PDB-5bq2: Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransf...

ID or keywords:

Entry

Database: PDB / ID: 5bq2

Title

Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa

Components

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Keywords

TRANSFERASE / SSGCID / UDP-N-acetylglucosamine 1-carboxyvinyltransferase / UDP-N-acetylglucosamine enolpyruvyl transferase / Enoylpyruvate transferase / EPT / murA / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease

Function / homology

Function and homology information

UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity / UDP-N-acetylgalactosamine biosynthetic process / UDP-N-acetylglucosamine 1-carboxyvinyltransferase / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / cell division / cytoplasm
Similarity search - Function

Biological species

Pseudomonas aeruginosa PAO1 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.7 Å

Authors

SSGCID / Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Citation

Journal: to be published
Title: Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
Authors: Abendroth, J. / Dranow, D.M. / Lorimer, D.D. / Edwards, T.E.

History

Deposition	May 28, 2015	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 15, 2015	Provider: repository / Type: Initial release
Revision 1.1	Sep 27, 2023	Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description / Source and taxonomy Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / entity_src_gen / pdbx_initial_refinement_model / pdbx_prerelease_seq / pdbx_struct_conn_angle / pdbx_struct_oper_list / pdbx_validate_close_contact / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Revision 1.2	Nov 15, 2023	Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.3	Oct 16, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5bq2.cif.gz	696.8 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	5bq2_validation.pdf.gz	1.9 MB	Display	wwPDB validaton report
Full document	5bq2_full_validation.pdf.gz	1.9 MB	Display
Data in XML	5bq2_validation.xml.gz	82.2 KB	Display
Data in CIF	5bq2_validation.cif.gz	123.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/bq/5bq2 ftp://data.pdbj.org/pub/pdb/validation_reports/bq/5bq2	HTTPS FTP

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Related structure data

Related structure data	3vcyS S: Starting model for refinement
Similar structure data	6q0a-1 6cn1-2 3swd-15 3swd-13 6q0y-1 3swe-2 1ryw-1 3v4t-2 3v4t-1 3swd-14 Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetTrack: PsaeA.00952.a

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#218 - Feb 2018 EPSP Synthase and Weedkillers similarity (4)

Deposited unit

A: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

B: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

C: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

D: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

hetero molecules

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

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	130.170, 166.810, 81.450
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	18
Space group name H-M	P2₁2₁2

#1: Protein	UDP-N-acetylglucosamine 1-carboxyvinyltransferase / Enoylpyruvate transferase / UDP-N-acetylglucosamine enolpyruvyl transferase / EPT Mass: 45891.738 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria) / Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 / Gene: murA, PA4450 / Plasmid: PsaeA.00952.a.B1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q9HVW7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase
#2: Chemical	ChemComp-EPU / URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID / ENOLPYRUVYL-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE Mass: 677.400 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₀H₂₉N₃O₁₉P₂
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 2048 / Source method: isolated from a natural source / Formula: H₂O
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: 2.42 Å³/Da / Density % sol: 49 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, sitting drop Details: Microlytics MCSG1 A11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH pH 6.5, PsaeA.00952.a.B1.PS02212 at 17mg/ml + 3mM UDP-N-acetylglucosamine + 3mM phosphoenolpyruvate, cryo: 20% EG in 2 steps; ...Details: Microlytics MCSG1 A11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH pH 6.5, PsaeA.00952.a.B1.PS02212 at 17mg/ml + 3mM UDP-N-acetylglucosamine + 3mM phosphoenolpyruvate, cryo: 20% EG in 2 steps; tray 260011a11, puck fvw9-7

Crystal

Density Matthews: 2.42 Å³/Da / Density % sol: 49 %

Crystal grow

Temperature: 290 K / Method: vapor diffusion, sitting drop
Details: Microlytics MCSG1 A11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH pH 6.5, PsaeA.00952.a.B1.PS02212 at 17mg/ml + 3mM UDP-N-acetylglucosamine + 3mM phosphoenolpyruvate, cryo: 20% EG in 2 steps; ...

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 21-ID-F / Wavelength: 0.97872 Å

Detector

Type: RAYONIX MX-225 / Detector: CCD / Date: Apr 2, 2015

Radiation

Monochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.97872 Å / Relative weight: 1

Reflection

Resolution: 1.7→50 Å / Num. all: 194666 / Num. obs: 193295 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 4 % / B_iso Wilson estimate: 13 Å² / R_merge F obs: 0.997 / R_merge(I) obs: 0.083 / R_rim(I) all: 0.095 / Χ²: 0.983 / Net I/σ(I): 12.07 / Num. measured all: 780951

Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)	Highest resolution (Å)	Redundancy (%)	R_merge F obs	R_merge(I) obs	Mean I/σ(I) obs	Num. measured obs	Num. possible	Num. unique obs	R_rim(I) all	% possible all
1.7-1.74		4.1	0.821	0.459	2.88	58698	14261	14225	0.526	99.7
1.74-1.79			0.876	0.373	3.52	57170	13888	13861	0.428	99.8
1.79-1.84			0.903	0.326	4.06	55896	13543	13500	0.373	99.7
1.84-1.9			0.934	0.263	5.08	53938	13131	13081	0.302	99.6
1.9-1.96			0.951	0.22	6.11	52195	12772	12700	0.253	99.4
1.96-2.03			0.965	0.183	7.42	50301	12360	12284	0.21	99.4
2.03-2.11			0.975	0.153	8.78	48152	11900	11823	0.176	99.4
2.11-2.19			0.981	0.128	10.33	46161	11508	11452	0.147	99.5
2.19-2.29			0.985	0.115	11.42	44112	11052	10963	0.133	99.2
2.29-2.4			0.989	0.097	13.24	41776	10545	10480	0.111	99.4
2.4-2.53			0.991	0.089	14.26	39863	10030	9969	0.102	99.4
2.53-2.69			0.992	0.079	15.63	37795	9522	9488	0.091	99.6
2.69-2.87			0.994	0.067	17.79	35215	8949	8913	0.077	99.6
2.87-3.1			0.996	0.059	19.88	32994	8390	8347	0.068	99.5
3.1-3.4			0.997	0.049	22.85	30035	7726	7663	0.057	99.2
3.4-3.8			0.997	0.043	25.67	27127	6994	6930	0.05	99.1
3.8-4.39			0.998	0.038	27.54	23910	6218	6137	0.043	98.7
4.39-5.38			0.998	0.035	28.59	20476	5300	5237	0.04	98.8
5.38-7.6			0.999	0.032	27.79	16440	4172	4057	0.037	97.2
	7.6		0.999	0.024	30.58	8697	2405	2185	0.028	90.9

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Phasing

Phasing

Method:

molecular replacement

Phasing MR

Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	6.67 Å	43.41 Å
Translation	6.67 Å	43.41 Å

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Processing

Software

Name	Classification
XDS	data reduction
XSCALE	data scaling
PHASER	phasing
ARP	model building
Coot	model building
PHENIX	refinement

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB entry 3vcy modified with CCP4 program CHAINSAW

3vcy

Resolution: 1.7→43.414 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 17.25 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.1809	9570	4.95 %	Random selection
R_work	0.1484	183696	-	-
obs	0.1501	193266	99.29 %	-

Solvent computation

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

Displacement parameters

B_iso max: 60.33 Å² / B_iso mean: 17.1776 Å² / B_iso min: 4.87 Å²

Refinement step

Cycle: final / Resolution: 1.7→43.414 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12630	0	182	2060	14872
B_iso mean	-	-	11.66	28.41	-
Num. residues	-	-	-	-	1700

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	13353
X-RAY DIFFRACTION	f_angle_d	1.169	18234
X-RAY DIFFRACTION	f_chiral_restr	0.051	2158
X-RAY DIFFRACTION	f_plane_restr	0.006	2379
X-RAY DIFFRACTION	f_dihedral_angle_d	12.6	8101

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
1.7-1.7193	0.2304	302	0.1974	6089	X-RAY DIFFRACTION	100
1.7193-1.7396	0.2312	325	0.196	6081	X-RAY DIFFRACTION	100
1.7396-1.7608	0.2374	291	0.1826	6095	X-RAY DIFFRACTION	100
1.7608-1.7831	0.2038	327	0.182	6150	X-RAY DIFFRACTION	100
1.7831-1.8065	0.2234	325	0.1802	6081	X-RAY DIFFRACTION	100
1.8065-1.8313	0.2176	296	0.1792	6072	X-RAY DIFFRACTION	100
1.8313-1.8575	0.2456	322	0.1778	6124	X-RAY DIFFRACTION	99
1.8575-1.8852	0.2126	296	0.1724	6056	X-RAY DIFFRACTION	100
1.8852-1.9146	0.2076	318	0.1717	6112	X-RAY DIFFRACTION	100
1.9146-1.946	0.2151	319	0.1657	6092	X-RAY DIFFRACTION	99
1.946-1.9796	0.1864	304	0.1611	6088	X-RAY DIFFRACTION	99
1.9796-2.0156	0.1894	325	0.1523	6069	X-RAY DIFFRACTION	99
2.0156-2.0543	0.1856	344	0.1495	6057	X-RAY DIFFRACTION	99
2.0543-2.0963	0.1928	294	0.1511	6145	X-RAY DIFFRACTION	99
2.0963-2.1419	0.1855	316	0.1542	6122	X-RAY DIFFRACTION	100
2.1419-2.1917	0.2114	298	0.148	6099	X-RAY DIFFRACTION	99
2.1917-2.2465	0.1875	299	0.1471	6117	X-RAY DIFFRACTION	99
2.2465-2.3072	0.1985	307	0.146	6085	X-RAY DIFFRACTION	99
2.3072-2.3751	0.1867	330	0.1403	6118	X-RAY DIFFRACTION	99
2.3751-2.4518	0.1717	334	0.1437	6099	X-RAY DIFFRACTION	99
2.4518-2.5394	0.1937	330	0.1459	6131	X-RAY DIFFRACTION	99
2.5394-2.641	0.1791	347	0.1498	6137	X-RAY DIFFRACTION	100
2.641-2.7612	0.1918	324	0.1473	6107	X-RAY DIFFRACTION	100
2.7612-2.9068	0.1692	317	0.1452	6222	X-RAY DIFFRACTION	100
2.9068-3.0888	0.1745	328	0.1504	6112	X-RAY DIFFRACTION	99
3.0888-3.3273	0.1798	303	0.1423	6209	X-RAY DIFFRACTION	99
3.3273-3.6619	0.1567	342	0.1325	6161	X-RAY DIFFRACTION	99
3.6619-4.1915	0.1432	338	0.123	6182	X-RAY DIFFRACTION	99
4.1915-5.2793	0.1357	332	0.1227	6240	X-RAY DIFFRACTION	99
5.2793-50	0.1682	337	0.1511	6244	X-RAY DIFFRACTION	95

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	1.5284	0.1055	0.6808	0.6957	-0.0357	2.1025	0.0263	-0.0456	-0.1548	0.017	-0.027	-0.0483	0.2381	0.0775	0.0249	0.1083	0.0239	0.0042	0.0471	0.0012	0.1128	-72.4936	15.7328	110.1793
2	1.8266	0.6766	0.4814	1.2778	0.2505	1.7652	-0.0257	0.0217	-0.2474	-0.0521	-0.0193	-0.0002	0.2266	-0.0335	0.046	0.1181	-0.0058	0.0058	0.0531	-0.0111	0.095	-92.5112	13.8195	97.3597
3	2.0204	-0.1367	0.1094	0.8244	-0.0938	0.7853	-0.0575	0.0932	-0.1742	-0.0607	0.0025	0.0625	0.213	-0.2106	0.048	0.1227	-0.0458	0.0016	0.1107	-0.01	0.0837	-102.3548	15.9561	100.7558
4	1.7601	-0.1196	0.3531	1.3088	-0.7531	2.0793	-0.0426	-0.0352	0.1098	-0.0168	0.058	0.11	-0.039	-0.3193	-0.0111	0.0659	0.0042	0.0123	0.1202	-0.0038	0.081	-106.6704	26.4	107.0282
5	2.2257	0.616	0.4723	1.5422	-0.1947	1.5257	-0.0484	0.0722	0.2889	-0.0851	0.0214	0.2156	-0.1044	-0.2737	0.0667	0.0788	0.0061	-0.0142	0.111	0.0094	0.1106	-102.2292	33.9438	95.7859
6	1.9846	0.1769	1.1089	0.2334	-0.0264	1.5266	-0.0196	0.1581	-0.0383	-0.0701	0.022	-0.0061	0.0316	0.0057	0.0032	0.089	-0.0115	0.0048	0.071	0.0057	0.0568	-84.8377	27.3941	94.2589
7	1.8744	-0.0562	0.234	0.7442	0.2108	1.5606	-0.028	0.1406	0.1458	-0.0375	0.0241	-0.1561	-0.1376	0.2132	-0.0006	0.0982	-0.0356	-0.0096	0.0882	0.0211	0.1063	-70.4413	35.7516	105.1648
8	0.9593	0.0359	0.6027	1.5073	-0.0265	1.186	-0.0503	-0.1106	-0.0023	0.1036	0.0331	-0.0275	-0.0433	-0.0182	0.0181	0.0649	0.006	0.0087	0.0784	0.0089	0.0622	-77.3729	28.2025	119.7603
9	3.2511	0.4193	0.0449	2.8554	-0.5099	2.1929	-0.0101	-0.0035	-0.5392	-0.0112	-0.0458	-0.0598	0.2284	0.076	0.0634	0.1062	0.0251	-0.0004	0.0762	0.0107	0.1253	-71.9263	13.0987	111.0548
10	1.4919	-0.1837	0.2905	0.9902	0.4793	2.0302	0.0281	-0.0557	-0.1622	0.0077	-0.05	0.0467	0.1333	-0.1266	0.047	0.0721	-0.0229	0.0041	0.0473	0.0219	0.1029	-109.9933	16.6379	136.163
11	0.9233	-0.2363	0.1254	0.4047	0.2457	1.0309	-0.0279	-0.1749	-0.2015	0.1493	-0.0287	-0.068	0.1376	0.172	0.0386	0.1379	0.0041	-0.0211	0.1354	0.0552	0.1208	-86.0686	16.3693	147.6163
12	1.4552	0.4337	0.641	1.1221	0.8519	2.1553	0.0104	0.0552	0.0924	0.0244	0.0246	-0.1391	-0.0384	0.3172	-0.03	0.0894	-0.0189	-0.0014	0.1713	0.0318	0.1181	-76.0213	27.5612	138.5038
13	1.5448	-0.2667	0.324	1.0037	0.3173	1.1927	0.024	-0.088	0.148	0.0958	-0.0533	-0.1449	-0.0938	0.1887	0.0354	0.1146	-0.0499	-0.0287	0.1381	0.0211	0.0951	-83.5809	34.7337	151.5281
14	1.3823	0.2708	0.7265	0.6886	0.1903	0.974	0.0614	-0.1752	-0.074	0.1301	-0.0316	-0.0688	0.0191	0.0444	-0.0369	0.0997	-0.0086	-0.0029	0.1059	0.0087	0.0574	-96.2884	27.4988	150.9535
15	1.4136	0.182	0.2651	0.7564	-0.0541	1.4661	-0.0261	-0.1072	0.1345	0.0196	-0.0101	0.0506	-0.1647	-0.1255	0.0231	0.0962	0.0147	-0.0053	0.0564	-0.0089	0.0786	-109.3766	35.0008	137.299
16	0.7914	0.0971	0.2962	0.9557	0.012	0.868	-0.0267	0.0612	0.0339	-0.0971	0.0209	0.012	-0.0686	0.065	0.0042	0.0758	-0.0069	0.008	0.0523	-0.0046	0.0612	-105.7341	25.1982	124.2604
17	2.9195	-1.6734	-0.8984	2.8794	0.858	1.7745	0.0047	-0.0678	-0.3929	0.1324	-0.0944	0.0218	0.2274	-0.0695	0.1093	0.0993	-0.0183	0.0024	0.0626	0.0205	0.1056	-110.5356	13.9111	135.5535
18	1.6937	0.4994	-0.9219	0.5225	-0.4197	1.3577	0.1058	-0.1349	0.2036	0.1244	-0.0321	-0.0546	-0.2587	0.1139	-0.0758	0.1551	-0.0201	-0.0122	0.0828	-0.0378	0.1444	-85.4483	71.5804	142.8719
19	1.5714	-0.8419	0.0871	0.8178	-0.5764	1.1478	-0.0252	-0.156	0.3468	0.1174	-0.0255	-0.0532	-0.2309	-0.05	0.0847	0.2136	-0.0059	0.0039	0.0971	-0.0377	0.1961	-97.0659	77.6615	144.2432
20	1.5886	0.2726	0.2495	0.8511	-0.3639	1.1585	-0.0092	-0.1815	0.2499	0.1414	0.0463	0.0458	-0.2278	-0.1526	-0.0382	0.119	0.0209	0.0159	0.1	-0.0308	0.1272	-105.8101	71.4614	141.2294
21	2.3336	0.4176	-0.7599	1.2392	-0.8228	1.8275	0.0126	0.0365	-0.0123	-0.0333	0.0953	0.0843	-0.0144	-0.1873	-0.0941	0.0593	-0.0072	-0.0098	0.0914	-0.0091	0.0753	-108.8598	61.2294	134.4035
22	1.9348	-0.2589	0.0339	0.997	-0.2731	1.1951	0.0002	-0.134	-0.1347	0.0756	0.0398	0.1068	0.036	-0.1989	-0.027	0.0824	-0.0144	0.004	0.0958	-0.0006	0.0832	-103.9651	54.7947	148.8012
23	1.3617	-0.0444	-0.6219	0.4698	-0.1452	1.3013	-0.0354	-0.1521	-0.0277	0.0686	-0.0138	-0.0938	-0.0008	0.1787	0.0455	0.0887	-0.0055	-0.011	0.0778	-0.0085	0.0865	-79.914	56.4527	142.4718
24	1.1238	-0.3088	-0.5608	1.4238	-0.0084	0.9074	0.0264	0.0831	0.0602	-0.1331	-0.0166	-0.1052	-0.0062	0.0489	-0.0077	0.0746	-0.0192	0.0006	0.0853	-0.0025	0.0854	-77.1984	63.0175	125.5538
25	4.1808	0.3912	-0.2395	2.7314	0.3853	2.271	0.1181	-0.2192	0.4945	0.0991	-0.0896	-0.0737	-0.4062	0.3711	0.0406	0.1411	-0.0682	-0.0024	0.1571	-0.0197	0.1628	-74.478	75.1386	136.8205
26	1.1004	-0.0985	-0.4042	0.3349	0.2	0.5847	0.0722	0.1012	0.2432	-0.1202	-0.0046	-0.0087	-0.1734	0.022	-0.0605	0.1655	-0.0099	0.0178	0.0848	0.044	0.1428	-87.5125	71.5711	99.8688
27	2.1558	-0.6546	-1.0292	0.9773	0.9549	1.7511	0.0111	-0.1493	0.0396	0.011	0.1072	-0.0438	-0.0252	0.271	-0.1108	0.0737	-0.0128	-0.0087	0.1066	0.0111	0.0799	-73.39	60.3774	108.8277
28	2.6444	0.2297	-0.6622	1.4332	0.3105	1.4201	-0.0533	-0.0122	-0.1086	-0.0071	0.0522	-0.0711	0.0703	0.1674	0.0117	0.0653	0.0026	-0.0051	0.0773	0.0095	0.0586	-75.7363	52.0092	97.1923
29	1.689	-0.0995	-0.8197	0.3449	0.3109	0.837	0.1056	0.3085	0.0863	-0.1229	-0.0513	0.0195	-0.1337	-0.1331	-0.0511	0.1246	0.0131	-0.0134	0.1084	0.0276	0.0656	-92.8461	58.7661	92.3796
30	2.1588	-0.0327	-0.6966	1.0113	0.1506	1.696	-0.0014	0.2799	-0.179	-0.1536	-0.0704	0.1998	0.0852	-0.2968	0.0488	0.1177	-0.0133	-0.0251	0.1204	-0.0274	0.1379	-108.8262	51.2722	101.0967
31	1.3058	-0.2349	-0.4359	1.3836	0.0702	0.8307	0.0065	-0.0023	0.0332	0.0315	-0.0203	0.0288	0.0051	-0.0388	0.0097	0.0666	-0.0078	-0.0072	0.0549	0.0062	0.0734	-104.9236	62.449	114.2432
32	2.077	-0.5991	0.2364	1.8458	-0.0224	1.1477	-0.0244	-0.1195	0.0478	0.1296	0.0262	0.0539	-0.0202	-0.0984	0.0061	0.1099	0.0065	0.0108	0.1128	0.0072	0.0977	-93.4292	30.7522	107.958
33	1.8576	0.4391	-0.485	1.6427	-0.7369	1.286	-0.0337	0.1551	0.0267	-0.2639	0.0023	-0.1234	-0.1611	0.1539	0.0338	0.1551	-0.0281	0.008	0.1586	0.0088	0.0974	-89.1052	31.8213	137.3808
34	0.9269	-0.0449	0.3334	1.4152	0.7256	0.979	0.0155	0.0573	-0.0924	-0.1245	0.0856	-0.0223	-0.045	-0.0399	-0.1008	0.1089	-0.0101	-0.0134	0.0927	-0.0013	0.1075	-95.6144	57.2276	136.0242
35	2.0672	-0.1272	0.4993	0.8459	-0.4568	0.8801	0.01	-0.044	-0.0476	0.0592	0.068	0.0642	-0.0738	0.0359	-0.0929	0.1247	-0.0055	0.0017	0.0724	0.0033	0.1187	-86.8227	56.2075	107.4786

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 -3 through 21 )	A	0
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 22 through 71 )	A	0
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 72 through 106 )	A	0
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 107 through 148 )	A	0
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 149 through 191 )	A	0
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 192 through 262 )	A	0
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 263 through 306 )	A	0
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 307 through 401 )	A	0
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 402 through 421 )	A	0
10	X-RAY DIFFRACTION	10	chain 'B' and (resid -3 through 21 )	B	0
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 22 through 106 )	B	0
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 107 through 148 )	B	0
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 149 through 214 )	B	0
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 215 through 247 )	B	0
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 248 through 335 )	B	0
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 336 through 401 )	B	0
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 402 through 421 )	B	0
18	X-RAY DIFFRACTION	18	chain 'C' and (resid -3 through 47 )	C	0
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 48 through 71 )	C	0
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 72 through 106 )	C	0
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 107 through 148 )	C	0
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 149 through 214 )	C	0
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 215 through 335 )	C	0
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 336 through 401 )	C	0
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 402 through 421 )	C	0
26	X-RAY DIFFRACTION	26	chain 'D' and (resid -3 through 106 )	D	0
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 107 through 148 )	D	0
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 149 through 191 )	D	0
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 192 through 262 )	D	0
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 263 through 306 )	D	0
31	X-RAY DIFFRACTION	31	chain 'D' and (resid 307 through 421 )	D	0
32	X-RAY DIFFRACTION	32	chain 'A' and resid 500	A	500
33	X-RAY DIFFRACTION	33	chain 'B' and resid 500	B	500
34	X-RAY DIFFRACTION	34	chain 'C' and resid 500	C	500
35	X-RAY DIFFRACTION	35	chain 'D' and resid 500	D	500

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