PDB-7tlh: Murine meteorin C-terminal NTR domain

ID or keywords:

Entry

Database: PDB / ID: 7tlh

Title

Murine meteorin C-terminal NTR domain

Components

Meteorin

Keywords

SIGNALING PROTEIN / meteorin / NTR / neurotrophic factor

Function / homology

: / radial glial cell differentiation / positive regulation of axonogenesis / axonogenesis / extracellular space / Meteorin

Function and homology information

Biological species

Mus musculus (house mouse)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.74 Å

Authors

Quan, C. / Arndt, J.W.

Funding support

1items

Citation

Journal: To Be Published
Title: Identification and structure determination of stable domains of meteorin and meteorin-like
Authors: Quan, C. / Arndt, J.W. / Gong, B.J. / Dolnikova, J. / Pepinsky, R.B.

History

Deposition	Jan 18, 2022	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jan 25, 2023	Provider: repository / Type: Initial release
Revision 1.1	Oct 23, 2024	Group: Data collection / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim Item: _pdbx_entry_details.has_protein_modification / _struct_ncs_dom_lim.beg_auth_comp_id ..._pdbx_entry_details.has_protein_modification / _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

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7tlh.cif.gz	282.5 KB	Display	PDBx/mmCIF format
PDB format	pdb7tlh.ent.gz	234.8 KB	Display	PDB format
PDBx/mmJSON format	7tlh.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	7tlh_validation.pdf.gz	462.8 KB	Display	wwPDB validaton report
Full document	7tlh_full_validation.pdf.gz	467.4 KB	Display
Data in XML	7tlh_validation.xml.gz	22.1 KB	Display
Data in CIF	7tlh_validation.cif.gz	31.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/tl/7tlh ftp://data.pdbj.org/pub/pdb/validation_reports/tl/7tlh	HTTPS FTP

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Related structure data

Related structure data	7tl6C 7tlwC C: citing same article (ref.)
Similar structure data	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

Deposited unit

B: Meteorin

C: Meteorin

A: Meteorin

D: Meteorin

hetero molecules

59.2 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

B: Meteorin

hetero molecules

defined by author
Evidence: gel filtration
14.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Meteorin

hetero molecules

defined by author
14.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

A: Meteorin

hetero molecules

defined by author
14.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Meteorin

hetero molecules

defined by author
14.7 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	120.757, 75.672, 75.725
Angle α, β, γ (deg.)	90.000, 128.500, 90.000
Int Tables number	5
Space group name H-M	C121
Symmetry operation	#1: x,y,z #2: -x,y,-z #3: x+1/2,y+1/2,z #4: -x+1/2,y+1/2,-z

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain A and (resid 147 through 157 or resid 159...
2	1	(chain B and (resid 147 through 157 or resid 159...
3	1	(chain C and (resid 147 through 157 or resid 159 through 178 or resid 180 through 270))
4	1	(chain D and (resid 13 through 23 or resid 25...

NCS domain segments:

Ens-ID: 1

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	ALA	ALA	LEU	LEU	(chain A and (resid 147 through 157 or resid 159...	A	C	147 - 157	13 - 23
1	2	ALA	ALA	THR	THR	(chain A and (resid 147 through 157 or resid 159...	A	C	159 - 178	25 - 44
1	3	LEU	LEU	PHE	PHE	(chain A and (resid 147 through 157 or resid 159...	A	C	180 - 200	46 - 66
1	4	LYS	LYS	LYS	LYS	(chain A and (resid 147 through 157 or resid 159...	A	C	201	67
1	5	ALA	ALA	ASP	ASP	(chain A and (resid 147 through 157 or resid 159...	A	C	147 - 270	13 - 136
1	6	ALA	ALA	ASP	ASP	(chain A and (resid 147 through 157 or resid 159...	A	C	147 - 270	13 - 136
1	7	ALA	ALA	ASP	ASP	(chain A and (resid 147 through 157 or resid 159...	A	C	147 - 270	13 - 136
1	8	ALA	ALA	ASP	ASP	(chain A and (resid 147 through 157 or resid 159...	A	C	147 - 270	13 - 136
2	1	ALA	ALA	LEU	LEU	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 157	13 - 23
2	2	ALA	ALA	THR	THR	(chain B and (resid 147 through 157 or resid 159...	B	A	159 - 178	25 - 44
2	3	LEU	LEU	PHE	PHE	(chain B and (resid 147 through 157 or resid 159...	B	A	180 - 200	46 - 66
2	4	ALA	ALA	ASP	ASP	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 270	13 - 136
2	5	ALA	ALA	ASP	ASP	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 270	13 - 136
2	6	ALA	ALA	ASP	ASP	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 270	13 - 136
2	7	ALA	ALA	ASP	ASP	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 270	13 - 136
2	8	ALA	ALA	ASP	ASP	(chain B and (resid 147 through 157 or resid 159...	B	A	147 - 270	13 - 136
3	1	ALA	ALA	LEU	LEU	(chain C and (resid 147 through 157 or resid 159 through 178 or resid 180 through 270))	C	B	147 - 157	13 - 23
3	2	ALA	ALA	THR	THR	(chain C and (resid 147 through 157 or resid 159 through 178 or resid 180 through 270))	C	B	159 - 178	25 - 44
3	3	LEU	LEU	ASP	ASP	(chain C and (resid 147 through 157 or resid 159 through 178 or resid 180 through 270))	C	B	180 - 270	46 - 136
4	1	ALA	ALA	LEU	LEU	(chain D and (resid 13 through 23 or resid 25...	D	D	13 - 23	13 - 23
4	2	ALA	ALA	THR	THR	(chain D and (resid 13 through 23 or resid 25...	D	D	25 - 44	25 - 44
4	3	LEU	LEU	LYS	LYS	(chain D and (resid 13 through 23 or resid 25...	D	D	46 - 67	46 - 67
4	4	GLN	GLN	ASP	ASP	(chain D and (resid 13 through 23 or resid 25...	D	D	74 - 136	74 - 136

NCS oper:

ID	Code	Matrix	Vector
1	given	(0.61008532493, -0.628205404804, 0.482860089135), (0.616303534103, -0.0067569970697, -0.78747971202), (0.497961695472, 0.778018195395, 0.38304286637)	-25.5670852058, 134.864524925, 2.15168141249
2	given	(0.599786099883, 0.651718964303, 0.464240267485), (-0.617824546376, 0.00850734344603, 0.786269963183), (0.508477594671, -0.758412827341, 0.407750559831)	-72.7283803668, -59.4944696864, 58.4512011124
3	given	(0.235735799726, 0.00431559298754, 0.97180759844), (0.00126082661317, -0.999990656401, 0.00413490355586), (0.97181636282, 0.000250536086464, -0.235739038319)	-73.1880135708, 75.1049267635, 92.7373886801

#1: Protein	Meteorin / Hypoxia/reoxygenation regulatory factor Mass: 14651.735 Da / Num. of mol.: 4 / Fragment: NTR domain (UNP residues 156-291) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Metrn, Hyrac / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: Q8C1Q4
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Formula: SO₄
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 298 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	N
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.54 Å³/Da / Density % sol: 46.75 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 0.1 M Bis-Tris, pH 5.4, 1 M ammonium sulfate, 1% w/v PEG3350

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 31-ID / Wavelength: 1.25 Å
Detector	Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 4, 2013
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.25 Å / Relative weight: 1
Reflection	Resolution: 1.74→20 Å / Num. obs: 55117 / % possible obs: 99.8 % / Redundancy: 7.4 % / B_iso Wilson estimate: 22.78 Å² / R_merge(I) obs: 0.09 / Net I/σ(I): 10.2
Reflection shell	Resolution: 1.74→1.83 Å / Redundancy: 7.3 % / R_merge(I) obs: 1.21 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 8027 / % possible all: 100

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Processing

Software

Name	Version	Classification
PHENIX	1.19.2_4158	refinement
autoPROC		data reduction
SCALA		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.74→19.99 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 21.75 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.204	2866	5.2 %
R_work	0.172	52231	-
obs	0.1737	55097	99.84 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso max: 119.56 Å² / B_iso mean: 34.3121 Å² / B_iso min: 15.06 Å²

Refinement step

Cycle: final / Resolution: 1.74→19.99 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3703	0	30	298	4031
B_iso mean	-	-	62.71	38.09	-
Num. residues	-	-	-	-	487

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	2140	X-RAY DIFFRACTION	6.095	TORSIONAL
1	2	B	2140	X-RAY DIFFRACTION	6.095	TORSIONAL
1	3	C	2140	X-RAY DIFFRACTION	6.095	TORSIONAL
1	4	D	2140	X-RAY DIFFRACTION	6.095	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 20

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.74-1.77	0.3161	182	0.2902	2558	2740	100
1.77-1.8	0.3306	116	0.2612	2605	2721	100
1.8-1.83	0.2887	188	0.2508	2583	2771	100
1.83-1.87	0.2747	159	0.2249	2581	2740	100
1.87-1.91	0.2265	101	0.2185	2608	2709	100
1.91-1.95	0.263	115	0.199	2652	2767	100
1.95-2	0.1858	118	0.1756	2622	2740	100
2-2.06	0.2359	143	0.166	2622	2765	100
2.06-2.12	0.1769	163	0.1734	2584	2747	100
2.12-2.19	0.2007	141	0.1514	2594	2735	100
2.19-2.26	0.2023	133	0.1541	2627	2760	100
2.26-2.35	0.1622	116	0.1496	2635	2751	100
2.35-2.46	0.175	119	0.1595	2653	2772	100
2.46-2.59	0.2101	136	0.16	2585	2721	100
2.59-2.75	0.175	156	0.156	2664	2820	100
2.75-2.96	0.2039	136	0.174	2610	2746	100
2.96-3.26	0.1956	131	0.1661	2632	2763	100
3.26-3.73	0.1844	163	0.1621	2601	2764	100
3.73-4.69	0.157	173	0.1454	2621	2794	100
4.69-19.99	0.2608	177	0.1941	2594	2771	98

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	0.0721	0.1023	0.0663	0.0811	0.0859	0.0959	0.3302	-0.3032	-0.1589	0.4048	-0.3708	-0.4317	-0.394	0.0745	-0.0046	0.4437	-0.1015	-0.045	0.2741	-0.0604	0.3613	-35.6884	54.6977	50.5742
2	0.1072	0.058	-0.0883	0.1258	0.0361	0.1299	-0.0418	-0.2503	0.1902	-0.0623	0.0526	0.1332	0.1758	-0.1646	0.0001	0.3322	-0.0576	0.051	0.2562	-0.0563	0.3706	-44.3056	53.9644	42.7186
3	0.1459	-0.0665	-0.1568	1.1976	-0.0069	0.0788	0.0601	-0.0588	-0.0744	-0.0233	0.0521	-0.1378	0.0834	-0.1402	0	0.2373	-0.0506	0.0099	0.2286	0.0004	0.2046	-32.1096	69.5835	43.9588
4	0.0942	0.1645	-0.05	0.3494	-0.1039	0.0458	-0.1929	0.3238	-0.1939	-0.7444	-0.0147	0.2458	0.0749	-0.5808	-0.0088	0.3473	-0.0751	-0.08	0.3732	0.0135	0.3604	-42.8971	62.4602	31.9383
5	0.0802	0.0253	0.3654	1.348	0.2148	1.9517	-0.4729	0.4783	0.8845	-0.6742	-0.1866	0.4165	-0.838	-0.5239	-0.6361	0.6404	-0.0278	-0.1849	0.383	0.0651	0.4665	-39.6935	71.5278	31.0134
6	0.3511	0.3253	0.1726	0.3175	0.1847	0.106	0.0631	-0.0082	0.0894	0.0142	-0.1181	-0.293	0.0145	0.0898	0.0047	0.2345	-0.0484	-0.048	0.2383	0.0096	0.2501	-33.2756	68.4003	46.7475
7	0.0587	0.0921	-0.0489	0.1253	-0.077	0.057	0.1601	-0.2682	-0.4507	0.1629	0.5697	-0.8075	0.5449	0.272	0.0556	0.3314	0.0137	0.0912	0.2968	-0.0779	0.5765	-24.2817	63.256	42.3473
8	0.1286	-0.0243	-0.0023	0.1803	-0.1331	0.0547	-0.0597	0.2397	-0.2199	0.1215	-0.2309	0.4427	0.3122	-0.2844	0.0001	0.2947	-0.0606	0.0251	0.2616	-0.004	0.339	-40.1524	64.78	43.0078
9	0.3694	0.376	0.0381	0.347	0.3362	0.0759	0.0447	0.0574	-0.002	-0.1145	-0.0508	-0.1299	-0.0655	0.0305	-0	0.2697	-0.0407	0.0342	0.2135	-0.0128	0.2347	-37.7879	53.769	38.1895
10	0.1123	-0.1077	0.1039	0.1398	-0.076	0.0468	-0.1429	0.2939	0.0047	-0.7449	0.0013	0.542	-0.1132	0.1256	-0.0059	0.3589	-0.0331	-0.0232	0.2877	0.0128	0.2739	-46.4333	49.2206	33.2458
11	0.103	-0.057	0.0072	0.0444	-0.0277	0.0022	-0.2779	0.501	0.1025	0.1546	-0.2815	-0.2118	0.0457	0.5728	0.0004	0.2671	0.0306	0.0304	0.2858	0.0458	0.2941	-26.926	20.7998	40.2478
12	0.6745	-0.1472	-0.3957	0.6422	-0.0095	0.1306	0.1289	-0.0105	0.0641	-0.058	-0.0013	0.128	-0.0907	-0.0298	0.0001	0.2311	-0.0055	0.0085	0.2118	0.0118	0.2243	-36.2386	14.6855	39.3909
13	0.1809	0.402	0.0567	0.869	0.3022	0.5277	-0.1153	0.0565	0.0709	-0.016	0.0457	-0.0145	0.1492	-0.0368	-0.0002	0.2135	-0.0118	-0.0177	0.2429	0.0449	0.2517	-29.7243	3.6909	44.0097
14	1.3126	-1.1824	-0.8187	1.2135	0.2597	1.9522	-0.2065	0.3898	-0.4301	-0.4151	0.1595	0.4519	0.319	-0.3452	-0.1712	0.2844	-0.0795	-0.0917	0.3495	0.0153	0.4343	-45.2156	9.2636	35.9815
15	0.1685	-0.2372	0.1103	0.3444	-0.161	0.1248	0.0791	0.1534	0.049	0.2515	0.0153	-0.047	0.1445	-0.0048	0.0001	0.2399	-0.0145	-0.0079	0.2327	0.0273	0.2386	-30.2556	7.0215	42.9696
16	0.0361	0.0351	-0.0236	0.0306	-0.0261	-0.0052	-0.4832	-0.2181	0.3457	1.1517	0.2024	-0.0076	-0.1715	0.1082	-0.001	0.506	0.0339	0.0426	0.2819	0.016	0.3227	-33.8936	12.7656	52.1746
17	0.2261	0.0217	0.2118	0.1769	-0.0468	0.2184	0.0235	0.0613	0.127	-0.3586	0.0539	-0.0986	-0.1742	0.1734	-0	0.3179	-0.0289	0.0043	0.2181	0.0158	0.2535	-34.7106	10.1826	35.9948
18	0.3627	-0.1239	-0.5577	0.5245	-0.6292	0.8119	0.0797	0.0506	-0.0021	0.1414	-0.0115	0.233	-0.105	-0.0429	0.0001	0.1957	-0.0205	0.0036	0.1908	0.011	0.229	-39.6811	22.1072	39.8385
19	0.1545	-0.0597	0.1586	0.1408	-0.0539	0.1008	0.1311	-0.3881	-0.1577	-0.0268	0.2297	0.7688	0.0472	-0.3905	-0.0011	0.266	-0.0414	-0.0285	0.3663	0.0768	0.331	-46.0206	25.1881	32.4954
20	0.2112	-0.2774	-0.2022	0.3194	0.1802	0.2105	0.1331	-0.0416	0.2241	0.099	-0.1134	0.0537	0.3852	0.2625	-0.0004	0.2135	-0.0016	0.0476	0.2863	-0.0422	0.2739	-37.7784	44.0655	72.4957
21	0.0676	-0.0185	-0.1437	0.0222	-0.0391	0.2536	0.0364	-0.1197	0.0555	0.02	-0.0688	-0.0209	0.1083	0.0178	-0	0.2014	0.0018	-0.0011	0.2204	-0.0232	0.2193	-26.9108	34.1501	64.6695
22	0.2684	-0.2346	-0.2342	0.3524	-0.0755	0.6205	-0.0216	-0.2765	0.0973	-0.2169	-0.1145	-0.0034	-0.1008	-0.0379	-0.0004	0.2031	0.0005	0.0004	0.2287	-0.0423	0.2114	-20.6257	39.5996	63.8035
23	0.3713	0.1062	-0.1492	0.0973	-0.0067	0.0622	-0.0846	0.1064	-0.1914	-0.542	0.0677	-0.2096	-0.0151	-0.1197	-0.0002	0.293	-0.0396	0.0219	0.2718	-0.0639	0.2971	-35.6229	32.3933	56.0401
24	0.8414	-0.0111	0.0614	0.0609	0.0399	0.0402	-0.2233	-0.2638	-0.2235	0.1124	0.0772	-0.0983	0.3429	0.2467	-0.0055	0.2662	0.0379	0.0171	0.2702	-0.0162	0.2444	-23.5498	36.9209	68.0272
25	0.3915	-0.1377	0.1218	0.1548	0.038	0.1495	0.2047	-0.1431	0.3395	0.2016	-0.06	0.1655	-0.2659	0.0198	-0.0002	0.2356	0.0151	0.0326	0.2482	-0.0367	0.2817	-31.7806	41.3996	63.8
26	0.5582	-0.4601	-0.2193	0.5905	0.1242	0.1654	-0.2733	0.0182	-0.2099	0.1175	0.1566	0.0054	0.1592	-0.0261	0	0.1862	0.0078	0.0135	0.2235	-0.0206	0.1961	-39.4692	36.2931	71.7594
27	0.1275	-0.1165	0.0963	0.0785	0.0014	0.2399	-0.015	0.4409	-0.2938	-0.1932	0.4027	0.1298	0.1499	-0.4704	0.0086	0.2498	-0.017	0.0167	0.3459	-0.027	0.2796	-49.917	38.0933	69.3602
28	0.2393	-0.2299	-0.1901	0.3341	0.3244	0.3002	0.0079	-0.3965	-0.0068	0.0509	-0.0344	-0.0255	0.2879	0.2409	0	0.2785	0.028	0.0094	0.2827	0.0021	0.1947	-11.3779	31.3562	38.9761
29	0.6659	0.015	-0.2734	0.1602	0.1753	0.5561	-0.0112	-0.0457	0.0328	0.0479	0.0519	-0.0529	-0.0022	0.1468	-0.0001	0.2053	0.0143	-0.0194	0.1798	-0.0303	0.1902	-16.1612	38.5725	54.4173
30	0.1965	0.0153	-0.0427	0.0042	-0.0043	0.0692	0.0701	0.257	0.2666	-0.1271	-0.0477	0.5035	-0.1377	-0.2112	-0	0.2354	0.0129	-0.0129	0.1942	-0.0166	0.233	-24.0517	40.9121	39.3106
31	0.2582	0.0114	-0.28	-0.0004	-0.0083	0.3492	-0.0372	-0.0918	0.2964	0.1461	-0.0425	0.524	-0.3851	-0.6956	0.048	0.3368	0.0825	0.0174	0.3097	-0.0172	0.3275	-27.7141	41.5702	46.4672
32	0.0618	0.217	-0.0417	0.3945	-0.0696	0.6245	0.1759	-0.2864	0.0422	-0.3117	-0.0063	-0.1819	-0.0264	0.4864	0.0004	0.229	0.0022	0.0016	0.3197	-0.0486	0.2179	-12.4368	38.5063	53.8779
33	0.5095	-0.0783	0.184	0.1083	-0.0721	0.1568	-0.1773	-0.091	-0.2078	-0.047	-0.0527	-0.2772	0.308	0.2266	-0.0014	0.241	-0.0102	0.0125	0.2595	-0.0432	0.221	-18.573	33.9447	46.765
34	0.34	-0.1524	-0.207	0.29	0.0465	0.7669	0.0656	0.0062	0.087	0.002	0.0064	-0.0266	-0.1524	0.0056	0	0.2124	-0.011	0.0005	0.1923	-0.0145	0.1852	-14.2329	38.425	34.3135

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'B' and (resid 147 through 152 )	B	147 - 152
2	X-RAY DIFFRACTION	2	chain 'B' and (resid 153 through 164 )	B	153 - 164
3	X-RAY DIFFRACTION	3	chain 'B' and (resid 165 through 189 )	B	165 - 189
4	X-RAY DIFFRACTION	4	chain 'B' and (resid 190 through 195 )	B	190 - 195
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 196 through 209 )	B	196 - 209
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 210 through 219 )	B	210 - 219
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 220 through 226 )	B	220 - 226
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 227 through 237 )	B	227 - 237
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 238 through 259 )	B	238 - 259
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 260 through 270 )	B	260 - 270
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 147 through 152 )	C	147 - 152
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 153 through 177 )	C	153 - 177
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 178 through 189 )	C	178 - 189
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 190 through 209 )	C	190 - 209
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 210 through 219 )	C	210 - 219
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 220 through 227 )	C	220 - 227
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 228 through 237 )	C	228 - 237
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 238 through 260 )	C	238 - 260
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 261 through 270 )	C	261 - 270
20	X-RAY DIFFRACTION	20	chain 'A' and (resid 147 through 164 )	A	147 - 164
21	X-RAY DIFFRACTION	21	chain 'A' and (resid 165 through 177 )	A	165 - 177
22	X-RAY DIFFRACTION	22	chain 'A' and (resid 178 through 189 )	A	178 - 189
23	X-RAY DIFFRACTION	23	chain 'A' and (resid 190 through 209 )	A	190 - 209
24	X-RAY DIFFRACTION	24	chain 'A' and (resid 210 through 226 )	A	210 - 226
25	X-RAY DIFFRACTION	25	chain 'A' and (resid 227 through 237 )	A	227 - 237
26	X-RAY DIFFRACTION	26	chain 'A' and (resid 238 through 259 )	A	238 - 259
27	X-RAY DIFFRACTION	27	chain 'A' and (resid 260 through 270 )	A	260 - 270
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 13 through 30 )	D	13 - 30
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 31 through 55 )	D	31 - 55
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 56 through 61 )	D	56 - 61
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 62 through 75 )	D	62 - 75
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 76 through 92 )	D	76 - 92
33	X-RAY DIFFRACTION	33	chain 'D' and (resid 93 through 103 )	D	93 - 103
34	X-RAY DIFFRACTION	34	chain 'D' and (resid 104 through 136 )	D	104 - 136

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