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+anno_start	anno_end	anno_text	entity_type	sentence	section
+26	31	human	species	Structural diversity in a human antibody germline library	TITLE
+32	40	antibody	protein_type	Structural diversity in a human antibody germline library	TITLE
+11	19	antibody	protein_type	To support antibody therapeutic development, the crystal structures of a set of 16 germline variants composed of 4 different kappa light chains paired with 4 different heavy chains have been determined.	ABSTRACT
+49	67	crystal structures	evidence	To support antibody therapeutic development, the crystal structures of a set of 16 germline variants composed of 4 different kappa light chains paired with 4 different heavy chains have been determined.	ABSTRACT
+125	143	kappa light chains	structure_element	To support antibody therapeutic development, the crystal structures of a set of 16 germline variants composed of 4 different kappa light chains paired with 4 different heavy chains have been determined.	ABSTRACT
+168	180	heavy chains	structure_element	To support antibody therapeutic development, the crystal structures of a set of 16 germline variants composed of 4 different kappa light chains paired with 4 different heavy chains have been determined.	ABSTRACT
+9	21	heavy chains	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+29	54	antigen-binding fragments	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+56	60	Fabs	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+76	110	complementarity-determining region	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+112	115	CDR	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+117	119	H3	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+152	155	Fab	structure_element	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+156	165	structure	evidence	All four heavy chains of the antigen-binding fragments (Fabs) have the same complementarity-determining region (CDR) H3 that was reported in an earlier Fab structure.	ABSTRACT
+4	22	structure analyses	experimental_method	The structure analyses include comparisons of the overall structures, canonical structures of the CDRs and the VH:VL packing interactions.	ABSTRACT
+58	68	structures	evidence	The structure analyses include comparisons of the overall structures, canonical structures of the CDRs and the VH:VL packing interactions.	ABSTRACT
+80	90	structures	evidence	The structure analyses include comparisons of the overall structures, canonical structures of the CDRs and the VH:VL packing interactions.	ABSTRACT
+98	102	CDRs	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the CDRs and the VH:VL packing interactions.	ABSTRACT
+111	137	VH:VL packing interactions	site	The structure analyses include comparisons of the overall structures, canonical structures of the CDRs and the VH:VL packing interactions.	ABSTRACT
+4	7	CDR	structure_element	The CDR conformations for the most part are tightly clustered, especially for the ones with shorter lengths.	ABSTRACT
+4	10	longer	protein_state	The longer CDRs with tandem glycines or serines have more conformational diversity than the others.	ABSTRACT
+11	15	CDRs	structure_element	The longer CDRs with tandem glycines or serines have more conformational diversity than the others.	ABSTRACT
+28	36	glycines	residue_name	The longer CDRs with tandem glycines or serines have more conformational diversity than the others.	ABSTRACT
+40	47	serines	residue_name	The longer CDRs with tandem glycines or serines have more conformational diversity than the others.	ABSTRACT
+0	3	CDR	structure_element	CDR H3, despite having the same amino acid sequence, exhibits the largest conformational diversity.	ABSTRACT
+4	6	H3	structure_element	CDR H3, despite having the same amino acid sequence, exhibits the largest conformational diversity.	ABSTRACT
+18	28	structures	evidence	About half of the structures have CDR H3 conformations similar to that of the parent; the others diverge significantly.	ABSTRACT
+34	37	CDR	structure_element	About half of the structures have CDR H3 conformations similar to that of the parent; the others diverge significantly.	ABSTRACT
+38	40	H3	structure_element	About half of the structures have CDR H3 conformations similar to that of the parent; the others diverge significantly.	ABSTRACT
+27	30	CDR	structure_element	One conclusion is that the CDR H3 conformations are influenced by both their amino acid sequence and their structural environment determined by the heavy and light chain pairing.	ABSTRACT
+31	33	H3	structure_element	One conclusion is that the CDR H3 conformations are influenced by both their amino acid sequence and their structural environment determined by the heavy and light chain pairing.	ABSTRACT
+148	153	heavy	structure_element	One conclusion is that the CDR H3 conformations are influenced by both their amino acid sequence and their structural environment determined by the heavy and light chain pairing.	ABSTRACT
+158	169	light chain	structure_element	One conclusion is that the CDR H3 conformations are influenced by both their amino acid sequence and their structural environment determined by the heavy and light chain pairing.	ABSTRACT
+4	16	stem regions	structure_element	The stem regions of 14 of the variant pairs are in the ‘kinked’ conformation, and only 2 are in the extended conformation.	ABSTRACT
+56	62	kinked	protein_state	The stem regions of 14 of the variant pairs are in the ‘kinked’ conformation, and only 2 are in the extended conformation.	ABSTRACT
+100	108	extended	protein_state	The stem regions of 14 of the variant pairs are in the ‘kinked’ conformation, and only 2 are in the extended conformation.	ABSTRACT
+19	21	VH	structure_element	The packing of the VH and VL domains is consistent with our knowledge of antibody structure, and the tilt angles between these domains cover a range of 11 degrees.	ABSTRACT
+26	28	VL	structure_element	The packing of the VH and VL domains is consistent with our knowledge of antibody structure, and the tilt angles between these domains cover a range of 11 degrees.	ABSTRACT
+73	81	antibody	protein_type	The packing of the VH and VL domains is consistent with our knowledge of antibody structure, and the tilt angles between these domains cover a range of 11 degrees.	ABSTRACT
+82	91	structure	evidence	The packing of the VH and VL domains is consistent with our knowledge of antibody structure, and the tilt angles between these domains cover a range of 11 degrees.	ABSTRACT
+101	112	tilt angles	evidence	The packing of the VH and VL domains is consistent with our knowledge of antibody structure, and the tilt angles between these domains cover a range of 11 degrees.	ABSTRACT
+10	20	structures	evidence	Two of 16 structures showed particularly large variations in the tilt angles when compared with the other pairings.	ABSTRACT
+65	76	tilt angles	evidence	Two of 16 structures showed particularly large variations in the tilt angles when compared with the other pairings.	ABSTRACT
+4	14	structures	evidence	The structures and their analyses provide a rich foundation for future antibody modeling and engineering efforts.	ABSTRACT
+71	79	antibody	protein_type	The structures and their analyses provide a rich foundation for future antibody modeling and engineering efforts.	ABSTRACT
+24	34	antibodies	protein_type	At present, therapeutic antibodies are the largest class of biotherapeutic proteins that are in clinical trials.	INTRO
+22	32	antibodies	protein_type	The use of monoclonal antibodies as therapeutics began in the early 1980s, and their composition has transitioned from murine antibodies to generally less immunogenic humanized and human antibodies.	INTRO
+119	125	murine	taxonomy_domain	The use of monoclonal antibodies as therapeutics began in the early 1980s, and their composition has transitioned from murine antibodies to generally less immunogenic humanized and human antibodies.	INTRO
+126	136	antibodies	protein_type	The use of monoclonal antibodies as therapeutics began in the early 1980s, and their composition has transitioned from murine antibodies to generally less immunogenic humanized and human antibodies.	INTRO
+181	186	human	species	The use of monoclonal antibodies as therapeutics began in the early 1980s, and their composition has transitioned from murine antibodies to generally less immunogenic humanized and human antibodies.	INTRO
+187	197	antibodies	protein_type	The use of monoclonal antibodies as therapeutics began in the early 1980s, and their composition has transitioned from murine antibodies to generally less immunogenic humanized and human antibodies.	INTRO
+42	47	human	species	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+48	58	antibodies	protein_type	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+78	82	mice	taxonomy_domain	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+94	99	human	species	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+100	108	antibody	protein_type	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+144	149	human	species	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+163	181	in vitro selection	experimental_method	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+187	205	antibody libraries	experimental_method	The technologies currently used to obtain human antibodies include transgenic mice containing human antibody repertoires, cloning directly from human B cells, and in vitro selection from antibody libraries using various display technologies.	INTRO
+17	25	antibody	protein_type	Once a candidate antibody is identified, protein engineering is usually required to produce a molecule with the right biophysical and functional properties.	INTRO
+41	60	protein engineering	experimental_method	Once a candidate antibody is identified, protein engineering is usually required to produce a molecule with the right biophysical and functional properties.	INTRO
+63	80	atomic structures	evidence	All engineering efforts are guided by our understanding of the atomic structures of antibodies.	INTRO
+84	94	antibodies	protein_type	All engineering efforts are guided by our understanding of the atomic structures of antibodies.	INTRO
+21	38	crystal structure	evidence	In such efforts, the crystal structure of the specific antibody may not be available, but modeling can be used to guide the engineering efforts.	INTRO
+55	63	antibody	protein_type	In such efforts, the crystal structure of the specific antibody may not be available, but modeling can be used to guide the engineering efforts.	INTRO
+8	16	antibody	protein_type	Today's antibody modeling approaches, which normally focus on the variable region, are being developed by the application of structural principles and insights that are evolving as our knowledge of antibody structures continues to expand.	INTRO
+66	81	variable region	structure_element	Today's antibody modeling approaches, which normally focus on the variable region, are being developed by the application of structural principles and insights that are evolving as our knowledge of antibody structures continues to expand.	INTRO
+198	206	antibody	protein_type	Today's antibody modeling approaches, which normally focus on the variable region, are being developed by the application of structural principles and insights that are evolving as our knowledge of antibody structures continues to expand.	INTRO
+207	217	structures	evidence	Today's antibody modeling approaches, which normally focus on the variable region, are being developed by the application of structural principles and insights that are evolving as our knowledge of antibody structures continues to expand.	INTRO
+36	46	antibodies	protein_type	Our current structural knowledge of antibodies is based on a multitude of studies that used many techniques to gain insight into the functional and structural properties of this class of macromolecule.	INTRO
+15	23	antibody	protein_type	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+40	43	IgG	protein	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+45	48	IgD	protein	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+50	53	IgE	protein	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+55	58	IgA	protein	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+63	66	IgM	protein	Five different antibody isotypes occur, IgG, IgD, IgE, IgA and IgM, and each isotype has a unique role in the adaptive immune system.	INTRO
+0	3	IgG	protein	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+5	8	IgD	protein	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+13	16	IgE	protein	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+44	56	heavy chains	structure_element	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+58	61	HCs	structure_element	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+69	81	light chains	structure_element	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+83	86	LCs	structure_element	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+103	118	disulfide bonds	ptm	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+126	129	IgA	protein	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+134	137	IgM	protein	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+175	185	antibodies	protein_type	IgG, IgD and IgE isotypes are composed of 2 heavy chains (HCs) and 2 light chains (LCs) linked through disulfide bonds, while IgA and IgM are double and quintuple versions of antibodies, respectively.	INTRO
+9	12	IgG	protein	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+14	17	IgD	protein	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+22	25	IgA	protein	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+51	59	variable	structure_element	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+61	62	V	structure_element	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+70	78	constant	structure_element	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+80	81	C	structure_element	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+98	101	IgE	protein	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+106	109	IgM	protein	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+164	172	C domain	structure_element	Isotypes IgG, IgD and IgA each have 4 domains, one variable (V) and 3 constant (C) domains, while IgE and IgM each have the same 4 domains along with an additional C domain.	INTRO
+53	54	J	structure_element	These multimeric forms are linked with an additional J chain.	INTRO
+4	7	LCs	structure_element	The LCs that associate with the HCs are divided into 2 functionally indistinguishable classes, κ and λ.	INTRO
+32	35	HCs	structure_element	The LCs that associate with the HCs are divided into 2 functionally indistinguishable classes, κ and λ.	INTRO
+95	96	κ	structure_element	The LCs that associate with the HCs are divided into 2 functionally indistinguishable classes, κ and λ.	INTRO
+101	102	λ	structure_element	The LCs that associate with the HCs are divided into 2 functionally indistinguishable classes, κ and λ.	INTRO
+5	6	κ	structure_element	Both κ and λ polypeptide chains are composed of a single V domain and a single C domain.	INTRO
+11	12	λ	structure_element	Both κ and λ polypeptide chains are composed of a single V domain and a single C domain.	INTRO
+57	65	V domain	structure_element	Both κ and λ polypeptide chains are composed of a single V domain and a single C domain.	INTRO
+79	87	C domain	structure_element	Both κ and λ polypeptide chains are composed of a single V domain and a single C domain.	INTRO
+4	9	heavy	structure_element	The heavy and light chains are composed of structural domains that have ∼110 amino acid residues.	INTRO
+14	26	light chains	structure_element	The heavy and light chains are composed of structural domains that have ∼110 amino acid residues.	INTRO
+43	61	structural domains	structure_element	The heavy and light chains are composed of structural domains that have ∼110 amino acid residues.	INTRO
+72	96	∼110 amino acid residues	residue_range	The heavy and light chains are composed of structural domains that have ∼110 amino acid residues.	INTRO
+70	89	immunoglobulin fold	structure_element	These domains have a common folding pattern often referred to as the “immunoglobulin fold,” formed by the packing together of 2 anti-parallel β-sheets.	INTRO
+128	150	anti-parallel β-sheets	structure_element	These domains have a common folding pattern often referred to as the “immunoglobulin fold,” formed by the packing together of 2 anti-parallel β-sheets.	INTRO
+4	25	immunoglobulin chains	protein_type	All immunoglobulin chains have an N-terminal V domain followed by 1 to 4 C domains, depending upon the chain type.	INTRO
+45	53	V domain	structure_element	All immunoglobulin chains have an N-terminal V domain followed by 1 to 4 C domains, depending upon the chain type.	INTRO
+73	82	C domains	structure_element	All immunoglobulin chains have an N-terminal V domain followed by 1 to 4 C domains, depending upon the chain type.	INTRO
+3	13	antibodies	protein_type	In antibodies, the heavy and light chain V domains pack together forming the antigen combining site.	INTRO
+19	40	heavy and light chain	structure_element	In antibodies, the heavy and light chain V domains pack together forming the antigen combining site.	INTRO
+41	50	V domains	structure_element	In antibodies, the heavy and light chain V domains pack together forming the antigen combining site.	INTRO
+77	99	antigen combining site	site	In antibodies, the heavy and light chain V domains pack together forming the antigen combining site.	INTRO
+81	89	antibody	protein_type	This site, which interacts with the antigen (or target), is the focus of current antibody modeling efforts.	INTRO
+5	21	interaction site	site	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+39	74	complementarity-determining regions	structure_element	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+76	80	CDRs	structure_element	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+112	149	antibody amino acid sequence analyses	experimental_method	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+156	169	hypervariable	protein_state	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+255	263	antibody	protein_type	This interaction site is composed of 6 complementarity-determining regions (CDRs) that were identified in early antibody amino acid sequence analyses to be hypervariable in nature, and thus are responsible for the sequence and structural diversity of our antibody repertoire.	INTRO
+30	41	CDR regions	structure_element	The sequence diversity of the CDR regions presents a substantial challenge to antibody modeling.	INTRO
+78	86	antibody	protein_type	The sequence diversity of the CDR regions presents a substantial challenge to antibody modeling.	INTRO
+20	39	structural analysis	experimental_method	However, an initial structural analysis of the combining sites of the small set of structures of immunoglobulin fragments available in the 1980s found that 5 of the 6 hypervariable loops or CDRs had canonical structures (a limited set of main-chain conformations).	INTRO
+47	62	combining sites	site	However, an initial structural analysis of the combining sites of the small set of structures of immunoglobulin fragments available in the 1980s found that 5 of the 6 hypervariable loops or CDRs had canonical structures (a limited set of main-chain conformations).	INTRO
+83	93	structures	evidence	However, an initial structural analysis of the combining sites of the small set of structures of immunoglobulin fragments available in the 1980s found that 5 of the 6 hypervariable loops or CDRs had canonical structures (a limited set of main-chain conformations).	INTRO
+167	186	hypervariable loops	structure_element	However, an initial structural analysis of the combining sites of the small set of structures of immunoglobulin fragments available in the 1980s found that 5 of the 6 hypervariable loops or CDRs had canonical structures (a limited set of main-chain conformations).	INTRO
+190	194	CDRs	structure_element	However, an initial structural analysis of the combining sites of the small set of structures of immunoglobulin fragments available in the 1980s found that 5 of the 6 hypervariable loops or CDRs had canonical structures (a limited set of main-chain conformations).	INTRO
+2	5	CDR	structure_element	A CDR canonical structure is defined by its length and conserved residues located in the hypervariable loop and framework residues (V-region residues that are not part of the CDRs).	INTRO
+89	107	hypervariable loop	structure_element	A CDR canonical structure is defined by its length and conserved residues located in the hypervariable loop and framework residues (V-region residues that are not part of the CDRs).	INTRO
+112	130	framework residues	structure_element	A CDR canonical structure is defined by its length and conserved residues located in the hypervariable loop and framework residues (V-region residues that are not part of the CDRs).	INTRO
+132	140	V-region	structure_element	A CDR canonical structure is defined by its length and conserved residues located in the hypervariable loop and framework residues (V-region residues that are not part of the CDRs).	INTRO
+175	179	CDRs	structure_element	A CDR canonical structure is defined by its length and conserved residues located in the hypervariable loop and framework residues (V-region residues that are not part of the CDRs).	INTRO
+24	32	antibody	protein_type	Furthermore, studies of antibody sequences revealed that the total number of canonical structures are limited for each CDR, indicating possibly that antigen recognition may be affected by structural restrictions at the antigen-binding site.	INTRO
+119	122	CDR	structure_element	Furthermore, studies of antibody sequences revealed that the total number of canonical structures are limited for each CDR, indicating possibly that antigen recognition may be affected by structural restrictions at the antigen-binding site.	INTRO
+219	239	antigen-binding site	site	Furthermore, studies of antibody sequences revealed that the total number of canonical structures are limited for each CDR, indicating possibly that antigen recognition may be affected by structural restrictions at the antigen-binding site.	INTRO
+29	37	CDR loop	structure_element	Later studies found that the CDR loop length is the primary determining factor of antigen-binding site topography because it is the primary factor for determining a canonical structure.	INTRO
+82	102	antigen-binding site	site	Later studies found that the CDR loop length is the primary determining factor of antigen-binding site topography because it is the primary factor for determining a canonical structure.	INTRO
+66	68	LC	structure_element	Additional efforts have led to our current understanding that the LC CDRs L1, L2, and L3 have preferred sets of canonical structures based on length and amino acid sequence composition.	INTRO
+69	73	CDRs	structure_element	Additional efforts have led to our current understanding that the LC CDRs L1, L2, and L3 have preferred sets of canonical structures based on length and amino acid sequence composition.	INTRO
+74	76	L1	structure_element	Additional efforts have led to our current understanding that the LC CDRs L1, L2, and L3 have preferred sets of canonical structures based on length and amino acid sequence composition.	INTRO
+78	80	L2	structure_element	Additional efforts have led to our current understanding that the LC CDRs L1, L2, and L3 have preferred sets of canonical structures based on length and amino acid sequence composition.	INTRO
+86	88	L3	structure_element	Additional efforts have led to our current understanding that the LC CDRs L1, L2, and L3 have preferred sets of canonical structures based on length and amino acid sequence composition.	INTRO
+43	45	H1	structure_element	This was also found to be the case for the H1 and H2 CDRs.	INTRO
+50	52	H2	structure_element	This was also found to be the case for the H1 and H2 CDRs.	INTRO
+53	57	CDRs	structure_element	This was also found to be the case for the H1 and H2 CDRs.	INTRO
+63	67	CDRs	structure_element	Classification schemes for the canonical structures of these 5 CDRs have emerged and evolved as the number of depositions in the Protein Data Bank of Fab fragments of antibodies grow.	INTRO
+150	153	Fab	structure_element	Classification schemes for the canonical structures of these 5 CDRs have emerged and evolved as the number of depositions in the Protein Data Bank of Fab fragments of antibodies grow.	INTRO
+167	177	antibodies	protein_type	Classification schemes for the canonical structures of these 5 CDRs have emerged and evolved as the number of depositions in the Protein Data Bank of Fab fragments of antibodies grow.	INTRO
+26	29	CDR	structure_element	Recently, a comprehensive CDR classification scheme was reported identifying 72 clusters of conformations observed in antibody structures.	INTRO
+118	126	antibody	protein_type	Recently, a comprehensive CDR classification scheme was reported identifying 72 clusters of conformations observed in antibody structures.	INTRO
+127	137	structures	evidence	Recently, a comprehensive CDR classification scheme was reported identifying 72 clusters of conformations observed in antibody structures.	INTRO
+42	45	CDR	structure_element	The knowledge and predictability of these CDR canonical structures have greatly advanced antibody modeling efforts.	INTRO
+56	66	structures	evidence	The knowledge and predictability of these CDR canonical structures have greatly advanced antibody modeling efforts.	INTRO
+89	97	antibody	protein_type	The knowledge and predictability of these CDR canonical structures have greatly advanced antibody modeling efforts.	INTRO
+15	19	CDRs	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+20	22	L1	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+24	26	L2	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+28	30	L3	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+32	34	H1	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+39	41	H2	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+56	66	structures	evidence	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+90	93	CDR	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+94	96	H3	structure_element	In contrast to CDRs L1, L2, L3, H1 and H2, no canonical structures have been observed for CDR H3, which is the most variable in length and amino acid sequence.	INTRO
+96	101	loops	structure_element	Some clustering of conformations was observed for the shortest lengths; however, for the longer loops, only the portions nearest the framework (torso, stem or anchor region) were found to have defined conformations.	INTRO
+133	142	framework	structure_element	Some clustering of conformations was observed for the shortest lengths; however, for the longer loops, only the portions nearest the framework (torso, stem or anchor region) were found to have defined conformations.	INTRO
+144	149	torso	structure_element	Some clustering of conformations was observed for the shortest lengths; however, for the longer loops, only the portions nearest the framework (torso, stem or anchor region) were found to have defined conformations.	INTRO
+151	155	stem	structure_element	Some clustering of conformations was observed for the shortest lengths; however, for the longer loops, only the portions nearest the framework (torso, stem or anchor region) were found to have defined conformations.	INTRO
+159	172	anchor region	structure_element	Some clustering of conformations was observed for the shortest lengths; however, for the longer loops, only the portions nearest the framework (torso, stem or anchor region) were found to have defined conformations.	INTRO
+7	19	torso region	structure_element	In the torso region, 2 primary groups could be identified, which led to sequence-based rules that can predict with some degree of reliability the conformation of the stem region.	INTRO
+166	177	stem region	structure_element	In the torso region, 2 primary groups could be identified, which led to sequence-based rules that can predict with some degree of reliability the conformation of the stem region.	INTRO
+5	11	kinked	protein_state	The “kinked” or “bulged” conformation is the most prevalent, but an “extended” or “non-bulged” conformation is also, but less frequently, observed.	INTRO
+17	23	bulged	protein_state	The “kinked” or “bulged” conformation is the most prevalent, but an “extended” or “non-bulged” conformation is also, but less frequently, observed.	INTRO
+69	77	extended	protein_state	The “kinked” or “bulged” conformation is the most prevalent, but an “extended” or “non-bulged” conformation is also, but less frequently, observed.	INTRO
+83	93	non-bulged	protein_state	The “kinked” or “bulged” conformation is the most prevalent, but an “extended” or “non-bulged” conformation is also, but less frequently, observed.	INTRO
+83	96	anchor region	structure_element	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+100	103	CDR	structure_element	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+104	106	H3	structure_element	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+162	165	CDR	structure_element	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+166	168	H3	structure_element	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+201	209	antibody	protein_type	The cataloging and development of the rules for predicting the conformation of the anchor region of CDR H3 continue to be refined, producing new insight into the CDR H3 conformations and new tools for antibody engineering.	INTRO
+8	16	antibody	protein_type	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+83	100	homology modeling	experimental_method	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+136	139	CDR	structure_element	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+150	160	structures	evidence	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+185	188	CDR	structure_element	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+189	191	H3	structure_element	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+225	233	antibody	protein_type	Current antibody modeling approaches take advantage of the most recent advances in homology modeling, the evolving understanding of the CDR canonical structures, the emerging rules for CDR H3 modeling and the growing body of antibody structural data available from the PDB.	INTRO
+7	36	antibody modeling assessments	experimental_method	Recent antibody modeling assessments show continued improvement in the quality of the models being generated by a variety of modeling methods.	INTRO
+9	17	antibody	protein_type	Although antibody modeling is improving, the latest assessment revealed a number of challenges that need to be overcome to provide accurate 3-dimensional models of antibody V regions, including accuracies in the modeling of CDR H3.	INTRO
+164	172	antibody	protein_type	Although antibody modeling is improving, the latest assessment revealed a number of challenges that need to be overcome to provide accurate 3-dimensional models of antibody V regions, including accuracies in the modeling of CDR H3.	INTRO
+173	182	V regions	structure_element	Although antibody modeling is improving, the latest assessment revealed a number of challenges that need to be overcome to provide accurate 3-dimensional models of antibody V regions, including accuracies in the modeling of CDR H3.	INTRO
+224	227	CDR	structure_element	Although antibody modeling is improving, the latest assessment revealed a number of challenges that need to be overcome to provide accurate 3-dimensional models of antibody V regions, including accuracies in the modeling of CDR H3.	INTRO
+228	230	H3	structure_element	Although antibody modeling is improving, the latest assessment revealed a number of challenges that need to be overcome to provide accurate 3-dimensional models of antibody V regions, including accuracies in the modeling of CDR H3.	INTRO
+137	145	antibody	protein_type	The need for improvement in this area was also highlighted in a recent study reporting an approach and results that may influence future antibody modeling efforts.	INTRO
+29	58	antibody modeling assessments	experimental_method	One important finding of the antibody modeling assessments was that errors in the structural templates that are used as the basis for homology models can propagate into the final models, producing inaccuracies that may negatively influence the predictive nature of the V region model.	INTRO
+134	149	homology models	experimental_method	One important finding of the antibody modeling assessments was that errors in the structural templates that are used as the basis for homology models can propagate into the final models, producing inaccuracies that may negatively influence the predictive nature of the V region model.	INTRO
+269	277	V region	structure_element	One important finding of the antibody modeling assessments was that errors in the structural templates that are used as the basis for homology models can propagate into the final models, producing inaccuracies that may negatively influence the predictive nature of the V region model.	INTRO
+11	19	antibody	protein_type	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+71	84	phage library	experimental_method	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+180	185	human	species	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+196	199	IGV	structure_element	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+204	207	IGJ	structure_element	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+234	257	antigen combining sites	site	To support antibody engineering and therapeutic development efforts, a phage library was designed and constructed based on a limited number of scaffolds built with frequently used human germ-line IGV and IGJ gene segments that encode antigen combining sites suitable for recognition of peptides and proteins.	INTRO
+5	8	Fab	structure_element	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+34	36	HC	structure_element	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+48	56	IGHV1-69	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+58	63	H1-69	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+66	74	IGHV3-23	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+76	81	H3-23	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+87	95	IGHV5-51	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+96	101	H5-51	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+110	112	LC	structure_element	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+128	129	κ	structure_element	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+132	140	IGKV1-39	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+142	147	L1-39	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+150	158	IGKV3-11	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+160	165	L3-11	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+168	176	IGKV3-20	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+178	183	L3-20	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+189	196	IGKV4-1	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+198	202	L4-1	mutant	This Fab library is composed of 3 HC germlines, IGHV1-69 (H1-69), IGHV3-23 (H3-23) and IGHV5-51(H5-51), and 4 LC germlines (all κ), IGKV1-39 (L1-39), IGKV3-11 (L3-11), IGKV3-20 (L3-20) and IGKV4-1 (L4-1).	INTRO
+98	108	structures	evidence	Selection of these genes was based on the high frequency of their use and their cognate canonical structures that were found binding to peptides and proteins, as well as their ability to be expressed in bacteria and displayed on filamentous phage.	INTRO
+190	211	expressed in bacteria	experimental_method	Selection of these genes was based on the high frequency of their use and their cognate canonical structures that were found binding to peptides and proteins, as well as their ability to be expressed in bacteria and displayed on filamentous phage.	INTRO
+216	246	displayed on filamentous phage	experimental_method	Selection of these genes was based on the high frequency of their use and their cognate canonical structures that were found binding to peptides and proteins, as well as their ability to be expressed in bacteria and displayed on filamentous phage.	INTRO
+70	75	human	species	The implementation of the library involves the diversification of the human germline genes to mimic that found in natural human libraries.	INTRO
+122	127	human	species	The implementation of the library involves the diversification of the human germline genes to mimic that found in natural human libraries.	INTRO
+4	36	crystal structure determinations	experimental_method	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+41	60	structural analyses	experimental_method	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+77	81	Fabs	structure_element	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+128	138	structures	evidence	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+151	153	HC	structure_element	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+164	172	IGHV3-53	mutant	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+174	179	H3-53	mutant	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+200	203	LCs	structure_element	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+252	260	antibody	protein_type	The crystal structure determinations and structural analyses of all germline Fabs in the library described above along with the structures of a fourth HC germline, IGHV3-53 (H3-53), paired with the 4 LCs of the library have been carried out to support antibody therapeutic development.	INTRO
+7	10	HCs	structure_element	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+18	22	Fabs	structure_element	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+37	40	CDR	structure_element	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+41	43	H3	structure_element	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+76	79	Fab	structure_element	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+80	89	structure	evidence	All 16 HCs of the Fabs have the same CDR H3 that was reported in an earlier Fab structure.	INTRO
+47	49	VH	structure_element	This is the first systematic study of the same VH and VL structures in the context of different pairings.	INTRO
+54	56	VL	structure_element	This is the first systematic study of the same VH and VL structures in the context of different pairings.	INTRO
+57	67	structures	evidence	This is the first systematic study of the same VH and VL structures in the context of different pairings.	INTRO
+58	68	structures	evidence	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+80	90	structures	evidence	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+98	100	L1	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+102	104	L2	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+106	108	L3	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+110	112	H1	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+117	119	H2	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+120	124	CDRs	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+130	140	structures	evidence	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+148	151	CDR	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+152	155	H3s	structure_element	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+165	191	VH:VL packing interactions	site	The structure analyses include comparisons of the overall structures, canonical structures of the L1, L2, L3, H1 and H2 CDRs, the structures of all CDR H3s, and the VH:VL packing interactions.	INTRO
+4	14	structures	evidence	The structures and their analyses provide a foundation for future antibody engineering and structure determination efforts.	INTRO
+66	74	antibody	protein_type	The structures and their analyses provide a foundation for future antibody engineering and structure determination efforts.	INTRO
+0	18	Crystal structures	evidence	Crystal structures	RESULTS
+0	12	Crystal data	evidence	Crystal data, X-ray data, and refinement statistics.	TABLE
+14	24	X-ray data	evidence	Crystal data, X-ray data, and refinement statistics.	TABLE
+30	51	refinement statistics	evidence	Crystal data, X-ray data, and refinement statistics.	TABLE
+12	24	Crystal data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+26	36	X-ray data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+42	63	refinement statistics	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+12	24	Crystal data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+26	36	X-ray data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+42	63	refinement statistics	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+12	24	Crystal data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+26	36	X-ray data	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+42	63	refinement statistics	evidence	(Continued) Crystal data, X-ray data, and refinement statistics.	TABLE
+4	22	crystal structures	evidence	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+28	44	germline library	experimental_method	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+60	64	Fabs	structure_element	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+90	93	HCs	structure_element	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+95	100	H1-69	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+102	107	H3-23	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+109	114	H3-53	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+119	124	H5-51	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+132	135	LCs	structure_element	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+137	142	L1-39	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+144	149	L3-11	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+151	156	L3-20	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+161	165	L4-1	mutant	The crystal structures of a germline library composed of 16 Fabs generated by combining 4 HCs (H1-69, H3-23, H3-53 and H5-51) and 4 LCs (L1-39, L3-11, L3-20 and L4-1) have been determined.	RESULTS
+4	7	Fab	structure_element	The Fab heavy and light chain sequences for the variants numbered according to Chothia are shown in Fig. S1.	RESULTS
+18	29	light chain	structure_element	The Fab heavy and light chain sequences for the variants numbered according to Chothia are shown in Fig. S1.	RESULTS
+19	22	HCs	structure_element	The four different HCs all have the same CDR H3 sequence, ARYDGIYGELDF.	RESULTS
+41	44	CDR	structure_element	The four different HCs all have the same CDR H3 sequence, ARYDGIYGELDF.	RESULTS
+45	47	H3	structure_element	The four different HCs all have the same CDR H3 sequence, ARYDGIYGELDF.	RESULTS
+58	70	ARYDGIYGELDF	structure_element	The four different HCs all have the same CDR H3 sequence, ARYDGIYGELDF.	RESULTS
+0	15	Crystallization	experimental_method	Crystallization of the 16 Fabs was previously reported.	RESULTS
+26	30	Fabs	structure_element	Crystallization of the 16 Fabs was previously reported.	RESULTS
+18	26	crystals	evidence	Three sets of the crystals were isomorphous with nearly identical unit cells (Table 1).	RESULTS
+18	29	H3-23:L3-11	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+34	44	H3-23:L4-1	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+61	72	H3-53:L1-39	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+74	85	H3-53:L3-11	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+90	101	H3-53:L3-20	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+120	131	H5-51:L1-39	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+133	144	H5-51:L3-11	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+149	160	H5-51:L3-20	complex_assembly	These include (1) H3-23:L3-11 and H3-23:L4-1 in P212121, (2) H3-53:L1-39, H3-53:L3-11 and H3-53:L3-20 in P6522, and (3) H5-51:L1-39, H5-51:L3-11 and H5-51:L3-20 in P212121.	RESULTS
+72	80	PEG 3350	chemical	Variations occur in the pH (buffer) and the additives, and, in group 3, PEG 3350 is the precipitant for one variants while ammonium sulfate is the precipitant for the other two.	RESULTS
+123	139	ammonium sulfate	chemical	Variations occur in the pH (buffer) and the additives, and, in group 3, PEG 3350 is the precipitant for one variants while ammonium sulfate is the precipitant for the other two.	RESULTS
+22	35	crystal forms	evidence	The similarity in the crystal forms is attributed in part to cross-seeding using the microseed matrix screening for groups 2 and 3.	RESULTS
+85	111	microseed matrix screening	experimental_method	The similarity in the crystal forms is attributed in part to cross-seeding using the microseed matrix screening for groups 2 and 3.	RESULTS
+4	22	crystal structures	evidence	The crystal structures of the 16 Fabs have been determined at resolutions ranging from 3.3 Å to 1.65 Å (Table 1).	RESULTS
+33	37	Fabs	structure_element	The crystal structures of the 16 Fabs have been determined at resolutions ranging from 3.3 Å to 1.65 Å (Table 1).	RESULTS
+14	17	Fab	structure_element	The number of Fab molecules in the crystallographic asymmetric unit varies from 1 (for 12 Fabs) to 2 (for 4 Fabs).	RESULTS
+90	94	Fabs	structure_element	The number of Fab molecules in the crystallographic asymmetric unit varies from 1 (for 12 Fabs) to 2 (for 4 Fabs).	RESULTS
+108	112	Fabs	structure_element	The number of Fab molecules in the crystallographic asymmetric unit varies from 1 (for 12 Fabs) to 2 (for 4 Fabs).	RESULTS
+12	22	structures	evidence	Overall the structures are fairly complete, and, as can be expected, the models for the higher resolution structures are more complete than those for the lower resolution structures (Table S1).	RESULTS
+106	116	structures	evidence	Overall the structures are fairly complete, and, as can be expected, the models for the higher resolution structures are more complete than those for the lower resolution structures (Table S1).	RESULTS
+171	181	structures	evidence	Overall the structures are fairly complete, and, as can be expected, the models for the higher resolution structures are more complete than those for the lower resolution structures (Table S1).	RESULTS
+16	19	HCs	structure_element	Invariably, the HCs have more disorder than the LCs.	RESULTS
+30	38	disorder	protein_state	Invariably, the HCs have more disorder than the LCs.	RESULTS
+48	51	LCs	structure_element	Invariably, the HCs have more disorder than the LCs.	RESULTS
+8	10	LC	structure_element	For the LC, the disorder is observed at 2 of the C-terminal residues with few exceptions.	RESULTS
+16	24	disorder	protein_state	For the LC, the disorder is observed at 2 of the C-terminal residues with few exceptions.	RESULTS
+58	60	LC	structure_element	Apart from the C-terminus, only a few surface residues in LC are disordered.	RESULTS
+65	75	disordered	protein_state	Apart from the C-terminus, only a few surface residues in LC are disordered.	RESULTS
+4	7	HCs	structure_element	The HCs feature the largest number of disordered residues, with the lower resolution structures having the most.	RESULTS
+38	48	disordered	protein_state	The HCs feature the largest number of disordered residues, with the lower resolution structures having the most.	RESULTS
+85	95	structures	evidence	The HCs feature the largest number of disordered residues, with the lower resolution structures having the most.	RESULTS
+53	63	disordered	protein_state	The C-terminal residues including the 6xHis tags are disordered in all 16 structures.	RESULTS
+74	84	structures	evidence	The C-terminal residues including the 6xHis tags are disordered in all 16 structures.	RESULTS
+93	103	structures	evidence	In addition to these, 2 primary disordered stretches of residues are observed in a number of structures (Table S1).	RESULTS
+17	21	loop	structure_element	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+45	54	β-strands	structure_element	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+62	77	constant domain	structure_element	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+86	90	Fabs	structure_element	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+98	109	H3-23:L1-39	complex_assembly	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+111	122	H3-23:L3-11	complex_assembly	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+127	138	H3-53:L1-39	complex_assembly	One involves the loop connecting the first 2 β-strands of the constant domain (in all Fabs except H3-23:L1-39, H3-23:L3-11 and H3-53:L1-39).	RESULTS
+24	27	CDR	structure_element	The other is located in CDR H3 (in H5-51:L3-11, H5-51:L3-20 and in one of 2 copies of H3-23:L4-1).	RESULTS
+28	30	H3	structure_element	The other is located in CDR H3 (in H5-51:L3-11, H5-51:L3-20 and in one of 2 copies of H3-23:L4-1).	RESULTS
+35	46	H5-51:L3-11	complex_assembly	The other is located in CDR H3 (in H5-51:L3-11, H5-51:L3-20 and in one of 2 copies of H3-23:L4-1).	RESULTS
+48	59	H5-51:L3-20	complex_assembly	The other is located in CDR H3 (in H5-51:L3-11, H5-51:L3-20 and in one of 2 copies of H3-23:L4-1).	RESULTS
+86	96	H3-23:L4-1	complex_assembly	The other is located in CDR H3 (in H5-51:L3-11, H5-51:L3-20 and in one of 2 copies of H3-23:L4-1).	RESULTS
+0	3	CDR	structure_element	CDR H1 and CDR H2 also show some degree of disorder, but to a lesser extent.	RESULTS
+4	6	H1	structure_element	CDR H1 and CDR H2 also show some degree of disorder, but to a lesser extent.	RESULTS
+11	14	CDR	structure_element	CDR H1 and CDR H2 also show some degree of disorder, but to a lesser extent.	RESULTS
+15	17	H2	structure_element	CDR H1 and CDR H2 also show some degree of disorder, but to a lesser extent.	RESULTS
+43	51	disorder	protein_state	CDR H1 and CDR H2 also show some degree of disorder, but to a lesser extent.	RESULTS
+0	3	CDR	structure_element	CDR canonical structures	RESULTS
+14	24	structures	evidence	CDR canonical structures	RESULTS
+8	11	CDR	structure_element	Several CDR definitions have evolved over decades of antibody research.	RESULTS
+53	61	antibody	protein_type	Several CDR definitions have evolved over decades of antibody research.	RESULTS
+41	44	CDR	structure_element	Depending on the focus of the study, the CDR boundaries differ slightly between various definitions.	RESULTS
+25	28	CDR	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+126	130	CDRs	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+131	133	H1	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+138	140	H3	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+169	172	Cys	residue_name	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+181	184	CDR	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+185	187	L2	structure_element	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+253	256	Tyr	residue_name	In this work, we use the CDR definition of North et al., which is similar to that of Martin with the following exceptions: 1) CDRs H1 and H3 begin immediately after the Cys; and 2) CDR L2 includes an additional residue at the N-terminal side, typically Tyr.	RESULTS
+0	3	CDR	structure_element	CDR H1	RESULTS
+4	6	H1	structure_element	CDR H1	RESULTS
+4	17	superposition	experimental_method	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+21	24	CDR	structure_element	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+25	27	H1	structure_element	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+46	51	HC:LC	complex_assembly	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+63	75	heavy chains	structure_element	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+81	86	H1-69	mutant	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+92	97	H3-23	mutant	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+103	108	H3-53	mutant	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+117	122	H5-51	mutant	The superposition of CDR H1 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+0	4	CDRs	structure_element	CDRs are defined using the Dunbrack convention [12].	TABLE
+32	35	Fab	structure_element	Assignments for 2 copies of the Fab in the asymmetric unit are given for 5 structures.	TABLE
+75	85	structures	evidence	Assignments for 2 copies of the Fab in the asymmetric unit are given for 5 structures.	TABLE
+23	27	CDRs	structure_element	No assignment (NA) for CDRs with missing residues.	TABLE
+9	12	HCs	structure_element	The four HCs feature CDR H1 of the same length, and their sequences are highly similar (Table 2).	RESULTS
+21	24	CDR	structure_element	The four HCs feature CDR H1 of the same length, and their sequences are highly similar (Table 2).	RESULTS
+25	27	H1	structure_element	The four HCs feature CDR H1 of the same length, and their sequences are highly similar (Table 2).	RESULTS
+4	7	CDR	structure_element	The CDR H1 backbone conformations for all variants for each of the HCs are shown in Fig. 1.	RESULTS
+8	10	H1	structure_element	The CDR H1 backbone conformations for all variants for each of the HCs are shown in Fig. 1.	RESULTS
+67	70	HCs	structure_element	The CDR H1 backbone conformations for all variants for each of the HCs are shown in Fig. 1.	RESULTS
+13	16	HCs	structure_element	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+18	23	H3-23	mutant	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+25	30	H3-53	mutant	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+35	40	H5-51	mutant	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+77	84	H1-13-1	mutant	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+155	158	Fab	structure_element	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+159	169	structures	evidence	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+190	201	rmsd values	evidence	Three of the HCs, H3-23, H3-53 and H5-51, have the same canonical structure, H1-13-1, and the backbone conformations are tightly clustered for each set of Fab structures as reflected in the rmsd values (Fig. 1B-D).	RESULTS
+31	36	H3-53	mutant	Some deviation is observed for H3-53, mostly due to H3-53:L4-1, which exhibits a significant degree of disorder in CDR H1.	RESULTS
+52	62	H3-53:L4-1	complex_assembly	Some deviation is observed for H3-53, mostly due to H3-53:L4-1, which exhibits a significant degree of disorder in CDR H1.	RESULTS
+115	118	CDR	structure_element	Some deviation is observed for H3-53, mostly due to H3-53:L4-1, which exhibits a significant degree of disorder in CDR H1.	RESULTS
+119	121	H1	structure_element	Some deviation is observed for H3-53, mostly due to H3-53:L4-1, which exhibits a significant degree of disorder in CDR H1.	RESULTS
+4	20	electron density	evidence	The electron density for the backbone is weak and discontinuous, and completely missing for several side chains.	RESULTS
+4	7	CDR	structure_element	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+8	10	H1	structure_element	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+11	21	structures	evidence	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+27	32	H1-69	mutant	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+83	93	structures	evidence	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+109	112	LCs	structure_element	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+144	147	Fab	structure_element	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+172	183	H1-69:L3-11	complex_assembly	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+188	199	H1-69:L3-20	complex_assembly	The CDR H1 structures with H1-69 shown in Fig. 1A are quite variable, both for the structures with different LCs and for the copies of the same Fab in the asymmetric unit, H1-69:L3-11 and H1-69:L3-20.	RESULTS
+24	27	Fab	structure_element	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+28	38	structures	evidence	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+69	79	structures	evidence	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+88	95	H1-13-1	mutant	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+97	104	H1-13-3	mutant	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+106	113	H1-13-4	mutant	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+115	122	H1-13-6	mutant	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+127	135	H1-13-10	mutant	In total, 6 independent Fab structures produce 5 different canonical structures, namely H1-13-1, H1-13-3, H1-13-4, H1-13-6 and H1-13-10.	RESULTS
+22	27	H1-69	mutant	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+101	104	Gly	residue_name	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+116	119	Phe	residue_name	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+123	126	Tyr	residue_name	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+139	141	27	residue_number	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+162	165	CDR	structure_element	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+166	168	H1	structure_element	A major difference of H1-69 from the other germlines in the experimental data set is the presence of Gly instead of Phe or Tyr at position 27 (residue 5 of 13 in CDR H1).	RESULTS
+0	7	Glycine	residue_name	Glycine introduces the possibility of a higher degree of conformational flexibility that undoubtedly translates to the differences observed, and contributes to the elevated thermal parameters for the atoms in the amino acid residues in this region.	RESULTS
+0	3	CDR	structure_element	CDR H2	RESULTS
+4	6	H2	structure_element	CDR H2	RESULTS
+4	17	superposition	experimental_method	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+21	24	CDR	structure_element	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+25	27	H2	structure_element	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+46	51	HC:LC	complex_assembly	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+63	75	heavy chains	structure_element	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+81	86	H1-69	mutant	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+92	97	H3-23	mutant	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+103	108	H3-53	mutant	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+117	122	H5-51	mutant	The superposition of CDR H2 backbones for all HC:LC pairs with heavy chains: (A) H1-69, (B) H3-23, (C) H3-53 and (D) H5-51.	FIG
+28	31	CDR	structure_element	The canonical structures of CDR H2 have fairly consistent conformations (Table 2, Fig. 2).	RESULTS
+32	34	H2	structure_element	The canonical structures of CDR H2 have fairly consistent conformations (Table 2, Fig. 2).	RESULTS
+14	17	HCs	structure_element	Each of the 4 HCs adopts only one canonical structure regardless of the pairing LC.	RESULTS
+80	82	LC	structure_element	Each of the 4 HCs adopts only one canonical structure regardless of the pairing LC.	RESULTS
+10	15	H1-69	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+20	25	H5-51	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+71	78	H2-10-1	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+80	85	H3-23	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+90	97	H2-10-2	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+103	108	H3-53	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+113	119	H2-9-3	mutant	Germlines H1-69 and H5-51 have the same canonical structure assignment H2-10-1, H3-23 has H2-10-2, and H3-53 has H2-9-3.	RESULTS
+35	38	CDR	structure_element	The conformations for all of these CDR H2s are tightly clustered (Fig. 2).	RESULTS
+39	42	H2s	structure_element	The conformations for all of these CDR H2s are tightly clustered (Fig. 2).	RESULTS
+27	30	Fab	structure_element	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+34	45	H1-69:L3-20	complex_assembly	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+47	50	CDR	structure_element	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+51	53	H2	structure_element	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+57	77	partially disordered	protein_state	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+79	85	Δ55-60	mutant	In one case, in the second Fab of H1-69:L3-20, CDR H2 is partially disordered (Δ55-60).	RESULTS
+37	40	CDR	structure_element	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+41	43	H2	structure_element	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+64	75	10 residues	residue_range	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+172	174	71	residue_number	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+194	197	CDR	structure_element	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+198	200	H4	structure_element	Although three of the germlines have CDR H2 of the same length, 10 residues, they adopt 2 distinctively different conformations depending mostly on the residue at position 71 from the so-called CDR H4.	RESULTS
+0	5	Arg71	residue_name_number	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+9	14	H3-23	mutant	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+39	43	CDRs	structure_element	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+44	46	H2	structure_element	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+51	53	H4	structure_element	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+98	101	CDR	structure_element	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+102	104	H2	structure_element	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+121	123	54	residue_number	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+145	165	antigen binding site	site	Arg71 in H3-23 fills the space between CDRs H2 and H4, and defines the conformation of the tip of CDR H2 so that residue 54 points away from the antigen binding site.	RESULTS
+10	15	H1-69	mutant	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+20	25	H5-51	mutant	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+44	49	human	species	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+74	77	Ala	residue_name	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+90	92	71	residue_number	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+122	123	H	structure_element	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+124	130	Pro52a	residue_name_number	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+154	157	CDR	structure_element	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+158	160	H4	structure_element	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+192	194	53	residue_number	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+199	201	54	residue_number	Germlines H1-69 and H5-51 are unique in the human repertoire in having an Ala at position 71 that leaves enough space for H-Pro52a to pack deeper against CDR H4 so that the following residues 53 and 54 point toward the putative antigen.	RESULTS
+17	20	CDR	structure_element	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+21	23	H2	structure_element	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+27	32	H1-69	mutant	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+37	42	H5-51	mutant	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+83	90	H2-10-1	mutant	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+135	145	structures	evidence	Conformations of CDR H2 in H1-69 and H5-51, both of which have canonical structure H2-10-1, show little deviation within each set of 4 structures.	RESULTS
+45	48	CDR	structure_element	However, there is a significant shift of the CDR as a rigid body when the 2 sets are superimposed.	RESULTS
+85	97	superimposed	experimental_method	However, there is a significant shift of the CDR as a rigid body when the 2 sets are superimposed.	RESULTS
+49	52	CDR	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+53	55	H2	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+61	64	CDR	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+65	67	H1	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+105	107	33	residue_number	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+129	132	CDR	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+133	135	H1	structure_element	Most likely this is the result of interaction of CDR H2 with CDR H1, namely with the residue at position 33 (residue 11 of 13 in CDR H1).	RESULTS
+9	14	H1-69	mutant	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+19	22	Ala	residue_name	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+35	37	33	residue_number	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+49	54	H5-51	mutant	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+64	66	33	residue_number	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+90	93	Trp	residue_name	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+116	117	H	structure_element	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+118	123	Tyr52	residue_name_number	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+135	138	CDR	structure_element	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+139	141	H2	structure_element	Germline H1-69 has Ala at position 33 whereas in H5-51 position 33 is occupied by a bulky Trp, which stacks against H-Tyr52 and drives CDR H2 away from the center.	RESULTS
+0	3	CDR	structure_element	CDR L1	RESULTS
+4	6	L1	structure_element	CDR L1	RESULTS
+4	17	superposition	experimental_method	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+21	24	CDR	structure_element	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+25	27	L1	structure_element	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+46	51	HC:LC	complex_assembly	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+63	75	light chains	structure_element	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+81	86	L1-39	mutant	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+92	97	L3-11	mutant	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+103	108	L3-20	mutant	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+117	121	L4-1	mutant	The superposition of CDR L1 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+9	11	LC	structure_element	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+12	16	CDRs	structure_element	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+17	19	L1	structure_element	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+49	51	11	residue_range	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+53	55	12	residue_range	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+60	62	17	residue_range	The four LC CDRs L1 feature 3 different lengths (11, 12 and 17 residues) having a total of 4 different canonical structure assignments.	RESULTS
+9	12	LCs	structure_element	Of these LCs, L1-39 and L3-11 have the same canonical structure, L1-11-1, and superimpose very well (Fig. 3A, B).	RESULTS
+14	19	L1-39	mutant	Of these LCs, L1-39 and L3-11 have the same canonical structure, L1-11-1, and superimpose very well (Fig. 3A, B).	RESULTS
+24	29	L3-11	mutant	Of these LCs, L1-39 and L3-11 have the same canonical structure, L1-11-1, and superimpose very well (Fig. 3A, B).	RESULTS
+65	72	L1-11-1	mutant	Of these LCs, L1-39 and L3-11 have the same canonical structure, L1-11-1, and superimpose very well (Fig. 3A, B).	RESULTS
+78	89	superimpose	experimental_method	Of these LCs, L1-39 and L3-11 have the same canonical structure, L1-11-1, and superimpose very well (Fig. 3A, B).	RESULTS
+21	26	L3-20	mutant	For the remaining 2, L3-20 has 2 different assignments, L1-12-1 and L1-12-2, while L4-1 has a single assignment, L1-17-1.	RESULTS
+56	63	L1-12-1	mutant	For the remaining 2, L3-20 has 2 different assignments, L1-12-1 and L1-12-2, while L4-1 has a single assignment, L1-17-1.	RESULTS
+68	75	L1-12-2	mutant	For the remaining 2, L3-20 has 2 different assignments, L1-12-1 and L1-12-2, while L4-1 has a single assignment, L1-17-1.	RESULTS
+83	87	L4-1	mutant	For the remaining 2, L3-20 has 2 different assignments, L1-12-1 and L1-12-2, while L4-1 has a single assignment, L1-17-1.	RESULTS
+113	120	L1-17-1	mutant	For the remaining 2, L3-20 has 2 different assignments, L1-12-1 and L1-12-2, while L4-1 has a single assignment, L1-17-1.	RESULTS
+0	4	L4-1	mutant	L4-1 has the longest CDR L1, composed of 17 amino acid residues (Fig. 3D).	RESULTS
+21	24	CDR	structure_element	L4-1 has the longest CDR L1, composed of 17 amino acid residues (Fig. 3D).	RESULTS
+25	27	L1	structure_element	L4-1 has the longest CDR L1, composed of 17 amino acid residues (Fig. 3D).	RESULTS
+41	63	17 amino acid residues	residue_range	L4-1 has the longest CDR L1, composed of 17 amino acid residues (Fig. 3D).	RESULTS
+55	59	rmsd	evidence	Despite this, the conformations are tightly clustered (rmsd is 0.20 Å).	RESULTS
+34	46	stem regions	structure_element	The backbone conformations of the stem regions superimpose well.	RESULTS
+52	55	30a	residue_number	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+60	63	30f	residue_number	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+74	75	8	residue_number	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+80	82	13	residue_number	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+86	88	17	residue_number	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+92	95	CDR	structure_element	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+96	98	L1	structure_element	Some changes in conformation occur between residues 30a and 30f (residues 8 and 13 of 17 in CDR L1).	RESULTS
+23	34	loop region	structure_element	This is the tip of the loop region, which appears to have similar conformations that fan out the structures because of the slight differences in torsion angles in the backbone near Tyr30a and Lys30f.	RESULTS
+97	107	structures	evidence	This is the tip of the loop region, which appears to have similar conformations that fan out the structures because of the slight differences in torsion angles in the backbone near Tyr30a and Lys30f.	RESULTS
+181	187	Tyr30a	residue_name_number	This is the tip of the loop region, which appears to have similar conformations that fan out the structures because of the slight differences in torsion angles in the backbone near Tyr30a and Lys30f.	RESULTS
+192	198	Lys30f	residue_name_number	This is the tip of the loop region, which appears to have similar conformations that fan out the structures because of the slight differences in torsion angles in the backbone near Tyr30a and Lys30f.	RESULTS
+0	5	L3-20	mutant	L3-20 is the most variable in CDR L1 among the 4 germlines as indicated by an rmsd of 0.54 Å (Fig. 3C).	RESULTS
+30	33	CDR	structure_element	L3-20 is the most variable in CDR L1 among the 4 germlines as indicated by an rmsd of 0.54 Å (Fig. 3C).	RESULTS
+34	36	L1	structure_element	L3-20 is the most variable in CDR L1 among the 4 germlines as indicated by an rmsd of 0.54 Å (Fig. 3C).	RESULTS
+78	82	rmsd	evidence	L3-20 is the most variable in CDR L1 among the 4 germlines as indicated by an rmsd of 0.54 Å (Fig. 3C).	RESULTS
+4	14	structures	evidence	Two structures, H3-53:L3-20 and H5-51:L3-20 are assigned to canonical structure L1-12-1 with virtually identical backbone conformations.	RESULTS
+16	27	H3-53:L3-20	complex_assembly	Two structures, H3-53:L3-20 and H5-51:L3-20 are assigned to canonical structure L1-12-1 with virtually identical backbone conformations.	RESULTS
+32	43	H5-51:L3-20	complex_assembly	Two structures, H3-53:L3-20 and H5-51:L3-20 are assigned to canonical structure L1-12-1 with virtually identical backbone conformations.	RESULTS
+80	87	L1-12-1	mutant	Two structures, H3-53:L3-20 and H5-51:L3-20 are assigned to canonical structure L1-12-1 with virtually identical backbone conformations.	RESULTS
+21	32	H3-23:L3-20	complex_assembly	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+38	41	CDR	structure_element	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+42	44	L1	structure_element	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+48	55	L1-12-2	mutant	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+77	84	L1-12-1	mutant	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+97	102	29-32	residue_range	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+155	165	11-residue	residue_range	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+166	169	CDR	structure_element	The third structure, H3-23:L3-20, has CDR L1 as L1-12-2, which deviates from L1-12-1 at residues 29-32, i.e., at the site of insertion with respect to the 11-residue CDR.	RESULTS
+30	41	H1-69:L3-20	complex_assembly	The fourth member of the set, H1-69:L3-20, was crystallized with 2 Fabs in the asymmetric unit.	RESULTS
+47	59	crystallized	experimental_method	The fourth member of the set, H1-69:L3-20, was crystallized with 2 Fabs in the asymmetric unit.	RESULTS
+67	71	Fabs	structure_element	The fourth member of the set, H1-69:L3-20, was crystallized with 2 Fabs in the asymmetric unit.	RESULTS
+20	23	CDR	structure_element	The conformation of CDR L1 in these 2 Fabs is slightly different, and both conformations fall somewhere between L1-12-1 and L1-12-2.	RESULTS
+24	26	L1	structure_element	The conformation of CDR L1 in these 2 Fabs is slightly different, and both conformations fall somewhere between L1-12-1 and L1-12-2.	RESULTS
+38	42	Fabs	structure_element	The conformation of CDR L1 in these 2 Fabs is slightly different, and both conformations fall somewhere between L1-12-1 and L1-12-2.	RESULTS
+112	119	L1-12-1	mutant	The conformation of CDR L1 in these 2 Fabs is slightly different, and both conformations fall somewhere between L1-12-1 and L1-12-2.	RESULTS
+124	131	L1-12-2	mutant	The conformation of CDR L1 in these 2 Fabs is slightly different, and both conformations fall somewhere between L1-12-1 and L1-12-2.	RESULTS
+42	51	structure	evidence	This reflects the lack of accuracy in the structure due to low resolution of the X-ray data (3.3 Å).	RESULTS
+81	91	X-ray data	evidence	This reflects the lack of accuracy in the structure due to low resolution of the X-ray data (3.3 Å).	RESULTS
+0	3	CDR	structure_element	CDR L2	RESULTS
+4	6	L2	structure_element	CDR L2	RESULTS
+4	17	superposition	experimental_method	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+21	24	CDR	structure_element	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+25	27	L2	structure_element	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+46	51	HC:LC	complex_assembly	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+63	75	light chains	structure_element	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+81	86	L1-39	mutant	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+92	97	L3-11	mutant	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+103	108	L3-20	mutant	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+117	121	L4-1	mutant	The superposition of CDR L2 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+9	12	LCs	structure_element	All four LCs have CDR L2 of the same length and canonical structure, L2-8-1 (Table 2).	RESULTS
+18	21	CDR	structure_element	All four LCs have CDR L2 of the same length and canonical structure, L2-8-1 (Table 2).	RESULTS
+22	24	L2	structure_element	All four LCs have CDR L2 of the same length and canonical structure, L2-8-1 (Table 2).	RESULTS
+69	75	L2-8-1	mutant	All four LCs have CDR L2 of the same length and canonical structure, L2-8-1 (Table 2).	RESULTS
+4	7	CDR	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+8	10	L2	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+41	44	LCs	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+63	66	HCs	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+116	120	CDRs	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+122	126	rmsd	evidence	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+255	259	loop	structure_element	The CDR L2 conformations for each of the LCs paired with the 4 HCs are clustered more tightly than any of the other CDRs (rmsd values are in the range 0.09-0.16 Å), and all 4 sets have virtually the same conformation despite the sequence diversity of the loop.	RESULTS
+0	3	CDR	structure_element	CDR L3	RESULTS
+4	6	L3	structure_element	CDR L3	RESULTS
+4	17	superposition	experimental_method	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+21	24	CDR	structure_element	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+25	27	L3	structure_element	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+46	51	HC:LC	complex_assembly	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+63	75	light chains	structure_element	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+81	86	L1-39	mutant	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+92	97	L3-11	mutant	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+103	108	L3-20	mutant	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+117	121	L4-1	mutant	The superposition of CDR L3 backbones for all HC:LC pairs with light chains: (A) L1-39, (B) L3-11, (C) L3-20 and (D) L4-1.	FIG
+8	11	CDR	structure_element	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+12	14	L2	structure_element	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+22	25	LCs	structure_element	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+31	34	CDR	structure_element	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+35	37	L3	structure_element	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+71	80	structure	evidence	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+82	93	L3-9-cis7-1	mutant	As with CDR L2, all 4 LCs have CDR L3 of the same length and canonical structure, L3-9-cis7-1 (Table 2).	RESULTS
+21	24	CDR	structure_element	The conformations of CDR L3 for L1-39, L3-11, and particularly for L320, are not as tightly clustered as those of L4-1 (Fig. 5).	RESULTS
+25	27	L3	structure_element	The conformations of CDR L3 for L1-39, L3-11, and particularly for L320, are not as tightly clustered as those of L4-1 (Fig. 5).	RESULTS
+32	37	L1-39	mutant	The conformations of CDR L3 for L1-39, L3-11, and particularly for L320, are not as tightly clustered as those of L4-1 (Fig. 5).	RESULTS
+39	44	L3-11	mutant	The conformations of CDR L3 for L1-39, L3-11, and particularly for L320, are not as tightly clustered as those of L4-1 (Fig. 5).	RESULTS
+114	118	L4-1	mutant	The conformations of CDR L3 for L1-39, L3-11, and particularly for L320, are not as tightly clustered as those of L4-1 (Fig. 5).	RESULTS
+82	87	90-92	residue_range	The slight conformational variability occurs in the region of amino acid residues 90-92, which is in contact with CDR H3.	RESULTS
+114	117	CDR	structure_element	The slight conformational variability occurs in the region of amino acid residues 90-92, which is in contact with CDR H3.	RESULTS
+118	120	H3	structure_element	The slight conformational variability occurs in the region of amino acid residues 90-92, which is in contact with CDR H3.	RESULTS
+0	3	CDR	structure_element	CDR H3 conformational diversity	RESULTS
+4	6	H3	structure_element	CDR H3 conformational diversity	RESULTS
+29	33	Fabs	structure_element	As mentioned earlier, all 16 Fabs have the same CDR H3, for which the amino acid sequence is derived from the anti-CCL2 antibody CNTO 888.	RESULTS
+48	51	CDR	structure_element	As mentioned earlier, all 16 Fabs have the same CDR H3, for which the amino acid sequence is derived from the anti-CCL2 antibody CNTO 888.	RESULTS
+52	54	H3	structure_element	As mentioned earlier, all 16 Fabs have the same CDR H3, for which the amino acid sequence is derived from the anti-CCL2 antibody CNTO 888.	RESULTS
+120	128	antibody	protein_type	As mentioned earlier, all 16 Fabs have the same CDR H3, for which the amino acid sequence is derived from the anti-CCL2 antibody CNTO 888.	RESULTS
+129	137	CNTO 888	chemical	As mentioned earlier, all 16 Fabs have the same CDR H3, for which the amino acid sequence is derived from the anti-CCL2 antibody CNTO 888.	RESULTS
+4	8	loop	structure_element	The loop and the 2 β-strands of the CDR H3 in this ‘parent’ structure are stabilized by H-bonds between the carbonyl oxygen and peptide nitrogen atoms in the 2 strands.	RESULTS
+19	28	β-strands	structure_element	The loop and the 2 β-strands of the CDR H3 in this ‘parent’ structure are stabilized by H-bonds between the carbonyl oxygen and peptide nitrogen atoms in the 2 strands.	RESULTS
+36	39	CDR	structure_element	The loop and the 2 β-strands of the CDR H3 in this ‘parent’ structure are stabilized by H-bonds between the carbonyl oxygen and peptide nitrogen atoms in the 2 strands.	RESULTS
+40	42	H3	structure_element	The loop and the 2 β-strands of the CDR H3 in this ‘parent’ structure are stabilized by H-bonds between the carbonyl oxygen and peptide nitrogen atoms in the 2 strands.	RESULTS
+60	69	structure	evidence	The loop and the 2 β-strands of the CDR H3 in this ‘parent’ structure are stabilized by H-bonds between the carbonyl oxygen and peptide nitrogen atoms in the 2 strands.	RESULTS
+32	35	CDR	structure_element	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+36	38	H3	structure_element	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+39	49	structures	evidence	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+71	76	water	chemical	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+167	171	loop	structure_element	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+189	198	β-strands	structure_element	An interesting feature of these CDR H3 structures is the presence of a water molecule that interacts with the peptide nitrogens and carbonyl oxygens near the bridging loop connecting the 2 β-strands.	RESULTS
+5	10	water	chemical	This water is present in both the bound (4DN4) and unbound (4DN3) forms of CNTO 888.	RESULTS
+34	39	bound	protein_state	This water is present in both the bound (4DN4) and unbound (4DN3) forms of CNTO 888.	RESULTS
+51	58	unbound	protein_state	This water is present in both the bound (4DN4) and unbound (4DN3) forms of CNTO 888.	RESULTS
+75	83	CNTO 888	chemical	This water is present in both the bound (4DN4) and unbound (4DN3) forms of CNTO 888.	RESULTS
+4	15	stem region	structure_element	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+19	22	CDR	structure_element	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+23	25	H3	structure_element	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+42	45	Fab	structure_element	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+55	61	kinked	protein_state	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+109	115	Trp103	residue_name_number	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+166	173	Leu100b	residue_name_number	The stem region of CDR H3 in the parental Fab is in a ‘kinked’ conformation, in which the indole nitrogen of Trp103 forms a hydrogen bond with the carbonyl oxygen of Leu100b.	RESULTS
+22	28	Asp101	residue_name_number	The carboxyl group of Asp101 forms a salt bridge with Arg94.	RESULTS
+54	59	Arg94	residue_name_number	The carboxyl group of Asp101 forms a salt bridge with Arg94.	RESULTS
+34	47	superposition	experimental_method	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+55	58	CDR	structure_element	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+59	62	H3s	structure_element	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+70	80	structures	evidence	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+120	123	CDR	structure_element	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+124	127	H3s	structure_element	Ribbon representations of (A) the superposition of all CDR H3s of the structures with complete backbone traces. (B) The CDR H3s rotated 90° about the y axis of the page.	FIG
+4	13	structure	evidence	The structure of each CDR H3 is represented with a different color.	FIG
+22	25	CDR	structure_element	The structure of each CDR H3 is represented with a different color.	FIG
+26	28	H3	structure_element	The structure of each CDR H3 is represented with a different color.	FIG
+61	64	CDR	structure_element	Despite having the same amino acid sequence in all variants, CDR H3 has the highest degree of structural diversity and disorder of all of the CDRs in the experimental set.	RESULTS
+65	67	H3	structure_element	Despite having the same amino acid sequence in all variants, CDR H3 has the highest degree of structural diversity and disorder of all of the CDRs in the experimental set.	RESULTS
+142	146	CDRs	structure_element	Despite having the same amino acid sequence in all variants, CDR H3 has the highest degree of structural diversity and disorder of all of the CDRs in the experimental set.	RESULTS
+16	19	Fab	structure_element	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+20	30	structures	evidence	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+83	94	H5-51:L3-11	complex_assembly	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+96	106	H551:L3-20	complex_assembly	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+111	121	H3-23:L4-1	complex_assembly	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+136	140	Fabs	structure_element	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+148	155	missing	protein_state	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+157	167	disordered	protein_state	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+197	205	CDR loop	structure_element	Three of the 21 Fab structures (including multiple copies in the asymmetric unit), H5-51:L3-11, H551:L3-20 and H3-23:L4-1 (one of the 2 Fabs), have missing (disordered) residues at the apex of the CDR loop.	RESULTS
+20	24	Fabs	structure_element	Another four of the Fabs, H3-23:L1-39, H3-53:L1-39, H3-53:L3-11 and H3-53:L4-1 have missing side-chain atoms.	RESULTS
+26	37	H3-23:L1-39	complex_assembly	Another four of the Fabs, H3-23:L1-39, H3-53:L1-39, H3-53:L3-11 and H3-53:L4-1 have missing side-chain atoms.	RESULTS
+39	50	H3-53:L1-39	complex_assembly	Another four of the Fabs, H3-23:L1-39, H3-53:L1-39, H3-53:L3-11 and H3-53:L4-1 have missing side-chain atoms.	RESULTS
+52	63	H3-53:L3-11	complex_assembly	Another four of the Fabs, H3-23:L1-39, H3-53:L1-39, H3-53:L3-11 and H3-53:L4-1 have missing side-chain atoms.	RESULTS
+68	78	H3-53:L4-1	complex_assembly	Another four of the Fabs, H3-23:L1-39, H3-53:L1-39, H3-53:L3-11 and H3-53:L4-1 have missing side-chain atoms.	RESULTS
+18	21	CDR	structure_element	The variations in CDR H3 conformation are illustrated in Fig. 6 for the 18 Fab structures that have ordered backbone atoms.	RESULTS
+22	24	H3	structure_element	The variations in CDR H3 conformation are illustrated in Fig. 6 for the 18 Fab structures that have ordered backbone atoms.	RESULTS
+75	78	Fab	structure_element	The variations in CDR H3 conformation are illustrated in Fig. 6 for the 18 Fab structures that have ordered backbone atoms.	RESULTS
+79	89	structures	evidence	The variations in CDR H3 conformation are illustrated in Fig. 6 for the 18 Fab structures that have ordered backbone atoms.	RESULTS
+40	46	kinked	protein_state	A comparison of representatives of the “kinked” and “extended” structures.	FIG
+53	61	extended	protein_state	A comparison of representatives of the “kinked” and “extended” structures.	FIG
+63	73	structures	evidence	A comparison of representatives of the “kinked” and “extended” structures.	FIG
+9	15	kinked	protein_state	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+17	20	CDR	structure_element	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+21	23	H3	structure_element	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+27	38	H1-69:L3-11	complex_assembly	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+120	127	Leu100b	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+134	140	Trp103	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+146	151	Arg94	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+159	165	Asp101	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+175	180	Arg94	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+189	195	Asp101	residue_name_number	(A) The “kinked” CDR H3 of H1-69:L3-11 with purple carbon atoms and yellow dashed lines connecting the H-bond pairs for Leu100b O and Trp103 NE1, Arg94 NE and Asp101 OD1, and Arg94 NH2 and Asp101 OD2.	FIG
+9	17	extended	protein_state	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+19	22	CDR	structure_element	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+23	25	H3	structure_element	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+29	40	H1-69:L3-20	complex_assembly	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+121	127	Asp101	residue_name_number	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+144	150	Trp103	residue_name_number	(B) The “extended” CDR H3 of H1-69:L3-20 with green carbon atoms and yellow dashed lines connecting the H-bond pairs for Asp101 OD1 and OD2 and Trp103 NE1.	FIG
+16	19	Fab	structure_element	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+20	30	structures	evidence	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+32	43	H1-69:L1-39	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+45	56	H1-69:L3-11	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+60	64	Fabs	structure_element	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+67	77	H1-69:L4-1	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+79	90	H3-23:L3-11	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+94	98	Fabs	structure_element	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+101	112	H3-23:L3-20	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+114	125	H3-53:L3-11	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+127	138	H3-53:L3-20	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+143	154	H5-51:L1-39	complex_assembly	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+160	164	CDRs	structure_element	In 10 of the 18 Fab structures, H1-69:L1-39, H1-69:L3-11 (2 Fabs), H1-69:L4-1, H3-23:L3-11 (2 Fabs), H3-23:L3-20, H3-53:L3-11, H3-53:L3-20 and H5-51:L1-39, the CDRs have similar conformations to that found in 4DN3.	RESULTS
+19	29	structures	evidence	The bases of these structures have the ‘kinked’ conformation with the H-bond between Trp103 and Leu100b.	RESULTS
+40	46	kinked	protein_state	The bases of these structures have the ‘kinked’ conformation with the H-bond between Trp103 and Leu100b.	RESULTS
+85	91	Trp103	residue_name_number	The bases of these structures have the ‘kinked’ conformation with the H-bond between Trp103 and Leu100b.	RESULTS
+96	103	Leu100b	residue_name_number	The bases of these structures have the ‘kinked’ conformation with the H-bond between Trp103 and Leu100b.	RESULTS
+17	20	CDR	structure_element	A representative CDR H3 structure for H1-69:L1-39 illustrating this is shown in Fig. 7A.	RESULTS
+21	23	H3	structure_element	A representative CDR H3 structure for H1-69:L1-39 illustrating this is shown in Fig. 7A.	RESULTS
+24	33	structure	evidence	A representative CDR H3 structure for H1-69:L1-39 illustrating this is shown in Fig. 7A.	RESULTS
+38	49	H1-69:L1-39	complex_assembly	A representative CDR H3 structure for H1-69:L1-39 illustrating this is shown in Fig. 7A.	RESULTS
+64	69	Tyr99	residue_name_number	The largest backbone conformational deviation for the set is at Tyr99, where the C=O is rotated by 90° relative to that observed in 4DN3.	RESULTS
+48	58	structures	evidence	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+60	70	H1-69:L4-1	complex_assembly	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+80	89	conserved	protein_state	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+90	95	water	chemical	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+108	111	CDR	structure_element	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+112	114	H3	structure_element	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+145	155	structures	evidence	Also, it is worth noting that only one of these structures, H1-69:L4-1, has the conserved water molecule in CDR H3 observed in the 4DN3 and 4DN4 structures.	RESULTS
+24	27	Fab	structure_element	In fact, it is the only Fab in the set that has a water molecule present at this site.	RESULTS
+50	55	water	chemical	In fact, it is the only Fab in the set that has a water molecule present at this site.	RESULTS
+4	7	CDR	structure_element	The CDR H3 for this structure is shown in Fig. S3.	RESULTS
+8	10	H3	structure_element	The CDR H3 for this structure is shown in Fig. S3.	RESULTS
+20	29	structure	evidence	The CDR H3 for this structure is shown in Fig. S3.	RESULTS
+16	20	Fabs	structure_element	The remaining 8 Fabs can be grouped into 5 different conformational classes.	RESULTS
+13	17	Fabs	structure_element	Three of the Fabs, H3-23:L1-39, H3-23:L4-1 and H3-53:L1-39, have distinctive conformations.	RESULTS
+19	30	H3-23:L1-39	complex_assembly	Three of the Fabs, H3-23:L1-39, H3-23:L4-1 and H3-53:L1-39, have distinctive conformations.	RESULTS
+32	42	H3-23:L4-1	complex_assembly	Three of the Fabs, H3-23:L1-39, H3-23:L4-1 and H3-53:L1-39, have distinctive conformations.	RESULTS
+47	58	H3-53:L1-39	complex_assembly	Three of the Fabs, H3-23:L1-39, H3-23:L4-1 and H3-53:L1-39, have distinctive conformations.	RESULTS
+4	16	stem regions	structure_element	The stem regions in these 3 cases are in the ‘kinked’ conformation consistent with that observed for 4DN3.	RESULTS
+46	52	kinked	protein_state	The stem regions in these 3 cases are in the ‘kinked’ conformation consistent with that observed for 4DN3.	RESULTS
+19	23	Fabs	structure_element	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+25	35	H5-51:L4-1	complex_assembly	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+48	59	H1-69:L3-20	complex_assembly	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+75	85	H3-53:L4-1	complex_assembly	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+104	107	CDR	structure_element	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+108	110	H3	structure_element	The five remaining Fabs, H5-51:L4-1 (2 copies), H1-69:L3-20 (2 copies) and H3-53:L4-1, have 3 different CDR H3 conformations (Fig. S4).	RESULTS
+4	16	stem regions	structure_element	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+20	23	CDR	structure_element	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+24	26	H3	structure_element	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+35	45	H5-51:L4-1	complex_assembly	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+46	50	Fabs	structure_element	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+63	69	kinked	protein_state	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+118	129	H1-69:L3-20	complex_assembly	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+139	149	H3-53:L4-1	complex_assembly	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+162	170	extended	protein_state	The stem regions of CDR H3 for the H5-51:L4-1 Fabs are in the ‘kinked’ conformation while, surprisingly, those of the H1-69:L3-20 pair and H3-53:L4-1 are in the ‘extended’ conformation (Fig. 7B).	RESULTS
+0	5	VH:VL	complex_assembly	VH:VL domain packing	RESULTS
+4	6	VH	structure_element	The VH and VL domains have a β-sandwich structure (also often referred as a Greek key motif) and each is composed of a 4-stranded and a 5-stranded antiparallel β-sheets.	RESULTS
+11	13	VL	structure_element	The VH and VL domains have a β-sandwich structure (also often referred as a Greek key motif) and each is composed of a 4-stranded and a 5-stranded antiparallel β-sheets.	RESULTS
+29	49	β-sandwich structure	structure_element	The VH and VL domains have a β-sandwich structure (also often referred as a Greek key motif) and each is composed of a 4-stranded and a 5-stranded antiparallel β-sheets.	RESULTS
+76	91	Greek key motif	structure_element	The VH and VL domains have a β-sandwich structure (also often referred as a Greek key motif) and each is composed of a 4-stranded and a 5-stranded antiparallel β-sheets.	RESULTS
+119	168	4-stranded and a 5-stranded antiparallel β-sheets	structure_element	The VH and VL domains have a β-sandwich structure (also often referred as a Greek key motif) and each is composed of a 4-stranded and a 5-stranded antiparallel β-sheets.	RESULTS
+44	63	5-stranded β-sheets	structure_element	The two domains pack together such that the 5-stranded β-sheets, which have hydrophobic surfaces, interact with each other bringing the CDRs from both the VH and VL domains into close proximity.	RESULTS
+136	140	CDRs	structure_element	The two domains pack together such that the 5-stranded β-sheets, which have hydrophobic surfaces, interact with each other bringing the CDRs from both the VH and VL domains into close proximity.	RESULTS
+155	157	VH	structure_element	The two domains pack together such that the 5-stranded β-sheets, which have hydrophobic surfaces, interact with each other bringing the CDRs from both the VH and VL domains into close proximity.	RESULTS
+162	164	VL	structure_element	The two domains pack together such that the 5-stranded β-sheets, which have hydrophobic surfaces, interact with each other bringing the CDRs from both the VH and VL domains into close proximity.	RESULTS
+65	81	domain interface	site	The domain packing of the variants was assessed by computing the domain interface interactions, the VH:VL tilt angles, the buried surface area and surface complementarity.	RESULTS
+100	105	VH:VL	complex_assembly	The domain packing of the variants was assessed by computing the domain interface interactions, the VH:VL tilt angles, the buried surface area and surface complementarity.	RESULTS
+106	117	tilt angles	evidence	The domain packing of the variants was assessed by computing the domain interface interactions, the VH:VL tilt angles, the buried surface area and surface complementarity.	RESULTS
+0	15	VH:VL interface	site	VH:VL interface amino acid residue interactions	RESULTS
+4	13	conserved	protein_state	The conserved VH:VL interactions as viewed along the VH/VL axis.	FIG
+14	19	VH:VL	complex_assembly	The conserved VH:VL interactions as viewed along the VH/VL axis.	FIG
+53	55	VH	structure_element	The conserved VH:VL interactions as viewed along the VH/VL axis.	FIG
+56	58	VL	structure_element	The conserved VH:VL interactions as viewed along the VH/VL axis.	FIG
+4	6	VH	structure_element	The VH residues are in blue, the VL residues are in orange.	FIG
+33	35	VL	structure_element	The VH residues are in blue, the VL residues are in orange.	FIG
+4	19	VH:VL interface	site	The VH:VL interface is pseudosymmetric, and involves 2 stretches of the polypeptide chain from each domain, namely CDR3 and the framework region between CDRs 1 and 2.	RESULTS
+23	38	pseudosymmetric	protein_state	The VH:VL interface is pseudosymmetric, and involves 2 stretches of the polypeptide chain from each domain, namely CDR3 and the framework region between CDRs 1 and 2.	RESULTS
+115	119	CDR3	structure_element	The VH:VL interface is pseudosymmetric, and involves 2 stretches of the polypeptide chain from each domain, namely CDR3 and the framework region between CDRs 1 and 2.	RESULTS
+128	144	framework region	structure_element	The VH:VL interface is pseudosymmetric, and involves 2 stretches of the polypeptide chain from each domain, namely CDR3 and the framework region between CDRs 1 and 2.	RESULTS
+153	165	CDRs 1 and 2	structure_element	The VH:VL interface is pseudosymmetric, and involves 2 stretches of the polypeptide chain from each domain, namely CDR3 and the framework region between CDRs 1 and 2.	RESULTS
+21	44	antiparallel β-hairpins	structure_element	These stretches form antiparallel β-hairpins within the internal 5-stranded β-sheet.	RESULTS
+65	83	5-stranded β-sheet	structure_element	These stretches form antiparallel β-hairpins within the internal 5-stranded β-sheet.	RESULTS
+110	114	Fabs	structure_element	There are a few principal inter-domain interactions that are conserved not only in the experimental set of 16 Fabs, but in all human antibodies.	RESULTS
+127	132	human	species	There are a few principal inter-domain interactions that are conserved not only in the experimental set of 16 Fabs, but in all human antibodies.	RESULTS
+133	143	antibodies	protein_type	There are a few principal inter-domain interactions that are conserved not only in the experimental set of 16 Fabs, but in all human antibodies.	RESULTS
+51	52	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+53	58	Gln38	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+63	64	H	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+65	70	Gln39	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+75	76	H	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+77	82	Leu45	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+88	106	hydrophobic pocket	site	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+115	116	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+117	122	Phe98	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+124	125	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+126	131	Tyr87	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+136	137	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+138	143	Pro44	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+148	149	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+150	155	Pro44	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+172	173	H	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+174	180	Trp103	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+189	190	L	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+191	196	Ala43	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+218	219	H	structure_element	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+220	225	Tyr91	residue_name_number	They include: 1) a bidentate hydrogen bond between L-Gln38 and H-Gln39; 2) H-Leu45 in a hydrophobic pocket between L-Phe98, L-Tyr87 and L-Pro44; 3) L-Pro44 stacked against H-Trp103; and 4) L-Ala43 opposite the face of H-Tyr91 (Fig. 8).	RESULTS
+22	23	L	structure_element	With the exception of L-Ala43, all other residues are conserved in human germlines.	RESULTS
+24	29	Ala43	residue_name_number	With the exception of L-Ala43, all other residues are conserved in human germlines.	RESULTS
+67	72	human	species	With the exception of L-Ala43, all other residues are conserved in human germlines.	RESULTS
+9	11	43	residue_number	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+45	48	Ser	residue_name	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+50	53	Val	residue_name	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+57	60	Pro	residue_name	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+68	72	L4-1	mutant	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+112	113	H	structure_element	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+114	119	Tyr91	residue_name_number	Position 43 may be alternatively occupied by Ser, Val or Pro (as in L4-1), but the hydrophobic interaction with H-Tyr91 is preserved.	RESULTS
+56	61	VH:VL	complex_assembly	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+62	67	dimer	oligomeric_state	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+87	101	VH-VL contacts	site	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+149	153	CDRs	structure_element	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+154	156	H3	structure_element	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+161	163	L3	structure_element	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+186	201	VH:VL interface	site	These core interactions provide enough stability to the VH:VL dimer so that additional VH-VL contacts can tolerate amino acid sequence variations in CDRs H3 and L3 that form part of the VH:VL interface.	RESULTS
+16	27	20 residues	residue_range	In total, about 20 residues are involved in the VH:VL interactions on each side (Fig. S5).	RESULTS
+48	53	VH:VL	complex_assembly	In total, about 20 residues are involved in the VH:VL interactions on each side (Fig. S5).	RESULTS
+24	41	framework regions	structure_element	Half of them are in the framework regions and those residues (except residue 61 in HC, which is actually in CDR2 in Kabat's definition) are conserved in the set of 16 Fabs.	RESULTS
+77	79	61	residue_number	Half of them are in the framework regions and those residues (except residue 61 in HC, which is actually in CDR2 in Kabat's definition) are conserved in the set of 16 Fabs.	RESULTS
+83	85	HC	structure_element	Half of them are in the framework regions and those residues (except residue 61 in HC, which is actually in CDR2 in Kabat's definition) are conserved in the set of 16 Fabs.	RESULTS
+108	112	CDR2	structure_element	Half of them are in the framework regions and those residues (except residue 61 in HC, which is actually in CDR2 in Kabat's definition) are conserved in the set of 16 Fabs.	RESULTS
+167	171	Fabs	structure_element	Half of them are in the framework regions and those residues (except residue 61 in HC, which is actually in CDR2 in Kabat's definition) are conserved in the set of 16 Fabs.	RESULTS
+25	26	H	structure_element	One notable exception is H-Trp47, which exhibits 2 conformations of the indole ring.	RESULTS
+27	32	Trp47	residue_name_number	One notable exception is H-Trp47, which exhibits 2 conformations of the indole ring.	RESULTS
+15	25	structures	evidence	In most of the structures, it has the χ2 angle of ∼80°, while the ring is flipped over (χ2 = −100°) in H5-51:L3:11 and H5-51:L3-20.	RESULTS
+38	40	χ2	evidence	In most of the structures, it has the χ2 angle of ∼80°, while the ring is flipped over (χ2 = −100°) in H5-51:L3:11 and H5-51:L3-20.	RESULTS
+88	90	χ2	evidence	In most of the structures, it has the χ2 angle of ∼80°, while the ring is flipped over (χ2 = −100°) in H5-51:L3:11 and H5-51:L3-20.	RESULTS
+103	114	H5-51:L3:11	complex_assembly	In most of the structures, it has the χ2 angle of ∼80°, while the ring is flipped over (χ2 = −100°) in H5-51:L3:11 and H5-51:L3-20.	RESULTS
+119	130	H5-51:L3-20	complex_assembly	In most of the structures, it has the χ2 angle of ∼80°, while the ring is flipped over (χ2 = −100°) in H5-51:L3:11 and H5-51:L3-20.	RESULTS
+36	46	structures	evidence	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+61	68	missing	protein_state	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+72	75	CDR	structure_element	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+76	78	H3	structure_element	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+114	124	structures	evidence	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+179	188	structure	evidence	Interestingly, these are the only 2 structures with residues missing in CDR H3 because of disorder, although both structures are determined at high resolution and the rest of the structure is well defined.	RESULTS
+30	33	CDR	structure_element	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+34	36	H3	structure_element	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+46	51	VH:VL	complex_assembly	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+87	93	stable	protein_state	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+110	113	CDR	structure_element	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+114	116	H3	structure_element	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+207	208	H	structure_element	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+209	214	Trp47	residue_name_number	Apparently, residues flanking CDR H3 in the 2 VH:VL pairings are inconsistent with any stable conformation of CDR H3, which translates into a less restricted conformational space for some of them, including H-Trp47.	RESULTS
+0	5	VH:VL	complex_assembly	VH:VL tilt angles	RESULTS
+6	17	tilt angles	evidence	VH:VL tilt angles	RESULTS
+28	30	VH	structure_element	The relative orientation of VH and VL has been measured in a number of different ways.	RESULTS
+35	37	VL	structure_element	The relative orientation of VH and VL has been measured in a number of different ways.	RESULTS
+24	32	ABangles	experimental_method	The first approach uses ABangles, the results of which are shown in Table S2.	RESULTS
+9	12	LCs	structure_element	The four LCs all are classified as Type A because they have a proline at position 44, and the results for each orientation parameter are within the range of values of this type reported by Dunbar and co-workers.	RESULTS
+62	69	proline	residue_name	The four LCs all are classified as Type A because they have a proline at position 44, and the results for each orientation parameter are within the range of values of this type reported by Dunbar and co-workers.	RESULTS
+82	84	44	residue_number	The four LCs all are classified as Type A because they have a proline at position 44, and the results for each orientation parameter are within the range of values of this type reported by Dunbar and co-workers.	RESULTS
+111	132	orientation parameter	evidence	The four LCs all are classified as Type A because they have a proline at position 44, and the results for each orientation parameter are within the range of values of this type reported by Dunbar and co-workers.	RESULTS
+48	52	Fabs	structure_element	In fact, the parameter values for the set of 16 Fabs are in the middle of the distribution observed for 351 non-redundant antibody structures determined at 3.0 Å resolution or better.	RESULTS
+122	130	antibody	protein_type	In fact, the parameter values for the set of 16 Fabs are in the middle of the distribution observed for 351 non-redundant antibody structures determined at 3.0 Å resolution or better.	RESULTS
+131	141	structures	evidence	In fact, the parameter values for the set of 16 Fabs are in the middle of the distribution observed for 351 non-redundant antibody structures determined at 3.0 Å resolution or better.	RESULTS
+22	25	HC1	structure_element	The only exception is HC1, which is shifted toward smaller angles with the mean value of 70.8° as compared to the distribution centered at 72° for the entire PDB.	RESULTS
+41	44	CDR	structure_element	This probably reflects the invariance of CDR H3 in the current set as opposed to the CDR H3 diversity in the PDB.	RESULTS
+45	47	H3	structure_element	This probably reflects the invariance of CDR H3 in the current set as opposed to the CDR H3 diversity in the PDB.	RESULTS
+85	88	CDR	structure_element	This probably reflects the invariance of CDR H3 in the current set as opposed to the CDR H3 diversity in the PDB.	RESULTS
+89	91	H3	structure_element	This probably reflects the invariance of CDR H3 in the current set as opposed to the CDR H3 diversity in the PDB.	RESULTS
+39	50	tilt angles	evidence	The second approach used for comparing tilt angles involved computing the difference in the tilt angles between all pairs of structures.	RESULTS
+74	84	difference	evidence	The second approach used for comparing tilt angles involved computing the difference in the tilt angles between all pairs of structures.	RESULTS
+92	103	tilt angles	evidence	The second approach used for comparing tilt angles involved computing the difference in the tilt angles between all pairs of structures.	RESULTS
+125	135	structures	evidence	The second approach used for comparing tilt angles involved computing the difference in the tilt angles between all pairs of structures.	RESULTS
+4	14	structures	evidence	For structures with 2 copies of the Fab in the asymmetric unit, only one structure was used.	RESULTS
+36	39	Fab	structure_element	For structures with 2 copies of the Fab in the asymmetric unit, only one structure was used.	RESULTS
+73	82	structure	evidence	For structures with 2 copies of the Fab in the asymmetric unit, only one structure was used.	RESULTS
+36	40	Fabs	structure_element	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+53	62	structure	evidence	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+76	87	H1-69:L3-20	complex_assembly	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+98	109	H1-69:L3-11	complex_assembly	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+120	130	H3-23:L4-1	complex_assembly	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+141	152	H3-23:L3-11	complex_assembly	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+167	177	H5-51:L4-1	complex_assembly	The differences between independent Fabs in the same structure are 4.9° for H1-69:L3-20, 1.6° for H1-69:L3-11, 1.4° for H3-23:L4-1, 3.3° for H3-23:L3-11, and 2.5° for H5-51:L4-1.	RESULTS
+22	33	H1-69:L3-20	complex_assembly	With the exception of H1-69:L3-20, the angles are within the range of 2-3° as are observed in the identical structures in the PDB.	RESULTS
+108	118	structures	evidence	With the exception of H1-69:L3-20, the angles are within the range of 2-3° as are observed in the identical structures in the PDB.	RESULTS
+3	14	H1-69:L3-20	complex_assembly	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+27	31	Fabs	structure_element	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+49	59	disordered	protein_state	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+76	79	CDR	structure_element	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+80	82	H2	structure_element	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+94	102	β-strand	structure_element	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+113	118	55-60	residue_range	In H1-69:L3-20, one of the Fabs is substantially disordered so that part of CDR H2 (the outer β-strand, residues 55-60) is completely missing.	RESULTS
+58	60	VH	structure_element	This kind of disorder may compromise the integrity of the VH domain and its interaction with the VL.	RESULTS
+97	99	VL	structure_element	This kind of disorder may compromise the integrity of the VH domain and its interaction with the VL.	RESULTS
+13	16	Fab	structure_element	Indeed, this Fab has the largest twist angle HC2 within the experimental set that exceeds the mean value by 2.5 standard deviations (Table S2).	RESULTS
+33	44	twist angle	evidence	Indeed, this Fab has the largest twist angle HC2 within the experimental set that exceeds the mean value by 2.5 standard deviations (Table S2).	RESULTS
+45	48	HC2	structure_element	Indeed, this Fab has the largest twist angle HC2 within the experimental set that exceeds the mean value by 2.5 standard deviations (Table S2).	RESULTS
+79	92	superposition	experimental_method	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+100	102	VH	structure_element	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+118	129	H1-69:L3-20	complex_assembly	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+141	152	H5-51:L1-39	complex_assembly	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+158	160	VL	structure_element	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+219	229	H1-69:L4-1	complex_assembly	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+241	252	H5-51:L1-39	complex_assembly	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+258	260	VL	structure_element	An illustration of the difference in tilt angle for 2 pairs of variants by the superposition of the VH domains of (A) H1-69:L3-20 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 10.5°) and (B) H1-69:L4-1 on that of H5-51:L1-39 (the VL domain is off by a rigid-body roatation of 1.6°).	FIG
+15	20	VH:VL	complex_assembly	Differences in VH:VL tilt angles.	TABLE
+21	32	tilt angles	evidence	Differences in VH:VL tilt angles.	TABLE
+4	15	differences	evidence	The differences in the tilt angle are shown for all pairs of V regions in Table 3.	RESULTS
+23	33	tilt angle	evidence	The differences in the tilt angle are shown for all pairs of V regions in Table 3.	RESULTS
+61	70	V regions	structure_element	The differences in the tilt angle are shown for all pairs of V regions in Table 3.	RESULTS
+32	42	tilt angle	evidence	The smallest differences in the tilt angle are between the Fabs in isomorphous crystal forms.	RESULTS
+59	63	Fabs	structure_element	The smallest differences in the tilt angle are between the Fabs in isomorphous crystal forms.	RESULTS
+79	92	crystal forms	evidence	The smallest differences in the tilt angle are between the Fabs in isomorphous crystal forms.	RESULTS
+30	40	tilt angle	evidence	The largest deviations in the tilt angle, up to 11.0°, are found for 2 structures, H1-69:L3-20 and H3-23:L3-20, that stand out from the other Fabs.	RESULTS
+71	81	structures	evidence	The largest deviations in the tilt angle, up to 11.0°, are found for 2 structures, H1-69:L3-20 and H3-23:L3-20, that stand out from the other Fabs.	RESULTS
+83	94	H1-69:L3-20	complex_assembly	The largest deviations in the tilt angle, up to 11.0°, are found for 2 structures, H1-69:L3-20 and H3-23:L3-20, that stand out from the other Fabs.	RESULTS
+99	110	H3-23:L3-20	complex_assembly	The largest deviations in the tilt angle, up to 11.0°, are found for 2 structures, H1-69:L3-20 and H3-23:L3-20, that stand out from the other Fabs.	RESULTS
+142	146	Fabs	structure_element	The largest deviations in the tilt angle, up to 11.0°, are found for 2 structures, H1-69:L3-20 and H3-23:L3-20, that stand out from the other Fabs.	RESULTS
+13	23	structures	evidence	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+25	36	H1-69:L3-20	complex_assembly	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+46	49	CDR	structure_element	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+50	52	H3	structure_element	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+61	69	extended	protein_state	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+120	126	kinked	protein_state	One of the 2 structures, H1-69:L3-20, has its CDR H3 in the ‘extended’ conformation; the other structure has it in the ‘kinked’ conformation.	RESULTS
+76	87	tilt angles	evidence	Two examples illustrating large (10.5°) and small (1.6°) differences in the tilt angles are shown in Fig. 9.	RESULTS
+0	5	VH:VL	complex_assembly	VH:VL buried surface area and complementarity	RESULTS
+0	5	VH:VL	complex_assembly	VH:VL surface areas and surface complementarity.	TABLE
+25	28	CDR	structure_element	Some side chain atoms in CDR H3 are missing.	TABLE
+29	31	H3	structure_element	Some side chain atoms in CDR H3 are missing.	TABLE
+12	15	CDR	structure_element	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+16	18	H3	structure_element	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+32	35	YGE	structure_element	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+39	50	H5-51:L3-11	complex_assembly	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+52	55	GIY	structure_element	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+59	70	H5-51:L3-20	complex_assembly	Residues in CDR H3 are missing: YGE in H5-51:L3-11, GIY in H5-51:L3-20.	TABLE
+19	23	PISA	experimental_method	The results of the PISA contact surface calculation and surface complementarity calculation are shown in Table 4.	RESULTS
+24	51	contact surface calculation	experimental_method	The results of the PISA contact surface calculation and surface complementarity calculation are shown in Table 4.	RESULTS
+56	91	surface complementarity calculation	experimental_method	The results of the PISA contact surface calculation and surface complementarity calculation are shown in Table 4.	RESULTS
+4	13	interface	site	The interface areas are calculated as the average of the VH and VL contact surfaces.	RESULTS
+57	83	VH and VL contact surfaces	site	The interface areas are calculated as the average of the VH and VL contact surfaces.	RESULTS
+14	24	structures	evidence	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+30	33	CDR	structure_element	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+34	36	H3	structure_element	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+70	77	missing	protein_state	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+99	109	interfaces	site	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+148	158	structures	evidence	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+164	172	complete	protein_state	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+173	177	CDRs	structure_element	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+212	216	Fabs	structure_element	Six of the 16 structures have CDR H3 side chains or complete residues missing, and therefore their interfaces are much smaller than in the other 10 structures with complete CDRs (the results are provided for all Fabs for completeness).	RESULTS
+10	18	complete	protein_state	Among the complete structures, the interface areas range from 684 to 836 Å2.	RESULTS
+19	29	structures	evidence	Among the complete structures, the interface areas range from 684 to 836 Å2.	RESULTS
+35	44	interface	site	Among the complete structures, the interface areas range from 684 to 836 Å2.	RESULTS
+21	31	structures	evidence	Interestingly, the 2 structures that have the largest tilt angle differences with the other variants, H3-23:L3-20 and H1-69:L3-20, have the smallest VH:VL interfaces, 684 and 725 Å2, respectively.	RESULTS
+54	76	tilt angle differences	evidence	Interestingly, the 2 structures that have the largest tilt angle differences with the other variants, H3-23:L3-20 and H1-69:L3-20, have the smallest VH:VL interfaces, 684 and 725 Å2, respectively.	RESULTS
+102	113	H3-23:L3-20	complex_assembly	Interestingly, the 2 structures that have the largest tilt angle differences with the other variants, H3-23:L3-20 and H1-69:L3-20, have the smallest VH:VL interfaces, 684 and 725 Å2, respectively.	RESULTS
+118	129	H1-69:L3-20	complex_assembly	Interestingly, the 2 structures that have the largest tilt angle differences with the other variants, H3-23:L3-20 and H1-69:L3-20, have the smallest VH:VL interfaces, 684 and 725 Å2, respectively.	RESULTS
+149	165	VH:VL interfaces	site	Interestingly, the 2 structures that have the largest tilt angle differences with the other variants, H3-23:L3-20 and H1-69:L3-20, have the smallest VH:VL interfaces, 684 and 725 Å2, respectively.	RESULTS
+0	11	H3-23:L3-20	complex_assembly	H3-23:L3-20 is also unique in that it has the lowest value (0.676) of surface complementarity.	RESULTS
+70	93	surface complementarity	evidence	H3-23:L3-20 is also unique in that it has the lowest value (0.676) of surface complementarity.	RESULTS
+0	20	Melting temperatures	evidence	Melting temperatures for the 16 Fabs.	TABLE
+32	36	Fabs	structure_element	Melting temperatures for the 16 Fabs.	TABLE
+14	16	Tm	evidence	Colors: blue (Tm < 70°C), green (70°C < Tm < 73°C), yellow (73°C < Tm < 78°C), orange (Tm > 78°C).	TABLE
+40	42	Tm	evidence	Colors: blue (Tm < 70°C), green (70°C < Tm < 73°C), yellow (73°C < Tm < 78°C), orange (Tm > 78°C).	TABLE
+67	69	Tm	evidence	Colors: blue (Tm < 70°C), green (70°C < Tm < 73°C), yellow (73°C < Tm < 78°C), orange (Tm > 78°C).	TABLE
+87	89	Tm	evidence	Colors: blue (Tm < 70°C), green (70°C < Tm < 73°C), yellow (73°C < Tm < 78°C), orange (Tm > 78°C).	TABLE
+0	20	Melting temperatures	evidence	Melting temperatures (Tm) were measured for all Fabs using differential scanning calorimetry (Table 5).	RESULTS
+22	24	Tm	evidence	Melting temperatures (Tm) were measured for all Fabs using differential scanning calorimetry (Table 5).	RESULTS
+48	52	Fabs	structure_element	Melting temperatures (Tm) were measured for all Fabs using differential scanning calorimetry (Table 5).	RESULTS
+59	92	differential scanning calorimetry	experimental_method	Melting temperatures (Tm) were measured for all Fabs using differential scanning calorimetry (Table 5).	RESULTS
+31	33	LC	structure_element	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+39	43	Fabs	structure_element	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+59	64	H1-69	mutant	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+69	74	H3-23	mutant	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+98	104	stable	protein_state	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+131	136	H3-53	mutant	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+141	146	H5-51	mutant	It appears that for each given LC, the Fabs with germlines H1-69 and H3-23 are substantially more stable than those with germlines H3-53 and H5-51.	RESULTS
+13	18	L1-39	mutant	In addition, L1-39 provides a much higher degree of stabilization than the other 3 LC germlines when combined with any of the HCs.	RESULTS
+83	85	LC	structure_element	In addition, L1-39 provides a much higher degree of stabilization than the other 3 LC germlines when combined with any of the HCs.	RESULTS
+126	129	HCs	structure_element	In addition, L1-39 provides a much higher degree of stabilization than the other 3 LC germlines when combined with any of the HCs.	RESULTS
+17	19	Tm	evidence	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+30	41	H1-69:L1-39	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+46	57	H3-23:L1-39	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+90	101	H3-53:L3-20	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+103	113	H3-53:L4-1	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+115	126	H5-51:L3-20	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+131	141	H5-51:L4-1	complex_assembly	As a result, the Tm for pairs H1-69:L1-39 and H3-23:L1-39 is 12-13° higher than for pairs H3-53:L3-20, H3-53:L4-1, H5-51:L3-20 and H5-51:L4-1.	RESULTS
+89	107	crystal structures	evidence	These findings correlate well with the degree of conformational disorder observed in the crystal structures.	RESULTS
+9	12	CDR	structure_element	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+13	15	H3	structure_element	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+42	52	disordered	protein_state	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+78	82	Fabs	structure_element	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+83	94	H5-51:L3-20	complex_assembly	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+99	110	H5-51:L3-11	complex_assembly	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+132	135	Tms	evidence	Parts of CDR H3 main chain are completely disordered, and were not modeled in Fabs H5-51:L3-20 and H5-51:L3-11 that have the lowest Tms in the set.	RESULTS
+3	19	electron density	evidence	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+63	67	CDRs	structure_element	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+68	70	H3	structure_element	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+75	77	L3	structure_element	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+85	89	Fabs	structure_element	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+104	109	H3-53	mutant	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+148	164	variable domains	structure_element	No electron density is observed for a number of side chains in CDRs H3 and L3 in all Fabs with germline H3-53, which indicates loose packing of the variable domains.	RESULTS
+74	77	Tms	evidence	All those molecules are relatively unstable, as is reflected in their low Tms.	RESULTS
+30	65	systematic structural investigation	experimental_method	This is the first report of a systematic structural investigation of a phage germline library.	DISCUSS
+71	93	phage germline library	experimental_method	This is the first report of a systematic structural investigation of a phage germline library.	DISCUSS
+7	10	Fab	structure_element	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+11	21	structures	evidence	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+73	76	HCs	structure_element	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+78	83	H1-69	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+85	90	H3-23	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+92	97	H3-53	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+103	108	H5-51	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+126	129	LCs	structure_element	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+131	136	L1-39	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+138	143	L3-11	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+145	150	L3-20	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+155	159	L4-1	mutant	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+180	183	CDR	structure_element	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+184	186	H3	structure_element	The 16 Fab structures offer a unique look at all pairings of 4 different HCs (H1-69, H3-23, H3-53, and H5-51) and 4 different LCs (L1-39, L3-11, L3-20 and L4-1), all with the same CDR H3.	DISCUSS
+4	19	structural data	evidence	The structural data set taken as a whole provides insight into how the backbone conformations of the CDRs of a specific heavy or light chain vary when it is paired with 4 different light or heavy chains, respectively.	DISCUSS
+101	105	CDRs	structure_element	The structural data set taken as a whole provides insight into how the backbone conformations of the CDRs of a specific heavy or light chain vary when it is paired with 4 different light or heavy chains, respectively.	DISCUSS
+129	140	light chain	structure_element	The structural data set taken as a whole provides insight into how the backbone conformations of the CDRs of a specific heavy or light chain vary when it is paired with 4 different light or heavy chains, respectively.	DISCUSS
+190	202	heavy chains	structure_element	The structural data set taken as a whole provides insight into how the backbone conformations of the CDRs of a specific heavy or light chain vary when it is paired with 4 different light or heavy chains, respectively.	DISCUSS
+27	30	CDR	structure_element	A large variability in the CDR conformations for the sets of HCs and LCs is observed.	DISCUSS
+61	64	HCs	structure_element	A large variability in the CDR conformations for the sets of HCs and LCs is observed.	DISCUSS
+69	72	LCs	structure_element	A large variability in the CDR conformations for the sets of HCs and LCs is observed.	DISCUSS
+18	21	CDR	structure_element	In some cases the CDR conformations for all members of a set are virtually identical, for others subtle changes occur in a few members of a set, and in some cases larger deviations are observed within a set.	DISCUSS
+23	35	crystallized	experimental_method	The five variants that crystallized with 2 copies of the Fab in the asymmetric unit serve somewhat as controls for the influence of crystal packing on the conformations of the CDRs.	DISCUSS
+57	60	Fab	structure_element	The five variants that crystallized with 2 copies of the Fab in the asymmetric unit serve somewhat as controls for the influence of crystal packing on the conformations of the CDRs.	DISCUSS
+176	180	CDRs	structure_element	The five variants that crystallized with 2 copies of the Fab in the asymmetric unit serve somewhat as controls for the influence of crystal packing on the conformations of the CDRs.	DISCUSS
+17	27	structures	evidence	In four of the 5 structures the CDR conformations are consistent.	DISCUSS
+32	35	CDR	structure_element	In four of the 5 structures the CDR conformations are consistent.	DISCUSS
+26	37	H1-69:L3-20	complex_assembly	In only one case, that of H1-69:L3-20 (the lowest resolution structure), do we see differences in the conformations of the 2 copies of CDRs H1 and L1.	DISCUSS
+61	70	structure	evidence	In only one case, that of H1-69:L3-20 (the lowest resolution structure), do we see differences in the conformations of the 2 copies of CDRs H1 and L1.	DISCUSS
+135	139	CDRs	structure_element	In only one case, that of H1-69:L3-20 (the lowest resolution structure), do we see differences in the conformations of the 2 copies of CDRs H1 and L1.	DISCUSS
+140	142	H1	structure_element	In only one case, that of H1-69:L3-20 (the lowest resolution structure), do we see differences in the conformations of the 2 copies of CDRs H1 and L1.	DISCUSS
+147	149	L1	structure_element	In only one case, that of H1-69:L3-20 (the lowest resolution structure), do we see differences in the conformations of the 2 copies of CDRs H1 and L1.	DISCUSS
+111	126	variable domain	structure_element	This variability is likely a result of 2 factors, crystal packing interactions and internal instability of the variable domain.	DISCUSS
+8	12	CDRs	structure_element	For the CDRs with canonical structures, the largest changes in conformation occur for CDR H1 of H1-69 and H3-53.	DISCUSS
+86	89	CDR	structure_element	For the CDRs with canonical structures, the largest changes in conformation occur for CDR H1 of H1-69 and H3-53.	DISCUSS
+90	92	H1	structure_element	For the CDRs with canonical structures, the largest changes in conformation occur for CDR H1 of H1-69 and H3-53.	DISCUSS
+96	101	H1-69	mutant	For the CDRs with canonical structures, the largest changes in conformation occur for CDR H1 of H1-69 and H3-53.	DISCUSS
+106	111	H3-53	mutant	For the CDRs with canonical structures, the largest changes in conformation occur for CDR H1 of H1-69 and H3-53.	DISCUSS
+12	15	HCs	structure_element	The other 2 HCs, H3-23 and H5-51, have canonical structures that are remarkably well conserved (Fig. 1).	DISCUSS
+17	22	H3-23	mutant	The other 2 HCs, H3-23 and H5-51, have canonical structures that are remarkably well conserved (Fig. 1).	DISCUSS
+27	32	H5-51	mutant	The other 2 HCs, H3-23 and H5-51, have canonical structures that are remarkably well conserved (Fig. 1).	DISCUSS
+69	94	remarkably well conserved	protein_state	The other 2 HCs, H3-23 and H5-51, have canonical structures that are remarkably well conserved (Fig. 1).	DISCUSS
+9	12	HCs	structure_element	Of the 4 HCs, H1-69 has the greatest number of canonical structure assignments (Table 2).	DISCUSS
+14	19	H1-69	mutant	Of the 4 HCs, H1-69 has the greatest number of canonical structure assignments (Table 2).	DISCUSS
+0	5	H1-69	mutant	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+36	43	glycine	residue_name	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+66	68	26	residue_number	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+73	75	27	residue_number	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+96	118	conformational freedom	protein_state	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+122	125	CDR	structure_element	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+126	128	H1	structure_element	H1-69 is unique in having a pair of glycine residues at positions 26 and 27, which provide more conformational freedom in CDR H1.	DISCUSS
+8	16	IGHV1-69	mutant	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+44	47	VH4	structure_element	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+70	78	glycines	residue_name	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+82	85	CDR	structure_element	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+86	88	H1	structure_element	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+141	166	conformationally unstable	protein_state	Besides IGHV1-69, only the germlines of the VH4 family possess double glycines in CDR H1, and it will be interesting to see if they are also conformationally unstable.	DISCUSS
+14	19	VH:VL	complex_assembly	Having all 16 VH:VL pairs with the same CDR H3 provides some insights into why molecular modeling efforts of CDR H3 have proven so difficult.	DISCUSS
+40	43	CDR	structure_element	Having all 16 VH:VL pairs with the same CDR H3 provides some insights into why molecular modeling efforts of CDR H3 have proven so difficult.	DISCUSS
+44	46	H3	structure_element	Having all 16 VH:VL pairs with the same CDR H3 provides some insights into why molecular modeling efforts of CDR H3 have proven so difficult.	DISCUSS
+109	112	CDR	structure_element	Having all 16 VH:VL pairs with the same CDR H3 provides some insights into why molecular modeling efforts of CDR H3 have proven so difficult.	DISCUSS
+113	115	H3	structure_element	Having all 16 VH:VL pairs with the same CDR H3 provides some insights into why molecular modeling efforts of CDR H3 have proven so difficult.	DISCUSS
+69	73	Fabs	structure_element	As mentioned in the Results section, this data set is composed of 21 Fabs, since 5 of the 16 variants have 2 Fab copies in the asymmetric unit.	DISCUSS
+109	112	Fab	structure_element	As mentioned in the Results section, this data set is composed of 21 Fabs, since 5 of the 16 variants have 2 Fab copies in the asymmetric unit.	DISCUSS
+11	15	Fabs	structure_element	For the 18 Fabs with complete backbone atoms for CDR H3, 10 have conformations similar to that of the parent, while the others have significantly different conformations (Fig. 6).	DISCUSS
+49	52	CDR	structure_element	For the 18 Fabs with complete backbone atoms for CDR H3, 10 have conformations similar to that of the parent, while the others have significantly different conformations (Fig. 6).	DISCUSS
+53	55	H3	structure_element	For the 18 Fabs with complete backbone atoms for CDR H3, 10 have conformations similar to that of the parent, while the others have significantly different conformations (Fig. 6).	DISCUSS
+28	31	CDR	structure_element	Thus, it is likely that the CDR H3 conformation is dependent upon 2 dominating factors: 1) amino acid sequence; and 2) VH and VL context.	DISCUSS
+32	34	H3	structure_element	Thus, it is likely that the CDR H3 conformation is dependent upon 2 dominating factors: 1) amino acid sequence; and 2) VH and VL context.	DISCUSS
+119	121	VH	structure_element	Thus, it is likely that the CDR H3 conformation is dependent upon 2 dominating factors: 1) amino acid sequence; and 2) VH and VL context.	DISCUSS
+126	128	VL	structure_element	Thus, it is likely that the CDR H3 conformation is dependent upon 2 dominating factors: 1) amino acid sequence; and 2) VH and VL context.	DISCUSS
+103	108	VH:VL	complex_assembly	More than half of the variants retain the conformation of the parent despite having differences in the VH:VL pairing.	DISCUSS
+23	33	structures	evidence	This subset includes 2 structures with 2 copies of the Fab in the asymmetric unit, all of which are nearly identical in conformation.	DISCUSS
+55	58	Fab	structure_element	This subset includes 2 structures with 2 copies of the Fab in the asymmetric unit, all of which are nearly identical in conformation.	DISCUSS
+16	26	structures	evidence	The remaining 8 structures exhibit “non-parental” conformations, indicating that the VH and VL context can also be a dominating factor influencing CDR H3.	DISCUSS
+85	87	VH	structure_element	The remaining 8 structures exhibit “non-parental” conformations, indicating that the VH and VL context can also be a dominating factor influencing CDR H3.	DISCUSS
+92	94	VL	structure_element	The remaining 8 structures exhibit “non-parental” conformations, indicating that the VH and VL context can also be a dominating factor influencing CDR H3.	DISCUSS
+147	150	CDR	structure_element	The remaining 8 structures exhibit “non-parental” conformations, indicating that the VH and VL context can also be a dominating factor influencing CDR H3.	DISCUSS
+151	153	H3	structure_element	The remaining 8 structures exhibit “non-parental” conformations, indicating that the VH and VL context can also be a dominating factor influencing CDR H3.	DISCUSS
+23	33	structures	evidence	This subset also has 2 structures with 2 Fab copies in the asymmetric unit.	DISCUSS
+41	44	Fab	structure_element	This subset also has 2 structures with 2 Fab copies in the asymmetric unit.	DISCUSS
+65	77	stem regions	structure_element	Interestingly, as described earlier, these 2 pairs differ in the stem regions with the H1-69:L3-20 pair in the ‘extended’ conformation and H5-51:L4-1 pair in the ‘kinked’ conformation.	DISCUSS
+87	98	H1-69:L3-20	complex_assembly	Interestingly, as described earlier, these 2 pairs differ in the stem regions with the H1-69:L3-20 pair in the ‘extended’ conformation and H5-51:L4-1 pair in the ‘kinked’ conformation.	DISCUSS
+112	120	extended	protein_state	Interestingly, as described earlier, these 2 pairs differ in the stem regions with the H1-69:L3-20 pair in the ‘extended’ conformation and H5-51:L4-1 pair in the ‘kinked’ conformation.	DISCUSS
+139	149	H5-51:L4-1	complex_assembly	Interestingly, as described earlier, these 2 pairs differ in the stem regions with the H1-69:L3-20 pair in the ‘extended’ conformation and H5-51:L4-1 pair in the ‘kinked’ conformation.	DISCUSS
+163	169	kinked	protein_state	Interestingly, as described earlier, these 2 pairs differ in the stem regions with the H1-69:L3-20 pair in the ‘extended’ conformation and H5-51:L4-1 pair in the ‘kinked’ conformation.	DISCUSS
+4	7	CDR	structure_element	The CDR H3 conformational analysis shows that, for each set of variants of one HC paired with the 4 different LCs, both “parental” and “non-parental” conformations are observed.	DISCUSS
+8	10	H3	structure_element	The CDR H3 conformational analysis shows that, for each set of variants of one HC paired with the 4 different LCs, both “parental” and “non-parental” conformations are observed.	DISCUSS
+11	34	conformational analysis	experimental_method	The CDR H3 conformational analysis shows that, for each set of variants of one HC paired with the 4 different LCs, both “parental” and “non-parental” conformations are observed.	DISCUSS
+79	81	HC	structure_element	The CDR H3 conformational analysis shows that, for each set of variants of one HC paired with the 4 different LCs, both “parental” and “non-parental” conformations are observed.	DISCUSS
+110	113	LCs	structure_element	The CDR H3 conformational analysis shows that, for each set of variants of one HC paired with the 4 different LCs, both “parental” and “non-parental” conformations are observed.	DISCUSS
+74	76	LC	structure_element	The same variability is observed for the sets of variants composed of one LC paired with each of the 4 HCs.	DISCUSS
+103	106	HCs	structure_element	The same variability is observed for the sets of variants composed of one LC paired with each of the 4 HCs.	DISCUSS
+64	66	HC	structure_element	Thus, no patterns of conformational preference for a particular HC or LC emerge to shed any direct light on what drives the conformational differences.	DISCUSS
+70	72	LC	structure_element	Thus, no patterns of conformational preference for a particular HC or LC emerge to shed any direct light on what drives the conformational differences.	DISCUSS
+65	67	H3	structure_element	This finding supports the hypothesis of Weitzner et al. that the H3 conformation is controlled both by its sequence and its environment.	DISCUSS
+49	59	tilt angle	evidence	In looking at a possible correlation between the tilt angle and the conformation of CDR H3, no clear trends are observed.	DISCUSS
+84	87	CDR	structure_element	In looking at a possible correlation between the tilt angle and the conformation of CDR H3, no clear trends are observed.	DISCUSS
+88	90	H3	structure_element	In looking at a possible correlation between the tilt angle and the conformation of CDR H3, no clear trends are observed.	DISCUSS
+14	25	H1-69:L3-20	complex_assembly	Two variants, H1-69:L3-20 and H3-23:L3-20, have the largest differences in the tilt angles compared to other variants as seen in Table 3.	DISCUSS
+30	41	H3-23:L3-20	complex_assembly	Two variants, H1-69:L3-20 and H3-23:L3-20, have the largest differences in the tilt angles compared to other variants as seen in Table 3.	DISCUSS
+13	18	VH:VL	complex_assembly	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+19	41	orientation parameters	evidence	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+52	56	Fabs	structure_element	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+85	94	deviation	evidence	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+98	100	HL	structure_element	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+102	105	LC1	structure_element	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+110	113	HC2	structure_element	The absolute VH:VL orientation parameters for the 2 Fabs (Table S2) show significant deviation in HL, LC1 and HC2 values (2-3 standard deviations from the mean).	DISCUSS
+21	32	H3-23:L3-20	complex_assembly	One of the variants, H3-23:L3-20, has the CDR H3 conformation similar to the parent, but the other, H1-69:L3-20, is different.	DISCUSS
+42	45	CDR	structure_element	One of the variants, H3-23:L3-20, has the CDR H3 conformation similar to the parent, but the other, H1-69:L3-20, is different.	DISCUSS
+46	48	H3	structure_element	One of the variants, H3-23:L3-20, has the CDR H3 conformation similar to the parent, but the other, H1-69:L3-20, is different.	DISCUSS
+100	111	H1-69:L3-20	complex_assembly	One of the variants, H3-23:L3-20, has the CDR H3 conformation similar to the parent, but the other, H1-69:L3-20, is different.	DISCUSS
+49	60	H1-69:L3-20	complex_assembly	As noted in the Results section, the 2 variants, H1-69:L3-20 and H3-23:L3-20, are outliers in terms of the tilt angle; at the same time, both have the smallest VH:VL interface.	DISCUSS
+65	76	H3-23:L3-20	complex_assembly	As noted in the Results section, the 2 variants, H1-69:L3-20 and H3-23:L3-20, are outliers in terms of the tilt angle; at the same time, both have the smallest VH:VL interface.	DISCUSS
+107	117	tilt angle	evidence	As noted in the Results section, the 2 variants, H1-69:L3-20 and H3-23:L3-20, are outliers in terms of the tilt angle; at the same time, both have the smallest VH:VL interface.	DISCUSS
+160	175	VH:VL interface	site	As noted in the Results section, the 2 variants, H1-69:L3-20 and H3-23:L3-20, are outliers in terms of the tilt angle; at the same time, both have the smallest VH:VL interface.	DISCUSS
+14	24	interfaces	site	These smaller interfaces may perhaps translate to a significant deviation in how VH is oriented relative to VL than the other variants.	DISCUSS
+81	83	VH	structure_element	These smaller interfaces may perhaps translate to a significant deviation in how VH is oriented relative to VL than the other variants.	DISCUSS
+108	110	VL	structure_element	These smaller interfaces may perhaps translate to a significant deviation in how VH is oriented relative to VL than the other variants.	DISCUSS
+76	81	VH:VL	complex_assembly	These deviations from the other variants can also be seen to some extent in VH:VL orientation parameters in Table S2, as well as in the smaller number of residues involved in the VH:VL interfaces of these 2 variants (Fig. S5).	DISCUSS
+179	195	VH:VL interfaces	site	These deviations from the other variants can also be seen to some extent in VH:VL orientation parameters in Table S2, as well as in the smaller number of residues involved in the VH:VL interfaces of these 2 variants (Fig. S5).	DISCUSS
+64	68	CDRs	structure_element	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+84	87	CDR	structure_element	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+88	90	H1	structure_element	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+105	108	CDR	structure_element	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+109	111	L1	structure_element	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+150	158	glycines	residue_name	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+172	179	serines	residue_name	These differences undoubtedly influence the conformation of the CDRs, in particular CDR H1 (Fig. 1A) and CDR L1 (Fig. 3C), especially with the tandem glycines and multiple serines present, respectively.	DISCUSS
+38	48	antibodies	protein_type	Pairing of different germlines yields antibodies with various degrees of stability.	DISCUSS
+20	40	melting temperatures	evidence	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+52	57	H1-69	mutant	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+62	67	H3-23	mutant	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+72	74	HC	structure_element	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+88	93	L1-39	mutant	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+98	100	LC	structure_element	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+114	120	stable	protein_state	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+121	125	Fabs	structure_element	As indicated by the melting temperatures, germlines H1-69 and H3-23 for HC and germline L1-39 for LC produce more stable Fabs compared to the other germlines in the experimental set.	DISCUSS
+52	54	LC	structure_element	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+64	69	L1-39	mutant	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+78	81	CDR	structure_element	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+82	84	L3	structure_element	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+119	121	91	residue_number	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+126	128	94	residue_number	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+168	171	CDR	structure_element	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+172	174	H3	structure_element	One possible explanation of the clear preference of LC germline L1-39 is that CDR L3 has smaller residues at positions 91 and 94, allowing for more room to accommodate CDR H3.	DISCUSS
+37	40	Tyr	residue_name	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+42	45	Arg	residue_name	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+50	53	Trp	residue_name	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+83	88	L1-39	mutant	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+93	96	Ser	residue_name	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+101	104	Thr	residue_name	Other germlines have bulky residues, Tyr, Arg and Trp, at these positions, whereas L1-39 has Ser and Thr.	DISCUSS
+47	49	VL	structure_element	Various combinations of germline sequences for VL and VH impose certain constraints on CDR H3, which has to adapt to the environment.	DISCUSS
+54	56	VH	structure_element	Various combinations of germline sequences for VL and VH impose certain constraints on CDR H3, which has to adapt to the environment.	DISCUSS
+87	90	CDR	structure_element	Various combinations of germline sequences for VL and VH impose certain constraints on CDR H3, which has to adapt to the environment.	DISCUSS
+91	93	H3	structure_element	Various combinations of germline sequences for VL and VH impose certain constraints on CDR H3, which has to adapt to the environment.	DISCUSS
+7	14	compact	protein_state	A more compact CDR L3 may be beneficial in this situation.	DISCUSS
+15	18	CDR	structure_element	A more compact CDR L3 may be beneficial in this situation.	DISCUSS
+19	21	L3	structure_element	A more compact CDR L3 may be beneficial in this situation.	DISCUSS
+43	45	LC	structure_element	At the other end of the stability range is LC germline L3-20, which yields antibodies with the lowest Tms.	DISCUSS
+55	60	L3-20	mutant	At the other end of the stability range is LC germline L3-20, which yields antibodies with the lowest Tms.	DISCUSS
+75	85	antibodies	protein_type	At the other end of the stability range is LC germline L3-20, which yields antibodies with the lowest Tms.	DISCUSS
+102	105	Tms	evidence	At the other end of the stability range is LC germline L3-20, which yields antibodies with the lowest Tms.	DISCUSS
+20	25	H3-53	mutant	While pairings with H3-53 and H5-51 may be safely called a mismatch, those with H1-69 and H3-23 have Tms about 5-6° higher.	DISCUSS
+30	35	H5-51	mutant	While pairings with H3-53 and H5-51 may be safely called a mismatch, those with H1-69 and H3-23 have Tms about 5-6° higher.	DISCUSS
+80	85	H1-69	mutant	While pairings with H3-53 and H5-51 may be safely called a mismatch, those with H1-69 and H3-23 have Tms about 5-6° higher.	DISCUSS
+90	95	H3-23	mutant	While pairings with H3-53 and H5-51 may be safely called a mismatch, those with H1-69 and H3-23 have Tms about 5-6° higher.	DISCUSS
+101	104	Tms	evidence	While pairings with H3-53 and H5-51 may be safely called a mismatch, those with H1-69 and H3-23 have Tms about 5-6° higher.	DISCUSS
+17	21	Fabs	structure_element	Curiously, the 2 Fabs, H1-69:L3-20 and H3-23:L3-20, deviate markedly in their tilt angles from the rest of the panel.	DISCUSS
+23	34	H1-69:L3-20	complex_assembly	Curiously, the 2 Fabs, H1-69:L3-20 and H3-23:L3-20, deviate markedly in their tilt angles from the rest of the panel.	DISCUSS
+39	50	H3-23:L3-20	complex_assembly	Curiously, the 2 Fabs, H1-69:L3-20 and H3-23:L3-20, deviate markedly in their tilt angles from the rest of the panel.	DISCUSS
+78	89	tilt angles	evidence	Curiously, the 2 Fabs, H1-69:L3-20 and H3-23:L3-20, deviate markedly in their tilt angles from the rest of the panel.	DISCUSS
+40	51	tilt angles	evidence	It is possible that by adopting extreme tilt angles the structure modulates CDR H3 and its environment, which apparently cannot be achieved solely by conformational rearrangement of the CDR.	DISCUSS
+56	65	structure	evidence	It is possible that by adopting extreme tilt angles the structure modulates CDR H3 and its environment, which apparently cannot be achieved solely by conformational rearrangement of the CDR.	DISCUSS
+76	79	CDR	structure_element	It is possible that by adopting extreme tilt angles the structure modulates CDR H3 and its environment, which apparently cannot be achieved solely by conformational rearrangement of the CDR.	DISCUSS
+80	82	H3	structure_element	It is possible that by adopting extreme tilt angles the structure modulates CDR H3 and its environment, which apparently cannot be achieved solely by conformational rearrangement of the CDR.	DISCUSS
+186	189	CDR	structure_element	It is possible that by adopting extreme tilt angles the structure modulates CDR H3 and its environment, which apparently cannot be achieved solely by conformational rearrangement of the CDR.	DISCUSS
+22	37	VH:VL interface	site	Note that most of the VH:VL interface residues are invariant; therefore, significant change of the tilt angle must come with a penalty in free energy.	DISCUSS
+15	25	antibodies	protein_type	Yet, for the 2 antibodies, the total gain in stability merits the domain repacking.	DISCUSS
+30	33	Fab	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+50	52	Tm	evidence	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+98	100	HC	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+105	107	LC	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+108	124	variable domains	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+143	146	CDR	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+147	149	H3	structure_element	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+157	168	VH:VL cleft	site	Overall, the stability of the Fab, as measured by Tm, is a result of the mutual adjustment of the HC and LC variable domains and adjustment of CDR H3 to the VH:VL cleft.	DISCUSS
+167	176	structure	evidence	The final conformation represents an energetic minimum; however, in most cases it is very shallow, so that a single mutation can cause a dramatic rearrangement of the structure.	DISCUSS
+33	51	structural library	experimental_method	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+100	103	HCs	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+109	112	LCs	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+132	135	CDR	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+136	138	H3	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+173	181	antibody	protein_type	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+182	191	structure	evidence	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+276	278	L1	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+280	282	L2	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+284	286	L3	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+288	290	H1	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+295	297	H2	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+298	302	CDRs	structure_element	In summary, the analysis of this structural library of germline variants composed of all pairs of 4 HCs and 4LCs, all with the same CDR H3, offers some unique insights into antibody structure and how pairing and sequence may influence, or not, the canonical structures of the L1, L2, L3, H1 and H2 CDRs.	DISCUSS
+18	21	CDR	structure_element	Comparison of the CDR H3s reveals a large set of variants with conformations similar to the parent, while a second set has significant conformational variability, indicating that both the sequence and the structural context define the CDR H3 conformation.	DISCUSS
+22	25	H3s	structure_element	Comparison of the CDR H3s reveals a large set of variants with conformations similar to the parent, while a second set has significant conformational variability, indicating that both the sequence and the structural context define the CDR H3 conformation.	DISCUSS
+235	238	CDR	structure_element	Comparison of the CDR H3s reveals a large set of variants with conformations similar to the parent, while a second set has significant conformational variability, indicating that both the sequence and the structural context define the CDR H3 conformation.	DISCUSS
+239	241	H3	structure_element	Comparison of the CDR H3s reveals a large set of variants with conformations similar to the parent, while a second set has significant conformational variability, indicating that both the sequence and the structural context define the CDR H3 conformation.	DISCUSS
+39	50	H1-69:L3-20	complex_assembly	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+55	65	H3-53:L4-1	complex_assembly	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+77	85	extended	protein_state	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+87	98	stem region	structure_element	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+140	146	kinked	protein_state	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+148	159	stem region	structure_element	Quite unexpectedly, 2 of the variants, H1-69:L3-20 and H3-53:L4-1, have the ‘extended’ stem region differing from the other 14 that have a ‘kinked’ stem region.	DISCUSS
+45	48	CDR	structure_element	These data reveal the difficulty of modeling CDR H3 accurately, as shown again in Antibody Modeling Assessment II.	DISCUSS
+49	51	H3	structure_element	These data reveal the difficulty of modeling CDR H3 accurately, as shown again in Antibody Modeling Assessment II.	DISCUSS
+13	21	antibody	protein_type	Furthermore, antibody CDRs, H3 in particular, may go through conformational changes upon binding their targets, making structural prediction for docking purposes an even more difficult task.	DISCUSS
+22	26	CDRs	structure_element	Furthermore, antibody CDRs, H3 in particular, may go through conformational changes upon binding their targets, making structural prediction for docking purposes an even more difficult task.	DISCUSS
+28	30	H3	structure_element	Furthermore, antibody CDRs, H3 in particular, may go through conformational changes upon binding their targets, making structural prediction for docking purposes an even more difficult task.	DISCUSS
+38	46	antibody	protein_type	Fortunately, for most applications of antibody modeling, such as engineering affinity and biophysical properties, an accurate CDR H3 structure is not always necessary.	DISCUSS
+126	129	CDR	structure_element	Fortunately, for most applications of antibody modeling, such as engineering affinity and biophysical properties, an accurate CDR H3 structure is not always necessary.	DISCUSS
+130	132	H3	structure_element	Fortunately, for most applications of antibody modeling, such as engineering affinity and biophysical properties, an accurate CDR H3 structure is not always necessary.	DISCUSS
+133	142	structure	evidence	Fortunately, for most applications of antibody modeling, such as engineering affinity and biophysical properties, an accurate CDR H3 structure is not always necessary.	DISCUSS
+38	41	CDR	structure_element	For those applications where accurate CDR structures are essential, such as docking, the results in this work demonstrate the importance of experimental structures.	DISCUSS
+42	52	structures	evidence	For those applications where accurate CDR structures are essential, such as docking, the results in this work demonstrate the importance of experimental structures.	DISCUSS
+153	163	structures	evidence	For those applications where accurate CDR structures are essential, such as docking, the results in this work demonstrate the importance of experimental structures.	DISCUSS
+28	66	expression and crystallization methods	experimental_method	With the recent advances in expression and crystallization methods, Fab structures can be obtained rapidly.	DISCUSS
+68	71	Fab	structure_element	With the recent advances in expression and crystallization methods, Fab structures can be obtained rapidly.	DISCUSS
+72	82	structures	evidence	With the recent advances in expression and crystallization methods, Fab structures can be obtained rapidly.	DISCUSS
+23	26	Fab	structure_element	The set of 16 germline Fab structures offers a unique dataset to facilitate software development for antibody modeling.	DISCUSS
+27	37	structures	evidence	The set of 16 germline Fab structures offers a unique dataset to facilitate software development for antibody modeling.	DISCUSS
+101	109	antibody	protein_type	The set of 16 germline Fab structures offers a unique dataset to facilitate software development for antibody modeling.	DISCUSS
+65	75	structures	evidence	The results essentially support the underlying idea of canonical structures, indicating that most CDRs with germline sequences tend to adopt predefined conformations.	DISCUSS
+98	102	CDRs	structure_element	The results essentially support the underlying idea of canonical structures, indicating that most CDRs with germline sequences tend to adopt predefined conformations.	DISCUSS
+66	74	antibody	protein_type	From this point of view, a novel approach to design combinatorial antibody libraries would be to cover the range of CDR conformations that may not necessarily coincide with the germline usage in the human repertoire.	DISCUSS
+116	119	CDR	structure_element	From this point of view, a novel approach to design combinatorial antibody libraries would be to cover the range of CDR conformations that may not necessarily coincide with the germline usage in the human repertoire.	DISCUSS
+199	204	human	species	From this point of view, a novel approach to design combinatorial antibody libraries would be to cover the range of CDR conformations that may not necessarily coincide with the germline usage in the human repertoire.	DISCUSS
+80	90	antibodies	protein_type	This would insure more structural diversity, leading to a more diverse panel of antibodies that would bind to a broad spectrum of targets.	DISCUSS