PDB-5mv3: ACC1 Fab fragment in complex with CII583-591 (CG10)

Basic information

• Entry: Database: PDB / ID: 5mv3
• Title: ACC1 Fab fragment in complex with CII583-591 (CG10)

Components

• (heavy chain of ACC1 Fab fragment) x 2
• light chain of ACC1 Fab fragment
• synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) 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

Function:

Non-integrin membrane-ECM interactions / Extracellular matrix organization / NCAM1 interactions / Signaling by PDGF / Collagen biosynthesis and modifying enzymes / Collagen chain trimerization / collagen type II trimer / collagen type XI trimer / MET activates PTK2 signaling / anterior head development / Collagen degradation / Assembly of collagen fibrils and other multimeric structures / embryonic skeletal joint morphogenesis / otic vesicle development / ECM proteoglycans / proteoglycan metabolic process / extracellular matrix structural constituent conferring tensile strength / platelet-derived growth factor binding / Integrin cell surface interactions / cartilage development involved in endochondral bone morphogenesis / notochord development / limb bud formation / limb morphogenesis / tissue homeostasis / MHC class II protein binding / cellular response to BMP stimulus / endochondral ossification / collagen trimer / collagen fibril organization / cartilage development / skeletal system morphogenesis / proteoglycan binding / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / inner ear morphogenesis / cartilage condensation / roof of mouth development / inner ear development / basement membrane / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / chondrocyte differentiation / heart morphogenesis / extrinsic apoptotic signaling pathway in absence of ligand / visual perception / extracellular matrix / ossification / central nervous system development / skeletal system development / sensory perception of sound / bone development / regulation of gene expression / collagen-containing extracellular matrix / protein homodimerization activity / extracellular space / identical protein binding / metal ion binding / cytoplasm

Domain/homology:

Fibrillar collagen, C-terminal / Fibrillar collagen C-terminal domain / Fibrillar collagen C-terminal non-collagenous (NC1) domain profile. / Fibrillar collagens C-terminal domain / von Willebrand factor type C domain / VWFC domain signature. / VWFC domain profile. / von Willebrand factor (vWF) type C domain / VWFC domain / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta

Component:

Collagen alpha-1(II) chain

• Biological species: Mus musculus (house mouse)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å
• Authors: Dobritzsch, D. / Holmdahl, R. / Ge, C.

Funding support

Sweden, 5items

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, 2015-02662 , K2009-75SX-21029-01-3, K2012-75SX-22072-01-3	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 15, 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: heavy chain of ACC1 Fab fragment

B: light chain of ACC1 Fab fragment

X: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

C: heavy chain of ACC1 Fab fragment

D: light chain of ACC1 Fab fragment

E: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

F: heavy chain of ACC1 Fab fragment

G: light chain of ACC1 Fab fragment

H: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

I: heavy chain of ACC1 Fab fragment

J: light chain of ACC1 Fab fragment

K: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

L: heavy chain of ACC1 Fab fragment

M: light chain of ACC1 Fab fragment

N: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

O: heavy chain of ACC1 Fab fragment

P: light chain of ACC1 Fab fragment

Q: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

R: heavy chain of ACC1 Fab fragment

S: light chain of ACC1 Fab fragment

T: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

U: heavy chain of ACC1 Fab fragment

V: light chain of ACC1 Fab fragment

W: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,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)	398,401	24
Polymers	398,401	24
Non-polymers	0	0
Water	0

1

A: heavy chain of ACC1 Fab fragment

B: light chain of ACC1 Fab fragment

X: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4750 Å2
ΔGint	-36 kcal/mol
Surface area	20150 Å2
Method	PISA

2

C: heavy chain of ACC1 Fab fragment

D: light chain of ACC1 Fab fragment

E: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4650 Å2
ΔGint	-32 kcal/mol
Surface area	19870 Å2
Method	PISA

3

F: heavy chain of ACC1 Fab fragment

G: light chain of ACC1 Fab fragment

H: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4620 Å2
ΔGint	-32 kcal/mol
Surface area	19940 Å2
Method	PISA

4

I: heavy chain of ACC1 Fab fragment

J: light chain of ACC1 Fab fragment

K: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

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	20130 Å2
Method	PISA

5

L: heavy chain of ACC1 Fab fragment

M: light chain of ACC1 Fab fragment

N: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by software
• 50 kDa, 3 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	49,988	3
Polymers	49,988	3
Non-polymers	0	0
Water	0

Symmetry operations:

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

Calculated values:

Buried area	4680 Å2
ΔGint	-34 kcal/mol
Surface area	20300 Å2
Method	PISA

6

O: heavy chain of ACC1 Fab fragment

P: light chain of ACC1 Fab fragment

Q: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4590 Å2
ΔGint	-32 kcal/mol
Surface area	19830 Å2
Method	PISA

7

R: heavy chain of ACC1 Fab fragment

S: light chain of ACC1 Fab fragment

T: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4730 Å2
ΔGint	-36 kcal/mol
Surface area	19890 Å2
Method	PISA

8

U: heavy chain of ACC1 Fab fragment

V: light chain of ACC1 Fab fragment

W: synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II,

Summary:

• defined by 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	0

Symmetry operations:

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

Calculated values:

Buried area	4830 Å2
ΔGint	-34 kcal/mol
Surface area	20120 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	87.353, 92.844, 121.706
Angle α, β, γ (deg.)	92.50, 106.53, 104.31
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	C
1	2	A
2	2	F
1	3	A
2	3	I
1	4	A
2	4	L
1	5	A
2	5	O
1	6	A
2	6	R
1	7	A
2	7	U
1	8	B
2	8	D
1	9	B
2	9	G
1	10	B
2	10	J
1	11	B
2	11	M
1	12	B
2	12	P
1	13	B
2	13	S
1	14	B
2	14	V
1	15	X
2	15	E
1	16	X
2	16	H
1	17	X
2	17	K
1	18	X
2	18	N
1	19	X
2	19	Q
1	20	X
2	20	T
1	21	X
2	21	W
1	22	C
2	22	F
1	23	C
2	23	I
1	24	C
2	24	L
1	25	C
2	25	O
1	26	C
2	26	R
1	27	C
2	27	U
1	28	D
2	28	G
1	29	D
2	29	J
1	30	D
2	30	M
1	31	D
2	31	P
1	32	D
2	32	S
1	33	D
2	33	V
1	34	E
2	34	H
1	35	E
2	35	K
1	36	E
2	36	N
1	37	E
2	37	Q
1	38	E
2	38	T
1	39	E
2	39	W
1	40	F
2	40	I
1	41	F
2	41	L
1	42	F
2	42	O
1	43	F
2	43	R
1	44	F
2	44	U
1	45	G
2	45	J
1	46	G
2	46	M
1	47	G
2	47	P
1	48	G
2	48	S
1	49	G
2	49	V
1	50	H
2	50	K
1	51	H
2	51	N
1	52	H
2	52	Q
1	53	H
2	53	T
1	54	H
2	54	W
1	55	I
2	55	L
1	56	I
2	56	O
1	57	I
2	57	R
1	58	I
2	58	U
1	59	J
2	59	M
1	60	J
2	60	P
1	61	J
2	61	S
1	62	J
2	62	V
1	63	K
2	63	N
1	64	K
2	64	Q
1	65	K
2	65	T
1	66	K
2	66	W
1	67	L
2	67	O
1	68	L
2	68	R
1	69	L
2	69	U
1	70	M
2	70	P
1	71	M
2	71	S
1	72	M
2	72	V
1	73	N
2	73	Q
1	74	N
2	74	T
1	75	N
2	75	W
1	76	O
2	76	R
1	77	O
2	77	U
1	78	P
2	78	S
1	79	P
2	79	V
1	80	Q
2	80	T
1	81	Q
2	81	W
1	82	R
2	82	U
1	83	S
2	83	V
1	84	T
2	84	W

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	D	1 - 218	1 - 218
1	2	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	2	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
1	3	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	3	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
1	4	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	4	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
1	5	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	5	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
1	6	VAL	VAL	PRO	PRO	A	A	2 - 218	2 - 218
2	6	VAL	VAL	PRO	PRO	R	S	2 - 218	2 - 218
1	7	GLU	GLU	PRO	PRO	A	A	1 - 218	1 - 218
2	7	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	8	ASP	ASP	ASN	ASN	B	B	1 - 216	1 - 216
2	8	ASP	ASP	ASN	ASN	D	E	1 - 216	1 - 216
1	9	ASP	ASP	ASN	ASN	B	B	1 - 216	1 - 216
2	9	ASP	ASP	ASN	ASN	G	H	1 - 216	1 - 216
1	10	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	10	ASP	ASP	CYS	CYS	J	K	1 - 218	1 - 218
1	11	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	11	ASP	ASP	CYS	CYS	M	N	1 - 218	1 - 218
1	12	ASP	ASP	ASN	ASN	B	B	1 - 214	1 - 214
2	12	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
1	13	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	13	ASP	ASP	CYS	CYS	S	T	1 - 218	1 - 218
1	14	ASP	ASP	CYS	CYS	B	B	1 - 218	1 - 218
2	14	ASP	ASP	CYS	CYS	V	W	1 - 218	1 - 218
1	15	HYP	HYP	GLY	GLY	X	C	12 - 22	12 - 22
2	15	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
1	16	HYP	HYP	GLY	GLY	X	C	12 - 22	12 - 22
2	16	HYP	HYP	GLY	GLY	H	I	12 - 22	12 - 22
1	17	PRO	PRO	GLY	GLY	X	C	11 - 22	11 - 22
2	17	PRO	PRO	GLY	GLY	K	L	11 - 22	11 - 22
1	18	PRO	PRO	GLY	GLY	X	C	11 - 22	11 - 22
2	18	PRO	PRO	GLY	GLY	N	O	11 - 22	11 - 22
1	19	HYP	HYP	GLY	GLY	X	C	12 - 22	12 - 22
2	19	HYP	HYP	GLY	GLY	Q	R	12 - 22	12 - 22
1	20	HYP	HYP	GLY	GLY	X	C	12 - 22	12 - 22
2	20	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
1	21	HYP	HYP	GLY	GLY	X	C	12 - 22	12 - 22
2	21	HYP	HYP	GLY	GLY	W	X	12 - 22	12 - 22
1	22	GLU	GLU	PRO	PRO	C	D	1 - 218	1 - 218
2	22	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
1	23	GLU	GLU	PRO	PRO	C	D	1 - 218	1 - 218
2	23	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
1	24	GLU	GLU	PRO	PRO	C	D	1 - 218	1 - 218
2	24	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
1	25	GLU	GLU	PRO	PRO	C	D	1 - 218	1 - 218
2	25	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
1	26	VAL	VAL	PRO	PRO	C	D	2 - 218	2 - 218
2	26	VAL	VAL	PRO	PRO	R	S	2 - 218	2 - 218
1	27	GLU	GLU	PRO	PRO	C	D	1 - 218	1 - 218
2	27	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	28	ASP	ASP	GLU	GLU	D	E	1 - 217	1 - 217
2	28	ASP	ASP	GLU	GLU	G	H	1 - 217	1 - 217
1	29	ASP	ASP	ASN	ASN	D	E	1 - 216	1 - 216
2	29	ASP	ASP	ASN	ASN	J	K	1 - 216	1 - 216
1	30	ASP	ASP	ASN	ASN	D	E	1 - 216	1 - 216
2	30	ASP	ASP	ASN	ASN	M	N	1 - 216	1 - 216
1	31	ASP	ASP	ASN	ASN	D	E	1 - 214	1 - 214
2	31	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
1	32	ASP	ASP	ASN	ASN	D	E	1 - 216	1 - 216
2	32	ASP	ASP	ASN	ASN	S	T	1 - 216	1 - 216
1	33	ASP	ASP	ASN	ASN	D	E	1 - 216	1 - 216
2	33	ASP	ASP	ASN	ASN	V	W	1 - 216	1 - 216
1	34	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	34	HYP	HYP	GLY	GLY	H	I	12 - 22	12 - 22
1	35	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	35	HYP	HYP	GLY	GLY	K	L	12 - 22	12 - 22
1	36	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	36	HYP	HYP	GLY	GLY	N	O	12 - 22	12 - 22
1	37	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	37	HYP	HYP	GLY	GLY	Q	R	12 - 22	12 - 22
1	38	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	38	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
1	39	HYP	HYP	GLY	GLY	E	F	12 - 22	12 - 22
2	39	HYP	HYP	GLY	GLY	W	X	12 - 22	12 - 22
1	40	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
2	40	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
1	41	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
2	41	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
1	42	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
2	42	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
1	43	VAL	VAL	PRO	PRO	F	G	2 - 218	2 - 218
2	43	VAL	VAL	PRO	PRO	R	S	2 - 218	2 - 218
1	44	GLU	GLU	PRO	PRO	F	G	1 - 218	1 - 218
2	44	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	45	ASP	ASP	ASN	ASN	G	H	1 - 216	1 - 216
2	45	ASP	ASP	ASN	ASN	J	K	1 - 216	1 - 216
1	46	ASP	ASP	ASN	ASN	G	H	1 - 216	1 - 216
2	46	ASP	ASP	ASN	ASN	M	N	1 - 216	1 - 216
1	47	ASP	ASP	ASN	ASN	G	H	1 - 214	1 - 214
2	47	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
1	48	ASP	ASP	ASN	ASN	G	H	1 - 216	1 - 216
2	48	ASP	ASP	ASN	ASN	S	T	1 - 216	1 - 216
1	49	ASP	ASP	ASN	ASN	G	H	1 - 216	1 - 216
2	49	ASP	ASP	ASN	ASN	V	W	1 - 216	1 - 216
1	50	HYP	HYP	GLY	GLY	H	I	12 - 22	12 - 22
2	50	HYP	HYP	GLY	GLY	K	L	12 - 22	12 - 22
1	51	HYP	HYP	GLY	GLY	H	I	12 - 22	12 - 22
2	51	HYP	HYP	GLY	GLY	N	O	12 - 22	12 - 22
1	52	HYP	HYP	PRO	PRO	H	I	12 - 23	12 - 23
2	52	HYP	HYP	PRO	PRO	Q	R	12 - 23	12 - 23
1	53	HYP	HYP	PRO	PRO	H	I	12 - 23	12 - 23
2	53	HYP	HYP	PRO	PRO	T	U	12 - 23	12 - 23
1	54	HYP	HYP	PRO	PRO	H	I	12 - 23	12 - 23
2	54	HYP	HYP	PRO	PRO	W	X	12 - 23	12 - 23
1	55	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
2	55	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
1	56	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
2	56	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
1	57	VAL	VAL	GLY	GLY	I	J	2 - 217	2 - 217
2	57	VAL	VAL	GLY	GLY	R	S	2 - 217	2 - 217
1	58	GLU	GLU	PRO	PRO	I	J	1 - 218	1 - 218
2	58	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	59	ASP	ASP	CYS	CYS	J	K	1 - 218	1 - 218
2	59	ASP	ASP	CYS	CYS	M	N	1 - 218	1 - 218
1	60	ASP	ASP	ASN	ASN	J	K	1 - 214	1 - 214
2	60	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
1	61	ASP	ASP	CYS	CYS	J	K	1 - 218	1 - 218
2	61	ASP	ASP	CYS	CYS	S	T	1 - 218	1 - 218
1	62	ASP	ASP	CYS	CYS	J	K	1 - 218	1 - 218
2	62	ASP	ASP	CYS	CYS	V	W	1 - 218	1 - 218
1	63	PRO	PRO	PRO	PRO	K	L	11 - 23	11 - 23
2	63	PRO	PRO	PRO	PRO	N	O	11 - 23	11 - 23
1	64	HYP	HYP	GLY	GLY	K	L	12 - 22	12 - 22
2	64	HYP	HYP	GLY	GLY	Q	R	12 - 22	12 - 22
1	65	HYP	HYP	GLY	GLY	K	L	12 - 22	12 - 22
2	65	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
1	66	HYP	HYP	GLY	GLY	K	L	12 - 22	12 - 22
2	66	HYP	HYP	GLY	GLY	W	X	12 - 22	12 - 22
1	67	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
2	67	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
1	68	VAL	VAL	PRO	PRO	L	M	2 - 218	2 - 218
2	68	VAL	VAL	PRO	PRO	R	S	2 - 218	2 - 218
1	69	GLU	GLU	PRO	PRO	L	M	1 - 218	1 - 218
2	69	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	70	ASP	ASP	ASN	ASN	M	N	1 - 214	1 - 214
2	70	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
1	71	ASP	ASP	CYS	CYS	M	N	1 - 218	1 - 218
2	71	ASP	ASP	CYS	CYS	S	T	1 - 218	1 - 218
1	72	ASP	ASP	CYS	CYS	M	N	1 - 218	1 - 218
2	72	ASP	ASP	CYS	CYS	V	W	1 - 218	1 - 218
1	73	HYP	HYP	GLY	GLY	N	O	12 - 22	12 - 22
2	73	HYP	HYP	GLY	GLY	Q	R	12 - 22	12 - 22
1	74	HYP	HYP	GLY	GLY	N	O	12 - 22	12 - 22
2	74	HYP	HYP	GLY	GLY	T	U	12 - 22	12 - 22
1	75	HYP	HYP	GLY	GLY	N	O	12 - 22	12 - 22
2	75	HYP	HYP	GLY	GLY	W	X	12 - 22	12 - 22
1	76	VAL	VAL	GLY	GLY	O	P	2 - 217	2 - 217
2	76	VAL	VAL	GLY	GLY	R	S	2 - 217	2 - 217
1	77	GLU	GLU	PRO	PRO	O	P	1 - 218	1 - 218
2	77	GLU	GLU	PRO	PRO	U	V	1 - 218	1 - 218
1	78	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
2	78	ASP	ASP	ASN	ASN	S	T	1 - 214	1 - 214
1	79	ASP	ASP	ASN	ASN	P	Q	1 - 214	1 - 214
2	79	ASP	ASP	ASN	ASN	V	W	1 - 214	1 - 214
1	80	HYP	HYP	PRO	PRO	Q	R	12 - 23	12 - 23
2	80	HYP	HYP	PRO	PRO	T	U	12 - 23	12 - 23
1	81	HYP	HYP	PRO	PRO	Q	R	12 - 23	12 - 23
2	81	HYP	HYP	PRO	PRO	W	X	12 - 23	12 - 23
1	82	VAL	VAL	PRO	PRO	R	S	2 - 218	2 - 218
2	82	VAL	VAL	PRO	PRO	U	V	2 - 218	2 - 218
1	83	ASP	ASP	CYS	CYS	S	T	1 - 218	1 - 218
2	83	ASP	ASP	CYS	CYS	V	W	1 - 218	1 - 218
1	84	HYP	HYP	PRO	PRO	T	U	12 - 23	12 - 23
2	84	HYP	HYP	PRO	PRO	W	X	12 - 23	12 - 23

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
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84

Components

#1: Antibody

A C F I O R U
heavy chain of ACC1 Fab fragment

Details:

Mass: 23353.164 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: B cell hybridoma / Strain: B10.RIII.Cia5

#2: Antibody

B D G J M P S V
light chain of ACC1 Fab fragment

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 / Strain: B10.RIII.Cia5

#3: Protein/peptide

X E H K N Q T W
synthetic peptide containing the CII583-591 epitope of collagen type II,Collagen alpha-1(II) chain,synthetic peptide containing the CII583-591 epitope of collagen type II, / Alpha-1 type II collagen

Details:

Mass: 2698.919 Da / Num. of mol.: 8 / Source method: obtained synthetically
Details: the synthesized peptide is homotrimeric and triple-helical in solution, but bound as single alpha chain to ACC1
Source: (synth.) Mus musculus (house mouse) / References: UniProt: P28481

#4: Antibody

L heavy chain of ACC1 Fab fragment

Details:

Mass: 23567.428 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / Cell line: B cell hybridoma / Strain: B10.RIII.Cia5

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.42 ų/Da / Density % sol: 48.7 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 ; Details: 20% (w/v) PEG3350, 0.1 M Bistris-Propane pH 7.0, 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: DECTRIS PILATUS 6M / 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: 2.95→48.9 Å / Num. obs: 73522 / % possible obs: 99 % / Redundancy: 3.2 % / B_iso Wilson estimate: 55.5 Ų / R_merge(I) obs: 0.073 / Net I/σ(I): 11.4
• Reflection shell: Resolution: 2.95→3.01 Å / Redundancy: 3.3 % / R_merge(I) obs: 0.511 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 4569 / % possible all: 98.6

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: 2.95→50.01 Å / Cor.coef. F_o:F_c: 0.939 / Cor.coef. F_o:F_c free: 0.898 / SU B: 58.786 / SU ML: 0.453 / Cross valid method: THROUGHOUT / ESU R Free: 0.488 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.26098	3639	4.9 %	RANDOM
Rwork	0.2015	-	-	-
obs	0.20442	69880	98.98 %	-

• 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: 77.264 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	2.49 Å2	-1.85 Å2	0.35 Å2
2-	-	-1.66 Å2	1.05 Å2
3-	-	-	-0.29 Å2

Refinement step

Cycle: 1 / Resolution: 2.95→50.01 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	26921	0	0	0	26921

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.02	27593
X-RAY DIFFRACTION	r_bond_other_d	0.002	0.02	25227
X-RAY DIFFRACTION	r_angle_refined_deg	1.471	1.946	37500
X-RAY DIFFRACTION	r_angle_other_deg	1.004	3	58464
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.507	5	3528
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.076	24.429	1077
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.699	15	4351
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.104	15	112
X-RAY DIFFRACTION	r_chiral_restr	0.111	0.2	4202
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.021	31086
X-RAY DIFFRACTION	r_gen_planes_other	0.003	0.02	6098
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	0.914	3.569	14208
X-RAY DIFFRACTION	r_mcbond_other	0.914	3.569	14207
X-RAY DIFFRACTION	r_mcangle_it	1.611	5.349	17704
X-RAY DIFFRACTION	r_mcangle_other	1.611	5.349	17705
X-RAY DIFFRACTION	r_scbond_it	0.697	3.567	13385
X-RAY DIFFRACTION	r_scbond_other	0.697	3.567	13386
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	1.239	5.335	19797
X-RAY DIFFRACTION	r_long_range_B_refined	2.599	40.017	28137
X-RAY DIFFRACTION	r_long_range_B_other	2.599	40.019	28138
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	1648	0.01
1	2	C	1648	0.01
2	1	A	1654	0.01
2	2	F	1654	0.01
3	1	A	1652	0.01
3	2	I	1652	0.01
4	1	A	1646	0.01
4	2	L	1646	0.01
5	1	A	1642	0.01
5	2	O	1642	0.01
6	1	A	1628	0.01
6	2	R	1628	0.01
7	1	A	1564	0.01
7	2	U	1564	0.01
8	1	B	1658	0.01
8	2	D	1658	0.01
9	1	B	1660	0.01
9	2	G	1660	0.01
10	1	B	1692	0.01
10	2	J	1692	0.01
11	1	B	1674	0.01
11	2	M	1674	0.01
12	1	B	1646	0.01
12	2	P	1646	0.01
13	1	B	1652	0.01
13	2	S	1652	0.01
14	1	B	1652	0.01
14	2	V	1652	0.01
15	1	X	52	0
15	2	E	52	0
16	1	X	52	0
16	2	H	52	0
17	1	X	58	0.01
17	2	K	58	0.01
18	1	X	62	0.01
18	2	N	62	0.01
19	1	X	58	0.01
19	2	Q	58	0.01
20	1	X	56	0
20	2	T	56	0
21	1	X	60	0
21	2	W	60	0
22	1	C	1656	0.01
22	2	F	1656	0.01
23	1	C	1668	0.01
23	2	I	1668	0.01
24	1	C	1672	0.01
24	2	L	1672	0.01
25	1	C	1654	0.01
25	2	O	1654	0.01
26	1	C	1636	0.01
26	2	R	1636	0.01
27	1	C	1564	0.01
27	2	U	1564	0.01
28	1	D	1662	0.01
28	2	G	1662	0.01
29	1	D	1666	0.01
29	2	J	1666	0.01
30	1	D	1680	0.01
30	2	M	1680	0.01
31	1	D	1640	0.01
31	2	P	1640	0.01
32	1	D	1646	0.01
32	2	S	1646	0.01
33	1	D	1618	0.01
33	2	V	1618	0.01
34	1	E	50	0
34	2	H	50	0
35	1	E	50	0
35	2	K	50	0
36	1	E	54	0
36	2	N	54	0
37	1	E	52	0
37	2	Q	52	0
38	1	E	52	0
38	2	T	52	0
39	1	E	50	0
39	2	W	50	0
40	1	F	1660	0.01
40	2	I	1660	0.01
41	1	F	1636	0.01
41	2	L	1636	0.01
42	1	F	1632	0.01
42	2	O	1632	0.01
43	1	F	1628	0.01
43	2	R	1628	0.01
44	1	F	1562	0.01
44	2	U	1562	0.01
45	1	G	1670	0.01
45	2	J	1670	0.01
46	1	G	1672	0.01
46	2	M	1672	0.01
47	1	G	1648	0.01
47	2	P	1648	0.01
48	1	G	1664	0.01
48	2	S	1664	0.01
49	1	G	1650	0.01
49	2	V	1650	0.01
50	1	H	54	0
50	2	K	54	0
51	1	H	54	0
51	2	N	54	0
52	1	H	58	0.01
52	2	Q	58	0.01
53	1	H	58	0
53	2	T	58	0
54	1	H	56	0
54	2	W	56	0
55	1	I	1664	0.01
55	2	L	1664	0.01
56	1	I	1656	0.01
56	2	O	1656	0.01
57	1	I	1634	0.01
57	2	R	1634	0.01
58	1	I	1550	0.01
58	2	U	1550	0.01
59	1	J	1696	0.01
59	2	M	1696	0.01
60	1	J	1662	0.01
60	2	P	1662	0.01
61	1	J	1672	0.01
61	2	S	1672	0.01
62	1	J	1662	0.01
62	2	V	1662	0.01
63	1	K	66	0.01
63	2	N	66	0.01
64	1	K	52	0.01
64	2	Q	52	0.01
65	1	K	54	0
65	2	T	54	0
66	1	K	52	0
66	2	W	52	0
67	1	L	1672	0.01
67	2	O	1672	0.01
68	1	L	1642	0.01
68	2	R	1642	0.01
69	1	L	1536	0.01
69	2	U	1536	0.01
70	1	M	1666	0.01
70	2	P	1666	0.01
71	1	M	1680	0.01
71	2	S	1680	0.01
72	1	M	1654	0.01
72	2	V	1654	0.01
73	1	N	56	0
73	2	Q	56	0
74	1	N	58	0
74	2	T	58	0
75	1	N	56	0
75	2	W	56	0
76	1	O	1626	0.01
76	2	R	1626	0.01
77	1	O	1540	0.01
77	2	U	1540	0.01
78	1	P	1652	0.01
78	2	S	1652	0.01
79	1	P	1632	0.01
79	2	V	1632	0.01
80	1	Q	58	0
80	2	T	58	0
81	1	Q	58	0.01
81	2	W	58	0.01
82	1	R	1556	0.01
82	2	U	1556	0.01
83	1	S	1676	0.01
83	2	V	1676	0.01
84	1	T	58	0
84	2	W	58	0

LS refinement shell

Resolution: 2.95→3.026 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.371	242	-
Rwork	0.327	5212	-
obs	-	-	98.66 %

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	9.4661	0.0294	1.804	1.5828	-0.2059	2.22	-0.4302	-0.8403	0.3907	0.5166	0.2016	-0.191	-0.1931	0.0367	0.2286	0.3015	0.0974	-0.0552	0.1618	-0.0291	0.0626	41.8299	20.2865	11.2489
2	7.7115	1.2203	2.4437	5.3094	1.1572	4.7497	0.055	-1.2787	-0.9972	0.4257	0.2056	0.5583	0.0088	-0.8633	-0.2606	0.1234	0.1004	0.1635	0.5336	0.2844	0.3761	15.5449	9.6933	7.3061
3	10.4735	4.658	4.2873	3.3794	3.2738	8.0124	-0.5646	1.9354	0.6484	-0.0792	0.2884	-0.0687	-0.4995	1.1586	0.2762	0.3533	-0.2526	-0.1571	0.7799	0.3491	0.1773	41.5753	26.2583	-14.5261
4	7.4785	1.1339	0.7549	1.7986	-0.3663	3.483	-0.2498	0.1993	0.0672	-0.0513	0.1807	0.4707	-0.3309	-0.2673	0.0691	0.149	0.0368	-0.0151	0.0415	0.0315	0.1439	22.2089	18.9514	-6.0297
5	3.2719	1.6224	-3.941	5.7892	-1.7273	7.8423	0.059	-0.0712	-0.3532	-0.68	-0.4824	-0.4888	0.8078	0.5423	0.4235	0.401	0.2472	-0.0463	0.1738	-0.0758	0.2806	12.3042	-47.3143	-29.7741
6	1.7959	2.4025	-1.0098	6.632	-3.4931	3.6607	0.1469	0.1294	-0.1283	-0.858	-0.6172	-0.685	0.344	1.1818	0.4703	0.4504	0.2691	0.0314	0.6712	0.0021	0.2164	22.38	-33.8255	-38.6938
7	3.6638	0.5664	1.0613	8.9366	-0.6476	3.9894	0.2237	0.1174	-0.0372	0.2838	0.1182	0.9089	-0.0079	0.0063	-0.3419	0.0638	0.0618	-0.0315	0.0676	-0.0605	0.1922	-2.8066	-31.5239	-28.2058
8	3.7039	-0.2241	-2.7126	2.0378	-0.9926	6.5002	0.1537	0.4474	0.1777	-0.8292	-0.0977	-0.1773	0.2429	0.7357	-0.056	0.481	0.0719	0.0914	0.3846	-0.0454	0.1782	19.8569	-14.0902	-51.6623
9	5.9645	-2.0322	-0.0267	6.521	-0.2934	3.9912	-0.0447	0.2883	0.4083	-0.1581	-0.023	-0.5368	-0.2238	-0.0283	0.0678	0.1766	-0.1219	-0.02	0.109	0.0488	0.2495	5.4829	25.6849	42.4876
10	2.8834	-1.2717	-0.7134	7.849	1.1871	4.5063	0.5461	0.5167	0.0395	-0.6374	-0.4311	0.0371	0.2945	-0.202	-0.1149	0.2729	0.2321	0.0817	0.5513	0.1337	0.0986	19.0056	-0.3862	28.6727
11	2.2651	-0.2002	-0.1346	8.5703	0.1989	0.8294	-0.1166	-0.1587	-0.0514	0.9212	-0.04	0.4692	-0.108	-0.3254	0.1566	0.3475	-0.0946	-0.0084	0.255	-0.0193	0.1104	-0.9793	8.3303	56.631
12	6.2077	-1.0399	-4.0946	3.6952	0.1958	6.172	0.6248	0.3728	0.1567	-0.1356	-0.6344	-0.6596	0.3996	0.6906	0.0096	0.3449	0.1874	-0.004	0.3856	0.0988	0.2202	26.4006	-9.5411	39.5989
13	7.4133	2.0026	0.486	1.4071	-0.7643	2.3845	-0.3507	0.541	0.166	-0.3746	0.226	0.1836	0.1443	-0.0066	0.1247	0.4717	-0.0436	-0.0968	0.1029	0.0112	0.0806	-28.1286	11.9715	-51.864
14	5.7354	-0.7646	0.4778	3.2282	-0.0823	6.9767	-0.259	0.4229	-0.0183	-0.1878	0.1968	-0.2621	0.1602	0.4614	0.0621	0.188	-0.099	0.0969	0.1275	-0.0622	0.1494	3.7448	9.1494	-43.1525
15	6.947	-0.2907	2.3002	2.3274	-0.6462	5.7417	-0.1187	-1.3374	0.6648	0.0347	-0.1553	0.5707	0.0084	-0.9884	0.274	0.2876	0.0365	-0.0433	0.3517	-0.21	0.2325	-28.4912	20.0967	-30.0629
16	7.3004	0.5311	-3.3113	1.6157	-0.2545	4.0626	-0.1885	0.3324	0.5338	-0.2791	0.2163	-0.4825	-0.4563	0.2464	-0.0278	0.2907	-0.0578	-0.0493	0.155	-0.0478	0.2779	7.6243	23.3739	-37.6035
17	3.1733	-1.4116	-0.4732	5.5554	1.058	6.7363	0.0674	-0.2912	-0.1151	0.724	-0.4517	0.1036	0.2987	-0.4432	0.3843	0.2323	-0.2651	-0.0449	0.3479	0.07	0.0572	44.2512	-52.1895	-15.204
18	2.3183	-0.4964	-1.1825	7.2348	-0.2599	2.579	0.2928	-0.0475	-0.0225	0.4479	-0.4242	0.9843	0.086	-0.1883	0.1314	0.1841	-0.1987	0.1241	0.4363	-0.244	0.2653	23.5276	-27.2403	-8.6697
19	5.829	-4.537	0.3005	6.8904	-1.0537	2.2456	0.3618	0.1297	0.4934	-0.2548	-0.2763	-1.415	-0.0357	-0.158	-0.0855	0.1214	-0.1131	-0.0644	0.1925	0.2232	0.5156	60.1849	-33.3231	-22.3848
20	3.3938	-3.0213	-1.605	6.2979	2.447	1.5178	0.359	0.206	0.2646	0.3479	-0.5729	-0.0769	-0.0937	-0.3642	0.2139	0.2732	-0.1584	-0.0702	0.3384	-0.002	0.2347	40.0764	-22.4031	-13.0281
21	4.5519	1.0987	0.0708	3.9825	0.3601	6.5939	-0.1071	-0.0421	0.2238	-0.1318	0.0158	0.3952	-0.1032	-0.5646	0.0914	0.0427	-0.0368	-0.1275	0.1058	0.1347	0.4195	-29.8846	-15.8853	-5.1987
22	0.183	-0.5553	0.1184	2.14	0.7609	6.2159	-0.1741	-0.1231	-0.0432	0.6436	0.1819	0.4522	0.1201	-0.5569	-0.0078	0.2709	-0.065	0.0051	0.3727	0.1478	0.6971	-28.8552	-10.6165	14.7647
23	6.0496	-0.9335	-0.9731	2.629	0.0607	4.7064	-0.0046	-0.2519	0.821	0.6387	0.498	0.2854	-0.2577	-0.1065	-0.4934	0.5978	0.041	0.09	0.3855	0.2179	0.7779	-26.9624	1.2105	29.9186
24	4.5424	1.5699	2.465	2.7368	0.74	4.2191	0.001	0.3667	-0.3471	-0.2109	0.2382	-0.8708	-0.1983	0.5326	-0.2392	0.0925	-0.085	-0.0347	0.1302	0.0473	0.5655	-7.7636	-17.5182	0.5891
25	5.535	1.3263	-3.8378	1.9589	-0.9655	5.3461	0.0402	-0.3257	0.5205	0.8321	0.2446	0.2571	0.2335	-0.0585	-0.2848	0.6285	-0.02	-0.0943	0.2894	0.0131	0.4476	-18.0525	-14.2615	35.4378
26	3.6154	-0.1572	1.8153	1.0724	0.7826	9.4384	-0.3905	0.9346	0.401	-0.1094	0.3447	-0.5699	-0.4042	1.8337	0.0458	0.4358	-0.0057	-0.079	0.5904	-0.0977	0.367	46.1914	-35.7844	62.8115
27	3.1831	1.1407	-0.6336	1.2877	0.0511	0.2164	0.052	-0.0495	0.1138	0.2434	0.0706	-0.3694	0.0594	0.0403	-0.1225	0.6398	0.1919	-0.0809	0.4755	0.0222	0.5879	55.4179	-40.4989	37.1329
28	5.5928	1.6498	0.1409	1.4312	1.5501	3.7767	-0.3251	0.4826	0.2003	-0.7286	0.7247	-0.4985	-0.1935	0.7871	-0.3996	1.3329	-0.3205	0.4415	0.8828	-0.1031	0.6012	43.1633	-33.9526	30.0162
29	2.4616	0.2922	2.4449	2.0516	1.7447	7.5632	0.0853	-0.461	-0.0149	0.2697	-0.0196	0.1808	-0.1692	-1.0631	-0.0657	0.1623	0.0787	0.0302	0.2041	0.0337	0.1638	25.2157	-42.5162	55.3798
30	7.2243	-0.1911	-4.7322	4.5358	1.5298	4.2149	-0.1247	0.1468	-0.7377	-0.8816	-0.1797	-0.6016	-0.2005	0.7404	0.3044	0.6838	0.0975	0.0344	1.1835	0.0192	0.1802	37.921	-47.6116	24.3478
31	0.3782	1.3627	-0.2171	8.0766	-2.2967	4.9958	0.0327	-0.0546	0.5429	1.6055	0.265	1.2631	-0.4952	-0.6073	-0.2978	0.6343	0.2425	-0.1766	0.3959	0.0838	1.1652	-6.6586	-35.5385	24.7426
32	8.0421	1.9775	1.4299	7.6476	-2.1107	1.2521	0.3876	-0.4058	0.7683	2.0029	-0.2798	0.1696	-0.8377	-0.1986	-0.1078	1.4778	0.0745	0.3424	0.8529	-0.0539	0.626	-9.2968	-57.8738	43.0019
33	12.2426	10.2526	-7.0871	8.6105	-5.9532	4.2091	0.1106	0.6975	0.142	0.3643	0.3569	0.2365	-0.242	-0.6322	-0.4675	2.2491	0.1232	0.2413	1.1924	-0.0279	0.8582	-11.7253	-52.7899	50.2244
34	0.4319	-0.5038	0.9369	12.2943	-4.3475	4.8091	-0.1403	0.4111	0.2598	-2.4873	0.2647	-1.1623	0.4842	0.5127	-0.1244	0.6584	-0.2631	0.0817	0.5238	0.2515	0.6798	0.7828	-53.0748	7.1927
35	3.472	1.2749	-0.4382	8.5988	-3.2443	3.2748	-0.2317	0.1926	0.3021	-0.0627	0.0525	-0.8482	0.1631	0.4032	0.1792	0.1239	-0.0725	-0.1467	0.3	0.0815	0.2841	1.9482	-54.8223	18.2999
36	8.917	1.0941	-4.6755	1.2612	-0.3233	3.9671	0.1207	0.148	0.7014	0.9203	0.3011	0.6036	-0.1703	-1.1177	-0.4217	0.9745	0.3379	0.2703	0.9895	0.4012	0.5169	-19.1136	-69.1188	37.95
37	0	0	0	0	0	0	0	0	0	0	0	0	0	0	-0	0.3213	0	0	0.3213	0	0.3213	0	0	0
38	5.703	-2.8257	3.3252	2.4367	-1.8996	2.0001	0.0003	-0.6937	0.1168	0.3659	0.0823	0.5655	-0.089	-0.3406	-0.0826	0.3832	-0.0607	0.1293	0.4525	-0.0129	0.5429	-10.3694	24.3812	53.369
39	1.1806	-3.0325	1.6903	8.8098	-4.0733	2.4957	-0.122	-0.4724	-0.2578	0.6658	0.453	0.8807	-0.0511	-0.8717	-0.331	0.3375	-0.1889	-0.0537	0.7619	-0.0622	0.3017	-43.4901	10.9186	-37.5588
40	0.7887	0.1998	0.9688	2.2916	-0.8026	1.6816	0.4018	0.3348	-0.176	-0.3193	-0.5192	-0.7459	0.7043	0.6758	0.1175	0.4856	0.0671	0.0638	0.5627	0.058	0.3055	56.2392	-51.8264	-30.2649
41	2.6705	0.1802	0.7872	0.2119	-1.1644	7.7276	0.0478	1.1242	0.2677	-0.0673	0.1013	0.0353	0.3148	0.2216	-0.1491	0.3207	-0.0709	0.1064	0.5032	0.0496	0.385	-15.9568	-15.3334	-16.2577
42	5.0172	1.4905	4.2905	10.8063	12.0531	14.883	0.1122	-1.683	0.2147	0.4553	-0.2298	0.0292	0.5094	-1.1712	0.1176	0.3711	0.1902	0.0228	0.71	-0.1072	0.4495	31.0179	-33.7976	74.0518
43	2.8378	-0.3704	-0.7901	0.2679	1.5341	10.2667	0.0297	0.6523	0.471	-0.1502	-0.0095	-0.1304	-0.8885	0.0971	-0.0202	0.3898	-0.064	0.0253	0.4201	0.0906	0.7182	8.7052	-34.7343	10.2975
44	37.2283	4.9481	-19.7002	29.02	-14.1364	15.1046	0.0742	0.2785	-0.9343	-0.2448	-0.7454	-0.5109	0.0697	0.1873	0.6712	0.2251	0.0752	-0.0081	0.4702	-0.003	0.2656	60.4608	14.6226	-1.7386
45	10.128	-2.2216	-9.0199	0.5094	1.9564	8.0639	0.5305	0.3557	0.6426	-0.0992	-0.0654	-0.2459	-0.491	-0.2614	-0.4651	0.0799	-0.0035	-0.0494	0.5423	-0.0194	0.5394	58.1266	19.0901	-3.9866

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 132
2	X-RAY DIFFRACTION	2	A	135 - 218
3	X-RAY DIFFRACTION	3	B	1 - 31
4	X-RAY DIFFRACTION	4	B	32 - 218
5	X-RAY DIFFRACTION	5	C	1 - 56
6	X-RAY DIFFRACTION	6	C	57 - 218
7	X-RAY DIFFRACTION	7	D	1 - 111
8	X-RAY DIFFRACTION	8	D	112 - 217
9	X-RAY DIFFRACTION	9	F	1 - 117
10	X-RAY DIFFRACTION	10	F	118 - 218
11	X-RAY DIFFRACTION	11	G	1 - 113
12	X-RAY DIFFRACTION	12	G	114 - 217
13	X-RAY DIFFRACTION	13	I	1 - 122
14	X-RAY DIFFRACTION	14	I	123 - 218
15	X-RAY DIFFRACTION	15	J	1 - 111
16	X-RAY DIFFRACTION	16	J	112 - 218
17	X-RAY DIFFRACTION	17	L	1 - 112
18	X-RAY DIFFRACTION	18	L	113 - 220
19	X-RAY DIFFRACTION	19	M	1 - 36
20	X-RAY DIFFRACTION	20	M	37 - 218
21	X-RAY DIFFRACTION	21	O	1 - 74
22	X-RAY DIFFRACTION	22	O	75 - 178
23	X-RAY DIFFRACTION	23	O	179 - 218
24	X-RAY DIFFRACTION	24	P	1 - 112
25	X-RAY DIFFRACTION	25	P	113 - 215
26	X-RAY DIFFRACTION	26	R	2 - 114
27	X-RAY DIFFRACTION	27	R	115 - 126
28	X-RAY DIFFRACTION	28	R	127 - 218
29	X-RAY DIFFRACTION	29	S	1 - 125
30	X-RAY DIFFRACTION	30	S	126 - 218
31	X-RAY DIFFRACTION	31	U	1 - 131
32	X-RAY DIFFRACTION	32	U	132 - 196
33	X-RAY DIFFRACTION	33	U	197 - 218
34	X-RAY DIFFRACTION	34	V	1 - 36
35	X-RAY DIFFRACTION	35	V	37 - 125
36	X-RAY DIFFRACTION	36	V	126 - 218
37	X-RAY DIFFRACTION	37	E	25 - 40
38	X-RAY DIFFRACTION	38	H	12 - 23
39	X-RAY DIFFRACTION	39	K	11 - 23
40	X-RAY DIFFRACTION	40	N	11 - 23
41	X-RAY DIFFRACTION	41	Q	12 - 23
42	X-RAY DIFFRACTION	42	T	12 - 23
43	X-RAY DIFFRACTION	43	W	12 - 23
44	X-RAY DIFFRACTION	44	X	10 - 16
45	X-RAY DIFFRACTION	45	X	17 - 23