PDB-6vhd: FphF, Staphylococcus aureus fluorophosphonate-binding serine hydr...

ID or keywords:

Entry

Database: PDB / ID: 6vhd

Title

FphF, Staphylococcus aureus fluorophosphonate-binding serine hydrolases F, KT129 bound

Components

Esterase family protein

Keywords

HYDROLASE / FphF / fluorophosphonate-binding / serine hydrolases / sodium bound / acyl / KT129 / intermediate

Function / homology

Function and homology information

S-formylglutathione hydrolase / S-formylglutathione hydrolase activity / formaldehyde catabolic process / carboxylic ester hydrolase activity / cytosol
Similarity search - Function

Biological species

Staphylococcus aureus (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.98 Å

Authors

Fellner, M. / Mace, P.D.

Citation

Journal: Acs Infect Dis. / Year: 2020
Title: Structural Basis for the Inhibitor and Substrate Specificity of the Unique Fph Serine Hydrolases of Staphylococcus aureus .
Authors: Fellner, M. / Lentz, C.S. / Jamieson, S.A. / Brewster, J.L. / Chen, L. / Bogyo, M. / Mace, P.D.

History

Deposition	Jan 9, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 16, 2020	Provider: repository / Type: Initial release
Revision 1.1	Oct 21, 2020	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2	Oct 11, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...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 ..._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 1.3	Nov 20, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6vhd.cif.gz	428.8 KB	Display	PDBx/mmCIF format
PDB format	pdb6vhd.ent.gz	355.5 KB	Display	PDB format
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Validation report

Summary document	6vhd_validation.pdf.gz	465.6 KB	Display	wwPDB validaton report
Full document	6vhd_full_validation.pdf.gz	468.3 KB	Display
Data in XML	6vhd_validation.xml.gz	2 KB	Display
Data in CIF	6vhd_validation.cif.gz	13 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/vh/6vhd ftp://data.pdbj.org/pub/pdb/validation_reports/vh/6vhd	HTTPS FTP

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Related structure data

Related structure data	6vh9SC 6vheC 6wcxC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6vhe-d 6vh9-d 6wcx-d 6jml-2 1g8j-2 4oy2-1 1g8j-1 6ouw-1 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

Deposited unit

A: Esterase family protein

B: Esterase family protein

C: Esterase family protein

D: Esterase family protein

hetero molecules

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

1

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	87.202, 87.202, 455.197
Angle α, β, γ (deg.)	90.000, 90.000, 120.000
Int Tables number	178
Space group name H-M	P6₁22

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain A and (resid -1 through 55 or resid 57 through 253 or resid 301))
2	1	(chain B and (resid -1 through 55 or resid 57 through 253 or resid 301))
3	1	(chain C and (resid -1 through 55 or resid 57 through 253 or resid 301))
4	1	(chain D and (resid -1 through 55 or resid 57 through 253 or resid 301))

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	GLY	GLY	TYR	TYR	(chain A and (resid -1 through 55 or resid 57 through 253 or resid 301))	A	A	-1 - 55	1 - 57
1	2	ARG	ARG	ASP	ASP	(chain A and (resid -1 through 55 or resid 57 through 253 or resid 301))	A	A	57 - 253	59 - 255
1	3	6WG	6WG	6WG	6WG	(chain A and (resid -1 through 55 or resid 57 through 253 or resid 301))	A	E	301
2	1	GLY	GLY	TYR	TYR	(chain B and (resid -1 through 55 or resid 57 through 253 or resid 301))	B	B	-1 - 55	1 - 57
2	2	ARG	ARG	ASP	ASP	(chain B and (resid -1 through 55 or resid 57 through 253 or resid 301))	B	B	57 - 253	59 - 255
2	3	6WG	6WG	6WG	6WG	(chain B and (resid -1 through 55 or resid 57 through 253 or resid 301))	B	F	301
3	1	GLY	GLY	TYR	TYR	(chain C and (resid -1 through 55 or resid 57 through 253 or resid 301))	C	C	-1 - 55	1 - 57
3	2	ARG	ARG	ASP	ASP	(chain C and (resid -1 through 55 or resid 57 through 253 or resid 301))	C	C	57 - 253	59 - 255
3	3	6WG	6WG	6WG	6WG	(chain C and (resid -1 through 55 or resid 57 through 253 or resid 301))	C	G	301
4	1	GLY	GLY	TYR	TYR	(chain D and (resid -1 through 55 or resid 57 through 253 or resid 301))	D	D	-1 - 55	1 - 57
4	2	ARG	ARG	ASP	ASP	(chain D and (resid -1 through 55 or resid 57 through 253 or resid 301))	D	D	57 - 253	59 - 255
4	3	6WG	6WG	6WG	6WG	(chain D and (resid -1 through 55 or resid 57 through 253 or resid 301))	D	H	301

#1: Protein	Esterase family protein / Putative esterase / Tributyrin esterase Mass: 29205.822 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus (bacteria) Gene: EP54_00010, EQ90_02595, HMPREF3211_01237, NCTC10654_02801, NCTC10702_04070, RK64_00235 Plasmid: M1366 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: A0A0D6GS23, UniProt: Q2FUY3*PLUS, S-formylglutathione hydrolase
#2: Chemical	ChemComp-6WG / (2~{R})-2-phenylpiperidine-1-carbaldehyde Mass: 189.254 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₂H₁₅NO / Feature type: SUBJECT OF INVESTIGATION
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 258 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y
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: 2.14 Å³/Da / Density % sol: 42.48 % / Mosaicity: 0.07 °
Crystal grow	Temperature: 289.15 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.2 uL ~7.5 mg/ml FphF+KT129 (0.12mM KT129, 12% DMSO, 18 mM HEPES pH 7.5, 8 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.2 M Sodium ...Details: 0.2 uL ~7.5 mg/ml FphF+KT129 (0.12mM KT129, 12% DMSO, 18 mM HEPES pH 7.5, 8 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.2 M Sodium citrate, 0.1 M Bis-Tris propane pH 6.5, 20% w/v PEG 3350. Crystals were soaked for ~20 seconds in 75% reservoir solution and 25% glycerol prior to freezing in liquid nitrogen

Crystal

Density Matthews: 2.14 Å³/Da / Density % sol: 42.48 % / Mosaicity: 0.07 °

Crystal grow

Temperature: 289.15 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 0.2 uL ~7.5 mg/ml FphF+KT129 (0.12mM KT129, 12% DMSO, 18 mM HEPES pH 7.5, 8 mM NaCl) were mixed with 0.2 uL of reservoir solution. Sitting drop reservoir contained 50 uL of 0.2 M Sodium ...

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

Australian Synchrotron

/ Beamline: MX2 / Wavelength: 0.954 Å

Detector

Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 31, 2019

Radiation

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

Radiation wavelength

Wavelength: 0.954 Å / Relative weight: 1

Reflection

Resolution: 1.98→49.28 Å / Num. obs: 73040 / % possible obs: 99.9 % / Redundancy: 27.1 % / CC_1/2: 0.999 / R_merge(I) obs: 0.151 / R_pim(I) all: 0.029 / R_rim(I) all: 0.154 / Net I/σ(I): 16.7

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. measured all	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Net I/σ(I) obs	% possible all
1.98-2.02	24.9	2.676	107296	4307	0.711	0.535	2.73	1.5	98.5
9.7-49.28	20.6	0.037	16651	809	1	0.008	0.038	63.1	99.4

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Phasing

Phasing

Method:

molecular replacement

Phasing MR

	Highest resolution	Lowest resolution
Rotation	7.29 Å	49.28 Å
Translation	7.29 Å	49.28 Å

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Processing

Software

Name	Version	Classification
XDS		data reduction
Aimless	0.7.4	data scaling
PHASER	2.8.3	phasing
PHENIX	dev-3699	refinement
PDB_EXTRACT	3.25	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 6VH9

6vh9

Resolution: 1.98→49.28 Å / SU ML: 0.23 / Cross valid method: THROUGHOUT / σ(F): 1.91 / Phase error: 23.04

	R_factor	Num. reflection	% reflection
R_free	0.2131	6711	4.99 %
R_work	0.1761	-	-
obs	0.178	72838	99.86 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Displacement parameters

B_iso max: 107.92 Å² / B_iso mean: 46.9353 Å² / B_iso min: 20.85 Å²

Refinement step

Cycle: final / Resolution: 1.98→49.28 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8236	0	56	258	8550
B_iso mean	-	-	55.99	48.31	-
Num. residues	-	-	-	-	1020

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	4885	X-RAY DIFFRACTION	8.434	TORSIONAL
1	2	B	4885	X-RAY DIFFRACTION	8.434	TORSIONAL
1	3	C	4885	X-RAY DIFFRACTION	8.434	TORSIONAL
1	4	D	4885	X-RAY DIFFRACTION	8.434	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.98-2	0.3331	205	0.3005	4055	4260	97
2-2.03	0.3022	253	0.282	4319	4572	100
2.03-2.05	0.3247	216	0.2714	4184	4400	100
2.05-2.08	0.2855	235	0.2798	4322	4557	100
2.08-2.1	0.3236	233	0.261	4191	4424	100
2.1-2.13	0.2939	236	0.2501	4327	4563	100
2.13-2.16	0.2807	219	0.2345	4238	4457	100
2.16-2.2	0.2927	214	0.2354	4295	4509	100
2.2-2.23	0.2553	237	0.2263	4276	4513	100
2.23-2.27	0.2965	210	0.2231	4237	4447	100
2.27-2.31	0.2401	216	0.2158	4294	4510	100
2.31-2.35	0.2144	215	0.2135	4292	4507	100
2.35-2.39	0.2366	219	0.2074	4218	4437	100
2.39-2.44	0.2673	221	0.2066	4304	4525	100
2.44-2.49	0.2741	245	0.2043	4261	4506	100
2.49-2.55	0.2841	219	0.1972	4267	4486	100
2.55-2.62	0.2808	222	0.2007	4244	4466	100
2.62-2.69	0.1958	196	0.1805	4295	4491	100
2.69-2.77	0.2341	191	0.182	4276	4467	100
2.77-2.86	0.2414	226	0.1812	4315	4541	100
2.86-2.96	0.1982	227	0.1878	4256	4483	100
2.96-3.08	0.23	188	0.1847	4310	4498	100
3.08-3.22	0.1999	211	0.1904	4294	4505	100
3.22-3.39	0.2294	250	0.174	4223	4473	100
3.39-3.6	0.1677	230	0.1564	4279	4509	100
3.6-3.88	0.1747	266	0.1444	4198	4464	100
3.88-4.26	0.1984	241	0.1385	4257	4498	100
4.27-4.88	0.1712	231	0.1251	4272	4503	100
4.88-6.15	0.1716	213	0.1531	4281	4494	100
6.15-49.28	0.1851	226	0.1604	4269	4495	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	1.1434	1.3335	1.8276	2.5436	1.8851	2.2143	0.0337	-0.1363	-0.0084	-0.1949	0.1046	-0.3121	0.2002	0.5455	-0.1804	0.2502	0.0897	0.0071	0.3068	0.0498	0.3056	-35.1209	33.7418	-11.7352
2	8.8748	-5.7791	7.0367	2.0957	-9.6923	9.8257	0.5599	0.6476	-0.4032	-0.9154	-0.0432	0.2906	1.061	-0.0937	-0.4782	0.5631	0.0007	-0.0755	0.3879	-0.059	0.3912	-43.7634	22.4596	-27.385
3	1.6198	0.2405	-0.3185	1.3015	0.3374	4.1657	0.0933	0.0118	0.0864	0.0262	-0.1128	-0.1199	0.1851	0.1257	0.0196	0.1779	0.0374	-0.003	0.2105	0.0677	0.2565	-31.5255	26.8527	-7.4674
4	4.5313	0.3143	2.4242	4.3701	-1.1938	7.564	0.3098	-0.3898	-0.5248	0.2785	-0.1206	0.1083	0.6376	-0.2157	-0.208	0.2991	0.0133	0.0369	0.2006	0.0236	0.278	-34.9354	17.4788	-4.0227
5	9.1395	2.4576	-1.5328	8.8293	-3.4235	4.8764	0.2368	-0.7237	-0.9189	0.406	-0.5368	-1.0809	0.4176	1.1375	0.3084	0.4242	0.0337	-0.0785	0.6514	0.0649	0.4425	-21.9084	28.0317	10.5452
6	5.8697	4.947	3.3772	2.2394	8.9389	9.2358	0.0415	-0.6712	0.0007	1.3329	-0.1666	0.5787	1.1102	-0.1157	0.0557	0.6058	0.0051	0.0128	0.378	0.1303	0.3862	-33.5529	16.8737	13.3493
7	6.8558	-0.8901	0.7316	3.4944	0.2289	5.7484	-0.118	-0.3205	-0.4973	0.1365	-0.0794	-0.0722	0.7713	0.0961	0.1811	0.4506	0.0491	-0.0219	0.2208	0.1216	0.3462	-28.2596	10.6727	-0.3425
8	6.2886	2.7558	0.0675	5.0988	-1.2164	4.0572	0.1093	-0.2578	-0.5824	0.2982	-0.1716	-0.3279	0.8604	0.4279	0.0908	0.5039	0.1429	-0.0258	0.3067	0.0963	0.4091	-23.5865	7.1917	1.939
9	6.768	5.4409	3.9304	6.6233	3.5422	7.9118	0.3963	0.0608	-0.7155	0.3452	-0.1819	-0.3232	0.8399	0.2544	-0.2205	0.4266	0.1546	0.014	0.2865	0.0439	0.3515	-25.006	13.6686	-12.7454
10	1.5668	1.0216	-0.2891	5.6556	-2.2255	5.8842	-0.0524	0.2807	0.1232	-0.4097	0.0508	-0.3263	-0.3999	0.3429	0.0001	0.2098	0.0223	0.043	0.3848	0.0242	0.3488	-16.5705	49.0926	-15.1461
11	1.9948	-0.3888	0.4514	1.4892	-0.3991	5.9995	0.1169	0.0064	0.0635	0.0228	-0.0619	-0.0222	-0.4845	0.1995	-0.0668	0.1885	-0.0235	0.0168	0.2199	-0.0099	0.2609	-23.5974	51.9711	-4.2099
12	2.8704	2.3017	0.3136	7.1099	-0.0746	4.2055	0.2703	-0.5315	0.0921	0.3118	-0.2379	0.5969	-0.2469	-0.5061	-0.044	0.3259	0.007	-0.0025	0.4552	-0.0298	0.3278	-31.0325	53.7538	6.2881
13	2.4711	3.0043	0.8532	7.828	2.8551	7.5755	0.3668	-0.4076	0.0611	0.6212	-0.3593	0.1093	-0.2887	-0.0313	-0.0235	0.2977	-0.019	0.0177	0.4196	-0.0469	0.2942	-26.3634	53.7205	16.474
14	5.7287	0.2336	2.0777	4.7764	1.3139	8.4012	-0.0015	-0.4704	0.6886	0.339	-0.0414	0.0121	-1.6053	-0.3158	0.0892	0.7118	0.0389	0.0777	0.3088	-0.029	0.4209	-31.1345	66.0101	6.9544
15	2.2018	3.3283	5.0989	9.6861	2.5477	8.1568	-0.3107	-0.2502	0.8804	-0.3277	-0.1134	0.4267	-1.8415	-0.45	0.5907	0.7717	0.1157	0.1048	0.4726	-0.1141	0.5407	-33.8268	67.776	1.9886
16	6.9666	0.461	-2.8275	8.8973	-2.4806	6.0211	0.4521	0.0553	0.9403	0.0558	-0.2888	-0.1024	-1.2499	-0.0484	-0.2055	0.5569	0.0543	-0.0268	0.3128	0.004	0.3498	-30.7672	63.6993	-9.0471
17	0.6251	0.5021	-1.1678	2.4185	-0.0194	4.3771	0.0602	-0.0726	-0.1237	0.2333	0.0936	-0.1442	0.0069	0.8072	-0.1634	0.2131	0.0422	0.0051	0.4446	0.0024	0.3159	-13.2688	43.499	-17.2886
18	1.0329	0.4219	-0.4953	2.0758	0.3204	1.9014	-0.0279	0.2227	0.0484	-0.0462	0.0635	-0.0421	0.0034	0.4757	-0.0444	0.1911	0.0745	0.0387	0.5625	0.0415	0.3171	-13.2271	37.1757	-27.6587
19	4.7037	1.4794	0.4187	4.0277	-0.2602	2.8749	0.037	0.5852	-0.0112	-0.2774	0.0511	-0.0804	-0.1166	0.2952	-0.1125	0.2604	0.1545	0.0441	0.7559	-0.0006	0.3305	-6.5707	33.0465	-36.5634
20	9.5618	-0.0869	-2.0925	1.1833	-0.1257	2.9988	-0.1368	1.3994	0.0891	-0.3776	0.1267	0.1983	0.232	0.1665	0.0474	0.4867	0.0986	-0.0011	0.8375	-0.0179	0.3943	-14.0266	32.8088	-48.1532
21	4.6169	0.568	-2.203	1.815	0.4197	4.0054	-0.0766	0.2269	-0.1657	-0.1055	0.0784	-0.2467	0.3425	0.5915	0.0316	0.3122	0.2103	0.0269	0.6499	-0.0046	0.3761	-4.6329	23.0059	-34.1972
22	2.2059	1.4891	0.7776	1.2685	-0.3974	2.1643	0.1952	-0.0076	0.0157	-0.1224	-0.0134	-0.272	-0.2226	0.3118	-0.155	0.2643	0.1077	0.0107	0.3375	0.0871	0.318	-35.2249	36.2987	-24.777
23	0.1389	0.9832	-1.0825	5.6519	-5.0712	6.3186	-0.0037	-0.0296	0.0492	0.101	0.1204	0.2297	-0.026	-0.3241	-0.1287	0.212	0.0847	-0.0283	0.3835	-0.0065	0.2713	-45.1211	39.2871	-19.2195
24	2.1252	1.6661	0.9734	3.6049	0.975	2.3644	-0.0477	0.0568	0.2094	0.0897	-0.108	0.1375	-0.3907	-0.3812	0.1394	0.328	0.1391	-0.045	0.4504	0.071	0.3478	-40.7015	48.9016	-19.1304
25	0.5132	-0.4288	0.8345	2.6989	-0.8897	3.2607	0.0211	0.2926	0.0144	-0.1639	-0.0427	0.0048	-0.1398	-0.2307	0.0206	0.1998	0.1004	-0.0329	0.4374	0.0464	0.3235	-42.0235	40.7335	-34.3833
26	8.3621	2.5177	-1.5453	5.4178	2.8357	2.515	0.0382	0.0385	0.0693	-0.4204	-0.0854	-0.0589	-0.2123	-0.3141	0.042	0.2931	0.1716	-0.0723	0.3718	0.1042	0.3358	-47.8294	49.1397	-36.2281
27	7.183	1.6674	6.1867	7.3548	2.6335	6.2572	-0.5574	0.8652	0.7109	-0.6102	0.4691	0.1834	-1.0406	0.5605	0.0613	0.5462	0.0182	0.0206	0.7332	0.1228	0.4874	-29.5209	52.3641	-44.9948
28	2.1294	2.0504	-2.5244	6.5107	-1.3789	7.0743	-0.0385	1.163	-0.0921	-0.5404	-0.2093	-0.4082	-0.0229	0.5846	0.2982	0.5125	0.2004	-0.0784	0.6875	0.0371	0.3835	-44.3427	48.8958	-50.6608
29	2.2889	1.2132	0.1706	4.8327	0.2156	3.4988	0.018	0.0698	0.0113	-0.2588	-0.0694	0.1614	-0.4186	-0.3241	0.0712	0.3871	0.1804	-0.0845	0.4454	0.1129	0.3513	-49.2262	55.2674	-36.9205
30	2.0661	9.4348	5.7206	8.9437	6.0243	6.5311	-0.2565	0.4904	0.3248	-0.3901	0.1585	0.2259	-0.849	-0.3312	0.1744	0.639	0.3033	0.0002	0.6063	0.118	0.4727	-50.163	61.3427	-43.259
31	6.3126	-0.5783	5.6423	0.2422	-0.547	5.5325	-0.316	-0.0624	0.4134	-0.0105	0.0312	0.2607	-1.4171	-0.505	0.4189	0.5622	0.2947	-0.0438	0.5956	0.0492	0.4489	-48.6042	61.294	-33.3747
32	6.0048	1.107	-0.6554	5.9004	-0.4526	4.9061	-0.0978	0.3588	0.6638	0.1418	0.2598	0.7757	-0.7407	-0.9426	-0.1845	0.412	0.2185	-0.0524	0.4528	0.0703	0.3504	-47.0321	55.3539	-23.9113

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid -1 through 24 )	A	-1 - 24
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 25 through 40 )	A	25 - 40
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 41 through 105 )	A	41 - 105
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 106 through 149 )	A	106 - 149
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 150 through 167 )	A	150 - 167
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 168 through 189 )	A	168 - 189
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 190 through 207 )	A	190 - 207
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 208 through 235 )	A	208 - 235
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 236 through 253 )	A	236 - 253
10	X-RAY DIFFRACTION	10	chain 'B' and (resid -1 through 40 )	B	-1 - 40
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 41 through 133 )	B	41 - 133
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 134 through 162 )	B	134 - 162
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 163 through 189 )	B	163 - 189
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 190 through 220 )	B	190 - 220
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 221 through 235 )	B	221 - 235
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 236 through 253 )	B	236 - 253
17	X-RAY DIFFRACTION	17	chain 'C' and (resid -1 through 40 )	C	-1 - 40
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 41 through 121 )	C	41 - 121
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 122 through 149 )	C	122 - 149
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 150 through 189 )	C	150 - 189
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 190 through 253 )	C	190 - 253
22	X-RAY DIFFRACTION	22	chain 'D' and (resid -1 through 24 )	D	-1 - 24
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 25 through 53 )	D	25 - 53
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 54 through 74 )	D	54 - 74
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 75 through 133 )	D	75 - 133
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 134 through 149 )	D	134 - 149
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 150 through 167 )	D	150 - 167
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 168 through 189 )	D	168 - 189
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 190 through 207 )	D	190 - 207
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 208 through 221 )	D	208 - 221
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 222 through 235 )	D	222 - 235
32	X-RAY DIFFRACTION	32	chain 'D' and (resid 236 through 253 )	D	236 - 253

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