.50


ATOM
2600
C
PHE
390
45.170
42.026
63.573
1.00
23.40


ATOM
2601
O
PHE
390
44.937
42.096
64.785
1.00
21.79


ATOM
2602
N
TYR
391
45.407
43.079
62.799
1.00
24.34


ATOM
2603
CA
TYR
391
45.399
44.468
63.253
1.00
26.72


ATOM
2604
CB
TYR
391
43.957
44.944
63.445
1.00
29.46


ATOM
2605
CG
TYR
391
43.030
44.570
62.312
1.00
32.43


ATOM
2606
CD1
TYR
391
42.389
43.336
62.297
1.00
34.89


ATOM
2607
CE1
TYR
391
41.537
42.978
61.262
1.00
37.09


ATOM
2608
CD2
TYR
391
42.801
45.445
61.252
1.00
35.38


ATOM
2609
CE2
TYR
391
41.951
45.095
60.204
1.00
37.31


ATOM
2610
CZ
TYR
391
41.321
43.860
60.221
1.00
37.51


ATOM
2611
OH
TYR
391
40.457
43.505
59.212
1.00
41.58


ATOM
2612
C
TYR
391
46.205
44.861
64.487
1.00
25.67


ATOM
2613
O
TYR
391
45.776
45.725
65.247
1.00
27.20


ATOM
2614
N
ASN
392
47.360
44.243
64.696
1.00
24.64


ATOM
2615
CA
ASN
392
48.200
44.613
65.829
1.00
24.09


ATOM
2616
CB
ASN
392
48.261
43.492
66.881
1.00
23.53


ATOM
2617
CG
ASN
392
48.960
42.241
66.380
1.00
22.41


ATOM
2618
OD1
ASN
392
49.428
42.181
65.247
1.00
21.54


ATOM
2619
ND2
ASN
392
49.032
41.229
67.236
1.00
23.26


ATOM
2620
C
ASN
392
49.592
44.930
65.295
1.00
24.22


ATOM
2621
O
ASN
392
50.548
45.073
66.055
1.00
23.88


ATOM
2622
N
GLY
393
49.679
45.040
63.969
1.00
22.80


ATOM
2623
CA
GLY
393
50.934
45.353
63.311
1.00
20.67


ATOM
2624
C
GLY
393
52.025
44.319
63.515
1.00
21.15


ATOM
2625
O
GLY
393
53.178
44.560
63.170
1.00
20.78


ATOM
2626
N
LYS
394
51.666
43.156
64.048
1.00
20.82


ATOM
2627
CA
LYS
394
52.657
42.118
64.308
1.00
22.60


ATOM
2628
CB
LYS
394
52.909
42.024
65.818
1.00
24.94


ATOM
2629
CG
LYS
394
54.363
42.153
66.216
1.00
30.63


ATOM
2630
CD
LYS
394
54.916
43.524
65.854
1.00
33.49


ATOM
2631
CE
LYS
394
54.355
44.606
66.757
1.00
35.47


ATOM
2632
NZ
LYS
394
54.708
44.359
68.185
1.00
37.56


ATOM
2633
C
LYS
394
52.253
40.745
63.789
1.00
21.67


ATOM
2634
O
LYS
394
53.079
40.001
63.261
1.00
22.03


ATOM
2635
N
ASP
395
50.973
40.427
63.940
1.00
21.32


ATOM
2636
CA
ASP
395
50.425
39.134
63.553
1.00
20.91


ATOM
2637
CB
ASP
395
49.440
38.689
64.642
1.00
19.12


ATOM
2638
CG
ASP
395
49.053
37.227
64.534
1.00
19.78


ATOM
2639
OD1
ASP
395
49.344
36.589
63.501
1.00
20.54


ATOM
2640
OD2
ASP
395
48.438
36.715
65.495
1.00
21.66


ATOM
2641
C
ASP
395
49.737
39.110
62.178
1.00
21.80


ATOM
2642
O
ASP
395
48.651
39.670
62.001
1.00
20.60


ATOM
2643
N
PHE
396
50.378
38.454
61.213
1.00
20.77


ATOM
2644
CA
PHE
396
49.830
38.312
59.863
1.00
20.20


ATOM
2645
CB
PHE
396
50.634
39.132
58.849
1.00
19.48


ATOM
2646
CG
PHE
396
51.005
40.501
59.330
1.00
19.47


ATOM
2647
CD1
PHE
396
52.212
40.715
59.987
1.00
18.23


ATOM
2648
CD2
PHE
396
50.149
41.580
59.127
1.00
19.80


ATOM
2649
CE1
PHE
396
52.564
41.989
60.436
1.00
16.62


ATOM
2650
CE2
PHE
396
50.492
42.855
59.572
1.00
18.16


ATOM
2651
CZ
PHE
396
51.703
43.059
60.228
1.00
18.20


ATOM
2652
C
PHE
396
49.945
36.832
59.514
1.00
19.88


ATOM
2653
O
PHE
396
50.942
36.193
59.847
1.00
22.26


ATOM
2654
N
ARG
397
48.945
36.281
58.840
1.00
19.00


ATOM
2655
CA
ARG
397
48.989
34.864
58.502
1.00
18.47


ATOM
2656
CB
ARG
397
48.286
34.037
59.579
1.00
19.59


ATOM
2657
CG
ARG
397
48.542
34.466
61.009
1.00
19.93


ATOM
2658
CD
ARG
397
47.667
33.642
61.944
1.00
20.65


ATOM
2659
NE
ARG
397
47.588
34.223
63.280
1.00
23.90


ATOM
2660
CZ
ARG
397
46.806
33.759
64.250
1.00
24.44


ATOM
2661
NH1
ARG
397
46.033
32.702
64.033
1.00
25.15


ATOM
2662
NH2
ARG
397
46.792
34.358
65.434
1.00
25.23


ATOM
2663
C
ARG
397
48.327
34.526
57.179
1.00
18.41


ATOM
2664
O
ARG
397
47.504
35.279
56.661
1.00
16.23


ATOM
2665
N
ILE
398
48.683
33.359
56.653
1.00
17.80


ATOM
2666
CA
ILE
398
48.098
32.867
55.419
1.00
17.44


ATOM
2667
CB
ILE
398
49.172
32.720
54.310
1.00
17.61


ATOM
2668
CG2
ILE
398
48.685
31.774
53.217
1.00
18.45


ATOM
2669
CG1
ILE
398
49.498
34.107
53.734
1.00
16.21


ATOM
2670
CD1
ILE
398
50.554
34.110
52.628
1.00
14.34


ATOM
2671
C
ILE
398
47.437
31.524
55.724
1.00
17.31


ATOM
2672
O
ILE
398
47.964
30.723
56.502
1.00
17.20


ATOM
2673
N
LYS
399
46.260
31.310
55.145
1.00
16.54


ATOM
2674
CA
LYS
399
45.506
30.074
55.326
1.00
17.03


ATOM
2675
CB
LYS
399
44.152
30.355
55.984
1.00
16.41


ATOM
2676
CG
LYS
399
43.323
29.102
56.237
1.00
16.93


ATOM
2677
CD
LYS
399
41.871
29.433
56.562
1.00
18.85


ATOM
2678
CE
LYS
399
41.218
30.234
55.439
1.00
19.45


ATOM
2679
NZ
LYS
399
41.423
29.599
54.106
1.00
18.46


ATOM
2680
C
LYS
399
45.294
29.498
53.934
1.00
18.35


ATOM
2681
O
LYS
399
44.492
30.013
53.149
1.00
17.47


ATOM
2682
N
GLN
400
46.010
28.421
53.633
1.00
18.80


ATOM
2683
CA
GLN
400
45.936
27.809
52.316
1.00
17.16


ATOM
2684
CB
GLN
400
46.963
28.505
51.413
1.00
16.79


ATOM
2685
CG
GLN
400
46.952
28.124
49.946
1.00
19.01


ATOM
2686
CD
GLN
400
47.967
28.933
49.144
1.00
19.64


ATOM
2687
OE1
GLN
400
48.171
30.118
49.401
1.00
19.74


ATOM
2688
NE2
GLN
400
48.598
28.296
48.163
1.00
21.63


ATOM
2689
C
GLN
400
46.236
26.313
52.382
1.00
17.92


ATOM
2690
O
GLN
400
47.236
25.909
52.966
1.00
16.80


ATOM
2691
N
CYS
401
45.363
25.495
51.805
1.00
19.15


ATOM
2692
CA
CYS
401
45.602
24.055
51.771
1.00
21.48


ATOM
2693
C
CYS
401
46.472
23.902
50.528
1.00
21.39


ATOM
2694
O
CYS
401
46.039
23.417
49.485
1.00
23.39


ATOM
2695
CB
CYS
401
44.288
23.278
51.619
1.00
20.09


ATOM
2696
SG
CYS
401
43.111
23.526
52.994
1.00
23.70


ATOM
2697
N
THR
402
47.706
24.363
50.663
1.00
21.55


ATOM
2698
CA
THR
402
48.681
24.362
49.591
1.00
21.97


ATOM
2699
CB
THR
402
50.022
24.915
50.096
1.00
21.86


ATOM
2700
OG1
THR
402
49.800
26.175
50.744
1.00
20.74


ATOM
2701
CG2
THR
402
50.995
25.103
48.936
1.00
20.95


ATOM
2702
C
THR
402
48.941
23.017
48.936
1.00
24.16


ATOM
2703
O
THR
402
49.112
21.999
49.612
1.00
24.28


ATOM
2704
N
THR
403
48.965
23.036
47.608
1.00
23.67


ATOM
2705
CA
THR
403
49.249
21.859
46.802
1.00
23.28


ATOM
2706
CB
THR
403
48.158
21.620
45.739
1.00
24.61


ATOM
2707
OG1
THR
403
46.922
21.312
46.390
1.00
25.63


ATOM
2708
CG2
THR
403
48.541
20.458
44.830
1.00
26.73


ATOM
2709
C
THR
403
50.571
22.162
46.108
1.00
23.10


ATOM
2710
O
THR
403
50.816
23.296
45.692
1.00
22.88


ATOM
2711
N
VAL
404
51.428
21.157
45.986
1.00
23.09


ATOM
2712
CA
VAL
404
52.724
21.359
45.359
1.00
23.31


ATOM
2713
CB
VAL
404
53.762
20.342
45.887
1.00
23.84


ATOM
2714
CG1
VAL
404
55.115
20.589
45.241
1.00
23.34


ATOM
2715
CG2
VAL
404
53.870
20.457
47.395
1.00
22.82


ATOM
2716
C
VAL
404
52.691
21.293
43.834
1.00
23.74


ATOM
2717
O
VAL
404
52.808
20.218
43.241
1.00
23.48


ATOM
2718
N
ASN
405
52.517
22.457
43.215
1.00
22.93


ATOM
2719
CA
ASN
405
52.500
22.602
41.762
1.00
22.84


ATOM
2720
CB
ASN
405
51.186
22.099
41.154
1.00
22.95


ATOM
2721
CG
ASN
405
49.970
22.816
41.702
1.00
24.71


ATOM
2722
OD1
ASN
405
49.970
24.036
41.861
1.00
24.62


ATOM
2723
ND2
ASN
405
48.915
22.058
41.981
1.00
24.60


ATOM
2724
C
ASN
405
52.705
24.078
41.423
1.00
22.93


ATOM
2725
O
ASN
405
52.654
24.938
42.306
1.00
19.22


ATOM
2726
N
LEU
406
52.932
24.368
40.147
1.00
23.26


ATOM
2727
CA
LEU
406
53.173
25.738
39.709
1.00
24.41


ATOM
2728
CB
LEU
406
53.514
25.762
38.214
1.00
26.22


ATOM
2729
CG
LEU
406
54.513
26.821
37.724
1.00
29.20


ATOM
2730
CD1
LEU
406
54.502
26.848
36.196
1.00
27.25


ATOM
2731
CD2
LEU
406
54.162
28.194
38.271
1.00
30.58


ATOM
2732
C
LEU
406
51.984
26.664
39.971
1.00
24.64


ATOM
2733
O
LEU
406
52.162
27.808
40.393
1.00
23.62


ATOM
2734
N
GLU
407
50.774
26.171
39.726
1.00
24.14


ATOM
2735
CA
GLU
407
49.584
26.987
39.927
1.00
24.63


ATOM
2736
CB
GLU
407
48.324
26.185
39.589
1.00
26.59


ATOM
2737
CG
GLU
407
47.126
27.059
39.257
1.00
30.80


ATOM
2738
CD
GLU
407
45.917
26.266
38.798
1.00
33.25


ATOM
2739
OE1
GLU
407
46.094
25.139
38.293
1.00
33.52


ATOM
2740
OE2
GLU
407
44.787
26.780
38.927
1.00
35.96


ATOM
2741
C
GLU
407
49.499
27.525
41.357
1.00
23.70


ATOM
2742
O
GLU
407
49.194
28.697
41.566
1.00
23.73


ATOM
2743
N
ASP
408
49.775
26.675
42.340
1.00
21.73


ATOM
2744
CA
ASP
408
49.717
27.107
43.731
1.00
21.63


ATOM
2745
CB
ASP
408
49.541
25.899
44.653
1.00
23.21


ATOM
2746
CG
ASP
408
48.247
25.958
45.438
1.00
23.22


ATOM
2747
OD1
ASP
408
47.301
26.620
44.963
1.00
25.47


ATOM
2748
OD2
ASP
408
48.166
25.340
46.519
1.00
25.23


ATOM
2749
C
ASP
408
50.944
27.926
44.138
1.00
20.39


ATOM
2750
O
ASP
408
50.922
28.635
45.146
1.00
19.37


ATOM
2751
N
LEU
409
52.016
27.831
43.360
1.00
18.98


ATOM
2752
CA
LEU
409
53.209
28.611
43.659
1.00
18.41


ATOM
2753
CB
LEU
409
54.383
28.173
42.780
1.00
20.25


ATOM
2754
CG
LEU
409
55.692
28.941
43.001
1.00
20.55


ATOM
2755
CD1
LEU
409
56.113
28.815
44.447
1.00
21.00


ATOM
2756
CD2
LEU
409
56.778
28.404
42.083
1.00
22.20


ATOM
2757
C
LEU
409
52.849
30.067
43.362
1.00
17.90


ATOM
2758
O
LEU
409
53.274
30.987
44.062
1.00
16.65


ATOM
2759
N
VAL
410
52.057
30.266
42.313
1.00
16.80


ATOM
2760
CA
VAL
410
51.618
31.605
41.943
1.00
16.49


ATOM
2761
CB
VAL
410
50.920
31.600
40.561
1.00
16.89


ATOM
2762
CG1
VAL
410
50.352
32.977
40.247
1.00
14.92


ATOM
2763
CG2
VAL
410
51.919
31.198
39.491
1.00
15.83


ATOM
2764
C
VAL
410
50.656
32.106
43.024
1.00
15.73


ATOM
2765
O
VAL
410
50.732
33.258
43.443
1.00
14.75


ATOM
2766
N
VAL
411
49.763
31.232
43.484
1.00
15.97


ATOM
2767
CA
VAL
411
48.813
31.603
44.533
1.00
15.75


ATOM
2768
CB
VAL
411
47.870
30.425
44.902
1.00
15.53


ATOM
2769
CG1
VAL
411
47.006
30.805
46.114
1.00
11.21


ATOM
2770
CG2
VAL
411
46.982
30.070
43.711
1.00
14.36


ATOM
2771
C
VAL
411
49.561
32.034
45.796
1.00
16.60


ATOM
2772
O
VAL
411
49.194
33.015
46.445
1.00
14.95


ATOM
2773
N
ALA
412
50.610
31.296
46.146
1.00
16.80


ATOM
2774
CA
ALA
412
51.392
31.624
47.328
1.00
16.33


ATOM
2775
CB
ALA
412
52.541
30.632
47.490
1.00
17.31


ATOM
2776
C
ALA
412
51.930
33.047
47.213
1.00
16.81


ATOM
2777
O
ALA
412
51.940
33.793
48.188
1.00
15.68


ATOM
2778
N
HIS
413
52.386
33.419
46.018
1.00
16.29


ATOM
2779
CA
HIS
413
52.908
34.764
45.802
1.00
14.95


ATOM
2780
CB
HIS
413
53.576
34.886
44.425
1.00
14.73


ATOM
2781
CG
HIS
413
54.942
34.282
44.362
1.00
14.13


ATOM
2782
CD2
HIS
413
56.169
34.855
44.354
1.00
14.28


ATOM
2783
ND1
HIS
413
55.155
32.920
44.333
1.00
13.46


ATOM
2784
CE1
HIS
413
56.454
32.681
44.310
1.00
14.23


ATOM
2785
NE2
HIS
413
57.091
33.837
44.322
1.00
15.75


ATOM
2786
C
HIS
413
51.768
35.765
45.910
1.00
13.28


ATOM
2787
O
HIS
413
51.923
36.834
46.493
1.00
11.46


ATOM
2788
N
HIS
414
50.620
35.409
45.342
1.00
14.51


ATOM
2789
CA
HIS
414
49.447
36.276
45.391
1.00
13.47


ATOM
2790
CB
HIS
414
48.235
35.570
44.775
1.00
15.00


ATOM
2791
CG
HIS
414
46.971
36.370
44.849
1.00
15.40


ATOM
2792
CD2
HIS
414
45.972
36.376
45.766
1.00
13.24


ATOM
2793
ND1
HIS
414
46.647
37.339
43.923
1.00
14.33


ATOM
2794
CE1
HIS
414
45.504
37.908
44.267
1.00
14.69


ATOM
2795
NE2
HIS
414
45.075
37.341
45.381
1.00
12.08


ATOM
2796
C
HIS
414
49.136
36.626
46.845
1.00
14.00


ATOM
2797
O
HIS
414
48.984
37.802
47.190
1.00
13.07


ATOM
2798
N
GLU
415
49.049
35.599
47.690
1.00
12.38


ATOM
2799
CA
GLU
415
48.742
35.788
49.105
1.00
13.04


ATOM
2800
CB
GLU
415
48.489
34.440
49.782
1.00
11.80


ATOM
2801
CG
GLU
415
47.322
33.650
49.205
1.00
12.84


ATOM
2802
CD
GLU
415
46.014
34.422
49.240
1.00
12.28


ATOM
2803
OE1
GLU
415
45.833
35.250
50.159
1.00
11.52


ATOM
2804
OE2
GLU
415
45.159
34.188
48.359
1.00
12.50


ATOM
2805
C
GLU
415
49.839
36.535
49.850
1.00
13.54


ATOM
2806
O
GLU
415
49.551
37.346
50.726
1.00
14.84


ATOM
2807
N
MET
416
51.096
36.258
49.512
1.00
13.52


ATOM
2808
CA
MET
416
52.208
36.941
50.167
1.00
14.41


ATOM
2809
CB
MET
416
53.542
36.304
49.767
1.00
14.35


ATOM
2810
CG
MET
416
53.786
34.943
50.429
1.00
15.99


ATOM
2811
SD
MET
416
54.132
35.070
52.218
1.00
17.59


ATOM
2812
CE
MET
416
55.885
35.543
52.156
1.00
14.94


ATOM
2813
C
MET
416
52.176
38.424
49.796
1.00
13.49


ATOM
2814
O
MET
416
52.660
39.276
50.543
1.00
11.88


ATOM
2815
N
GLY
417
51.592
38.725
48.642
1.00
13.47


ATOM
2816
CA
GLY
417
51.473
40.107
48.217
1.00
11.88


ATOM
2817
C
GLY
417
50.547
40.833
49.186
1.00
10.84


ATOM
2818
O
GLY
417
50.774
41.995
49.517
1.00
10.89


ATOM
2819
N
HIS
418
49.499
40.146
49.639
1.00
11.02


ATOM
2820
CA
HIS
418
48.555
40.732
50.595
1.00
12.04


ATOM
2821
CB
HIS
418
47.382
39.784
50.864
1.00
11.04


ATOM
2822
CG
HIS
418
46.385
39.711
49.752
1.00
12.59


ATOM
2823
CD2
HIS
418
45.842
38.648
49.112
1.00
9.69


ATOM
2824
ND1
HIS
418
45.783
40.830
49.214
1.00
13.07


ATOM
2825
CE1
HIS
418
44.912
40.458
48.294
1.00
11.52


ATOM
2826
NE2
HIS
418
44.928
39.140
48.213
1.00
12.75


ATOM
2827
C
HIS
418
49.271
41.003
51.916
1.00
11.39


ATOM
2828
O
HIS
418
49.122
42.071
52.512
1.00
11.43


ATOM
2829
N
ILE
419
50.039
40.018
52.373
1.00
11.02


ATOM
2830
CA
ILE
419
50.788
40.147
53.619
1.00
11.33


ATOM
2831
CB
ILE
419
51.613
38.874
53.905
1.00
12.82


ATOM
2832
CG2
ILE
419
52.405
39.042
55.195
1.00
12.45


ATOM
2833
CG1
ILE
419
50.681
37.658
53.991
1.00
12.12


ATOM
2834
CD1
ILE
419
49.672
37.730
55.117
1.00
14.37


ATOM
2835
C
ILE
419
51.738
41.343
53.548
1.00
11.48


ATOM
2836
O
ILE
419
51.853
42.113
54.500
1.00
12.38


ATOM
2837
N
GLN
420
52.417
41.496
52.417
1.00
11.52


ATOM
2838
CA
GLN
420
53.347
42.607
52.245
1.00
13.30


ATOM
2839
CB
GLN
420
54.004
42.544
50.859
1.00
12.77


ATOM
2840
CG
GLN
420
55.044
43.636
50.636
1.00
14.92


ATOM
2841
CD
GLN
420
56.256
43.491
51.546
1.00
14.49


ATOM
2842
OE1
GLN
420
56.897
44.479
51.904
1.00
17.00


ATOM
2843
NE2
GLN
420
56.585
42.255
51.908
1.00
14.95


ATOM
2844
C
GLN
420
52.599
43.932
52.412
1.00
13.79


ATOM
2845
O
GLN
420
53.065
44.844
53.101
1.00
14.70


ATOM
2846
N
TYR
421
51.435
44.035
51.780
1.00
13.96


ATOM
2847
CA
TYR
421
50.631
45.246
51.876
1.00
13.60


ATOM
2848
CB
TYR
421
49.372
45.099
51.014
1.00
10.92


ATOM
2849
CG
TYR
421
49.037
46.321
50.179
1.00
11.34


ATOM
2850
CD1
TYR
421
48.590
46.183
48.862
1.00
10.38


ATOM
2851
CE1
TYR
421
48.255
47.287
48.093
1.00
8.53


ATOM
2852
CD2
TYR
421
49.140
47.611
50.706
1.00
10.33


ATOM
2853
CE2
TYR
421
48.799
48.737
49.940
1.00
11.19


ATOM
2854
CZ
TYR
421
48.356
48.561
48.634
1.00
12.22


ATOM
2855
OH
TYR
421
47.985
49.647
47.872
1.00
10.08


ATOM
2856
C
TYR
421
50.259
45.499
53.348
1.00
13.85


ATOM
2857
O
TYR
421
50.371
46.626
53.835
1.00
12.91


ATOM
2858
N
PHE
422
49.823
44.451
54.049
1.00
15.40


ATOM
2859
CA
PHE
422
49.461
44.567
55.466
1.00
17.19


ATOM
2860
CB
PHE
422
49.173
43.189
56.076
1.00
15.34


ATOM
2861
CG
PHE
422
47.925
42.526
55.559
1.00
15.78


ATOM
2862
CD1
PHE
422
47.776
41.143
55.655
1.00
14.31


ATOM
2863
CD2
PHE
422
46.896
43.272
54.994
1.00
14.76


ATOM
2864
CE1
PHE
422
46.621
40.510
55.197
1.00
16.76


ATOM
2865
CE2
PHE
422
45.734
42.649
54.532
1.00
16.42


ATOM
2866
CZ
PHE
422
45.599
41.265
54.633
1.00
16.96


ATOM
2867
C
PHE
422
50.611
45.185
56.254
1.00
17.06


ATOM
2868
O
PHE
422
50.412
46.105
57.045
1.00
17.66


ATOM
2869
N
MET
423
51.814
44.664
56.031
1.00
16.17


ATOM
2870
CA
MET
423
53.000
45.134
56.737
1.00
17.00


ATOM
2871
CB
MET
423
54.181
44.190
56.486
1.00
18.15


ATOM
2872
CG
MET
423
53.943
42.754
56.931
1.00
19.99


ATOM
2873
SD
MET
423
55.472
41.792
57.000
1.00
20.03


ATOM
2874
CE
MET
423
55.783
41.471
55.247
1.00
18.10


ATOM
2875
C
MET
423
53.413
46.552
56.373
1.00
17.22


ATOM
2876
O
MET
423
53.849
47.315
57.236
1.00
16.52


ATOM
2877
N
GLN
424
53.277
46.905
55.097
1.00
16.46


ATOM
2878
CA
GLN
424
53.659
48.234
54.631
1.00
15.32


ATOM
2879
CB
GLN
424
53.579
48.301
53.102
1.00
16.47


ATOM
2880
CG
GLN
424
54.640
47.495
52.360
1.00
17.02


ATOM
2881
CD
GLN
424
56.031
48.092
52.496
1.00
19.21


ATOM
2882
OE1
GLN
424
56.184
49.288
52.757
1.00
16.73


ATOM
2883
NE2
GLN
424
57.053
47.266
52.297
1.00
17.82


ATOM
2884
C
GLN
424
52.836
49.377
55.224
1.00
15.29


ATOM
2885
O
GLN
424
53.372
50.455
55.482
1.00
15.54


ATOM
2886
N
TYR
425
51.539
49.157
55.433
1.00
15.59


ATOM
2887
CA
TYR
425
50.687
50.213
55.980
1.00
15.62


ATOM
2888
CB
TYR
425
49.454
50.432
55.078
1.00
14.74


ATOM
2889
CG
TYR
425
48.519
49.240
54.865
1.00
14.73


ATOM
2890
CD1
TYR
425
48.073
48.457
55.935
1.00
11.96


ATOM
2891
CE1
TYR
425
47.115
47.446
55.750
1.00
13.33


ATOM
2892
CD2
TYR
425
47.990
48.972
53.597
1.00
14.45


ATOM
2893
CE2
TYR
425
47.033
47.969
53.401
1.00
14.29


ATOM
2894
CZ
TYR
425
46.599
47.213
54.481
1.00
15.26


ATOM
2895
OH
TYR
425
45.633
46.253
54.287
1.00
13.69


ATOM
2896
C
TYR
425
50.235
49.999
57.420
1.00
15.99


ATOM
2897
O
TYR
425
49.311
50.662
57.887
1.00
15.53


ATOM
2898
N
LYS
426
50.903
49.096
58.131
1.00
18.15


ATOM
2899
CA
LYS
426
50.535
48.777
59.509
1.00
19.68


ATOM
2900
CB
LYS
426
51.446
47.669
60.053
1.00
19.35


ATOM
2901
CG
LYS
426
52.893
48.084
60.268
1.00
21.71


ATOM
2902
CD
LYS
426
53.700
46.947
60.895
1.00
23.93


ATOM
2903
CE
LYS
426
55.145
47.355
61.133
1.00
25.11


ATOM
2904
NZ
LYS
426
55.224
48.568
61.996
1.00
30.09


ATOM
2905
C
LYS
426
50.533
49.947
60.495
1.00
20.54


ATOM
2906
O
LYS
426
49.903
49.864
61.550
1.00
20.64


ATOM
2907
N
ASP
427
51.221
51.034
60.160
1.00
21.79


ATOM
2908
CA
ASP
427
51.281
52.177
61.064
1.00
23.05


ATOM
2909
CB
ASP
427
52.692
52.763
61.078
1.00
23.93


ATOM
2910
CG
ASP
427
53.698
51.805
61.664
1.00
26.63


ATOM
2911
OD1
ASP
427
53.394
51.228
62.732
1.00
26.74


ATOM
2912
OD2
ASP
427
54.780
51.631
61.066
1.00
26.70


ATOM
2913
C
ASP
427
50.275
53.280
60.787
1.00
22.13


ATOM
2914
O
ASP
427
50.265
54.302
61.472
1.00
21.25


ATOM
2915
N
LEU
428
49.433
53.078
59.783
1.00
21.00


ATOM
2916
CA
LEU
428
48.422
54.071
59.456
1.00
20.38


ATOM
2917
CB
LEU
428
48.002
53.953
57.988
1.00
20.36


ATOM
2918
CG
LEU
428
49.012
54.228
56.874
1.00
18.26


ATOM
2919
CD1
LEU
428
48.314
54.052
55.532
1.00
16.44


ATOM
2920
CD2
LEU
428
49.571
55.642
57.005
1.00
17.84


ATOM
2921
C
LEU
428
47.200
53.831
60.324
1.00
19.95


ATOM
2922
O
LEU
428
47.041
52.754
60.899
1.00
20.02


ATOM
2923
N
PRO
429
46.332
54.846
60.457
1.00
20.13


ATOM
2924
CD
PRO
429
46.480
56.257
60.062
1.00
18.31


ATOM
2925
CA
PRO
429
45.129
54.650
61.269
1.00
19.43


ATOM
2926
CB
PRO
429
44.377
55.960
61.083
1.00
18.57


ATOM
2927
CG
PRO
429
45.487
56.952
60.980
1.00
19.44


ATOM
2928
C
PRO
429
44.394
53.459
60.652
1.00
19.56


ATOM
2929
O
PRO
429
44.330
53.336
59.429
1.00
18.88


ATOM
2930
N
VAL
430
43.851
52.591
61.495
1.00
19.81


ATOM
2931
CA
VAL
430
43.159
51.393
61.038
1.00
21.00


ATOM
2932
CB
VAL
430
42.475
50.677
62.232
1.00
23.09


ATOM
2933
CG1
VAL
430
41.214
51.418
62.644
1.00
23.83


ATOM
2934
CG2
VAL
430
42.168
49.241
61.870
1.00
24.99


ATOM
2935
C
VAL
430
42.135
51.614
59.913
1.00
20.48


ATOM
2936
O
VAL
430
42.021
50.789
59.006
1.00
18.44


ATOM
2937
N
ALA
431
41.405
52.724
59.957
1.00
20.17


ATOM
2938
CA
ALA
431
40.401
53.002
58.933
1.00
20.14


ATOM
2939
CB
ALA
431
39.587
54.236
59.311
1.00
21.04


ATOM
2940
C
ALA
431
41.029
53.197
57.560
1.00
19.75


ATOM
2941
O
ALA
431
40.350
53.110
56.540
1.00
20.64


ATOM
2942
N
LEU
432
42.330
53.456
57.537
1.00
19.42


ATOM
2943
CA
LEU
432
43.023
53.667
56.277
1.00
17.67


ATOM
2944
CB
LEU
432
43.821
54.974
56.336
1.00
17.92


ATOM
2945
CG
LEU
432
43.038
56.238
56.721
1.00
16.23


ATOM
2946
CD1
LEU
432
43.996
57.416
56.789
1.00
18.02


ATOM
2947
CD2
LEU
432
41.929
56.512
55.703
1.00
17.85


ATOM
2948
C
LEU
432
43.946
52.500
55.935
1.00
18.33


ATOM
2949
O
LEU
432
44.758
52.592
55.010
1.00
19.78


ATOM
2950
N
ARG
433
43.824
51.401
56.676
1.00
17.58


ATOM
2951
CA
ARG
433
44.654
50.231
56.410
1.00
19.13


ATOM
2952
CB
ARG
433
44.894
49.428
57.695
1.00
20.01


ATOM
2953
CG
ARG
433
45.700
50.170
58.761
1.00
24.17


ATOM
2954
CD
ARG
433
46.094
49.238
59.910
1.00
25.60


ATOM
2955
NE
ARG
433
46.572
49.977
61.076
1.00
30.87


ATOM
2956
CZ
ARG
433
47.022
49.413
62.196
1.00
32.45


ATOM
2957
NH1
ARG
433
47.065
48.091
62.317
1.00
31.35


ATOM
2958
NH2
ARG
433
47.423
50.177
63.203
1.00
33.39


ATOM
2959
C
ARG
433
44.029
49.333
55.339
1.00
17.92


ATOM
2960
O
ARG
433
43.527
48.245
55.626
1.00
16.81


ATOM
2961
N
GLU
434
44.055
49.817
54.102
1.00
17.88


ATOM
2962
CA
GLU
434
43.532
49.088
52.951
1.00
18.38


ATOM
2963
CB
GLU
434
42.062
49.454
52.704
1.00
21.40


ATOM
2964
CG
GLU
434
41.126
49.146
53.866
1.00
30.47


ATOM
2965
CD
GLU
434
40.964
47.655
54.121
1.00
35.68


ATOM
2966
OE1
GLU
434
41.691
46.848
53.498
1.00
39.78


ATOM
2967
OE2
GLU
434
40.105
47.288
54.953
1.00
39.56


ATOM
2968
C
GLU
434
44.369
49.490
51.741
1.00
15.81


ATOM
2969
O
GLU
434
45.184
50.408
51.827
1.00
14.18


ATOM
2970
N
GLY
435
44.178
48.804
50.617
1.00
15.92


ATOM
2971
CA
GLY
435
44.926
49.153
49.419
1.00
14.49


ATOM
2972
C
GLY
435
44.383
50.441
48.818
1.00
14.11


ATOM
2973
O
GLY
435
43.296
50.881
49.201
1.00
12.46


ATOM
2974
N
ALA
436
45.132
51.054
47.900
1.00
13.32


ATOM
2975
CA
ALA
436
44.687
52.293
47.248
1.00
13.39


ATOM
2976
CB
ALA
436
45.571
52.601
46.044
1.00
10.25


ATOM
2977
C
ALA
436
43.230
52.066
46.828
1.00
11.87


ATOM
2978
O
ALA
436
42.389
52.956
46.927
1.00
12.19


ATOM
2979
N
ASN
437
42.965
50.864
46.329
1.00
12.23


ATOM
2980
CA
ASN
437
41.619
50.400
45.989
1.00
11.91


ATOM
2981
CB
ASN
437
41.104
50.904
44.617
1.00
12.44


ATOM
2982
CG
ASN
437
41.809
50.287
43.430
1.00
10.41


ATOM
2983
OD1
ASN
437
42.024
49.079
43.363
1.00
12.22


ATOM
2984
ND2
ASN
437
42.144
51.126
42.458
1.00
10.38


ATOM
2985
C
ASN
437
41.771
48.885
46.051
1.00
11.58


ATOM
2986
O
ASN
437
42.890
48.383
46.049
1.00
12.17


ATOM
2987
N
PRO
438
40.663
48.136
46.142
1.00
12.13


ATOM
2988
CD
PRO
438
39.250
48.549
46.234
1.00
10.54


ATOM
2989
CA
PRO
438
40.789
46.677
46.220
1.00
10.70


ATOM
2990
CB
PRO
438
39.338
46.205
46.162
1.00
12.07


ATOM
2991
CG
PRO
438
38.607
47.326
46.867
1.00
11.56


ATOM
2992
C
PRO
438
41.674
46.026
45.160
1.00
11.01


ATOM
2993
O
PRO
438
42.343
45.031
45.441
1.00
9.92


ATOM
2994
N
GLY
439
41.682
46.591
43.955
1.00
10.86


ATOM
2995
CA
GLY
439
42.494
46.049
42.876
1.00
11.19


ATOM
2996
C
GLY
439
43.984
46.073
43.175
1.00
11.99


ATOM
2997
O
GLY
439
44.710
45.135
42.830
1.00
10.62


ATOM
2998
N
PHE
440
44.452
47.148
43.806
1.00
11.06


ATOM
2999
CA
PHE
440
45.866
47.260
44.156
1.00
11.17


ATOM
3000
CB
PHE
440
46.157
48.609
44.831
1.00
11.18


ATOM
3001
CG
PHE
440
46.364
49.745
43.864
1.00
12.13


ATOM
3002
CD1
PHE
440
45.377
50.089
42.947
1.00
11.54


ATOM
3003
CD2
PHE
440
47.554
50.472
43.871
1.00
12.86


ATOM
3004
CE1
PHE
440
45.572
51.146
42.045
1.00
11.15


ATOM
3005
CE2
PHE
440
47.755
51.526
42.977
1.00
12.18


ATOM
3005
CZ
PHE
440
46.763
51.860
42.065
1.00
11.17


ATOM
3007
C
PHE
440
46.275
46.135
45.098
1.00
11.04


ATOM
3008
O
PHE
440
47.326
45.519
44.926
1.00
10.51


ATOM
3009
N
HIS
441
45.445
45.873
46.104
1.00
10.42


ATOM
3010
CA
HIS
441
45.753
44.822
47.066
1.00
11.23


ATOM
3011
CB
HIS
441
44.640
44.720
48.116
1.00
11.68


ATOM
3012
CG
HIS
441
45.144
44.607
49.523
1.00
11.91


ATOM
3013
CD2
HIS
441
44.919
45.379
50.614
1.00
10.21


ATOM
3014
ND1
HIS
441
45.976
43.589
49.941
1.00
10.64


ATOM
3015
CE1
HIS
441
46.237
43.736
51.228
1.00
11.94


ATOM
3016
NE2
HIS
441
45.607
44.815
51.661
1.00
11.66


ATOM
3017
C
HIS
441
45.921
43.475
46.364
1.00
10.83


ATOM
3018
O
HIS
441
46.780
42.674
46.736
1.00
9.33


ATOM
3019
N
GLU
442
45.106
43.241
45.339
1.00
12.01


ATOM
3020
CA
GLU
442
45.144
41.991
44.586
1.00
10.66


ATOM
3021
CB
GLU
442
43.838
41.819
43.801
1.00
11.06


ATOM
3022
CG
GLU
442
42.565
41.755
44.645
1.00
7.88


ATOM
3023
CD
GLU
442
42.614
40.643
45.677
1.00
8.56


ATOM
3024
OE1
GLU
442
43.226
39.598
45.376
1.00
8.96


ATOM
3025
OE2
GLU
442
42.044
40.809
46.778
1.00
8.52


ATOM
3026
C
GLU
442
46.320
41.897
43.607
1.00
13.30


ATOM
3027
O
GLU
442
46.815
40.807
43.323
1.00
14.12


ATOM
3028
N
ALA
443
46.782
43.038
43.105
1.00
14.06


ATOM
3029
CA
ALA
443
47.860
43.056
42.112
1.00
14.79


ATOM
3030
CB
ALA
443
47.801
44.369
41.336
1.00
13.68


ATOM
3031
C
ALA
443
49.299
42.808
42.575
1.00
14.18


ATOM
3032
O
ALA
443
50.096
42.229
41.835
1.00
13.95


ATOM
3033
N
ILE
444
49.631
43.249
43.784
1.00
13.76


ATOM
3034
CA
ILE
444
50.989
43.119
44.311
1.00
13.53


ATOM
3035
CB
ILE
444
51.035
43.500
45.810
1.00
13.26


ATOM
3036
CG2
ILE
444
52.476
43.493
46.312
1.00
11.75


ATOM
3037
CG1
ILE
444
50.430
44.898
46.002
1.00
11.55


ATOM
3038
CD1
ILE
444
51.090
45.972
45.158
1.00
13.98


ATOM
3039
C
ILE
444
51.671
41.757
44.116
1.00
13.95


ATOM
3040
O
ILE
444
52.710
41.666
43.454
1.00
10.36


ATOM
3041
N
GLY
445
51.095
40.709
44.695
1.00
12.71


ATOM
3042
CA
GLY
445
51.678
39.389
44.562
1.00
12.69


ATOM
3043
C
GLY
445
51.785
38.914
43.125
1.00
13.85


ATOM
3044
O
GLY
445
52.774
38.284
42.746
1.00
14.14


ATOM
3045
N
ASP
446
50.767
39.215
42.324
1.00
12.80


ATOM
3046
CA
ASP
446
50.742
38.805
40.923
1.00
12.50


ATOM
3047
CB
ASP
446
49.398
39.181
40.282
1.00
9.49


ATOM
3048
CG
ASP
446
48.261
38.259
40.714
1.00
10.86


ATOM
3049
OD1
ASP
446
48.321
37.706
41.831
1.00
9.74


ATOM
3050
OD2
ASP
446
47.293
38.098
39.946
1.00
11.31


ATOM
3051
C
ASP
446
51.885
39.421
40.125
1.00
13.90


ATOM
3052
O
ASP
446
52.437
38.782
39.224
1.00
12.58


ATOM
3053
N
VAL
447
52.230
40.665
40.452
1.00
13.86


ATOM
3054
CA
VAL
447
53.307
41.351
39.758
1.00
13.18


ATOM
3055
CB
VAL
447
53.520
42.778
40.313
1.00
13.78


ATOM
3056
CG1
VAL
447
54.745
43.414
39.661
1.00
13.13


ATOM
3057
CG2
VAL
447
52.280
43.634
40.037
1.00
11.10


ATOM
3058
C
VAL
447
54.600
40.553
39.891
1.00
13.89


ATOM
3059
O
VAL
447
55.263
40.274
38.897
1.00
14.12


ATOM
3060
N
LEU
448
54.954
40.184
41.119
1.00
13.93


ATOM
3061
CA
LEU
448
56.164
39.403
41.345
1.00
14.69


ATOM
3062
CB
LEU
448
56.424
39.217
42.845
1.00
13.90


ATOM
3063
CG
LEU
448
57.185
40.346
43.548
1.00
14.37


ATOM
3064
CD1
LEU
448
56.377
41.638
43.511
1.00
13.68


ATOM
3065
CD2
LEU
448
57.474
39.937
44.980
1.00
14.99


ATOM
3066
C
LEU
448
56.068
38.040
40.665
1.00
14.58


ATOM
3067
O
LEU
448
57.030
37.580
40.047
1.00
16.65


ATOM
3068
N
ALA
449
54.909
37.400
40.776
1.00
14.25


ATOM
3069
CA
ALA
449
54.696
36.094
40.161
1.00
14.13


ATOM
3070
CB
ALA
449
53.303
35.576
40.499
1.00
12.41


ATOM
3071
C
ALA
449
54.890
36.143
38.639
1.00
14.00


ATOM
3072
O
ALA
449
55.241
35.136
38.020
1.00
14.32


ATOM
3073
N
LEU
450
54.652
37.304
38.033
1.00
13.43


ATOM
3074
CA
LEU
450
54.850
37.440
36.592
1.00
13.96


ATOM
3075
CB
LEU
450
54.473
38.853
36.121
1.00
13.77


ATOM
3076
CG
LEU
450
52.976
39.149
35.969
1.00
12.17


ATOM
3077
CD1
LEU
450
52.758
40.620
35.637
1.00
9.82


ATOM
3078
CD2
LEU
450
52.398
38.262
34.869
1.00
11.71


ATOM
3079
C
LEU
450
56.325
37.165
36.283
1.00
14.53


ATOM
3080
O
LEU
450
56.651
36.443
35.339
1.00
15.40


ATOM
3081
N
SER
451
57.212
37.745
37.085
1.00
13.59


ATOM
3082
CA
SER
451
58.644
37.540
36.900
1.00
15.77


ATOM
3083
CB
SER
451
59.441
38.498
37.789
1.00
14.12


ATOM
3084
OG
SER
451
59.381
39.818
37.273
1.00
14.82


ATOM
3085
C
SER
451
59.035
36.098
37.211
1.00
15.90


ATOM
3086
O
SER
451
59.843
35.501
36.501
1.00
16.58


ATOM
3087
N
VAL
452
58.448
35.543
38.269
1.00
16.02


ATOM
3088
CA
VAL
452
58.722
34.169
38.674
1.00
17.43


ATOM
3089
CB
VAL
452
57.903
33.786
39.933
1.00
16.72


ATOM
3090
CG1
VAL
452
58.108
32.308
40.274
1.00
16.74


ATOM
3091
CG2
VAL
452
58.321
34.657
41.102
1.00
18.21


ATOM
3092
C
VAL
452
58.381
33.182
37.554
1.00
18.85


ATOM
3093
O
VAL
452
59.101
32.205
37.337
1.00
18.12


ATOM
3094
N
SER
453
57.287
33.453
36.843
1.00
18.69


ATOM
3095
CA
SER
453
56.820
32.590
35.755
1.00
18.97


ATOM
3096
CB
SER
453
55.402
33.001
35.336
1.00
18.72


ATOM
3097
OG
SER
453
54.463
32.712
36.356
1.00
19.55


ATOM
3098
C
SER
453
57.693
32.523
34.506
1.00
18.98


ATOM
3099
O
SER
453
57.559
31.593
33.707
1.00
17.86


ATOM
3100
N
THR
454
58.576
33.499
34.320
1.00
18.89


ATOM
3101
CA
THR
454
59.426
33.499
33.138
1.00
19.78


ATOM
3102
CB
THR
454
60.385
34.699
33.123
1.00
18.87


ATOM
3103
OG1
THR
454
61.150
34.722
34.336
1.00
19.79


ATOM
3104
CG2
THR
454
59.603
35.997
32.975
1.00
18.32


ATOM
3105
C
THR
454
60.239
32.217
33.041
1.00
21.57


ATOM
3106
O
THR
454
60.734
31.707
34.045
1.00
22.35


ATOM
3107
N
PRO
455
60.378
31.673
31.822
1.00
21.55


ATOM
3108
CD
PRO
455
59.824
32.153
30.540
1.00
21.60


ATOM
3109
CA
PRO
455
61.142
30.440
31.632
1.00
23.12


ATOM
3110
CB
PRO
455
61.278
30.354
30.113
1.00
22.44


ATOM
3111
CG
PRO
455
59.972
30.933
29.641
1.00
20.77


ATOM
3112
C
PRO
455
62.489
30.489
32.338
1.00
23.94


ATOM
3113
O
PRO
455
62.854
29.566
33.064
1.00
23.00


ATOM
3114
N
LYS
456
63.216
31.582
32.140
1.00
24.94


ATOM
3115
CA
LYS
456
64.527
31.726
32.748
1.00
25.77


ATOM
3116
CB
LYS
456
65.186
33.029
32.289
1.00
28.54


ATOM
3117
CG
LYS
456
66.708
32.960
32.293
1.00
33.33


ATOM
3118
CD
LYS
456
67.343
34.308
31.998
1.00
36.84


ATOM
3119
CE
LYS
456
68.857
34.190
31.983
1.00
39.24


ATOM
3120
NZ
LYS
456
69.341
33.419
33.163
1.00
42.84


ATOM
3121
C
LYS
456
64.479
31.679
34.274
1.00
25.66


ATOM
3122
O
LYS
456
65.334
31.055
34.905
1.00
24.62


ATOM
3123
N
HIS
457
63.485
32.332
34.873
1.00
23.14


ATOM
3124
CA
HIS
457
63.386
32.325
36.326
1.00
22.18


ATOM
3125
CB
HIS
457
62.312
33.299
36.817
1.00
22.71


ATOM
3126
CG
HIS
457
62.327
33.495
38.301
1.00
21.95


ATOM
3127
CD2
HIS
457
61.859
32.717
39.307
1.00
24.49


ATOM
3128
ND1
HIS
457
62.959
34.560
38.904
1.00
21.90


ATOM
3129
CE1
HIS
457
62.884
34.429
40.217
1.00
24.67


ATOM
3130
NE2
HIS
457
62.222
33.317
40.488
1.00
24.22


ATOM
3131
C
HIS
457
63.067
30.922
36.836
1.00
21.29


ATOM
3132
O
HIS
457
63.643
30.470
37.826
1.00
20.13


ATOM
3133
N
LEU
458
62.136
30.243
36.170
1.00
21.42


ATOM
3134
CA
LEU
458
61.764
28.890
36.564
1.00
22.05


ATOM
3135
CB
LEU
458
60.633
28.355
35.677
1.00
21.29


ATOM
3136
CG
LEU
458
59.243
28.976
35.857
1.00
21.21


ATOM
3137
CD1
LEU
458
58.267
28.346
34.873
1.00
20.79


ATOM
3138
CD2
LEU
458
58.768
28.762
37.294
1.00
20.98


ATOM
3139
C
LEU
458
62.983
27.976
36.465
1.00
22.14


ATOM
3140
O
LEU
458
63.166
27.082
37.287
1.00
21.63


ATOM
3141
N
HIS
459
63.820
28.213
35.461
1.00
23.49


ATOM
3142
CA
HIS
459
65.019
27.404
35.284
1.00
25.12


ATOM
3143
CB
HIS
459
65.688
27.713
33.939
1.00
26.57


ATOM
3144
CG
HIS
459
66.953
26.941
33.701
1.00
32.18


ATOM
3145
CD2
HIS
459
67.171
25.755
33.084
1.00
33.64


ATOM
3146
ND1
HIS
459
68.180
27.358
34.173
1.00
34.37


ATOM
3147
CE1
HIS
459
69.099
26.461
33.859
1.00
34.36


ATOM
3148
NE2
HIS
459
68.513
25.478
33.199
1.00
35.32


ATOM
3149
C
HIS
459
65.985
27.657
36.441
1.00
23.17


ATOM
3150
O
HIS
459
66.698
26.751
36.867
1.00
22.80


ATOM
3151
N
SER
460
65.991
28.882
36.963
1.00
22.86


ATOM
3152
CA
SER
460
66.870
29.218
38.083
1.00
22.31


ATOM
3153
CB
SER
460
66.877
30.734
38.341
1.00
22.68


ATOM
3154
OG
SER
460
65.731
31.148
39.071
1.00
26.41


ATOM
3155
C
SER
460
66.407
28.480
39.339
1.00
21.77


ATOM
3156
O
SER
460
67.176
28.297
40.283
1.00
18.91


ATOM
3157
N
LEU
461
65.141
28.069
39.349
1.00
21.28


ATOM
3158
CA
LEU
461
64.589
27.326
40.480
1.00
23.33


ATOM
3159
CB
LEU
461
63.103
27.652
40.678
1.00
21.27


ATOM
3160
CG
LEU
461
62.745
29.061
41.153
1.00
21.36


ATOM
3161
CD1
LEU
461
61.230
29.193
41.235
1.00
21.05


ATOM
3162
CD2
LEU
461
63.383
29.330
42.513
1.00
19.25


ATOM
3163
C
LEU
461
64.748
25.839
40.197
1.00
24.98


ATOM
3164
O
LEU
461
64.394
24.992
41.022
1.00
25.06


ATOM
3165
N
ASN
462
65.280
25.543
39.012
1.00
27.22


ATOM
3166
CA
ASN
462
65.515
24.178
38.555
1.00
28.33


ATOM
3167
CB
ASN
462
66.329
23.411
39.604
1.00
30.22


ATOM
3168
CG
ASN
462
67.032
22.196
39.026
1.00
32.38


ATOM
3169
OD1
ASN
462
67.571
22.245
37.919
1.00
31.35


ATOM
3170
ND2
ASN
462
67.043
21.102
39.780
1.00
33.86


ATOM
3171
C
ASN
462
64.200
23.454
38.249
1.00
29.21


ATOM
3172
O
ASN
462
64.074
22.246
38.465
1.00
28.02


ATOM
3173
N
LEU
463
63.227
24.200
37.731
1.00
29.99


ATOM
3174
CA
LEU
463
61.923
23.641
37.394
1.00
32.41


ATOM
3175
CB
LEU
463
60.809
24.456
38.056
1.00
31.50


ATOM
3176
CG
LEU
463
60.935
24.584
39.579
1.00
31.61


ATOM
3177
CD1
LEU
463
59.736
25.346
40.125
1.00
30.85


ATOM
3178
CD2
LEU
463
61.028
23.200
40.214
1.00
30.38


ATOM
3179
C
LEU
463
61.713
23.594
35.886
1.00
34.49


ATOM
3180
O
LEU
463
60.746
23.011
35.400
1.00
37.47


ATOM
3181
N
LEU
464
62.622
24.223
35.155
1.00
36.34


ATOM
3182
CA
LEU
464
62.580
24.233
33.696
1.00
39.11


ATOM
3183
CB
LEU
464
62.053
25.574
33.163
1.00
39.04


ATOM
3184
CG
LEU
464
60.557
25.635
32.834
1.00
39.75


ATOM
3185
CD1
LEU
464
60.214
26.987
32.218
1.00
38.92


ATOM
3186
CD2
LEU
464
60.208
24.511
31.865
1.00
38.93


ATOM
3187
C
LEU
464
63.987
23.987
33.172
1.00
40.46


ATOM
3188
O
LEU
464
64.966
24.186
33.892
1.00
41.21


ATOM
3189
N
SER
465
64.089
23.546
31.923
1.00
42.64


ATOM
3190
CA
SER
465
65.390
23.281
31.323
1.00
44.44


ATOM
3191
CB
SER
465
65.500
21.805
30.926
1.00
44.95


ATOM
3192
OG
SER
465
64.454
21.428
30.048
1.00
47.16


ATOM
3193
C
SER
465
65.618
24.166
30.105
1.00
44.78


ATOM
3194
O
SER
465
66.208
25.243
30.212
1.00
45.25


ATOM
3195
N
GLY
470
64.492
32.666
21.953
1.00
45.58


ATOM
3196
CA
GLY
470
63.932
31.868
20.878
1.00
45.90


ATOM
3197
C
GLY
470
62.479
32.197
20.591
1.00
45.14


ATOM
3198
O
GLY
470
61.641
32.185
21.493
1.00
45.19


ATOM
3199
N
ALA
471
62.180
32.479
19.327
1.00
44.31


ATOM
3200
CA
ALA
471
60.829
32.832
18.904
1.00
42.77


ATOM
3201
CB
ALA
471
60.801
33.040
17.399
1.00
42.61


ATOM
3202
C
ALA
471
59.772
31.807
19.307
1.00
41.97


ATOM
3203
O
ALA
471
58.822
32.140
20.017
1.00
42.12


ATOM
3204
N
GLU
472
59.933
30.567
18.855
1.00
40.07


ATOM
3205
CA
GLU
472
58.974
29.515
19.168
1.00
38.02


ATOM
3206
CB
GLU
472
59.369
28.213
18.471
1.00
38.51


ATOM
3207
CG
GLU
472
58.968
28.190
17.001
1.00
39.98


ATOM
3208
CD
GLU
472
59.374
26.913
16.293
1.00
40.39


ATOM
3209
OE1
GLU
472
59.651
25.908
16.982
1.00
39.63


ATOM
3210
OE2
GLU
472
59.397
26.915
15.043
1.00
40.40


ATOM
3211
C
GLU
472
58.790
29.276
20.660
1.00
37.16


ATOM
3212
O
GLU
472
57.703
28.901
21.105
1.00
34.83


ATOM
3213
N
HIS
473
59.847
29.487
21.435
1.00
35.29


ATOM
3214
CA
HIS
473
59.740
29.305
22.872
1.00
35.03


ATOM
3215
CB
HIS
473
61.123
29.172
23.510
1.00
37.48


ATOM
3216
CG
HIS
473
61.817
27.889
23.179
1.00
40.71


ATOM
3217
CD2
HIS
473
61.971
26.749
23.894
1.00
41.63


ATOM
3218
ND1
HIS
473
62.435
27.665
21.967
1.00
41.83


ATOM
3219
CE1
HIS
473
62.939
26.444
21.951
1.00
42.38


ATOM
3220
NE2
HIS
473
62.671
25.866
23.109
1.00
42.85


ATOM
3221
C
HIS
473
58.993
30.497
23.464
1.00
33.66


ATOM
3222
O
HIS
473
58.305
30.361
24.474
1.00
33.56


ATOM
3223
N
ASP
474
59.129
31.660
22.829
1.00
31.69


ATOM
3224
CA
ASP
474
58.448
32.864
23.289
1.00
31.39


ATOM
3225
CB
ASP
474
58.886
34.096
22.488
1.00
33.71


ATOM
3226
CG
ASP
474
60.219
34.644
22.939
1.00
36.85


ATOM
3227
OD1
ASP
474
60.417
34.795
24.163
1.00
38.01


ATOM
3228
OD2
ASP
474
61.063
34.939
22.065
1.00
40.28


ATOM
3229
C
ASP
474
56.943
32.705
23.131
1.00
28.93


ATOM
3230
O
ASP
474
56.182
33.000
24.054
1.00
27.31


ATOM
3231
N
ILE
475
56.525
32.252
21.950
1.00
25.74


ATOM
3232
CA
ILE
475
55.110
32.059
21.658
1.00
21.87


ATOM
3233
CB
ILE
475
54.893
31.631
20.183
1.00
21.83


ATOM
3234
CG2
ILE
475
53.398
31.481
19.887
1.00
18.55


ATOM
3235
CG1
ILE
475
55.498
32.680
19.244
1.00
20.20


ATOM
3236
CD1
ILE
475
54.942
34.083
19.432
1.00
18.72


ATOM
3237
C
ILE
475
54.522
31.009
22.591
1.00
20.48


ATOM
3238
O
ILE
475
53.405
31.171
23.081
1.00
19.85


ATOM
3239
N
ASN
476
55.270
29.937
22.844
1.00
18.44


ATOM
3240
CA
ASN
476
54.795
28.894
23.746
1.00
19.25


ATOM
3241
CB
ASN
476
55.788
27.727
23.817
1.00
20.64


ATOM
3242
CG
ASN
476
55.621
26.738
22.670
1.00
22.25


ATOM
3243
OD1
ASN
476
54.645
26.785
21.917
1.00
19.60


ATOM
3244
ND2
ASN
476
56.575
25.822
22.546
1.00
20.31


ATOM
3245
C
ASN
476
54.598
29.475
25.151
1.00
18.68


ATOM
3246
O
ASN
476
53.601
29.183
25.816
1.00
17.02


ATOM
3247
N
PHE
477
55.554
30.288
25.598
1.00
15.56


ATOM
3248
CA
PHE
477
55.474
30.913
26.918
1.00
15.68


ATOM
3249
CB
PHE
477
56.779
31.646
27.248
1.00
14.76


ATOM
3250
CG
PHE
477
56.688
32.527
28.465
1.00
14.35


ATOM
3251
CD1
PHE
477
56.384
31.987
29.711
1.00
15.03


ATOM
3252
CD2
PHE
477
56.901
33.898
28.365
1.00
13.50


ATOM
3253
CE1
PHE
477
56.294
32.798
30.841
1.00
14.00


ATOM
3254
CE2
PHE
477
56.813
34.720
29.488
1.00
15.93


ATOM
3255
CZ
PHE
477
56.509
34.167
30.730
1.00
14.91


ATOM
3256
C
PHE
477
54.318
31.908
26.980
1.00
14.40


ATOM
3257
O
PHE
477
53.541
31.917
27.935
1.00
13.41


ATOM
3258
N
LEU
478
54.220
32.758
25.964
1.00
14.15


ATOM
3259
CA
LEU
478
53.155
33.750
25.917
1.00
14.48


ATOM
3260
CB
LEU
478
53.317
34.647
24.688
1.00
12.70


ATOM
3261
CG
LEU
478
54.454
35.664
24.818
1.00
13.21


ATOM
3262
CD1
LEU
478
54.637
36.396
23.508
1.00
13.86


ATOM
3263
CD2
LEU
478
54.137
36.649
25.946
1.00
14.40


ATOM
3264
C
LEU
478
51.792
33.071
25.904
1.00
13.02


ATOM
3265
O
LEU
478
50.833
33.585
26.476
1.00
11.74


ATOM
3266
N
MET
479
51.708
31.915
25.253
1.00
13.08


ATOM
3267
CA
MET
479
50.448
31.183
25.199
1.00
14.20


ATOM
3268
CB
MET
479
50.547
29.989
24.242
1.00
14.09


ATOM
3269
CG
MET
479
49.301
29.106
24.220
1.00
13.18


ATOM
3270
SD
MET
479
47.788
30.012
23.801
1.00
19.98


ATOM
3271
CE
MET
479
48.041
30.307
22.061
1.00
13.75


ATOM
3272
C
MET
479
50.105
30.688
26.599
1.00
14.85


ATOM
3273
O
MET
479
48.958
30.778
27.035
1.00
14.35


ATOM
3274
N
LYS
480
51.102
30.165
27.304
1.00
15.49


ATOM
3275
CA
LYS
480
50.868
29.669
28.648
1.00
17.00


ATOM
3276
CB
LYS
480
52.136
29.016
29.221
1.00
19.28


ATOM
3277
CG
LYS
480
51.911
28.409
30.600
1.00
26.30


ATOM
3278
CD
LYS
480
52.934
27.329
30.981
1.00
32.36


ATOM
3279
CE
LYS
480
54.279
27.910
31.400
1.00
35.11


ATOM
3280
NZ
LYS
480
55.168
26.878
32.033
1.00
35.89


ATOM
3281
C
LYS
480
50.395
30.804
29.553
1.00
14.63


ATOM
3282
O
LYS
480
49.513
30.613
30.386
1.00
16.02


ATOM
3283
N
MET
481
50.971
31.988
29.374
1.00
13.07


ATOM
3284
CA
MET
481
50.602
33.147
30.178
1.00
12.02


ATOM
3285
CB
MET
481
51.612
34.282
29.976
1.00
12.55


ATOM
3286
CG
MET
481
53.015
33.998
30.509
1.00
11.44


ATOM
3287
SD
MET
481
53.051
33.565
32.265
1.00
18.83


ATOM
3288
CE
MET
481
52.416
35.085
33.001
1.00
12.30


ATOM
3289
C
MET
481
49.202
33.644
29.821
1.00
12.65


ATOM
3290
O
MET
481
48.430
34.045
30.696
1.00
12.46


ATOM
3291
N
ALA
482
48.886
33.619
28.531
1.00
10.95


ATOM
3292
CA
ALA
482
47.588
34.067
28.046
1.00
11.63


ATOM
3293
CB
ALA
482
47.596
34.125
26.530
1.00
11.09


ATOM
3294
C
ALA
482
46.463
33.152
28.524
1.00
13.21


ATOM
3295
O
ALA
482
45.372
33.620
28.861
1.00
10.82


ATOM
3296
N
LEU
483
46.722
31.848
28.538
1.00
11.90


ATOM
3297
CA
LEU
483
45.712
30.897
28.978
1.00
14.01


ATOM
3298
CB
LEU
483
46.260
29.468
28.910
1.00
11.66


ATOM
3299
CG
LEU
483
46.455
28.896
27.498
1.00
10.77


ATOM
3300
CD1
LEU
483
47.098
27.517
27.587
1.00
8.72


ATOM
3301
CD2
LEU
483
45.118
28.813
26.785
1.00
7.73


ATOM
3302
C
LEU
483
45.268
31.232
30.401
1.00
14.37


ATOM
3303
O
LEU
483
44.158
30.898
30.814
1.00
14.12


ATOM
3304
N
ASP
484
46.142
31.894
31.147
1.00
15.19


ATOM
3305
CA
ASP
484
45.810
32.281
32.511
1.00
17.15


ATOM
3306
CB
ASP
484
47.038
32.146
33.416
1.00
19.74


ATOM
3307
CG
ASP
484
46.787
32.653
34.830
1.00
26.92


ATOM
3308
OD1
ASP
484
45.717
32.353
35.399
1.00
31.69


ATOM
3309
OD2
ASP
484
47.667
33.344
35.383
1.00
30.93


ATOM
3310
C
ASP
484
45.271
33.711
32.560
1.00
16.03


ATOM
3311
O
ASP
484
44.101
33.927
32.860
1.00
17.57


ATOM
3312
N
LYS
485
46.119
34.676
32.217
1.00
14.15


ATOM
3313
CA
LYS
485
45.772
36.094
32.265
1.00
12.86


ATOM
3314
CB
LYS
485
47.042
36.932
32.080
1.00
12.78


ATOM
3315
CG
LYS
485
48.152
36.589
33.070
1.00
13.51


ATOM
3316
CD
LYS
485
47.721
36.847
34.509
1.00
13.07


ATOM
3317
CE
LYS
485
48.838
36.502
35.488
1.00
14.28


ATOM
3318
NZ
LYS
485
48.482
36.832
36.899
1.00
12.83


ATOM
3319
C
LYS
485
44.690
36.616
31.319
1.00
12.35


ATOM
3320
O
LYS
485
43.823
37.382
31.739
1.00
12.38


ATOM
3321
N
ILE
486
44.744
36.233
30.047
1.00
11.02


ATOM
3322
CA
ILE
486
43.753
36.707
29.084
1.00
11.30


ATOM
3323
CB
ILE
486
44.243
36.506
27.632
1.00
10.39


ATOM
3324
CG2
ILE
486
43.126
36.849
26.649
1.00
9.22


ATOM
3325
CG1
ILE
486
45.487
37.366
27.376
1.00
9.66


ATOM
3326
CD1
ILE
486
45.269
38.863
27.555
1.00
12.52


ATOM
3327
C
ILE
486
42.400
36.016
29.255
1.00
10.85


ATOM
3328
O
ILE
486
41.354
36.664
29.228
1.00
9.72


ATOM
3329
N
ALA
487
42.418
34.700
29.433
1.00
11.32


ATOM
3330
CA
ALA
487
41.176
33.954
29.610
1.00
10.28


ATOM
3331
CB
ALA
487
41.484
32.464
29.773
1.00
9.81


ATOM
3332
C
ALA
487
40.390
34.462
30.823
1.00
10.73


ATOM
3333
O
ALA
487
39.161
34.432
30.836
1.00
11.37


ATOM
3334
N
PHE
488
41.110
34.937
31.834
1.00
10.32


ATOM
3335
CA
PHE
488
40.500
35.426
33.067
1.00
11.62


ATOM
3336
CB
PHE
488
41.574
35.560
34.149
1.00
11.67


ATOM
3337
CG
PHE
488
41.027
35.846
35.523
1.00
14.14


ATOM
3338
CD1
PHE
488
40.310
34.873
36.222
1.00
13.10


ATOM
3339
CD2
PHE
488
41.256
37.075
36.134
1.00
13.14


ATOM
3340
CE1
PHE
488
39.834
35.122
37.510
1.00
13.40


ATOM
3341
CE2
PHE
488
40.788
37.332
37.414
1.00
11.72


ATOM
3342
CZ
PHE
488
40.076
36.355
38.107
1.00
13.66


ATOM
3343
C
PHE
488
39.765
36.763
32.931
1.00
11.30


ATOM
3344
O
PHE
488
38.809
37.022
33.662
1.00
10.92


ATOM
3345
N
ILE
489
40.208
37.604
32.000
1.00
11.64


ATOM
3346
CA
ILE
489
39.600
38.915
31.807
1.00
10.62


ATOM
3347
CB
ILE
489
40.193
39.615
30.568
1.00
12.52


ATOM
3348
CG2
ILE
489
39.378
40.870
30.215
1.00
11.83


ATOM
3349
CG1
ILE
489
41.652
39.993
30.842
1.00
14.27


ATOM
3350
CD1
ILE
489
41.824
41.029
31.952
1.00
13.73


ATOM
3351
C
ILE
489
38.067
38.919
31.723
1.00
12.80


ATOM
3352
O
ILE
489
37.406
39.590
32.514
1.00
12.29


ATOM
3353
N
PRO
490
37.482
38.183
30.764
1.00
11.12


ATOM
3354
CD
PRO
490
38.069
37.429
29.644
1.00
10.46


ATOM
3355
CA
PRO
490
36.020
38.185
30.683
1.00
10.14


ATOM
3356
CB
PRO
490
35.742
37.410
29.390
1.00
10.83


ATOM
3357
CG
PRO
490
36.942
36.516
29.258
1.00
12.17


ATOM
3358
C
PRO
490
35.325
37.586
31.911
1.00
9.58


ATOM
3359
O
PRO
490
34.257
38.049
32.306
1.00
8.62


ATOM
3360
N
PHE
491
35.925
36.568
32.521
1.00
6.98


ATOM
3361
CA
PHE
491
35.321
35.969
33.709
1.00
9.75


ATOM
3362
CB
PHE
491
36.067
34.703
34.137
1.00
8.88


ATOM
3363
CG
PHE
491
35.512
34.074
35.393
1.00
9.15


ATOM
3364
CD1
PHE
491
34.374
33.271
35.344
1.00
8.95


ATOM
3365
CD2
PHE
491
36.109
34.311
36.630
1.00
7.55


ATOM
3366
CE1
PHE
491
33.837
32.713
36.508
1.00
9.82


ATOM
3367
CE2
PHE
491
35.580
33.757
37.803
1.00
9.83


ATOM
3368
CZ
PHE
491
34.442
32.957
37.740
1.00
8.83


ATOM
3369
C
PHE
491
35.329
36.948
34.885
1.00
9.97


ATOM
3370
O
PHE
491
34.312
37.127
35.558
1.00
10.66


ATOM
3371
N
SER
492
36.475
37.579
35.132
1.00
9.34


ATOM
3372
CA
SER
492
36.589
38.512
36.249
1.00
11.14


ATOM
3373
CB
SER
492
38.046
38.946
36.439
1.00
8.12


ATOM
3374
OG
SER
492
38.534
39.643
35.307
1.00
11.50


ATOM
3375
C
SER
492
35.692
39.738
36.083
1.00
11.76


ATOM
3376
O
SER
492
35.327
40.391
37.064
1.00
13.67


ATOM
3377
N
TYR
493
35.344
40.042
34.840
1.00
11.79


ATOM
3378
CA
TYR
493
34.482
41.177
34.527
1.00
12.20


ATOM
3379
CB
TYR
493
34.633
41.544
33.048
1.00
12.22


ATOM
3380
CG
TYR
493
33.904
42.801
32.642
1.00
13.21


ATOM
3381
CD1
TYR
493
34.295
44.045
33.134
1.00
14.67


ATOM
3382
CE1
TYR
493
33.630
45.210
32.763
1.00
16.44


ATOM
3383
CD2
TYR
493
32.821
42.751
31.764
1.00
13.82


ATOM
3384
CE2
TYR
493
32.150
43.912
31.385
1.00
16.41


ATOM
3385
CZ
TYR
493
32.561
45.137
31.889
1.00
15.04


ATOM
3386
OH
TYR
493
31.912
46.285
31.510
1.00
14.56


ATOM
3387
C
TYR
493
33.022
40.811
34.793
1.00
13.05


ATOM
3388
O
TYR
493
32.254
41.585
35.363
1.00
13.30


ATOM
3389
N
LEU
494
32.670
39.604
34.372
1.00
13.45


ATOM
3390
CA
LEU
494
31.327
39.053
34.475
1.00
13.55


ATOM
3391
CB
LEU
494
31.319
37.739
33.685
1.00
16.41


ATOM
3392
CG
LEU
494
30.282
36.622
33.731
1.00
20.60


ATOM
3393
CD1
LEU
494
30.701
35.590
32.689
1.00
21.31


ATOM
3394
CD2
LEU
494
30.192
35.977
35.100
1.00
15.36


ATOM
3395
C
LEU
494
30.741
38.834
35.874
1.00
11.95


ATOM
3396
O
LEU
494
29.566
39.112
36.102
1.00
11.20


ATOM
3397
N
VAL
495
31.544
38.347
36.810
1.00
10.36


ATOM
3398
CA
VAL
495
31.019
38.055
38.141
1.00
10.58


ATOM
3399
CB
VAL
495
32.139
37.621
39.109
1.00
9.66


ATOM
3400
CG1
VAL
495
31.549
37.318
40.486
1.00
9.24


ATOM
3401
CG2
VAL
495
32.833
36.376
38.564
1.00
12.37


ATOM
3402
C
VAL
495
30.197
39.171
38.785
1.00
9.62


ATOM
3403
O
VAL
495
29.047
38.955
39.154
1.00
7.39


ATOM
3404
N
ASP
496
30.768
40.360
38.919
1.00
9.30


ATOM
3405
CA
ASP
496
30.012
41.435
39.538
1.00
10.89


ATOM
3406
CB
ASP
496
30.954
42.439
40.207
1.00
10.57


ATOM
3407
CG
ASP
496
31.513
41.909
41.526
1.00
9.77


ATOM
3408
OD1
ASP
496
31.025
40.855
41.993
1.00
9.79


ATOM
3409
OD2
ASP
496
32.426
42.532
42.098
1.00
9.45


ATOM
3410
C
ASP
496
29.015
42.125
38.609
1.00
11.41


ATOM
3411
O
ASP
496
28.125
42.837
39.081
1.00
11.26


ATOM
3412
N
GLN
497
29.143
41.923
37.298
1.00
9.61


ATOM
3413
CA
GLN
497
28.150
42.511
36.400
1.00
11.24


ATOM
3414
CB
GLN
497
28.471
42.231
34.926
1.00
11.55


ATOM
3415
CG
GLN
497
29.702
42.954
34.377
1.00
13.89


ATOM
3416
CD
GLN
497
29.672
44.459
34.613
1.00
16.12


ATOM
3417
OE1
GLN
497
28.615
45.082
34.607
1.00
14.20


ATOM
3418
NE2
GLN
497
30.844
45.048
34.809
1.00
17.36


ATOM
3419
C
GLN
497
26.847
41.804
36.787
1.00
10.45


ATOM
3420
O
GLN
497
25.774
42.403
36.794
1.00
10.85


ATOM
3421
N
TRP
498
26.961
40.520
37.120
1.00
9.86


ATOM
3422
CA
TRP
498
25.812
39.717
37.537
1.00
10.64


ATOM
3423
CB
TRP
498
26.189
38.231
37.571
1.00
9.73


ATOM
3424
CG
TRP
498
25.057
37.318
37.978
1.00
9.08


ATOM
3425
CD2
TRP
498
24.815
36.788
39.287
1.00
9.94


ATOM
3426
CE2
TRP
498
23.634
36.009
39.213
1.00
11.43


ATOM
3427
CE3
TRP
498
25.480
36.898
40.518
1.00
9.53


ATOM
3428
CD1
TRP
498
24.044
36.851
37.182
1.00
10.54


ATOM
3429
NE1
TRP
498
23.185
36.063
37.919
1.00
9.96


ATOM
3430
CZ2
TRP
498
23.105
35.343
40.325
1.00
10.04


ATOM
3431
CZ3
TRP
498
24.950
36.232
41.629
1.00
13.16


ATOM
3432
CH2
TRP
498
23.773
35.465
41.520
1.00
12.54


ATOM
3433
C
TRP
498
25.333
40.151
38.928
1.00
9.68


ATOM
3434
O
TRP
498
24.146
40.398
39.132
1.00
10.04


ATOM
3435
N
ARG
499
26.252
40.243
39.885
1.00
10.21


ATOM
3436
CA
ARG
499
25.871
40.643
41.240
1.00
11.86


ATOM
3437
CB
ARG
499
27.038
40.468
42.222
1.00
11.07


ATOM
3438
CG
ARG
499
27.106
39.070
42.824
1.00
12.83


ATOM
3439
CD
ARG
499
27.992
39.005
44.062
1.00
12.47


ATOM
3440
NE
ARG
499
29.395
39.250
43.748
1.00
10.15


ATOM
3441
CZ
ARG
499
30.409
38.744
44.439
1.00
12.88


ATOM
3442
NH1
ARG
499
30.171
37.961
45.491
1.00
10.18


ATOM
3443
NH2
ARG
499
31.657
39.000
44.067
1.00
10.68


ATOM
3444
C
ARG
499
25.325
42.065
41.336
1.00
12.18


ATOM
3445
O
ARG
499
24.395
42.311
42.098
1.00
11.36


ATOM
3446
N
TRP
500
25.887
42.996
40.568
1.00
11.77


ATOM
3447
CA
TRP
500
25.391
44.368
40.605
1.00
12.08


ATOM
3448
CB
TRP
500
26.202
45.289
39.684
1.00
10.66


ATOM
3449
CG
TRP
500
27.602
45.521
40.139
1.00
10.40


ATOM
3450
CD2
TRP
500
28.677
46.051
39.357
1.00
11.41


ATOM
3451
CE2
TRP
500
29.821
46.074
40.183
1.00
11.19


ATOM
3452
CE3
TRP
500
28.786
46.504
38.034
1.00
11.44


ATOM
3453
CD1
TRP
500
28.119
45.261
41.374
1.00
9.78


ATOM
3454
NE1
TRP
500
29.451
45.589
41.409
1.00
10.36


ATOM
3455
CZ2
TRP
500
31.062
46.536
39.731
1.00
10.56


ATOM
3456
CZ3
TRP
500
30.021
46.963
37.585
1.00
11.49


ATOM
3457
CH2
TRP
500
31.143
46.972
38.434
1.00
9.70


ATOM
3458
C
TRP
500
23.933
44.407
40.174
1.00
13.08


ATOM
3459
O
TRP
500
23.143
45.188
40.703
1.00
12.40


ATOM
3460
N
ARG
501
23.581
43.565
39.207
1.00
11.92


ATOM
3461
CA
ARG
501
22.209
43.525
38.719
1.00
12.19


ATOM
3462
CB
ARG
501
22.176
42.962
37.298
1.00
13.67


ATOM
3463
CG
ARG
501
22.833
43.881
36.281
1.00
17.51


ATOM
3464
CD
ARG
501
22.956
43.199
34.929
1.00
23.14


ATOM
3465
NE
ARG
501
21.650
42.807
34.407
1.00
28.87


ATOM
3466
CZ
ARG
501
21.443
41.731
33.656
1.00
30.18


ATOM
3467
NH1
ARG
501
22.458
40.936
33.340
1.00
30.67


ATOM
3468
NH2
ARG
501
20.222
41.448
33.223
1.00
31.24


ATOM
3469
C
ARG
501
21.296
42.732
39.653
1.00
10.77


ATOM
3470
O
ARG
501
20.081
42.891
39.626
1.00
10.89


ATOM
3471
N
VAL
502
21.884
41.865
40.468
1.00
9.90


ATOM
3472
CA
VAL
502
21.100
41.120
41.439
1.00
10.52


ATOM
3473
CB
VAL
502
21.896
39.940
42.034
1.00
9.49


ATOM
3474
CG1
VAL
502
21.205
39.425
43.285
1.00
8.80


ATOM
3475
CG2
VAL
502
22.008
38.812
41.002
1.00
12.29


ATOM
3476
C
VAL
502
20.786
42.126
42.551
1.00
12.15


ATOM
3477
O
VAL
502
19.643
42.245
42.999
1.00
10.37


ATOM
3478
N
PHE
503
21.815
42.865
42.965
1.00
11.50


ATOM
3479
CA
PHE
503
21.678
43.864
44.018
1.00
11.51


ATOM
3480
CB
PHE
503
23.057
44.434
44.386
1.00
10.31


ATOM
3481
CG
PHE
503
23.939
43.463
45.144
1.00
11.73


ATOM
3482
CD1
PHE
503
25.324
43.571
45.085
1.00
11.85


ATOM
3483
CD2
PHE
503
23.384
42.451
45.925
1.00
12.62


ATOM
3484
CE1
PHE
503
26.146
42.693
45.787
1.00
10.68


ATOM
3485
CE2
PHE
503
24.199
41.564
46.633
1.00
10.51


ATOM
3486
CZ
PHE
503
25.582
41.686
46.563
1.00
12.31


ATOM
3487
C
PHE
503
20.711
44.995
43.661
1.00
10.96


ATOM
3488
O
PHE
503
19.896
45.384
44.497
1.00
9.00


ATOM
3489
N
ASP
504
20.779
45.519
42.435
1.00
12.29


ATOM
3490
CA
ASP
504
19.866
46.599
42.058
1.00
12.07


ATOM
3491
CB
ASP
504
20.451
47.479
40.931
1.00
13.57


ATOM
3492
CG
ASP
504
20.413
46.822
39.548
1.00
13.98


ATOM
3493
OD1
ASP
504
19.775
45.766
39.358
1.00
14.51


ATOM
3494
OD2
ASP
504
21.033
47.396
38.633
1.00
15.18


ATOM
3495
C
ASP
504
18.470
46.107
41.685
1.00
13.54


ATOM
3496
O
ASP
504
17.615
46.892
41.278
1.00
13.18


ATOM
3497
N
GLY
505
18.239
44.805
41.833
1.00
14.58


ATOM
3498
CA
GLY
505
16.929
44.244
41.540
1.00
15.30


ATOM
3499
C
GLY
505
16.590
43.920
40.095
1.00
16.54


ATOM
3500
O
GLY
505
15.457
43.528
39.808
1.00
17.31


ATOM
3501
N
SER
506
17.547
44.088
39.185
1.00
15.04


ATOM
3502
CA
SER
506
17.324
43.793
37.770
1.00
15.72


ATOM
3503
CB
SER
506
18.498
44.294
36.925
1.00
15.59


ATOM
3504
OG
SER
506
18.587
45.701
36.956
1.00
22.52


ATOM
3505
C
SER
506
17.167
42.292
37.541
1.00
15.40


ATOM
3506
O
SER
506
16.505
41.869
36.594
1.00
15.35


ATOM
3507
N
ILE
507
17.797
41.496
38.401
1.00
13.34


ATOM
3508
CA
ILE
507
17.731
40.041
38.303
1.00
13.69


ATOM
3509
CB
ILE
507
19.148
39.426
38.171
1.00
14.13


ATOM
3510
CG2
ILE
507
19.057
37.904
38.086
1.00
11.80


ATOM
3511
CG1
ILE
507
19.858
40.002
36.939
1.00
11.87


ATOM
3512
CD1
ILE
507
21.333
39.646
36.867
1.00
10.97


ATOM
3513
C
ILE
507
17.082
39.496
39.574
1.00
14.19


ATOM
3514
O
ILE
507
17.602
39.698
40.669
1.00
13.99


ATOM
3515
N
THR
508
15.946
38.815
39.428
1.00
13.82


ATOM
3516
CA
THR
508
15.237
38.239
40.573
1.00
13.91


ATOM
3517
CB
THR
508
13.707
38.241
40.364
1.00
14.70


ATOM
3518
OG1
THR
508
13.358
37.257
39.381
1.00
15.53


ATOM
3519
CG2
THR
508
13.232
39.606
39.894
1.00
13.66


ATOM
3520
C
THR
508
15.678
36.794
40.736
1.00
14.81


ATOM
3521
O
THR
508
16.327
36.241
39.846
1.00
11.64


ATOM
3522
N
LYS
509
15.310
36.176
41.858
1.00
15.94


ATOM
3523
CA
LYS
509
15.694
34.790
42.106
1.00
17.89


ATOM
3524
CB
LYS
509
15.249
34.334
43.502
1.00
18.63


ATOM
3525
CG
LYS
509
13.769
33.992
43.637
1.00
20.95


ATOM
3526
CD
LYS
509
13.463
33.460
45.033
1.00
21.83


ATOM
3527
CE
LYS
509
11.988
33.146
45.204
1.00
23.26


ATOM
3528
NZ
LYS
509
11.687
32.724
46.600
1.00
23.66


ATOM
3529
C
LYS
509
15.109
33.854
41.057
1.00
18.81


ATOM
3530
O
LYS
509
15.497
32.690
40.979
1.00
20.85


ATOM
3531
N
GLU
510
14.171
34.353
40.257
1.00
18.47


ATOM
3532
CA
GLU
510
13.574
33.535
39.206
1.00
20.76


ATOM
3533
CB
GLU
510
12.282
34.163
38.696
1.00
22.98


ATOM
3534
CG
GLU
510
11.274
34.507
39.761
1.00
33.06


ATOM
3535
CD
GLU
510
10.120
35.306
39.196
1.00
36.53


ATOM
3536
OE1
GLU
510
10.366
36.379
38.599
1.00
39.46


ATOM
3537
OE2
GLU
510
8.971
34.859
39.349
1.00
39.85


ATOM
3538
C
GLU
510
14.536
33.437
38.025
1.00
20.25


ATOM
3539
O
GLU
510
14.526
32.452
37.283
1.00
19.03


ATOM
3540
N
ASN
511
15.365
34.465
37.862
1.00
17.63


ATOM
3541
CA
ASN
511
16.298
34.522
36.746
1.00
17.82


ATOM
3542
CB
ASN
511
15.984
35.756
35.891
1.00
19.14


ATOM
3543
CG
ASN
511
14.541
35.779
35.410
1.00
25.49


ATOM
3544
OD1
ASN
511
14.080
34.843
34.756
1.00
27.61


ATOM
3545
ND2
ASN
511
13.819
36.848
35.734
1.00
24.85


ATOM
3546
C
ASN
511
17.785
34.510
37.111
1.00
16.09


ATOM
3547
O
ASN
511
18.630
34.792
36.260
1.00
13.99


ATOM
3548
N
TYR
512
18.102
34.187
38.363
1.00
12.83


ATOM
3549
CA
TYR
512
19.494
34.128
38.804
1.00
11.97


ATOM
3550
CB
TYR
512
19.617
33.360
40.120
1.00
12.23


ATOM
3551
CG
TYR
512
19.249
34.090
41.390
1.00
12.34


ATOM
3552
CD1
TYR
512
19.016
33.370
42.561
1.00
13.62


ATOM
3553
CE1
TYR
512
18.717
34.007
43.755
1.00
14.61


ATOM
3554
CD2
TYR
512
19.172
35.484
41.446
1.00
12.45


ATOM
3555
CE2
TYR
512
18.872
36.137
42.651
1.00
13.77


ATOM
3556
CZ
TYR
512
18.647
35.381
43.799
1.00
13.86


ATOM
3557
OH
TYR
512
18.358
35.977
45.004
1.00
17.23


ATOM
3558
C
TYR
512
20.385
33.396
37.798
1.00
12.56


ATOM
3559
O
TYR
512
21.299
33.970
37.199
1.00
10.13


ATOM
3560
N
ASN
513
20.105
32.108
37.639
1.00
11.91


ATOM
3561
CA
ASN
513
20.894
31.247
36.776
1.00
11.83


ATOM
3562
CB
ASN
513
20.482
29.792
36.985
1.00
11.58


ATOM
3563
CG
ASN
513
21.672
28.859
36.980
1.00
11.83


ATOM
3564
OD1
ASN
513
22.613
29.054
37.743
1.00
14.77


ATOM
3565
ND2
ASN
513
21.644
27.848
36.118
1.00
7.41


ATOM
3566
C
ASN
513
20.872
31.572
35.299
1.00
12.10


ATOM
3567
O
ASN
513
21.918
31.536
34.637
1.00
10.25


ATOM
3568
N
GLN
514
19.690
31.882
34.775
1.00
11.72


ATOM
3569
CA
GLN
514
19.568
32.194
33.362
1.00
14.72


ATOM
3570
CB
GLN
514
18.089
32.356
32.979
1.00
17.46


ATOM
3571
CG
GLN
514
17.260
31.066
33.144
1.00
23.70


ATOM
3572
CD
GLN
514
16.576
30.934
34.510
1.00
25.81


ATOM
3573
OE1
GLN
514
17.121
31.322
35.552
1.00
21.12


ATOM
3574
NE2
GLN
514
15.375
30.363
34.502
1.00
29.42


ATOM
3575
C
GLN
514
20.369
33.446
32.994
1.00
14.10


ATOM
3576
O
GLN
514
20.973
33.511
31.918
1.00
13.15


ATOM
3577
N
GLU
515
20.391
34.432
33.887
1.00
13.07


ATOM
3578
CA
GLU
515
21.136
35.660
33.615
1.00
12.06


ATOM
3579
CB
GLU
515
20.656
36.802
34.519
1.00
16.07


ATOM
3580
CG
GLU
515
19.244
37.290
34.190
1.00
18.59


ATOM
3581
CD
GLU
515
19.084
37.659
32.719
1.00
24.12


ATOM
3582
OE1
GLU
515
19.829
38.544
32.235
1.00
24.75


ATOM
3583
OE2
GLU
515
18.214
37.060
32.046
1.00
26.20


ATOM
3584
C
GLU
515
22.626
35.420
33.805
1.00
10.94


ATOM
3585
O
GLU
515
23.454
36.089
33.190
1.00
12.49


ATOM
3586
N
TRP
516
22.970
34.466
34.660
1.00
9.41


ATOM
3587
CA
TRP
516
24.374
34.135
34.873
1.00
9.43


ATOM
3588
CB
TRP
516
24.513
33.135
36.030
1.00
9.02


ATOM
3589
CG
TRP
516
25.865
32.477
36.148
1.00
10.43


ATOM
3590
CD2
TRP
516
27.026
33.004
36.804
1.00
10.48


ATOM
3591
CE2
TRP
516
28.037
32.019
36.718
1.00
10.91


ATOM
3592
CE3
TRP
516
27.311
34.210
37.458
1.00
10.58


ATOM
3593
CD1
TRP
516
26.212
31.235
35.697
1.00
11.18


ATOM
3594
NE1
TRP
516
27.514
30.951
36.038
1.00
12.53


ATOM
3595
CZ2
TRP
516
29.314
32.201
37.263
1.00
11.44


ATOM
3596
CZ3
TRP
516
28.583
34.393
38.002
1.00
11.75


ATOM
3597
CH2
TRP
516
29.568
33.390
37.899
1.00
11.65


ATOM
3598
C
TRP
516
24.912
33.542
33.575
1.00
9.00


ATOM
3599
O
TRP
516
25.971
33.943
33.088
1.00
10.05


ATOM
3600
N
TRP
517
24.167
32.605
32.993
1.00
9.12


ATOM
3601
CA
TRP
517
24.609
31.995
31.746
1.00
9.56


ATOM
3602
CB
TRP
517
23.855
30.689
31.497
1.00
8.95


ATOM
3603
CG
TRP
517
24.458
29.614
32.334
1.00
7.44


ATOM
3604
CD2
TRP
517
25.729
28.992
32.118
1.00
8.27


ATOM
3605
CE2
TRP
517
25.994
28.176
33.240
1.00
7.79


ATOM
3606
CE3
TRP
517
26.678
29.052
31.084
1.00
9.26


ATOM
3607
CD1
TRP
517
24.007
29.154
33.540
1.00
6.42


ATOM
3608
NE1
TRP
517
24.927
28.292
34.093
1.00
8.16


ATOM
3609
CZ2
TRP
517
27.166
27.424
33.359
1.00
9.24


ATOM
3610
CZ3
TRP
517
27.848
28.301
31.204
1.00
10.00


ATOM
3611
CH2
TRP
517
28.080
27.500
32.333
1.00
8.75


ATOM
3612
C
TRP
517
24.549
32.927
30.538
1.00
10.22


ATOM
3613
O
TRP
517
25.321
32.769
29.593
1.00
10.24


ATOM
3614
N
SER
518
23.654
33.908
30.566
1.00
11.02


ATOM
3615
CA
SER
518
23.588
34.863
29.467
1.00
13.01


ATOM
3616
CB
SER
518
22.407
35.823
29.631
1.00
14.72


ATOM
3617
OG
SER
518
21.187
35.175
29.332
1.00
22.10


ATOM
3618
C
SER
518
24.887
35.663
29.462
1.00
11.80


ATOM
3619
O
SER
518
25.375
36.072
28.405
1.00
10.96


ATOM
3620
N
LEU
519
25.441
35.889
30.650
1.00
10.02


ATOM
3621
CA
LEU
519
26.685
36.638
30.763
1.00
11.52


ATOM
3622
CB
LEU
519
26.828
37.219
32.173
1.00
11.07


ATOM
3623
CG
LEU
519
25.804
38.316
32.491
1.00
13.05


ATOM
3624
CD1
LEU
519
25.934
38.733
33.949
1.00
12.54


ATOM
3625
CD2
LEU
519
26.017
39.504
31.570
1.00
13.76


ATOM
3626
C
LEU
519
27.876
35.744
30.430
1.00
11.25


ATOM
3627
O
LEU
519
28.826
36.179
29.773
1.00
10.48


ATOM
3628
N
ARG
520
27.817
34.497
30.887
1.00
10.34


ATOM
3629
CA
ARG
520
28.875
33.529
30.611
1.00
11.93


ATOM
3630
CB
ARG
520
28.493
32.160
31.186
1.00
10.95


ATOM
3631
CG
ARG
520
28.568
32.095
32.713
1.00
10.19


ATOM
3632
CD
ARG
520
29.973
31.757
33.176
1.00
9.98


ATOM
3633
NE
ARG
520
30.136
30.320
33.403
1.00
11.36


ATOM
3634
CZ
ARG
520
31.303
29.717
33.615
1.00
12.10


ATOM
3635
NH1
ARG
520
31.342
28.404
33.827
1.00
10.85


ATOM
3636
NH2
ARG
520
32.432
30.419
33.595
1.00
7.63


ATOM
3637
C
ARG
520
29.062
33.433
29.097
1.00
12.63


ATOM
3638
O
ARG
520
30.186
33.326
28.595
1.00
11.60


ATOM
3639
N
LEU
521
27.944
33.472
28.378
1.00
11.30


ATOM
3640
CA
LEU
521
27.957
33.406
26.924
1.00
11.63


ATOM
3641
CB
LEU
521
26.545
33.129
26.387
1.00
11.64


ATOM
3642
CG
LEU
521
26.436
33.222
24.858
1.00
14.85


ATOM
3643
CD1
LEU
521
27.324
32.153
24.237
1.00
11.78


ATOM
3644
CD2
LEU
521
24.988
33.049
24.405
1.00
13.95


ATOM
3645
C
LEU
521
28.460
34.717
26.328
1.00
10.66


ATOM
3646
O
LEU
521
29.408
34.738
25.554
1.00
12.28


ATOM
3647
N
LYS
522
27.813
35.811
26.703
1.00
12.13


ATOM
3648
CA
LYS
522
28.159
37.127
26.180
1.00
14.27


ATOM
3649
CB
LYS
522
27.267
38.191
26.826
1.00
16.64


ATOM
3650
CG
LYS
522
27.524
39.608
26.333
1.00
19.99


ATOM
3651
CD
LYS
522
26.592
40.589
27.029
1.00
21.89


ATOM
3652
CE
LYS
522
26.868
42.022
26.602
1.00
24.69


ATOM
3653
NZ
LYS
522
25.926
42.969
27.263
1.00
26.36


ATOM
3654
C
LYS
522
29.620
37.528
26.354
1.00
13.91


ATOM
3655
O
LYS
522
30.242
38.026
25.418
1.00
13.31


ATOM
3656
N
TYR
523
30.165
37.314
27.547
1.00
12.72


ATOM
3657
CA
TYR
523
31.544
37.699
27.820
1.00
13.45


ATOM
3658
CB
TYR
523
31.648
38.236
29.254
1.00
14.60


ATOM
3659
CG
TYR
523
30.942
39.563
29.417
1.00
17.65


ATOM
3660
CD1
TYR
523
29.840
39.699
30.259
1.00
19.64


ATOM
3661
CE1
TYR
523
29.146
40.916
30.347
1.00
20.74


ATOM
3662
CD2
TYR
523
31.340
40.675
28.671
1.00
20.48


ATOM
3663
CE2
TYR
523
30.662
41.880
28.752
1.00
20.67


ATOM
3664
CZ
TYR
523
29.567
41.994
29.587
1.00
21.24


ATOM
3665
OH
TYR
523
28.890
43.192
29.642
1.00
27.03


ATOM
3666
C
TYR
523
32.604
36.628
27.576
1.00
13.38


ATOM
3667
O
TYR
523
33.616
36.899
26.930
1.00
12.98


ATOM
3668
N
GLN
524
32.378
35.416
28.072
1.00
11.98


ATOM
3669
CA
GLN
524
33.355
34.336
27.891
1.00
11.74


ATOM
3670
CB
GLN
524
33.367
33.425
29.114
1.00
11.09


ATOM
3671
CG
GLN
524
34.010
34.009
30.338
1.00
9.28


ATOM
3672
CD
GLN
524
34.003
33.021
31.476
1.00
11.02


ATOM
3673
OE1
GLN
524
32.979
32.832
32.135
1.00
12.58


ATOM
3674
NE2
GLN
524
35.138
32.356
31.696
1.00
7.73


ATOM
3675
C
GLN
524
33.145
33.459
26.661
1.00
9.96


ATOM
3676
O
GLN
524
34.057
32.746
26.244
1.00
9.58


ATOM
3677
N
GLY
525
31.950
33.492
26.085
1.00
11.25


ATOM
3678
CA
GLY
525
31.684
32.655
24.927
1.00
10.07


ATOM
3679
C
GLY
525
31.639
31.190
25.332
1.00
11.60


ATOM
3680
O
GLY
525
32.148
30.316
24.623
1.00
12.24


ATOM
3681
N
LEU
526
31.044
30.921
26.489
1.00
9.03


ATOM
3682
CA
LEU
526
30.928
29.554
26.984
1.00
9.89


ATOM
3683
CB
LEU
526
31.560
29.421
28.374
1.00
9.34


ATOM
3684
CG
LEU
526
33.030
29.805
28.536
1.00
9.90


ATOM
3685
CD1
LEU
526
33.426
29.727
30.015
1.00
9.26


ATOM
3686
CD2
LEU
526
33.889
28.888
27.687
1.00
8.55


ATOM
3687
C
LEU
526
29.470
29.146
27.082
1.00
11.13


ATOM
3688
O
LEU
526
28.580
29.998
27.174
1.00
11.49


ATOM
3689
N
CYS
527
29.235
27.838
27.051
1.00
10.63


ATOM
3690
CA
CYS
527
27.894
27.288
27.177
1.00
11.97


ATOM
3691
CB
CYS
527
27.352
26.801
25.815
1.00
10.95


ATOM
3692
SG
CYS
527
28.394
25.617
24.900
1.00
18.23


ATOM
3693
C
CYS
527
27.936
26.137
28.173
1.00
10.37


ATOM
3694
O
CYS
527
28.964
25.482
28.346
1.00
10.79


ATOM
3695
N
PRO
528
26.825
25.900
28.876
1.00
11.53


ATOM
3696
CD
PRO
528
25.563
26.667
28.912
1.00
11.52


ATOM
3697
CA
PRO
528
26.818
24.800
29.844
1.00
11.48


ATOM
3698
CB
PRO
528
25.578
25.095
30.689
1.00
10.83


ATOM
3699
CG
PRO
528
24.638
25.744
29.689
1.00
12.92


ATOM
3700
C
PRO
528
26.727
23.472
29.091
1.00
12.66


ATOM
3701
O
PRO
528
25.890
23.317
28.199
1.00
12.63


ATOM
3702
N
PRO
529
27.599
22.504
29.426
1.00
11.66


ATOM
3703
CD
PRO
529
28.616
22.533
30.490
1.00
13.05


ATOM
3704
CA
PRO
529
27.585
21.199
28.756
1.00
13.58


ATOM
3705
CB
PRO
529
28.801
20.496
29.353
1.00
13.06


ATOM
3706
CG
PRO
529
28.864
21.064
30.732
1.00
12.29


ATOM
3707
C
PRO
529
26.279
20.448
29.008
1.00
14.96


ATOM
3708
O
PRO
529
25.888
19.587
28.227
1.00
15.87


ATOM
3709
N
VAL
530
25.613
20.787
30.108
1.00
14.85


ATOM
3710
CA
VAL
530
24.339
20.178
30.463
1.00
16.23


ATOM
3711
CB
VAL
530
24.449
19.366
31.779
1.00
17.35


ATOM
3712
CG1
VAL
530
23.070
19.037
32.314
1.00
17.95


ATOM
3713
CG2
VAL
530
25.222
18.084
31.525
1.00
18.24


ATOM
3714
C
VAL
530
23.326
21.306
30.642
1.00
16.73


ATOM
3715
O
VAL
530
23.589
22.282
31.344
1.00
16.65


ATOM
3716
N
PRO
531
22.156
21.198
29.996
1.00
16.87


ATOM
3717
CD
PRO
531
21.626
20.094
29.180
1.00
18.50


ATOM
3718
CA
PRO
531
21.165
22.269
30.149
1.00
17.92


ATOM
3719
CB
PRO
531
19.994
21.785
29.292
1.00
19.57


ATOM
3720
CG
PRO
531
20.136
20.284
29.328
1.00
21.45


ATOM
3721
C
PRO
531
20.796
22.473
31.617
1.00
18.39


ATOM
3722
O
PRO
531
20.591
21.510
32.361
1.00
16.67


ATOM
3723
N
ARG
532
20.735
23.732
32.039
1.00
17.31


ATOM
3724
CA
ARG
532
20.406
24.037
33.423
1.00
18.29


ATOM
3725
CB
ARG
532
20.853
25.460
33.770
1.00
16.22


ATOM
3726
CG
ARG
532
22.199
25.856
33.165
1.00
15.05


ATOM
3727
CD
ARG
532
23.254
24.770
33.337
1.00
15.19


ATOM
3728
NE
ARG
532
23.590
24.508
34.735
1.00
14.35


ATOM
3729
CZ
ARG
532
23.800
23.293
35.228
1.00
15.95


ATOM
3730
NH1
ARG
532
23.698
22.228
34.433
1.00
13.26


ATOM
3731
NH2
ARG
532
24.127
23.138
36.506
1.00
12.05


ATOM
3732
C
ARG
532
18.906
23.883
33.650
1.00
20.23


ATOM
3733
O
ARG
532
18.105
24.076
32.733
1.00
19.63


ATOM
3734
N
THR
533
18.530
23.532
34.876
1.00
21.65


ATOM
3735
CA
THR
533
17.124
23.340
35.220
1.00
23.17


ATOM
3736
CB
THR
533
16.819
21.857
35.519
1.00
24.29


ATOM
3737
OG1
THR
533
17.679
21.393
36.570
1.00
25.97


ATOM
3738
CG2
THR
533
17.031
21.006
34.277
1.00
25.60


ATOM
3739
C
THR
533
16.753
24.153
36.447
1.00
23.60


ATOM
3740
O
THR
533
17.629
24.635
37.171
1.00
21.92


ATOM
3741
N
GLN
534
15.452
24.300
36.681
1.00
24.71


ATOM
3742
CA
GLN
534
14.973
25.052
37.832
1.00
26.41


ATOM
3743
CB
GLN
534
13.440
25.044
37.872
1.00
28.54


ATOM
3744
CG
GLN
534
12.845
25.925
38.964
1.00
33.07


ATOM
3745
CD
GLN
534
12.569
25.166
40.249
1.00
36.01


ATOM
3746
OE1
GLN
534
13.114
24.084
40.475
1.00
38.09


ATOM
3747
NE2
GLN
534
11.722
25.735
41.104
1.00
36.23


ATOM
3748
C
GLN
534
15.550
24.404
39.087
1.00
25.91


ATOM
3749
O
GLN
534
15.444
23.192
39.279
1.00
28.56


ATOM
3750
N
GLY
535
16.173
25.211
39.936
1.00
24.41


ATOM
3751
CA
GLY
535
16.775
24.673
41.140
1.00
20.69


ATOM
3752
C
GLY
535
18.281
24.852
41.105
1.00
18.98


ATOM
3753
O
GLY
535
18.934
24.861
42.146
1.00
20.39


ATOM
3754
N
ASP
536
18.842
24.986
39.906
1.00
16.53


ATOM
3755
CA
ASP
536
20.281
25.186
39.778
1.00
15.72


ATOM
3756
CB
ASP
536
20.761
24.930
38.341
1.00
14.56


ATOM
3757
CG
ASP
536
20.792
23.451
37.980
1.00
15.32


ATOM
3758
OD1
ASP
536
20.996
22.613
38.883
1.00
16.51


ATOM
3759
OD2
ASP
536
20.632
23.131
36.784
1.00
15.49


ATOM
3760
C
ASP
536
20.635
26.620
40.157
1.00
13.62


ATOM
3761
O
ASP
536
19.855
27.539
39.930
1.00
15.72


ATOM
3762
N
PHE
537
21.809
26.794
40.747
1.00
12.29


ATOM
3763
CA
PHE
537
22.308
28.109
41.139
1.00
11.39


ATOM
3764
CB
PHE
537
21.913
28.443
42.583
1.00
10.12


ATOM
3765
CG
PHE
537
22.366
29.807
43.042
1.00
9.09


ATOM
3766
CD1
PHE
537
22.014
30.950
42.335
1.00
9.35


ATOM
3767
CD2
PHE
537
23.151
29.943
44.189
1.00
12.40


ATOM
3768
CE1
PHE
537
22.433
32.218
42.759
1.00
12.30


ATOM
3769
CE2
PHE
537
23.578
31.205
44.627
1.00
11.45


ATOM
3770
CZ
PHE
537
23.217
32.344
43.908
1.00
12.12


ATOM
3771
C
PHE
537
23.817
27.983
41.008
1.00
9.37


ATOM
3772
O
PHE
537
24.548
27.889
41.991
1.00
7.21


ATOM
3773
N
ASP
538
24.266
27.956
39.762
1.00
11.11


ATOM
3774
CA
ASP
538
25.675
27.811
39.461
1.00
10.38


ATOM
3775
CB
ASP
538
25.853
27.736
37.944
1.00
10.80


ATOM
3776
CG
ASP
538
25.031
26.605
37.329
1.00
12.13


ATOM
3777
OD1
ASP
538
24.925
25.533
37.965
1.00
11.88


ATOM
3778
OD2
ASP
538
24.491
26.778
36.220
1.00
13.46


ATOM
3779
C
ASP
538
26.567
28.882
40.095
1.00
10.52


ATOM
3780
O
ASP
538
27.694
28.590
40.489
1.00
11.65


ATOM
3781
N
PRO
539
26.079
30.132
40.219
1.00
10.22


ATOM
3782
CD
PRO
539
24.848
30.756
39.699
1.00
9.12


ATOM
3783
CA
PRO
539
26.951
31.138
40.841
1.00
10.73


ATOM
3784
CB
PRO
539
26.076
32.390
40.868
1.00
9.39


ATOM
3785
CG
PRO
539
25.233
32.228
39.636
1.00
11.07


ATOM
3786
C
PRO
539
27.367
30.710
42.254
1.00
11.37


ATOM
3787
O
PRO
539
28.469
31.021
42.716
1.00
11.84


ATOM
3788
N
GLY
540
26.472
30.001
42.935
1.00
10.64


ATOM
3789
CA
GLY
540
26.762
29.551
44.287
1.00
12.15


ATOM
3790
C
GLY
540
27.897
28.547
44.348
1.00
11.90


ATOM
3791
O
GLY
540
28.416
28.254
45.427
1.00
11.97


ATOM
3792
N
ALA
541
28.285
28.022
43.189
1.00
11.60


ATOM
3793
CA
ALA
541
29.370
27.048
43.107
1.00
11.56


ATOM
3794
CB
ALA
541
29.133
26.093
41.931
1.00
13.00


ATOM
3795
C
ALA
541
30.737
27.725
42.965
1.00
11.57


ATOM
3796
O
ALA
541
31.753
27.057
42.760
1.00
11.83


ATOM
3797
N
LYS
542
30.752
29.052
43.064
1.00
11.43


ATOM
3798
CA
LYS
542
31.992
29.824
42.984
1.00
11.78


ATOM
3799
CB
LYS
542
31.891
30.884
41.878
1.00
10.91


ATOM
3800
CG
LYS
542
33.109
31.805
41.772
1.00
8.80


ATOM
3801
CD
LYS
542
34.399
31.022
41.509
1.00
8.48


ATOM
3802
CE
LYS
542
35.618
31.946
41.540
1.00
8.38


ATOM
3803
NZ
LYS
542
36.909
31.210
41.407
1.00
9.81


ATOM
3804
C
LYS
542
32.199
30.484
44.353
1.00
12.26


ATOM
3805
O
LYS
542
31.374
31.280
44.803
1.00
11.13


ATOM
3806
N
PHE
543
33.305
30.137
45.004
1.00
13.11


ATOM
3807
CA
PHE
543
33.637
30.632
46.343
1.00
13.89


ATOM
3808
CB
PHE
543
35.152
30.580
46.561
1.00
13.28


ATOM
3809
CG
PHE
543
35.591
31.133
47.890
1.00
15.40


ATOM
3810
CD1
PHE
543
35.490
30.363
49.048
1.00
14.58


ATOM
3811
CD2
PHE
543
36.082
32.435
47.990
1.00
13.56


ATOM
3812
CE1
PHE
543
35.873
30.883
50.289
1.00
12.64


ATOM
3813
CE2
PHE
543
36.465
32.961
49.223
1.00
14.52


ATOM
3814
CZ
PHE
543
36.360
32.182
50.376
1.00
12.86


ATOM
3815
C
PHE
543
33.146
32.028
46.734
1.00
13.70


ATOM
3816
O
PHE
543
32.413
32.183
47.714
1.00
14.70


ATOM
3817
N
HIS
544
33.564
33.035
45.973
1.00
11.85


ATOM
3818
CA
HIS
544
33.230
34.430
46.257
1.00
12.43


ATOM
3819
CB
HIS
544
33.899
35.330
45.216
1.00
11.22


ATOM
3820
CG
HIS
544
35.380
35.131
45.129
1.00
12.39


ATOM
3821
CD2
HIS
544
36.412
35.944
45.460
1.00
10.77


ATOM
3822
ND1
HIS
544
35.945
33.952
44.694
1.00
12.50


ATOM
3823
CE1
HIS
544
37.262
34.045
44.762
1.00
12.26


ATOM
3824
NE2
HIS
544
37.570
35.243
45.223
1.00
12.30


ATOM
3825
C
HIS
544
31.754
34.791
46.389
1.00
12.49


ATOM
3826
O
HIS
544
31.414
35.774
47.053
1.00
13.33


ATOM
3827
N
ILE
545
30.880
34.004
45.773
1.00
12.62


ATOM
3828
CA
ILE
545
29.455
34.278
45.848
1.00
11.82


ATOM
3829
CB
ILE
545
28.685
33.471
44.772
1.00
12.66


ATOM
3830
CG2
ILE
545
27.178
33.627
44.955
1.00
11.69


ATOM
3831
CG1
ILE
545
29.117
33.943
43.380
1.00
13.17


ATOM
3832
CD1
ILE
545
28.898
35.423
43.130
1.00
13.67


ATOM
3833
C
ILE
545
28.926
33.980
47.251
1.00
13.02


ATOM
3834
O
ILE
545
28.437
34.880
47.933
1.00
12.86


ATOM
3835
N
PRO
546
29.021
32.719
47.712
1.00
12.59


ATOM
3836
CD
PRO
546
29.404
31.462
47.045
1.00
10.20


ATOM
3837
CA
PRO
546
28.511
32.463
49.064
1.00
11.85


ATOM
3838
CB
PRO
546
28.527
30.932
49.162
1.00
14.53


ATOM
3839
CG
PRO
546
29.629
30.530
48.217
1.00
11.49


ATOM
3840
C
PRO
546
29.346
33.146
50.154
1.00
13.09


ATOM
3841
O
PRO
546
28.848
33.420
51.248
1.00
11.43


ATOM
3842
N
SER
547
30.611
33.433
49.850
1.00
11.87


ATOM
3843
CA
SER
547
31.488
34.090
50.817
1.00
12.43


ATOM
3844
CB
SER
547
32.950
33.734
50.550
1.00
14.52


ATOM
3845
OG
SER
547
33.188
32.370
50.842
1.00
18.88


ATOM
3846
C
SER
547
31.332
35.601
50.811
1.00
10.80


ATOM
3847
O
SER
547
31.946
36.294
51.617
1.00
10.64


ATOM
3848
N
SER
548
30.515
36.105
49.891
1.00
11.41


ATOM
3849
CA
SER
548
30.259
37.538
49.777
1.00
11.67


ATOM
3850
CB
SER
548
29.419
38.020
50.968
1.00
12.24


ATOM
3851
OG
SER
548
28.977
39.360
50.781
1.00
11.61


ATOM
3852
C
SER
548
31.537
38.380
49.669
1.00
13.36


ATOM
3853
O
SER
548
31.711
39.366
50.396
1.00
13.15


ATOM
3854
N
VAL
549
32.430
37.978
48.768
1.00
11.75


ATOM
3855
CA
VAL
549
33.672
38.714
48.529
1.00
11.24


ATOM
3856
CB
VAL
549
34.911
37.786
48.533
1.00
11.58


ATOM
3857
CG1
VAL
549
36.169
38.594
48.199
1.00
10.79


ATOM
3858
CG2
VAL
549
35.058
37.105
49.888
1.00
12.34


ATOM
3859
C
VAL
549
33.550
39.347
47.139
1.00
9.01


ATOM
3860
O
VAL
549
33.356
38.637
46.149
1.00
9.01


ATOM
3861
N
PRO
550
33.651
40.687
47.049
1.00
7.69


ATOM
3862
CD
PRO
550
33.852
41.644
48.152
1.00
8.15


ATOM
3863
CA
PRO
550
33.547
41.388
45.757
1.00
9.25


ATOM
3864
CB
PRO
550
33.846
42.841
46.127
1.00
8.76


ATOM
3865
CG
PRO
550
33.325
42.934
47.551
1.00
8.40


ATOM
3866
C
PRO
550
34.546
40.819
44.747
1.00
8.58


ATOM
3867
O
PRO
550
35.645
40.411
45.122
1.00
8.68


ATOM
3868
N
TYR
551
34.179
40.813
43.469
1.00
8.90


ATOM
3869
CA
TYR
551
35.050
40.234
42.452
1.00
8.19


ATOM
3870
CB
TYR
551
34.282
39.168
41.661
1.00
8.98


ATOM
3871
CG
TYR
551
35.155
38.019
41.221
1.00
8.00


ATOM
3872
CD1
TYR
551
35.496
37.008
42.119
1.00
7.60


ATOM
3873
CE1
TYR
551
36.367
35.985
41.759
1.00
8.68


ATOM
3874
CD2
TYR
551
35.705
37.978
39.935
1.00
8.09


ATOM
3875
CE2
TYR
551
36.589
36.948
39.562
1.00
8.21


ATOM
3876
CZ
TYR
551
36.913
35.960
40.486
1.00
8.67


ATOM
3877
OH
TYR
551
37.794
34.955
40.160
1.00
9.65


ATOM
3878
C
TYR
551
35.706
41.182
41.452
1.00
9.16


ATOM
3879
O
TYR
551
36.728
40.839
40.865
1.00
9.22


ATOM
3880
N
ILE
552
35.124
42.358
41.243
1.00
8.84


ATOM
3881
CA
ILE
552
35.676
43.299
40.275
1.00
9.21


ATOM
3882
CB
ILE
552
34.790
44.576
40.189
1.00
9.04


ATOM
3883
CG2
ILE
552
35.055
45.494
41.365
1.00
9.74


ATOM
3884
CG1
ILE
552
35.028
45.280
38.851
1.00
8.56


ATOM
3885
CD1
ILE
552
34.587
44.457
37.637
1.00
5.07


ATOM
3886
C
ILE
552
37.141
43.652
40.565
1.00
10.06


ATOM
3887
O
ILE
552
37.892
44.025
39.664
1.00
11.40


ATOM
3888
N
ARG
553
37.549
43.508
41.821
1.00
10.58


ATOM
3889
CA
ARG
553
38.928
43.775
42.217
1.00
9.70


ATOM
3890
CB
ARG
553
39.106
43.467
43.708
1.00
10.44


ATOM
3891
CG
ARG
553
38.642
42.058
44.103
1.00
11.05


ATOM
3892
CD
ARG
553
38.629
41.861
45.620
1.00
10.48


ATOM
3893
NE
ARG
553
37.815
42.881
46.274
1.00
9.50


ATOM
3894
CZ
ARG
553
37.562
42.928
47.577
1.00
9.87


ATOM
3895
NH1
ARG
553
38.059
42.002
48.389
1.00
9.94


ATOM
3896
NH2
ARG
553
36.816
43.909
48.071
1.00
9.97


ATOM
3897
C
ARG
553
39.910
42.920
41.396
1.00
10.71


ATOM
3898
O
ARG
553
41.049
43.331
41.151
1.00
9.61


ATOM
3899
N
TYR
554
39.468
41.739
40.967
1.00
8.53


ATOM
3900
CA
TYR
554
40.334
40.844
40.195
1.00
10.58


ATOM
3901
CB
TYR
554
39.815
39.401
40.264
1.00
9.50


ATOM
3902
CG
TYR
554
39.759
38.865
41.679
1.00
10.20


ATOM
3903
CD1
TYR
554
38.534
38.602
42.297
1.00
9.83


ATOM
3904
CE1
TYR
554
38.471
38.161
43.620
1.00
9.58


ATOM
3905
CD2
TYR
554
40.930
38.670
42.421
1.00
9.15


ATOM
3906
CE2
TYR
554
40.881
38.229
43.747
1.00
8.88


ATOM
3907
CZ
TYR
554
39.645
37.977
44.339
1.00
10.44


ATOM
3908
OH
TYR
554
39.572
37.561
45.648
1.00
8.38


ATOM
3909
C
TYR
554
40.472
41.286
38.746
1.00
10.64


ATOM
3910
O
TYR
554
41.518
41.083
38.122
1.00
11.41


ATOM
3911
N
PHE
555
39.414
41.884
38.209
1.00
10.46


ATOM
3912
CA
PHE
555
39.452
42.393
36.842
1.00
10.84


ATOM
3913
CB
PHE
555
38.060
42.855
36.400
1.00
10.26


ATOM
3914
CG
PHE
555
38.046
43.526
35.061
1.00
10.17


ATOM
3915
CD1
PHE
555
38.027
42.776
33.889
1.00
11.11


ATOM
3916
CD2
PHE
555
38.081
44.911
34.968
1.00
11.00


ATOM
3917
CE1
PHE
555
38.044
43.402
32.641
1.00
10.56


ATOM
3918
CE2
PHE
555
38.101
45.547
33.723
1.00
11.95


ATOM
3919
CZ
PHE
555
38.083
44.792
32.560
1.00
10.41


ATOM
3920
C
PHE
555
40.417
43.586
36.850
1.00
10.22


ATOM
3921
O
PHE
555
41.309
43.689
36.007
1.00
9.16


ATOM
3922
N
VAL
556
40.225
44.483
37.810
1.00
8.84


ATOM
3923
CA
VAL
556
41.083
45.652
37.947
1.00
10.41


ATOM
3924
CB
VAL
556
40.657
46.515
39.163
1.00
11.27


ATOM
3925
CG1
VAL
556
41.651
47.663
39.377
1.00
11.42


ATOM
3926
CG2
VAL
556
39.256
47.074
38.934
1.00
10.95


ATOM
3927
C
VAL
556
42.530
45.183
38.135
1.00
10.85


ATOM
3928
O
VAL
556
43.448
45.679
37.485
1.00
9.24


ATOM
3929
N
SER
557
42.722
44.213
39.021
1.00
10.92


ATOM
3930
CA
SER
557
44.055
43.681
39.283
1.00
12.23


ATOM
3931
CB
SER
557
43.986
42.547
40.311
1.00
12.25


ATOM
3932
OG
SER
557
45.242
41.895
40.418
1.00
11.90


ATOM
3933
C
SER
557
44.781
43.167
38.042
1.00
10.88


ATOM
3934
O
SER
557
45.944
43.491
37.823
1.00
11.61


ATOM
3935
N
PHE
558
44.108
42.358
37.233
1.00
11.01


ATOM
3936
CA
PHE
558
44.760
41.805
36.054
1.00
12.87


ATOM
3937
CB
PHE
558
43.874
40.728
35.419
1.00
13.39


ATOM
3938
CG
PHE
558
44.053
39.374
36.041
1.00
14.43


ATOM
3939
CD1
PHE
558
43.973
39.217
37.425
1.00
16.42


ATOM
3940
CD2
PHE
558
44.343
38.263
35.254
1.00
14.78


ATOM
3941
CE1
PHE
558
44.185
37.969
38.017
1.00
16.88


ATOM
3942
CE2
PHE
558
44.554
37.016
35.830
1.00
15.76


ATOM
3943
CZ
PHE
558
44.476
36.868
37.218
1.00
17.97


ATOM
3944
C
PHE
558
45.191
42.844
35.032
1.00
13.85


ATOM
3945
O
PHE
558
46.164
42.640
34.308
1.00
12.86


ATOM
3946
N
ILE
559
44.479
43.963
34.979
1.00
14.42


ATOM
3947
CA
ILE
559
44.840
45.028
34.051
1.00
13.66


ATOM
3948
CB
ILE
559
43.677
46.038
33.853
1.00
14.20


ATOM
3949
CG2
ILE
559
44.179
47.274
33.112
1.00
12.67


ATOM
3950
CG1
ILE
559
42.513
45.381
33.098
1.00
15.77


ATOM
3951
CD1
ILE
559
42.788
45.101
31.635
1.00
17.17


ATOM
3952
C
ILE
559
46.039
45.796
34.611
1.00
12.63


ATOM
3953
O
ILE
559
47.080
45.907
33.964
1.00
12.70


ATOM
3954
N
ILE
560
45.892
46.304
35.831
1.00
11.72


ATOM
3955
CA
ILE
560
46.946
47.104
36.441
1.00
10.69


ATOM
3956
CB
ILE
560
46.436
47.844
37.706
1.00
10.54


ATOM
3957
CG2
ILE
560
45.153
48.614
37.370
1.00
8.48


ATOM
3958
CG1
ILE
560
46.206
46.858
38.854
1.00
8.80


ATOM
3959
CD1
ILE
560
45.770
47.529
40.158
1.00
8.36


ATOM
3960
C
ILE
560
48.227
46.355
36.793
1.00
12.09


ATOM
3961
O
ILE
560
49.296
46.962
36.854
1.00
10.94


ATOM
3962
N
GLN
561
48.144
45.049
37.023
1.00
10.67


ATOM
3963
CA
GLN
561
49.364
44.324
37.354
1.00
11.49


ATOM
3964
CB
GLN
561
49.060
42.882
37.778
1.00
10.52


ATOM
3965
CG
GLN
561
48.500
41.975
36.701
1.00
9.92


ATOM
3966
CD
GLN
561
48.154
40.604
37.254
1.00
12.40


ATOM
3967
OE1
GLN
561
48.678
39.589
36.799
1.00
11.82


ATOM
3968
NE2
GLN
561
47.269
40.571
38.250
1.00
10.71


ATOM
3969
C
GLN
561
50.341
44.363
36.176
1.00
11.50


ATOM
3970
O
GLN
561
51.554
44.347
36.372
1.00
11.27


ATOM
3971
N
PHE
562
49.817
44.424
34.953
1.00
11.69


ATOM
3972
CA
PHE
562
50.691
44.503
33.790
1.00
11.21


ATOM
3973
CB
PHE
562
49.956
44.080
32.510
1.00
11.05


ATOM
3974
CG
PHE
562
49.863
42.591
32.352
1.00
11.29


ATOM
3975
CD1
PHE
562
48.793
41.884
32.890
1.00
9.06


ATOM
3976
CD2
PHE
562
50.913
41.880
31.768
1.00
12.56


ATOM
3977
CE1
PHE
562
48.772
40.488
32.858
1.00
12.27


ATOM
3978
CE2
PHE
562
50.903
40.485
31.732
1.00
12.36


ATOM
3979
CZ
PHE
562
49.831
39.787
32.280
1.00
11.90


ATOM
3980
C
PHE
562
51.231
45.925
33.675
1.00
12.75


ATOM
3981
O
PHE
562
52.351
46.140
33.199
1.00
11.93


ATOM
3982
N
GLN
563
50.437
46.897
34.117
1.00
10.72


ATOM
3983
CA
GLN
563
50.891
48.281
34.097
1.00
12.88


ATOM
3984
CB
GLN
563
49.767
49.234
34.519
1.00
11.19


ATOM
3985
CG
GLN
563
48.737
49.532
33.435
1.00
11.49


ATOM
3986
CD
GLN
563
47.675
50.507
33.912
1.00
12.70


ATOM
3987
OE1
GLN
563
46.589
50.107
34.331
1.00
12.32


ATOM
3988
NE2
GLN
563
47.997
51.799
33.872
1.00
11.50


ATOM
3989
C
GLN
563
52.047
48.395
35.092
1.00
12.39


ATOM
3990
O
GLN
563
53.025
49.093
34.839
1.00
13.44


ATOM
3991
N
PHE
564
51.925
47.706
36.225
1.00
11.63


ATOM
3992
CA
PHE
564
52.963
47.740
37.252
1.00
13.10


ATOM
3993
CB
PHE
564
52.464
47.095
38.554
1.00
11.20


ATOM
3994
CG
PHE
564
51.333
47.841
39.221
1.00
12.19


ATOM
3995
CD1
PHE
564
50.907
49.082
38.746
1.00
14.04


ATOM
3996
CD2
PHE
564
50.687
47.294
40.329
1.00
12.60


ATOM
3997
CE1
PHE
564
49.852
49.766
39.365
1.00
13.68


ATOM
3998
CE2
PHE
564
49.634
47.967
40.956
1.00
11.39


ATOM
3999
CZ
PHE
564
49.215
49.203
40.473
1.00
11.65


ATOM
4000
C
PHE
564
54.216
47.013
36.768
1.00
12.91


ATOM
4001
O
PHE
564
55.333
47.480
36.971
1.00
12.87


ATOM
4002
N
HIS
565
54.019
45.865
36.132
1.00
13.20


ATOM
4003
CA
HIS
565
55.121
45.070
35.599
1.00
14.27


ATOM
4004
CB
HIS
565
54.560
43.825
34.906
1.00
12.73


ATOM
4005
CG
HIS
565
55.607
42.908
34.354
1.00
15.74


ATOM
4006
CD2
HIS
565
55.857
42.500
33.086
1.00
12.69


ATOM
4007
ND1
HIS
565
56.545
42.283
35.148
1.00
14.29


ATOM
4008
CE1
HIS
565
57.326
41.532
34.394
1.00
14.80


ATOM
4009
NE2
HIS
565
56.930
41.647
33.138
1.00
14.33


ATOM
4010
C
HIS
565
55.923
45.920
34.600
1.00
14.86


ATOM
4011
O
HIS
565
57.153
45.973
34.652
1.00
14.50


ATOM
4012
N
GLU
566
55.213
46.593
33.702
1.00
13.69


ATOM
4013
CA
GLU
566
55.848
47.443
32.702
1.00
15.17


ATOM
4014
CB
GLU
566
54.778
48.065
31.797
1.00
15.39


ATOM
4015
CG
GLU
566
55.313
48.964
30.695
1.00
15.92


ATOM
4016
CD
GLU
566
54.202
49.652
29.931
1.00
15.19


ATOM
4017
OE1
GLU
566
53.539
50.538
30.505
1.00
17.62


ATOM
4018
OE2
GLU
566
53.980
49.295
28.758
1.00
18.81


ATOM
4019
C
GLU
566
56.695
48.551
33.339
1.00
15.89


ATOM
4020
O
GLU
566
57.859
48.737
32.976
1.00
14.18


ATOM
4021
N
ALA
567
56.112
49.282
34.287
1.00
15.39


ATOM
4022
CA
ALA
567
56.828
50.372
34.948
1.00
16.88


ATOM
4023
CB
ALA
567
55.865
51.183
35.819
1.00
14.89


ATOM
4024
C
ALA
567
58.019
49.897
35.784
1.00
16.62


ATOM
4025
O
ALA
567
59.096
50.488
35.727
1.00
15.99


ATOM
4026
N
LEU
568
57.825
48.833
36.557
1.00
15.41


ATOM
4027
CA
LEU
568
58.893
48.309
37.398
1.00
16.13


ATOM
4028
CB
LEU
568
58.359
47.201
38.314
1.00
17.30


ATOM
4029
CG
LEU
568
57.250
47.612
39.299
1.00
20.05


ATOM
4030
CD1
LEU
568
56.889
46.432
40.190
1.00
18.53


ATOM
4031
CD2
LEU
568
57.711
48.778
40.145
1.00
18.19


ATOM
4032
C
LEU
568
60.048
47.784
36.552
1.00
18.07


ATOM
4033
O
LEU
568
61.214
47.911
36.929
1.00
17.90


ATOM
4034
N
CYS
569
59.720
47.202
35.403
1.00
18.05


ATOM
4035
CA
CYS
569
60.732
46.672
34.502
1.00
18.25


ATOM
4036
C
CYS
569
61.549
47.820
33.923
1.00
20.30


ATOM
4037
O
CYS
569
62.773
47.723
33.798
1.00
20.29


ATOM
4038
CB
CYS
569
60.067
45.860
33.388
1.00
16.73


ATOM
4039
SG
CYS
569
59.390
44.286
34.002
1.00
19.14


ATOM
4040
N
GLN
570
60.868
48.905
33.571
1.00
20.33


ATOM
4041
CA
GLN
570
61.543
50.077
33.035
1.00
23.99


ATOM
4042
CB
GLN
570
60.520
51.120
32.572
1.00
26.88


ATOM
4043
CG
GLN
570
61.128
52.411
32.026
1.00
33.15


ATOM
4044
CD
GLN
570
61.464
53.420
33.112
1.00
38.69


ATOM
4045
OE1
GLN
570
62.144
54.418
32.859
1.00
42.37


ATOM
4046
NE2
GLN
570
60.979
53.172
34.327
1.00
41.47


ATOM
4047
C
GLN
570
62.433
50.659
34.135
1.00
23.86


ATOM
4048
O
GLN
570
63.580
51.019
33.890
1.00
24.65


ATOM
4049
N
ALA
571
61.902
50.730
35.351
1.00
24.19


ATOM
4050
CA
ALA
571
62.656
51.266
36.479
1.00
24.23


ATOM
4051
CB
ALA
571
61.760
51.366
37.707
1.00
22.96


ATOM
4052
C
ALA
571
63.864
50.384
36.783
1.00
25.45


ATOM
4053
O
ALA
571
64.875
50.860
37.305
1.00
25.42


ATOM
4054
N
ALA
572
63.750
49.099
36.459
1.00
24.84


ATOM
4055
CA
ALA
572
64.827
48.147
36.699
1.00
25.13


ATOM
4056
CB
ALA
572
64.254
46.750
36.870
1.00
23.83


ATOM
4057
C
ALA
572
65.863
48.152
35.573
1.00
25.94


ATOM
4058
O
ALA
572
66.867
47.442
35.642
1.00
26.07


ATOM
4059
N
GLY
573
65.609
48.947
34.537
1.00
26.23


ATOM
4060
CA
GLY
573
66.532
49.025
33.419
1.00
27.16


ATOM
4061
C
GLY
573
66.339
47.967
32.344
1.00
28.15


ATOM
4062
O
GLY
573
67.187
47.812
31.460
1.00
27.38


ATOM
4063
N
HIS
574
65.229
47.238
32.400
1.00
28.43


ATOM
4064
CA
HIS
574
64.969
46.204
31.406
1.00
27.36


ATOM
4065
CB
HIS
574
63.768
45.348
31.814
1.00
27.79


ATOM
4066
CG
HIS
574
63.425
44.284
30.818
1.00
27.40


ATOM
4067
CD2
HIS
574
62.483
44.244
29.845
1.00
26.79


ATOM
4068
ND1
HIS
574
64.132
43.105
30.714
1.00
28.45


ATOM
4069
CE1
HIS
574
63.643
42.386
29.720
1.00
27.27


ATOM
4070
NE2
HIS
574
62.642
43.055
29.175
1.00
26.73


ATOM
4071
C
HIS
574
64.702
46.794
30.025
1.00
27.12


ATOM
4072
O
HIS
574
64.038
47.820
29.886
1.00
26.50


ATOM
4073
N
THR
575
65.226
46.130
29.004
1.00
27.68


ATOM
4074
CA
THR
575
65.036
46.562
27.630
1.00
28.87


ATOM
4075
CB
THR
575
66.326
47.153
27.038
1.00
29.42


ATOM
4076
OG1
THR
575
67.310
46.121
26.914
1.00
30.33


ATOM
4077
CG2
THR
575
66.864
48.254
27.942
1.00
30.67


ATOM
4078
C
THR
575
64.640
45.336
26.821
1.00
28.31


ATOM
4079
O
THR
575
64.940
44.204
27.205
1.00
28.82


ATOM
4080
N
GLY
576
63.969
45.560
25.700
1.00
28.44


ATOM
4081
CA
GLY
576
63.539
44.448
24.875
1.00
27.18


ATOM
4082
C
GLY
576
62.119
44.050
25.230
1.00
25.91


ATOM
4083
O
GLY
576
61.465
44.737
26.018
1.00
24.77


ATOM
4084
N
PRO
577
61.619
42.933
24.678
1.00
24.95


ATOM
4085
CD
PRO
577
62.349
41.978
23.827
1.00
23.68


ATOM
4086
CA
PRO
577
60.258
42.457
24.946
1.00
22.59


ATOM
4087
CB
PRO
577
60.259
41.056
24.341
1.00
22.99


ATOM
4088
CG
PRO
577
61.219
41.191
23.196
1.00
24.60


ATOM
4089
C
PRO
577
59.910
42.446
26.431
1.00
21.80


ATOM
4090
O
PRO
577
60.659
41.917
27.254
1.00
19.91


ATOM
4091
N
LEU
578
58.766
43.033
26.762
1.00
20.01


ATOM
4092
CA
LEU
578
58.307
43.099
28.140
1.00
19.37


ATOM
4093
CB
LEU
578
56.978
43.849
28.201
1.00
19.91


ATOM
4094
CG
LEU
578
56.331
44.032
29.575
1.00
20.71


ATOM
4095
CD1
LEU
578
57.289
44.770
30.506
1.00
19.94


ATOM
4096
CD2
LEU
578
55.027
44.807
29.412
1.00
19.01


ATOM
4097
C
LEU
578
58.155
41.723
28.792
1.00
19.24


ATOM
4098
O
LEU
578
58.455
41.558
29.977
1.00
19.94


ATOM
4099
N
HIS
579
57.707
40.731
28.025
1.00
18.28


ATOM
4100
CA
HIS
579
57.506
39.399
28.584
1.00
17.96


ATOM
4101
CB
HIS
579
56.750
38.496
27.598
1.00
17.78


ATOM
4102
CG
HIS
579
57.550
38.091
26.397
1.00
19.87


ATOM
4103
CD2
HIS
579
58.261
36.967
26.140
1.00
19.63


ATOM
4104
ND1
HIS
579
57.660
38.881
25.272
1.00
20.33


ATOM
4105
CE1
HIS
579
58.403
38.259
24.372
1.00
21.49


ATOM
4106
NE2
HIS
579
58.781
37.096
24.873
1.00
21.52


ATOM
4107
C
HIS
579
58.788
38.703
29.038
1.00
18.92


ATOM
4108
O
HIS
579
58.736
37.704
29.753
1.00
18.97


ATOM
4109
N
LYS
580
59.939
39.227
28.628
1.00
19.36


ATOM
4110
CA
LYS
580
61.213
38.633
29.024
1.00
20.72


ATOM
4111
CB
LYS
580
62.249
38.793
27.906
1.00
22.61


ATOM
4112
CG
LYS
580
61.921
38.033
26.637
1.00
26.07


ATOM
4113
CD
LYS
580
63.026
38.210
25.603
1.00
30.62


ATOM
4114
CE
LYS
580
62.691
37.498
24.303
1.00
32.64


ATOM
4115
NZ
LYS
580
63.739
37.735
23.272
1.00
36.23


ATOM
4116
C
LYS
580
61.759
39.261
30.304
1.00
19.60


ATOM
4117
O
LYS
580
62.820
38.868
30.791
1.00
19.03


ATOM
4118
N
CYS
581
61.035
40.231
30.850
1.00
18.42


ATOM
4119
CA
CYS
581
61.481
40.906
32.064
1.00
17.07


ATOM
4120
C
CYS
581
61.314
40.101
33.347
1.00
17.10


ATOM
4121
O
CYS
581
60.304
39.418
33.547
1.00
15.04


ATOM
4122
CB
CYS
581
60.760
42.250
32.216
1.00
18.37


ATOM
4123
SG
CYS
581
60.969
43.013
33.857
1.00
17.47


ATOM
4124
N
ASP
582
62.326
40.198
34.207
1.00
15.09


ATOM
4125
CA
ASP
582
62.349
39.536
35.508
1.00
16.68


ATOM
4126
CB
ASP
582
63.280
38.317
35.483
1.00
17.27


ATOM
4127
CG
ASP
582
63.346
37.599
36.823
1.00
17.46


ATOM
4128
OD1
ASP
582
62.896
38.168
37.840
1.00
20.34


ATOM
4129
OD2
ASP
582
63.863
36.464
36.864
1.00
18.13


ATOM
4130
C
ASP
582
62.905
40.596
36.455
1.00
17.47


ATOM
4131
O
ASP
582
64.090
40.934
36.391
1.00
17.45


ATOM
4132
N
ILE
583
62.053
41.128
37.326
1.00
16.24


ATOM
4133
CA
ILE
583
62.486
42.171
38.250
1.00
15.41


ATOM
4134
CB
ILE
583
61.307
43.072
38.690
1.00
14.68


ATOM
4135
CG2
ILE
583
60.632
43.673
37.470
1.00
14.39


ATOM
4136
CG1
ILE
583
60.311
42.260
39.523
1.00
15.92


ATOM
4137
CD1
ILE
583
59.269
43.108
40.237
1.00
14.64


ATOM
4138
C
ILE
583
63.153
41.641
39.510
1.00
14.69


ATOM
4139
O
ILE
583
63.339
42.393
40.461
1.00
15.92


ATOM
4140
N
TYR
584
63.515
40.361
39.525
1.00
14.71


ATOM
4141
CA
TYR
584
64.159
39.793
40.707
1.00
16.16


ATOM
4142
CB
TYR
584
64.674
38.379
40.435
1.00
17.42


ATOM
4143
CG
TYR
584
65.201
37.707
41.687
1.00
20.19


ATOM
4144
CD1
TYR
584
64.335
37.319
42.710
1.00
19.90


ATOM
4145
CE1
TYR
584
64.818
36.736
43.882
1.00
22.35


ATOM
4146
CD2
TYR
584
66.569
37.496
41.868
1.00
21.27


ATOM
4147
CE2
TYR
584
67.062
36.917
43.040
1.00
21.55


ATOM
4148
CZ
TYR
584
66.182
36.540
44.040
1.00
23.16


ATOM
4149
OH
TYR
584
66.667
35.970
45.197
1.00
24.33


ATOM
4150
C
TYR
584
65.313
40.665
41.203
1.00
17.22


ATOM
4151
O
TYR
584
66.181
41.077
40.430
1.00
15.46


ATOM
4152
N
GLN
585
65.280
40.919
42.511
1.00
19.21


ATOM
4153
CA
GLN
565
66.220
41.732
43.291
1.00
20.56


ATOM
4154
CB
GLN
585
67.547
40.975
43.537
1.00
22.86


ATOM
4155
CG
GLN
585
68.714
41.237
42.615
1.00
25.28


ATOM
4156
CD
GLN
585
70.041
40.759
43.227
1.00
25.98


ATOM
4157
OE1
GLN
585
70.858
41.563
43.688
1.00
27.46


ATOM
4158
NE2
GLN
585
70.246
39.449
43.244
1.00
21.75


ATOM
4159
C
GLN
585
66.473
43.182
42.874
1.00
20.42


ATOM
4160
O
GLN
585
67.461
43.798
43.278
1.00
21.28


ATOM
4161
N
SER
586
65.550
43.745
42.102
1.00
19.19


ATOM
4162
CA
SER
586
65.660
45.139
41.690
1.00
19.32


ATOM
4163
CB
SER
586
64.786
45.414
40.471
1.00
18.80


ATOM
4164
OG
SER
586
64.601
46.811
40.310
1.00
18.57


ATOM
4165
C
SER
586
65.189
46.029
42.843
1.00
19.72


ATOM
4166
O
SER
586
64.024
45.974
43.242
1.00
19.41


ATOM
4167
N
LYS
587
66.089
46.850
43.373
1.00
19.62


ATOM
4168
CA
LYS
587
65.732
47.732
44.478
1.00
19.54


ATOM
4169
CB
LYS
587
66.993
48.220
45.201
1.00
19.75


ATOM
4170
CG
LYS
587
67.817
47.097
45.824
1.00
19.70


ATOM
4171
CD
LYS
587
66.996
46.278
46.807
1.00
19.79


ATOM
4172
CE
LYS
587
67.818
45.169
47.454
1.00
18.62


ATOM
4173
NZ
LYS
587
68.332
44.187
46.455
1.00
17.59


ATOM
4174
C
LYS
587
64.903
48.918
43.998
1.00
18.61


ATOM
4175
O
LYS
587
64.079
49.442
44.746
1.00
18.91


ATOM
4176
N
GLU
588
65.125
49.340
42.756
1.00
17.99


ATOM
4177
CA
GLU
588
64.368
50.453
42.189
1.00
19.42


ATOM
4178
CB
GLU
588
64.886
50.814
40.793
1.00
21.76


ATOM
4179
CG
GLU
588
66.272
51.445
40.746
1.00
27.43


ATOM
4180
CD
GLU
588
67.376
50.476
41.117
1.00
29.76


ATOM
4181
OE1
GLU
588
67.323
49.311
40.666
1.00
30.34


ATOM
4182
OE2
GLU
588
68.304
50.885
41.849
1.00
33.88


ATOM
4183
C
GLU
588
62.898
50.048
42.081
1.00
19.93


ATOM
4184
O
GLU
588
61.995
50.836
42.376
1.00
17.54


ATOM
4185
N
ALA
589
62.669
48.813
41.645
1.00
19.54


ATOM
4186
CA
ALA
589
61.315
48.292
41.503
1.00
19.77


ATOM
4187
CB
ALA
589
61.351
46.904
40.875
1.00
19.22


ATOM
4188
C
ALA
589
60.657
48.231
42.879
1.00
19.77


ATOM
4189
O
ALA
589
59.564
48.756
43.081
1.00
18.88


ATOM
4190
N
GLY
590
61.339
47.596
43.825
1.00
19.84


ATOM
4191
CA
GLY
590
60.802
47.485
45.169
1.00
20.54


ATOM
4192
C
GLY
590
60.463
48.824
45.808
1.00
21.45


ATOM
4193
O
GLY
590
59.471
48.940
46.527
1.00
21.87


ATOM
4194
N
GLN
591
61.274
49.842
45.541
1.00
21.62


ATOM
4195
CA
GLN
591
61.039
51.156
46.125
1.00
23.40


ATOM
4196
CB
GLN
591
62.209
52.093
45.822
1.00
27.20


ATOM
4197
CG
GLN
591
62.105
53.431
46.537
1.00
33.72


ATOM
4198
CD
GLN
591
62.006
53.271
48.049
1.00
37.72


ATOM
4199
OE1
GLN
591
62.942
52.804
48.701
1.00
40.06


ATOM
4200
NE2
GLN
591
60.862
53.650
48.610
1.00
40.38


ATOM
4201
C
GLN
591
59.734
51.797
45.657
1.00
22.75


ATOM
4202
O
GLN
591
59.049
52.458
46.436
1.00
22.38


ATOM
4203
N
ARG
592
59.383
51.612
44.391
1.00
21.41


ATOM
4204
CA
ARG
592
58.141
52.189
43.900
1.00
23.04


ATOM
4205
CB
ARG
592
58.056
52.092
42.380
1.00
24.83


ATOM
4206
CG
ARG
592
59.000
53.041
41.678
1.00
27.16


ATOM
4207
CD
ARG
592
58.672
53.136
40.216
1.00
30.01


ATOM
4208
NE
ARG
592
59.631
53.965
39.500
1.00
30.87


ATOM
4209
CZ
ARG
592
59.574
54.207
38.197
1.00
33.37


ATOM
4210
NH1
ARG
592
58.597
53.680
37.468
1.00
33.76


ATOM
4211
NH2
ARG
592
60.498
54.961
37.620
1.00
33.43


ATOM
4212
C
ARG
592
56.940
51.501
44.529
1.00
22.47


ATOM
4213
O
ARG
592
55.957
52.151
44.884
1.00
23.13


ATOM
4214
N
LEU
593
57.022
50.183
44.670
1.00
20.30


ATOM
4215
CA
LEU
593
55.928
49.439
45.268
1.00
19.74


ATOM
4216
CB
LEU
593
56.173
47.932
45.147
1.00
19.55


ATOM
4217
CG
LEU
593
55.936
47.315
43.765
1.00
21.26


ATOM
4218
CD1
LEU
593
56.137
45.807
43.847
1.00
20.22


ATOM
4219
CD2
LEU
593
54.518
47.639
43.289
1.00
18.77


ATOM
4220
C
LEU
593
55.756
49.819
46.734
1.00
18.89


ATOM
4221
O
LEU
593
54.633
49.946
47.218
1.00
17.61


ATOM
4222
N
ALA
594
56.872
50.003
47.434
1.00
17.55


ATOM
4223
CA
ALA
594
56.827
50.358
48.851
1.00
19.25


ATOM
4224
CB
ALA
594
58.236
50.327
49.449
1.00
17.33


ATOM
4225
C
ALA
594
56.184
51.724
49.091
1.00
18.56


ATOM
4226
O
ALA
594
55.281
51.852
49.914
1.00
19.48


ATOM
4227
N
THR
595
56.647
52.744
48.378
1.00
19.12


ATOM
4228
CA
THR
595
56.091
54.081
48.558
1.00
20.47


ATOM
4229
CB
THR
595
56.754
55.105
47.602
1.00
22.14


ATOM
4230
OG1
THR
595
56.482
54.744
46.242
1.00
27.28


ATOM
4231
CG2
THR
595
58.255
55.134
47.814
1.00
22.28


ATOM
4232
C
THR
595
54.584
54.067
48.306
1.00
20.42


ATOM
4233
O
THR
595
53.823
54.741
49.006
1.00
20.17


ATOM
4234
N
ALA
596
54.158
53.286
47.315
1.00
17.08


ATOM
4235
CA
ALA
596
52.744
53.191
46.972
1.00
15.64


ATOM
4236
CB
ALA
596
52.577
52.497
45.619
1.00
14.14


ATOM
4237
C
ALA
596
51.948
52.448
48.043
1.00
14.88


ATOM
4238
O
ALA
596
50.891
52.914
48.474
1.00
15.10


ATOM
4239
N
MET
597
52.451
51.294
48.472
1.00
12.78


ATOM
4240
CA
MET
597
51.762
50.511
49.488
1.00
14.01


ATOM
4241
CB
MET
597
52.464
49.162
49.702
1.00
13.50


ATOM
4242
CG
MET
597
52.266
48.171
48.562
1.00
14.73


ATOM
4243
SD
MET
597
52.878
46.512
48.914
1.00
17.16


ATOM
4244
CE
MET
597
54.598
46.708
48.490
1.00
16.02


ATOM
4245
C
MET
597
51.644
51.249
50.820
1.00
14.90


ATOM
4246
O
MET
597
50.648
51.108
51.525
1.00
13.57


ATOM
4247
N
LYS
598
52.659
52.037
51.157
1.00
15.99


ATOM
4248
CA
LYS
598
52.660
52.786
52.412
1.00
17.02


ATOM
4249
CB
LYS
598
53.998
53.509
52.588
1.00
17.91


ATOM
4250
CG
LYS
598
55.146
52.592
52.970
1.00
22.00


ATOM
4251
CD
LYS
598
56.439
53.374
53.127
1.00
25.95


ATOM
4252
CE
LYS
598
57.505
52.545
53.830
1.00
28.04


ATOM
4253
NZ
LYS
598
57.829
51.285
53.106
1.00
28.00


ATOM
4254
C
LYS
598
51.512
53.790
52.513
1.00
17.35


ATOM
4255
O
LYS
598
51.098
54.155
53.613
1.00
19.76


ATOM
4256
N
LEU
599
51.000
54.234
51.369
1.00
15.18


ATOM
4257
CA
LEU
599
49.892
55.184
51.355
1.00
14.61


ATOM
4258
CB
LEU
599
49.652
55.722
49.940
1.00
15.70


ATOM
4259
CG
LEU
599
50.701
56.621
49.288
1.00
15.36


ATOM
4260
CD1
LEU
599
50.234
56.968
47.888
1.00
15.46


ATOM
4261
CD2
LEU
599
50.911
57.884
50.113
1.00
15.35


ATOM
4262
C
LEU
599
48.607
54.534
51.845
1.00
14.55


ATOM
4263
O
LEU
599
47.686
55.222
52.285
1.00
16.32


ATOM
4264
N
GLY
600
48.544
53.209
51.767
1.00
13.23


ATOM
4265
CA
GLY
600
47.341
52.517
52.184
1.00
14.20


ATOM
4266
C
GLY
600
46.128
53.091
51.468
1.00
14.55


ATOM
4267
O
GLY
600
46.116
53.212
50.240
1.00
14.07


ATOM
4268
N
PHE
601
45.117
53.468
52.242
1.00
15.08


ATOM
4269
CA
PHE
601
43.883
54.031
51.700
1.00
16.39


ATOM
4270
CB
PHE
601
42.684
53.251
52.271
1.00
16.50


ATOM
4271
CG
PHE
601
41.376
53.527
51.574
1.00
18.08


ATOM
4272
CD1
PHE
601
41.221
53.255
50.217
1.00
18.28


ATOM
4273
CD2
PHE
601
40.290
54.033
52.284
1.00
18.21


ATOM
4274
CE1
PHE
601
40.002
53.478
49.577
1.00
19.49


ATOM
4275
CE2
PHE
601
39.060
54.262
51.653
1.00
19.93


ATOM
4276
CZ
PHE
601
38.918
53.982
50.297
1.00
18.56


ATOM
4277
C
PHE
601
43.786
55.518
52.079
1.00
16.63


ATOM
4278
O
PHE
601
42.698
56.083
52.144
1.00
16.35


ATOM
4279
N
SER
602
44.934
56.152
52.302
1.00
18.17


ATOM
4280
CA
SER
602
44.968
57.561
52.699
1.00
19.16


ATOM
4281
CB
SER
602
46.294
57.868
53.395
1.00
19.08


ATOM
4282
OG
SER
602
47.375
57.759
52.484
1.00
16.23


ATOM
4283
C
SER
602
44.751
58.593
51.590
1.00
21.31


ATOM
4284
O
SER
602
44.388
59.735
51.874
1.00
19.96


ATOM
4285
N
ARG
603
44.973
58.199
50.337
1.00
20.09


ATOM
4286
CA
ARG
603
44.816
59.118
49.207
1.00
21.67


ATOM
4287
CB
ARG
603
46.201
59.533
48.685
1.00
22.66


ATOM
4288
CG
ARG
603
47.124
60.184
49.711
1.00
26.63


ATOM
4289
CD
ARG
603
46.639
61.574
50.087
1.00
28.83


ATOM
4290
NE
ARG
603
46.453
62.415
48.908
1.00
33.44


ATOM
4291
CZ
ARG
603
45.955
63.648
48.939
1.00
35.92


ATOM
4292
NH1
ARG
603
45.594
64.189
50.096
1.00
35.88


ATOM
4293
NH2
ARG
603
45.808
64.337
47.816
1.00
35.28


ATOM
4294
C
ARG
603
44.037
58.471
48.058
1.00
20.33


ATOM
4295
O
ARG
603
43.926
57.257
47.987
1.00
21.14


ATOM
4296
N
PRO
604
43.486
59.283
47.141
1.00
21.16


ATOM
4297
CD
PRO
604
43.484
60.757
47.074
1.00
20.84


ATOM
4298
CA
PRO
604
42.742
58.700
46.016
1.00
20.12


ATOM
4299
CB
PRO
604
42.380
59.920
45.171
1.00
21.00


ATOM
4300
CG
PRO
604
42.288
61.033
46.199
1.00
22.41


ATOM
4301
C
PRO
604
43.717
57.765
45.294
1.00
18.21


ATOM
4302
O
PRO
604
44.879
58.123
45.108
1.00
16.62


ATOM
4303
N
TRP
605
43.256
56.588
44.871
1.00
16.20


ATOM
4304
CA
TRP
605
44.155
55.631
44.222
1.00
14.88


ATOM
4305
CB
TRP
605
43.404
54.352
43.807
1.00
11.66


ATOM
4306
CG
TRP
605
42.419
54.500
42.687
1.00
11.73


ATOM
4307
CD2
TRP
605
42.712
54.543
41.285
1.00
10.38


ATOM
4308
CE2
TRP
605
41.478
54.643
40.605
1.00
9.76


ATOM
4309
CE3
TRP
605
43.897
54.513
40.537
1.00
11.00


ATOM
4310
CD1
TRP
605
41.059
54.575
42.797
1.00
11.94


ATOM
4311
NE1
TRP
605
40.487
54.657
41.551
1.00
12.01


ATOM
4312
CZ2
TRP
605
41.393
54.706
39.211
1.00
10.56


ATOM
4313
CZ3
TRP
605
43.813
54.577
39.147
1.00
12.40


ATOM
4314
CH2
TRP
605
42.569
54.675
38.500
1.00
10.93


ATOM
4315
C
TRP
605
44.990
56.138
43.048
1.00
14.01


ATOM
4316
O
TRP
605
46.088
55.639
42.819
1.00
14.77


ATOM
4317
N
PRO
606
44.491
57.132
42.287
1.00
14.29


ATOM
4318
CD
PRO
606
43.145
57.734
42.275
1.00
12.19


ATOM
4319
CA
PRO
606
45.286
57.629
41.158
1.00
15.72


ATOM
4320
CB
PRO
606
44.432
58.770
40.613
1.00
15.01


ATOM
4321
CG
PRO
606
43.046
58.272
40.859
1.00
14.40


ATOM
4322
C
PRO
606
46.687
58.091
41.559
1.00
17.03


ATOM
4323
O
PRO
606
47.600
58.098
40.740
1.00
16.15


ATOM
4324
N
GLU
607
46.852
58.481
42.818
1.00
17.28


ATOM
4325
CA
GLU
607
48.157
58.925
43.298
1.00
19.19


ATOM
4326
CB
GLU
607
48.017
59.648
44.639
1.00
21.09


ATOM
4327
CG
GLU
607
47.456
61.060
44.503
1.00
25.25


ATOM
4328
CD
GLU
607
47.359
61.785
45.837
1.00
27.88


ATOM
4329
OE1
GLU
607
48.311
61.683
46.641
1.00
28.02


ATOM
4330
OE2
GLU
607
46.334
62.462
46.075
1.00
29.69


ATOM
4331
C
GLU
607
49.106
57.739
43.430
1.00
17.57


ATOM
4332
O
GLU
607
50.268
57.828
43.052
1.00
18.96


ATOM
4333
N
ALA
608
48.611
56.626
43.962
1.00
16.29


ATOM
4334
CA
ALA
608
49.438
55.434
44.094
1.00
16.79


ATOM
4335
CB
ALA
608
48.693
54.353
44.871
1.00
14.91


ATOM
4336
C
ALA
608
49.775
54.947
42.683
1.00
16.09


ATOM
4337
O
ALA
608
50.886
54.488
42.425
1.00
16.14


ATOM
4338
N
MET
609
48.810
55.056
41.772
1.00
15.85


ATOM
4339
CA
MET
609
49.024
54.649
40.383
1.00
15.49


ATOM
4340
CB
MET
609
47.742
54.841
39.569
1.00
14.89


ATOM
4341
CG
MET
609
47.885
54.548
38.068
1.00
12.61


ATOM
4342
SD
MET
609
48.373
52.846
37.686
1.00
14.89


ATOM
4343
CE
MET
609
46.752
52.007
37.746
1.00
9.67


ATOM
4344
C
MET
609
50.152
55.486
39.769
1.00
17.04


ATOM
4345
O
MET
609
51.018
54.963
39.063
1.00
16.25


ATOM
4346
N
GLN
610
50.131
56.787
40.044
1.00
16.65


ATOM
4347
CA
GLN
610
51.149
57.697
39.527
1.00
17.56


ATOM
4348
CB
GLN
610
50.798
59.148
39.865
1.00
21.08


ATOM
4349
CG
GLN
610
51.631
60.167
39.093
1.00
24.06


ATOM
4350
CD
GLN
610
50.775
61.060
38.219
1.00
27.95


ATOM
4351
OE1
GLN
610
50.227
62.066
38.675
1.00
30.67


ATOM
4352
NE2
GLN
610
50.637
60.684
36.959
1.00
31.02


ATOM
4353
C
GLN
610
52.521
57.362
40.103
1.00
18.21


ATOM
4354
O
GLN
610
53.513
57.324
39.375
1.00
17.58


ATOM
4355
N
LEU
611
52.574
57.120
41.410
1.00
17.37


ATOM
4356
CA
LEU
611
53.831
56.775
42.069
1.00
19.20


ATOM
4357
CB
LEU
611
53.593
56.498
43.560
1.00
20.05


ATOM
4358
CG
LEU
611
53.385
57.741
44.430
1.00
22.61


ATOM
4359
CD1
LEU
611
53.020
57.324
45.839
1.00
22.10


ATOM
4360
CD2
LEU
611
54.660
58.580
44.431
1.00
21.77


ATOM
4361
C
LEU
611
54.517
55.567
41.434
1.00
18.06


ATOM
4362
O
LEU
611
55.743
55.524
41.319
1.00
17.10


ATOM
4363
N
ILE
612
53.728
54.585
41.019
1.00
17.78


ATOM
4364
CA
ILE
612
54.289
53.384
40.408
1.00
15.89


ATOM
4365
CB
ILE
612
53.356
52.167
40.609
1.00
17.36


ATOM
4366
CG2
ILE
612
53.944
50.944
39.917
1.00
17.31


ATOM
4367
CG1
ILE
612
53.158
51.888
42.099
1.00
17.99


ATOM
4368
CD1
ILE
612
52.075
50.865
42.391
1.00
16.14


ATOM
4369
C
ILE
612
54.562
53.505
38.907
1.00
16.86


ATOM
4370
O
ILE
612
55.643
53.151
38.440
1.00
18.03


ATOM
4371
N
THR
613
53.586
54.018
38.162
1.00
16.36


ATOM
4372
CA
THR
613
53.684
54.108
36.707
1.00
15.96


ATOM
4373
CB
THR
613
52.368
53.622
36.079
1.00
14.90


ATOM
4374
OG1
THR
613
51.341
54.594
36.320
1.00
12.04


ATOM
4375
CG2
THR
613
51.941
52.289
36.701
1.00
12.12


ATOM
4376
C
THR
613
54.035
55.452
36.059
1.00
17.25


ATOM
4377
O
THR
613
54.323
55.502
34.860
1.00
16.91


ATOM
4378
N
GLY
614
54.000
56.538
36.826
1.00
16.88


ATOM
4379
CA
GLY
614
54.315
57.836
36.251
1.00
16.24


ATOM
4380
C
GLY
614
53.126
58.496
35.572
1.00
17.22


ATOM
4381
O
GLY
614
53.256
59.556
34.962
1.00
16.05


ATOM
4382
N
GLN
615
51.965
57.854
35.659
1.00
17.32


ATOM
4383
CA
GLN
615
50.736
58.391
35.086
1.00
15.68


ATOM
4384
CB
GLN
615
50.551
57.895
33.644
1.00
15.80


ATOM
4385
CG
GLN
615
50.422
56.397
33.467
1.00
16.06


ATOM
4386
CD
GLN
615
49.041
55.919
33.822
1.00
14.47


ATOM
4387
OE1
GLN
615
48.045
56.448
33.322
1.00
14.28


ATOM
4388
NE2
GLN
615
48.966
54.919
34.686
1.00
12.42


ATOM
4389
C
GLN
615
49.622
57.957
36.048
1.00
14.75


ATOM
4390
O
GLN
615
49.815
57.042
36.837
1.00
14.61


ATOM
4391
N
PRO
616
48.443
58.599
35.994
1.00
14.37


ATOM
4392
CD
PRO
616
48.129
59.856
35.288
1.00
15.57


ATOM
4393
CA
PRO
616
47.357
58.248
36.917
1.00
14.41


ATOM
4394
CB
PRO
616
46.829
59.617
37.298
1.00
15.41


ATOM
4395
CG
PRO
616
46.800
60.287
35.933
1.00
14.41


ATOM
4396
C
PRO
616
46.202
57.320
36.543
1.00
14.55


ATOM
4397
O
PRO
616
45.390
56.988
37.409
1.00
13.74


ATOM
4398
N
ASN
617
46.108
56.904
35.289
1.00
14.76


ATOM
4399
CA
ASN
617
44.985
56.072
34.869
1.00
16.09


ATOM
4400
CB
ASN
617
44.495
56.545
33.501
1.00
17.02


ATOM
4401
CG
ASN
617
44.216
58.029
33.462
1.00
18.18


ATOM
4402
OD1
ASN
617
44.489
58.692
32.463
1.00
22.94


ATOM
4403
ND2
ASN
617
43.658
58.557
34.542
1.00
18.54


ATOM
4404
C
ASN
617
45.226
54.573
34.777
1.00
14.02


ATOM
4405
O
ASN
617
46.364
54.105
34.776
1.00
13.88


ATOM
4406
N
MET
618
44.124
53.829
34.710
1.00
13.32


ATOM
4407
CA
MET
618
44.179
52.387
34.516
1.00
14.06


ATOM
4408
CB
MET
618
42.868
51.709
34.929
1.00
11.91


ATOM
4409
CG
MET
618
42.667
51.565
36.425
1.00
12.29


ATOM
4410
SD
MET
618
41.194
50.589
36.832
1.00
13.39


ATOM
4411
CE
MET
618
39.927
51.842
36.691
1.00
14.36


ATOM
4412
C
MET
618
44.316
52.322
32.997
1.00
14.48


ATOM
4413
O
MET
618
43.788
53.187
32.291
1.00
13.59


ATOM
4414
N
SER
619
45.013
51.318
32.488
1.00
12.87


ATOM
4415
CA
SER
619
45.194
51.215
31.049
1.00
13.47


ATOM
4416
CB
SER
619
46.309
52.168
30.599
1.00
13.34


ATOM
4417
OG
SER
619
46.562
52.039
29.215
1.00
16.20


ATOM
4418
C
SER
619
45.540
49.797
30.631
1.00
12.99


ATOM
4419
O
SER
619
46.338
49.131
31.288
1.00
12.36


ATOM
4420
N
ALA
620
44.937
49.350
29.533
1.00
12.12


ATOM
4421
CA
ALA
620
45.177
48.012
29.001
1.00
13.20


ATOM
4422
CB
ALA
620
43.968
47.555
28.189
1.00
9.78


ATOM
4423
C
ALA
620
46.433
47.971
28.125
1.00
13.52


ATOM
4424
O
ALA
620
46.845
46.901
27.672
1.00
12.99


ATOM
4425
N
SER
621
47.036
49.135
27.886
1.00
14.24


ATOM
4426
CA
SER
621
48.239
49.219
27.049
1.00
14.97


ATOM
4427
CB
SER
621
48.788
50.649
27.037
1.00
15.46


ATOM
4428
OG
SER
621
47.972
51.485
26.239
1.00
22.97


ATOM
4429
C
SER
621
49.361
48.266
27.446
1.00
13.26


ATOM
4430
O
SER
621
49.919
47.576
26.600
1.00
12.69


ATOM
4431
N
ALA
622
49.697
48.241
28.730
1.00
12.55


ATOM
4432
CA
ALA
622
50.761
47.374
29.220
1.00
12.62


ATOM
4433
CB
ALA
622
50.945
47.576
30.718
1.00
13.96


ATOM
4434
C
ALA
622
50.476
45.902
28.917
1.00
13.74


ATOM
4435
O
ALA
622
51.344
45.181
28.412
1.00
13.46


ATOM
4436
N
MET
623
49.261
45.458
29.227
1.00
12.23


ATOM
4437
CA
MET
623
48.882
44.074
28.977
1.00
11.27


ATOM
4438
CB
MET
623
47.501
43.792
29.578
1.00
11.37


ATOM
4439
CG
MET
623
47.048
42.354
29.452
1.00
12.71


ATOM
4440
SD
MET
623
45.490
42.044
30.308
1.00
16.84


ATOM
4441
CE
MET
623
45.878
40.541
31.173
1.00
14.59


ATOM
4442
C
MET
623
48.892
43.767
27.476
1.00
11.91


ATOM
4443
O
MET
623
49.352
42.706
27.058
1.00
13.42


ATOM
4444
N
LEU
624
48.397
44.694
26.662
1.00
13.23


ATOM
4445
CA
LEU
624
48.392
44.486
25.212
1.00
15.53


ATOM
4446
CB
LEU
624
47.622
45.611
24.505
1.00
15.98


ATOM
4447
CG
LEU
624
46.108
45.644
24.741
1.00
19.16


ATOM
4448
CD1
LEU
624
45.483
46.800
23.970
1.00
18.76


ATOM
4449
CD2
LEU
624
45.496
44.322
24.302
1.00
21.48


ATOM
4450
C
LEU
624
49.824
44.419
24.674
1.00
15.45


ATOM
4451
O
LEU
624
50.141
43.602
23.808
1.00
15.14


ATOM
4452
N
SER
625
50.688
45.281
25.198
1.00
15.79


ATOM
4453
CA
SER
625
52.088
45.315
24.788
1.00
16.37


ATOM
4454
CB
SER
625
52.788
46.502
25.462
1.00
16.92


ATOM
4455
OG
SER
625
54.196
46.404
25.354
1.00
22.26


ATOM
4456
C
SER
625
52.777
43.995
25.168
1.00
16.55


ATOM
4457
O
SER
625
53.544
43.426
24.385
1.00
17.40


ATOM
4458
N
TYR
626
52.490
43.511
26.372
1.00
14.61


ATOM
4459
CA
TYR
626
53.055
42.253
26.858
1.00
13.80


ATOM
4460
CB
TYR
626
52.487
41.939
28.251
1.00
13.59


ATOM
4461
CG
TYR
626
53.024
40.679
28.896
1.00
14.23


ATOM
4462
CD1
TYR
626
54.061
40.733
29.827
1.00
15.51


ATOM
4463
CE1
TYR
626
54.538
39.574
30.438
1.00
14.52


ATOM
4464
CD2
TYR
626
52.481
39.431
28.587
1.00
12.73


ATOM
4465
CE2
TYR
626
52.951
38.275
29.186
1.00
12.06


ATOM
4466
CZ
TYR
626
53.975
38.348
30.111
1.00
14.06


ATOM
4467
OH
TYR
626
54.425
37.193
30.713
1.00
13.54


ATOM
4468
C
TYR
626
52.721
41.101
25.901
1.00
13.64


ATOM
4469
O
TYR
626
53.585
40.287
25.567
1.00
12.40


ATOM
4470
N
PHE
627
51.467
41.039
25.461
1.00
12.53


ATOM
4471
CA
PHE
627
51.021
39.969
24.567
1.00
14.30


ATOM
4472
CB
PHE
627
49.608
39.515
24.955
1.00
11.92


ATOM
4473
CG
PHE
627
49.534
38.832
26.285
1.00
12.27


ATOM
4474
CD1
PHE
627
49.087
39.517
27.414
1.00
12.27


ATOM
4475
CD2
PHE
627
49.902
37.497
26.410
1.00
10.91


ATOM
4476
CE1
PHE
627
49.008
38.880
28.649
1.00
12.53


ATOM
4477
CE2
PHE
627
49.829
36.848
27.639
1.00
11.87


ATOM
4478
CZ
PHE
627
49.379
37.539
28.762
1.00
13.01


ATOM
4479
C
PHE
627
51.030
40.267
23.066
1.00
14.21


ATOM
4480
O
PHE
627
50.575
39.446
22.274
1.00
15.37


ATOM
4481
N
LYS
628
51.538
41.430
22.671
1.00
15.87


ATOM
4482
CA
LYS
628
51.570
41.801
21.258
1.00
15.56


ATOM
4483
CB
LYS
628
52.415
43.065
21.065
1.00
18.34


ATOM
4484
CG
LYS
628
52.689
43.436
19.608
1.00
20.03


ATOM
4485
CD
LYS
628
51.421
43.755
18.835
1.00
21.75


ATOM
4486
CE
LYS
628
51.754
44.104
17.378
1.00
25.43


ATOM
4487
NZ
LYS
628
50.542
44.288
16.531
1.00
24.46


ATOM
4488
C
LYS
628
52.080
40.682
20.345
1.00
15.60


ATOM
4489
O
LYS
628
51.462
40.383
19.324
1.00
17.04


ATOM
4490
N
PRO
629
53.215
40.054
20.693
1.00
15.51


ATOM
4491
CD
PRO
629
54.172
40.346
21.775
1.00
16.28


ATOM
4492
CA
PRO
629
53.715
38.978
19.830
1.00
16.88


ATOM
4493
CB
PRO
629
54.987
38.522
20.545
1.00
17.11


ATOM
4494
CG
PRO
629
55.463
39.781
21.218
1.00
16.67


ATOM
4495
C
PRO
629
52.690
37.848
19.676
1.00
17.03


ATOM
4496
O
PRO
629
52.496
37.320
18.579
1.00
17.38


ATOM
4497
N
LEU
630
52.027
37.486
20.771
1.00
16.19


ATOM
4498
CA
LEU
630
51.033
36.424
20.718
1.00
15.34


ATOM
4499
CB
LEU
630
50.570
36.044
22.126
1.00
14.76


ATOM
4500
CG
LEU
630
49.601
34.856
22.206
1.00
15.06


ATOM
4501
CD1
LEU
630
50.308
33.587
21.767
1.00
15.11


ATOM
4502
CD2
LEU
630
49.086
34.696
23.623
1.00
14.11


ATOM
4503
C
LEU
630
49.831
36.835
19.872
1.00
15.75


ATOM
4504
O
LEU
630
49.308
36.035
19.098
1.00
15.82


ATOM
4505
N
LEU
631
49.389
38.081
20.018
1.00
16.88


ATOM
4506
CA
LEU
631
48.249
38.564
19.245
1.00
17.64


ATOM
4507
CB
LEU
631
47.959
40.036
19.556
1.00
17.22


ATOM
4508
CG
LEU
631
46.810
40.681
18.765
1.00
20.26


ATOM
4509
CD1
LEU
631
45.498
39.989
19.100
1.00
20.21


ATOM
4510
CD2
LEU
631
46.719
42.161
19.093
1.00
19.79


ATOM
4511
C
LEU
631
48.533
38.405
17.753
1.00
18.65


ATOM
4512
O
LEU
631
47.681
37.929
17.005
1.00
18.10


ATOM
4513
N
ASP
632
49.731
38.802
17.326
1.00
17.92


ATOM
4514
CA
ASP
632
50.109
38.692
15.920
1.00
18.59


ATOM
4515
CB
ASP
632
51.485
39.326
15.671
1.00
19.38


ATOM
4516
CG
ASP
632
51.480
40.827
15.866
1.00
19.25


ATOM
4517
OD1
ASP
632
50.445
41.457
15.585
1.00
23.41


ATOM
4518
OD2
ASP
632
52.514
41.385
16.283
1.00
23.91


ATOM
4519
C
ASP
632
50.138
37.234
15.476
1.00
17.19


ATOM
4520
O
ASP
632
49.677
36.898
14.385
1.00
15.78


ATOM
4521
N
TRP
633
50.682
36.368
16.326
1.00
16.49


ATOM
4522
CA
TRP
633
50.756
34.950
15.997
1.00
16.56


ATOM
4523
CB
TRP
633
51.565
34.194
17.057
1.00
16.10


ATOM
4524
CG
TRP
633
51.804
32.763
16.687
1.00
17.24


ATOM
4525
CD2
TRP
633
50.971
31.645
17.015
1.00
17.80


ATOM
4526
CE2
TRP
633
51.523
30.510
16.380
1.00
18.16


ATOM
4527
CE3
TRP
633
49.807
31.491
17.782
1.00
17.82


ATOM
4528
CD1
TRP
633
52.804
32.273
15.892
1.00
17.18


ATOM
4529
NE1
TRP
633
52.641
30.922
15.703
1.00
17.98


ATOM
4530
CZ2
TRP
633
50.952
29.240
16.486
1.00
17.93


ATOM
4531
CZ3
TRP
633
49.240
30.226
17.889
1.00
19.24


ATOM
4532
CH2
TRP
633
49.815
29.117
17.243
1.00
17.03


ATOM
4533
C
TRP
633
49.347
34.359
15.912
1.00
16.87


ATOM
4534
O
TRP
633
49.048
33.559
15.024
1.00
15.40


ATOM
4535
N
LEU
634
48.480
34.770
16.833
1.00
16.10


ATOM
4536
CA
LEU
634
47.108
34.275
16.872
1.00
15.03


ATOM
4537
CB
LEU
634
46.406
34.749
18.151
1.00
13.27


ATOM
4538
CG
LEU
634
46.720
33.957
19.419
1.00
14.68


ATOM
4539
CD1
LEU
634
46.010
34.593
20.609
1.00
11.99


ATOM
4540
CD2
LEU
634
46.276
32.498
19.240
1.00
15.41


ATOM
4541
C
LEU
634
46.291
34.686
15.655
1.00
14.79


ATOM
4542
O
LEU
634
45.509
33.896
15.130
1.00
13.57


ATOM
4543
N
ARG
635
46.460
35.923
15.208
1.00
14.72


ATOM
4544
CA
ARG
635
45.720
36.385
14.041
1.00
16.48


ATOM
4545
CB
ARG
635
45.919
37.888
13.839
1.00
16.73


ATOM
4546
CG
ARG
635
45.030
38.742
14.722
1.00
20.60


ATOM
4547
CD
ARG
635
45.367
40.211
14.574
1.00
25.55


ATOM
4548
NE
ARG
635
44.462
41.063
15.340
1.00
29.96


ATOM
4549
CZ
ARG
635
44.726
42.325
15.659
1.00
31.82


ATOM
4550
NH1
ARG
635
45.871
42.880
15.280
1.00
31.36


ATOM
4551
NH2
ARG
635
43.846
43.034
16.353
1.00
34.01


ATOM
4552
C
ARG
635
46.158
35.618
12.797
1.00
16.36


ATOM
4553
O
ARG
635
45.327
35.194
11.997
1.00
16.07


ATOM
4554
N
THR
636
47.463
35.430
12.645
1.00
16.74


ATOM
4555
CA
THR
636
47.983
34.698
11.494
1.00
16.97


ATOM
4556
CB
THR
636
49.524
34.739
11.463
1.00
17.36


ATOM
4557
OG1
THR
636
49.956
36.094
11.282
1.00
18.76


ATOM
4558
CG2
THR
636
50.064
33.874
10.324
1.00
17.64


ATOM
4559
C
THR
636
47.513
33.243
11.522
1.00
15.76


ATOM
4560
O
THR
636
47.099
32.707
10.501
1.00
14.02


ATOM
4561
N
GLU
637
47.568
32.615
12.695
1.00
15.46


ATOM
4562
CA
GLU
637
47.137
31.223
12.842
1.00
15.45


ATOM
4563
CB
GLU
637
47.484
30.695
14.241
1.00
15.84


ATOM
4564
CG
GLU
637
46.905
29.309
14.562
1.00
17.40


ATOM
4565
CD
GLU
637
47.626
28.165
13.849
1.00
21.20


ATOM
4566
OE1
GLU
637
48.417
28.429
12.922
1.00
20.76


ATOM
4567
OE2
GLU
637
47.394
26.992
14.217
1.00
24.25


ATOM
4568
C
GLU
637
45.638
31.059
12.601
1.00
14.61


ATOM
4569
O
GLU
637
45.224
30.163
11.869
1.00
14.03


ATOM
4570
N
ASN
638
44.825
31.911
13.222
1.00
15.50


ATOM
4571
CA
ASN
638
43.378
31.824
13.046
1.00
15.74


ATOM
4572
CB
ASN
638
42.643
32.768
14.006
1.00
15.40


ATOM
4573
CG
ASN
638
42.690
32.288
15.447
1.00
15.23


ATOM
4574
OD1
ASN
638
42.765
31.084
15.713
1.00
12.88


ATOM
4575
ND2
ASN
638
42.633
33.228
16.387
1.00
11.63


ATOM
4576
C
ASN
638
42.972
32.146
11.617
1.00
17.16


ATOM
4577
O
ASN
638
42.029
31.563
11.086
1.00
16.41


ATOM
4578
N
GLU
639
43.691
33.076
10.996
1.00
18.19


ATOM
4579
CA
GLU
639
43.402
33.476
9.628
1.00
20.22


ATOM
4580
CB
GLU
639
44.260
34.686
9.240
1.00
20.36


ATOM
4581
CG
GLU
639
44.222
35.028
7.756
1.00
25.06


ATOM
4582
CD
GLU
639
45.156
36.172
7.400
1.00
26.81


ATOM
4583
OE1
GLU
639
44.849
37.324
7.773
1.00
29.07


ATOM
4584
OE2
GLU
639
46.201
35.917
6.759
1.00
25.74


ATOM
4585
C
GLU
639
43.635
32.343
8.630
1.00
20.09


ATOM
4586
O
GLU
639
42.799
32.092
7.763
1.00
18.73


ATOM
4587
N
LEU
640
44.760
31.647
8.751
1.00
20.74


ATOM
4588
CA
LEU
640
45.044
30.572
7.811
1.00
20.59


ATOM
4589
CB
LEU
640
46.506
30.127
7.936
1.00
22.92


ATOM
4590
CG
LEU
640
47.008
29.340
9.139
1.00
24.43


ATOM
4591
CD1
LEU
640
46.740
27.859
8.916
1.00
25.30


ATOM
4592
CD2
LEU
640
48.508
29.571
9.297
1.00
25.43


ATOM
4593
C
LEU
640
44.086
29.393
7.976
1.00
19.55


ATOM
4594
O
LEU
640
43.888
28.610
7.047
1.00
17.75


ATOM
4595
N
HIS
641
43.474
29.280
9.151
1.00
19.69


ATOM
4596
CA
HIS
641
42.518
28.208
9.400
1.00
19.52


ATOM
4597
CB
HIS
641
42.655
27.687
10.832
1.00
18.00


ATOM
4598
CG
HIS
641
43.861
26.829
11.038
1.00
20.33


ATOM
4599
CD2
HIS
641
44.212
25.645
10.485
1.00
19.67


ATOM
4600
ND1
HIS
641
44.902
27.188
11.867
1.00
22.38


ATOM
4601
CE1
HIS
641
45.843
26.264
11.814
1.00
19.87


ATOM
4602
NE2
HIS
641
45.450
25.317
10.982
1.00
23.55


ATOM
4603
C
HIS
642
41.088
28.668
9.139
1.00
18.42


ATOM
4604
O
HIS
641
40.144
27.894
9.282
1.00
19.70


ATOM
4605
N
GLY
642
40.941
29.931
8.749
1.00
18.10


ATOM
4606
CA
GLY
642
39.627
30.480
8.456
1.00
19.31


ATOM
4607
C
GLY
642
38.673
30.513
9.638
1.00
20.19


ATOM
4608
O
GLY
642
37.473
30.272
9.482
1.00
20.13


ATOM
4609
N
GLU
643
39.192
30.817
10.820
1.00
18.07


ATOM
4610
CA
GLU
643
38.353
30.866
12.013
1.00
18.39


ATOM
4611
CB
GLU
643
39.216
30.975
13.275
1.00
16.96


ATOM
4612
CG
GLU
643
40.297
29.914
13.395
1.00
17.41


ATOM
4613
CD
GLU
643
39.741
28.519
13.602
1.00
15.36


ATOM
4614
OE1
GLU
643
38.504
28.345
13.574
1.00
15.16


ATOM
4615
OE2
GLU
643
40.554
27.595
13.794
1.00
18.49


ATOM
4616
C
GLU
643
37.395
32.048
11.980
1.00
18.65


ATOM
4617
O
GLU
643
37.744
33.136
11.516
1.00
20.72


ATOM
4618
N
LYS
644
36.181
31.818
12.469
1.00
18.08


ATOM
4619
CA
LYS
644
35.168
32.859
12.560
1.00
17.63


ATOM
4620
CB
LYS
644
33.796
32.312
12.169
1.00
21.41


ATOM
4621
CG
LYS
644
32.658
33.304
12.356
1.00
27.52


ATOM
4622
CD
LYS
644
31.314
32.656
12.064
1.00
33.74


ATOM
4623
CE
LYS
644
30.179
33.660
12.149
1.00
36.34


ATOM
4624
NZ
LYS
644
28.880
33.042
11.750
1.00
39.29


ATOM
4625
C
LYS
644
35.165
33.262
14.030
1.00
17.75


ATOM
4626
O
LYS
644
34.652
32.527
14.876
1.00
17.16


ATOM
4627
N
LEU
645
35.753
34.417
14.330
1.00
16.17


ATOM
4628
CA
LEU
645
35.841
34.899
15.705
1.00
16.77


ATOM
4629
CB
LEU
645
36.665
36.186
15.767
1.00
15.16


ATOM
4630
CG
LEU
645
38.096
36.118
15.230
1.00
16.86


ATOM
4631
CD1
LEU
645
38.773
37.464
15.445
1.00
16.62


ATOM
4632
CD2
LEU
645
38.865
35.008
15.924
1.00
15.25


ATOM
4633
C
LEU
645
34.479
35.149
16.328
1.00
16.42


ATOM
4634
O
LEU
645
33.562
35.621
15.668
1.00
15.27


ATOM
4635
N
GLY
646
34.352
34.832
17.611
1.00
16.60


ATOM
4636
CA
GLY
646
33.089
35.048
18.287
1.00
16.22


ATOM
4637
C
GLY
646
32.126
33.881
18.183
1.00
17.80


ATOM
4638
O
GLY
646
32.501
32.773
17.793
1.00
17.07


ATOM
4639
N
TRP
647
30.872
34.142
18.529
1.00
18.98


ATOM
4640
CA
TRP
647
29.840
33.116
18.516
1.00
25.11


ATOM
4641
CB
TRP
647
29.775
32.464
19.896
1.00
21.13


ATOM
4642
CG
TRP
647
29.941
33.462
21.022
1.00
17.17


ATOM
4643
CD2
TRP
647
31.178
33.914
21.590
1.00
14.61


ATOM
4644
CE2
TRP
647
30.857
34.870
22.583
1.00
14.82


ATOM
4645
CE3
TRP
647
32.526
33.609
21.354
1.00
12.25


ATOM
4646
CD1
TRP
647
28.950
34.139
21.676
1.00
16.56


ATOM
4647
NE1
TRP
647
29.491
34.984
22.616
1.00
15.68


ATOM
4648
CZ2
TRP
647
31.838
35.523
23.343
1.00
12.54


ATOM
4649
CZ3
TRP
647
33.504
34.258
22.110
1.00
13.82


ATOM
4650
CH2
TRP
647
33.151
35.206
23.094
1.00
13.80


ATOM
4651
C
TRP
647
28.480
33.697
18.135
1.00
31.34


ATOM
4652
O
TRP
647
27.675
34.038
18.995
1.00
31.85


ATOM
4653
N
PRO
648
28.207
33.807
16.823
1.00
37.87


ATOM
4654
CD
PRO
648
29.017
33.206
15.747
1.00
39.60


ATOM
4655
CA
PRO
648
26.951
34.344
16.284
1.00
41.15


ATOM
4656
CB
PRO
648
27.117
34.156
14.778
1.00
42.26


ATOM
4657
CG
PRO
648
27.978
32.919
14.693
1.00
41.09


ATOM
4658
C
PRO
648
25.709
33.627
16.822
1.00
43.83


ATOM
4659
O
PRO
648
24.732
34.318
17.183
1.00
45.84


ATOM
4660
OXT
PRO
648
25.725
32.377
16.859
1.00
46.26


ATOM
4661
OH2
WAT
705
33.593
46.605
44.423
1.00
9.31


ATOM
4662
OH2
WAT
706
32.965
26.053
34.132
1.00
8.96


ATOM
4663
OH2
WAT
707
24.287
47.413
42.078
1.00
8.51


ATOM
4664
OH2
WAT
708
41.492
22.684
37.822
1.00
11.40


ATOM
4665
OH2
WAT
709
57.508
41.508
37.660
1.00
13.76


ATOM
4666
OH2
WAT
710
39.412
23.942
39.181
1.00
8.91


ATOM
4667
OH2
WAT
711
51.091
36.475
38.087
1.00
10.07


ATOM
4668
OH2
WAT
712
53.042
51.060
33.144
1.00
16.13


ATOM
4669
OH2
WAT
713
52.228
34.436
36.844
1.00
10.52


ATOM
4670
OH2
WAT
714
16.492
44.739
50.912
1.00
12.73


ATOM
4671
OH2
WAT
715
47.496
46.775
31.239
1.00
10.24


ATOM
4672
OH2
WAT
716
33.685
54.185
42.672
1.00
16.09


ATOM
4673
OH2
WAT
717
33.197
41.542
38.210
1.00
12.21


ATOM
4674
OH2
WAT
718
37.259
27.514
46.151
1.00
11.50


ATOM
4675
OH2
WAT
719
17.570
40.507
43.225
1.00
12.99


ATOM
4676
OH2
WAT
720
40.862
49.469
48.991
1.00
9.86


ATOM
4677
OH2
WAT
721
37.202
32.888
29.681
1.00
9.25


ATOM
4678
OH2
WAT
722
48.308
52.095
48.720
1.00
13.18


ATOM
4679
OH2
WAT
723
44.174
25.251
17.566
1.00
11.48


ATOM
4680
OH2
WAT
724
37.635
28.226
16.249
1.00
13.61


ATOM
4681
OH2
WAT
725
31.657
44.896
43.119
1.00
8.30


ATOM
4682
OH2
WAT
726
48.823
40.553
46.220
1.00
14.22


ATOM
4683
OH2
WAT
727
43.137
28.430
14.664
1.00
15.95


ATOM
4684
OH2
WAT
728
36.288
33.431
19.194
1.00
9.04


ATOM
4685
OH2
WAT
729
45.181
39.323
41.443
1.00
15.73


ATOM
4686
OH2
WAT
730
19.065
49.680
43.390
1.00
14.42


ATOM
4687
OH2
WAT
731
18.532
48.145
47.790
1.00
14.97


ATOM
4688
OH2
WAT
732
16.291
39.074
47.581
1.00
12.27


ATOM
4689
OH2
WAT
734
27.683
37.166
46.929
1.00
9.69


ATOM
4690
OH2
WAT
735
43.137
42.880
22.592
1.00
14.48


ATOM
4691
OH2
WAT
736
23.024
50.329
41.657
1.00
17.32


ATOM
4692
OH2
WAT
737
40.667
28.535
40.057
1.00
16.00


ATOM
4693
OH2
WAT
738
44.387
45.117
56.435
1.00
14.17


ATOM
4694
OH2
WAT
739
42.945
25.383
33.384
1.00
13.52


ATOM
4695
OH2
WAT
740
36.456
23.986
32.241
1.00
8.95


ATOM
4696
OH2
WAT
741
39.950
39.788
48.186
1.00
12.78


ATOM
4697
OH2
WAT
742
47.924
45.637
61.414
1.00
20.16


ATOM
4698
OH2
WAT
743
48.523
42.505
62.565
1.00
17.18


ATOM
4699
OH2
WAT
744
16.710
44.022
47.985
1.00
15.86


ATOM
4700
OH2
WAT
745
50.722
52.452
33.013
1.00
14.62


ATOM
4701
OH2
WAT
746
42.905
51.202
39.594
1.00
14.40


ATOM
4702
OH2
WAT
747
43.215
36.931
50.988
1.00
16.61


ATOM
4703
OH2
WAT
748
37.286
29.700
43.929
1.00
19.60


ATOM
4704
OH2
WAT
749
31.745
23.237
13.527
1.00
19.26


ATOM
4705
OH2
WAT
750
50.872
32.438
13.257
1.00
13.65


ATOM
4706
OH2
WAT
751
23.924
24.786
40.648
1.00
14.00


ATOM
4707
OH2
WAT
752
46.065
55.788
48.966
1.00
12.21


ATOM
4708
OH2
WAT
753
17.359
38.412
45.074
1.00
16.22


ATOM
4709
OH2
WAT
754
30.402
54.271
37.540
1.00
19.90


ATOM
4710
OH2
WAT
755
30.166
28.862
39.171
1.00
11.86


ATOM
4711
OH2
WAT
756
40.401
56.296
45.617
1.00
19.60


ATOM
4712
OH2
WAT
757
48.250
46.266
58.848
1.00
15.18


ATOM
4713
OH2
WAT
758
23.481
22.074
39.456
1.00
13.04


ATOM
4714
OH2
WAT
759
39.537
29.868
42.153
1.00
13.71


ATOM
4715
OH2
WAT
760
41.465
55.169
34.794
1.00
16.56


ATOM
4716
OH2
WAT
761
50.211
32.756
35.889
1.00
22.03


ATOM
4717
OH2
WAT
762
55.270
39.776
52.027
1.00
16.82


ATOM
4718
OH2
WAT
763
17.787
47.082
45.179
1.00
17.96


ATOM
4719
OH2
WAT
764
41.349
43.344
47.624
1.00
13.85


ATOM
4720
OH2
WAT
765
31.365
48.033
33.699
1.00
17.60


ATOM
4721
OH2
WAT
766
35.820
29.185
13.398
1.00
14.60


ATOM
4722
OH2
WAT
767
42.075
46.950
49.736
1.00
18.28


ATOM
4723
OH2
WAT
768
40.009
19.530
28.487
1.00
17.39


ATOM
4724
OH2
WAT
770
52.878
28.814
13.591
1.00
22.84


ATOM
4725
OH2
WAT
771
39.380
57.861
40.522
1.00
20.88


ATOM
4726
OH2
WAT
772
34.750
20.720
49.137
1.00
24.09


ATOM
4727
OH2
WAT
773
17.366
31.093
38.464
1.00
23.54


ATOM
4728
OH2
WAT
774
44.804
23.924
14.000
1.00
19.88


ATOM
4729
OH2
WAT
775
31.146
56.380
49.556
1.00
21.05


ATOM
4730
OH2
WAT
776
46.715
56.401
46.506
1.00
19.22


ATOM
4731
OH2
WAT
777
42.869
58.288
37.166
1.00
15.61


ATOM
4732
OH2
WAT
778
40.831
33.557
7.130
1.00
24.79


ATOM
4733
OH2
WAT
779
35.162
52.317
73.577
1.00
20.05


ATOM
4734
OH2
WAT
780
14.809
39.247
36.520
1.00
18.70


ATOM
4735
OH2
WAT
781
39.527
31.879
53.125
1.00
13.72


ATOM
4736
OH2
WAT
782
27.757
50.041
53.223
1.00
27.53


ATOM
4737
OH2
WAT
783
49.394
26.247
11.787
1.00
19.81


ATOM
4738
OH2
WAT
784
44.777
26.399
15.119
1.00
21.30


ATOM
4739
OH2
WAT
785
57.867
38.875
52.198
1.00
18.47


ATOM
4740
OH2
WAT
786
34.155
51.047
61.985
1.00
19.93


ATOM
4741
OH2
WAT
787
45.141
27.154
46.412
1.00
22.42


ATOM
4742
OH2
WAT
788
43.475
51.366
28.087
1.00
18.86


ATOM
4743
OH2
WAT
789
20.668
25.724
29.782
1.00
24.21


ATOM
4744
OH2
WAT
790
32.083
32.320
15.051
1.00
19.38


ATOM
4745
OH2
WAT
791
49.913
48.449
23.710
1.00
18.63


ATOM
4746
OH2
WAT
792
42.785
27.563
47.669
1.00
25.09


ATOM
4747
OH2
WAT
793
39.850
53.780
46.033
1.00
22.72


ATOM
4748
OH2
WAT
794
27.466
13.978
27.601
1.00
20.70


ATOM
4749
OH2
WAT
795
40.190
34.656
11.736
1.00
32.79


ATOM
4750
OH2
WAT
796
39.109
10.985
33.519
1.00
22.45


ATOM
4751
OH2
WAT
797
27.558
21.410
51.556
1.00
17.72


ATOM
4752
OH2
WAT
798
66.163
40.174
37.797
1.00
19.68


ATOM
4753
OH2
WAT
799
22.819
49.816
39.224
1.00
23.29


ATOM
4754
OH2
WAT
800
25.950
37.105
65.162
1.00
25.58


ATOM
4755
OH2
WAT
801
34.253
10.439
28.187
1.00
25.36


ATOM
4756
OH2
WAT
802
59.840
33.669
44.222
1.00
19.20


ATOM
4757
OH2
WAT
803
38.496
20.697
31.902
1.00
16.24


ATOM
4758
OH2
WAT
804
40.729
21.319
12.133
1.00
28.36


ATOM
4759
OH2
WAT
805
56.117
41.173
25.206
1.00
19.73


ATOM
4760
OH2
WAT
806
37.047
26.923
50.890
1.00
22.30


ATOM
4761
OH2
WAT
807
42.476
46.612
21.569
1.00
21.24


ATOM
4762
OH2
WAT
808
35.171
28.146
10.829
1.00
23.83


ATOM
4763
OH2
WAT
809
29.225
19.649
23.377
1.00
20.44


ATOM
4764
OH2
WAT
810
52.753
51.832
57.912
1.00
24.14


ATOM
4765
OH2
WAT
811
53.307
37.708
61.763
1.00
20.90


ATOM
4766
OH2
WAT
812
11.971
34.982
48.268
1.00
25.05


ATOM
4767
OH2
WAT
813
24.990
48.789
37.974
1.00
24.58


ATOM
4768
OH2
WAT
814
43.951
19.262
20.770
1.00
21.14


ATOM
4769
OH2
WAT
815
36.259
14.934
14.740
1.00
22.42


ATOM
4770
OH2
WAT
816
35.820
12.642
25.488
1.00
20.65


ATOM
4771
OH2
WAT
817
39.436
55.386
36.440
1.00
12.53


ATOM
4772
OH2
WAT
818
62.583
34.233
30.419
1.00
22.07


ATOM
4773
OH2
WAT
819
19.790
54.852
50.868
1.00
29.06


ATOM
4774
OH2
WAT
820
50.697
29.832
12.471
1.00
22.39


ATOM
4775
OH2
WAT
821
27.847
56.381
70.315
1.00
23.46


ATOM
4776
OH2
WAT
823
27.949
17.733
50.193
1.00
31.12


ATOM
4777
OH2
WAT
824
55.965
37.522
32.909
1.00
17.65


ATOM
4778
OH2
WAT
825
9.432
31.570
48.180
1.00
32.33


ATOM
4779
OH2
WAT
826
41.473
54.399
62.185
1.00
30.40


ATOM
4780
OH2
WAT
827
50.992
18.343
24.030
1.00
25.41


ATOM
4781
OH2
WAT
828
26.053
14.477
12.460
1.00
20.39


ATOM
4782
OH2
WAT
829
69.827
44.579
41.736
1.00
22.45


ATOM
4783
OH2
WAT
830
56.552
22.658
16.664
1.00
27.42


ATOM
4784
OH2
WAT
831
26.288
20.159
49.712
1.00
24.06


ATOM
4785
OH2
WAT
832
16.705
33.141
51.058
1.00
19.06


ATOM
4786
OH2
WAT
833
21.271
53.952
59.470
1.00
23.51


ATOM
4787
OH2
WAT
834
47.427
53.353
64.227
1.00
34.99


ATOM
4788
OH2
WAT
835
45.817
26.456
42.450
1.00
37.42


ATOM
4789
OH2
WAT
836
49.720
39.114
12.538
1.00
29.15


ATOM
4790
OH2
WAT
837
36.955
41.394
51.137
1.00
26.94


ATOM
4791
OH2
WAT
838
42.624
25.634
37.851
1.00
23.28


ATOM
4792
OH2
WAT
839
51.315
24.980
58.259
1.00
30.21


ATOM
4793
OH2
WAT
840
54.566
56.838
50.490
1.00
30.20


ATOM
4794
OH2
WAT
841
40.512
53.418
32.693
1.00
26.12


ATOM
4795
OH2
WAT
842
26.362
47.983
54.146
1.00
26.40


ATOM
4796
OH2
WAT
843
37.201
32.434
54.478
1.00
19.11


ATOM
4797
OH2
WAT
844
57.961
39.008
32.080
1.00
20.99


ATOM
4798
OH2
WAT
845
18.271
24.342
44.501
1.00
22.93


ATOM
4799
OH2
WAT
846
41.486
21.860
67.124
1.00
40.66


ATOM
4800
OH2
WAT
847
13.917
29.508
37.265
1.00
42.07


ATOM
4801
OH2
WAT
848
17.295
33.378
57.585
1.00
24.15


ATOM
4802
OH2
WAT
849
22.558
38.571
32.120
1.00
36.71


ATOM
4803
OH2
WAT
850
35.628
59.228
37.704
1.00
24.98


ATOM
4804
OH2
WAT
851
24.241
59.727
65.168
1.00
27.57


ATOM
4805
OH2
WAT
852
30.466
55.002
34.566
1.00
20.81


ATOM
4806
OH2
WAT
853
39.487
26.456
44.048
1.00
27.56


ATOM
4807
OH2
WAT
854
32.107
46.093
71.751
1.00
28.54


ATOM
4808
OH2
WAT
855
48.700
24.975
15.218
1.00
27.62


ATOM
4809
OH2
WAT
856
71.051
37.353
44.254
1.00
24.64


ATOM
4810
OH2
WAT
857
18.705
30.001
40.624
1.00
24.61


ATOM
4811
OH2
WAT
858
67.822
43.137
39.600
1.00
24.92


ATOM
4812
OH2
WAT
859
28.879
64.576
58.006
1.00
30.86


ATOM
4813
OH2
WAT
860
50.121
23.822
38.157
1.00
29.74


ATOM
4814
OH2
WAT
861
50.504
23.835
16.516
1.00
41.06


ATOM
4815
OH2
WAT
862
50.897
18.482
46.813
1.00
28.35


ATOM
4816
OH2
WAT
863
54.681
37.002
16.795
1.00
25.10


ATOM
4817
OH2
WAT
864
23.493
23.940
53.772
1.00
22.53


ATOM
4818
OH2
WAT
865
33.356
54.985
26.024
1.00
43.50


ATOM
4819
OH2
WAT
866
43.404
31.760
41.951
1.00
21.02


ATOM
4820
OH2
WAT
867
28.231
42.794
54.526
1.00
30.76


ATOM
4821
OH2
WAT
868
14.847
43.548
34.779
1.00
34.44


ATOM
4822
OH2
WAT
869
14.659
39.207
57.645
1.00
33.41


ATOM
4823
OH2
WAT
870
57.510
37.601
64.872
1.00
30.64


ATOM
4824
OH2
WAT
871
20.651
32.033
29.682
1.00
28.82


ATOM
4825
OH2
WAT
872
52.056
50.326
27.360
1.00
24.49


ATOM
4826
OH2
WAT
873
51.657
35.863
62.500
1.00
26.14


ATOM
4827
OH2
WAT
874
47.279
21.024
51.484
1.00
23.69


ATOM
4828
OH2
WAT
875
29.576
44.197
56.830
1.00
26.36


ATOM
4829
OH2
WAT
876
40.524
18.980
31.059
1.00
25.48


ATOM
4830
OH2
WAT
877
56.572
42.868
23.278
1.00
31.20


ATOM
4831
OH2
WAT
878
34.210
18.018
53.038
1.00
32.11


ATOM
4832
OH2
WAT
879
27.258
18.647
26.109
1.00
26.96


ATOM
4833
OH2
WAT
880
62.773
54.373
39.531
1.00
36.25


ATOM
4834
OH2
WAT
881
35.089
9.269
50.485
1.00
38.55


ATOM
4835
OH2
WAT
882
38.082
57.888
33.414
1.00
23.60


ATOM
4836
OH2
WAT
883
20.570
20.572
35.734
1.00
30.32


ATOM
4837
OH2
WAT
884
64.060
48.729
47.598
1.00
25.68


ATOM
4838
OH2
WAT
885
61.993
33.237
54.293
1.00
38.10


ATOM
4839
OH2
WAT
886
46.176
15.310
31.633
1.00
32.63


ATOM
4840
OH2
WAT
887
14.968
50.857
53.881
1.00
42.97


ATOM
4841
OH2
WAT
888
21.704
24.366
51.887
1.00
36.24


ATOM
4842
OH2
WAT
889
39.839
19.775
14.153
1.00
24.51


ATOM
4843
OH2
WAT
890
44.365
68.561
56.122
1.00
31.90


ATOM
4844
OH2
WAT
891
47.553
30.301
39.926
1.00
25.30


ATOM
4845
OH2
WAT
892
32.268
20.759
14.108
1.00
23.29


ATOM
4846
OH2
WAT
893
69.343
41.988
48.078
1.00
32.22


ATOM
4847
OH2
WAT
894
24.297
15.185
41.737
1.00
31.91


ATOM
4848
OH2
WAT
895
30.655
11.104
25.446
1.00
26.78


ATOM
4849
OH2
WAT
896
42.362
40.299
57.293
1.00
20.70


ATOM
4850
OH2
WAT
898
41.774
36.340
13.554
1.00
34.25


ATOM
4851
OH2
WAT
899
39.152
38.465
60.315
1.00
25.51


ATOM
4852
OH2
WAT
900
41.147
24.781
9.266
1.00
37.67


ATOM
4853
OH2
WAT
901
69.407
36.691
46.483
1.00
26.53


ATOM
4854
OH2
WAT
902
55.637
47.942
26.959
1.00
32.37


ATOM
4855
OH2
WAT
903
33.913
34.460
58.201
1.00
38.45


ATOM
4856
OH2
WAT
904
56.269
58.664
39.628
1.00
38.97


ATOM
4857
OH2
WAT
905
57.309
45.050
24.747
1.00
30.45


ATOM
4858
OH2
WAT
906
67.831
30.631
34.349
1.00
30.40


ATOM
4859
OH2
WAT
907
17.422
51.937
47.071
1.00
26.07


ATOM
4860
OH2
WAT
908
35.633
30.975
66.612
1.00
24.07


ATOM
4861
OH2
WAT
910
61.975
46.612
53.486
1.00
26.87


ATOM
4862
OH2
WAT
911
47.029
38.251
67.425
1.00
30.22


ATOM
4863
OH2
WAT
912
60.210
33.638
26.728
1.00
31.35


ATOM
4864
OH2
WAT
913
17.482
36.558
63.602
1.00
44.50


ATOM
4865
OH2
WAT
914
24.128
36.324
26.146
1.00
20.37


ATOM
4866
OH2
WAT
915
15.719
30.346
47.149
1.00
24.17


ATOM
4867
OH2
WAT
916
23.359
62.099
63.265
1.00
40.09


ATOM
4868
OH2
WAT
917
50.740
48.721
64.156
1.00
39.37


ATOM
4869
OH2
WAT
918
64.987
41.178
33.243
1.00
37.88


ATOM
4870
OH2
WAT
919
47.126
55.164
71.884
1.00
33.61


ATOM
4871
OH2
WAT
920
15.488
43.883
65.882
1.00
23.44


ATOM
4872
OH2
WAT
921
37.706
50.611
24.676
1.00
33.21


ATOM
4873
OH2
WAT
922
37.379
23.810
9.516
1.00
34.84


ATOM
4874
OH2
WAT
923
38.957
20.044
55.559
1.00
43.10


ATOM
4875
OH2
WAT
924
24.959
16.071
14.898
1.00
34.26


ATOM
4876
OH2
WAT
925
22.429
16.629
37.874
1.00
31.87


ATOM
4877
OH2
WAT
926
29.356
53.921
43.835
1.00
38.69


ATOM
4878
OH2
WAT
927
60.523
35.360
57.102
1.00
40.12


ATOM
4879
OH2
WAT
928
29.303
20.134
16.704
1.00
26.85


ATOM
4880
OH2
WAT
929
19.799
33.303
59.063
1.00
32.03


ATOM
4881
OH2
WAT
930
19.367
18.997
32.033
1.00
30.19


ATOM
4882
OH2
WAT
931
48.165
22.382
58.513
1.00
36.12


ATOM
4883
OH2
WAT
932
43.741
63.487
53.233
1.00
33.28


ATOM
4884
OH2
WAT
933
33.863
20.218
11.695
1.00
26.21


ATOM
4885
OH2
WAT
934
49.235
59.976
52.718
1.00
28.98


ATOM
4886
OH2
WAT
935
63.989
32.978
44.987
1.00
35.98


ATOM
4887
OH2
WAT
936
38.155
21.333
49.259
1.00
27.87


ATOM
4888
OH2
WAT
937
28.080
14.345
39.095
1.00
31.98


ATOM
4889
OH2
WAT
938
15.034
38.648
61.496
1.00
35.94


ATOM
4890
OH2
WAT
939
58.771
42.322
58.976
1.00
26.19


ATOM
4891
OH2
WAT
940
47.485
42.154
69.878
1.00
35.48


ATOM
4892
OH2
WAT
941
26.602
32.519
69.106
1.00
23.36


ATOM
4893
OH2
WAT
942
28.022
17.338
22.711
1.00
31.24


ATOM
4894
OH2
WAT
943
26.711
49.956
71.239
1.00
38.80


ATOM
4895
OH2
WAT
944
64.021
22.891
42.685
1.00
33.14


ATOM
4896
OH2
WAT
945
47.677
33.744
7.930
1.00
25.60


ATOM
4897
OH2
WAT
946
34.908
23.405
49.212
1.00
24.56


ATOM
4898
OH2
WAT
947
46.968
46.697
68.856
1.00
35.00


ATOM
4899
OH2
WAT
948
41.692
11.412
30.635
1.00
31.37


ATOM
4900
OH2
WAT
949
34.423
48.837
63.936
1.00
25.42


ATOM
4901
OH2
WAT
950
38.612
61.793
51.417
1.00
33.87


ATOM
4902
OH2
WAT
951
45.067
50.306
71.708
1.00
44.52


ATOM
4903
OH2
WAT
952
46.249
23.672
42.556
1.00
31.95


ATOM
4904
OH2
WAT
953
22.948
57.447
63.178
1.00
39.30


ATOM
4905
OH2
WAT
954
53.305
20.101
34.868
1.00
41.13


ATOM
4906
OH2
WAT
955
39.320
63.985
53.074
1.00
28.86


ATOM
4907
OH2
WAT
956
20.574
21.558
47.751
1.00
30.99


ATOM
4908
OH2
WAT
957
70.490
44.479
44.539
1.00
22.23


ATOM
4909
OH2
WAT
958
13.638
23.050
34.936
1.00
28.58


ATOM
4910
OH2
WAT
959
61.304
38.113
59.657
1.00
31.77


ATOM
4911
OH2
WAT
960
70.418
49.240
43.244
1.00
47.36


ATOM
4912
OH2
WAT
961
27.272
13.615
45.529
1.00
35.16


ATOM
4913
OH2
WAT
962
40.595
52.830
28.676
1.00
35.25


ATOM
4914
OH2
WAT
963
41.406
39.978
15.308
1.00
23.02


ATOM
4915
OH2
WAT
964
47.358
18.488
60.102
1.00
48.76


ATOM
4916
OH2
WAT
965
30.061
44.962
27.407
1.00
28.02


ATOM
4917
OH2
WAT
966
69.978
22.947
32.361
1.00
35.17


ATOM
4918
OH2
WAT
967
54.106
56.970
32.477
1.00
27.90


ATOM
4919
OH2
WAT
968
48.115
18.063
53.954
1.00
37.64


ATOM
4920
OH2
WAT
969
38.320
16.416
14.841
1.00
28.53


ATOM
4921
OH2
WAT
970
29.037
12.266
32.860
1.00
24.29


ATOM
4922
OH2
WAT
971
29.314
35.536
60.124
1.00
39.44


ATOM
4923
OH2
WAT
972
47.444
23.555
12.870
1.00
36.87


ATOM
4924
OH2
WAT
973
40.389
49.471
57.522
1.00
28.51


ATOM
4925
OH2
WAT
974
47.998
48.009
65.323
1.00
45.77


ATOM
4926
OH2
WAT
975
38.192
25.689
48.335
1.00
36.54


ATOM
4927
OH2
WAT
976
22.607
20.057
46.747
1.00
33.16


ATOM
4928
OH2
WAT
977
37.372
23.697
52.106
1.00
21.54


ATOM
4929
OH2
WAT
978
33.554
55.985
48.705
1.00
26.17


ATOM
4930
OH2
WAT
979
48.510
43.090
21.681
1.00
30.35


ATOM
4931
OH2
WAT
980
47.263
49.883
23.397
1.00
41.75


ATOM
4932
OH2
WAT
981
19.519
18.617
44.162
1.00
42.73


ATOM
4933
OH2
WAT
982
37.700
6.935
33.344
1.00
44.09


ATOM
4934
OH2
WAT
983
44.887
20.648
40.251
1.00
45.35


ATOM
4935
OH2
WAT
984
67.007
44.355
29.244
1.00
44.80


ATOM
4936
OH2
WAT
985
65.458
35.373
34.954
1.00
44.52


ATOM
4937
OH2
WAT
986
30.989
20.633
65.111
1.00
35.79


ATOM
4938
OH2
WAT
987
26.918
36.574
22.781
1.00
35.02


ATOM
4939
OH2
WAT
988
19.103
25.427
48.338
1.00
25.31


ATOM
4940
OH2
WAT
989
47.801
58.546
30.861
1.00
32.01


ATOM
4941
OH2
WAT
990
33.665
57.659
31.778
1.00
36.66


ATOM
4942
OH2
WAT
991
60.170
48.247
52.476
1.00
32.47


ATOM
4943
OH2
WAT
993
63.978
36.551
52.728
1.00
34.68


ATOM
4944
OH2
WAT
994
29.804
56.958
72.469
1.00
49.60


ATOM
4945
OH2
WAT
995
9.989
39.449
62.826
1.00
44.68


ATOM
4946
OH2
WAT
996
36.235
28.967
7.281
1.00
44.34


ATOM
4947
OH2
WAT
997
49.505
50.913
30.172
1.00
29.44


ATOM
4948
OH2
WAT
998
11.062
37.216
34.519
1.00
29.29


ATOM
4949
OH2
WAT
999
44.702
22.987
39.107
1.00
36.93


ATOM
4950
OH2
WAT
1000
50.857
38.850
67.888
1.00
36.37


ATOM
4951
OH2
WAT
1002
60.252
35.317
28.988
1.00
29.45


ATOM
4952
OH2
WAT
1003
20.726
30.784
57.864
1.00
29.69


ATOM
4953
OH2
WAT
1004
20.309
29.029
31.082
1.00
23.76


ATOM
4954
OH2
WAT
1005
21.059
52.048
61.212
1.00
28.93


ATOM
4955
OH2
WAT
1006
44.854
20.536
43.319
1.00
44.76


ATOM
4956
OH2
WAT
1007
19.996
28.678
33.868
1.00
30.03


ATOM
4957
OH2
WAT
1008
33.822
36.086
54.053
1.00
31.99


ATOM
4958
OH2
WAT
1009
53.120
30.359
35.501
1.00
32.80


ATOM
4959
OH2
WAT
1010
54.882
53.339
33.303
1.00
30.28


ATOM
4960
OH2
WAT
1012
55.781
39.618
64.945
1.00
34.34


ATOM
4961
OH2
WAT
1013
48.371
45.507
17.871
1.00
36.20


ATOM
4962
OH2
WAT
1014
66.334
38.117
49.319
1.00
23.90


ATOM
4963
OH2
WAT
1015
16.758
47.920
39.004
1.00
37.89


ATOM
4964
OH2
WAT
1016
54.280
18.755
56.686
1.00
52.80


ATOM
4965
OH2
WAT
1017
31.023
49.906
52.390
1.00
45.47


ATOM
4966
OH2
WAT
1018
12.055
42.758
50.614
1.00
49.35


ATOM
4967
OH2
WAT
1019
31.945
53.747
53.015
1.00
35.87


ATOM
4968
OH2
WAT
1020
13.807
43.996
63.471
1.00
38.90


ATOM
4969
OH2
WAT
1021
55.521
22.445
54.252
1.00
28.52


ATOM
4970
OH2
WAT
1022
17.175
28.274
38.843
1.00
32.21


ATOM
4971
OH2
WAT
1024
36.313
20.402
51.637
1.00
43.69


ATOM
4972
OH2
WAT
1025
48.801
20.762
30.306
1.00
24.61


ATOM
4973
OH2
WAT
1026
40.208
59.687
47.657
1.00
44.52


ATOM
4974
OH2
WAT
1027
14.148
45.044
52.430
1.00
40.64


ATOM
4975
OH2
WAT
1028
38.755
17.199
55.396
1.00
42.40


ATOM
4976
OH2
WAT
1029
62.000
22.562
29.636
1.00
43.07


ATOM
4977
OH2
WAT
1030
20.078
45.714
34.052
1.00
44.28


ATOM
4978
OH2
WAT
1031
63.279
47.962
24.894
1.00
31.08


ATOM
4979
OH2
WAT
1032
35.585
5.069
31.352
1.00
35.03


ATOM
4980
OH2
WAT
1033
29.682
34.108
53.939
1.00
26.25


ATOM
4981
OH2
WAT
1034
46.780
38.540
9.889
1.00
51.06


ATOM
4982
OH2
WAT
1035
44.882
34.636
67.334
1.00
46.95


ATOM
4983
OH2
WAT
1036
37.415
12.859
50.188
0.50
42.02


ATOM
4984
OH2
WAT
1037
25.981
44.789
34.946
1.00
24.59


ATOM
4985
OH2
WAT
1038
43.445
29.058
41.261
1.00
45.80


ATOM
4986
OH2
WAT
1039
12.090
30.084
45.723
1.00
38.62


ATOM
4987
OH2
WAT
1040
11.364
36.356
54.939
1.00
40.96


ATOM
4988
OH2
WAT
1041
29.272
41.003
52.730
1.00
42.87


ATOM
4989
OH2
WAT
1042
37.324
27.042
8.738
1.00
46.28


ATOM
4990
OH2
WAT
1043
57.492
28.350
30.232
1.00
46.70


ATOM
4991
OH2
WAT
1044
15.052
49.656
56.840
1.00
37.66


ATOM
4992
OH2
WAT
1045
46.768
51.835
70.126
1.00
51.14


ATOM
4993
OH2
WAT
1046
33.162
57.841
46.992
1.00
41.63


ATOM
4994
OH2
WAT
1047
44.092
26.222
49.137
1.00
40.14


ATOM
4995
OH2
WAT
1048
42.496
32.208
38.770
1.00
40.63


ATOM
4996
OH2
WAT
1049
58.978
48.444
30.591
1.00
27.79


ATOM
4997
OH2
WAT
1050
55.619
13.932
32.119
1.00
39.09


ATOM
4998
OH2
WAT
1051
46.458
60.895
55.459
1.00
37.85


ATOM
4999
OH2
WAT
1052
42.873
26.465
64.734
1.00
39.73


ATOM
5000
OH2
WAT
1053
56.101
17.530
47.784
1.00
39.99


ATOM
5001
OH2
WAT
1054
31.203
38.751
53.971
1.00
30.66


ATOM
5002
OH2
WAT
1055
47.563
17.129
46.637
1.00
45.01


ATOM
5003
OH2
WAT
1056
58.815
30.610
63.372
1.00
32.58


ATOM
5004
OH2
WAT
1057
26.459
10.748
26.222
1.00
46.82


ATOM
5005
OH2
WAT
1058
45.017
29.344
39.141
1.00
43.86


ATOM
5006
OH2
WAT
1059
26.313
26.119
59.271
1.00
36.72


ATOM
5007
OH2
WAT
1061
28.236
58.748
55.454
1.00
30.55


ATOM
5008
OH2
WAT
1062
61.906
32.814
43.031
1.00
29.09


ATOM
5009
OH2
WAT
1063
69.011
47.015
42.506
1.00
28.30


ATOM
5010
OH2
WAT
1066
52.729
54.024
56.720
1.00
49.30


ATOM
5011
OH2
WAT
1068
44.439
16.568
20.527
1.00
40.67


ATOM
5012
OH2
WAT
1070
45.820
25.970
61.887
1.00
41.07


ATOM
5013
OH2
WAT
1071
60.712
46.310
28.186
0.50
40.28


ATOM
5014
OH2
WAT
1072
36.208
36.373
12.341
1.00
29.35


ATOM
5015
OH2
WAT
1073
35.114
41.414
67.958
1.00
46.06


ATOM
5016
OH2
WAT
1074
65.518
34.727
51.474
1.00
29.02


ATOM
5017
OH2
WAT
1075
13.571
35.140
58.001
1.00
38.14


ATOM
5018
OH2
WAT
1076
34.047
38.447
58.618
1.00
35.93


ATOM
5019
OH2
WAT
1077
48.507
37.783
69.502
1.00
45.44


ATOM
5020
OH2
WAT
1078
41.210
38.536
55.002
0.50
37.11


ATOM
5021
OH2
WAT
1079
29.344
38.728
22.988
1.00
40.16


ATOM
5022
OH2
WAT
1080
14.136
37.604
50.804
1.00
38.19


ATOM
5023
OH2
WAT
1081
48.142
54.501
25.745
1.00
36.15


ATOM
5024
OH2
WAT
1082
40.910
25.680
40.947
1.00
20.33


ATOM
5025
OH2
WAT
1083
40.233
57.746
37.797
1.00
16.93


ATOM
5026
OH2
WAT
1084
54.670
59.272
48.665
1.00
32.72


ATOM
5027
OH2
WAT
1085
53.699
57.790
52.915
1.00
30.15


ATOM
5028
OH2
WAT
1086
16.670
32.247
54.833
1.00
41.51


ATOM
5029
OH2
WAT
1087
22.296
31.936
27.500
1.00
28.36


ATOM
5030
OH2
WAT
1088
47.914
17.001
32.454
1.00
37.63


ATOM
5031
OH2
WAT
1089
57.985
47.492
28.231
1.00
32.60


ATOM
5032
OH2
WAT
1090
35.749
34.442
55.271
1.00
34.51


ATOM
5033
OH2
WAT
1091
31.476
35.919
55.030
1.00
29.00


ATOM
5034
OH2
WAT
1092
57.549
59.850
42.071
1.00
37.12


ATOM
5035
OH2
WAT
1093
37.244
31.058
68.548
1.00
28.12


ATOM
5036
OH2
WAT
1094
37.707
33.592
70.255
1.00
33.05


ATOM
5037
OH2
WAT
1095
65.341
43.727
34.421
1.00
39.40


ATOM
5038
OH2
WAT
1096
29.571
56.164
45.104
1.00
27.27


ATOM
5039
OH2
WAT
1097
28.460
20.997
19.168
1.00
29.57


ATOM
5040
OH2
WAT
1098
18.695
33.000
61.504
1.00
27.80


ATOM
5041
OH2
WAT
1099
19.269
34.045
63.767
1.00
40.98


ATOM
5042
OH2
WAT
1100
50.893
61.236
50.969
1.00
35.01


ATOM
5043
OH2
WAT
1101
56.400
43.894
59.831
1.00
32.48


ATOM
5044
OH2
WAT
1102
56.721
41.861
63.860
1.00
30.95


ATOM
5045
OH2
WAT
1103
34.429
49.906
71.937
1.00
27.35


ATOM
5046
OH2
WAT
1104
41.246
9.747
32.571
1.00
29.28


ATOM
5047
OH2
WAT
1105
20.981
21.798
50.939
1.00
39.38


ATOM
5048
OH2
WAT
1106
23.739
19.876
50.550
1.00
40.52


ATOM
5049
OH2
WAT
1107
38.769
41.131
17.011
1.00
45.24


ATOM
5050
OH2
WAT
1108
29.718
9.526
34.248
1.00
37.08


ATOM
5051
OH2
WAT
1109
27.449
9.015
35.782
1.00
29.46


ATOM
5052
OH2
WAT
1110
26.205
9.875
37.838
1.00
37.18


ATOM
5053
OH2
WAT
1111
24.669
47.026
35.553
1.00
25.36


ATOM
5054
OH2
WAT
1112
31.450
56.875
43.413
1.00
35.79


ATOM
5055
OH2
WAT
1113
29.193
57.847
41.895
1.00
28.59


ATOM
5056
OH2
WAT
1114
48.270
62.126
54.057
1.00
47.11


ATOM
5057
OH2
WAT
1115
25.062
58.442
56.552
1.00
44.02


ATOM
5058
OH2
WAT
1116
22.740
60.186
60.488
1.00
34.22


ATOM
5059
OH2
WAT
1117
39.213
37.453
56.336
1.00
40.31


ATOM
5060
OH2
WAT
1118
38.121
40.798
59.573
1.00
43.24


ATOM
5061
OH2
WAT
1119
37.346
43.433
61.501
1.00
37.73


ATOM
5062
OH2
WAT
1120
37.001
39.773
55.197
1.00
42.52


ATOM
5063
OH2
WAT
1121
18.157
30.227
56.161
1.00
37.69


ATOM
5064
OH2
WAT
1122
33.762
10.574
25.544
1.00
23.70


ATOM
5065
OH2
WAT
1123
37.474
59.970
39.757
1.00
21.11


ATOM
5066
OH2
WAT
1124
41.061
44.584
49.861
1.00
25.81


ATOM
5067
OH2
WAT
1125
70.442
38.041
48.255
1.00
29.55


ATOM
5068
OH2
WAT
1126
15.491
41.776
47.873
1.00
30.31


ATOM
5069
OH2
WAT
1127
25.212
43.116
32.288
1.00
28.62


ATOM
5070
OH2
WAT
1128
26.383
21.154
54.156
1.00
29.70


ATOM
5071
OH2
WAT
1129
50.740
60.798
47.331
1.00
38.19


ATOM
5072
OH2
WAT
1130
41.735
39.836
50.778
1.00
37.70


ATOM
5073
OH2
WAT
1131
42.701
60.987
37.812
1.00
41.12


ATOM
5074
OH2
WAT
1132
14.659
29.765
44.894
1.00
33.95


ATOM
5075
OH2
WAT
1133
34.102
38.199
24.717
1.00
27.35


ATOM
5076
OH2
WAT
1134
45.354
44.890
68.080
1.00
31.32


ATOM
5077
OH2
WAT
1135
35.915
44.195
50.574
1.00
32.69


ATOM
5078
OH2
WAT
1136
15.867
48.663
59.058
1.00
34.96


ATOM
5079
OH2
WAT
1137
15.232
36.067
62.441
1.00
39.53


ATOM
5080
OH2
WAT
1138
24.046
35.123
64.133
1.00
33.21


ATOM
5081
OH2
WAT
1140
42.820
43.043
56.106
1.00
40.38


ATOM
5082
OH2
WAT
1142
30.164
46.247
60.234
1.00
27.89


ATOM
5083
OH2
WAT
1143
36.787
20.701
62.513
1.00
40.11


ATOM
5084
OH2
WAT
1144
55.849
49.287
57.410
1.00
29.15


ATOM
5085
OH2
WAT
1145
50.753
46.872
21.712
1.00
35.52


ATOM
5086
OH2
WAT
1146
45.737
64.613
61.498
1.00
44.87


ATOM
5087
OH2
WAT
1147
28.723
16.491
52.376
1.00
48.22


ATOM
5088
OH2
WAT
1148
41.105
13.562
41.818
1.00
29.30


ATOM
5089
OH2
WAT
1149
26.685
14.349
42.039
1.00
42.43


ATOM
5090
OH2
WAT
1150
38.358
50.484
49.443
1.00
35.16


ATOM
5091
OH2
WAT
1151
69.920
42.965
37.954
1.00
40.56


ATOM
5092
OH2
WAT
1152
52.738
59.405
31.453
1.00
35.45


ATOM
5093
OH2
WAT
1153
32.404
39.258
22.528
1.00
39.05


ATOM
5094
OH2
WAT
1154
22.666
50.694
36.768
1.00
36.83


ATOM
5095
OH2
WAT
1155
14.698
50.360
47.308
1.00
38.90


ATOM
5096
OH2
WAT
1156
39.143
11.155
36.210
1.00
39.07


ATOM
5097
OH2
WAT
1157
55.657
18.795
54.147
1.00
34.85


ATOM
5098
OH2
WAT
1158
62.362
32.941
24.043
1.00
41.87


ATOM
5099
OH2
WAT
1159
29.902
43.547
51.918
1.00
32.04


ATOM
5100
OH2
WAT
1160
26.171
30.161
18.201
1.00
39.60


ATOM
5101
OH2
WAT
1161
41.218
21.756
70.370
1.00
41.36


ATOM
5102
OH2
WAT
1162
26.190
30.492
28.185
1.00
27.88


ATOM
5103
OH2
WAT
1163
50.602
53.898
30.780
1.00
30.62


ATOM
5104
OH2
WAT
1164
26.955
17.640
16.849
1.00
31.56


ATOM
5105
OH2
WAT
1165
41.691
10.374
28.028
1.00
32.37


ATOM
5106
OH2
WAT
1166
57.418
56.385
51.476
1.00
35.94


ATOM
5107
OH2
WAT
1167
55.642
43.654
62.253
1.00
41.27


ATOM
5108
OH2
WAT
1168
41.479
56.703
63.461
1.00
34.93


ATOM
5109
OH2
WAT
1169
39.613
58.154
43.178
1.00
35.49


ATOM
5110
OH2
WAT
1170
45.356
56.475
68.496
1.00
37.27


ATOM
5111
OH2
WAT
1171
44.916
53.775
27.876
1.00
31.35


ATOM
5112
OH2
WAT
1172
25.722
27.696
18.138
1.00
38.58


ATOM
5113
OH2
WAT
1173
43.375
49.025
22.195
1.00
33.80


ATOM
5114
OH2
WAT
1174
21.889
34.531
26.210
1.00
36.18


ATOM
5115
OH2
WAT
1175
41.736
39.433
59.697
1.00
36.02


ATOM
5116
OH2
WAT
1176
47.436
28.894
63.907
1.00
33.93


ATOM
5117
OH2
WAT
1177
28.538
47.783
33.721
1.00
39.02


ATOM
5118
OH2
WAT
1178
45.541
19.730
50.210
1.00
43.10


ATOM
5119
OH2
WAT
1179
68.291
39.466
47.597
1.00
37.89


ATOM
5120
OH2
WAT
1180
66.025
32.351
42.560
1.00
35.69


ATOM
5121
OH2
WAT
1181
61.703
29.189
16.524
1.00
36.27


ATOM
5122
OH2
WAT
1182
14.548
30.540
42.421
1.00
42.06


ATOM
5123
OH2
WAT
1183
15.496
27.270
47.838
1.00
46.85


ATOM
5124
OH2
WAT
1184
14.095
47.673
48.381
1.00
47.62


ATOM
5125
OH2
WAT
1185
47.204
19.227
33.252
1.00
36.81


ATOM
5126
OH2
WAT
1186
15.661
33.106
31.093
1.00
46.85


ATOM
5127
OH2
WAT
1187
67.150
47.220
39.295
1.00
36.46


ATOM
5128
OH2
WAT
1188
29.557
22.635
20.946
1.00
41.67


ATOM
5129
OH2
WAT
1189
28.682
26.265
60.679
1.00
46.57


ATOM
5130
OH2
WAT
1190
17.693
23.606
49.850
1.00
36.98


ATOM
5131
OH2
WAT
1191
51.486
56.952
54.132
1.00
32.03


ATOM
5132
OH2
WAT
1192
55.843
23.209
25.565
1.00
44.63


ATOM
5133
OH2
WAT
1193
43.669
45.262
17.620
1.00
41.89


ATOM
5134
OH2
WAT
1194
36.029
14.373
12.084
1.00
39.33


ATOM
5135
OH2
WAT
1195
14.318
32.026
49.337
1.00
35.36


ATOM
5136
OH2
WAT
1196
13.222
35.202
50.716
1.00
45.32


ATOM
5137
OH2
WAT
1197
54.042
24.106
57.247
1.00
47.39


ATOM
5138
OH2
WAT
1198
34.685
14.060
23.512
1.00
39.90


ATOM
5139
OH2
WAT
1199
45.704
57.109
65.615
1.00
46.14


ATOM
5140
OH2
WAT
1200
44.873
24.284
46.545
1.00
34.57


ATOM
5141
OH2
WAT
1201
35.967
56.594
50.557
1.00
39.33


ATOM
5142
OH2
WAT
1202
30.036
57.668
47.644
1.00
37.79


ATOM
5143
OH2
WAT
1203
49.131
18.854
41.508
1.00
42.53


ATOM
5144
OH2
WAT
1204
30.102
43.586
25.149
1.00
40.72


ATOM
5145
OH2
WAT
1205
16.998
53.914
48.758
1.00
48.89


ATOM
5146
OH2
WAT
1207
22.805
15.462
43.888
1.00
41.37


ATOM
5147
OH2
WAT
1208
21.497
24.519
27.314
1.00
37.24


ATOM
5148
OH2
WAT
1209
17.651
41.303
33.491
1.00
42.96


ATOM
5149
OH2
WAT
1210
60.654
28.310
58.903
1.00
50.25


ATOM
5150
OH2
WAT
1212
46.533
63.565
52.672
1.00
46.38


ATOM
5151
OH2
WAT
1213
46.413
53.655
68.053
1.00
39.92


ATOM
5152
OH2
WAT
1214
14.311
46.777
37.971
1.00
50.08


ATOM
5153
OH2
WAT
1216
55.429
29.530
33.565
1.00
45.03


ATOM
5154
OH2
WAT
1217
53.478
35.792
14.453
1.00
40.11


ATOM
5155
OH2
WAT
1218
40.345
43.339
56.627
1.00
47.78


ATOM
5156
OH2
WAT
1219
36.529
52.046
58.807
1.00
38.42


ATOM
5157
OH2
WAT
1220
24.511
41.919
29.518
1.00
41.70


ATOM
5158
OH2
WAT
1222
17.693
27.672
35.440
1.00
43.96


ATOM
5159
OH2
WAT
1223
23.641
21.252
53.576
1.00
44.70


ATOM
5160
OH2
WAT
1224
51.161
18.080
43.110
1.00
37.11


ATOM
5161
OH2
WAT
1225
44.467
44.673
20.294
1.00
44.46


ATOM
5162
OH2
WAT
1226
50.788
19.723
49.959
1.00
37.29


ATOM
5163
OH2
WAT
1227
54.752
25.906
65.096
1.00
46.67


ATOM
5164
OH2
WAT
1228
63.418
32.799
51.922
1.00
39.05


ATOM
5165
OH2
WAT
1229
49.352
29.893
33.234
1.00
44.01


ATOM
5166
OH2
WAT
1230
31.202
38.938
20.335
1.00
49.64


ATOM
5167
OH2
WAT
1231
33.715
51.957
58.093
1.00
40.80


ATOM
5168
OH2
WAT
1232
23.578
22.341
27.377
1.00
33.04


ATOM
5169
OH2
WAT
1233
48.877
30.829
37.399
1.00
42.38


ATOM
5170
OH2
WAT
1235
52.077
39.927
11.643
1.00
50.91


ATOM
5171
OH2
WAT
1236
46.727
47.936
20.766
1.00
39.36


ATOM
5172
OH2
WAT
1237
19.932
16.273
39.489
1.00
39.93


ATOM
5173
OH2
WAT
1239
40.814
60.178
74.599
1.00
41.48


ATOM
5174
OH2
WAT
1240
51.750
29.763
9.713
1.00
41.37


ATOM
5175
OH2
WAT
1241
38.610
58.856
35.877
1.00
44.28


ATOM
5176
OH2
WAT
1242
21.432
26.708
58.173
1.00
37.52


ATOM
5177
OH2
WAT
1243
46.966
33.870
68.743
1.00
45.93


ATOM
5178
OH2
WAT
1244
61.246
43.773
58.961
1.00
40.96


ATOM
5179
OH2
WAT
1246
64.751
48.614
51.387
1.00
40.01


ATOM
5180
OH2
WAT
1249
28.908
23.979
70.000
1.00
50.21


ATOM
5181
OH2
WAT
1250
35.092
50.916
23.964
1.00
43.45


ATOM
5182
OH2
WAT
1251
40.260
47.302
20.071
1.00
39.21


ATOM
5183
OH2
WAT
1252
35.991
60.939
52.084
1.00
42.26


ATOM
5184
OH2
WAT
1253
27.391
37.137
20.202
1.00
43.08


ATOM
5185
OH2
WAT
1255
12.393
50.408
52.301
0.50
37.03


ATOM
5186
OH2
WAT
1256
23.608
55.162
64.150
1.00
41.77


ATOM
5187
OH2
WAT
1258
47.269
17.174
22.065
1.00
46.22


ATOM
5188
OH2
WAT
1259
28.456
62.543
55.786
1.00
41.70


ATOM
5189
OH2
WAT
1260
18.167
46.909
66.948
1.00
43.73


ATOM
5190
OH2
WAT
1261
26.966
45.286
26.641
1.00
48.72


ATOM
5191
OH2
WAT
1264
17.101
45.276
33.425
1.00
43.21


ATOM
5192
OH2
WAT
1265
63.613
36.746
57.666
1.00
42.19


ATOM
5193
OH2
WAT
1266
24.775
12.094
44.611
1.00
43.78


ATOM
5194
OH2
WAT
1267
14.567
43.639
54.809
1.00
43.19


ATOM
5195
OH2
WAT
1268
62.111
49.250
49.919
1.00
45.57


ATOM
5196
OH2
WAT
1269
50.495
37.209
8.544
1.00
41.23


ATOM
5197
OH2
WAT
1270
25.496
43.939
68.768
1.00
38.89


ATOM
5198
OH2
WAT
1271
46.561
47.854
71.850
1.00
47.32


ATOM
5199
OH2
WAT
1272
34.624
40.398
52.220
1.00
40.23


ATOM
5200
OH2
WAT
1273
23.826
29.701
27.112
1.00
37.37


ATOM
5201
OH2
WAT
1275
58.487
56.076
44.456
1.00
49.60


ATOM
5202
OH2
WAT
1276
47.004
19.336
65.956
1.00
44.67


ATOM
5203
OH2
WAT
1277
35.331
60.688
71.296
1.00
49.05


ATOM
5204
OH2
WAT
1278
64.248
43.852
53.276
1.00
45.61


ATOM
5205
OH2
WAT
1279
38.265
60.125
44.267
1.00
40.24


ATOM
5206
OH2
WAT
1280
32.716
19.954
61.811
1.00
48.51


ATOM
5207
OH2
WAT
1282
37.969
28.502
70.587
1.00
45.47


ATOM
5208
OH2
WAT
1283
45.149
43.238
70.422
1.00
51.48


ATOM
5209
OH2
WAT
1284
59.891
53.118
51.539
1.00
48.96


ATOM
5210
OH2
WAT
1285
34.867
45.533
72.885
1.00
47.50


ATOM
5211
OH2
WAT
1286
21.880
52.964
63.592
1.00
43.17


ATOM
5212
OH2
WAT
1288
49.993
22.986
32.101
1.00
43.19


ATOM
5213
OH2
WAT
1289
46.808
19.421
38.578
1.00
44.53


ATOM
5214
OH2
WAT
1290
30.906
19.264
11.986
1.00
42.77


ATOM
5215
OH2
WAT
1293
9.566
38.464
32.587
1.00
48.38


ATOM
5216
OH2
WAT
1294
42.359
12.879
35.960
1.00
39.40


ATOM
5217
OH2
WAT
1296
43.735
54.908
30.034
1.00
43.21


ATOM
5218
OH2
WAT
1298
38.663
10.988
25.018
1.00
37.95


ATOM
5219
OH2
WAT
1299
32.861
26.550
10.296
1.00
46.61


ATOM
5220
OH2
WAT
1300
43.628
37.637
11.420
1.00
44.84


ATOM
5221
OH2
WAT
1302
47.573
23.475
60.712
1.00
38.95


ATOM
5222
OH2
WAT
1303
64.973
53.331
38.090
1.00
38.57


ATOM
5223
OH2
WAT
1304
16.881
19.232
30.969
1.00
47.01


ATOM
5224
OH2
WAT
1306
48.262
21.848
19.919
1.00
44.43


ATOM
5225
OH2
WAT
1307
11.425
37.923
51.890
1.00
34.09


ATOM
5226
OH2
WAT
1308
63.096
29.357
20.027
1.00
40.25


ATOM
5227
OH2
WAT
1309
23.170
21.317
25.128
1.00
38.17


ATOM
5228
OH2
WAT
1310
20.030
19.255
25.175
1.00
29.39


ATOM
5229
OH2
WAT
1311
51.597
27.670
8.159
1.00
42.04


ATOM
5230
OH2
WAT
1312
48.948
36.803
6.527
1.00
41.43


ATOM
5231
O1
LIS
702
40.291
33.743
45.120
1.00
13.04


ATOM
5232
O2
LIS
702
43.369
36.201
48.269
1.00
15.16


ATOM
5233
O3
LIS
702
41.939
37.283
47.069
1.00
13.89


ATOM
5234
O4
LIS
702
38.843
33.368
41.867
1.00
13.99


ATOM
5235
O5
LIS
702
40.703
32.272
42.326
1.00
11.94


ATOM
5236
N1
LIS
702
41.897
34.063
47.266
1.00
14.83


ATOM
5237
N2
LIS
702
41.810
34.533
43.599
1.00
13.77


ATOM
5238
N3
LIS
702
43.329
27.774
44.087
1.00
21.85


ATOM
5239
C1
LIS
702
41.502
34.052
44.840
1.00
13.99


ATOM
5240
C2
LIS
702
42.612
33.852
45.943
1.00
12.80


ATOM
5241
C3
LIS
702
42.259
36.267
47.654
1.00
13.57


ATOM
5242
C4
LIS
702
41.315
35.065
47.682
1.00
14.83


ATOM
5243
C5
LIS
702
40.715
34.685
42.559
1.00
14.91


ATOM
5244
C6
LIS
702
41.505
35.237
41.353
1.00
14.97


ATOM
5245
C7
LIS
702
42.826
35.369
41.680
1.00
16.22


ATOM
5246
C8
LIS
702
43.138
34.956
43.062
1.00
12.52


ATOM
5247
C9
LIS
702
40.081
33.284
42.224
1.00
13.82


ATOM
5248
C10
LIS
702
43.252
32.473
45.784
1.00
14.69


ATOM
5249
C11
LIS
702
42.484
31.248
45.536
1.00
16.12


ATOM
5250
C12
LIS
702
43.296
30.062
44.842
1.00
17.50


ATOM
5251
C13
LIS
702
42.487
28.895
44.629
1.00
20.10


ATOM
5252
C14
LIS
702
40.586
35.365
48.932
1.00
12.04


ATOM
5253
C15
LIS
702
39.408
36.299
49.163
1.00
13.87


ATOM
5254
C16
LIS
702
38.847
36.401
50.549
1.00
15.99


ATOM
5255
C17
LIS
702
38.566
35.206
51.331
1.00
14.59


ATOM
5256
C18
LIS
702
38.016
35.319
52.656
1.00
17.75


ATOM
5257
C19
LIS
702
37.737
36.627
53.218
1.00
18.68


ATOM
5258
C20
LIS
702
38.014
37.822
52.443
1.00
18.46


ATOM
5259
C21
LIS
702
38.568
37.710
51.112
1.00
16.62


ATOM
5260
N
GLY
2000
46.347
33.778
41.598
1.00
29.94


ATOM
5261
CA
GLY
2000
46.605
34.757
40.562
1.00
28.86


ATOM
5262
C
GLY
2000
46.815
34.072
39.230
1.00
29.89


ATOM
5263
O
GLY
2000
47.218
34.695
38.260
1.00
28.89


ATOM
5264
ZN + 2
ZN2
701
43.821
38.240
46.712
1.00
25.11


ATOM
5265
CL
CL
703
29.172
28.069
36.210
1.00
12.41


ATOM
5266
CL
CL
704
36.272
45.081
44.766
1.00
15.28


END

















Sequences









Seq ID No. 1









WT-ACE



SQQVTVTHGTSSQATTSSQTTTHQATAHQTSAQSPNLVTDEAEASKFVEE


YDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQAR


KFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVAT


VCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKY


VELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAY


VRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMD


TTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREV


VCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVA


LREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKM


ALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVP


RTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKC


DIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLL


DWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQA


RVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRH


S


 








Seq ID No. 2









ACE-Δ36NJ



LVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNM


QIANHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYN


KILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWR


DKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERL


FQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNI


YDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFW


NKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMG


HIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSE


GGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWW


SLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEA


LCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPN


MSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNS

## Claims

1. A method of preparing a crystal of ACE protein comprising the steps of:
(a) culturing host cells comprising an underglycosylated ACE protein;
(b) purifying the underglycosylated ACE protein; and
(c) crystallising the underglycosylated ACE protein.

2. A method according to claim 1 wherein the ACE protein is underglycosylated by removing one or more glycosylation sites and/or one or more partially glycosylated sites.

3. A method according to claim 1 wherein the underglycosylated ACE protein comprises a mutation at amino acid 337 of SEQ ID No 2 or amino acids 90, 109, 155, 337 and 586 of SEQ ID No 2.

4. A method according claim 1 wherein the ACE protein is crystallised using about 10 mM HEPES and about 0.1% PMSF with an equal volume of a reservoir solution containing about 15% PEG 4000, about 50 mM CH3COONa.3H2O pH 4.7 and about 10 μM ZnSO4.7H2O.

5. A method according claim 1 wherein the crystal that is prepared has a structure defined by at least a portion of the structure co-ordinates of Table A.

6. A method according claim 1 wherein the crystal belongs to the space group P212121 or wherein the crystal has the unit cell dimensions: a=56.47 Å, b=84.90 Å and c=133.99 Å.

7. A method according to claim 1 wherein the ACE protein is human ACE protein.

8. A method according to claim 1 wherein the ACE protein is crystallised in the presence of an entity.

9. A method according to claim 8 wherein the entity is a modulator of ACE.

10. A method according to claim 9 wherein the entity is an inhibitor of ACE.

11. A method according to claim 10 wherein the inhibitor of ACE is lisinopril or a derivative thereof.

12. A method according to claim 11 wherein the crystal that is prepared has a structure defined by at least a portion of the structure co-ordinates of Table B.