PDB-5opw: Crystal structure of the GroEL mutant A109C

Basic information

• Entry: Database: PDB / ID: 5opw
• Title: Crystal structure of the GroEL mutant A109C
• Components: 60 kDa chaperonin
• Keywords: CHAPERONE / chaperonin

Function / homology

Function:

GroEL-GroES complex / chaperonin ATPase / virion assembly / : / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / unfolded protein binding / protein folding / response to heat / protein refolding / magnesium ion binding / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / cytosol

Domain/homology:

GROEL; domain 1 / GroEL-like equatorial domain / GROEL; domain 2 / TCP-1-like chaperonin intermediate domain / Chaperonin Cpn60, conserved site / Chaperonins cpn60 signature. / Chaperonin Cpn60/GroEL / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta

Component:

Chaperonin GroEL

• Biological species: Escherichia coli (E. coli)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.19 Å
• Authors: Yan, X. / Shi, Q. / Bracher, A. / Milicic, G. / Singh, A.K. / Hartl, F.U. / Hayer-Hartl, M.
• Citation: Journal: Cell / Year: 2018; Title: GroEL Ring Separation and Exchange in the Chaperonin Reaction.; Authors: Yan, X. / Shi, Q. / Bracher, A. / Milicic, G. / Singh, A.K. / Hartl, F.U. / Hayer-Hartl, M.

History

Deposition	Aug 10, 2017	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 10, 2018	Provider: repository / Type: Initial release
Revision 1.1	Jan 24, 2018	Group: Database references / Category: citation Item: _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Feb 7, 2018	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.3	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
Revision 1.4	Nov 20, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Assembly

Deposited unit

A: 60 kDa chaperonin

B: 60 kDa chaperonin

C: 60 kDa chaperonin

D: 60 kDa chaperonin

E: 60 kDa chaperonin

F: 60 kDa chaperonin

G: 60 kDa chaperonin

H: 60 kDa chaperonin

I: 60 kDa chaperonin

J: 60 kDa chaperonin

K: 60 kDa chaperonin

L: 60 kDa chaperonin

M: 60 kDa chaperonin

N: 60 kDa chaperonin

Summary:

• 802 kDa, 14 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	802,096	14
Polymers	802,096	14
Non-polymers	0	0
Water	0	0

1

Summary:

• Idetical with deposited unit
• defined by software
• Evidence: Textbook

Symmetry operations:

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

Calculated values:

Buried area	48690 Å2
ΔGint	-223 kcal/mol
Surface area	293870 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	135.695, 262.047, 149.213
Angle α, β, γ (deg.)	90.000, 100.810, 90.000
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
1	2	A
2	2	C
1	3	A
2	3	D
1	4	A
2	4	E
1	5	A
2	5	F
1	6	A
2	6	G
1	7	A
2	7	H
1	8	A
2	8	I
1	9	A
2	9	J
1	10	A
2	10	K
1	11	A
2	11	L
1	12	A
2	12	M
1	13	A
2	13	N
1	14	B
2	14	C
1	15	B
2	15	D
1	16	B
2	16	E
1	17	B
2	17	F
1	18	B
2	18	G
1	19	B
2	19	H
1	20	B
2	20	I
1	21	B
2	21	J
1	22	B
2	22	K
1	23	B
2	23	L
1	24	B
2	24	M
1	25	B
2	25	N
1	26	C
2	26	D
1	27	C
2	27	E
1	28	C
2	28	F
1	29	C
2	29	G
1	30	C
2	30	H
1	31	C
2	31	I
1	32	C
2	32	J
1	33	C
2	33	K
1	34	C
2	34	L
1	35	C
2	35	M
1	36	C
2	36	N
1	37	D
2	37	E
1	38	D
2	38	F
1	39	D
2	39	G
1	40	D
2	40	H
1	41	D
2	41	I
1	42	D
2	42	J
1	43	D
2	43	K
1	44	D
2	44	L
1	45	D
2	45	M
1	46	D
2	46	N
1	47	E
2	47	F
1	48	E
2	48	G
1	49	E
2	49	H
1	50	E
2	50	I
1	51	E
2	51	J
1	52	E
2	52	K
1	53	E
2	53	L
1	54	E
2	54	M
1	55	E
2	55	N
1	56	F
2	56	G
1	57	F
2	57	H
1	58	F
2	58	I
1	59	F
2	59	J
1	60	F
2	60	K
1	61	F
2	61	L
1	62	F
2	62	M
1	63	F
2	63	N
1	64	G
2	64	H
1	65	G
2	65	I
1	66	G
2	66	J
1	67	G
2	67	K
1	68	G
2	68	L
1	69	G
2	69	M
1	70	G
2	70	N
1	71	H
2	71	I
1	72	H
2	72	J
1	73	H
2	73	K
1	74	H
2	74	L
1	75	H
2	75	M
1	76	H
2	76	N
1	77	I
2	77	J
1	78	I
2	78	K
1	79	I
2	79	L
1	80	I
2	80	M
1	81	I
2	81	N
1	82	J
2	82	K
1	83	J
2	83	L
1	84	J
2	84	M
1	85	J
2	85	N
1	86	K
2	86	L
1	87	K
2	87	M
1	88	K
2	88	N
1	89	L
2	89	M
1	90	L
2	90	N
1	91	M
2	91	N

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: PRO / End label comp-ID: PRO / Refine code: _ / Auth seq-ID: 2 - 525 / Label seq-ID: 1 - 524

Dom-ID	Ens-ID	Auth asym-ID	Label asym-ID
1	1	A	A
2	1	B	B
1	2	A	A
2	2	C	C
1	3	A	A
2	3	D	D
1	4	A	A
2	4	E	E
1	5	A	A
2	5	F	F
1	6	A	A
2	6	G	G
1	7	A	A
2	7	H	H
1	8	A	A
2	8	I	I
1	9	A	A
2	9	J	J
1	10	A	A
2	10	K	K
1	11	A	A
2	11	L	L
1	12	A	A
2	12	M	M
1	13	A	A
2	13	N	N
1	14	B	B
2	14	C	C
1	15	B	B
2	15	D	D
1	16	B	B
2	16	E	E
1	17	B	B
2	17	F	F
1	18	B	B
2	18	G	G
1	19	B	B
2	19	H	H
1	20	B	B
2	20	I	I
1	21	B	B
2	21	J	J
1	22	B	B
2	22	K	K
1	23	B	B
2	23	L	L
1	24	B	B
2	24	M	M
1	25	B	B
2	25	N	N
1	26	C	C
2	26	D	D
1	27	C	C
2	27	E	E
1	28	C	C
2	28	F	F
1	29	C	C
2	29	G	G
1	30	C	C
2	30	H	H
1	31	C	C
2	31	I	I
1	32	C	C
2	32	J	J
1	33	C	C
2	33	K	K
1	34	C	C
2	34	L	L
1	35	C	C
2	35	M	M
1	36	C	C
2	36	N	N
1	37	D	D
2	37	E	E
1	38	D	D
2	38	F	F
1	39	D	D
2	39	G	G
1	40	D	D
2	40	H	H
1	41	D	D
2	41	I	I
1	42	D	D
2	42	J	J
1	43	D	D
2	43	K	K
1	44	D	D
2	44	L	L
1	45	D	D
2	45	M	M
1	46	D	D
2	46	N	N
1	47	E	E
2	47	F	F
1	48	E	E
2	48	G	G
1	49	E	E
2	49	H	H
1	50	E	E
2	50	I	I
1	51	E	E
2	51	J	J
1	52	E	E
2	52	K	K
1	53	E	E
2	53	L	L
1	54	E	E
2	54	M	M
1	55	E	E
2	55	N	N
1	56	F	F
2	56	G	G
1	57	F	F
2	57	H	H
1	58	F	F
2	58	I	I
1	59	F	F
2	59	J	J
1	60	F	F
2	60	K	K
1	61	F	F
2	61	L	L
1	62	F	F
2	62	M	M
1	63	F	F
2	63	N	N
1	64	G	G
2	64	H	H
1	65	G	G
2	65	I	I
1	66	G	G
2	66	J	J
1	67	G	G
2	67	K	K
1	68	G	G
2	68	L	L
1	69	G	G
2	69	M	M
1	70	G	G
2	70	N	N
1	71	H	H
2	71	I	I
1	72	H	H
2	72	J	J
1	73	H	H
2	73	K	K
1	74	H	H
2	74	L	L
1	75	H	H
2	75	M	M
1	76	H	H
2	76	N	N
1	77	I	I
2	77	J	J
1	78	I	I
2	78	K	K
1	79	I	I
2	79	L	L
1	80	I	I
2	80	M	M
1	81	I	I
2	81	N	N
1	82	J	J
2	82	K	K
1	83	J	J
2	83	L	L
1	84	J	J
2	84	M	M
1	85	J	J
2	85	N	N
1	86	K	K
2	86	L	L
1	87	K	K
2	87	M	M
1	88	K	K
2	88	N	N
1	89	L	L
2	89	M	M
1	90	L	L
2	90	N	N
1	91	M	M
2	91	N	N

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
85
86
87
88
89
90
91

Components

#1: Protein

A B C D E F G H I J K L M N
60 kDa chaperonin / GroEL protein / Protein Cpn60

Details:

Mass: 57292.566 Da / Num. of mol.: 14 / Fragment: GroEL / Mutation: A109C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Gene: groL, groEL, mopA, b4143, JW4103 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0A6F5

• Has protein modification: Y

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 3.37 ų/Da / Density % sol: 63.49 % / Mosaicity: 0.11 °
• Crystal grow: Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5 / Details: 0.1 M sodium citrate, pH 5.5, and 15 % PEG 6000

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-1 / Wavelength: 0.966 Å
• Detector: Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Aug 25, 2016
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.966 Å / Relative weight: 1
• Reflection: Resolution: 3.19→50 Å / Num. obs: 168385 / % possible obs: 99.5 % / Redundancy: 3.5 % / CC_1/2: 0.987 / R_merge(I) obs: 0.175 / R_pim(I) all: 0.109 / R_rim(I) all: 0.207 / Net I/σ(I): 6.3

Reflection shell

Diffraction-ID: 1 / Redundancy: 3.1 %

Resolution (Å)	Rmerge(I) obs	Num. unique obs	CC1/2	Rpim(I) all	Rrim(I) all	% possible all
3.19-3.25	0.861	7846	0.575	0.57	1.036	93.7
17.49-49.35	0.039	1017	0.999	0.027	0.048	94.7

Phasing

• Phasing: Method: molecular replacement

Phasing MR

R rigid body: 0.518

	Highest resolution	Lowest resolution
Rotation	49.35 Å	3.33 Å

Processing

Software

Name	Version	Classification
Aimless	0.3.11	data scaling
MOLREP	11.2.08	phasing
REFMAC	5.8.0071	refinement
PDB_EXTRACT	3.22	data extraction
XDS		data reduction

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: pdbid 4WSC

4wsc

Resolution: 3.19→50 Å / Cor.coef. F_o:F_c: 0.899 / Cor.coef. F_o:F_c free: 0.891 / SU B: 62.815 / SU ML: 0.444 / SU R Cruickshank DPI: 0.4858 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.477
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.2524	8289	4.9 %	RANDOM
Rwork	0.2446	-	-	-
obs	0.2449	160056	99.49 %	-

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

Displacement parameters

B_iso max: 227.07 Ų / B_iso mean: 83.96 Ų / B_iso min: 33.13 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	-1.69 Å2	-0 Å2	0.68 Å2
2-	-	-0.46 Å2	-0 Å2
3-	-	-	1.77 Å2

Refinement step

Cycle: final / Resolution: 3.19→50 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	53984	0	0	0	53984
Num. residues	-	-	-	-	7336

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.005	0.019	54383
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.02	54866
X-RAY DIFFRACTION	r_angle_refined_deg	0.822	1.988	73430
X-RAY DIFFRACTION	r_angle_other_deg	0.939	3	126420
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	3.733	5	7322
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	31.713	26.067	2100
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	12.621	15	10094
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	15.961	15	308
X-RAY DIFFRACTION	r_chiral_restr	0.045	0.2	8932
X-RAY DIFFRACTION	r_gen_planes_refined	0.002	0.02	61824
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	10248

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	32397	0.04
1	2	B	32397	0.04
2	1	A	32404	0.03
2	2	C	32404	0.03
3	1	A	32422	0.03
3	2	D	32422	0.03
4	1	A	32335	0.03
4	2	E	32335	0.03
5	1	A	32277	0.04
5	2	F	32277	0.04
6	1	A	32404	0.03
6	2	G	32404	0.03
7	1	A	32319	0.04
7	2	H	32319	0.04
8	1	A	32353	0.04
8	2	I	32353	0.04
9	1	A	32359	0.04
9	2	J	32359	0.04
10	1	A	32345	0.04
10	2	K	32345	0.04
11	1	A	32197	0.05
11	2	L	32197	0.05
12	1	A	32272	0.04
12	2	M	32272	0.04
13	1	A	32301	0.04
13	2	N	32301	0.04
14	1	B	32525	0.03
14	2	C	32525	0.03
15	1	B	32506	0.03
15	2	D	32506	0.03
16	1	B	32458	0.03
16	2	E	32458	0.03
17	1	B	32395	0.04
17	2	F	32395	0.04
18	1	B	32466	0.03
18	2	G	32466	0.03
19	1	B	32469	0.03
19	2	H	32469	0.03
20	1	B	32487	0.03
20	2	I	32487	0.03
21	1	B	32463	0.04
21	2	J	32463	0.04
22	1	B	32485	0.03
22	2	K	32485	0.03
23	1	B	32315	0.04
23	2	L	32315	0.04
24	1	B	32358	0.04
24	2	M	32358	0.04
25	1	B	32430	0.04
25	2	N	32430	0.04
26	1	C	32488	0.03
26	2	D	32488	0.03
27	1	C	32427	0.03
27	2	E	32427	0.03
28	1	C	32434	0.03
28	2	F	32434	0.03
29	1	C	32524	0.02
29	2	G	32524	0.02
30	1	C	32443	0.03
30	2	H	32443	0.03
31	1	C	32474	0.03
31	2	I	32474	0.03
32	1	C	32438	0.04
32	2	J	32438	0.04
33	1	C	32399	0.03
33	2	K	32399	0.03
34	1	C	32316	0.04
34	2	L	32316	0.04
35	1	C	32356	0.04
35	2	M	32356	0.04
36	1	C	32423	0.04
36	2	N	32423	0.04
37	1	D	32360	0.04
37	2	E	32360	0.04
38	1	D	32397	0.04
38	2	F	32397	0.04
39	1	D	32484	0.03
39	2	G	32484	0.03
40	1	D	32372	0.04
40	2	H	32372	0.04
41	1	D	32452	0.03
41	2	I	32452	0.03
42	1	D	32426	0.04
42	2	J	32426	0.04
43	1	D	32396	0.04
43	2	K	32396	0.04
44	1	D	32301	0.04
44	2	L	32301	0.04
45	1	D	32309	0.04
45	2	M	32309	0.04
46	1	D	32353	0.04
46	2	N	32353	0.04
47	1	E	32377	0.04
47	2	F	32377	0.04
48	1	E	32382	0.03
48	2	G	32382	0.03
49	1	E	32496	0.03
49	2	H	32496	0.03
50	1	E	32490	0.03
50	2	I	32490	0.03
51	1	E	32397	0.04
51	2	J	32397	0.04
52	1	E	32373	0.03
52	2	K	32373	0.03
53	1	E	32313	0.04
53	2	L	32313	0.04
54	1	E	32441	0.03
54	2	M	32441	0.03
55	1	E	32418	0.04
55	2	N	32418	0.04
56	1	F	32364	0.03
56	2	G	32364	0.03
57	1	F	32444	0.04
57	2	H	32444	0.04
58	1	F	32518	0.03
58	2	I	32518	0.03
59	1	F	32323	0.04
59	2	J	32323	0.04
60	1	F	32272	0.04
60	2	K	32272	0.04
61	1	F	32369	0.04
61	2	L	32369	0.04
62	1	F	32296	0.04
62	2	M	32296	0.04
63	1	F	32421	0.04
63	2	N	32421	0.04
64	1	G	32377	0.03
64	2	H	32377	0.03
65	1	G	32417	0.03
65	2	I	32417	0.03
66	1	G	32461	0.03
66	2	J	32461	0.03
67	1	G	32464	0.03
67	2	K	32464	0.03
68	1	G	32284	0.04
68	2	L	32284	0.04
69	1	G	32346	0.04
69	2	M	32346	0.04
70	1	G	32389	0.04
70	2	N	32389	0.04
71	1	H	32554	0.03
71	2	I	32554	0.03
72	1	H	32425	0.04
72	2	J	32425	0.04
73	1	H	32376	0.04
73	2	K	32376	0.04
74	1	H	32403	0.04
74	2	L	32403	0.04
75	1	H	32384	0.04
75	2	M	32384	0.04
76	1	H	32473	0.04
76	2	N	32473	0.04
77	1	I	32450	0.04
77	2	J	32450	0.04
78	1	I	32422	0.03
78	2	K	32422	0.03
79	1	I	32449	0.04
79	2	L	32449	0.04
80	1	I	32442	0.03
80	2	M	32442	0.03
81	1	I	32544	0.03
81	2	N	32544	0.03
82	1	J	32479	0.03
82	2	K	32479	0.03
83	1	J	32286	0.04
83	2	L	32286	0.04
84	1	J	32350	0.04
84	2	M	32350	0.04
85	1	J	32375	0.04
85	2	N	32375	0.04
86	1	K	32286	0.04
86	2	L	32286	0.04
87	1	K	32326	0.04
87	2	M	32326	0.04
88	1	K	32354	0.04
88	2	N	32354	0.04
89	1	L	32241	0.05
89	2	M	32241	0.05
90	1	L	32338	0.04
90	2	N	32338	0.04
91	1	M	32388	0.04
91	2	N	32388	0.04

LS refinement shell

Resolution: 3.193→3.276 Å / R_factor R_free error: 0 / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.34	614	-
Rwork	0.348	11339	-
all	-	11953	-
obs	-	-	96.02 %

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	3.0049	-0.6259	0.1202	2.7402	0.2733	0.3684	0.0288	0.0793	-0.0332	0.19	0.0554	0.0232	-0.0157	-0.0211	-0.0843	0.0376	0.002	-0.0374	0.0467	0.024	0.3375	60.2456	-9.6097	8.746
2	1.8002	1.6193	2.8261	2.2468	1.689	6.4789	0.1984	-0.048	-0.3422	-0.2105	-0.0201	-0.1002	0.5038	-0.4164	-0.1783	0.4172	0.0461	-0.0675	0.421	-0.1267	0.644	66.1217	-26.5463	-15.8812
3	4.0007	0.6368	0.6975	5.9534	-0.2311	3.0628	0.1015	0.3312	0.9183	-0.7394	0.0938	1.0854	-0.0937	-0.2562	-0.1953	0.771	-0.0121	-0.1925	0.7741	0.0701	1.1658	56.2228	-5.6896	-29.8703
4	2.2131	0.3446	0.2011	3.3067	-0.0457	0.9764	0.1419	0.0382	-0.1349	0.0434	-0.0763	-0.0492	0.1433	0.0572	-0.0656	0.0367	-0.0164	-0.0125	0.1446	-0.0358	0.4407	35.5946	-41.1017	9.2913
5	4.5687	-0.4396	2.1311	0.5617	-1.0288	4.8813	0.1524	0.0293	-0.271	-0.0783	0.1878	0.3635	0.2336	-0.22	-0.3402	0.514	-0.051	-0.076	0.3156	-0.1593	0.8685	25.7192	-56.7281	-14.9408
6	3.5482	1.7046	0.2073	5.4733	-0.6699	2.0751	-0.3051	0.7703	0.8537	-0.6136	0.5096	0.4513	-0.0521	0.0296	-0.2044	0.689	-0.1827	-0.0918	0.901	0.071	0.9904	36.2442	-36.4352	-29.1619
7	3.2428	0.2912	0.1743	2.5899	0.2028	0.8276	-0.0372	-0.1608	-0.0271	-0.0528	0.0051	-0.0339	0.1655	0.0286	0.0321	0.0478	0.0204	-0.0356	0.0227	-0.0403	0.33	-4.3588	-41.1852	9.7848
8	1.5448	-1.4194	1.3243	2.6059	-3.7002	6.05	0.0849	0.184	-0.1048	0.1432	0.1779	0.3644	-0.3952	-0.5204	-0.2627	0.3453	-0.043	-0.0536	0.2479	-0.0115	0.7102	-22.8903	-43.378	-14.3212
9	4.1117	-0.0966	0.0616	4.8619	0.1545	2.7479	0.1019	0.3989	1.0162	-0.3201	0.1604	-0.6766	-0.5245	0.2477	-0.2623	0.4571	-0.0082	0.0486	0.2994	0.0938	0.964	-0.6121	-39.1668	-28.8786
10	2.8728	-0.306	-0.1988	2.5213	0.3522	0.9995	-0.0482	0.0196	-0.0624	0.0391	0.0428	0.0277	-0.0545	-0.0757	0.0054	0.0167	0.0127	-0.0611	0.0123	-0.0392	0.3477	-29.3526	-10.3443	10.6928
11	1.8476	1.0348	-0.3097	6.4379	-4.5695	3.8247	0.455	0.214	0.4144	0.5289	-0.1604	0.2138	-0.6762	0.0516	-0.2946	0.6092	0.0395	0.0773	0.4386	0.0297	0.6987	-43.0851	2.4735	-13.2668
12	4.9104	-1.2441	0.4988	5.6339	-0.1291	4.7524	0.3397	0.6776	0.0908	-0.9023	-0.2685	-1.2446	-0.0117	0.2594	-0.0712	0.7927	0.1694	0.1724	0.5194	0.092	1.0313	-25.8948	-12.1349	-27.959
13	2.2762	-0.0382	-0.3308	3.5833	0.1577	0.9881	0.1152	0.0489	0.1677	0.1313	-0.0689	0.119	-0.1283	-0.1584	-0.0463	0.1166	-0.014	-0.0671	0.0379	0.0259	0.3916	-21.0177	28.6976	10.8966
14	3.0943	1.5333	-1.8174	1.1718	-1.3768	6.0268	-0.12	0.2175	0.4772	-0.3092	0.1694	0.178	-0.1868	0.4105	-0.0494	0.7205	-0.0305	-0.1251	0.3994	0.1907	0.8533	-20.1817	47.1596	-13.3455
15	3.2451	0.0853	-0.0426	5.5668	0.05	3.9209	-0.2963	0.5017	-0.9791	-0.7243	0.4085	-0.9892	0.2158	0.1719	-0.1122	1.1887	-0.2062	-0.0021	0.6872	-0.0131	1.2471	-21.7455	24.4271	-27.7046
16	2.3732	1.1137	-0.2671	2.8954	-0.0746	0.9819	0.0791	-0.1632	0.0667	0.0343	-0.0619	-0.0138	-0.0918	-0.0543	-0.0172	0.0534	0.0045	-0.1046	0.0249	0.022	0.429	14.869	46.08	9.9271
17	0.9968	-0.8798	-1.6509	1.1668	2.5545	6.2504	0.0246	0.0375	0.2892	0.02	0.2492	-0.3544	0.1686	0.7489	-0.2738	0.4219	0.0855	-0.0155	0.2678	-0.0045	0.7222	29.5612	56.1608	-14.8209
18	5.2994	-0.3284	-0.2247	3.8605	0.5096	2.7716	0.01	0.3037	-1.5188	-0.2108	0.1024	0.2651	0.6692	0.046	-0.1123	0.5697	0.0624	-0.0735	0.3349	-0.0983	1.0545	10.9306	42.4475	-28.6423
19	3.6221	-0.1999	0.1588	2.3863	0.1343	1.1448	-0.141	0.0149	0.0448	0.0298	0.1528	-0.1105	-0.1463	0.2258	-0.0117	0.1233	0.0286	-0.0533	0.1099	0.0562	0.3318	50.9326	29.0659	9.0607
20	0.6457	-0.4145	-0.1023	1.1748	2.1643	6.0107	0.2752	0.2083	-0.1892	-0.0512	0.0274	-0.3454	0.4385	0.3489	-0.3025	0.455	0.0843	-0.0361	0.7004	0.0864	0.8553	68.05	23.8326	-15.7332
21	6.6938	-0.4617	-0.2804	4.7481	-0.0348	4.2477	0.2052	0.6244	-0.6053	-0.5105	-0.2455	0.9375	0.0742	-0.2011	0.0404	0.6696	0.2941	-0.1763	0.7528	-0.1092	0.9736	45.9627	30.1345	-29.7837
22	3.2804	-0.0039	-0.0614	2.6072	-0.272	0.7432	-0.114	0.1582	0.0981	0.0516	0.1484	0.0812	-0.1018	-0.1268	-0.0344	0.1568	-0.0036	-0.0422	0.1282	0.0135	0.4098	-7.0147	39.9167	44.0013
23	2.4118	2.334	-0.0734	4.9717	-3.0726	4.9154	0.0767	-0.104	-0.0718	-0.0988	0.3238	0.3667	0.1755	-0.7583	-0.4005	0.4375	0.123	0.0446	0.5717	-0.0017	0.7235	-24.5778	40.3599	68.8946
24	4.9374	-0.3329	-0.5974	5.4153	-0.038	3.6776	0.2172	-0.2145	-0.3202	0.3141	-0.0179	-0.7021	0.0142	0.3329	-0.1993	0.598	0.046	-0.0537	0.6176	-0.0529	0.7974	-1.396	37.6559	82.3146
25	2.6932	0.1296	0.1118	2.2068	0.198	1.0642	0.0019	-0.0717	0.0041	-0.1381	-0.0231	0.0291	0.0438	-0.1845	0.0212	0.0656	-0.0086	-0.0413	0.1516	0.0004	0.3778	-29.3976	6.9257	44.1654
26	1.1178	0.7246	1.2825	4.936	-2.2801	5.2241	0.0578	-0.0757	-0.4173	0.1831	0.1195	0.175	0.538	-0.1424	-0.1773	0.4254	-0.0396	0.0097	0.579	0.0078	0.6622	-40.9505	-7.1213	68.6091
27	4.5371	1.9794	-0.4443	4.4794	-0.1643	3.2966	0.2737	-0.4404	-0.1125	0.6092	-0.1302	-0.8758	0.0937	0.1453	-0.1435	0.8013	-0.0578	-0.1181	0.6287	-0.0108	0.907	-24.5327	8.9761	82.6079
28	2.2201	-0.5262	-0.0003	3.1226	-0.0424	0.8167	0.0796	-0.0085	-0.1333	-0.0261	-0.0929	0.1195	0.189	-0.1023	0.0132	0.1802	-0.0178	-0.0041	0.1655	-0.0245	0.3669	-17.7805	-31.1875	43.6356
29	2.2543	-0.5595	2.4429	0.4483	-1.1569	5.7802	0.2074	0.1078	-0.3377	0.2511	-0.0764	-0.2345	0.2896	0.3614	-0.1309	0.8215	-0.065	-0.0378	0.4655	0.0502	0.9289	-14.4273	-49.6488	67.7303
30	3.5441	0.126	-0.4239	3.9324	0.4662	3.7499	0.1005	-0.3087	0.8013	0.4523	0.0963	-0.4112	-0.1829	-0.0301	-0.1968	0.9617	0.0467	-0.0206	0.6989	0.0374	1.0264	-16.8658	-27.1557	82.3135
31	3.8005	-1.1215	0.0219	2.4182	0.527	0.8515	0.0376	-0.0018	-0.1688	0.1796	-0.0068	-0.1409	0.1538	0.1155	-0.0308	0.1826	-0.003	-0.0565	0.1941	0.0317	0.437	19.3085	-45.8359	42.9683
32	3.9214	0.6988	1.1045	0.1849	0.0942	3.6539	0.3402	-0.0667	-0.2143	0.1955	0.1266	-0.1427	-0.1452	0.4817	-0.4669	0.8282	0.1576	-0.1016	0.8227	0.0934	1.0284	35.5012	-55.3936	67.0693
33	3.2969	-1.2206	-0.5094	1.7179	-0.5574	1.5947	0.1714	-0.252	0.4872	0.2387	0.1681	0.3544	-0.4518	-0.2266	-0.3395	1.2005	0.0786	0.0709	1.2037	0.1085	1.1877	15.9839	-44.1457	81.7781
34	3.2659	0.4834	-0.2202	2.0357	0.1036	0.9967	-0.0463	-0.0108	-0.0818	-0.0759	0.0582	-0.1263	0.0923	0.2223	-0.0119	0.1709	0.0093	-0.0674	0.2496	0.0334	0.3897	53.8079	-25.9456	42.4951
35	0.5653	1.0294	1.3388	3.8231	3.1575	6.2668	0.1698	-0.1327	0.1126	0.0508	0.1221	-0.3456	-0.543	0.3327	-0.292	0.5524	-0.0247	-0.0039	0.8736	0.039	0.8527	70.9645	-19.3399	66.903
36	3.5769	1.3272	0.7373	2.7503	0.261	2.4865	0.6598	-0.8664	0.1114	0.631	-0.7301	1.1887	0.0453	-0.2936	0.0703	1.1304	-0.3041	0.1704	1.3041	-0.0647	1.4077	49.9241	-27.5156	81.7111
37	2.936	0.2869	-0.3391	3.001	0.0844	0.8507	-0.0192	-0.0103	0.0408	-0.1214	0.0718	0.0476	-0.0804	0.1458	-0.0526	0.0764	-0.0043	-0.088	0.2129	0.0257	0.3667	59.9231	13.441	42.3687
38	2.3738	-2.1909	-2.0936	4.138	0.3831	6.3314	0.2116	-0.2886	0.3432	0.2009	0.2497	0.2194	-0.7925	-0.1816	-0.4613	0.5071	-0.0362	0.0272	0.6469	-0.0394	0.7247	65.168	30.8751	66.7892
39	1.6106	-0.2225	-0.4213	5.823	-1.0716	3.3211	-0.1363	-0.2406	-0.7785	0.5301	0.3163	1.472	0.114	-0.5399	-0.18	0.6343	0.067	0.2426	0.9389	0.0856	1.4094	57.5774	9.2223	80.9408
40	2.6558	-0.3279	-0.2096	3.2492	-0.0429	1.0886	0.1117	0.0679	0.1947	0.0508	-0.0329	-0.1104	-0.275	0.1733	-0.0788	0.1505	-0.0211	-0.0628	0.1761	-0.0009	0.4549	32.8417	42.8573	42.9014
41	3.5482	-1.1513	-3.6582	1.5189	1.2031	3.9619	-0.1069	-0.1013	0.1766	0.1865	0.2838	0.2466	0.0349	-0.2265	-0.177	0.742	0.0855	-0.1261	0.6746	-0.0351	0.8989	22.9274	57.7078	67.6153
42	2.525	-2.9293	-0.0132	4.8915	-0.2129	2.569	-0.4545	-1.0414	-1.3752	0.5003	0.7804	0.7326	0.2233	-0.1394	-0.3259	0.9287	0.1949	0.0192	1.3584	0.3553	1.6867	35.8077	38.4297	81.2544

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	2 - 135
2	X-RAY DIFFRACTION	1	A	410 - 525
3	X-RAY DIFFRACTION	2	A	136 - 190
4	X-RAY DIFFRACTION	2	A	375 - 409
5	X-RAY DIFFRACTION	3	A	191 - 374
6	X-RAY DIFFRACTION	4	B	2 - 135
7	X-RAY DIFFRACTION	4	B	410 - 525
8	X-RAY DIFFRACTION	5	B	136 - 190
9	X-RAY DIFFRACTION	5	B	375 - 409
10	X-RAY DIFFRACTION	6	B	191 - 374
11	X-RAY DIFFRACTION	7	C	2 - 135
12	X-RAY DIFFRACTION	7	C	410 - 525
13	X-RAY DIFFRACTION	8	C	136 - 190
14	X-RAY DIFFRACTION	8	C	375 - 409
15	X-RAY DIFFRACTION	9	C	191 - 374
16	X-RAY DIFFRACTION	10	D	2 - 135
17	X-RAY DIFFRACTION	10	D	410 - 525
18	X-RAY DIFFRACTION	11	D	136 - 190
19	X-RAY DIFFRACTION	11	D	375 - 409
20	X-RAY DIFFRACTION	12	D	191 - 374
21	X-RAY DIFFRACTION	13	E	2 - 135
22	X-RAY DIFFRACTION	13	E	410 - 525
23	X-RAY DIFFRACTION	14	E	136 - 190
24	X-RAY DIFFRACTION	14	E	375 - 409
25	X-RAY DIFFRACTION	15	E	191 - 374
26	X-RAY DIFFRACTION	16	F	2 - 135
27	X-RAY DIFFRACTION	16	F	410 - 525
28	X-RAY DIFFRACTION	17	F	136 - 190
29	X-RAY DIFFRACTION	17	F	375 - 409
30	X-RAY DIFFRACTION	18	F	191 - 374
31	X-RAY DIFFRACTION	19	G	2 - 135
32	X-RAY DIFFRACTION	19	G	410 - 525
33	X-RAY DIFFRACTION	20	G	136 - 190
34	X-RAY DIFFRACTION	20	G	375 - 409
35	X-RAY DIFFRACTION	21	G	191 - 374
36	X-RAY DIFFRACTION	22	H	2 - 135
37	X-RAY DIFFRACTION	22	H	410 - 525
38	X-RAY DIFFRACTION	23	H	136 - 190
39	X-RAY DIFFRACTION	23	H	375 - 409
40	X-RAY DIFFRACTION	24	H	191 - 374
41	X-RAY DIFFRACTION	25	I	2 - 135
42	X-RAY DIFFRACTION	25	I	410 - 525
43	X-RAY DIFFRACTION	26	I	136 - 190
44	X-RAY DIFFRACTION	26	I	375 - 409
45	X-RAY DIFFRACTION	27	I	191 - 374
46	X-RAY DIFFRACTION	28	J	2 - 135
47	X-RAY DIFFRACTION	28	J	410 - 525
48	X-RAY DIFFRACTION	29	J	136 - 190
49	X-RAY DIFFRACTION	29	J	375 - 409
50	X-RAY DIFFRACTION	30	J	191 - 374
51	X-RAY DIFFRACTION	31	K	2 - 135
52	X-RAY DIFFRACTION	31	K	410 - 525
53	X-RAY DIFFRACTION	32	K	136 - 190
54	X-RAY DIFFRACTION	32	K	375 - 409
55	X-RAY DIFFRACTION	33	K	191 - 374
56	X-RAY DIFFRACTION	34	L	2 - 135
57	X-RAY DIFFRACTION	34	L	410 - 525
58	X-RAY DIFFRACTION	35	L	136 - 190
59	X-RAY DIFFRACTION	35	L	375 - 409
60	X-RAY DIFFRACTION	36	L	191 - 374
61	X-RAY DIFFRACTION	37	M	2 - 135
62	X-RAY DIFFRACTION	37	M	410 - 525
63	X-RAY DIFFRACTION	38	M	136 - 190
64	X-RAY DIFFRACTION	38	M	375 - 409
65	X-RAY DIFFRACTION	39	M	191 - 374
66	X-RAY DIFFRACTION	40	N	2 - 135
67	X-RAY DIFFRACTION	40	N	410 - 525
68	X-RAY DIFFRACTION	41	N	136 - 190
69	X-RAY DIFFRACTION	41	N	375 - 409
70	X-RAY DIFFRACTION	42	N	191 - 374