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HEADER DE NOVO PROTEIN 03-AUG-16 5L33
TITLE CRYSTAL STRUCTURE OF A DE NOVO DESIGNED PROTEIN WITH CURVED BETA-SHEET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DENOVO NTF2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DE NOVO NTF2, DE NOVO PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.OBERDORFER,E.MARCOS,B.BASANTA,T.M.CHIDYAUSIKU,B.SANKARAN,D.BAKER
REVDAT 2 01-FEB-17 5L33 1 JRNL
REVDAT 1 25-JAN-17 5L33 0
JRNL AUTH E.MARCOS,B.BASANTA,T.M.CHIDYAUSIKU,Y.TANG,G.OBERDORFER,
JRNL AUTH 2 G.LIU,G.V.SWAPNA,R.GUAN,D.A.SILVA,J.DOU,J.H.PEREIRA,R.XIAO,
JRNL AUTH 3 B.SANKARAN,P.H.ZWART,G.T.MONTELIONE,D.BAKER
JRNL TITL PRINCIPLES FOR DESIGNING PROTEINS WITH CAVITIES FORMED BY
JRNL TITL 2 CURVED BETA SHEETS.
JRNL REF SCIENCE V. 355 201 2017
JRNL REFN ESSN 1095-9203
JRNL PMID 28082595
JRNL DOI 10.1126/SCIENCE.AAH7389
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1616
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 6503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.720
REMARK 3 FREE R VALUE TEST SET COUNT : 307
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 50.2108 - 2.5199 0.94 3276 151 0.1653 0.1851
REMARK 3 2 2.5199 - 2.0001 0.90 2920 156 0.1922 0.2433
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 937
REMARK 3 ANGLE : 0.875 1265
REMARK 3 CHIRALITY : 0.037 130
REMARK 3 PLANARITY : 0.003 171
REMARK 3 DIHEDRAL : 17.211 371
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5915 11.5904 63.3732
REMARK 3 T TENSOR
REMARK 3 T11: 0.0995 T22: 0.2882
REMARK 3 T33: 0.1931 T12: 0.0367
REMARK 3 T13: 0.0425 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.0106 L22: 0.3384
REMARK 3 L33: 0.7953 L12: 0.0029
REMARK 3 L13: 0.2237 L23: 0.4597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: -0.3008 S13: -0.1340
REMARK 3 S21: -0.1052 S22: -0.0288 S23: -0.2702
REMARK 3 S31: 0.0384 S32: 0.8099 S33: 0.0152
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7903 15.2078 70.2200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0006 T22: 0.2225
REMARK 3 T33: 0.2138 T12: -0.0064
REMARK 3 T13: -0.0341 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 0.1192 L22: 0.3572
REMARK 3 L33: 0.2302 L12: -0.0803
REMARK 3 L13: -0.1435 L23: -0.2097
REMARK 3 S TENSOR
REMARK 3 S11: 0.4481 S12: 0.0666 S13: -0.1464
REMARK 3 S21: 0.7042 S22: 0.0209 S23: 0.3380
REMARK 3 S31: -0.7604 S32: -0.0328 S33: 0.0433
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3445 7.8822 64.1183
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.1421
REMARK 3 T33: 0.1259 T12: 0.0295
REMARK 3 T13: 0.0347 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.7606 L22: 0.6434
REMARK 3 L33: 0.7246 L12: 0.4802
REMARK 3 L13: 0.3939 L23: 0.9782
REMARK 3 S TENSOR
REMARK 3 S11: 0.1883 S12: -0.2082 S13: 0.0173
REMARK 3 S21: 0.1240 S22: -0.1681 S23: -0.0607
REMARK 3 S31: 0.2345 S32: -0.0010 S33: 0.0196
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8876 13.7542 59.3635
REMARK 3 T TENSOR
REMARK 3 T11: 0.1669 T22: 0.1174
REMARK 3 T33: 0.1550 T12: 0.0231
REMARK 3 T13: 0.0127 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.3388 L22: 0.2891
REMARK 3 L33: 1.2752 L12: 0.1611
REMARK 3 L13: -0.0725 L23: -0.6991
REMARK 3 S TENSOR
REMARK 3 S11: 0.1410 S12: -0.1006 S13: 0.0162
REMARK 3 S21: -0.1355 S22: -0.1534 S23: 0.0080
REMARK 3 S31: -0.2327 S32: -0.2210 S33: -0.0032
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5L33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223150.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6503
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.195
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM MOPS/HEPES, PH 7.5, 12.5%
REMARK 280 PEG 1000, 12.5% PEG 3350 AND 12.5% 2-METHYL-2,4-PENTANEDIOL AND
REMARK 280 0.2 M OF AMINO ACIDS (SODIUM GLUTAMATE, DL-ALANINE, GLYCINE, DL-
REMARK 280 LYSINE HCL AND DL-SERINE), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 14.12500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.19500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.18000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.19500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 14.12500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 17.18000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 206 O HOH A 232 2.11
REMARK 500 OE2 GLU A 15 O HOH A 201 2.12
REMARK 500 OE1 GLU A 15 O HOH A 202 2.17
REMARK 500 OD2 ASP A 29 O HOH A 203 2.18
REMARK 500 NH2 ARG A 31 O HOH A 204 2.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5L33 A -3 104 PDB 5L33 5L33 -3 104
SEQRES 1 A 108 GLY SER HIS MET PRO GLU GLU GLU LYS ALA ALA ARG LEU
SEQRES 2 A 108 PHE ILE GLU ALA LEU GLU LYS GLY ASP PRO GLU LEU MET
SEQRES 3 A 108 ARG LYS VAL ILE SER PRO ASP THR ARG MET GLU ASP ASN
SEQRES 4 A 108 GLY ARG GLU PHE THR GLY ASP GLU VAL VAL GLU TYR VAL
SEQRES 5 A 108 LYS GLU ILE GLN LYS ARG GLY GLU GLN TRP HIS LEU ARG
SEQRES 6 A 108 ARG TYR THR LYS GLU GLY ASN SER TRP ARG PHE GLU VAL
SEQRES 7 A 108 GLN VAL ASP ASN ASN GLY GLN THR GLU GLN TRP GLU VAL
SEQRES 8 A 108 GLN ILE GLU VAL ARG ASN GLY ARG ILE LYS ARG VAL THR
SEQRES 9 A 108 ILE THR HIS VAL
FORMUL 2 HOH *69(H2 O)
HELIX 1 AA1 PRO A 1 GLY A 17 1 17
HELIX 2 AA2 ASP A 18 ILE A 26 1 9
HELIX 3 AA3 GLY A 41 GLY A 55 1 15
SHEET 1 AA1 6 ARG A 37 THR A 40 0
SHEET 2 AA1 6 ARG A 31 ASP A 34 -1 N MET A 32 O PHE A 39
SHEET 3 AA1 6 ARG A 95 THR A 102 1 O ILE A 101 N GLU A 33
SHEET 4 AA1 6 GLN A 81 ARG A 92 -1 N GLN A 88 O THR A 100
SHEET 5 AA1 6 SER A 69 ASN A 78 -1 N PHE A 72 O VAL A 87
SHEET 6 AA1 6 GLN A 57 GLU A 66 -1 N GLN A 57 O ASP A 77
CRYST1 28.250 34.360 100.390 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.035398 0.000000 0.000000 0.00000
SCALE2 0.000000 0.029103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009961 0.00000
ATOM 1 N HIS A -1 37.000 18.222 51.819 1.00 65.70 N
ANISOU 1 N HIS A -1 7281 9719 7965 -722 1021 -356 N
ATOM 2 CA HIS A -1 36.936 18.773 53.168 1.00 70.42 C
ANISOU 2 CA HIS A -1 7826 10397 8532 -778 934 -356 C
ATOM 3 C HIS A -1 35.516 19.181 53.529 1.00 72.52 C
ANISOU 3 C HIS A -1 8240 10500 8814 -823 887 -372 C
ATOM 4 O HIS A -1 34.750 19.627 52.679 1.00 73.04 O
ANISOU 4 O HIS A -1 8474 10394 8883 -896 906 -417 O
ATOM 5 CB HIS A -1 37.871 19.980 53.316 1.00 70.20 C
ANISOU 5 CB HIS A -1 7762 10490 8422 -949 904 -408 C
ATOM 6 CG HIS A -1 37.832 20.610 54.678 1.00 68.26 C
ANISOU 6 CG HIS A -1 7474 10324 8138 -1008 815 -411 C
ATOM 7 ND1 HIS A -1 38.379 20.011 55.794 1.00 68.02 N
ANISOU 7 ND1 HIS A -1 7290 10441 8114 -907 780 -364 N
ATOM 8 CD2 HIS A -1 37.303 21.782 55.105 1.00 66.33 C
ANISOU 8 CD2 HIS A -1 7333 10025 7845 -1148 751 -456 C
ATOM 9 CE1 HIS A -1 38.193 20.788 56.846 1.00 68.59 C
ANISOU 9 CE1 HIS A -1 7369 10549 8144 -986 703 -377 C
ATOM 10 NE2 HIS A -1 37.543 21.869 56.456 1.00 68.02 N
ANISOU 10 NE2 HIS A -1 7450 10358 8038 -1130 684 -432 N
ATOM 11 N MET A 0 35.180 19.045 54.805 1.00 74.13 N
ANISOU 11 N MET A 0 8387 10754 9026 -782 820 -342 N
ATOM 12 CA MET A 0 33.829 19.307 55.268 1.00 64.64 C
ANISOU 12 CA MET A 0 7308 9408 7843 -808 773 -355 C
ATOM 13 C MET A 0 33.835 20.246 56.472 1.00 54.23 C
ANISOU 13 C MET A 0 5967 8165 6473 -912 679 -373 C
ATOM 14 O MET A 0 34.466 19.951 57.486 1.00 56.07 O
ANISOU 14 O MET A 0 6058 8551 6694 -854 643 -332 O
ATOM 15 CB MET A 0 33.149 17.983 55.612 1.00 65.98 C
ANISOU 15 CB MET A 0 7451 9534 8086 -620 790 -294 C
ATOM 16 CG MET A 0 31.648 18.034 55.700 1.00 63.21 C
ANISOU 16 CG MET A 0 7252 8994 7769 -629 772 -317 C
ATOM 17 SD MET A 0 31.011 16.369 55.920 1.00 53.17 S
ANISOU 17 SD MET A 0 5955 7668 6581 -384 802 -248 S
ATOM 18 CE MET A 0 30.877 15.829 54.209 1.00 35.55 C
ANISOU 18 CE MET A 0 3854 5258 4395 -312 893 -262 C
ATOM 19 N PRO A 1 33.142 21.390 56.357 1.00 44.33 N
ANISOU 19 N PRO A 1 4868 6792 5183 -1055 635 -437 N
ATOM 20 CA PRO A 1 33.003 22.335 57.475 1.00 42.11 C
ANISOU 20 CA PRO A 1 4597 6556 4847 -1140 543 -456 C
ATOM 21 C PRO A 1 32.424 21.668 58.723 1.00 42.39 C
ANISOU 21 C PRO A 1 4565 6618 4922 -1037 494 -403 C
ATOM 22 O PRO A 1 31.745 20.640 58.632 1.00 35.83 O
ANISOU 22 O PRO A 1 3735 5716 4161 -921 524 -367 O
ATOM 23 CB PRO A 1 32.049 23.403 56.931 1.00 41.00 C
ANISOU 23 CB PRO A 1 4677 6228 4674 -1252 515 -528 C
ATOM 24 CG PRO A 1 31.425 22.792 55.691 1.00 42.97 C
ANISOU 24 CG PRO A 1 5034 6308 4985 -1212 583 -542 C
ATOM 25 CD PRO A 1 32.443 21.848 55.147 1.00 41.17 C
ANISOU 25 CD PRO A 1 4660 6197 4787 -1130 666 -496 C
ATOM 26 N GLU A 2 32.697 22.256 59.882 1.00 44.50 N
ANISOU 26 N GLU A 2 4783 6985 5139 -1073 423 -398 N
ATOM 27 CA GLU A 2 32.383 21.616 61.147 1.00 45.55 C
ANISOU 27 CA GLU A 2 4834 7173 5300 -974 376 -343 C
ATOM 28 C GLU A 2 30.875 21.424 61.352 1.00 39.29 C
ANISOU 28 C GLU A 2 4160 6212 4556 -949 346 -349 C
ATOM 29 O GLU A 2 30.444 20.430 61.936 1.00 36.97 O
ANISOU 29 O GLU A 2 3806 5927 4314 -831 341 -298 O
ATOM 30 CB GLU A 2 32.973 22.425 62.297 1.00 56.76 C
ANISOU 30 CB GLU A 2 6204 8715 6648 -1030 311 -344 C
ATOM 31 CG GLU A 2 33.026 21.671 63.611 1.00 69.12 C
ANISOU 31 CG GLU A 2 7658 10373 8233 -919 270 -282 C
ATOM 32 CD GLU A 2 33.393 22.564 64.779 1.00 76.60 C
ANISOU 32 CD GLU A 2 8590 11404 9109 -978 210 -287 C
ATOM 33 OE1 GLU A 2 33.775 23.728 64.541 1.00 81.03 O
ANISOU 33 OE1 GLU A 2 9208 11976 9605 -1096 208 -334 O
ATOM 34 OE2 GLU A 2 33.293 22.105 65.937 1.00 77.29 O
ANISOU 34 OE2 GLU A 2 8618 11543 9205 -903 170 -242 O
ATOM 35 N GLU A 3 30.075 22.366 60.868 1.00 34.72 N
ANISOU 35 N GLU A 3 3759 5478 3957 -1046 326 -412 N
ATOM 36 CA GLU A 3 28.630 22.278 61.041 1.00 33.18 C
ANISOU 36 CA GLU A 3 3696 5106 3805 -1019 292 -427 C
ATOM 37 C GLU A 3 28.045 21.144 60.221 1.00 30.52 C
ANISOU 37 C GLU A 3 3379 4663 3556 -945 358 -420 C
ATOM 38 O GLU A 3 27.223 20.370 60.710 1.00 32.54 O
ANISOU 38 O GLU A 3 3628 4866 3868 -866 349 -396 O
ATOM 39 CB GLU A 3 27.955 23.591 60.652 1.00 41.94 C
ANISOU 39 CB GLU A 3 5006 6058 4869 -1079 266 -474 C
ATOM 40 CG GLU A 3 26.435 23.513 60.639 1.00 44.88 C
ANISOU 40 CG GLU A 3 5526 6223 5303 -996 238 -467 C
ATOM 41 CD GLU A 3 25.776 24.831 60.258 1.00 48.24 C
ANISOU 41 CD GLU A 3 6099 6512 5719 -972 218 -448 C
ATOM 42 OE1 GLU A 3 26.322 25.897 60.611 1.00 50.33 O
ANISOU 42 OE1 GLU A 3 6352 6849 5923 -1031 208 -443 O
ATOM 43 OE2 GLU A 3 24.709 24.805 59.608 1.00 47.76 O
ANISOU 43 OE2 GLU A 3 6142 6282 5723 -875 203 -424 O
ATOM 44 N GLU A 4 28.465 21.048 58.967 1.00 26.50 N
ANISOU 44 N GLU A 4 2901 4115 3052 -963 435 -439 N
ATOM 45 CA GLU A 4 27.969 19.998 58.095 1.00 24.62 C
ANISOU 45 CA GLU A 4 2714 3752 2890 -859 515 -425 C
ATOM 46 C GLU A 4 28.428 18.625 58.602 1.00 23.55 C
ANISOU 46 C GLU A 4 2422 3734 2792 -664 540 -333 C
ATOM 47 O GLU A 4 27.666 17.644 58.560 1.00 21.35 O
ANISOU 47 O GLU A 4 2208 3322 2580 -509 540 -297 O
ATOM 48 CB GLU A 4 28.434 20.229 56.659 1.00 21.58 C
ANISOU 48 CB GLU A 4 2398 3309 2493 -913 595 -461 C
ATOM 49 CG GLU A 4 27.890 19.190 55.680 1.00 22.42 C
ANISOU 49 CG GLU A 4 2610 3234 2676 -753 647 -440 C
ATOM 50 CD GLU A 4 28.402 19.393 54.271 1.00 27.38 C
ANISOU 50 CD GLU A 4 3300 3813 3289 -804 729 -474 C
ATOM 51 OE1 GLU A 4 29.111 20.402 54.050 1.00 32.91 O
ANISOU 51 OE1 GLU A 4 3984 4601 3918 -960 728 -516 O
ATOM 52 OE2 GLU A 4 28.110 18.539 53.399 1.00 27.62 O
ANISOU 52 OE2 GLU A 4 3403 3714 3379 -674 779 -455 O
ATOM 53 N LYS A 5 29.669 18.568 59.079 1.00 22.07 N
ANISOU 53 N LYS A 5 2040 3786 2561 -667 554 -298 N
ATOM 54 CA LYS A 5 30.255 17.336 59.605 1.00 24.78 C
ANISOU 54 CA LYS A 5 2228 4260 2929 -486 568 -215 C
ATOM 55 C LYS A 5 29.459 16.766 60.777 1.00 25.43 C
ANISOU 55 C LYS A 5 2301 4322 3040 -391 506 -172 C
ATOM 56 O LYS A 5 29.228 15.556 60.851 1.00 27.94 O
ANISOU 56 O LYS A 5 2612 4597 3408 -210 518 -111 O
ATOM 57 CB LYS A 5 31.707 17.579 60.046 1.00 30.60 C
ANISOU 57 CB LYS A 5 2820 5191 3614 -504 545 -193 C
ATOM 58 CG LYS A 5 32.358 16.401 60.790 1.00 36.72 C
ANISOU 58 CG LYS A 5 3455 6090 4408 -328 535 -116 C
ATOM 59 CD LYS A 5 33.781 16.730 61.277 1.00 40.47 C
ANISOU 59 CD LYS A 5 3800 6750 4827 -363 510 -113 C
ATOM 60 CE LYS A 5 34.341 15.630 62.184 1.00 41.82 C
ANISOU 60 CE LYS A 5 3855 7028 5007 -203 482 -47 C
ATOM 61 NZ LYS A 5 35.803 15.802 62.463 1.00 41.44 N
ANISOU 61 NZ LYS A 5 3681 7157 4906 -221 475 -52 N
ATOM 62 N ALA A 6 29.059 17.634 61.702 1.00 23.13 N
ANISOU 62 N ALA A 6 2021 4052 2715 -508 431 -200 N
ATOM 63 CA ALA A 6 28.319 17.193 62.883 1.00 22.45 C
ANISOU 63 CA ALA A 6 1932 3948 2650 -432 364 -162 C
ATOM 64 C ALA A 6 26.977 16.580 62.491 1.00 19.15 C
ANISOU 64 C ALA A 6 1696 3277 2303 -337 360 -163 C
ATOM 65 O ALA A 6 26.587 15.540 63.010 1.00 16.20 O
ANISOU 65 O ALA A 6 1312 2876 1968 -189 349 -104 O
ATOM 66 CB ALA A 6 28.110 18.351 63.838 1.00 20.84 C
ANISOU 66 CB ALA A 6 1747 3775 2395 -575 276 -200 C
ATOM 67 N ALA A 7 26.271 17.240 61.580 1.00 16.65 N
ANISOU 67 N ALA A 7 1549 2776 2000 -426 367 -235 N
ATOM 68 CA ALA A 7 24.978 16.740 61.124 1.00 18.53 C
ANISOU 68 CA ALA A 7 1964 2769 2306 -345 364 -249 C
ATOM 69 C ALA A 7 25.152 15.408 60.402 1.00 17.71 C
ANISOU 69 C ALA A 7 1857 2613 2258 -163 434 -190 C
ATOM 70 O ALA A 7 24.344 14.490 60.563 1.00 17.11 O
ANISOU 70 O ALA A 7 1847 2418 2237 -34 427 -156 O
ATOM 71 CB ALA A 7 24.291 17.769 60.223 1.00 17.04 C
ANISOU 71 CB ALA A 7 1957 2402 2116 -477 356 -345 C
ATOM 72 N ARG A 8 26.225 15.306 59.622 1.00 19.44 N
ANISOU 72 N ARG A 8 1998 2928 2459 -157 500 -178 N
ATOM 73 CA ARG A 8 26.544 14.088 58.891 1.00 16.43 C
ANISOU 73 CA ARG A 8 1600 2519 2124 13 568 -124 C
ATOM 74 C ARG A 8 26.830 12.921 59.830 1.00 18.78 C
ANISOU 74 C ARG A 8 1773 2928 2434 177 553 -34 C
ATOM 75 O ARG A 8 26.430 11.793 59.561 1.00 20.42 O
ANISOU 75 O ARG A 8 2032 3033 2696 337 576 12 O
ATOM 76 CB ARG A 8 27.737 14.309 57.972 1.00 18.02 C
ANISOU 76 CB ARG A 8 1721 2833 2294 -28 639 -135 C
ATOM 77 CG ARG A 8 27.380 14.928 56.637 1.00 23.25 C
ANISOU 77 CG ARG A 8 2545 3325 2966 -117 679 -205 C
ATOM 78 CD ARG A 8 26.461 14.020 55.842 1.00 25.80 C
ANISOU 78 CD ARG A 8 3017 3418 3367 23 707 -193 C
ATOM 79 NE ARG A 8 27.102 12.767 55.448 1.00 29.10 N
ANISOU 79 NE ARG A 8 3350 3893 3816 199 767 -124 N
ATOM 80 CZ ARG A 8 27.911 12.630 54.395 1.00 33.32 C
ANISOU 80 CZ ARG A 8 3852 4466 4343 212 842 -129 C
ATOM 81 NH1 ARG A 8 28.209 13.673 53.626 1.00 32.20 N
ANISOU 81 NH1 ARG A 8 3759 4313 4161 52 870 -196 N
ATOM 82 NH2 ARG A 8 28.434 11.443 54.110 1.00 37.36 N
ANISOU 82 NH2 ARG A 8 4286 5027 4883 385 887 -67 N
ATOM 83 N LEU A 9 27.541 13.181 60.918 1.00 18.59 N
ANISOU 83 N LEU A 9 1592 3114 2357 140 514 -11 N
ATOM 84 CA LEU A 9 27.832 12.133 61.893 1.00 20.36 C
ANISOU 84 CA LEU A 9 1703 3450 2584 291 492 71 C
ATOM 85 C LEU A 9 26.562 11.609 62.585 1.00 20.22 C
ANISOU 85 C LEU A 9 1796 3281 2606 359 442 95 C
ATOM 86 O LEU A 9 26.466 10.420 62.876 1.00 20.03 O
ANISOU 86 O LEU A 9 1759 3242 2610 523 445 163 O
ATOM 87 CB LEU A 9 28.832 12.643 62.934 1.00 17.28 C
ANISOU 87 CB LEU A 9 1126 3315 2125 222 455 83 C
ATOM 88 CG LEU A 9 30.247 12.833 62.390 1.00 21.40 C
ANISOU 88 CG LEU A 9 1553 3965 2615 188 487 71 C
ATOM 89 CD1 LEU A 9 31.120 13.409 63.482 1.00 24.69 C
ANISOU 89 CD1 LEU A 9 1859 4551 2970 109 423 71 C
ATOM 90 CD2 LEU A 9 30.796 11.510 61.911 1.00 21.76 C
ANISOU 90 CD2 LEU A 9 1581 3992 2693 363 518 122 C
ATOM 91 N PHE A 10 25.603 12.501 62.842 1.00 16.60 N
ANISOU 91 N PHE A 10 1447 2713 2146 231 396 34 N
ATOM 92 CA PHE A 10 24.312 12.112 63.413 1.00 16.10 C
ANISOU 92 CA PHE A 10 1499 2497 2121 275 353 39 C
ATOM 93 C PHE A 10 23.641 11.120 62.474 1.00 13.42 C
ANISOU 93 C PHE A 10 1289 1958 1851 408 401 55 C
ATOM 94 O PHE A 10 23.133 10.086 62.899 1.00 12.32 O
ANISOU 94 O PHE A 10 1178 1759 1744 537 393 109 O
ATOM 95 CB PHE A 10 23.414 13.342 63.631 1.00 11.09 C
ANISOU 95 CB PHE A 10 968 1771 1474 108 299 -47 C
ATOM 96 CG PHE A 10 22.105 13.037 64.320 1.00 12.27 C
ANISOU 96 CG PHE A 10 1220 1787 1655 139 251 -52 C
ATOM 97 CD1 PHE A 10 21.006 12.609 63.603 1.00 13.48 C
ANISOU 97 CD1 PHE A 10 1537 1714 1870 193 270 -81 C
ATOM 98 CD2 PHE A 10 21.989 13.180 65.694 1.00 16.21 C
ANISOU 98 CD2 PHE A 10 1648 2393 2119 110 189 -32 C
ATOM 99 CE1 PHE A 10 19.818 12.317 64.242 1.00 15.00 C
ANISOU 99 CE1 PHE A 10 1816 1793 2089 217 229 -91 C
ATOM 100 CE2 PHE A 10 20.791 12.897 66.345 1.00 16.42 C
ANISOU 100 CE2 PHE A 10 1764 2305 2170 132 148 -41 C
ATOM 101 CZ PHE A 10 19.708 12.465 65.616 1.00 16.90 C
ANISOU 101 CZ PHE A 10 1984 2145 2293 183 170 -72 C
ATOM 102 N ILE A 11 23.621 11.465 61.194 1.00 12.55 N
ANISOU 102 N ILE A 11 1264 1741 1763 370 449 6 N
ATOM 103 CA ILE A 11 23.007 10.631 60.175 1.00 12.99 C
ANISOU 103 CA ILE A 11 1450 1602 1886 484 496 12 C
ATOM 104 C ILE A 11 23.742 9.311 60.031 1.00 15.05 C
ANISOU 104 C ILE A 11 1640 1932 2146 621 504 90 C
ATOM 105 O ILE A 11 23.110 8.253 59.861 1.00 15.69 O
ANISOU 105 O ILE A 11 1822 1904 2235 644 442 107 O
ATOM 106 CB ILE A 11 22.987 11.358 58.806 1.00 17.54 C
ANISOU 106 CB ILE A 11 2127 2066 2472 397 539 -61 C
ATOM 107 CG1 ILE A 11 22.132 12.623 58.891 1.00 16.26 C
ANISOU 107 CG1 ILE A 11 2078 1803 2295 230 487 -155 C
ATOM 108 CG2 ILE A 11 22.487 10.439 57.696 1.00 16.04 C
ANISOU 108 CG2 ILE A 11 2053 1742 2300 444 500 -42 C
ATOM 109 CD1 ILE A 11 20.682 12.394 59.252 1.00 11.37 C
ANISOU 109 CD1 ILE A 11 1581 1042 1697 236 404 -165 C
ATOM 110 N GLU A 12 25.073 9.367 60.115 1.00 15.46 N
ANISOU 110 N GLU A 12 1524 2188 2162 646 543 122 N
ATOM 111 CA GLU A 12 25.910 8.164 60.045 1.00 17.98 C
ANISOU 111 CA GLU A 12 1790 2572 2470 740 523 177 C
ATOM 112 C GLU A 12 25.597 7.187 61.182 1.00 18.78 C
ANISOU 112 C GLU A 12 1901 2674 2561 801 456 232 C
ATOM 113 O GLU A 12 25.565 5.978 60.976 1.00 18.90 O
ANISOU 113 O GLU A 12 1977 2624 2581 859 434 261 O
ATOM 114 CB GLU A 12 27.395 8.530 60.088 1.00 30.75 C
ANISOU 114 CB GLU A 12 3224 4417 4041 725 556 185 C
ATOM 115 CG GLU A 12 28.349 7.343 59.967 1.00 46.67 C
ANISOU 115 CG GLU A 12 5191 6494 6047 827 544 231 C
ATOM 116 CD GLU A 12 28.452 6.815 58.541 1.00 60.99 C
ANISOU 116 CD GLU A 12 7085 8197 7892 859 582 215 C
ATOM 117 OE1 GLU A 12 27.648 5.938 58.161 1.00 61.08 O
ANISOU 117 OE1 GLU A 12 7235 8041 7932 895 552 226 O
ATOM 118 OE2 GLU A 12 29.335 7.283 57.789 1.00 74.12 O
ANISOU 118 OE2 GLU A 12 8671 9948 9542 828 636 185 O
ATOM 119 N ALA A 13 25.367 7.722 62.376 1.00 13.62 N
ANISOU 119 N ALA A 13 1187 2103 1886 773 427 241 N
ATOM 120 CA ALA A 13 25.045 6.895 63.536 1.00 15.64 C
ANISOU 120 CA ALA A 13 1456 2362 2125 821 370 289 C
ATOM 121 C ALA A 13 23.732 6.145 63.321 1.00 15.52 C
ANISOU 121 C ALA A 13 1618 2136 2143 811 343 274 C
ATOM 122 O ALA A 13 23.587 5.004 63.732 1.00 18.30 O
ANISOU 122 O ALA A 13 2007 2462 2484 850 316 306 O
ATOM 123 CB ALA A 13 24.971 7.746 64.788 1.00 15.54 C
ANISOU 123 CB ALA A 13 1347 2478 2080 770 336 293 C
ATOM 124 N LEU A 14 22.785 6.789 62.655 1.00 16.42 N
ANISOU 124 N LEU A 14 1835 2115 2288 736 347 212 N
ATOM 125 CA LEU A 14 21.519 6.158 62.308 1.00 17.36 C
ANISOU 125 CA LEU A 14 2096 2078 2423 674 300 173 C
ATOM 126 C LEU A 14 21.733 5.074 61.250 1.00 21.74 C
ANISOU 126 C LEU A 14 2691 2596 2975 697 312 188 C
ATOM 127 O LEU A 14 21.208 3.961 61.365 1.00 20.42 O
ANISOU 127 O LEU A 14 2579 2397 2782 721 321 230 O
ATOM 128 CB LEU A 14 20.521 7.224 61.821 1.00 15.31 C
ANISOU 128 CB LEU A 14 1918 1721 2180 569 278 95 C
ATOM 129 CG LEU A 14 20.155 8.328 62.828 1.00 16.11 C
ANISOU 129 CG LEU A 14 2003 1836 2284 543 277 76 C
ATOM 130 CD1 LEU A 14 19.245 9.363 62.191 1.00 18.47 C
ANISOU 130 CD1 LEU A 14 2396 2035 2585 426 243 -10 C
ATOM 131 CD2 LEU A 14 19.500 7.730 64.030 1.00 18.61 C
ANISOU 131 CD2 LEU A 14 2324 2158 2590 550 229 98 C
ATOM 132 N GLU A 15 22.499 5.420 60.214 1.00 18.58 N
ANISOU 132 N GLU A 15 2263 2210 2586 705 344 172 N
ATOM 133 CA GLU A 15 22.821 4.501 59.135 1.00 21.35 C
ANISOU 133 CA GLU A 15 2648 2537 2925 745 379 206 C
ATOM 134 C GLU A 15 23.514 3.243 59.644 1.00 24.12 C
ANISOU 134 C GLU A 15 2953 2956 3255 841 384 269 C
ATOM 135 O GLU A 15 23.214 2.143 59.190 1.00 26.01 O
ANISOU 135 O GLU A 15 3256 3156 3471 872 406 307 O
ATOM 136 CB GLU A 15 23.711 5.183 58.092 1.00 21.97 C
ANISOU 136 CB GLU A 15 2682 2641 3023 740 409 169 C
ATOM 137 CG GLU A 15 22.980 6.139 57.180 1.00 30.63 C
ANISOU 137 CG GLU A 15 3866 3645 4128 650 415 119 C
ATOM 138 CD GLU A 15 23.848 6.598 56.011 1.00 32.66 C
ANISOU 138 CD GLU A 15 4099 3917 4395 654 464 95 C
ATOM 139 OE1 GLU A 15 23.674 6.049 54.912 1.00 25.97 O
ANISOU 139 OE1 GLU A 15 3317 3009 3541 651 481 116 O
ATOM 140 OE2 GLU A 15 24.702 7.505 56.194 1.00 35.11 O
ANISOU 140 OE2 GLU A 15 4324 4311 4706 674 536 91 O
ATOM 141 N LYS A 16 24.449 3.414 60.569 1.00 24.10 N
ANISOU 141 N LYS A 16 2833 3072 3250 887 370 282 N
ATOM 142 CA LYS A 16 25.190 2.299 61.114 1.00 24.94 C
ANISOU 142 CA LYS A 16 2889 3254 3331 975 364 336 C
ATOM 143 C LYS A 16 24.422 1.619 62.240 1.00 28.21 C
ANISOU 143 C LYS A 16 3352 3646 3721 986 338 371 C
ATOM 144 O LYS A 16 24.797 0.534 62.681 1.00 33.29 O
ANISOU 144 O LYS A 16 3986 4328 4333 1061 338 420 O
ATOM 145 CB LYS A 16 26.548 2.765 61.624 1.00 24.54 C
ANISOU 145 CB LYS A 16 2687 3385 3251 1040 385 371 C
ATOM 146 CG LYS A 16 27.505 3.249 60.559 1.00 30.53 C
ANISOU 146 CG LYS A 16 3376 4206 4016 1050 431 353 C
ATOM 147 CD LYS A 16 27.904 2.125 59.632 1.00 42.81 C
ANISOU 147 CD LYS A 16 4970 5718 5579 1102 440 361 C
ATOM 148 CE LYS A 16 28.719 2.637 58.442 1.00 51.49 C
ANISOU 148 CE LYS A 16 6015 6860 6690 1100 491 333 C
ATOM 149 NZ LYS A 16 30.145 2.215 58.516 1.00 58.78 N
ANISOU 149 NZ LYS A 16 6808 7941 7583 1180 505 358 N
ATOM 150 N GLY A 17 23.344 2.250 62.700 1.00 22.52 N
ANISOU 150 N GLY A 17 2683 2863 3012 913 318 341 N
ATOM 151 CA GLY A 17 22.592 1.729 63.824 1.00 21.20 C
ANISOU 151 CA GLY A 17 2552 2680 2823 914 296 363 C
ATOM 152 C GLY A 17 23.493 1.584 65.033 1.00 23.52 C
ANISOU 152 C GLY A 17 2743 3095 3100 972 265 399 C
ATOM 153 O GLY A 17 23.414 0.602 65.768 1.00 27.98 O
ANISOU 153 O GLY A 17 3325 3672 3634 1022 259 441 O
ATOM 154 N ASP A 18 24.374 2.554 65.225 1.00 21.12 N
ANISOU 154 N ASP A 18 2328 2915 2781 992 277 412 N
ATOM 155 CA ASP A 18 25.424 2.426 66.209 1.00 25.64 C
ANISOU 155 CA ASP A 18 2783 3654 3307 1060 264 465 C
ATOM 156 C ASP A 18 25.271 3.432 67.346 1.00 26.34 C
ANISOU 156 C ASP A 18 2800 3837 3372 1021 236 470 C
ATOM 157 O ASP A 18 25.628 4.597 67.202 1.00 26.22 O
ANISOU 157 O ASP A 18 2698 3910 3353 974 243 448 O
ATOM 158 CB ASP A 18 26.785 2.591 65.548 1.00 31.97 C
ANISOU 158 CB ASP A 18 3477 4577 4095 1104 290 472 C
ATOM 159 CG ASP A 18 27.922 2.548 66.545 1.00 39.39 C
ANISOU 159 CG ASP A 18 4280 5707 4979 1155 267 511 C
ATOM 160 OD1 ASP A 18 27.727 1.986 67.644 1.00 39.89 O
ANISOU 160 OD1 ASP A 18 4356 5785 5015 1185 233 544 O
ATOM 161 OD2 ASP A 18 29.006 3.089 66.231 1.00 43.43 O
ANISOU 161 OD2 ASP A 18 4673 6356 5472 1155 281 502 O
ATOM 162 N PRO A 19 24.763 2.964 68.494 1.00 28.34 N
ANISOU 162 N PRO A 19 3081 4082 3605 1030 203 495 N
ATOM 163 CA PRO A 19 24.548 3.825 69.667 1.00 27.68 C
ANISOU 163 CA PRO A 19 2934 4088 3494 987 167 501 C
ATOM 164 C PRO A 19 25.829 4.473 70.157 1.00 23.37 C
ANISOU 164 C PRO A 19 2226 3755 2900 987 151 517 C
ATOM 165 O PRO A 19 25.794 5.601 70.653 1.00 24.01 O
ANISOU 165 O PRO A 19 2233 3925 2963 908 127 496 O
ATOM 166 CB PRO A 19 23.995 2.862 70.724 1.00 26.54 C
ANISOU 166 CB PRO A 19 2852 3900 3333 1018 140 532 C
ATOM 167 CG PRO A 19 23.436 1.708 69.944 1.00 32.33 C
ANISOU 167 CG PRO A 19 3710 4475 4100 1037 164 519 C
ATOM 168 CD PRO A 19 24.308 1.580 68.728 1.00 32.49 C
ANISOU 168 CD PRO A 19 3702 4512 4132 1070 196 513 C
ATOM 169 N GLU A 20 26.944 3.770 70.035 1.00 21.45 N
ANISOU 169 N GLU A 20 1926 3594 2631 1061 159 545 N
ATOM 170 CA GLU A 20 28.216 4.325 70.466 1.00 28.12 C
ANISOU 170 CA GLU A 20 2618 4640 3427 1051 142 549 C
ATOM 171 C GLU A 20 28.568 5.591 69.685 1.00 31.21 C
ANISOU 171 C GLU A 20 2934 5097 3828 961 164 499 C
ATOM 172 O GLU A 20 28.946 6.599 70.283 1.00 33.60 O
ANISOU 172 O GLU A 20 3141 5531 4095 873 138 478 O
ATOM 173 CB GLU A 20 29.332 3.289 70.334 1.00 28.60 C
ANISOU 173 CB GLU A 20 2639 4765 3463 1155 149 580 C
ATOM 174 CG GLU A 20 29.223 2.188 71.371 1.00 36.15 C
ANISOU 174 CG GLU A 20 3637 5706 4392 1231 120 625 C
ATOM 175 CD GLU A 20 29.172 2.733 72.797 1.00 39.12 C
ANISOU 175 CD GLU A 20 3956 6183 4726 1188 73 637 C
ATOM 176 OE1 GLU A 20 30.055 3.539 73.161 1.00 41.70 O
ANISOU 176 OE1 GLU A 20 4158 6671 5015 1145 55 623 O
ATOM 177 OE2 GLU A 20 28.246 2.363 73.548 1.00 37.97 O
ANISOU 177 OE2 GLU A 20 3890 5954 4582 1187 54 655 O
ATOM 178 N LEU A 21 28.442 5.552 68.362 1.00 27.38 N
ANISOU 178 N LEU A 21 2499 4516 3386 968 211 475 N
ATOM 179 CA LEU A 21 28.703 6.763 67.587 1.00 27.66 C
ANISOU 179 CA LEU A 21 2474 4604 3431 871 239 422 C
ATOM 180 C LEU A 21 27.729 7.873 67.973 1.00 21.96 C
ANISOU 180 C LEU A 21 1772 3855 2718 759 219 385 C
ATOM 181 O LEU A 21 28.147 9.011 68.154 1.00 27.48 O
ANISOU 181 O LEU A 21 2383 4674 3386 644 208 347 O
ATOM 182 CB LEU A 21 28.630 6.507 66.077 1.00 34.55 C
ANISOU 182 CB LEU A 21 3415 5361 4354 899 298 399 C
ATOM 183 CG LEU A 21 28.773 7.794 65.235 1.00 38.37 C
ANISOU 183 CG LEU A 21 3853 5881 4846 787 337 338 C
ATOM 184 CD1 LEU A 21 29.973 8.667 65.649 1.00 36.72 C
ANISOU 184 CD1 LEU A 21 3488 5886 4579 699 325 316 C
ATOM 185 CD2 LEU A 21 28.829 7.489 63.732 1.00 36.30 C
ANISOU 185 CD2 LEU A 21 3656 5510 4627 820 399 316 C
ATOM 186 N MET A 22 26.446 7.553 68.106 1.00 17.62 N
ANISOU 186 N MET A 22 1345 3146 2205 780 211 391 N
ATOM 187 CA MET A 22 25.452 8.572 68.459 1.00 18.91 C
ANISOU 187 CA MET A 22 1529 3278 2378 680 189 350 C
ATOM 188 C MET A 22 25.765 9.271 69.778 1.00 23.18 C
ANISOU 188 C MET A 22 1970 3977 2859 595 128 350 C
ATOM 189 O MET A 22 25.567 10.478 69.921 1.00 19.46 O
ANISOU 189 O MET A 22 1464 3558 2372 460 107 297 O
ATOM 190 CB MET A 22 24.052 7.971 68.555 1.00 13.75 C
ANISOU 190 CB MET A 22 1028 2428 1770 724 183 356 C
ATOM 191 CG MET A 22 22.985 9.045 68.829 1.00 13.18 C
ANISOU 191 CG MET A 22 987 2312 1711 622 158 302 C
ATOM 192 SD MET A 22 22.880 10.307 67.541 1.00 19.32 S
ANISOU 192 SD MET A 22 1832 3005 2506 470 188 199 S
ATOM 193 CE MET A 22 21.756 9.531 66.356 1.00 13.14 C
ANISOU 193 CE MET A 22 1243 1944 1805 561 239 182 C
ATOM 194 N AARG A 23 26.246 8.499 70.748 0.50 26.73 N
ANISOU 194 N AARG A 23 2391 4492 3273 663 98 403 N
ATOM 195 N BARG A 23 26.254 8.497 70.739 0.50 26.77 N
ANISOU 195 N BARG A 23 2397 4498 3278 663 98 403 N
ATOM 196 CA AARG A 23 26.576 9.042 72.062 0.50 30.11 C
ANISOU 196 CA AARG A 23 2744 5053 3643 594 42 405 C
ATOM 197 CA BARG A 23 26.571 9.026 72.059 0.50 30.18 C
ANISOU 197 CA BARG A 23 2754 5060 3653 595 43 406 C
ATOM 198 C AARG A 23 27.630 10.133 71.946 0.50 29.57 C
ANISOU 198 C AARG A 23 2568 5132 3534 484 39 363 C
ATOM 199 C BARG A 23 27.651 10.102 71.973 0.50 29.63 C
ANISOU 199 C BARG A 23 2575 5142 3542 488 38 365 C
ATOM 200 O AARG A 23 27.585 11.130 72.657 0.50 28.40 O
ANISOU 200 O AARG A 23 2394 5045 3352 365 -1 330 O
ATOM 201 O BARG A 23 27.639 11.063 72.733 0.50 28.65 O
ANISOU 201 O BARG A 23 2422 5082 3380 372 -2 334 O
ATOM 202 CB AARG A 23 27.062 7.934 72.999 0.50 34.24 C
ANISOU 202 CB AARG A 23 3256 5620 4134 700 23 468 C
ATOM 203 CB BARG A 23 27.008 7.891 72.987 0.50 34.10 C
ANISOU 203 CB BARG A 23 3244 5595 4119 704 24 469 C
ATOM 204 CG AARG A 23 27.132 8.354 74.460 0.50 37.79 C
ANISOU 204 CG AARG A 23 3660 6167 4532 642 -31 474 C
ATOM 205 CG BARG A 23 26.939 8.239 74.462 0.50 37.94 C
ANISOU 205 CG BARG A 23 3696 6161 4557 651 -31 477 C
ATOM 206 CD AARG A 23 27.707 7.250 75.325 0.50 42.00 C
ANISOU 206 CD AARG A 23 4177 6750 5032 750 -45 532 C
ATOM 207 CD BARG A 23 27.220 7.024 75.322 0.50 42.36 C
ANISOU 207 CD BARG A 23 4267 6735 5091 764 -43 538 C
ATOM 208 NE AARG A 23 27.019 5.980 75.113 0.50 42.53 N
ANISOU 208 NE AARG A 23 4352 6675 5132 859 -25 571 N
ATOM 209 NE BARG A 23 27.955 7.384 76.528 0.50 44.25 N
ANISOU 209 NE BARG A 23 4421 7119 5272 729 -83 545 N
ATOM 210 CZ AARG A 23 25.918 5.606 75.757 0.50 42.47 C
ANISOU 210 CZ AARG A 23 4434 6567 5136 863 -41 585 C
ATOM 211 CZ BARG A 23 29.269 7.576 76.563 0.50 47.04 C
ANISOU 211 CZ BARG A 23 4672 7614 5589 733 -83 541 C
ATOM 212 NH1AARG A 23 25.370 6.409 76.660 0.50 40.81 N
ANISOU 212 NH1AARG A 23 4212 6388 4907 772 -81 566 N
ATOM 213 NH1BARG A 23 29.992 7.440 75.458 0.50 46.14 N
ANISOU 213 NH1BARG A 23 4521 7521 5489 768 -46 531 N
ATOM 214 NH2AARG A 23 25.364 4.428 75.497 0.50 41.81 N
ANISOU 214 NH2AARG A 23 4458 6349 5080 948 -19 612 N
ATOM 215 NH2BARG A 23 29.858 7.899 77.704 0.50 50.62 N
ANISOU 215 NH2BARG A 23 5060 8183 5992 701 -119 545 N
ATOM 216 N LYS A 24 28.563 9.948 71.018 1.00 33.03 N
ANISOU 216 N LYS A 24 2960 5614 3977 520 82 361 N
ATOM 217 CA LYS A 24 29.650 10.906 70.821 1.00 36.65 C
ANISOU 217 CA LYS A 24 3323 6208 4395 418 86 319 C
ATOM 218 C LYS A 24 29.225 12.164 70.070 1.00 30.95 C
ANISOU 218 C LYS A 24 2628 5446 3685 269 101 249 C
ATOM 219 O LYS A 24 29.904 13.182 70.145 1.00 33.71 O
ANISOU 219 O LYS A 24 2928 5888 3992 150 90 207 O
ATOM 220 CB LYS A 24 30.807 10.238 70.080 1.00 45.30 C
ANISOU 220 CB LYS A 24 4357 7366 5490 506 128 336 C
ATOM 221 CG LYS A 24 31.577 9.244 70.928 1.00 50.58 C
ANISOU 221 CG LYS A 24 4975 8119 6124 622 104 389 C
ATOM 222 CD LYS A 24 32.182 9.930 72.136 1.00 54.16 C
ANISOU 222 CD LYS A 24 5350 8712 6516 546 56 380 C
ATOM 223 CE LYS A 24 33.003 8.964 72.956 1.00 57.75 C
ANISOU 223 CE LYS A 24 5751 9257 6936 661 35 428 C
ATOM 224 NZ LYS A 24 33.682 9.659 74.078 1.00 60.26 N
ANISOU 224 NZ LYS A 24 5990 9710 7194 591 -6 415 N
ATOM 225 N VAL A 25 28.108 12.096 69.352 1.00 27.90 N
ANISOU 225 N VAL A 25 2332 4915 3353 275 126 232 N
ATOM 226 CA VAL A 25 27.638 13.226 68.553 1.00 26.26 C
ANISOU 226 CA VAL A 25 2166 4655 3154 133 144 158 C
ATOM 227 C VAL A 25 26.725 14.189 69.313 1.00 24.51 C
ANISOU 227 C VAL A 25 1999 4397 2916 1 83 113 C
ATOM 228 O VAL A 25 26.795 15.401 69.130 1.00 22.88 O
ANISOU 228 O VAL A 25 1818 4195 2681 -153 67 47 O
ATOM 229 CB VAL A 25 26.868 12.742 67.306 1.00 29.11 C
ANISOU 229 CB VAL A 25 2613 4867 3581 200 210 150 C
ATOM 230 CG1 VAL A 25 26.443 13.921 66.467 1.00 30.44 C
ANISOU 230 CG1 VAL A 25 2889 4926 3752 36 220 60 C
ATOM 231 CG2 VAL A 25 27.714 11.794 66.500 1.00 30.97 C
ANISOU 231 CG2 VAL A 25 2823 5110 3836 329 267 190 C
ATOM 232 N ILE A 26 25.861 13.648 70.164 1.00 23.81 N
ANISOU 232 N ILE A 26 2505 3474 3068 -406 -522 -655 N
ATOM 233 CA ILE A 26 24.834 14.469 70.801 1.00 21.20 C
ANISOU 233 CA ILE A 26 2222 3124 2711 -437 -488 -653 C
ATOM 234 C ILE A 26 25.320 15.147 72.075 1.00 24.75 C
ANISOU 234 C ILE A 26 2814 3511 3079 -562 -520 -641 C
ATOM 235 O ILE A 26 26.400 14.846 72.582 1.00 29.54 O
ANISOU 235 O ILE A 26 3467 4093 3664 -614 -578 -631 O
ATOM 236 CB ILE A 26 23.571 13.647 71.160 1.00 23.36 C
ANISOU 236 CB ILE A 26 2439 3389 3049 -382 -483 -642 C
ATOM 237 CG1 ILE A 26 23.927 12.494 72.100 1.00 27.64 C
ANISOU 237 CG1 ILE A 26 2993 3903 3604 -429 -554 -600 C
ATOM 238 CG2 ILE A 26 22.847 13.150 69.916 1.00 20.71 C
ANISOU 238 CG2 ILE A 26 1999 3078 2791 -239 -442 -683 C
ATOM 239 CD1 ILE A 26 22.784 12.125 73.026 1.00 33.15 C
ANISOU 239 CD1 ILE A 26 3691 4575 4328 -439 -556 -575 C
ATOM 240 N SER A 27 24.504 16.068 72.578 1.00 22.28 N
ANISOU 240 N SER A 27 2579 3165 2723 -593 -468 -660 N
ATOM 241 CA SER A 27 24.761 16.770 73.826 1.00 22.57 C
ANISOU 241 CA SER A 27 2772 3135 2666 -689 -449 -683 C
ATOM 242 C SER A 27 23.586 16.509 74.765 1.00 24.45 C
ANISOU 242 C SER A 27 3049 3325 2917 -695 -432 -683 C
ATOM 243 O SER A 27 22.509 16.120 74.303 1.00 23.83 O
ANISOU 243 O SER A 27 2877 3264 2911 -631 -428 -666 O
ATOM 244 CB SER A 27 24.950 18.271 73.563 1.00 24.49 C
ANISOU 244 CB SER A 27 3123 3370 2811 -735 -354 -716 C
ATOM 245 OG SER A 27 26.057 18.480 72.693 1.00 28.43 O
ANISOU 245 OG SER A 27 3578 3915 3308 -730 -375 -714 O
ATOM 246 N PRO A 28 23.777 16.707 76.082 1.00 25.73 N
ANISOU 246 N PRO A 28 3342 3435 3000 -779 -400 -695 N
ATOM 247 CA PRO A 28 22.683 16.470 77.021 1.00 25.53 C
ANISOU 247 CA PRO A 28 3369 3351 2979 -788 -368 -699 C
ATOM 248 C PRO A 28 21.400 17.227 76.670 1.00 25.02 C
ANISOU 248 C PRO A 28 3354 3246 2907 -749 -274 -725 C
ATOM 249 O PRO A 28 20.320 16.760 77.023 1.00 24.05 O
ANISOU 249 O PRO A 28 3208 3114 2817 -765 -236 -743 O
ATOM 250 CB PRO A 28 23.259 16.971 78.352 1.00 27.91 C
ANISOU 250 CB PRO A 28 3862 3602 3141 -911 -293 -693 C
ATOM 251 CG PRO A 28 24.701 16.772 78.204 1.00 28.08 C
ANISOU 251 CG PRO A 28 3852 3675 3143 -949 -353 -676 C
ATOM 252 CD PRO A 28 25.021 17.068 76.780 1.00 28.38 C
ANISOU 252 CD PRO A 28 3786 3766 3232 -880 -380 -690 C
ATOM 253 N ASP A 29 21.518 18.351 75.963 1.00 27.41 N
ANISOU 253 N ASP A 29 3722 3552 3142 -746 -191 -749 N
ATOM 254 CA ASP A 29 20.351 19.160 75.595 1.00 26.59 C
ANISOU 254 CA ASP A 29 3698 3445 2958 -793 14 -824 C
ATOM 255 C ASP A 29 19.883 19.001 74.140 1.00 25.12 C
ANISOU 255 C ASP A 29 3290 3369 2886 -693 -19 -860 C
ATOM 256 O ASP A 29 19.016 19.744 73.693 1.00 23.82 O
ANISOU 256 O ASP A 29 3171 3201 2677 -676 169 -945 O
ATOM 257 CB ASP A 29 20.636 20.637 75.860 1.00 30.18 C
ANISOU 257 CB ASP A 29 4411 3811 3246 -858 193 -815 C
ATOM 258 CG ASP A 29 21.867 21.136 75.121 1.00 34.27 C
ANISOU 258 CG ASP A 29 4862 4379 3780 -822 88 -789 C
ATOM 259 OD1 ASP A 29 22.645 20.297 74.637 1.00 33.53 O
ANISOU 259 OD1 ASP A 29 4587 4358 3794 -772 -86 -769 O
ATOM 260 OD2 ASP A 29 22.068 22.366 75.031 1.00 43.80 O
ANISOU 260 OD2 ASP A 29 6222 5534 4886 -861 215 -780 O
ATOM 261 N THR A 30 20.455 18.057 73.397 1.00 25.17 N
ANISOU 261 N THR A 30 3104 3429 3030 -591 -212 -763 N
ATOM 262 CA THR A 30 19.926 17.722 72.070 1.00 18.29 C
ANISOU 262 CA THR A 30 2015 2662 2274 -475 -219 -753 C
ATOM 263 C THR A 30 18.479 17.252 72.148 1.00 19.75 C
ANISOU 263 C THR A 30 2021 2917 2567 -418 -157 -836 C
ATOM 264 O THR A 30 18.171 16.339 72.914 1.00 20.19 O
ANISOU 264 O THR A 30 2053 2941 2676 -425 -210 -783 O
ATOM 265 CB THR A 30 20.726 16.610 71.398 1.00 16.65 C
ANISOU 265 CB THR A 30 1677 2509 2138 -400 -303 -696 C
ATOM 266 OG1 THR A 30 22.064 17.050 71.164 1.00 16.39 O
ANISOU 266 OG1 THR A 30 1709 2480 2040 -452 -321 -704 O
ATOM 267 CG2 THR A 30 20.076 16.218 70.053 1.00 14.79 C
ANISOU 267 CG2 THR A 30 1287 2336 1996 -243 -272 -716 C
ATOM 268 N ARG A 31 17.593 17.855 71.366 1.00 16.23 N
ANISOU 268 N ARG A 31 1430 2553 2184 -347 -54 -954 N
ATOM 269 CA ARG A 31 16.203 17.421 71.347 1.00 17.03 C
ANISOU 269 CA ARG A 31 1352 2668 2451 -192 30 -894 C
ATOM 270 C ARG A 31 15.814 16.879 69.984 1.00 16.82 C
ANISOU 270 C ARG A 31 1265 2638 2489 -23 -60 -748 C
ATOM 271 O ARG A 31 16.109 17.485 68.964 1.00 18.12 O
ANISOU 271 O ARG A 31 1459 2819 2607 8 -55 -756 O
ATOM 272 CB ARG A 31 15.259 18.557 71.704 1.00 24.71 C
ANISOU 272 CB ARG A 31 2571 3491 3326 -85 354 -790 C
ATOM 273 CG ARG A 31 15.600 19.293 72.971 1.00 37.45 C
ANISOU 273 CG ARG A 31 4570 4935 4726 -223 504 -781 C
ATOM 274 CD ARG A 31 14.468 20.242 73.320 1.00 48.32 C
ANISOU 274 CD ARG A 31 6150 6167 6041 -88 826 -661 C
ATOM 275 NE ARG A 31 13.231 19.508 73.578 1.00 55.62 N
ANISOU 275 NE ARG A 31 6920 7082 7132 59 881 -551 N
ATOM 276 CZ ARG A 31 12.860 19.084 74.781 1.00 59.70 C
ANISOU 276 CZ ARG A 31 7553 7496 7635 21 933 -492 C
ATOM 277 NH1 ARG A 31 13.627 19.327 75.837 1.00 61.29 N
ANISOU 277 NH1 ARG A 31 8029 7596 7662 -161 936 -534 N
ATOM 278 NH2 ARG A 31 11.724 18.416 74.932 1.00 62.14 N
ANISOU 278 NH2 ARG A 31 7703 7802 8105 163 980 -391 N
ATOM 279 N MET A 32 15.114 15.757 69.978 1.00 13.30 N
ANISOU 279 N MET A 32 818 2134 2102 34 -112 -576 N
ATOM 280 CA MET A 32 14.694 15.122 68.734 1.00 16.35 C
ANISOU 280 CA MET A 32 1195 2507 2509 107 -158 -547 C
ATOM 281 C MET A 32 13.215 14.791 68.796 1.00 20.01 C
ANISOU 281 C MET A 32 1586 2959 3056 191 -98 -423 C
ATOM 282 O MET A 32 12.702 14.379 69.847 1.00 24.07 O
ANISOU 282 O MET A 32 2072 3461 3612 197 -64 -359 O
ATOM 283 CB MET A 32 15.509 13.856 68.464 1.00 12.21 C
ANISOU 283 CB MET A 32 705 1962 1973 87 -256 -617 C
ATOM 284 CG MET A 32 15.054 13.085 67.233 1.00 13.57 C
ANISOU 284 CG MET A 32 854 2119 2181 144 -287 -628 C
ATOM 285 SD MET A 32 16.165 11.722 66.877 1.00 22.77 S
ANISOU 285 SD MET A 32 2050 3254 3347 140 -353 -704 S
ATOM 286 CE MET A 32 15.484 10.499 68.010 1.00 16.87 C
ANISOU 286 CE MET A 32 1268 2473 2669 125 -383 -640 C
ATOM 287 N GLU A 33 12.531 15.031 67.686 1.00 15.13 N
ANISOU 287 N GLU A 33 943 2351 2456 260 -70 -382 N
ATOM 288 CA GLU A 33 11.136 14.692 67.520 1.00 20.71 C
ANISOU 288 CA GLU A 33 1587 3057 3225 347 -10 -258 C
ATOM 289 C GLU A 33 11.019 13.732 66.357 1.00 22.71 C
ANISOU 289 C GLU A 33 1823 3312 3493 336 -110 -304 C
ATOM 290 O GLU A 33 11.564 13.984 65.281 1.00 23.99 O
ANISOU 290 O GLU A 33 2013 3484 3617 322 -151 -379 O
ATOM 291 CB GLU A 33 10.290 15.951 67.271 1.00 31.40 C
ANISOU 291 CB GLU A 33 2939 4420 4573 465 163 -142 C
ATOM 292 CG GLU A 33 8.784 15.710 67.109 1.00 43.98 C
ANISOU 292 CG GLU A 33 4503 6047 6159 576 230 -31 C
ATOM 293 CD GLU A 33 8.347 15.391 65.671 1.00 54.38 C
ANISOU 293 CD GLU A 33 5770 7374 7517 583 174 -15 C
ATOM 294 OE1 GLU A 33 8.949 15.922 64.716 1.00 58.29 O
ANISOU 294 OE1 GLU A 33 6268 7856 8023 558 149 -62 O
ATOM 295 OE2 GLU A 33 7.391 14.604 65.498 1.00 58.48 O
ANISOU 295 OE2 GLU A 33 6252 7933 8035 619 150 14 O
ATOM 296 N ASP A 34 10.309 12.633 66.571 1.00 21.93 N
ANISOU 296 N ASP A 34 1683 3205 3443 347 -136 -264 N
ATOM 297 CA ASP A 34 10.007 11.689 65.501 1.00 20.10 C
ANISOU 297 CA ASP A 34 1430 2969 3236 351 -200 -294 C
ATOM 298 C ASP A 34 8.511 11.383 65.495 1.00 23.83 C
ANISOU 298 C ASP A 34 1828 3470 3758 424 -143 -171 C
ATOM 299 O ASP A 34 8.025 10.649 66.357 1.00 21.24 O
ANISOU 299 O ASP A 34 1476 3136 3458 428 -142 -139 O
ATOM 300 CB ASP A 34 10.817 10.411 65.664 1.00 21.69 C
ANISOU 300 CB ASP A 34 1670 3129 3443 293 -294 -396 C
ATOM 301 CG ASP A 34 10.425 9.331 64.665 1.00 25.90 C
ANISOU 301 CG ASP A 34 2178 3649 4014 308 -341 -420 C
ATOM 302 OD1 ASP A 34 9.767 9.634 63.657 1.00 31.43 O
ANISOU 302 OD1 ASP A 34 2843 4377 4721 346 -321 -386 O
ATOM 303 OD2 ASP A 34 10.790 8.167 64.884 1.00 25.92 O
ANISOU 303 OD2 ASP A 34 2195 3611 4041 284 -394 -470 O
ATOM 304 N ASN A 35 7.796 11.950 64.523 1.00 27.15 N
ANISOU 304 N ASN A 35 2214 3925 4176 488 -92 -111 N
ATOM 305 CA ASN A 35 6.346 11.777 64.428 1.00 31.81 C
ANISOU 305 CA ASN A 35 2741 4573 4774 582 -29 -11 C
ATOM 306 C ASN A 35 5.617 11.906 65.766 1.00 37.94 C
ANISOU 306 C ASN A 35 3526 5374 5516 639 36 2 C
ATOM 307 O ASN A 35 4.861 11.020 66.147 1.00 40.94 O
ANISOU 307 O ASN A 35 3863 5750 5941 654 15 -3 O
ATOM 308 CB ASN A 35 6.018 10.418 63.824 1.00 34.01 C
ANISOU 308 CB ASN A 35 2985 4833 5104 551 -113 -46 C
ATOM 309 CG ASN A 35 6.036 10.434 62.315 1.00 33.21 C
ANISOU 309 CG ASN A 35 2873 4736 5011 552 -145 -71 C
ATOM 310 OD1 ASN A 35 6.506 11.389 61.684 1.00 34.20 O
ANISOU 310 OD1 ASN A 35 3024 4863 5108 554 -126 -84 O
ATOM 311 ND2 ASN A 35 5.514 9.376 61.721 1.00 34.99 N
ANISOU 311 ND2 ASN A 35 3061 4958 5275 551 -193 -86 N
ATOM 312 N GLY A 36 5.869 12.982 66.497 1.00 37.99 N
ANISOU 312 N GLY A 36 3590 5379 5466 664 106 -20 N
ATOM 313 CA GLY A 36 5.194 13.191 67.767 1.00 39.42 C
ANISOU 313 CA GLY A 36 3774 5511 5693 703 167 -69 C
ATOM 314 C GLY A 36 5.970 12.779 69.006 1.00 39.22 C
ANISOU 314 C GLY A 36 3769 5472 5662 650 157 -54 C
ATOM 315 O GLY A 36 5.876 13.441 70.042 1.00 39.10 O
ANISOU 315 O GLY A 36 3799 5396 5661 668 247 -77 O
ATOM 316 N ARG A 37 6.728 11.686 68.914 1.00 34.03 N
ANISOU 316 N ARG A 37 4305 4686 3939 -506 639 -845 N
ATOM 317 CA ARG A 37 7.530 11.223 70.040 1.00 32.70 C
ANISOU 317 CA ARG A 37 4188 4571 3664 -603 650 -786 C
ATOM 318 C ARG A 37 8.693 12.188 70.248 1.00 30.78 C
ANISOU 318 C ARG A 37 3893 4325 3476 -539 635 -741 C
ATOM 319 O ARG A 37 9.374 12.559 69.286 1.00 27.00 O
ANISOU 319 O ARG A 37 3415 3771 3073 -402 614 -678 O
ATOM 320 CB ARG A 37 8.061 9.807 69.806 1.00 43.09 C
ANISOU 320 CB ARG A 37 5640 5828 4902 -591 619 -644 C
ATOM 321 CG ARG A 37 7.086 8.845 69.148 1.00 58.66 C
ANISOU 321 CG ARG A 37 7672 7769 6848 -601 628 -663 C
ATOM 322 CD ARG A 37 7.817 7.817 68.267 1.00 70.06 C
ANISOU 322 CD ARG A 37 9220 9114 8285 -498 586 -519 C
ATOM 323 NE ARG A 37 8.657 6.900 69.040 1.00 79.82 N
ANISOU 323 NE ARG A 37 10555 10343 9430 -554 548 -405 N
ATOM 324 CZ ARG A 37 9.527 6.040 68.510 1.00 80.99 C
ANISOU 324 CZ ARG A 37 10787 10411 9573 -471 497 -280 C
ATOM 325 NH1 ARG A 37 9.694 5.968 67.195 1.00 79.05 N
ANISOU 325 NH1 ARG A 37 10537 10093 9404 -333 487 -251 N
ATOM 326 NH2 ARG A 37 10.239 5.249 69.302 1.00 82.77 N
ANISOU 326 NH2 ARG A 37 11101 10628 9718 -526 450 -190 N
ATOM 327 N GLU A 38 8.927 12.600 71.490 1.00 30.67 N
ANISOU 327 N GLU A 38 3834 4397 3421 -642 650 -777 N
ATOM 328 CA GLU A 38 10.037 13.505 71.773 1.00 31.44 C
ANISOU 328 CA GLU A 38 3878 4500 3568 -589 641 -742 C
ATOM 329 C GLU A 38 11.140 12.773 72.507 1.00 27.65 C
ANISOU 329 C GLU A 38 3478 4028 2999 -622 613 -622 C
ATOM 330 O GLU A 38 10.860 11.923 73.362 1.00 28.78 O
ANISOU 330 O GLU A 38 3686 4218 3031 -746 611 -609 O
ATOM 331 CB GLU A 38 9.561 14.700 72.586 1.00 40.14 C
ANISOU 331 CB GLU A 38 4849 5685 4717 -661 665 -877 C
ATOM 332 CG GLU A 38 8.422 15.451 71.937 1.00 50.85 C
ANISOU 332 CG GLU A 38 6124 7007 6190 -622 643 -977 C
ATOM 333 CD GLU A 38 7.724 16.391 72.902 1.00 61.25 C
ANISOU 333 CD GLU A 38 7317 8393 7560 -718 629 -1093 C
ATOM 334 OE1 GLU A 38 7.429 15.975 74.042 1.00 59.14 O
ANISOU 334 OE1 GLU A 38 7044 8208 7220 -861 641 -1121 O
ATOM 335 OE2 GLU A 38 7.478 17.553 72.523 1.00 73.42 O
ANISOU 335 OE2 GLU A 38 8772 9907 9217 -657 601 -1155 O
ATOM 336 N PHE A 39 12.386 13.091 72.157 1.00 21.16 N
ANISOU 336 N PHE A 39 2658 3159 2224 -513 588 -537 N
ATOM 337 CA PHE A 39 13.571 12.523 72.816 1.00 19.34 C
ANISOU 337 CA PHE A 39 2491 2932 1928 -521 551 -433 C
ATOM 338 C PHE A 39 14.571 13.629 73.143 1.00 21.28 C
ANISOU 338 C PHE A 39 2650 3203 2232 -475 558 -442 C
ATOM 339 O PHE A 39 14.807 14.512 72.329 1.00 23.35 O
ANISOU 339 O PHE A 39 2851 3426 2596 -377 574 -463 O
ATOM 340 CB PHE A 39 14.270 11.474 71.932 1.00 17.78 C
ANISOU 340 CB PHE A 39 2398 2636 1722 -419 501 -311 C
ATOM 341 CG PHE A 39 13.339 10.467 71.322 1.00 19.31 C
ANISOU 341 CG PHE A 39 2669 2787 1883 -433 496 -301 C
ATOM 342 CD1 PHE A 39 12.589 10.784 70.203 1.00 17.06 C
ANISOU 342 CD1 PHE A 39 2349 2461 1670 -366 522 -350 C
ATOM 343 CD2 PHE A 39 13.209 9.209 71.869 1.00 22.51 C
ANISOU 343 CD2 PHE A 39 3183 3188 2182 -515 462 -243 C
ATOM 344 CE1 PHE A 39 11.737 9.861 69.650 1.00 21.08 C
ANISOU 344 CE1 PHE A 39 2923 2935 2151 -378 521 -347 C
ATOM 345 CE2 PHE A 39 12.346 8.281 71.315 1.00 26.81 C
ANISOU 345 CE2 PHE A 39 3796 3693 2696 -532 462 -237 C
ATOM 346 CZ PHE A 39 11.618 8.610 70.201 1.00 25.15 C
ANISOU 346 CZ PHE A 39 3542 3451 2563 -461 495 -293 C
ATOM 347 N ATHR A 40 15.152 13.567 74.340 0.45 22.25 N
ANISOU 347 N ATHR A 40 2774 3392 2288 -552 546 -427 N
ATOM 348 N BTHR A 40 15.141 13.583 74.344 0.55 22.32 N
ANISOU 348 N BTHR A 40 2781 3401 2297 -553 547 -428 N
ATOM 349 CA ATHR A 40 16.186 14.512 74.768 0.45 21.08 C
ANISOU 349 CA ATHR A 40 2548 3275 2185 -515 552 -434 C
ATOM 350 CA BTHR A 40 16.207 14.503 74.728 0.55 20.96 C
ANISOU 350 CA BTHR A 40 2535 3257 2173 -510 551 -431 C
ATOM 351 C ATHR A 40 17.412 13.767 75.307 0.45 20.61 C
ANISOU 351 C ATHR A 40 2564 3207 2060 -500 495 -333 C
ATOM 352 C BTHR A 40 17.418 13.737 75.257 0.55 20.75 C
ANISOU 352 C BTHR A 40 2585 3221 2078 -496 494 -330 C
ATOM 353 O ATHR A 40 17.271 12.751 75.992 0.45 20.37 O
ANISOU 353 O ATHR A 40 2626 3192 1922 -585 457 -286 O
ATOM 354 O BTHR A 40 17.275 12.687 75.890 0.55 20.75 O
ANISOU 354 O BTHR A 40 2680 3231 1972 -576 454 -280 O
ATOM 355 CB ATHR A 40 15.658 15.474 75.860 0.45 20.95 C
ANISOU 355 CB ATHR A 40 2422 3370 2167 -629 597 -550 C
ATOM 356 CB BTHR A 40 15.747 15.493 75.808 0.55 21.14 C
ANISOU 356 CB BTHR A 40 2447 3390 2197 -618 596 -545 C
ATOM 357 OG1ATHR A 40 14.502 16.169 75.371 0.45 23.67 O
ANISOU 357 OG1ATHR A 40 2691 3719 2584 -637 637 -660 O
ATOM 358 OG1BTHR A 40 15.394 14.768 76.987 0.55 17.78 O
ANISOU 358 OG1BTHR A 40 2071 3038 1645 -765 585 -545 O
ATOM 359 CG2ATHR A 40 16.729 16.486 76.255 0.45 18.64 C
ANISOU 359 CG2ATHR A 40 2044 3109 1931 -584 607 -561 C
ATOM 360 CG2BTHR A 40 14.542 16.269 75.330 0.55 23.47 C
ANISOU 360 CG2BTHR A 40 2658 3692 2568 -629 639 -662 C
ATOM 361 N GLY A 41 18.607 14.262 74.992 1.00 19.47 N
ANISOU 361 N GLY A 41 2384 3036 1978 -395 486 -304 N
ATOM 362 CA GLY A 41 19.828 13.667 75.507 1.00 22.46 C
ANISOU 362 CA GLY A 41 2816 3408 2308 -369 427 -229 C
ATOM 363 C GLY A 41 19.981 12.179 75.234 1.00 20.22 C
ANISOU 363 C GLY A 41 2670 3054 1959 -349 352 -132 C
ATOM 364 O GLY A 41 19.846 11.725 74.084 1.00 20.21 O
ANISOU 364 O GLY A 41 2708 2974 1999 -268 345 -100 O
ATOM 365 N ASP A 42 20.249 11.415 76.286 1.00 19.66 N
ANISOU 365 N ASP A 42 2675 3010 1786 -425 293 -87 N
ATOM 366 CA ASP A 42 20.521 9.981 76.157 1.00 25.86 C
ANISOU 366 CA ASP A 42 3598 3720 2508 -406 204 9 C
ATOM 367 C ASP A 42 19.346 9.184 75.593 1.00 20.74 C
ANISOU 367 C ASP A 42 3024 3027 1828 -449 212 24 C
ATOM 368 O ASP A 42 19.535 8.068 75.133 1.00 22.23 O
ANISOU 368 O ASP A 42 3315 3136 1996 -405 146 97 O
ATOM 369 CB ASP A 42 20.935 9.387 77.510 1.00 35.16 C
ANISOU 369 CB ASP A 42 4852 4934 3571 -498 131 53 C
ATOM 370 CG ASP A 42 22.410 9.614 77.822 1.00 46.05 C
ANISOU 370 CG ASP A 42 6204 6313 4981 -409 76 71 C
ATOM 371 OD1 ASP A 42 23.233 9.650 76.877 1.00 50.63 O
ANISOU 371 OD1 ASP A 42 6757 6831 5650 -268 62 80 O
ATOM 372 OD2 ASP A 42 22.750 9.754 79.015 1.00 50.51 O
ANISOU 372 OD2 ASP A 42 6771 6943 5477 -484 49 69 O
ATOM 373 N GLU A 43 18.136 9.735 75.635 1.00 21.18 N
ANISOU 373 N GLU A 43 3027 3137 1885 -533 289 -54 N
ATOM 374 CA GLU A 43 17.012 9.105 74.937 1.00 21.68 C
ANISOU 374 CA GLU A 43 3142 3160 1937 -557 307 -58 C
ATOM 375 C GLU A 43 17.272 8.974 73.437 1.00 18.33 C
ANISOU 375 C GLU A 43 2715 2643 1608 -404 304 -30 C
ATOM 376 O GLU A 43 16.802 8.045 72.793 1.00 15.62 O
ANISOU 376 O GLU A 43 2448 2238 1249 -389 284 7 O
ATOM 377 CB GLU A 43 15.729 9.889 75.164 1.00 20.99 C
ANISOU 377 CB GLU A 43 2970 3149 1854 -656 391 -173 C
ATOM 378 CG GLU A 43 15.345 10.023 76.628 1.00 26.43 C
ANISOU 378 CG GLU A 43 3653 3945 2443 -827 405 -219 C
ATOM 379 CD GLU A 43 14.005 10.696 76.792 1.00 29.35 C
ANISOU 379 CD GLU A 43 3936 4392 2823 -927 485 -352 C
ATOM 380 OE1 GLU A 43 13.812 11.785 76.207 1.00 26.16 O
ANISOU 380 OE1 GLU A 43 3414 3994 2533 -855 531 -431 O
ATOM 381 OE2 GLU A 43 13.136 10.124 77.485 1.00 30.05 O
ANISOU 381 OE2 GLU A 43 4075 4533 2808 -1081 498 -382 O
ATOM 382 N VAL A 44 18.012 9.917 72.876 1.00 19.94 N
ANISOU 382 N VAL A 44 2830 2839 1909 -299 327 -52 N
ATOM 383 CA VAL A 44 18.376 9.832 71.466 1.00 16.05 C
ANISOU 383 CA VAL A 44 2335 2265 1499 -163 325 -25 C
ATOM 384 C VAL A 44 19.264 8.610 71.249 1.00 16.88 C
ANISOU 384 C VAL A 44 2535 2301 1578 -100 241 64 C
ATOM 385 O VAL A 44 19.141 7.904 70.238 1.00 20.04 O
ANISOU 385 O VAL A 44 2981 2631 2002 -34 223 97 O
ATOM 386 CB VAL A 44 19.082 11.103 70.984 1.00 16.20 C
ANISOU 386 CB VAL A 44 2249 2292 1614 -80 367 -65 C
ATOM 387 CG1 VAL A 44 19.510 10.959 69.509 1.00 16.09 C
ANISOU 387 CG1 VAL A 44 2244 2198 1672 46 365 -35 C
ATOM 388 CG2 VAL A 44 18.137 12.295 71.129 1.00 16.91 C
ANISOU 388 CG2 VAL A 44 2247 2436 1742 -134 437 -158 C
ATOM 389 N VAL A 45 20.144 8.337 72.204 1.00 19.82 N
ANISOU 389 N VAL A 45 2936 2691 1903 -120 182 98 N
ATOM 390 CA VAL A 45 20.980 7.138 72.128 1.00 22.19 C
ANISOU 390 CA VAL A 45 3329 2922 2179 -63 82 175 C
ATOM 391 C VAL A 45 20.105 5.892 72.234 1.00 19.69 C
ANISOU 391 C VAL A 45 3133 2563 1783 -134 40 224 C
ATOM 392 O VAL A 45 20.301 4.917 71.505 1.00 18.82 O
ANISOU 392 O VAL A 45 3088 2372 1689 -66 -15 272 O
ATOM 393 CB VAL A 45 22.066 7.118 73.238 1.00 26.97 C
ANISOU 393 CB VAL A 45 3946 3556 2746 -73 14 195 C
ATOM 394 CG1 VAL A 45 22.869 5.812 73.188 1.00 26.00 C
ANISOU 394 CG1 VAL A 45 3926 3351 2601 -12 -109 267 C
ATOM 395 CG2 VAL A 45 22.979 8.333 73.097 1.00 26.83 C
ANISOU 395 CG2 VAL A 45 3806 3580 2809 -1 60 139 C
ATOM 396 N GLU A 46 19.126 5.939 73.133 1.00 21.52 N
ANISOU 396 N GLU A 46 3390 2854 1932 -278 70 204 N
ATOM 397 CA GLU A 46 18.190 4.839 73.298 1.00 19.14 C
ANISOU 397 CA GLU A 46 3202 2523 1546 -370 46 240 C
ATOM 398 C GLU A 46 17.420 4.600 71.996 1.00 20.11 C
ANISOU 398 C GLU A 46 3316 2596 1727 -312 90 222 C
ATOM 399 O GLU A 46 17.186 3.453 71.614 1.00 24.38 O
ANISOU 399 O GLU A 46 3954 3068 2241 -306 42 274 O
ATOM 400 CB GLU A 46 17.232 5.112 74.460 1.00 26.06 C
ANISOU 400 CB GLU A 46 4086 3491 2324 -549 91 196 C
ATOM 401 CG GLU A 46 17.890 4.953 75.844 1.00 34.18 C
ANISOU 401 CG GLU A 46 5169 4558 3259 -632 26 235 C
ATOM 402 CD GLU A 46 16.975 5.316 77.012 1.00 41.14 C
ANISOU 402 CD GLU A 46 6045 5547 4040 -822 81 179 C
ATOM 403 OE1 GLU A 46 15.781 5.615 76.787 1.00 44.23 O
ANISOU 403 OE1 GLU A 46 6392 5981 4432 -894 165 102 O
ATOM 404 OE2 GLU A 46 17.464 5.305 78.165 1.00 41.25 O
ANISOU 404 OE2 GLU A 46 6093 5605 3973 -901 37 204 O
ATOM 405 N TYR A 47 17.028 5.681 71.320 1.00 16.64 N
ANISOU 405 N TYR A 47 2766 2190 1368 -270 175 148 N
ATOM 406 CA TYR A 47 16.414 5.594 69.984 1.00 15.06 C
ANISOU 406 CA TYR A 47 2547 1942 1233 -196 213 129 C
ATOM 407 C TYR A 47 17.271 4.767 69.027 1.00 15.15 C
ANISOU 407 C TYR A 47 2604 1864 1290 -69 151 196 C
ATOM 408 O TYR A 47 16.744 3.928 68.260 1.00 18.15 O
ANISOU 408 O TYR A 47 3035 2189 1672 -45 141 216 O
ATOM 409 CB TYR A 47 16.177 7.008 69.414 1.00 14.35 C
ANISOU 409 CB TYR A 47 2332 1889 1230 -150 292 49 C
ATOM 410 CG TYR A 47 15.432 7.098 68.083 1.00 20.78 C
ANISOU 410 CG TYR A 47 3124 2663 2108 -83 332 18 C
ATOM 411 CD1 TYR A 47 14.045 7.137 68.040 1.00 19.27 C
ANISOU 411 CD1 TYR A 47 2926 2497 1899 -154 377 -48 C
ATOM 412 CD2 TYR A 47 16.119 7.185 66.879 1.00 21.38 C
ANISOU 412 CD2 TYR A 47 3182 2682 2261 47 325 45 C
ATOM 413 CE1 TYR A 47 13.366 7.243 66.851 1.00 16.55 C
ANISOU 413 CE1 TYR A 47 2560 2116 1612 -89 407 -80 C
ATOM 414 CE2 TYR A 47 15.444 7.296 65.669 1.00 18.48 C
ANISOU 414 CE2 TYR A 47 2798 2280 1945 105 358 20 C
ATOM 415 CZ TYR A 47 14.071 7.310 65.664 1.00 18.88 C
ANISOU 415 CZ TYR A 47 2846 2351 1977 41 394 -39 C
ATOM 416 OH TYR A 47 13.387 7.407 64.479 1.00 19.92 O
ANISOU 416 OH TYR A 47 2963 2447 2158 102 419 -68 O
ATOM 417 N VAL A 48 18.585 4.982 69.050 1.00 17.76 N
ANISOU 417 N VAL A 48 2908 2182 1659 12 109 220 N
ATOM 418 CA VAL A 48 19.465 4.246 68.135 1.00 18.69 C
ANISOU 418 CA VAL A 48 3050 2223 1828 132 49 262 C
ATOM 419 C VAL A 48 19.569 2.782 68.557 1.00 19.95 C
ANISOU 419 C VAL A 48 3334 2322 1925 107 -51 332 C
ATOM 420 O VAL A 48 19.568 1.880 67.714 1.00 19.18 O
ANISOU 420 O VAL A 48 3279 2155 1854 170 -88 360 O
ATOM 421 CB VAL A 48 20.872 4.874 68.044 1.00 21.27 C
ANISOU 421 CB VAL A 48 3308 2559 2216 222 33 250 C
ATOM 422 CG1 VAL A 48 21.788 4.009 67.179 1.00 14.86 C
ANISOU 422 CG1 VAL A 48 2519 1675 1454 336 -36 278 C
ATOM 423 CG2 VAL A 48 20.775 6.267 67.428 1.00 21.93 C
ANISOU 423 CG2 VAL A 48 3281 2684 2367 253 129 189 C
ATOM 424 N LYS A 49 19.592 2.533 69.856 1.00 18.84 N
ANISOU 424 N LYS A 49 3255 2205 1697 9 -97 360 N
ATOM 425 CA LYS A 49 19.602 1.154 70.325 1.00 23.29 C
ANISOU 425 CA LYS A 49 3956 2703 2191 -31 -201 432 C
ATOM 426 C LYS A 49 18.408 0.378 69.783 1.00 25.88 C
ANISOU 426 C LYS A 49 4347 2995 2493 -78 -174 441 C
ATOM 427 O LYS A 49 18.527 -0.796 69.411 1.00 28.72 O
ANISOU 427 O LYS A 49 4792 3269 2850 -42 -251 493 O
ATOM 428 CB LYS A 49 19.590 1.093 71.844 1.00 23.35 C
ANISOU 428 CB LYS A 49 4030 2752 2089 -160 -242 459 C
ATOM 429 CG LYS A 49 20.795 1.700 72.507 1.00 26.35 C
ANISOU 429 CG LYS A 49 4363 3165 2485 -119 -284 454 C
ATOM 430 CD LYS A 49 20.767 1.415 74.007 1.00 30.29 C
ANISOU 430 CD LYS A 49 4954 3694 2861 -251 -343 494 C
ATOM 431 CE LYS A 49 21.811 2.210 74.747 1.00 32.71 C
ANISOU 431 CE LYS A 49 5194 4055 3178 -225 -364 473 C
ATOM 432 NZ LYS A 49 21.711 1.949 76.197 1.00 32.04 N
ANISOU 432 NZ LYS A 49 5202 4006 2966 -364 -419 511 N
ATOM 433 N GLU A 50 17.261 1.040 69.728 1.00 24.10 N
ANISOU 433 N GLU A 50 4073 2832 2252 -153 -69 383 N
ATOM 434 CA GLU A 50 16.045 0.407 69.247 1.00 27.75 C
ANISOU 434 CA GLU A 50 4582 3273 2688 -204 -32 372 C
ATOM 435 C GLU A 50 16.076 0.161 67.749 1.00 26.16 C
ANISOU 435 C GLU A 50 4344 3014 2582 -73 -19 366 C
ATOM 436 O GLU A 50 15.514 -0.823 67.273 1.00 27.37 O
ANISOU 436 O GLU A 50 4564 3113 2721 -78 -36 388 O
ATOM 437 CB GLU A 50 14.835 1.249 69.624 1.00 34.41 C
ANISOU 437 CB GLU A 50 5369 4206 3498 -318 72 289 C
ATOM 438 CG GLU A 50 14.621 1.251 71.127 1.00 45.07 C
ANISOU 438 CG GLU A 50 6773 5617 4734 -478 61 293 C
ATOM 439 CD GLU A 50 14.773 -0.148 71.709 1.00 52.18 C
ANISOU 439 CD GLU A 50 7834 6451 5541 -545 -37 384 C
ATOM 440 OE1 GLU A 50 13.938 -1.013 71.371 1.00 55.12 O
ANISOU 440 OE1 GLU A 50 8280 6785 5879 -592 -30 393 O
ATOM 441 OE2 GLU A 50 15.732 -0.390 72.481 1.00 54.11 O
ANISOU 441 OE2 GLU A 50 8135 6678 5748 -548 -125 447 O
ATOM 442 N ILE A 51 16.741 1.045 67.012 1.00 28.39 N
ANISOU 442 N ILE A 51 4522 3309 2955 39 11 335 N
ATOM 443 CA ILE A 51 16.922 0.850 65.574 1.00 28.25 C
ANISOU 443 CA ILE A 51 4468 3242 3022 162 21 330 C
ATOM 444 C ILE A 51 17.732 -0.411 65.332 1.00 28.86 C
ANISOU 444 C ILE A 51 4618 3237 3112 228 -84 391 C
ATOM 445 O ILE A 51 17.375 -1.244 64.501 1.00 25.85 O
ANISOU 445 O ILE A 51 4268 2802 2751 267 -96 403 O
ATOM 446 CB ILE A 51 17.615 2.065 64.915 1.00 24.32 C
ANISOU 446 CB ILE A 51 3857 2776 2609 253 69 289 C
ATOM 447 CG1 ILE A 51 16.607 3.200 64.731 1.00 24.75 C
ANISOU 447 CG1 ILE A 51 3841 2887 2675 213 167 222 C
ATOM 448 CG2 ILE A 51 18.214 1.691 63.560 1.00 21.56 C
ANISOU 448 CG2 ILE A 51 3484 2373 2336 378 53 296 C
ATOM 449 CD1 ILE A 51 17.237 4.527 64.319 1.00 28.75 C
ANISOU 449 CD1 ILE A 51 4248 3425 3250 276 212 184 C
ATOM 450 N GLN A 52 18.819 -0.538 66.081 1.00 31.48 N
ANISOU 450 N GLN A 52 4972 3558 3432 242 -164 423 N
ATOM 451 CA GLN A 52 19.706 -1.684 66.003 1.00 36.70 C
ANISOU 451 CA GLN A 52 5698 4137 4110 309 -284 471 C
ATOM 452 C GLN A 52 18.974 -2.968 66.397 1.00 39.37 C
ANISOU 452 C GLN A 52 6169 4413 4376 231 -345 527 C
ATOM 453 O GLN A 52 19.117 -3.994 65.744 1.00 36.90 O
ANISOU 453 O GLN A 52 5899 4023 4098 292 -407 551 O
ATOM 454 CB GLN A 52 20.917 -1.459 66.906 1.00 37.27 C
ANISOU 454 CB GLN A 52 5767 4217 4175 327 -362 484 C
ATOM 455 CG GLN A 52 21.988 -2.519 66.803 1.00 44.32 C
ANISOU 455 CG GLN A 52 6709 5024 5104 416 -499 515 C
ATOM 456 CD GLN A 52 23.185 -2.188 67.667 1.00 50.65 C
ANISOU 456 CD GLN A 52 7496 5842 5906 442 -573 511 C
ATOM 457 OE1 GLN A 52 23.035 -1.716 68.793 1.00 51.48 O
ANISOU 457 OE1 GLN A 52 7628 5996 5938 349 -566 527 O
ATOM 458 NE2 GLN A 52 24.380 -2.415 67.137 1.00 52.55 N
ANISOU 458 NE2 GLN A 52 7688 6048 6231 566 -642 479 N
ATOM 459 N LYS A 53 18.180 -2.888 67.459 1.00 40.01 N
ANISOU 459 N LYS A 53 6314 4532 4356 88 -322 541 N
ATOM 460 CA LYS A 53 17.363 -4.009 67.906 1.00 39.70 C
ANISOU 460 CA LYS A 53 6408 4445 4231 -17 -363 589 C
ATOM 461 C LYS A 53 16.379 -4.492 66.836 1.00 37.79 C
ANISOU 461 C LYS A 53 6163 4177 4018 -1 -303 566 C
ATOM 462 O LYS A 53 16.312 -5.687 66.557 1.00 32.02 O
ANISOU 462 O LYS A 53 5506 3369 3292 11 -369 603 O
ATOM 463 CB LYS A 53 16.593 -3.637 69.176 1.00 43.61 C
ANISOU 463 CB LYS A 53 6950 5010 4608 -190 -321 586 C
ATOM 464 CG LYS A 53 15.338 -4.480 69.404 1.00 52.28 C
ANISOU 464 CG LYS A 53 8155 6091 5617 -324 -300 599 C
ATOM 465 CD LYS A 53 14.547 -4.043 70.641 1.00 57.76 C
ANISOU 465 CD LYS A 53 8873 6875 6200 -508 -243 571 C
ATOM 466 CE LYS A 53 13.077 -4.473 70.535 1.00 59.43 C
ANISOU 466 CE LYS A 53 9108 7106 6365 -625 -165 522 C
ATOM 467 NZ LYS A 53 12.237 -4.141 71.725 1.00 54.17 N
ANISOU 467 NZ LYS A 53 8447 6531 5605 -811 -108 469 N
ATOM 468 N ARG A 54 15.617 -3.575 66.242 1.00 37.71 N
ANISOU 468 N ARG A 54 6053 4235 4039 0 -182 495 N
ATOM 469 CA ARG A 54 14.558 -3.966 65.320 1.00 38.35 C
ANISOU 469 CA ARG A 54 6131 4302 4137 2 -121 464 C
ATOM 470 C ARG A 54 15.096 -4.299 63.928 1.00 37.74 C
ANISOU 470 C ARG A 54 6003 4172 4165 156 -139 462 C
ATOM 471 O ARG A 54 14.345 -4.733 63.062 1.00 40.74 O
ANISOU 471 O ARG A 54 6379 4532 4567 176 -101 441 O
ATOM 472 CB ARG A 54 13.505 -2.866 65.209 1.00 39.81 C
ANISOU 472 CB ARG A 54 6231 4577 4318 -51 3 379 C
ATOM 473 CG ARG A 54 12.744 -2.614 66.491 1.00 47.07 C
ANISOU 473 CG ARG A 54 7191 5560 5133 -220 36 356 C
ATOM 474 CD ARG A 54 11.673 -1.544 66.300 1.00 53.27 C
ANISOU 474 CD ARG A 54 7878 6431 5932 -261 150 251 C
ATOM 475 NE ARG A 54 12.233 -0.196 66.221 1.00 55.46 N
ANISOU 475 NE ARG A 54 8042 6759 6273 -197 182 215 N
ATOM 476 CZ ARG A 54 12.294 0.523 65.105 1.00 55.79 C
ANISOU 476 CZ ARG A 54 7990 6798 6408 -82 223 176 C
ATOM 477 NH1 ARG A 54 12.821 1.742 65.125 1.00 53.38 N
ANISOU 477 NH1 ARG A 54 7595 6534 6152 -38 248 147 N
ATOM 478 NH2 ARG A 54 11.823 0.023 63.969 1.00 56.38 N
ANISOU 478 NH2 ARG A 54 8066 6831 6524 -15 237 167 N
ATOM 479 N GLY A 55 16.392 -4.089 63.726 1.00 32.51 N
ANISOU 479 N GLY A 55 5296 3492 3565 259 -196 476 N
ATOM 480 CA GLY A 55 17.020 -4.306 62.438 1.00 32.08 C
ANISOU 480 CA GLY A 55 5179 3401 3608 397 -209 461 C
ATOM 481 C GLY A 55 16.594 -3.310 61.369 1.00 27.42 C
ANISOU 481 C GLY A 55 4481 2864 3071 447 -99 400 C
ATOM 482 O GLY A 55 16.717 -3.592 60.189 1.00 26.55 O
ANISOU 482 O GLY A 55 4332 2730 3025 535 -91 383 O
ATOM 483 N GLU A 56 16.097 -2.152 61.800 1.00 22.35 N
ANISOU 483 N GLU A 56 3795 2295 2404 387 -22 364 N
ATOM 484 CA GLU A 56 15.647 -1.091 60.918 1.00 23.29 C
ANISOU 484 CA GLU A 56 3822 2459 2569 425 71 307 C
ATOM 485 C GLU A 56 16.837 -0.530 60.144 1.00 23.27 C
ANISOU 485 C GLU A 56 3743 2457 2641 533 67 298 C
ATOM 486 O GLU A 56 17.874 -0.250 60.724 1.00 22.00 O
ANISOU 486 O GLU A 56 3569 2305 2487 547 27 311 O
ATOM 487 CB GLU A 56 14.955 -0.006 61.743 1.00 26.31 C
ANISOU 487 CB GLU A 56 4176 2911 2910 333 135 267 C
ATOM 488 CG GLU A 56 14.223 1.041 60.941 1.00 31.00 C
ANISOU 488 CG GLU A 56 4692 3542 3546 357 219 202 C
ATOM 489 CD GLU A 56 13.408 1.954 61.834 1.00 34.61 C
ANISOU 489 CD GLU A 56 5123 4064 3966 259 270 148 C
ATOM 490 OE1 GLU A 56 13.982 2.918 62.378 1.00 35.39 O
ANISOU 490 OE1 GLU A 56 5173 4200 4074 251 279 138 O
ATOM 491 OE2 GLU A 56 12.203 1.685 62.015 1.00 33.82 O
ANISOU 491 OE2 GLU A 56 5045 3979 3826 185 302 108 O
ATOM 492 N GLN A 57 16.701 -0.407 58.831 1.00 19.63 N
ANISOU 492 N GLN A 57 3236 1989 2234 606 106 273 N
ATOM 493 CA GLN A 57 17.816 0.015 57.986 1.00 24.79 C
ANISOU 493 CA GLN A 57 3823 2644 2951 697 106 259 C
ATOM 494 C GLN A 57 17.671 1.442 57.459 1.00 20.92 C
ANISOU 494 C GLN A 57 3264 2201 2485 706 187 221 C
ATOM 495 O GLN A 57 16.729 1.724 56.722 1.00 23.43 O
ANISOU 495 O GLN A 57 3572 2522 2808 709 238 199 O
ATOM 496 CB GLN A 57 17.959 -0.943 56.798 1.00 35.38 C
ANISOU 496 CB GLN A 57 5135 3972 4337 736 82 246 C
ATOM 497 CG GLN A 57 18.540 -2.286 57.160 1.00 50.90 C
ANISOU 497 CG GLN A 57 7136 5894 6309 739 -13 270 C
ATOM 498 CD GLN A 57 19.874 -2.146 57.851 1.00 67.22 C
ANISOU 498 CD GLN A 57 9193 7956 8391 766 -74 277 C
ATOM 499 OE1 GLN A 57 19.974 -2.315 59.064 1.00 72.43 O
ANISOU 499 OE1 GLN A 57 9930 8587 9003 741 -127 318 O
ATOM 500 NE2 GLN A 57 20.909 -1.824 57.085 1.00 75.22 N
ANISOU 500 NE2 GLN A 57 10116 9000 9463 810 -69 233 N
ATOM 501 N TRP A 58 18.613 2.321 57.804 1.00 15.50 N
ANISOU 501 N TRP A 58 2532 1543 1814 714 193 212 N
ATOM 502 CA TRP A 58 18.627 3.687 57.284 1.00 15.83 C
ANISOU 502 CA TRP A 58 2515 1618 1882 724 261 180 C
ATOM 503 C TRP A 58 19.700 3.886 56.222 1.00 16.14 C
ANISOU 503 C TRP A 58 2494 1672 1965 764 262 161 C
ATOM 504 O TRP A 58 20.833 3.459 56.399 1.00 18.21 O
ANISOU 504 O TRP A 58 2743 1931 2244 794 219 160 O
ATOM 505 CB TRP A 58 18.872 4.704 58.403 1.00 14.34 C
ANISOU 505 CB TRP A 58 2300 1470 1677 671 276 169 C
ATOM 506 CG TRP A 58 17.808 4.739 59.447 1.00 15.38 C
ANISOU 506 CG TRP A 58 2462 1620 1760 586 282 165 C
ATOM 507 CD1 TRP A 58 17.269 3.677 60.091 1.00 18.23 C
ANISOU 507 CD1 TRP A 58 2887 1966 2073 538 242 189 C
ATOM 508 CD2 TRP A 58 17.155 5.901 59.965 1.00 18.63 C
ANISOU 508 CD2 TRP A 58 2838 2073 2166 531 330 126 C
ATOM 509 NE1 TRP A 58 16.315 4.100 60.985 1.00 21.56 N
ANISOU 509 NE1 TRP A 58 3315 2425 2452 448 270 163 N
ATOM 510 CE2 TRP A 58 16.225 5.463 60.921 1.00 21.20 C
ANISOU 510 CE2 TRP A 58 3202 2415 2437 447 322 120 C
ATOM 511 CE3 TRP A 58 17.259 7.269 59.702 1.00 20.42 C
ANISOU 511 CE3 TRP A 58 3005 2321 2431 542 376 92 C
ATOM 512 CZ2 TRP A 58 15.416 6.345 61.632 1.00 26.14 C
ANISOU 512 CZ2 TRP A 58 3795 3088 3049 374 361 68 C
ATOM 513 CZ3 TRP A 58 16.452 8.139 60.400 1.00 21.99 C
ANISOU 513 CZ3 TRP A 58 3176 2555 2622 479 406 47 C
ATOM 514 CH2 TRP A 58 15.540 7.678 61.348 1.00 23.12 C
ANISOU 514 CH2 TRP A 58 3346 2724 2716 397 400 30 C
ATOM 515 N HIS A 59 19.364 4.606 55.165 1.00 17.12 N
ANISOU 515 N HIS A 59 2578 1824 2104 741 301 139 N
ATOM 516 CA HIS A 59 20.338 4.921 54.124 1.00 24.24 C
ANISOU 516 CA HIS A 59 3428 2748 3033 747 307 119 C
ATOM 517 C HIS A 59 20.172 6.366 53.668 1.00 18.52 C
ANISOU 517 C HIS A 59 2681 2042 2312 721 356 108 C
ATOM 518 O HIS A 59 19.101 6.761 53.213 1.00 17.49 O
ANISOU 518 O HIS A 59 2562 1911 2173 696 370 109 O
ATOM 519 CB HIS A 59 20.192 3.966 52.932 1.00 37.40 C
ANISOU 519 CB HIS A 59 5085 4414 4710 748 284 112 C
ATOM 520 CG HIS A 59 20.454 2.527 53.263 1.00 53.38 C
ANISOU 520 CG HIS A 59 7125 6413 6743 772 226 119 C
ATOM 521 ND1 HIS A 59 19.577 1.513 52.931 1.00 61.86 N
ANISOU 521 ND1 HIS A 59 8222 7471 7810 763 206 128 N
ATOM 522 CD2 HIS A 59 21.501 1.924 53.875 1.00 64.53 C
ANISOU 522 CD2 HIS A 59 8535 7810 8175 806 176 115 C
ATOM 523 CE1 HIS A 59 20.068 0.355 53.332 1.00 65.24 C
ANISOU 523 CE1 HIS A 59 8665 7870 8254 785 146 134 C
ATOM 524 NE2 HIS A 59 21.236 0.575 53.909 1.00 65.36 N
ANISOU 524 NE2 HIS A 59 8665 7883 8286 813 121 127 N
ATOM 525 N LEU A 60 21.224 7.164 53.799 1.00 15.09 N
ANISOU 525 N LEU A 60 2218 1623 1893 728 377 93 N
ATOM 526 CA LEU A 60 21.169 8.544 53.342 1.00 16.25 C
ANISOU 526 CA LEU A 60 2353 1777 2044 703 420 86 C
ATOM 527 C LEU A 60 21.132 8.588 51.810 1.00 18.52 C
ANISOU 527 C LEU A 60 2642 2064 2330 697 429 85 C
ATOM 528 O LEU A 60 21.922 7.924 51.140 1.00 19.53 O
ANISOU 528 O LEU A 60 2754 2202 2466 715 422 72 O
ATOM 529 CB LEU A 60 22.360 9.338 53.876 1.00 16.70 C
ANISOU 529 CB LEU A 60 2377 1851 2116 708 447 66 C
ATOM 530 CG LEU A 60 22.562 10.717 53.246 1.00 19.30 C
ANISOU 530 CG LEU A 60 2700 2182 2453 683 493 57 C
ATOM 531 CD1 LEU A 60 21.438 11.661 53.598 1.00 18.20 C
ANISOU 531 CD1 LEU A 60 2576 2025 2313 658 502 66 C
ATOM 532 CD2 LEU A 60 23.901 11.272 53.675 1.00 23.16 C
ANISOU 532 CD2 LEU A 60 3148 2695 2955 686 521 26 C
ATOM 533 N ARG A 61 20.201 9.350 51.263 1.00 15.72 N
ANISOU 533 N ARG A 61 2308 1697 1967 676 442 94 N
ATOM 534 CA ARG A 61 20.076 9.473 49.814 1.00 19.78 C
ANISOU 534 CA ARG A 61 2838 2205 2471 675 453 100 C
ATOM 535 C ARG A 61 20.646 10.787 49.314 1.00 22.73 C
ANISOU 535 C ARG A 61 3225 2567 2845 671 500 101 C
ATOM 536 O ARG A 61 21.540 10.807 48.463 1.00 21.08 O
ANISOU 536 O ARG A 61 3017 2363 2629 680 532 93 O
ATOM 537 CB ARG A 61 18.620 9.334 49.403 1.00 22.06 C
ANISOU 537 CB ARG A 61 3148 2483 2750 663 429 107 C
ATOM 538 CG ARG A 61 18.156 7.896 49.370 1.00 34.01 C
ANISOU 538 CG ARG A 61 4656 4007 4259 667 397 106 C
ATOM 539 CD ARG A 61 16.667 7.792 49.074 1.00 43.55 C
ANISOU 539 CD ARG A 61 5878 5210 5460 652 378 101 C
ATOM 540 NE ARG A 61 16.306 8.342 47.770 1.00 53.62 N
ANISOU 540 NE ARG A 61 7168 6477 6726 653 383 104 N
ATOM 541 CZ ARG A 61 15.525 9.403 47.591 1.00 56.26 C
ANISOU 541 CZ ARG A 61 7518 6794 7064 645 379 97 C
ATOM 542 NH1 ARG A 61 15.015 10.046 48.636 1.00 56.52 N
ANISOU 542 NH1 ARG A 61 7541 6818 7115 633 372 79 N
ATOM 543 NH2 ARG A 61 15.250 9.821 46.364 1.00 58.38 N
ANISOU 543 NH2 ARG A 61 7812 7049 7320 654 380 104 N
ATOM 544 N ARG A 62 20.133 11.886 49.855 1.00 20.64 N
ANISOU 544 N ARG A 62 2971 2283 2588 656 507 103 N
ATOM 545 CA ARG A 62 20.579 13.205 49.457 1.00 23.25 C
ANISOU 545 CA ARG A 62 3326 2588 2921 651 551 105 C
ATOM 546 C ARG A 62 20.267 14.245 50.522 1.00 17.77 C
ANISOU 546 C ARG A 62 2619 1881 2252 635 551 94 C
ATOM 547 O ARG A 62 19.441 14.030 51.403 1.00 16.88 O
ANISOU 547 O ARG A 62 2485 1777 2150 628 517 82 O
ATOM 548 CB ARG A 62 19.941 13.615 48.123 1.00 27.01 C
ANISOU 548 CB ARG A 62 3858 3027 3377 656 555 125 C
ATOM 549 CG ARG A 62 18.435 13.603 48.123 1.00 32.44 C
ANISOU 549 CG ARG A 62 4553 3703 4068 651 500 124 C
ATOM 550 CD ARG A 62 17.884 14.251 46.846 1.00 42.03 C
ANISOU 550 CD ARG A 62 5830 4875 5266 660 496 140 C
ATOM 551 NE ARG A 62 17.889 13.355 45.689 1.00 47.83 N
ANISOU 551 NE ARG A 62 6583 5622 5968 674 500 153 N
ATOM 552 CZ ARG A 62 16.822 12.681 45.265 1.00 51.14 C
ANISOU 552 CZ ARG A 62 6994 6054 6381 676 457 146 C
ATOM 553 NH1 ARG A 62 15.669 12.801 45.914 1.00 55.31 N
ANISOU 553 NH1 ARG A 62 7496 6584 6935 663 409 121 N
ATOM 554 NH2 ARG A 62 16.901 11.890 44.198 1.00 47.05 N
ANISOU 554 NH2 ARG A 62 6491 5549 5837 689 465 156 N
ATOM 555 N TYR A 63 20.945 15.377 50.442 1.00 15.82 N
ANISOU 555 N TYR A 63 2384 1612 2013 628 597 91 N
ATOM 556 CA TYR A 63 20.616 16.466 51.352 1.00 17.88 C
ANISOU 556 CA TYR A 63 2631 1857 2306 613 596 75 C
ATOM 557 C TYR A 63 21.046 17.824 50.859 1.00 21.00 C
ANISOU 557 C TYR A 63 3067 2202 2712 605 642 78 C
ATOM 558 O TYR A 63 21.880 17.950 49.948 1.00 23.83 O
ANISOU 558 O TYR A 63 3465 2544 3046 605 696 88 O
ATOM 559 CB TYR A 63 21.237 16.221 52.723 1.00 13.23 C
ANISOU 559 CB TYR A 63 1979 1316 1731 603 602 50 C
ATOM 560 CG TYR A 63 22.744 16.254 52.783 1.00 17.06 C
ANISOU 560 CG TYR A 63 2438 1832 2212 598 648 36 C
ATOM 561 CD1 TYR A 63 23.423 17.436 53.040 1.00 19.89 C
ANISOU 561 CD1 TYR A 63 2784 2186 2589 575 695 17 C
ATOM 562 CD2 TYR A 63 23.492 15.096 52.642 1.00 19.87 C
ANISOU 562 CD2 TYR A 63 2772 2224 2552 613 639 30 C
ATOM 563 CE1 TYR A 63 24.813 17.466 53.132 1.00 16.90 C
ANISOU 563 CE1 TYR A 63 2368 1849 2205 559 735 -11 C
ATOM 564 CE2 TYR A 63 24.884 15.121 52.734 1.00 19.61 C
ANISOU 564 CE2 TYR A 63 2701 2229 2521 606 671 -3 C
ATOM 565 CZ TYR A 63 25.525 16.314 52.982 1.00 18.57 C
ANISOU 565 CZ TYR A 63 2554 2102 2402 575 719 -25 C
ATOM 566 OH TYR A 63 26.894 16.361 53.084 1.00 22.88 O
ANISOU 566 OH TYR A 63 3053 2693 2948 558 748 -70 O
ATOM 567 N THR A 64 20.462 18.834 51.494 1.00 22.15 N
ANISOU 567 N THR A 64 3205 2318 2893 594 624 62 N
ATOM 568 CA THR A 64 20.718 20.236 51.207 1.00 25.19 C
ANISOU 568 CA THR A 64 3633 2639 3301 581 653 63 C
ATOM 569 C THR A 64 20.686 21.006 52.510 1.00 24.64 C
ANISOU 569 C THR A 64 3500 2583 3279 564 652 24 C
ATOM 570 O THR A 64 20.154 20.521 53.506 1.00 21.60 O
ANISOU 570 O THR A 64 3053 2246 2906 564 620 -3 O
ATOM 571 CB THR A 64 19.669 20.848 50.263 1.00 27.28 C
ANISOU 571 CB THR A 64 3971 2824 3568 590 600 84 C
ATOM 572 OG1 THR A 64 18.363 20.597 50.790 1.00 26.02 O
ANISOU 572 OG1 THR A 64 3766 2687 3432 598 524 54 O
ATOM 573 CG2 THR A 64 19.775 20.256 48.872 1.00 29.09 C
ANISOU 573 CG2 THR A 64 4273 3036 3745 601 608 124 C
ATOM 574 N LYS A 65 21.245 22.207 52.499 1.00 21.10 N
ANISOU 574 N LYS A 65 3059 2109 2848 524 673 20 N
ATOM 575 CA LYS A 65 21.091 23.102 53.628 1.00 24.59 C
ANISOU 575 CA LYS A 65 3443 2555 3345 508 666 -22 C
ATOM 576 C LYS A 65 19.918 24.019 53.329 1.00 30.26 C
ANISOU 576 C LYS A 65 4201 3188 4107 521 604 -31 C
ATOM 577 O LYS A 65 19.910 24.707 52.301 1.00 32.60 O
ANISOU 577 O LYS A 65 4580 3410 4395 510 587 3 O
ATOM 578 CB LYS A 65 22.368 23.891 53.874 1.00 29.43 C
ANISOU 578 CB LYS A 65 4033 3188 3961 459 722 -31 C
ATOM 579 CG LYS A 65 22.294 24.836 55.047 1.00 34.75 C
ANISOU 579 CG LYS A 65 4638 3872 4694 441 721 -79 C
ATOM 580 CD LYS A 65 23.674 25.301 55.461 1.00 40.00 C
ANISOU 580 CD LYS A 65 5260 4581 5355 398 787 -97 C
ATOM 581 CE LYS A 65 23.603 26.212 56.676 1.00 42.45 C
ANISOU 581 CE LYS A 65 5493 4910 5727 381 788 -149 C
ATOM 582 NZ LYS A 65 22.696 25.647 57.708 1.00 39.89 N
ANISOU 582 NZ LYS A 65 5106 4629 5423 407 751 -182 N
ATOM 583 N GLU A 66 18.911 23.991 54.200 1.00 30.41 N
ANISOU 583 N GLU A 66 4166 3219 4170 541 565 -81 N
ATOM 584 CA GLU A 66 17.708 24.807 54.042 1.00 33.21 C
ANISOU 584 CA GLU A 66 4533 3511 4574 552 484 -113 C
ATOM 585 C GLU A 66 17.639 25.811 55.176 1.00 37.73 C
ANISOU 585 C GLU A 66 5031 4087 5219 534 484 -178 C
ATOM 586 O GLU A 66 17.308 25.452 56.305 1.00 32.21 O
ANISOU 586 O GLU A 66 4244 3462 4530 523 486 -232 O
ATOM 587 CB GLU A 66 16.435 23.953 54.048 1.00 36.93 C
ANISOU 587 CB GLU A 66 4981 4016 5034 572 418 -142 C
ATOM 588 CG GLU A 66 16.418 22.768 53.102 1.00 41.05 C
ANISOU 588 CG GLU A 66 5549 4557 5490 585 418 -89 C
ATOM 589 CD GLU A 66 16.219 23.170 51.660 1.00 48.41 C
ANISOU 589 CD GLU A 66 6572 5414 6407 596 380 -46 C
ATOM 590 OE1 GLU A 66 15.653 24.257 51.419 1.00 54.99 O
ANISOU 590 OE1 GLU A 66 7428 6178 7287 600 320 -66 O
ATOM 591 OE2 GLU A 66 16.635 22.399 50.767 1.00 48.44 O
ANISOU 591 OE2 GLU A 66 6624 5429 6353 600 406 6 O
ATOM 592 N GLY A 67 17.940 27.070 54.880 1.00 44.46 N
ANISOU 592 N GLY A 67 6800 4708 5387 666 361 -109 N
ATOM 593 CA GLY A 67 18.051 28.065 55.926 1.00 44.84 C
ANISOU 593 CA GLY A 67 6941 4704 5391 641 389 -129 C
ATOM 594 C GLY A 67 19.214 27.689 56.819 1.00 47.80 C
ANISOU 594 C GLY A 67 7349 5036 5777 525 399 -112 C
ATOM 595 O GLY A 67 20.323 27.467 56.337 1.00 49.03 O
ANISOU 595 O GLY A 67 7505 5172 5953 461 392 -66 O
ATOM 596 N ASN A 68 18.965 27.602 58.120 1.00 45.51 N
ANISOU 596 N ASN A 68 7081 4738 5471 493 417 -144 N
ATOM 597 CA ASN A 68 20.011 27.214 59.057 1.00 47.80 C
ANISOU 597 CA ASN A 68 7401 4989 5770 364 427 -125 C
ATOM 598 C ASN A 68 19.807 25.792 59.584 1.00 36.72 C
ANISOU 598 C ASN A 68 5904 3632 4417 339 422 -129 C
ATOM 599 O ASN A 68 20.162 25.477 60.718 1.00 34.66 O
ANISOU 599 O ASN A 68 5603 3410 4155 228 420 -122 O
ATOM 600 CB ASN A 68 20.087 28.209 60.221 1.00 59.11 C
ANISOU 600 CB ASN A 68 8945 6372 7143 308 452 -155 C
ATOM 601 CG ASN A 68 21.011 29.387 59.928 1.00 62.92 C
ANISOU 601 CG ASN A 68 9533 6791 7582 251 454 -123 C
ATOM 602 OD1 ASN A 68 21.459 29.579 58.797 1.00 61.55 O
ANISOU 602 OD1 ASN A 68 9350 6616 7422 273 440 -86 O
ATOM 603 ND2 ASN A 68 21.298 30.181 60.956 1.00 67.76 N
ANISOU 603 ND2 ASN A 68 10251 7356 8138 173 471 -139 N
ATOM 604 N SER A 69 19.227 24.935 58.758 1.00 30.12 N
ANISOU 604 N SER A 69 4976 2851 3619 418 403 -127 N
ATOM 605 CA SER A 69 19.161 23.525 59.100 1.00 29.29 C
ANISOU 605 CA SER A 69 4724 2842 3561 366 376 -109 C
ATOM 606 C SER A 69 19.526 22.664 57.913 1.00 25.52 C
ANISOU 606 C SER A 69 4195 2372 3130 388 358 -66 C
ATOM 607 O SER A 69 19.425 23.084 56.754 1.00 27.00 O
ANISOU 607 O SER A 69 4426 2524 3309 468 357 -63 O
ATOM 608 CB SER A 69 17.773 23.150 59.622 1.00 39.96 C
ANISOU 608 CB SER A 69 6001 4279 4902 433 365 -160 C
ATOM 609 OG SER A 69 16.767 23.600 58.742 1.00 44.66 O
ANISOU 609 OG SER A 69 6628 4867 5475 575 368 -191 O
ATOM 610 N TRP A 70 19.980 21.458 58.206 1.00 23.17 N
ANISOU 610 N TRP A 70 3793 2132 2877 310 341 -29 N
ATOM 611 CA TRP A 70 20.280 20.496 57.163 1.00 19.58 C
ANISOU 611 CA TRP A 70 3291 1686 2463 332 327 9 C
ATOM 612 C TRP A 70 19.110 19.552 56.986 1.00 21.71 C
ANISOU 612 C TRP A 70 3475 2030 2745 390 298 -24 C
ATOM 613 O TRP A 70 18.544 19.031 57.959 1.00 18.80 O
ANISOU 613 O TRP A 70 3028 1733 2379 353 282 -45 O
ATOM 614 CB TRP A 70 21.543 19.737 57.501 1.00 19.75 C
ANISOU 614 CB TRP A 70 3262 1720 2524 219 332 80 C
ATOM 615 CG TRP A 70 22.708 20.637 57.568 1.00 28.10 C
ANISOU 615 CG TRP A 70 4398 2714 3565 156 356 126 C
ATOM 616 CD1 TRP A 70 23.124 21.376 58.645 1.00 29.48 C
ANISOU 616 CD1 TRP A 70 4612 2879 3711 66 366 129 C
ATOM 617 CD2 TRP A 70 23.617 20.925 56.508 1.00 28.88 C
ANISOU 617 CD2 TRP A 70 4553 2755 3666 172 370 180 C
ATOM 618 NE1 TRP A 70 24.244 22.098 58.312 1.00 28.60 N
ANISOU 618 NE1 TRP A 70 4576 2707 3584 17 381 186 N
ATOM 619 CE2 TRP A 70 24.571 21.831 57.007 1.00 29.42 C
ANISOU 619 CE2 TRP A 70 4666 2805 3707 82 377 215 C
ATOM 620 CE3 TRP A 70 23.725 20.497 55.178 1.00 27.03 C
ANISOU 620 CE3 TRP A 70 4280 2545 3445 238 355 192 C
ATOM 621 CZ2 TRP A 70 25.612 22.318 56.225 1.00 35.86 C
ANISOU 621 CZ2 TRP A 70 5483 3628 4514 66 370 260 C
ATOM 622 CZ3 TRP A 70 24.760 20.978 54.412 1.00 29.15 C
ANISOU 622 CZ3 TRP A 70 4556 2815 3704 221 355 234 C
ATOM 623 CH2 TRP A 70 25.688 21.880 54.935 1.00 33.03 C
ANISOU 623 CH2 TRP A 70 5088 3289 4174 139 361 269 C
ATOM 624 N ARG A 71 18.725 19.353 55.737 1.00 17.92 N
ANISOU 624 N ARG A 71 3009 1535 2265 476 287 -27 N
ATOM 625 CA ARG A 71 17.581 18.510 55.443 1.00 17.68 C
ANISOU 625 CA ARG A 71 2907 1574 2235 526 253 -54 C
ATOM 626 C ARG A 71 18.028 17.274 54.701 1.00 17.05 C
ANISOU 626 C ARG A 71 2790 1498 2190 504 238 -17 C
ATOM 627 O ARG A 71 18.427 17.355 53.535 1.00 17.03 O
ANISOU 627 O ARG A 71 2843 1441 2188 550 246 2 O
ATOM 628 CB ARG A 71 16.541 19.269 54.630 1.00 21.80 C
ANISOU 628 CB ARG A 71 3477 2090 2717 648 249 -90 C
ATOM 629 CG ARG A 71 15.276 18.474 54.369 1.00 29.59 C
ANISOU 629 CG ARG A 71 4386 3164 3694 692 208 -110 C
ATOM 630 CD ARG A 71 14.206 19.359 53.740 1.00 38.69 C
ANISOU 630 CD ARG A 71 5576 4324 4800 812 208 -137 C
ATOM 631 NE ARG A 71 13.883 20.496 54.602 1.00 44.43 N
ANISOU 631 NE ARG A 71 6334 5050 5497 836 236 -162 N
ATOM 632 CZ ARG A 71 13.122 21.526 54.242 1.00 48.99 C
ANISOU 632 CZ ARG A 71 6930 5646 6036 901 241 -171 C
ATOM 633 NH1 ARG A 71 12.590 21.578 53.024 1.00 49.27 N
ANISOU 633 NH1 ARG A 71 6954 5706 6059 948 219 -156 N
ATOM 634 NH2 ARG A 71 12.895 22.508 55.104 1.00 52.06 N
ANISOU 634 NH2 ARG A 71 7357 6026 6397 919 271 -192 N
ATOM 635 N PHE A 72 17.945 16.136 55.375 1.00 11.88 N
ANISOU 635 N PHE A 72 2047 904 1562 437 217 -8 N
ATOM 636 CA PHE A 72 18.390 14.859 54.825 1.00 13.36 C
ANISOU 636 CA PHE A 72 2204 1091 1782 409 207 27 C
ATOM 637 C PHE A 72 17.200 14.029 54.397 1.00 17.95 C
ANISOU 637 C PHE A 72 2742 1727 2349 444 162 -2 C
ATOM 638 O PHE A 72 16.231 13.890 55.157 1.00 17.64 O
ANISOU 638 O PHE A 72 2640 1766 2298 433 133 -31 O
ATOM 639 CB PHE A 72 19.223 14.073 55.853 1.00 14.99 C
ANISOU 639 CB PHE A 72 2345 1321 2028 303 216 69 C
ATOM 640 CG PHE A 72 20.429 14.823 56.355 1.00 16.70 C
ANISOU 640 CG PHE A 72 2593 1497 2254 249 255 110 C
ATOM 641 CD1 PHE A 72 21.659 14.696 55.724 1.00 17.91 C
ANISOU 641 CD1 PHE A 72 2781 1597 2426 238 285 173 C
ATOM 642 CD2 PHE A 72 20.337 15.654 57.462 1.00 18.03 C
ANISOU 642 CD2 PHE A 72 2760 1686 2406 205 261 90 C
ATOM 643 CE1 PHE A 72 22.769 15.399 56.191 1.00 17.89 C
ANISOU 643 CE1 PHE A 72 2802 1569 2426 177 315 222 C
ATOM 644 CE2 PHE A 72 21.450 16.360 57.928 1.00 14.99 C
ANISOU 644 CE2 PHE A 72 2412 1265 2020 140 291 131 C
ATOM 645 CZ PHE A 72 22.659 16.231 57.297 1.00 14.43 C
ANISOU 645 CZ PHE A 72 2367 1149 1968 121 315 200 C
ATOM 646 N GLU A 73 17.279 13.513 53.170 1.00 15.92 N
ANISOU 646 N GLU A 73 2526 1435 2089 484 155 10 N
ATOM 647 CA GLU A 73 16.355 12.518 52.643 1.00 17.24 C
ANISOU 647 CA GLU A 73 2665 1645 2241 494 109 -6 C
ATOM 648 C GLU A 73 16.961 11.150 52.890 1.00 16.04 C
ANISOU 648 C GLU A 73 2480 1490 2124 421 107 27 C
ATOM 649 O GLU A 73 18.022 10.811 52.366 1.00 16.40 O
ANISOU 649 O GLU A 73 2570 1470 2191 418 140 65 O
ATOM 650 CB GLU A 73 16.078 12.734 51.139 1.00 16.72 C
ANISOU 650 CB GLU A 73 2672 1537 2142 575 103 -13 C
ATOM 651 CG GLU A 73 15.355 14.046 50.795 1.00 21.74 C
ANISOU 651 CG GLU A 73 3339 2180 2740 659 104 -42 C
ATOM 652 CD GLU A 73 15.133 14.212 49.282 1.00 32.62 C
ANISOU 652 CD GLU A 73 4784 3522 4087 732 97 -42 C
ATOM 653 OE1 GLU A 73 14.545 13.304 48.646 1.00 35.52 O
ANISOU 653 OE1 GLU A 73 5145 3916 4435 728 59 -46 O
ATOM 654 OE2 GLU A 73 15.559 15.249 48.730 1.00 38.47 O
ANISOU 654 OE2 GLU A 73 5542 4253 4820 733 119 -34 O
ATOM 655 N AVAL A 74 16.307 10.372 53.735 0.44 18.52 N
ANISOU 655 N AVAL A 74 2716 1878 2444 363 70 17 N
ATOM 656 N BVAL A 74 16.276 10.353 53.700 0.56 18.41 N
ANISOU 656 N BVAL A 74 2702 1864 2429 365 69 16 N
ATOM 657 CA AVAL A 74 16.831 9.069 54.073 0.44 19.26 C
ANISOU 657 CA AVAL A 74 2777 1968 2571 292 68 49 C
ATOM 658 CA BVAL A 74 16.803 9.072 54.151 0.56 18.98 C
ANISOU 658 CA BVAL A 74 2737 1938 2537 289 67 48 C
ATOM 659 C AVAL A 74 15.812 8.012 53.681 0.44 20.27 C
ANISOU 659 C AVAL A 74 2890 2137 2674 279 10 30 C
ATOM 660 C BVAL A 74 15.816 7.952 53.843 0.56 20.26 C
ANISOU 660 C BVAL A 74 2879 2143 2677 269 9 32 C
ATOM 661 O AVAL A 74 14.608 8.257 53.699 0.44 20.71 O
ANISOU 661 O AVAL A 74 2915 2262 2694 296 -34 -2 O
ATOM 662 O BVAL A 74 14.624 8.086 54.109 0.56 20.86 O
ANISOU 662 O BVAL A 74 2907 2298 2722 271 -37 1 O
ATOM 663 CB AVAL A 74 17.182 8.976 55.575 0.44 16.13 C
ANISOU 663 CB AVAL A 74 2298 1620 2210 212 77 65 C
ATOM 664 CB BVAL A 74 17.101 9.104 55.667 0.56 15.34 C
ANISOU 664 CB BVAL A 74 2194 1527 2108 213 75 61 C
ATOM 665 CG1AVAL A 74 18.224 10.031 55.934 0.44 15.21 C
ANISOU 665 CG1AVAL A 74 2207 1463 2109 211 129 88 C
ATOM 666 CG1BVAL A 74 17.689 7.782 56.137 0.56 14.47 C
ANISOU 666 CG1BVAL A 74 2042 1418 2037 138 77 102 C
ATOM 667 CG2AVAL A 74 15.950 9.153 56.426 0.44 14.35 C
ANISOU 667 CG2AVAL A 74 1998 1491 1962 196 33 26 C
ATOM 668 CG2BVAL A 74 18.043 10.260 55.992 0.56 14.27 C
ANISOU 668 CG2BVAL A 74 2088 1351 1984 218 126 78 C
ATOM 669 N GLN A 75 16.304 6.850 53.277 1.00 19.62 N
ANISOU 669 N GLN A 75 2837 2010 2606 250 13 56 N
ATOM 670 CA GLN A 75 15.447 5.708 53.010 1.00 16.60 C
ANISOU 670 CA GLN A 75 2451 1659 2199 214 -43 44 C
ATOM 671 C GLN A 75 15.513 4.779 54.220 1.00 16.39 C
ANISOU 671 C GLN A 75 2343 1678 2207 124 -59 63 C
ATOM 672 O GLN A 75 16.601 4.461 54.699 1.00 18.48 O
ANISOU 672 O GLN A 75 2601 1905 2518 96 -14 102 O
ATOM 673 CB GLN A 75 15.881 4.993 51.725 1.00 20.75 C
ANISOU 673 CB GLN A 75 3082 2095 2708 242 -31 55 C
ATOM 674 CG GLN A 75 15.214 3.648 51.516 1.00 23.62 C
ANISOU 674 CG GLN A 75 3460 2470 3046 186 -84 50 C
ATOM 675 CD GLN A 75 15.625 2.984 50.222 1.00 30.19 C
ANISOU 675 CD GLN A 75 4415 3205 3851 217 -68 56 C
ATOM 676 OE1 GLN A 75 15.639 3.619 49.163 1.00 33.74 O
ANISOU 676 OE1 GLN A 75 4933 3618 4271 285 -55 43 O
ATOM 677 NE2 GLN A 75 15.962 1.698 50.298 1.00 26.90 N
ANISOU 677 NE2 GLN A 75 4032 2745 3443 169 -66 76 N
ATOM 678 N VAL A 76 14.360 4.368 54.732 1.00 18.15 N
ANISOU 678 N VAL A 76 2500 1991 2407 78 -122 43 N
ATOM 679 CA VAL A 76 14.308 3.533 55.936 1.00 17.09 C
ANISOU 679 CA VAL A 76 2279 1912 2303 -11 -143 61 C
ATOM 680 C VAL A 76 13.552 2.243 55.625 1.00 21.47 C
ANISOU 680 C VAL A 76 2844 2485 2829 -66 -206 60 C
ATOM 681 O VAL A 76 12.391 2.300 55.229 1.00 23.72 O
ANISOU 681 O VAL A 76 3121 2830 3062 -62 -264 36 O
ATOM 682 CB VAL A 76 13.628 4.259 57.110 1.00 20.18 C
ANISOU 682 CB VAL A 76 2564 2411 2693 -29 -162 43 C
ATOM 683 CG1 VAL A 76 13.551 3.339 58.346 1.00 19.78 C
ANISOU 683 CG1 VAL A 76 2420 2424 2672 -126 -188 64 C
ATOM 684 CG2 VAL A 76 14.364 5.561 57.452 1.00 18.77 C
ANISOU 684 CG2 VAL A 76 2392 2206 2534 15 -102 42 C
ATOM 685 N ASP A 77 14.218 1.096 55.780 1.00 18.85 N
ANISOU 685 N ASP A 77 2535 2101 2527 -117 -194 91 N
ATOM 686 CA ASP A 77 13.632 -0.203 55.453 1.00 26.13 C
ANISOU 686 CA ASP A 77 3491 3018 3420 -175 -250 92 C
ATOM 687 C ASP A 77 13.475 -1.054 56.689 1.00 26.79 C
ANISOU 687 C ASP A 77 3483 3162 3532 -270 -280 114 C
ATOM 688 O ASP A 77 14.338 -1.043 57.557 1.00 22.39 O
ANISOU 688 O ASP A 77 2876 2600 3032 -287 -234 143 O
ATOM 689 CB ASP A 77 14.499 -0.999 54.473 1.00 34.78 C
ANISOU 689 CB ASP A 77 4715 3983 4515 -152 -210 110 C
ATOM 690 CG ASP A 77 14.985 -0.182 53.311 1.00 49.29 C
ANISOU 690 CG ASP A 77 6643 5748 6336 -56 -163 99 C
ATOM 691 OD1 ASP A 77 14.198 0.598 52.752 1.00 56.72 O
ANISOU 691 OD1 ASP A 77 7589 6728 7234 -19 -194 67 O
ATOM 692 OD2 ASP A 77 16.166 -0.333 52.944 1.00 57.33 O
ANISOU 692 OD2 ASP A 77 7726 6675 7384 -15 -93 130 O
ATOM 693 N ASN A 78 12.396 -1.822 56.732 1.00 33.40 N
ANISOU 693 N ASN A 78 4302 4060 4330 -336 -359 105 N
ATOM 694 CA ASN A 78 12.292 -2.933 57.665 1.00 35.69 C
ANISOU 694 CA ASN A 78 4535 4383 4641 -433 -393 131 C
ATOM 695 C ASN A 78 11.196 -3.906 57.263 1.00 31.43 C
ANISOU 695 C ASN A 78 4025 3875 4041 -505 -481 125 C
ATOM 696 O ASN A 78 10.101 -3.503 56.860 1.00 29.54 O
ANISOU 696 O ASN A 78 3769 3712 3744 -502 -539 104 O
ATOM 697 CB ASN A 78 12.038 -2.434 59.088 1.00 43.84 C
ANISOU 697 CB ASN A 78 5419 5534 5706 -468 -401 136 C
ATOM 698 CG ASN A 78 12.682 -3.329 60.140 1.00 49.09 C
ANISOU 698 CG ASN A 78 6030 6196 6427 -542 -387 176 C
ATOM 699 OD1 ASN A 78 13.144 -4.434 59.835 1.00 48.50 O
ANISOU 699 OD1 ASN A 78 6027 6040 6362 -573 -382 201 O
ATOM 700 ND2 ASN A 78 12.717 -2.857 61.381 1.00 51.19 N
ANISOU 700 ND2 ASN A 78 6176 6549 6725 -570 -380 185 N
ATOM 701 N ASN A 79 11.509 -5.193 57.372 1.00 37.80 N
ANISOU 701 N ASN A 79 4881 4622 4859 -571 -491 149 N
ATOM 702 CA ASN A 79 10.532 -6.258 57.193 1.00 40.90 C
ANISOU 702 CA ASN A 79 5302 5043 5196 -665 -580 150 C
ATOM 703 C ASN A 79 9.861 -6.201 55.824 1.00 40.32 C
ANISOU 703 C ASN A 79 5337 4941 5041 -646 -621 123 C
ATOM 704 O ASN A 79 8.668 -6.468 55.697 1.00 42.13 O
ANISOU 704 O ASN A 79 5543 5257 5207 -714 -710 121 O
ATOM 705 CB ASN A 79 9.468 -6.200 58.300 1.00 47.17 C
ANISOU 705 CB ASN A 79 5941 6001 5981 -741 -654 158 C
ATOM 706 CG ASN A 79 10.061 -6.289 59.709 1.00 51.59 C
ANISOU 706 CG ASN A 79 6388 6598 6614 -771 -622 184 C
ATOM 707 OD1 ASN A 79 11.040 -7.004 59.948 1.00 52.57 O
ANISOU 707 OD1 ASN A 79 6553 6634 6788 -785 -575 211 O
ATOM 708 ND2 ASN A 79 9.457 -5.564 60.650 1.00 51.03 N
ANISOU 708 ND2 ASN A 79 6187 6657 6545 -749 -619 175 N
ATOM 709 N GLY A 80 10.625 -5.836 54.804 1.00 42.34 N
ANISOU 709 N GLY A 80 5707 5083 5297 -558 -555 110 N
ATOM 710 CA GLY A 80 10.110 -5.810 53.444 1.00 44.25 C
ANISOU 710 CA GLY A 80 6064 5286 5462 -540 -586 86 C
ATOM 711 C GLY A 80 9.414 -4.523 53.038 1.00 39.57 C
ANISOU 711 C GLY A 80 5416 4780 4837 -478 -603 65 C
ATOM 712 O GLY A 80 8.959 -4.394 51.905 1.00 39.66 O
ANISOU 712 O GLY A 80 5512 4772 4784 -460 -629 49 O
ATOM 713 N GLN A 81 9.326 -3.567 53.956 1.00 34.65 N
ANISOU 713 N GLN A 81 4658 4253 4256 -445 -585 66 N
ATOM 714 CA GLN A 81 8.720 -2.286 53.633 1.00 32.59 C
ANISOU 714 CA GLN A 81 4347 4067 3967 -373 -590 49 C
ATOM 715 C GLN A 81 9.757 -1.167 53.588 1.00 27.96 C
ANISOU 715 C GLN A 81 3770 3419 3434 -265 -495 38 C
ATOM 716 O GLN A 81 10.569 -1.042 54.499 1.00 30.19 O
ANISOU 716 O GLN A 81 4003 3687 3782 -262 -444 50 O
ATOM 717 CB GLN A 81 7.631 -1.940 54.632 1.00 34.57 C
ANISOU 717 CB GLN A 81 4445 4484 4205 -410 -647 58 C
ATOM 718 CG GLN A 81 6.844 -0.705 54.236 1.00 39.68 C
ANISOU 718 CG GLN A 81 5048 5216 4812 -332 -655 47 C
ATOM 719 CD GLN A 81 5.528 -0.600 54.966 1.00 42.01 C
ANISOU 719 CD GLN A 81 5208 5686 5069 -374 -727 67 C
ATOM 720 OE1 GLN A 81 4.574 -1.320 54.660 1.00 43.29 O
ANISOU 720 OE1 GLN A 81 5363 5917 5168 -452 -811 88 O
ATOM 721 NE2 GLN A 81 5.465 0.297 55.935 1.00 39.09 N
ANISOU 721 NE2 GLN A 81 4731 5390 4730 -326 -694 64 N
ATOM 722 N THR A 82 9.713 -0.360 52.528 1.00 20.67 N
ANISOU 722 N THR A 82 2910 2464 2479 -184 -477 21 N
ATOM 723 CA THR A 82 10.651 0.732 52.332 1.00 17.62 C
ANISOU 723 CA THR A 82 2546 2015 2133 -85 -394 13 C
ATOM 724 C THR A 82 9.951 2.083 52.441 1.00 18.95 C
ANISOU 724 C THR A 82 2644 2273 2284 -20 -399 -2 C
ATOM 725 O THR A 82 8.934 2.298 51.817 1.00 23.08 O
ANISOU 725 O THR A 82 3165 2857 2746 -9 -450 -8 O
ATOM 726 CB THR A 82 11.334 0.639 50.969 1.00 21.17 C
ANISOU 726 CB THR A 82 3139 2340 2565 -31 -356 8 C
ATOM 727 OG1 THR A 82 12.112 -0.561 50.905 1.00 24.56 O
ANISOU 727 OG1 THR A 82 3644 2675 3014 -73 -334 24 O
ATOM 728 CG2 THR A 82 12.237 1.829 50.753 1.00 19.36 C
ANISOU 728 CG2 THR A 82 2927 2059 2372 67 -278 6 C
ATOM 729 N GLU A 83 10.495 2.990 53.244 1.00 19.55 N
ANISOU 729 N GLU A 83 2664 2357 2408 21 -345 -3 N
ATOM 730 CA GLU A 83 9.888 4.302 53.432 1.00 20.82 C
ANISOU 730 CA GLU A 83 2769 2591 2552 89 -340 -18 C
ATOM 731 C GLU A 83 10.884 5.430 53.152 1.00 19.69 C
ANISOU 731 C GLU A 83 2680 2362 2439 174 -262 -26 C
ATOM 732 O GLU A 83 12.103 5.252 53.305 1.00 18.78 O
ANISOU 732 O GLU A 83 2602 2162 2373 165 -209 -12 O
ATOM 733 CB GLU A 83 9.336 4.438 54.865 1.00 21.42 C
ANISOU 733 CB GLU A 83 2717 2780 2641 50 -359 -15 C
ATOM 734 CG GLU A 83 8.279 3.408 55.239 1.00 25.41 C
ANISOU 734 CG GLU A 83 3153 3389 3114 -38 -442 0 C
ATOM 735 CD GLU A 83 7.499 3.767 56.506 1.00 33.51 C
ANISOU 735 CD GLU A 83 4046 4550 4137 -54 -463 4 C
ATOM 736 OE1 GLU A 83 7.895 4.692 57.239 1.00 29.92 O
ANISOU 736 OE1 GLU A 83 3560 4098 3712 -9 -410 -8 O
ATOM 737 OE2 GLU A 83 6.470 3.113 56.768 1.00 44.42 O
ANISOU 737 OE2 GLU A 83 5358 6039 5480 -114 -535 21 O
ATOM 738 N GLN A 84 10.350 6.575 52.736 1.00 17.71 N
ANISOU 738 N GLN A 84 2432 2141 2157 255 -257 -41 N
ATOM 739 CA GLN A 84 11.125 7.801 52.577 1.00 14.81 C
ANISOU 739 CA GLN A 84 2110 1706 1812 333 -190 -49 C
ATOM 740 C GLN A 84 10.835 8.756 53.723 1.00 16.38 C
ANISOU 740 C GLN A 84 2235 1970 2019 352 -172 -60 C
ATOM 741 O GLN A 84 9.722 9.241 53.893 1.00 20.87 O
ANISOU 741 O GLN A 84 2751 2630 2548 388 -200 -69 O
ATOM 742 CB GLN A 84 10.823 8.472 51.234 1.00 15.90 C
ANISOU 742 CB GLN A 84 2322 1813 1907 417 -189 -57 C
ATOM 743 CG GLN A 84 10.955 7.517 50.039 1.00 20.77 C
ANISOU 743 CG GLN A 84 3019 2372 2500 397 -212 -50 C
ATOM 744 CD GLN A 84 12.358 6.949 49.892 1.00 32.66 C
ANISOU 744 CD GLN A 84 4593 3765 4052 376 -161 -35 C
ATOM 745 OE1 GLN A 84 13.350 7.654 50.093 1.00 37.23 O
ANISOU 745 OE1 GLN A 84 5191 4287 4669 410 -101 -27 O
ATOM 746 NE2 GLN A 84 12.450 5.658 49.547 1.00 36.95 N
ANISOU 746 NE2 GLN A 84 5175 4276 4586 318 -185 -27 N
ATOM 747 N TRP A 85 11.862 9.008 54.514 1.00 15.77 N
ANISOU 747 N TRP A 85 2156 1846 1989 328 -123 -54 N
ATOM 748 CA TRP A 85 11.761 9.852 55.689 1.00 17.70 C
ANISOU 748 CA TRP A 85 2346 2138 2242 332 -101 -66 C
ATOM 749 C TRP A 85 12.571 11.114 55.473 1.00 20.31 C
ANISOU 749 C TRP A 85 2751 2386 2581 392 -40 -72 C
ATOM 750 O TRP A 85 13.499 11.135 54.676 1.00 19.78 O
ANISOU 750 O TRP A 85 2758 2226 2530 406 -10 -57 O
ATOM 751 CB TRP A 85 12.284 9.133 56.925 1.00 14.69 C
ANISOU 751 CB TRP A 85 1899 1780 1904 235 -98 -50 C
ATOM 752 CG TRP A 85 11.490 7.966 57.417 1.00 19.86 C
ANISOU 752 CG TRP A 85 2469 2525 2553 165 -158 -43 C
ATOM 753 CD1 TRP A 85 10.571 7.222 56.729 1.00 22.47 C
ANISOU 753 CD1 TRP A 85 2793 2899 2847 158 -217 -41 C
ATOM 754 CD2 TRP A 85 11.558 7.405 58.733 1.00 23.54 C
ANISOU 754 CD2 TRP A 85 2847 3050 3047 81 -169 -32 C
ATOM 755 NE1 TRP A 85 10.064 6.230 57.542 1.00 23.94 N
ANISOU 755 NE1 TRP A 85 2893 3166 3036 73 -266 -28 N
ATOM 756 CE2 TRP A 85 10.655 6.323 58.778 1.00 25.77 C
ANISOU 756 CE2 TRP A 85 3072 3410 3311 28 -235 -23 C
ATOM 757 CE3 TRP A 85 12.304 7.712 59.880 1.00 23.54 C
ANISOU 757 CE3 TRP A 85 2813 3048 3084 37 -131 -25 C
ATOM 758 CZ2 TRP A 85 10.473 5.545 59.926 1.00 22.98 C
ANISOU 758 CZ2 TRP A 85 2624 3130 2976 -60 -264 -9 C
ATOM 759 CZ3 TRP A 85 12.116 6.948 61.020 1.00 24.32 C
ANISOU 759 CZ3 TRP A 85 2817 3223 3202 -49 -157 -12 C
ATOM 760 CH2 TRP A 85 11.211 5.870 61.028 1.00 22.99 C
ANISOU 760 CH2 TRP A 85 2589 3129 3017 -94 -222 -4 C
ATOM 761 N GLU A 86 12.232 12.164 56.203 1.00 21.84 N
ANISOU 761 N GLU A 86 2928 2611 2759 427 -19 -92 N
ATOM 762 CA GLU A 86 12.975 13.407 56.146 1.00 21.12 C
ANISOU 762 CA GLU A 86 2914 2440 2670 472 36 -99 C
ATOM 763 C GLU A 86 13.554 13.659 57.513 1.00 20.09 C
ANISOU 763 C GLU A 86 2754 2317 2562 405 63 -98 C
ATOM 764 O GLU A 86 12.845 13.511 58.513 1.00 16.97 O
ANISOU 764 O GLU A 86 2283 2008 2156 380 45 -112 O
ATOM 765 CB GLU A 86 12.069 14.567 55.734 1.00 28.89 C
ANISOU 765 CB GLU A 86 3932 3441 3605 581 43 -124 C
ATOM 766 CG GLU A 86 12.725 15.921 55.812 1.00 33.28 C
ANISOU 766 CG GLU A 86 4574 3915 4156 624 98 -134 C
ATOM 767 CD GLU A 86 11.727 17.057 55.690 1.00 35.91 C
ANISOU 767 CD GLU A 86 4933 4273 4439 733 110 -159 C
ATOM 768 OE1 GLU A 86 11.372 17.405 54.546 1.00 42.10 O
ANISOU 768 OE1 GLU A 86 5760 5036 5201 813 106 -156 O
ATOM 769 OE2 GLU A 86 11.296 17.591 56.735 1.00 36.09 O
ANISOU 769 OE2 GLU A 86 4932 4337 4442 742 126 -178 O
ATOM 770 N VAL A 87 14.836 14.014 57.563 1.00 15.48 N
ANISOU 770 N VAL A 87 2226 1650 2005 372 104 -77 N
ATOM 771 CA VAL A 87 15.508 14.281 58.831 1.00 15.61 C
ANISOU 771 CA VAL A 87 2222 1671 2040 294 129 -69 C
ATOM 772 C VAL A 87 16.084 15.679 58.809 1.00 16.37 C
ANISOU 772 C VAL A 87 2413 1691 2115 325 174 -76 C
ATOM 773 O VAL A 87 16.983 15.964 58.026 1.00 20.22 O
ANISOU 773 O VAL A 87 2971 2099 2614 334 196 -50 O
ATOM 774 CB VAL A 87 16.630 13.280 59.106 1.00 15.23 C
ANISOU 774 CB VAL A 87 2140 1605 2042 197 135 -19 C
ATOM 775 CG1 VAL A 87 17.326 13.603 60.440 1.00 18.74 C
ANISOU 775 CG1 VAL A 87 2558 2062 2499 108 158 -4 C
ATOM 776 CG2 VAL A 87 16.087 11.894 59.119 1.00 13.72 C
ANISOU 776 CG2 VAL A 87 1870 1476 1868 165 92 -12 C
ATOM 777 N GLN A 88 15.572 16.566 59.658 1.00 14.63 N
ANISOU 777 N GLN A 88 2203 1494 1861 340 187 -111 N
ATOM 778 CA GLN A 88 15.997 17.954 59.618 1.00 16.68 C
ANISOU 778 CA GLN A 88 2572 1675 2091 373 228 -123 C
ATOM 779 C GLN A 88 16.836 18.239 60.853 1.00 16.36 C
ANISOU 779 C GLN A 88 2536 1624 2055 267 250 -111 C
ATOM 780 O GLN A 88 16.401 17.994 61.976 1.00 17.19 O
ANISOU 780 O GLN A 88 2578 1800 2155 222 242 -128 O
ATOM 781 CB GLN A 88 14.776 18.873 59.532 1.00 22.95 C
ANISOU 781 CB GLN A 88 3400 2488 2833 487 234 -170 C
ATOM 782 CG GLN A 88 15.078 20.327 59.294 1.00 31.00 C
ANISOU 782 CG GLN A 88 4549 3413 3816 542 276 -186 C
ATOM 783 CD GLN A 88 13.944 21.030 58.559 1.00 41.70 C
ANISOU 783 CD GLN A 88 5940 4773 5129 684 281 -214 C
ATOM 784 OE1 GLN A 88 13.850 20.973 57.327 1.00 44.60 O
ANISOU 784 OE1 GLN A 88 6329 5116 5502 746 270 -201 O
ATOM 785 NE2 GLN A 88 13.078 21.693 59.312 1.00 42.87 N
ANISOU 785 NE2 GLN A 88 6097 4957 5234 740 300 -249 N
ATOM 786 N ILE A 89 18.051 18.728 60.656 1.00 13.72 N
ANISOU 786 N ILE A 89 2274 1211 1728 218 275 -77 N
ATOM 787 CA ILE A 89 18.953 18.920 61.785 1.00 13.86 C
ANISOU 787 CA ILE A 89 2293 1225 1748 98 291 -52 C
ATOM 788 C ILE A 89 19.393 20.364 61.913 1.00 16.61 C
ANISOU 788 C ILE A 89 2771 1490 2050 96 323 -64 C
ATOM 789 O ILE A 89 19.882 20.939 60.945 1.00 19.83 O
ANISOU 789 O ILE A 89 3262 1822 2452 136 335 -47 O
ATOM 790 CB ILE A 89 20.191 18.022 61.646 1.00 16.89 C
ANISOU 790 CB ILE A 89 2628 1607 2182 6 289 23 C
ATOM 791 CG1 ILE A 89 19.740 16.573 61.415 1.00 15.61 C
ANISOU 791 CG1 ILE A 89 2358 1512 2063 15 259 33 C
ATOM 792 CG2 ILE A 89 21.075 18.136 62.864 1.00 20.59 C
ANISOU 792 CG2 ILE A 89 3080 2092 2651 -127 300 58 C
ATOM 793 CD1 ILE A 89 20.837 15.524 61.518 1.00 13.33 C
ANISOU 793 CD1 ILE A 89 2006 1235 1825 -72 261 107 C
ATOM 794 N GLU A 90 19.208 20.958 63.088 1.00 17.62 N
ANISOU 794 N GLU A 90 2925 1630 2140 51 335 -95 N
ATOM 795 CA GLU A 90 19.776 22.273 63.355 1.00 25.25 C
ANISOU 795 CA GLU A 90 4026 2510 3056 19 364 -102 C
ATOM 796 C GLU A 90 21.031 22.116 64.200 1.00 22.50 C
ANISOU 796 C GLU A 90 3665 2166 2717 -145 365 -45 C
ATOM 797 O GLU A 90 20.986 21.581 65.294 1.00 21.68 O
ANISOU 797 O GLU A 90 3485 2133 2621 -226 356 -44 O
ATOM 798 CB GLU A 90 18.776 23.186 64.060 1.00 37.64 C
ANISOU 798 CB GLU A 90 5664 4074 4565 81 385 -173 C
ATOM 799 CG GLU A 90 17.512 23.483 63.267 1.00 51.64 C
ANISOU 799 CG GLU A 90 7452 5849 6319 249 390 -220 C
ATOM 800 CD GLU A 90 16.584 24.467 63.978 1.00 64.29 C
ANISOU 800 CD GLU A 90 9131 7442 7855 321 421 -282 C
ATOM 801 OE1 GLU A 90 16.697 24.625 65.216 1.00 65.55 O
ANISOU 801 OE1 GLU A 90 9298 7620 7986 241 433 -299 O
ATOM 802 OE2 GLU A 90 15.738 25.084 63.295 1.00 70.23 O
ANISOU 802 OE2 GLU A 90 9936 8170 8580 462 438 -311 O
ATOM 803 N VAL A 91 22.156 22.563 63.663 1.00 23.10 N
ANISOU 803 N VAL A 91 3810 2175 2792 -194 373 9 N
ATOM 804 CA VAL A 91 23.418 22.556 64.378 1.00 25.94 C
ANISOU 804 CA VAL A 91 4165 2539 3151 -353 374 78 C
ATOM 805 C VAL A 91 23.671 23.966 64.867 1.00 32.45 C
ANISOU 805 C VAL A 91 5142 3285 3901 -401 392 54 C
ATOM 806 O VAL A 91 23.860 24.873 64.065 1.00 36.74 O
ANISOU 806 O VAL A 91 5802 3740 4417 -352 403 52 O
ATOM 807 CB VAL A 91 24.586 22.116 63.481 1.00 29.56 C
ANISOU 807 CB VAL A 91 4596 2985 3650 -386 372 170 C
ATOM 808 CG1 VAL A 91 25.833 21.910 64.303 1.00 28.86 C
ANISOU 808 CG1 VAL A 91 4466 2934 3565 -551 369 254 C
ATOM 809 CG2 VAL A 91 24.229 20.850 62.692 1.00 23.18 C
ANISOU 809 CG2 VAL A 91 3677 2225 2905 -305 361 181 C
ATOM 810 N ARG A 92 23.645 24.166 66.175 1.00 36.06 N
ANISOU 810 N ARG A 92 5607 3770 4323 -497 394 35 N
ATOM 811 CA ARG A 92 23.916 25.488 66.721 1.00 41.29 C
ANISOU 811 CA ARG A 92 6431 4352 4907 -558 411 11 C
ATOM 812 C ARG A 92 25.190 25.419 67.548 1.00 46.64 C
ANISOU 812 C ARG A 92 7090 5059 5572 -751 397 88 C
ATOM 813 O ARG A 92 25.320 24.562 68.418 1.00 41.68 O
ANISOU 813 O ARG A 92 6330 4536 4971 -824 380 110 O
ATOM 814 CB ARG A 92 22.741 25.987 67.566 1.00 40.85 C
ANISOU 814 CB ARG A 92 6427 4295 4798 -498 429 -85 C
ATOM 815 CG ARG A 92 21.383 26.014 66.843 1.00 41.47 C
ANISOU 815 CG ARG A 92 6500 4371 4885 -301 441 -153 C
ATOM 816 CD ARG A 92 21.332 27.084 65.759 1.00 41.09 C
ANISOU 816 CD ARG A 92 6596 4209 4806 -200 460 -169 C
ATOM 817 NE ARG A 92 19.969 27.343 65.300 1.00 43.23 N
ANISOU 817 NE ARG A 92 6883 4478 5065 -18 478 -236 N
ATOM 818 CZ ARG A 92 19.470 26.901 64.150 1.00 47.10 C
ANISOU 818 CZ ARG A 92 7311 4988 5599 102 467 -231 C
ATOM 819 NH1 ARG A 92 20.227 26.177 63.339 1.00 50.44 N
ANISOU 819 NH1 ARG A 92 7662 5424 6079 65 442 -169 N
ATOM 820 NH2 ARG A 92 18.220 27.189 63.806 1.00 47.28 N
ANISOU 820 NH2 ARG A 92 7345 5018 5602 259 483 -284 N
ATOM 821 N ASN A 93 26.134 26.306 67.255 1.00 53.63 N
ANISOU 821 N ASN A 93 8026 5929 6420 -777 377 117 N
ATOM 822 CA ASN A 93 27.402 26.364 67.981 1.00 58.99 C
ANISOU 822 CA ASN A 93 8618 6704 7090 -888 333 172 C
ATOM 823 C ASN A 93 28.163 25.044 67.963 1.00 55.49 C
ANISOU 823 C ASN A 93 7959 6387 6738 -896 300 248 C
ATOM 824 O ASN A 93 28.641 24.590 68.998 1.00 59.23 O
ANISOU 824 O ASN A 93 8329 6951 7224 -959 275 271 O
ATOM 825 CB ASN A 93 27.167 26.800 69.430 1.00 66.11 C
ANISOU 825 CB ASN A 93 9577 7618 7925 -980 336 127 C
ATOM 826 CG ASN A 93 26.597 28.199 69.530 1.00 72.52 C
ANISOU 826 CG ASN A 93 10615 8299 8638 -969 372 56 C
ATOM 827 OD1 ASN A 93 27.008 29.103 68.802 1.00 75.84 O
ANISOU 827 OD1 ASN A 93 11133 8656 9026 -943 369 62 O
ATOM 828 ND2 ASN A 93 25.638 28.386 70.429 1.00 73.07 N
ANISOU 828 ND2 ASN A 93 10771 8330 8664 -979 406 -13 N
ATOM 829 N GLY A 94 28.264 24.429 66.790 1.00 47.85 N
ANISOU 829 N GLY A 94 6931 5417 5833 -817 304 286 N
ATOM 830 CA GLY A 94 28.974 23.169 66.639 1.00 41.20 C
ANISOU 830 CA GLY A 94 5901 4674 5077 -799 284 359 C
ATOM 831 C GLY A 94 28.334 21.936 67.267 1.00 40.30 C
ANISOU 831 C GLY A 94 5678 4623 5009 -795 285 350 C
ATOM 832 O GLY A 94 28.902 20.843 67.213 1.00 38.02 O
ANISOU 832 O GLY A 94 5245 4407 4794 -766 276 405 O
ATOM 833 N ARG A 95 27.157 22.089 67.871 1.00 36.59 N
ANISOU 833 N ARG A 95 5280 4123 4499 -816 304 279 N
ATOM 834 CA ARG A 95 26.507 20.955 68.531 1.00 31.51 C
ANISOU 834 CA ARG A 95 4526 3551 3897 -822 301 268 C
ATOM 835 C ARG A 95 25.122 20.677 67.946 1.00 23.98 C
ANISOU 835 C ARG A 95 3636 2531 2944 -771 341 212 C
ATOM 836 O ARG A 95 24.492 21.583 67.413 1.00 25.98 O
ANISOU 836 O ARG A 95 4012 2703 3157 -685 358 150 O
ATOM 837 CB ARG A 95 26.394 21.216 70.035 1.00 37.85 C
ANISOU 837 CB ARG A 95 5321 4403 4658 -902 288 236 C
ATOM 838 CG ARG A 95 27.689 21.002 70.811 1.00 41.78 C
ANISOU 838 CG ARG A 95 5713 4982 5177 -933 251 293 C
ATOM 839 CD ARG A 95 27.794 21.954 71.988 1.00 43.83 C
ANISOU 839 CD ARG A 95 6054 5244 5356 -1020 243 258 C
ATOM 840 NE ARG A 95 26.570 22.000 72.782 1.00 47.14 N
ANISOU 840 NE ARG A 95 6519 5659 5732 -1055 263 188 N
ATOM 841 CZ ARG A 95 26.465 21.528 74.023 1.00 50.12 C
ANISOU 841 CZ ARG A 95 6819 6117 6109 -1091 244 180 C
ATOM 842 NH1 ARG A 95 27.516 20.969 74.611 1.00 50.60 N
ANISOU 842 NH1 ARG A 95 6767 6251 6209 -1088 208 234 N
ATOM 843 NH2 ARG A 95 25.312 21.614 74.675 1.00 47.48 N
ANISOU 843 NH2 ARG A 95 6527 5781 5733 -1123 269 114 N
ATOM 844 N ILE A 96 24.652 19.433 68.054 1.00 22.55 N
ANISOU 844 N ILE A 96 3329 2421 2818 -756 332 218 N
ATOM 845 CA ILE A 96 23.321 19.080 67.562 1.00 20.29 C
ANISOU 845 CA ILE A 96 3017 2147 2546 -613 324 141 C
ATOM 846 C ILE A 96 22.274 19.664 68.485 1.00 18.93 C
ANISOU 846 C ILE A 96 2878 1994 2322 -593 326 56 C
ATOM 847 O ILE A 96 22.176 19.279 69.665 1.00 19.04 O
ANISOU 847 O ILE A 96 2822 2079 2333 -678 318 55 O
ATOM 848 CB ILE A 96 23.091 17.571 67.466 1.00 20.83 C
ANISOU 848 CB ILE A 96 2938 2294 2681 -601 303 169 C
ATOM 849 CG1 ILE A 96 24.180 16.881 66.642 1.00 22.24 C
ANISOU 849 CG1 ILE A 96 3080 2459 2910 -620 309 261 C
ATOM 850 CG2 ILE A 96 21.708 17.294 66.871 1.00 19.61 C
ANISOU 850 CG2 ILE A 96 2768 2153 2531 -461 288 96 C
ATOM 851 CD1 ILE A 96 24.343 17.433 65.271 1.00 22.04 C
ANISOU 851 CD1 ILE A 96 3148 2349 2877 -523 321 260 C
ATOM 852 N LYS A 97 21.475 20.587 67.962 1.00 19.08 N
ANISOU 852 N LYS A 97 3001 1951 2298 -474 340 -12 N
ATOM 853 CA LYS A 97 20.524 21.296 68.816 1.00 19.07 C
ANISOU 853 CA LYS A 97 3051 1957 2236 -441 354 -90 C
ATOM 854 C LYS A 97 19.119 20.714 68.743 1.00 16.63 C
ANISOU 854 C LYS A 97 2657 1721 1940 -323 341 -141 C
ATOM 855 O LYS A 97 18.494 20.423 69.772 1.00 17.80 O
ANISOU 855 O LYS A 97 2742 1948 2075 -346 336 -170 O
ATOM 856 CB LYS A 97 20.496 22.779 68.449 1.00 27.37 C
ANISOU 856 CB LYS A 97 4283 2896 3222 -384 384 -130 C
ATOM 857 CG LYS A 97 19.439 23.585 69.168 1.00 34.80 C
ANISOU 857 CG LYS A 97 5297 3830 4095 -316 409 -212 C
ATOM 858 CD LYS A 97 19.678 23.627 70.664 1.00 46.05 C
ANISOU 858 CD LYS A 97 6715 5297 5484 -447 413 -218 C
ATOM 859 CE LYS A 97 18.616 24.475 71.365 1.00 52.51 C
ANISOU 859 CE LYS A 97 7621 6105 6227 -366 446 -301 C
ATOM 860 NZ LYS A 97 18.651 24.346 72.851 1.00 52.40 N
ANISOU 860 NZ LYS A 97 7579 6151 6179 -480 449 -314 N
ATOM 861 N ARG A 98 18.615 20.547 67.532 1.00 17.05 N
ANISOU 861 N ARG A 98 2707 1757 2015 -202 334 -149 N
ATOM 862 CA ARG A 98 17.262 20.046 67.347 1.00 18.38 C
ANISOU 862 CA ARG A 98 2798 1997 2187 -92 317 -188 C
ATOM 863 C ARG A 98 17.234 19.151 66.116 1.00 17.92 C
ANISOU 863 C ARG A 98 2679 1948 2184 -41 290 -157 C
ATOM 864 O ARG A 98 17.819 19.495 65.079 1.00 18.67 O
ANISOU 864 O ARG A 98 2844 1961 2286 -10 300 -135 O
ATOM 865 CB ARG A 98 16.269 21.212 67.218 1.00 23.72 C
ANISOU 865 CB ARG A 98 3576 2639 2799 39 347 -252 C
ATOM 866 CG ARG A 98 14.797 20.812 67.237 1.00 36.64 C
ANISOU 866 CG ARG A 98 5127 4371 4425 148 333 -286 C
ATOM 867 CD ARG A 98 13.866 22.006 67.511 1.00 50.38 C
ANISOU 867 CD ARG A 98 6961 6091 6090 265 374 -342 C
ATOM 868 NE ARG A 98 14.181 22.719 68.756 1.00 65.45 N
ANISOU 868 NE ARG A 98 8945 7974 7950 195 407 -369 N
ATOM 869 CZ ARG A 98 13.556 22.541 69.924 1.00 71.63 C
ANISOU 869 CZ ARG A 98 9670 8843 8704 179 412 -394 C
ATOM 870 NH1 ARG A 98 12.567 21.663 70.030 1.00 73.22 N
ANISOU 870 NH1 ARG A 98 9728 9168 8923 226 383 -391 N
ATOM 871 NH2 ARG A 98 13.921 23.244 70.995 1.00 72.38 N
ANISOU 871 NH2 ARG A 98 9852 8902 8747 109 444 -420 N
ATOM 872 N VAL A 99 16.573 18.007 66.237 1.00 15.42 N
ANISOU 872 N VAL A 99 2236 1725 1898 -37 256 -153 N
ATOM 873 CA VAL A 99 16.415 17.077 65.126 1.00 16.11 C
ANISOU 873 CA VAL A 99 2271 1823 2028 8 228 -128 C
ATOM 874 C VAL A 99 14.943 16.776 64.944 1.00 20.16 C
ANISOU 874 C VAL A 99 2724 2414 2521 102 201 -164 C
ATOM 875 O VAL A 99 14.236 16.503 65.911 1.00 21.49 O
ANISOU 875 O VAL A 99 2817 2672 2676 83 189 -182 O
ATOM 876 CB VAL A 99 17.194 15.764 65.354 1.00 16.27 C
ANISOU 876 CB VAL A 99 2196 1879 2109 -100 206 -71 C
ATOM 877 CG1 VAL A 99 16.854 14.734 64.255 1.00 15.48 C
ANISOU 877 CG1 VAL A 99 2050 1789 2041 -48 175 -55 C
ATOM 878 CG2 VAL A 99 18.686 16.053 65.384 1.00 16.18 C
ANISOU 878 CG2 VAL A 99 2235 1798 2114 -185 233 -18 C
ATOM 879 N THR A 100 14.476 16.857 63.707 1.00 16.72 N
ANISOU 879 N THR A 100 2320 1953 2081 203 193 -170 N
ATOM 880 CA THR A 100 13.085 16.599 63.409 1.00 17.78 C
ANISOU 880 CA THR A 100 2398 2169 2191 291 165 -192 C
ATOM 881 C THR A 100 12.960 15.527 62.351 1.00 16.19 C
ANISOU 881 C THR A 100 2151 1980 2021 298 124 -165 C
ATOM 882 O THR A 100 13.432 15.700 61.239 1.00 18.76 O
ANISOU 882 O THR A 100 2545 2228 2355 335 132 -153 O
ATOM 883 CB THR A 100 12.375 17.859 62.925 1.00 18.05 C
ANISOU 883 CB THR A 100 2518 2171 2171 422 194 -226 C
ATOM 884 OG1 THR A 100 12.478 18.848 63.948 1.00 19.15 O
ANISOU 884 OG1 THR A 100 2715 2289 2273 416 235 -255 O
ATOM 885 CG2 THR A 100 10.930 17.557 62.673 1.00 20.23 C
ANISOU 885 CG2 THR A 100 2719 2550 2419 509 164 -235 C
ATOM 886 N ILE A 101 12.331 14.421 62.706 1.00 12.59 N
ANISOU 886 N ILE A 101 1586 1621 1577 258 79 -156 N
ATOM 887 CA ILE A 101 12.153 13.313 61.776 1.00 12.35 C
ANISOU 887 CA ILE A 101 1520 1603 1569 252 36 -132 C
ATOM 888 C ILE A 101 10.703 13.266 61.349 1.00 21.18 C
ANISOU 888 C ILE A 101 2596 2807 2643 331 0 -145 C
ATOM 889 O ILE A 101 9.814 13.225 62.192 1.00 21.82 O
ANISOU 889 O ILE A 101 2600 2992 2700 332 -17 -154 O
ATOM 890 CB ILE A 101 12.565 11.985 62.430 1.00 18.93 C
ANISOU 890 CB ILE A 101 2268 2476 2447 135 8 -102 C
ATOM 891 CG1 ILE A 101 14.006 12.093 62.925 1.00 17.64 C
ANISOU 891 CG1 ILE A 101 2136 2242 2323 57 47 -76 C
ATOM 892 CG2 ILE A 101 12.386 10.816 61.460 1.00 23.53 C
ANISOU 892 CG2 ILE A 101 2836 3060 3046 127 -35 -80 C
ATOM 893 CD1 ILE A 101 14.500 10.897 63.652 1.00 14.99 C
ANISOU 893 CD1 ILE A 101 1719 1945 2033 -52 29 -40 C
ATOM 894 N THR A 102 10.453 13.297 60.044 1.00 25.75 N
ANISOU 894 N THR A 102 3222 3353 3209 397 -13 -141 N
ATOM 895 CA THR A 102 9.088 13.272 59.537 1.00 26.14 C
ANISOU 895 CA THR A 102 3230 3491 3212 469 -50 -142 C
ATOM 896 C THR A 102 8.891 12.117 58.572 1.00 28.73 C
ANISOU 896 C THR A 102 3541 3830 3546 436 -104 -119 C
ATOM 897 O THR A 102 9.690 11.926 57.664 1.00 25.73 O
ANISOU 897 O THR A 102 3234 3354 3188 431 -94 -112 O
ATOM 898 CB THR A 102 8.716 14.572 58.814 1.00 29.03 C
ANISOU 898 CB THR A 102 3673 3821 3537 596 -16 -158 C
ATOM 899 OG1 THR A 102 8.897 15.683 59.689 1.00 28.89 O
ANISOU 899 OG1 THR A 102 3692 3778 3505 630 37 -183 O
ATOM 900 CG2 THR A 102 7.258 14.528 58.363 1.00 32.48 C
ANISOU 900 CG2 THR A 102 4049 4369 3921 670 -55 -146 C
ATOM 901 N HIS A 103 7.846 11.327 58.803 1.00 31.60 N
ANISOU 901 N HIS A 103 3811 4311 3886 407 -162 -105 N
ATOM 902 CA HIS A 103 7.438 10.301 57.858 1.00 32.40 C
ANISOU 902 CA HIS A 103 3905 4432 3975 376 -221 -84 C
ATOM 903 C HIS A 103 5.949 10.026 57.982 1.00 36.87 C
ANISOU 903 C HIS A 103 4374 5149 4487 386 -279 -65 C
ATOM 904 O HIS A 103 5.503 9.336 58.905 1.00 39.41 O
ANISOU 904 O HIS A 103 4601 5564 4808 317 -315 -53 O
ATOM 905 CB HIS A 103 8.238 9.012 58.059 1.00 32.60 C
ANISOU 905 CB HIS A 103 3924 4415 4047 261 -240 -70 C
ATOM 906 CG HIS A 103 8.299 8.533 59.478 1.00 29.90 C
ANISOU 906 CG HIS A 103 3492 4136 3731 180 -247 -65 C
ATOM 907 ND1 HIS A 103 7.636 7.403 59.909 1.00 27.66 N
ANISOU 907 ND1 HIS A 103 3123 3946 3440 100 -310 -45 N
ATOM 908 CD2 HIS A 103 8.972 9.004 60.556 1.00 27.75 C
ANISOU 908 CD2 HIS A 103 3206 3847 3490 158 -202 -74 C
ATOM 909 CE1 HIS A 103 7.881 7.212 61.193 1.00 27.86 C
ANISOU 909 CE1 HIS A 103 3079 4012 3495 39 -302 -43 C
ATOM 910 NE2 HIS A 103 8.691 8.170 61.610 1.00 24.54 N
ANISOU 910 NE2 HIS A 103 2701 3527 3097 71 -236 -61 N
ATOM 911 N VAL A 104 5.177 10.579 57.057 1.00 40.43 N
ANISOU 911 N VAL A 104 4844 5630 4888 473 -289 -57 N
ATOM 912 CA VAL A 104 3.735 10.392 57.071 1.00 47.21 C
ANISOU 912 CA VAL A 104 5607 6643 5688 490 -344 -26 C
ATOM 913 C VAL A 104 3.267 9.765 55.770 1.00 55.62 C
ANISOU 913 C VAL A 104 6696 7720 6716 473 -403 0 C
ATOM 914 O VAL A 104 3.960 9.844 54.754 1.00 56.89 O
ANISOU 914 O VAL A 104 6960 7766 6892 489 -385 -13 O
ATOM 915 CB VAL A 104 2.986 11.718 57.283 1.00 50.28 C
ANISOU 915 CB VAL A 104 5975 7094 6035 621 -303 -25 C
ATOM 916 CG1 VAL A 104 3.340 12.316 58.627 1.00 51.58 C
ANISOU 916 CG1 VAL A 104 6122 7254 6221 633 -249 -52 C
ATOM 917 CG2 VAL A 104 3.308 12.694 56.166 1.00 53.04 C
ANISOU 917 CG2 VAL A 104 6432 7345 6376 722 -261 -37 C
ATOM 918 OXT VAL A 104 2.186 9.178 55.710 1.00 59.90 O
ANISOU 918 OXT VAL A 104 7157 8390 7210 438 -470 37 O
TER 919 VAL A 104
HETATM 920 O HOH A 201 26.515 8.586 56.398 1.00 60.39 O
HETATM 921 O HOH A 202 23.605 4.160 53.849 1.00 53.31 O
HETATM 922 O HOH A 203 20.654 23.670 74.003 1.00 48.30 O
HETATM 923 O HOH A 204 10.269 17.796 73.411 1.00 56.44 O
HETATM 924 O HOH A 205 18.271 21.444 72.388 1.00 40.18 O
HETATM 925 O HOH A 206 26.992 26.178 62.787 1.00 61.64 O
HETATM 926 O HOH A 207 8.268 -5.937 50.352 1.00 39.47 O
HETATM 927 O HOH A 208 20.479 29.974 63.190 1.00 36.04 O
HETATM 928 O HOH A 209 12.492 4.427 69.210 1.00 56.55 O
HETATM 929 O HOH A 210 25.926 3.006 73.577 1.00 48.31 O
HETATM 930 O HOH A 211 21.703 0.462 57.345 1.00 41.31 O
HETATM 931 O HOH A 212 17.267 1.803 53.764 1.00 34.93 O
HETATM 932 O HOH A 213 9.358 6.259 64.225 1.00 39.90 O
HETATM 933 O HOH A 214 20.252 -2.309 70.408 1.00 37.33 O
HETATM 934 O HOH A 215 11.988 -0.332 69.945 1.00 41.38 O
HETATM 935 O HOH A 216 26.055 17.723 69.771 1.00 26.83 O
HETATM 936 O HOH A 217 13.613 -6.744 60.779 1.00 64.40 O
HETATM 937 O HOH A 218 19.861 15.317 79.077 1.00 29.09 O
HETATM 938 O HOH A 219 5.444 11.286 53.250 1.00 53.48 O
HETATM 939 O HOH A 220 31.311 1.288 56.425 1.00 41.73 O
HETATM 940 O HOH A 221 12.026 8.196 76.114 1.00 44.50 O
HETATM 941 O HOH A 222 22.059 23.701 61.282 1.00 29.14 O
HETATM 942 O HOH A 223 17.181 18.281 51.253 1.00 25.09 O
HETATM 943 O HOH A 224 7.759 10.895 53.201 1.00 42.49 O
HETATM 944 O HOH A 225 17.353 -7.674 67.987 1.00 29.37 O
HETATM 945 O HOH A 226 16.564 -6.022 59.106 1.00 41.20 O
HETATM 946 O HOH A 227 13.189 4.661 64.253 1.00 23.14 O
HETATM 947 O HOH A 228 11.466 16.447 59.429 1.00 22.63 O
HETATM 948 O HOH A 229 32.386 3.166 71.832 1.00 40.80 O
HETATM 949 O HOH A 230 26.054 10.730 57.086 1.00 24.66 O
HETATM 950 O HOH A 231 3.028 8.391 59.532 1.00 40.55 O
HETATM 951 O HOH A 232 27.515 26.166 64.832 1.00 49.88 O
HETATM 952 O HOH A 233 9.911 3.100 62.457 1.00 39.36 O
HETATM 953 O HOH A 234 12.260 15.875 52.463 1.00 42.03 O
HETATM 954 O HOH A 235 10.385 9.430 74.379 1.00 40.50 O
HETATM 955 O HOH A 236 35.052 11.970 73.557 1.00 38.36 O
HETATM 956 O HOH A 237 17.189 26.565 61.344 1.00 46.83 O
HETATM 957 O HOH A 238 23.181 20.938 71.620 1.00 26.45 O
HETATM 958 O HOH A 239 13.139 -4.722 54.537 1.00 43.51 O
HETATM 959 O HOH A 240 30.550 6.239 72.813 1.00 31.87 O
HETATM 960 O HOH A 241 13.358 26.283 62.530 1.00 51.95 O
HETATM 961 O HOH A 242 20.385 1.653 60.055 1.00 21.75 O
HETATM 962 O HOH A 243 3.865 14.080 71.874 1.00 46.77 O
HETATM 963 O HOH A 244 14.859 20.181 63.323 1.00 24.45 O
HETATM 964 O HOH A 245 21.931 -0.828 60.409 1.00 38.77 O
HETATM 965 O HOH A 246 31.521 25.175 63.658 1.00 55.93 O
HETATM 966 O HOH A 247 10.171 -2.817 49.903 1.00 29.88 O
HETATM 967 O HOH A 248 28.755 18.379 50.644 1.00 50.87 O
HETATM 968 O HOH A 249 7.061 8.264 54.193 1.00 43.13 O
HETATM 969 O HOH A 250 20.220 -1.218 62.063 1.00 31.41 O
HETATM 970 O HOH A 251 14.118 3.623 67.056 1.00 29.33 O
HETATM 971 O HOH A 252 17.873 17.041 48.944 1.00 34.12 O
HETATM 972 O HOH A 253 13.617 10.584 51.783 1.00 29.02 O
HETATM 973 O HOH A 254 10.456 3.910 65.211 1.00 53.18 O
HETATM 974 O HOH A 255 20.479 12.880 78.860 1.00 33.88 O
HETATM 975 O HOH A 256 24.438 6.587 52.027 1.00 50.85 O
HETATM 976 O HOH A 257 7.048 12.003 55.175 1.00 46.53 O
HETATM 977 O HOH A 258 15.039 22.773 61.473 1.00 59.12 O
HETATM 978 O HOH A 259 21.236 5.222 49.966 1.00 36.43 O
HETATM 979 O HOH A 260 12.303 10.147 47.003 1.00 51.80 O
HETATM 980 O HOH A 261 14.381 6.675 74.020 1.00 38.60 O
HETATM 981 O HOH A 262 14.701 22.257 64.071 1.00 65.91 O
HETATM 982 O HOH A 263 32.461 18.454 63.682 1.00 40.61 O
HETATM 983 O HOH A 264 29.176 24.462 63.588 1.00 62.46 O
HETATM 984 O HOH A 265 14.064 17.435 51.066 1.00 35.51 O
HETATM 985 O HOH A 266 22.881 4.464 51.273 1.00 58.14 O
HETATM 986 O HOH A 267 18.650 -2.707 54.160 1.00 50.07 O
HETATM 987 O HOH A 268 13.498 4.641 71.648 1.00 45.38 O
HETATM 988 O HOH A 269 8.858 2.238 65.614 1.00 50.32 O
MASTER 276 0 0 3 6 0 0 6 962 1 0 9
END
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