PDB-2qc7: Crystal structure of the protein-disulfide isomerase related chap...

ID or keywords:

Entry

Database: PDB / ID: 2qc7

Title

Crystal structure of the protein-disulfide isomerase related chaperone ERp29

Components

Endoplasmic reticulum protein ERp29

Keywords

CHAPERONE / b domain (residues 33-153) / D domain (residues 154-261)

Function / homology

Function and homology information

regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / smooth endoplasmic reticulum / protein secretion / protein unfolding / negative regulation of protein secretion / intracellular protein transport / melanosome / protein folding / protein-folding chaperone binding / positive regulation of MAPK cascade ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Barak, N.N. / Sevvana, M. / Neumann, P. / Malesevic, M. / Naumann, K. / Fischer, G. / Sheldrick, G.M. / Stubbs, M.T. / Ferrari, D.M.

Citation

Journal: J.Mol.Biol. / Year: 2009
Title: Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29.
Authors: Barak, N.N. / Neumann, P. / Sevvana, M. / Schutkowski, M. / Naumann, K. / Malesevic, M. / Reichardt, H. / Fischer, G. / Stubbs, M.T. / Ferrari, D.M.

History

Deposition	Jun 19, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 24, 2008	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Aug 30, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2qc7.cif.gz	101 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2qc7_validation.pdf.gz	441.5 KB	Display	wwPDB validaton report
Full document	2qc7_full_validation.pdf.gz	480.2 KB	Display
Data in XML	2qc7_validation.xml.gz	22.1 KB	Display
Data in CIF	2qc7_validation.cif.gz	29.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qc/2qc7 ftp://data.pdbj.org/pub/pdb/validation_reports/qc/2qc7	HTTPS FTP

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Related structure data

Related structure data	1ovnS 1g7d 1g7e S: Starting model for refinement
Similar structure data	1oxq-d 3f7g-d 1oxn-d 6mq7-d 5urb-2 6cdf-2 6bfq-3 3omg-d 1yt5-1 6bfq-1 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#32 - Aug 2002 Chaperones similarity (1) #108 - Dec 2008 Hsp90 similarity (1) #110 - Feb 2009 Auxin and TIR1 Ubiquitin Ligase similarity (1)

Deposited unit

A: Endoplasmic reticulum protein ERp29

B: Endoplasmic reticulum protein ERp29

54.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Endoplasmic reticulum protein ERp29

defined by author
54.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Endoplasmic reticulum protein ERp29

defined by author
54.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	58.044, 68.025, 70.088
Angle α, β, γ (deg.)	90.00, 107.46, 90.00
Int Tables number	3
Space group name H-M	P121

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	VAL	VAL	LYS	LYS	6	A	A	33 - 36	2 - 5
2	1	1	VAL	VAL	LYS	LYS	6	B	B	33 - 36	2 - 5
3	2	1	GLY	GLY	TYR	TYR	1	A	A	37 - 47	6 - 16
4	2	1	GLY	GLY	TYR	TYR	1	B	B	37 - 47	6 - 16
5	3	1	LYS	LYS	LYS	LYS	3	A	A	48	17
6	3	1	LYS	LYS	LYS	LYS	3	B	B	48	17
7	4	1	VAL	VAL	LYS	LYS	1	A	A	49 - 52	18 - 21
8	4	1	VAL	VAL	LYS	LYS	1	B	B	49 - 52	18 - 21
9	5	1	LYS	LYS	LYS	LYS	3	A	A	54	23
10	5	1	LYS	LYS	LYS	LYS	3	B	B	54	23
11	6	1	PHE	PHE	VAL	VAL	1	A	A	55 - 58	24 - 27
12	6	1	PHE	PHE	VAL	VAL	1	B	B	55 - 58	24 - 27
13	7	1	TYR	TYR	LYS	LYS	6	A	A	66 - 69	35 - 38
14	7	1	TYR	TYR	LYS	LYS	6	B	B	66 - 69	35 - 38
15	8	1	GLN	GLN	PHE	PHE	1	A	A	70 - 73	39 - 42
16	8	1	GLN	GLN	PHE	PHE	1	B	B	70 - 73	39 - 42
17	9	1	ASP	ASP	TYR	TYR	6	A	A	95 - 96	64 - 65
18	9	1	ASP	ASP	TYR	TYR	6	B	B	95 - 96	64 - 65
19	10	1	GLY	GLY	ASP	ASP	1	A	A	97 - 98	66 - 67
20	10	1	GLY	GLY	ASP	ASP	1	B	B	97 - 98	66 - 67
21	11	1	LEU	LEU	LEU	LEU	3	A	A	100	69
22	11	1	LEU	LEU	LEU	LEU	3	B	B	100	69
23	12	1	ASN	ASN	ASN	ASN	1	A	A	101	70
24	12	1	ASN	ASN	ASN	ASN	1	B	B	101	70
25	13	1	ASP	ASP	ASP	ASP	1	A	A	111	80
26	13	1	ASP	ASP	ASP	ASP	1	B	B	111	80
27	14	1	SER	SER	PHE	PHE	1	A	A	114 - 121	83 - 90
28	14	1	SER	SER	PHE	PHE	1	B	B	114 - 121	83 - 90
29	15	1	ARG	ARG	ARG	ARG	3	A	A	122	91
30	15	1	ARG	ARG	ARG	ARG	3	B	B	122	91
31	16	1	ASP	ASP	TYR	TYR	1	A	A	123 - 132	92 - 101
32	16	1	ASP	ASP	TYR	TYR	1	B	B	123 - 132	92 - 101
33	17	1	LYS	LYS	LYS	LYS	3	A	A	137	106
34	17	1	LYS	LYS	LYS	LYS	3	B	B	137	106
35	18	1	VAL	VAL	GLN	GLN	1	A	A	138 - 142	107 - 111
36	18	1	VAL	VAL	GLN	GLN	1	B	B	138 - 142	107 - 111
37	19	1	ARG	ARG	ARG	ARG	3	A	A	170	139
38	19	1	ARG	ARG	ARG	ARG	3	B	B	170	139
39	20	1	ALA	ALA	VAL	VAL	1	A	A	171 - 174	140 - 143
40	20	1	ALA	ALA	VAL	VAL	1	B	B	171 - 174	140 - 143
41	21	1	GLU	GLU	ARG	ARG	3	A	A	175 - 177	144 - 146
42	21	1	GLU	GLU	ARG	ARG	3	B	B	175 - 177	144 - 146
43	22	1	GLN	GLN	LEU	LEU	1	A	A	178 - 181	147 - 150
44	22	1	GLN	GLN	LEU	LEU	1	B	B	178 - 181	147 - 150
45	23	1	LYS	LYS	GLN	GLN	3	A	A	182 - 185	151 - 154
46	23	1	LYS	LYS	GLN	GLN	3	B	B	182 - 185	151 - 154
47	24	1	SER	SER	SER	SER	3	A	A	189	158
48	24	1	SER	SER	SER	SER	3	B	B	189	158
49	25	1	SER	SER	LYS	LYS	1	A	A	190 - 192	159 - 161
50	25	1	SER	SER	LYS	LYS	1	B	B	190 - 192	159 - 161
51	26	1	LYS	LYS	GLY	GLY	1	A	A	197 - 213	166 - 182
52	26	1	LYS	LYS	GLY	GLY	1	B	B	197 - 213	166 - 182
53	27	1	GLU	GLU	ASP	ASP	6	A	A	214 - 215	183 - 184
54	27	1	GLU	GLU	ASP	ASP	6	B	B	214 - 215	183 - 184
55	28	1	PHE	PHE	ILE	ILE	1	A	A	216 - 228	185 - 197
56	28	1	PHE	PHE	ILE	ILE	1	B	B	216 - 228	185 - 197
57	29	1	GLU	GLU	LYS	LYS	3	A	A	229 - 230	198 - 199
58	29	1	GLU	GLU	LYS	LYS	3	B	B	229 - 230	198 - 199
59	30	1	ASN	ASN	GLY	GLY	1	A	A	231 - 236	200 - 205
60	30	1	ASN	ASN	GLY	GLY	1	B	B	231 - 236	200 - 205
61	31	1	LYS	LYS	LYS	LYS	3	A	A	237	206
62	31	1	LYS	LYS	LYS	LYS	3	B	B	237	206
63	32	1	LYS	LYS	GLU	GLU	1	A	A	238 - 239	207 - 208
64	32	1	LYS	LYS	GLU	GLU	1	B	B	238 - 239	207 - 208
65	33	1	GLU	GLU	GLU	GLU	3	A	A	240	209
66	33	1	GLU	GLU	GLU	GLU	3	B	B	240	209
67	34	1	LEU	LEU	PHE	PHE	1	A	A	241 - 251	210 - 220
68	34	1	LEU	LEU	PHE	PHE	1	B	B	241 - 251	210 - 220
69	35	1	GLN	GLN	ALA	ALA	6	A	A	252 - 256	221 - 225
70	35	1	GLN	GLN	ALA	ALA	6	B	B	252 - 256	221 - 225
1	1	2	LYS	LYS	LYS	LYS	3	A	A	59	28
2	1	2	LYS	LYS	LYS	LYS	3	B	B	59	28
3	2	2	PHE	PHE	PRO	PRO	1	A	A	60 - 65	29 - 34
4	2	2	PHE	PHE	PRO	PRO	1	B	B	60 - 65	29 - 34
5	3	2	LYS	LYS	LYS	LYS	3	A	A	74	43
6	3	2	LYS	LYS	LYS	LYS	3	B	B	74	43
7	4	2	ARG	ARG	SER	SER	1	A	A	75 - 94	44 - 63
8	4	2	ARG	ARG	SER	SER	1	B	B	75 - 94	44 - 63
9	5	2	LYS	LYS	LYS	LYS	3	A	A	99	68
10	5	2	LYS	LYS	LYS	LYS	3	B	B	99	68
11	6	2	MET	MET	GLU	GLU	3	A	A	102 - 103	71 - 72
12	6	2	MET	MET	GLU	GLU	3	B	B	102 - 103	71 - 72
13	7	2	LEU	LEU	GLU	GLU	1	A	A	104 - 106	73 - 75
14	7	2	LEU	LEU	GLU	GLU	1	B	B	104 - 106	73 - 75
15	8	2	LYS	LYS	LYS	LYS	3	A	A	107	76
16	8	2	LYS	LYS	LYS	LYS	3	B	B	107	76
17	9	2	TYR	TYR	TYR	TYR	1	A	A	108	77
18	9	2	TYR	TYR	TYR	TYR	1	B	B	108	77
19	10	2	LYS	LYS	LEU	LEU	3	A	A	109 - 110	78 - 79
20	10	2	LYS	LYS	LEU	LEU	3	B	B	109 - 110	78 - 79
21	11	2	LYS	LYS	GLU	GLU	3	A	A	112 - 113	81 - 82
22	11	2	LYS	LYS	GLU	GLU	3	B	B	112 - 113	81 - 82
23	12	2	THR	THR	THR	THR	3	A	A	133	102
24	12	2	THR	THR	THR	THR	3	B	B	133	102
25	13	2	GLY	GLY	VAL	VAL	1	A	A	134 - 136	103 - 105
26	13	2	GLY	GLY	VAL	VAL	1	B	B	134 - 136	103 - 105
27	14	2	ARG	ARG	ARG	ARG	3	A	A	143	112
28	14	2	ARG	ARG	ARG	ARG	3	B	B	143	112
29	15	2	TRP	TRP	LEU	LEU	1	A	A	144 - 145	113 - 114
30	15	2	TRP	TRP	LEU	LEU	1	B	B	144 - 145	113 - 114
31	16	2	LYS	LYS	LYS	LYS	3	A	A	146	115
32	16	2	LYS	LYS	LYS	LYS	3	B	B	146	115
33	17	2	GLY	GLY	PHE	PHE	1	A	A	147 - 168	116 - 137
34	17	2	GLY	GLY	PHE	PHE	1	B	B	147 - 168	116 - 137
35	18	2	ASP	ASP	LEU	LEU	6	A	A	186 - 188	155 - 157
36	18	2	ASP	ASP	LEU	LEU	6	B	B	186 - 188	155 - 157
37	19	2	GLU	GLU	LYS	LYS	3	A	A	193 - 196	162 - 165
38	19	2	GLU	GLU	LYS	LYS	3	B	B	193 - 196	162 - 165

NCS ensembles :

ID
1
2

#1: Protein	Endoplasmic reticulum protein ERp29 / ERp31 / ERp28 Mass: 27222.059 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERP29, C12orf8, ERP28 / Plasmid: pQE60 / Production host: Escherichia coli (E. coli) / References: UniProt: P30040

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.42 Å³/Da / Density % sol: 49.22 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and ...Details: 10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and 18-20% (w/v) PEG 2000 monomethyl ether. Crystals of about 0.1 mm in size grew in two days. , VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystal

Density Matthews: 2.42 Å³/Da / Density % sol: 49.22 %

Crystal grow

Temperature: 277 K / Method: vapor diffusion, hanging drop
Details: 10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and ...

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Data collection

Diffraction

Mean temperature: 180 K

Diffraction source

Source:

SYNCHROTRON / Site:

EMBL/DESY, HAMBURG

/ Beamline: BW7A / Wavelength: 0.96676 Å

Detector

Type: MAR CCD 130 mm / Detector: CCD / Date: May 21, 2003

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.96676 Å / Relative weight: 1

Reflection

Resolution: 2.9→28.981 Å / Num. obs: 11070 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.8 % / B_iso Wilson estimate: 89.5 Å² / R_merge(I) obs: 0.075 / R_sym value: 0.075 / Net I/σ(I): 7.3

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured all	Num. unique all	R_sym value	% possible all
2.9-3.06	5.9	0.599	1.3	10055	1712	0.599	100
3.06-3.24	5.9	0.348	2.2	9231	1575	0.348	100
3.24-3.47	5.9	0.228	3.2	7664	1299	0.228	85.1
3.47-3.74	5.9	0.137	5.3	7021	1194	0.137	85
3.74-4.1	5.8	0.091	7.7	6517	1116	0.091	86.1
4.1-4.59	5.8	0.061	11	6781	1160	0.061	100
4.59-5.29	5.9	0.055	12	6211	1058	0.055	100
5.29-6.48	5.8	0.063	10.7	5146	887	0.063	100
6.48-9.17	5.8	0.046	13.3	3945	684	0.046	100
9.17-29.98	5.4	0.034	16.2	2091	385	0.034	96.5

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Phasing

Phasing MR

	Highest resolution	Lowest resolution
Rotation	2.9 Å	29.98 Å
Translation	2.9 Å	29.98 Å

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Processing

Software

Name	Version	Classification
SCALA		data scaling
PHASER		phasing
REFMAC	5.2.0019	refinement
PDB_EXTRACT	2	data extraction
MAR345dtb		data collection
MOSFLM		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1OVN

1ovn

Resolution: 2.9→28.98 Å / Cor.coef. F_o:F_c: 0.925 / Cor.coef. F_o:F_c free: 0.913 / SU B: 65.046 / SU ML: 0.536 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic, TLS / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R Free: 0.486 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: Used NCS restraines and TLS refinement. 4 TLS groups were used, 2 for each of the monomers (one for b and d domain respectively.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.279	560	5.1 %	RANDOM
R_work	0.265	-	-	-
all	0.265	11701	-	-
obs	0.265	11068	94.69 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 54.235 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.11 Å²	0 Å²	7.49 Å²
2-	-	-3.12 Å²	0 Å²
3-	-	-	7.5 Å²

Refine analyze

	Free	Obs
Luzzati coordinate error	0.486 Å	-
Luzzati d res low	-	6 Å
Luzzati sigma a	0.536 Å	-

Refinement step

Cycle: LAST / Resolution: 2.9→28.98 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3526	0	0	0	3526

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.015	0.022	3598
X-RAY DIFFRACTION	r_angle_refined_deg	1.597	1.987	4838
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.066	5	444
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	42.033	25.25	160
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.726	15	674
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.328	15	14
X-RAY DIFFRACTION	r_chiral_restr	0.085	0.2	518
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	2690
X-RAY DIFFRACTION	r_nbd_refined	0.346	0.3	2145
X-RAY DIFFRACTION	r_nbtor_refined	0.361	0.5	2529
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.293	0.5	275
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.391	0.3	72
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.332	0.5	7
X-RAY DIFFRACTION	r_mcbond_it	0.771	2	2262
X-RAY DIFFRACTION	r_mcangle_it	1.272	3	3542
X-RAY DIFFRACTION	r_scbond_it	0.684	2	1515
X-RAY DIFFRACTION	r_scangle_it	1.083	3	1296

Refine LS restraints NCS

Dom-ID: 1 / Auth asym-ID: A / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Number	Type	Rms dev position (Å)	Weight position
1	939	TIGHT POSITIONAL	0.02	0.02
1	225	LOOSE POSITIONAL	1.5	5
1	939	TIGHT THERMAL	0.1	0.5
1	225	LOOSE THERMAL	1.75	10
2	493	TIGHT POSITIONAL	0.02	0.02
2	94	LOOSE POSITIONAL	0.99	5
2	493	TIGHT THERMAL	0.13	0.5
2	94	LOOSE THERMAL	1.49	10

LS refinement shell

Resolution: 2.9→3.055 Å / Total num. of bins used: 10

	R_factor	Num. reflection	% reflection
R_free	0.398	85	-
R_work	0.382	1612	-
obs	-	1697	100 %

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	12.1118	0.9623	-2.1799	3.7368	-0.0511	5.7262	0.0946	-1.3198	0.0445	0.4588	-0.0649	-0.0631	-0.3574	0.3596	-0.0298	-0.1921	-0.008	-0.0363	-0.0081	0.0082	-0.3659	9.9423	3.5766	6.3168
2	4.1708	1.5385	-0.4446	15.6081	1.5656	5.8948	0.0622	0.4644	0.4412	-1.6879	-0.0876	-0.0571	-0.1211	0.2484	0.0254	0.3212	0.0641	0.0406	-0.1221	0.0869	-0.0806	22.7622	-1.9323	-22.571
3	8.0089	0.3399	-3.3044	4.3841	0.0231	8.2142	0.1745	0.7299	-0.058	-0.43	0.0113	0.7535	-0.209	-0.902	-0.1857	0.2127	0.1098	-0.0639	0.0468	0.0168	-0.1833	13.8836	35.7125	22.7343
4	6.0875	1.4007	0.3499	19.4833	3.1268	3.5287	-0.1994	0.3106	0.0298	0.6691	0.248	-1.2312	0.2022	0.3382	-0.0486	0.2416	0.1237	-0.0052	-0.1205	0.097	-0.0652	44.2049	41.3948	14.347

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	33 - 154	2 - 123
2	X-RAY DIFFRACTION	2	A	A	155 - 256	124 - 225
3	X-RAY DIFFRACTION	3	B	B	33 - 154	2 - 123
4	X-RAY DIFFRACTION	4	B	B	155 - 256	124 - 225

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