PDB-5mu2: ACC1 Fab fragment in complex with CII583-591 (CG10)

Basic information

• Entry: Database: PDB / ID: 5mu2
• Title: ACC1 Fab fragment in complex with CII583-591 (CG10)

Components

• ACC1 Fab fragment heavy chain
• ACC1 Fab fragment light chain
• synthetic peptide containing the CII583-591 epitope of collagen type II

• Keywords: IMMUNE SYSTEM / anti-citrullinated protein antibody (ACPA) Fab fragment collagen type II
• Function / homology: Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
• Biological species: Mus musculus (house mouse)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
• Authors: Dobritzsch, D. / Holmdahl, R. / Ge, C.

Funding support

Sweden, 6items

Organization	Grant number	Country
Swedish Foundation for Strategic Research	RBa08-0047	Sweden
Swedish Foundation for Strategic Research	RB13-015	Sweden
Knut and Alice Wallenberg Foundation	KAW 2010.0148	Sweden
Swedish Research Council	K2011-52X-07931-25-5	Sweden
Swedish Research Council	2015-02662	Sweden
European Union	IMI 115142

• Citation: Journal: JCI Insight / Year: 2017; Title: Anti-citrullinated protein antibodies cause arthritis by cross-reactivity to joint cartilage.; Authors: Ge, C. / Tong, D. / Liang, B. / Lonnblom, E. / Schneider, N. / Hagert, C. / Viljanen, J. / Ayoglu, B. / Stawikowska, R. / Nilsson, P. / Fields, G.B. / Skogh, T. / Kastbom, A. / Kihlberg, J. / Burkhardt, H. / Dobritzsch, D. / Holmdahl, R.

History

Deposition	Jan 12, 2017	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 19, 2017	Provider: repository / Type: Initial release
Revision 1.1	Sep 13, 2017	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Jan 17, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Assembly

Deposited unit

A: ACC1 Fab fragment heavy chain

B: ACC1 Fab fragment light chain

C: ACC1 Fab fragment heavy chain

D: ACC1 Fab fragment light chain

E: ACC1 Fab fragment heavy chain

F: ACC1 Fab fragment light chain

G: ACC1 Fab fragment heavy chain

H: ACC1 Fab fragment light chain

I: ACC1 Fab fragment heavy chain

J: ACC1 Fab fragment light chain

K: ACC1 Fab fragment heavy chain

L: ACC1 Fab fragment light chain

M: ACC1 Fab fragment heavy chain

N: ACC1 Fab fragment light chain

O: ACC1 Fab fragment heavy chain

P: ACC1 Fab fragment light chain

X: synthetic peptide containing the CII583-591 epitope of collagen type II

Q: synthetic peptide containing the CII583-591 epitope of collagen type II

R: synthetic peptide containing the CII583-591 epitope of collagen type II

S: synthetic peptide containing the CII583-591 epitope of collagen type II

T: synthetic peptide containing the CII583-591 epitope of collagen type II

U: synthetic peptide containing the CII583-591 epitope of collagen type II

V: synthetic peptide containing the CII583-591 epitope of collagen type II

W: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• 398 kDa, 24 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	398,186	24
Polymers	398,186	24
Non-polymers	0	0
Water	7,945	441

1

A: ACC1 Fab fragment heavy chain

B: ACC1 Fab fragment light chain

X: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4680 Å2
ΔGint	-35 kcal/mol
Surface area	19990 Å2
Method	PISA

2

C: ACC1 Fab fragment heavy chain

D: ACC1 Fab fragment light chain

Q: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4670 Å2
ΔGint	-36 kcal/mol
Surface area	20120 Å2
Method	PISA

3

E: ACC1 Fab fragment heavy chain

F: ACC1 Fab fragment light chain

R: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4560 Å2
ΔGint	-32 kcal/mol
Surface area	19930 Å2
Method	PISA

4

G: ACC1 Fab fragment heavy chain

H: ACC1 Fab fragment light chain

S: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4370 Å2
ΔGint	-31 kcal/mol
Surface area	19840 Å2
Method	PISA

5

I: ACC1 Fab fragment heavy chain

J: ACC1 Fab fragment light chain

T: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4710 Å2
ΔGint	-36 kcal/mol
Surface area	19880 Å2
Method	PISA

6

K: ACC1 Fab fragment heavy chain

L: ACC1 Fab fragment light chain

U: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	54	3

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4840 Å2
ΔGint	-36 kcal/mol
Surface area	19900 Å2
Method	PISA

7

M: ACC1 Fab fragment heavy chain

N: ACC1 Fab fragment light chain

V: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	36	2

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4690 Å2
ΔGint	-37 kcal/mol
Surface area	19780 Å2
Method	PISA

8

O: ACC1 Fab fragment heavy chain

P: ACC1 Fab fragment light chain

W: synthetic peptide containing the CII583-591 epitope of collagen type II

Summary:

• defined by author&software
• 49.8 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,773	3
Polymers	49,773	3
Non-polymers	0	0
Water	36	2

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	4480 Å2
ΔGint	-33 kcal/mol
Surface area	19530 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	148.861, 156.008, 156.592
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P212121

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	C
1	2	A
2	2	E
1	3	A
2	3	G
1	4	A
2	4	I
1	5	A
2	5	K
1	6	A
2	6	M
1	7	A
2	7	O
1	8	B
2	8	D
1	9	B
2	9	F
1	10	B
2	10	H
1	11	B
2	11	J
1	12	B
2	12	L
1	13	B
2	13	N
1	14	B
2	14	P
1	15	C
2	15	E
1	16	C
2	16	G
1	17	C
2	17	I
1	18	C
2	18	K
1	19	C
2	19	M
1	20	C
2	20	O
1	21	D
2	21	F
1	22	D
2	22	H
1	23	D
2	23	J
1	24	D
2	24	L
1	25	D
2	25	N
1	26	D
2	26	P
1	27	E
2	27	G
1	28	E
2	28	I
1	29	E
2	29	K
1	30	E
2	30	M
1	31	E
2	31	O
1	32	F
2	32	H
1	33	F
2	33	J
1	34	F
2	34	L
1	35	F
2	35	N
1	36	F
2	36	P
1	37	G
2	37	I
1	38	G
2	38	K
1	39	G
2	39	M
1	40	G
2	40	O
1	41	H
2	41	J
1	42	H
2	42	L
1	43	H
2	43	N
1	44	H
2	44	P
1	45	I
2	45	K
1	46	I
2	46	M
1	47	I
2	47	O
1	48	J
2	48	L
1	49	J
2	49	N
1	50	J
2	50	P
1	51	K
2	51	M
1	52	K
2	52	O
1	53	L
2	53	N
1	54	L
2	54	P
1	55	M
2	55	O
1	56	N
2	56	P
1	57	X
2	57	Q
1	58	X
2	58	R
1	59	X
2	59	S
1	60	X
2	60	T
1	61	X
2	61	U
1	62	X
2	62	V
1	63	Q
2	63	R
1	64	Q
2	64	S
1	65	Q
2	65	T
1	66	R
2	66	S
1	67	R
2	67	T
1	68	R
2	68	U
1	69	R
2	69	V
1	70	S
2	70	T
1	71	S
2	71	U
1	72	S
2	72	V
1	73	T
2	73	U
1	74	T
2	74	V
1	75	U
2	75	V

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	1	GLU	GLU	PRO	PRO	C	C	1 - 218	1 - 218
1	2	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	2	GLU	GLU	PRO	PRO	E	E	1 - 218	1 - 218
1	3	GLU	GLU	ARG	ARG	A	A	1 - 216	1 - 216
2	3	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
1	4	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	4	GLU	GLU	PRO	PRO	I	I	1 - 218	1 - 218
1	5	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	5	GLU	GLU	PRO	PRO	K	K	1 - 218	1 - 218
1	6	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	6	GLU	GLU	PRO	PRO	M	M	1 - 218	1 - 218
1	7	GLU	GLU	GLY	GLY	A	A	1 - 217	1 - 217
2	7	GLU	GLU	GLY	GLY	O	O	1 - 217	1 - 217
1	8	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	8	ASP	ASP	CYS	CYS	D	D	1 - 218	1 - 218
1	9	ASP	ASP	ASN	ASN	B	B	1 - 216	1 - 216
2	9	ASP	ASP	ASN	ASN	F	F	1 - 216	1 - 216
1	10	ASP	ASP	ASN	ASN	B	B	1 - 216	1 - 216
2	10	ASP	ASP	ASN	ASN	H	H	1 - 216	1 - 216
1	11	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	11	ASP	ASP	CYS	CYS	J	J	1 - 218	1 - 218
1	12	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	12	ASP	ASP	CYS	CYS	L	L	1 - 218	1 - 218
1	13	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	13	ASP	ASP	CYS	CYS	N	N	1 - 218	1 - 218
1	14	ASP	ASP	ASN	ASN	B	B	1 - 216	1 - 216
2	14	ASP	ASP	ASN	ASN	P	P	1 - 216	1 - 216
1	15	GLU	GLU	PRO	PRO	C	C	1 - 218	1 - 218
2	15	GLU	GLU	PRO	PRO	E	E	1 - 218	1 - 218
1	16	GLU	GLU	ARG	ARG	C	C	1 - 216	1 - 216
2	16	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
1	17	GLU	GLU	PRO	PRO	C	C	1 - 218	1 - 218
2	17	GLU	GLU	PRO	PRO	I	I	1 - 218	1 - 218
1	18	GLU	GLU	PRO	PRO	C	C	1 - 218	1 - 218
2	18	GLU	GLU	PRO	PRO	K	K	1 - 218	1 - 218
1	19	GLU	GLU	PRO	PRO	C	C	1 - 218	1 - 218
2	19	GLU	GLU	PRO	PRO	M	M	1 - 218	1 - 218
1	20	GLU	GLU	GLY	GLY	C	C	1 - 217	1 - 217
2	20	GLU	GLU	GLY	GLY	O	O	1 - 217	1 - 217
1	21	ASP	ASP	ASN	ASN	D	D	1 - 216	1 - 216
2	21	ASP	ASP	ASN	ASN	F	F	1 - 216	1 - 216
1	22	ASP	ASP	ASN	ASN	D	D	1 - 216	1 - 216
2	22	ASP	ASP	ASN	ASN	H	H	1 - 216	1 - 216
1	23	ASP	ASP	CYS	CYS	D	D	1 - 218	1 - 218
2	23	ASP	ASP	CYS	CYS	J	J	1 - 218	1 - 218
1	24	ASP	ASP	CYS	CYS	D	D	1 - 218	1 - 218
2	24	ASP	ASP	CYS	CYS	L	L	1 - 218	1 - 218
1	25	ASP	ASP	CYS	CYS	D	D	1 - 218	1 - 218
2	25	ASP	ASP	CYS	CYS	N	N	1 - 218	1 - 218
1	26	ASP	ASP	ASN	ASN	D	D	1 - 216	1 - 216
2	26	ASP	ASP	ASN	ASN	P	P	1 - 216	1 - 216
1	27	GLU	GLU	ARG	ARG	E	E	1 - 216	1 - 216
2	27	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
1	28	GLU	GLU	PRO	PRO	E	E	1 - 218	1 - 218
2	28	GLU	GLU	PRO	PRO	I	I	1 - 218	1 - 218
1	29	GLU	GLU	PRO	PRO	E	E	1 - 218	1 - 218
2	29	GLU	GLU	PRO	PRO	K	K	1 - 218	1 - 218
1	30	GLU	GLU	PRO	PRO	E	E	1 - 218	1 - 218
2	30	GLU	GLU	PRO	PRO	M	M	1 - 218	1 - 218
1	31	GLU	GLU	ARG	ARG	E	E	1 - 216	1 - 216
2	31	GLU	GLU	ARG	ARG	O	O	1 - 216	1 - 216
1	32	ASP	ASP	GLU	GLU	F	F	1 - 217	1 - 217
2	32	ASP	ASP	GLU	GLU	H	H	1 - 217	1 - 217
1	33	ASP	ASP	ASN	ASN	F	F	1 - 216	1 - 216
2	33	ASP	ASP	ASN	ASN	J	J	1 - 216	1 - 216
1	34	ASP	ASP	ASN	ASN	F	F	1 - 216	1 - 216
2	34	ASP	ASP	ASN	ASN	L	L	1 - 216	1 - 216
1	35	ASP	ASP	ASN	ASN	F	F	1 - 216	1 - 216
2	35	ASP	ASP	ASN	ASN	N	N	1 - 216	1 - 216
1	36	ASP	ASP	GLU	GLU	F	F	1 - 217	1 - 217
2	36	ASP	ASP	GLU	GLU	P	P	1 - 217	1 - 217
1	37	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
2	37	GLU	GLU	ARG	ARG	I	I	1 - 216	1 - 216
1	38	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
2	38	GLU	GLU	ARG	ARG	K	K	1 - 216	1 - 216
1	39	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
2	39	GLU	GLU	ARG	ARG	M	M	1 - 216	1 - 216
1	40	GLU	GLU	ARG	ARG	G	G	1 - 216	1 - 216
2	40	GLU	GLU	ARG	ARG	O	O	1 - 216	1 - 216
1	41	ASP	ASP	ASN	ASN	H	H	1 - 216	1 - 216
2	41	ASP	ASP	ASN	ASN	J	J	1 - 216	1 - 216
1	42	ASP	ASP	ASN	ASN	H	H	1 - 216	1 - 216
2	42	ASP	ASP	ASN	ASN	L	L	1 - 216	1 - 216
1	43	ASP	ASP	ASN	ASN	H	H	1 - 216	1 - 216
2	43	ASP	ASP	ASN	ASN	N	N	1 - 216	1 - 216
1	44	ASP	ASP	GLU	GLU	H	H	1 - 217	1 - 217
2	44	ASP	ASP	GLU	GLU	P	P	1 - 217	1 - 217
1	45	GLU	GLU	PRO	PRO	I	I	1 - 218	1 - 218
2	45	GLU	GLU	PRO	PRO	K	K	1 - 218	1 - 218
1	46	GLU	GLU	PRO	PRO	I	I	1 - 218	1 - 218
2	46	GLU	GLU	PRO	PRO	M	M	1 - 218	1 - 218
1	47	GLU	GLU	GLY	GLY	I	I	1 - 217	1 - 217
2	47	GLU	GLU	GLY	GLY	O	O	1 - 217	1 - 217
1	48	ASP	ASP	CYS	CYS	J	J	1 - 218	1 - 218
2	48	ASP	ASP	CYS	CYS	L	L	1 - 218	1 - 218
1	49	ASP	ASP	CYS	CYS	J	J	1 - 218	1 - 218
2	49	ASP	ASP	CYS	CYS	N	N	1 - 218	1 - 218
1	50	ASP	ASP	ASN	ASN	J	J	1 - 216	1 - 216
2	50	ASP	ASP	ASN	ASN	P	P	1 - 216	1 - 216
1	51	GLU	GLU	PRO	PRO	K	K	1 - 218	1 - 218
2	51	GLU	GLU	PRO	PRO	M	M	1 - 218	1 - 218
1	52	GLU	GLU	GLY	GLY	K	K	1 - 217	1 - 217
2	52	GLU	GLU	GLY	GLY	O	O	1 - 217	1 - 217
1	53	ASP	ASP	CYS	CYS	L	L	1 - 218	1 - 218
2	53	ASP	ASP	CYS	CYS	N	N	1 - 218	1 - 218
1	54	ASP	ASP	ASN	ASN	L	L	1 - 216	1 - 216
2	54	ASP	ASP	ASN	ASN	P	P	1 - 216	1 - 216
1	55	GLU	GLU	GLY	GLY	M	M	1 - 217	1 - 217
2	55	GLU	GLU	GLY	GLY	O	O	1 - 217	1 - 217
1	56	ASP	ASP	ASN	ASN	N	N	1 - 216	1 - 216
2	56	ASP	ASP	ASN	ASN	P	P	1 - 216	1 - 216
1	57	HYP	HYP	ILE	ILE	X	Q	9 - 21	9 - 21
2	57	HYP	HYP	ILE	ILE	Q	R	9 - 21	9 - 21
1	58	HYP	HYP	PRO	PRO	X	Q	9 - 23	9 - 23
2	58	HYP	HYP	PRO	PRO	R	S	9 - 23	9 - 23
1	59	HYP	HYP	PRO	PRO	X	Q	9 - 23	9 - 23
2	59	HYP	HYP	PRO	PRO	S	T	9 - 23	9 - 23
1	60	PRO	PRO	GLY	GLY	X	Q	11 - 22	11 - 22
2	60	PRO	PRO	GLY	GLY	T	U	11 - 22	11 - 22
1	61	HYP	HYP	GLY	GLY	X	Q	12 - 22	12 - 22
2	61	HYP	HYP	GLY	GLY	U	V	12 - 22	12 - 22
1	62	HYP	HYP	GLY	GLY	X	Q	12 - 22	12 - 22
2	62	HYP	HYP	GLY	GLY	V	W	12 - 22	12 - 22
1	63	HYP	HYP	ILE	ILE	Q	R	9 - 21	9 - 21
2	63	HYP	HYP	ILE	ILE	R	S	9 - 21	9 - 21
1	64	HYP	HYP	ILE	ILE	Q	R	9 - 21	9 - 21
2	64	HYP	HYP	ILE	ILE	S	T	9 - 21	9 - 21
1	65	PRO	PRO	ILE	ILE	Q	R	11 - 21	11 - 21
2	65	PRO	PRO	ILE	ILE	T	U	11 - 21	11 - 21
1	66	HYP	HYP	PRO	PRO	R	S	9 - 23	9 - 23
2	66	HYP	HYP	PRO	PRO	S	T	9 - 23	9 - 23
1	67	PRO	PRO	GLY	GLY	R	S	11 - 22	11 - 22
2	67	PRO	PRO	GLY	GLY	T	U	11 - 22	11 - 22
1	68	HYP	HYP	GLY	GLY	R	S	12 - 22	12 - 22
2	68	HYP	HYP	GLY	GLY	U	V	12 - 22	12 - 22
1	69	HYP	HYP	GLY	GLY	R	S	12 - 22	12 - 22
2	69	HYP	HYP	GLY	GLY	V	W	12 - 22	12 - 22
1	70	PRO	PRO	GLY	GLY	S	T	11 - 22	11 - 22
2	70	PRO	PRO	GLY	GLY	T	U	11 - 22	11 - 22
1	71	HYP	HYP	GLY	GLY	S	T	12 - 22	12 - 22
2	71	HYP	HYP	GLY	GLY	U	V	12 - 22	12 - 22
1	72	HYP	HYP	GLY	GLY	S	T	12 - 22	12 - 22
2	72	HYP	HYP	GLY	GLY	V	W	12 - 22	12 - 22
1	73	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
2	73	HYP	HYP	GLY	GLY	U	V	12 - 22	12 - 22
1	74	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
2	74	HYP	HYP	GLY	GLY	V	W	12 - 22	12 - 22
1	75	HYP	HYP	GLY	GLY	U	V	12 - 22	12 - 22
2	75	HYP	HYP	GLY	GLY	V	W	12 - 22	12 - 22

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
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68
69
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73
74
75

Components

#1: Antibody

A C E G I K M O
ACC1 Fab fragment heavy chain

Details:

Mass: 23353.164 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: B cell hybridoma / Variant: B10.RIII.Cia5

#2: Antibody

B D F H J L N P
ACC1 Fab fragment light chain

Details:

Mass: 23721.199 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: B cell hybridoma / Variant: B10.RIII.Cia5

#3: Protein/peptide

X Q R S T U V W
synthetic peptide containing the CII583-591 epitope of collagen type II

Details:

Mass: 2698.919 Da / Num. of mol.: 8 / Source method: obtained synthetically
Details: the synthesized peptide is a triple-helical homotrimer of the above provided sequence, but only a single alpha-chain is bound to ACC1 in the crystal structure
Source: (synth.) Mus musculus (house mouse)

#4: Water

ChemComp-HOH / water / Water

Details:

Mass: 18.015 Da / Num. of mol.: 441 / Source method: isolated from a natural source / Formula: H₂O

Experimental details

Experiment

• Experiment: Method: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

• Crystal: Density Matthews: 2.36 ų/Da / Density % sol: 47.91 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 ; Details: 20% (w/v) PEG3350, 0.1 M Bistris-Propane pH 7.5, 0.2 M sodium acetate

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å
• Detector: Type: PILATUS 6 / Detector: PIXEL / Date: Oct 16, 2014
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.9184 Å / Relative weight: 1
• Reflection: Resolution: 2.7→49.09 Å / Num. obs: 100498 / % possible obs: 100 % / Redundancy: 6.2 % / B_iso Wilson estimate: 46.4 Ų / R_merge(I) obs: 0.121 / Net I/σ(I): 12.1
• Reflection shell: Resolution: 2.7→2.75 Å / Redundancy: 6.3 % / R_merge(I) obs: 0.799 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 4899 / % possible all: 100

Processing

Software

Name	Version	Classification
REFMAC	5.8.0155	refinement
XDS		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 5MU0

5mu0

Resolution: 2.7→49.09 Å / Cor.coef. F_o:F_c: 0.933 / Cor.coef. F_o:F_c free: 0.92 / SU B: 31.297 / SU ML: 0.292 / Cross valid method: THROUGHOUT / ESU R Free: 0.336 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.22845	4864	4.8 %	RANDOM
Rwork	0.20629	-	-	-
obs	0.20737	95561	99.93 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 57.939 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	-0.2 Å2	-0 Å2	-0 Å2
2-	-	-0.57 Å2	0 Å2
3-	-	-	0.77 Å2

Refinement step

Cycle: 1 / Resolution: 2.7→49.09 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	27006	0	0	441	27447

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.02	27684
X-RAY DIFFRACTION	r_bond_other_d	0.002	0.02	25288
X-RAY DIFFRACTION	r_angle_refined_deg	1.484	1.947	37631
X-RAY DIFFRACTION	r_angle_other_deg	1.005	3	58617
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.743	5	3544
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.399	24.444	1080
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.918	15	4355
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.315	15	112
X-RAY DIFFRACTION	r_chiral_restr	0.111	0.2	4213
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.021	31216
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	6112
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	0.832	2.526	14266
X-RAY DIFFRACTION	r_mcbond_other	0.832	2.526	14265
X-RAY DIFFRACTION	r_mcangle_it	1.482	3.784	17780
X-RAY DIFFRACTION	r_mcangle_other	1.481	3.784	17781
X-RAY DIFFRACTION	r_scbond_it	0.78	2.568	13418
X-RAY DIFFRACTION	r_scbond_other	0.78	2.568	13419
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	1.354	3.821	19852
X-RAY DIFFRACTION	r_long_range_B_refined	2.705	28.126	27879
X-RAY DIFFRACTION	r_long_range_B_other	2.705	28.126	27880
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	12870	0.06
1	2	C	12870	0.06
2	1	A	12856	0.06
2	2	E	12856	0.06
3	1	A	12784	0.05
3	2	G	12784	0.05
4	1	A	12908	0.05
4	2	I	12908	0.05
5	1	A	12926	0.05
5	2	K	12926	0.05
6	1	A	12918	0.06
6	2	M	12918	0.06
7	1	A	12878	0.05
7	2	O	12878	0.05
8	1	B	13324	0.05
8	2	D	13324	0.05
9	1	B	13346	0.03
9	2	F	13346	0.03
10	1	B	13276	0.05
10	2	H	13276	0.05
11	1	B	13372	0.04
11	2	J	13372	0.04
12	1	B	13420	0.04
12	2	L	13420	0.04
13	1	B	13420	0.03
13	2	N	13420	0.03
14	1	B	13208	0.05
14	2	P	13208	0.05
15	1	C	12804	0.07
15	2	E	12804	0.07
16	1	C	12716	0.06
16	2	G	12716	0.06
17	1	C	13062	0.06
17	2	I	13062	0.06
18	1	C	12832	0.07
18	2	K	12832	0.07
19	1	C	12926	0.06
19	2	M	12926	0.06
20	1	C	12798	0.06
20	2	O	12798	0.06
21	1	D	13270	0.05
21	2	F	13270	0.05
22	1	D	13226	0.05
22	2	H	13226	0.05
23	1	D	13368	0.05
23	2	J	13368	0.05
24	1	D	13362	0.05
24	2	L	13362	0.05
25	1	D	13330	0.05
25	2	N	13330	0.05
26	1	D	13186	0.06
26	2	P	13186	0.06
27	1	E	12746	0.06
27	2	G	12746	0.06
28	1	E	12864	0.05
28	2	I	12864	0.05
29	1	E	12758	0.07
29	2	K	12758	0.07
30	1	E	12928	0.04
30	2	M	12928	0.04
31	1	E	12812	0.05
31	2	O	12812	0.05
32	1	F	13346	0.05
32	2	H	13346	0.05
33	1	F	13318	0.04
33	2	J	13318	0.04
34	1	F	13326	0.04
34	2	L	13326	0.04
35	1	F	13342	0.03
35	2	N	13342	0.03
36	1	F	13302	0.05
36	2	P	13302	0.05
37	1	G	12772	0.06
37	2	I	12772	0.06
38	1	G	12724	0.06
38	2	K	12724	0.06
39	1	G	12796	0.05
39	2	M	12796	0.05
40	1	G	12826	0.04
40	2	O	12826	0.04
41	1	H	13344	0.04
41	2	J	13344	0.04
42	1	H	13326	0.04
42	2	L	13326	0.04
43	1	H	13282	0.05
43	2	N	13282	0.05
44	1	H	13328	0.05
44	2	P	13328	0.05
45	1	I	12884	0.05
45	2	K	12884	0.05
46	1	I	12988	0.04
46	2	M	12988	0.04
47	1	I	12854	0.05
47	2	O	12854	0.05
48	1	J	13452	0.03
48	2	L	13452	0.03
49	1	J	13392	0.04
49	2	N	13392	0.04
50	1	J	13286	0.04
50	2	P	13286	0.04
51	1	K	12920	0.05
51	2	M	12920	0.05
52	1	K	12836	0.05
52	2	O	12836	0.05
53	1	L	13400	0.04
53	2	N	13400	0.04
54	1	L	13312	0.04
54	2	P	13312	0.04
55	1	M	12918	0.04
55	2	O	12918	0.04
56	1	N	13208	0.05
56	2	P	13208	0.05
57	1	X	444	0.07
57	2	Q	444	0.07
58	1	X	514	0.15
58	2	R	514	0.15
59	1	X	502	0.15
59	2	S	502	0.15
60	1	X	416	0.09
60	2	T	416	0.09
61	1	X	374	0.03
61	2	U	374	0.03
62	1	X	362	0.13
62	2	V	362	0.13
63	1	Q	444	0.11
63	2	R	444	0.11
64	1	Q	440	0.1
64	2	S	440	0.1
65	1	Q	384	0.08
65	2	T	384	0.08
66	1	R	504	0.11
66	2	S	504	0.11
67	1	R	418	0.09
67	2	T	418	0.09
68	1	R	374	0.03
68	2	U	374	0.03
69	1	R	362	0.13
69	2	V	362	0.13
70	1	S	430	0.01
70	2	T	430	0.01
71	1	S	362	0.1
71	2	U	362	0.1
72	1	S	376	0.09
72	2	V	376	0.09
73	1	T	364	0.1
73	2	U	364	0.1
74	1	T	380	0.09
74	2	V	380	0.09
75	1	U	364	0.13
75	2	V	364	0.13

LS refinement shell

Resolution: 2.7→2.77 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.326	325	-
Rwork	0.319	6989	-
obs	-	-	99.97 %

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°2)	L12 (°2)	L13 (°2)	L22 (°2)	L23 (°2)	L33 (°2)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å2)	T12 (Å2)	T13 (Å2)	T22 (Å2)	T23 (Å2)	T33 (Å2)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	2.2118	-1.7308	-1.0008	3.4494	-0.1613	5.2555	0.0211	-0.2031	0.3568	-0.0261	0.1122	-0.6087	0.1076	0.2752	-0.1333	0.0326	-0.0037	0.0045	0.0545	-0.0849	0.2206	5.7903	-40.5456	30.7431
2	2.334	-0.705	-0.7637	6.7058	-0.8271	3.2879	0.0016	0.2271	0.2319	-0.5743	-0.2936	-0.8286	0.1163	0.0439	0.2921	0.2935	0.0063	0.2612	0.1206	0.0826	0.4659	5.1385	-17.3093	8.2228
3	1.773	-0.1209	-0.1088	3.8871	-1.6563	2.4633	0.0196	0.2089	0.2406	-0.4896	0.0702	-0.0685	-0.0111	-0.0726	-0.0898	0.1299	-0.0329	0.0703	0.0735	-0.0577	0.1977	-11.7795	-24.2373	17.8278
4	3.9287	-1.9387	-0.4833	4.6642	1.6301	6.4051	0.2035	0.0295	-0.0594	-0.2084	-0.1159	0.4394	-0.3654	-0.5345	-0.0876	0.1498	0.027	-0.0208	0.1281	0.0412	0.0716	-78.2931	4.5932	34.2511
5	2.9833	-1.7556	0.7677	6.8896	0.7782	4.8477	-0.0694	0.069	-0.3375	-0.1169	-0.0275	0.2712	-0.0806	-0.9164	0.0968	0.1466	-0.0383	0.0033	0.442	0.0156	0.0964	-79.1072	-17.6233	10.9711
6	3.6034	-2.4755	-1.8506	4.3612	2.4192	3.781	-0.1627	-0.7939	0.1483	0.4527	0.3837	-0.2681	0.2525	0.3634	-0.221	0.1947	-0.0434	-0.0945	0.2091	0.0036	0.049	-58.2182	-5.3624	37.7993
7	1.5632	0.3451	2.0015	1.0496	0.5301	7.4409	-0.0842	0.22	-0.0255	-0.2354	-0.0149	-0.1391	-0.0532	0.0291	0.0991	0.1796	-0.0206	-0.0215	0.0531	0.0199	0.12	-64.9386	-17.8501	4.3859
8	4.9467	-0.2551	0.3079	3.3868	-1.2997	4.5453	-0.1097	0.2492	-0.2416	-0.2065	0.0565	-0.3132	0.2831	-0.3896	0.0532	0.052	-0.0604	-0.0161	0.0898	0.0303	0.1086	-46.6756	-1.9363	12.3812
9	6.4814	1.3785	-2.1629	2.165	0.6577	5.5464	-0.1949	0.3704	0.0615	-0.4653	0.2742	-0.498	-0.2423	-0.1175	-0.0793	0.1791	-0.0496	0.0931	0.1699	0.0895	0.3309	-42.0061	12.0344	-16.0082
10	4.1458	1.755	-0.7581	3.3742	-1.2407	4.0042	0.0115	-0.2124	0.0658	0.1367	-0.156	-0.7722	0.1453	0.3308	0.1445	0.0336	0.0082	-0.0937	0.0799	0.0111	0.3836	-30.4085	12.5909	18.0693
11	1.6598	0.5217	1.8381	3.7291	0.3902	5.5146	-0.2933	0.2584	0.5386	-1.0192	0.2409	-0.0836	-0.9027	-0.1281	0.0525	0.4963	-0.0741	0.101	0.2208	0.1812	0.5419	-38.7495	27.7725	-13.8767
12	5.496	0.1563	0.8448	5.0879	1.479	5.3245	0.0744	0.4898	0.3225	-0.3753	-0.06	-0.1653	-0.0678	0.4919	-0.0144	0.0503	0.0343	0.0604	0.1123	0.0556	0.1354	-27.9371	-33.7367	11.0392
13	3.2645	1.955	-0.3443	3.0094	2.719	5.4912	-0.453	0.4901	0.6335	-0.7944	0.6321	0.3498	0.3035	0.6734	-0.1791	1.6195	0.1921	-0.2323	0.3039	-0.0193	0.7066	-33.6725	-49.0556	-13.1377
14	10.6207	5.7335	7.3003	6.1972	6.5771	7.3385	0.2954	0.6408	1.3756	-0.3181	-0.1994	-0.2403	0.0597	-0.1059	-0.096	1.4038	-0.0464	-0.371	0.7719	0.3752	1.0016	-40.1761	-45.6536	-22.5657
15	3.4593	1.52	1.2947	4.4318	0.9034	3.4752	0.5282	-0.5066	-0.3812	0.0675	-0.263	0.3254	0.3874	-0.5618	-0.2652	0.1919	-0.0331	-0.0673	0.1733	0.077	0.2325	-43.831	-50.1813	16.0275
16	4.985	0.0476	-2.1258	1.0828	0.1982	4.1723	-0.2186	0.7628	-0.1982	-1.1562	0.1716	-0.2044	0.898	0.3347	0.047	1.7271	0.0778	-0.0327	0.419	-0.1664	0.4927	-36.8032	-64.7655	-15.7354
17	5.042	-1.0381	-0.4667	2.0287	-0.1011	1.4461	-0.0195	-0.0699	-0.0989	-0.1502	0.0507	0.3044	0.0324	-0.2177	-0.0312	0.1505	-0.0329	-0.0455	0.0708	-0.0167	0.0809	-13.1222	2.8303	49.7972
18	5.7577	-0.4547	-1.4735	2.1369	-0.6951	2.2774	0.1109	0.3293	0.4443	-0.0356	0.0179	0.3188	-0.5242	-0.3166	-0.1288	0.2846	0.0045	-0.0597	0.1235	0.0093	0.122	-15.5028	19.3979	42.3595
19	5.6756	-0.7798	1.3659	4.549	0.8681	2.706	0.1007	0.3083	0.0154	-0.4599	-0.013	-0.4793	-0.1652	0.157	-0.0877	0.1135	0.0023	-0.0577	0.0231	0.0189	0.412	-41.2065	37.0409	8.5662
20	2.5191	-0.7934	0.7628	7.5041	0.2663	3.4151	0.178	0.3121	0.1811	-0.3843	-0.2511	0.0934	-0.1374	-0.0012	0.0731	0.2431	0.0693	-0.1138	0.2307	0.0447	0.3518	-62.5921	59.558	-0.4412
21	2.7295	-1.5494	0.5237	2.8242	-0.8006	1.8843	-0.0589	-0.042	0.3003	0.2744	0.0104	-0.0213	-0.1122	-0.1482	0.0485	0.2335	-0.04	-0.0977	0.0377	-0.0379	0.4021	-60.5711	53.0492	19.0217
22	4.2241	1.6479	0.0773	1.7331	0.0357	1.2023	-0.221	0.1314	0.2676	-0.1842	0.0547	0.2447	-0.3098	-0.2216	0.1663	0.4713	0.0903	0.0089	0.1337	-0.1289	0.2334	-86.5839	37.4708	28.659
23	3.2849	0.8187	0.7999	1.9772	0.1496	1.7087	-0.0815	-0.3267	-0.2041	0.2022	-0.0716	0.0789	-0.1081	-0.2894	0.1531	0.3443	0.0681	0.1152	0.2217	-0.1007	0.1639	-87.8495	21.3316	37.6012
24	3.971	2.2637	0.2	3.1286	-0.8978	1.6266	-0.0045	-0.687	-0.4376	0.5484	-0.0082	-0.4262	-0.1545	-0.2895	0.0128	0.2767	0.1657	-0.0117	0.3314	-0.0032	0.335	25.5842	-7.453	72.3443
25	4.0765	1.7751	0.0572	3.2742	-0.7956	2.019	-0.0159	-0.2573	-0.4389	-0.0881	0.0903	-0.2102	0.0286	-0.1137	-0.0744	0.1009	0.0624	0.0107	0.1328	-0.0715	0.2651	14.8307	-12.1046	57.8852
26	8.8167	5.0332	-3.6281	7.6766	3.077	7.0165	0.9101	-1.7382	0.0724	0.9077	-0.046	-0.7247	0.0156	1.6907	-0.864	0.5084	0.0498	-0.0054	0.7052	-0.0399	0.2208	-67.7162	1.5958	51.7466
27	6.6722	-0.8955	0.7999	2.1348	3.2294	5.6331	-0.0685	-0.6862	-0.1377	0.5185	0.1966	-0.0382	0.8258	0.1428	-0.1282	0.2872	-0.0206	-0.0739	0.3672	0.0386	0.3785	-32.9447	-3.4227	26.6636
28	8.0525	1.7917	3.6771	9.9069	-9.3333	12.5177	0.4508	-2.1303	0.5724	1.7336	0.0417	0.8235	-1.5348	-1.5254	-0.4925	0.4115	0.0019	0.1414	0.6056	-0.1407	0.261	-39.9997	-32.4631	26.8638
29	11.7541	0.3568	-10.4509	6.1218	-2.1196	9.8459	0.2924	0.5408	-0.8724	-1.6389	-1.3263	-0.9379	0.2582	0.014	1.0339	0.5081	0.3627	0.2577	0.8045	-0.042	0.3001	9.0257	-1.2804	30.1718
30	6.3457	0.3515	1.0249	0.0266	0.0592	0.1845	-0.1026	0.1145	-0.3158	-0.0001	0.0596	-0.0273	-0.006	0.0534	0.043	0.4419	0.0509	-0.0688	0.4133	0.009	0.58	-28.4892	37.8189	22.8889
31	2.7077	2.9199	4.3039	7.536	4.2233	6.9486	0.0626	0.1157	-0.0781	0.086	0.0069	-0.6678	-0.0852	0.2651	-0.0696	0.5242	-0.0764	-0.0082	0.3537	-0.0634	0.3652	-64.6496	44.2471	47.1628
32	5.3833	-4.951	-2.1538	23.9658	-10.8264	10.946	-0.212	0.3802	0.3194	-0.4417	0.2215	-0.3437	-0.1005	0.3091	-0.0095	0.3546	-0.264	0.0066	0.5834	-0.0139	0.344	43.1618	3.2497	53.3213
33	11.1382	0.029	-2.6582	7.0172	-4.735	5.7843	0.0471	-1.1563	-0.4988	0.4211	-0.0207	0.3802	0.3082	0.3611	-0.0264	0.4005	0.0148	0.01	0.3189	-0.0503	0.2275	-4.3303	-38.1597	49.2875

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 120
2	X-RAY DIFFRACTION	2	A	121 - 218
3	X-RAY DIFFRACTION	3	B	1 - 218
4	X-RAY DIFFRACTION	4	C	1 - 114
5	X-RAY DIFFRACTION	5	C	115 - 218
6	X-RAY DIFFRACTION	6	D	1 - 104
7	X-RAY DIFFRACTION	7	D	105 - 218
8	X-RAY DIFFRACTION	8	E	1 - 112
9	X-RAY DIFFRACTION	9	E	113 - 218
10	X-RAY DIFFRACTION	10	F	1 - 105
11	X-RAY DIFFRACTION	11	F	106 - 217
12	X-RAY DIFFRACTION	12	G	1 - 109
13	X-RAY DIFFRACTION	13	G	110 - 185
14	X-RAY DIFFRACTION	14	G	186 - 216
15	X-RAY DIFFRACTION	15	H	1 - 120
16	X-RAY DIFFRACTION	16	H	121 - 217
17	X-RAY DIFFRACTION	17	I	1 - 218
18	X-RAY DIFFRACTION	18	J	1 - 218
19	X-RAY DIFFRACTION	19	K	1 - 117
20	X-RAY DIFFRACTION	20	K	118 - 218
21	X-RAY DIFFRACTION	21	L	1 - 218
22	X-RAY DIFFRACTION	22	M	1 - 218
23	X-RAY DIFFRACTION	23	N	1 - 218
24	X-RAY DIFFRACTION	24	O	1 - 217
25	X-RAY DIFFRACTION	25	P	1 - 217
26	X-RAY DIFFRACTION	26	Q	8 - 22
27	X-RAY DIFFRACTION	27	R	9 - 23
28	X-RAY DIFFRACTION	28	S	9 - 23
29	X-RAY DIFFRACTION	29	T	11 - 23
30	X-RAY DIFFRACTION	30	U	12 - 26
31	X-RAY DIFFRACTION	31	V	12 - 23
32	X-RAY DIFFRACTION	32	W	13 - 21
33	X-RAY DIFFRACTION	33	X	9 - 23