PDB-5g3t: The structure of the L-tryptophan oxidase VioA from Chromobacteri...

ID or keywords:

Entry

Database: PDB / ID: 5g3t

Title

The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum

Components

L-TRYPTOPHAN OXIDASE VIOA

Keywords

OXIDOREDUCTASE / VIOLACEIN / L-TRYPTOPHAN OXIDASE / FLAVOENZYME

Function / homology

7-chloro-L-tryptophan oxidase / Amine oxidase / Flavin containing amine oxidoreductase / antibiotic biosynthetic process / FAD/NAD(P)-binding domain superfamily / oxidoreductase activity / metal ion binding / DIHYDROFLAVINE-ADENINE DINUCLEOTIDE / Flavin-dependent L-tryptophan oxidase VioA

Function and homology information

Biological species

CHROMOBACTERIUM VIOLACEUM (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.8 Å

Authors

Krausze, J. / Rabe, J. / Moser, J.

Citation

Journal: J.Biol.Chem. / Year: 2016
Title: Biosynthesis of Violacein: Structure and Function of L-Tryptophan Oxidase Vioa Chromobacterium Violaceum
Authors: Fuller, J. / Roepke, R. / Krausze, J. / Rennhack, K.E. / Daniel, N.P. / Blankenfeldt, W. / Schulz, S. / Jahn, D. / Moser, J.

History

Deposition	May 1, 2016	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Aug 3, 2016	Provider: repository / Type: Initial release
Revision 1.1	Aug 10, 2016	Group: Database references
Revision 1.2	Oct 5, 2016	Group: Database references
Revision 1.3	Mar 6, 2019	Group: Data collection / Experimental preparation / Other Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 2.0	Oct 23, 2019	Group: Atomic model / Data collection / Other / Category: atom_site / pdbx_database_status Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _pdbx_database_status.status_code_sf
Revision 2.1	May 8, 2024	Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_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 / _struct_conn.pdbx_dist_value / _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_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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	5g3t_validation.pdf.gz	1.3 MB	Display	wwPDB validaton report
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Data in CIF	5g3t_validation.cif.gz	107.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/g3/5g3t ftp://data.pdbj.org/pub/pdb/validation_reports/g3/5g3t	HTTPS FTP

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Related structure data

Related structure data	5g3sC 5g3uC C: citing same article (ref.)
Similar structure data	5g3u-d 5zbc-d 4kip-d 6zr5-d 6fw7-d 5w6a-d 3zzt-1 2q7y-d 2wo6-d 5g3s-d 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	#231 - Mar 2019 Measles Virus Proteins similarity (2)

Deposited unit

A: L-TRYPTOPHAN OXIDASE VIOA

B: L-TRYPTOPHAN OXIDASE VIOA

C: L-TRYPTOPHAN OXIDASE VIOA

D: L-TRYPTOPHAN OXIDASE VIOA

hetero molecules

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

1

A: L-TRYPTOPHAN OXIDASE VIOA

B: L-TRYPTOPHAN OXIDASE VIOA

hetero molecules

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

2

C: L-TRYPTOPHAN OXIDASE VIOA

D: L-TRYPTOPHAN OXIDASE VIOA

hetero molecules

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

Unit cell

Length a, b, c (Å)	68.090, 89.160, 144.430
Angle α, β, γ (deg.)	90.00, 92.66, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.99974, 0.01948, -0.01207), (0.0194, 0.99979, 0.00666), (0.0122, 0.00642, -0.9999)	177.48364, -2.64028, 183.06073
2	given	(0.99455, -0.10322, 0.0148), (0.09965, 0.98262, 0.15663), (-0.03073, -0.1543, 0.98755)	-18.3603, -63.97067, 34.74739
3	given	(-0.99197, 0.12504, -0.01888), (0.12029, 0.97904, 0.16435), (0.03904, 0.16076, -0.98622)	161.98184, -66.70381, 213.30214
4	given	(-0.9965, -0.08355, -0.00353), (-0.08209, 0.9854, -0.14917), (0.01595, -0.14835, -0.98881)	158.91324, -19.47407, 212.55051
5	given	(0.9944, 0.10541, 0.00774), (-0.10291, 0.9823, -0.15654), (-0.0241, 0.15487, 0.98764)	-15.63145, -17.16276, 37.18066
6	given	(-0.99975, 0.02109, -0.00746), (0.02104, 0.99975, 0.00739), (0.00761, 0.00723, -0.99994)	145.2356, -2.61166, 248.65086

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Protein , 1 types, 4 molecules ABCD

#1: Protein	L-TRYPTOPHAN OXIDASE VIOA Mass: 47213.609 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHROMOBACTERIUM VIOLACEUM (bacteria) / Strain: 12472 / Plasmid: PGEX / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): LAMBDA / References: UniProt: Q9S3V1, 7-chloro-L-tryptophan oxidase

#1: Protein

L-TRYPTOPHAN OXIDASE VIOA

Mass: 47213.609 Da / Num. of mol.: 4 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

CHROMOBACTERIUM VIOLACEUM (bacteria) / Strain: 12472 / Plasmid: PGEX / Production host:

ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): LAMBDA / References: UniProt: Q9S3V1, 7-chloro-L-tryptophan oxidase

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Non-polymers , 6 types, 1386 molecules

#2: Chemical	ChemComp-FDA / DIHYDROFLAVINE-ADENINE DINUCLEOTIDE Mass: 787.566 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₇H₃₅N₉O₁₅P₂
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Cl
#5: Chemical	ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER Mass: 122.143 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₄H₁₂NO₃ / Comment: pH buffer*YM
#6: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₈O₃
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1361 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.32 Å³/Da / Density % sol: 47.12 % / Description: NONE
Crystal grow	Temperature: 277 K / pH: 8.5 Details: 0.08 M TRIS PH 8.5, 24 %(W/V) PEG 4000, 0.16 M MGCL2, 20 %(V/V) GLYCEROL AT 277 K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.033184
Detector	Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 25, 2013 / Details: FOCUSSING MIRRORS
Radiation	Monochromator: DOUBLE CRYSTAL SI(111) AND SI(113) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.033184 Å / Relative weight: 1
Reflection	Resolution: 1.8→19.98 Å / Num. obs: 157109 / % possible obs: 98 % / Observed criterion σ(I): -3 / Redundancy: 6.9 % / B_iso Wilson estimate: 22.91 Å² / R_merge(I) obs: 0.1 / Net I/σ(I): 10.91
Reflection shell	Resolution: 1.8→1.85 Å / Redundancy: 6.94 % / R_merge(I) obs: 0.95 / Mean I/σ(I) obs: 2 / % possible all: 97.3

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
XDS		data reduction
XSCALE		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: NONE

Resolution: 1.8→19.992 Å / SU ML: 0.17 / σ(F): 1.35 / Phase error: 21.26 / Stereochemistry target values: ML
Details: THE HYDROGEN ATOMS IN THE STRUCTURE ARE RIDING HYDROGENS AND THEIR POSITIONS WERE NOT REFINED

	R_factor	Num. reflection	% reflection
R_free	0.1922	7851	5 %
R_work	0.1568	-	-
obs	0.1585	157061	98.46 %

Solvent computation

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

Displacement parameters

B_iso mean: 26.46 Å²

Refinement step

Cycle: LAST / Resolution: 1.8→19.992 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12747	0	259	1361	14367

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	13460
X-RAY DIFFRACTION	f_angle_d	0.935	18284
X-RAY DIFFRACTION	f_dihedral_angle_d	14.458	7896
X-RAY DIFFRACTION	f_chiral_restr	0.053	1925
X-RAY DIFFRACTION	f_plane_restr	0.006	2345

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 (%)
1.8-1.8205	0.2507	257	0.2406	4878	X-RAY DIFFRACTION	97
1.8205-1.8419	0.2865	260	0.2309	4944	X-RAY DIFFRACTION	97
1.8419-1.8643	0.274	255	0.2146	4849	X-RAY DIFFRACTION	97
1.8643-1.8879	0.2387	258	0.2091	4901	X-RAY DIFFRACTION	97
1.8879-1.9127	0.2278	259	0.197	4921	X-RAY DIFFRACTION	98
1.9127-1.9389	0.2301	261	0.1945	4954	X-RAY DIFFRACTION	98
1.9389-1.9666	0.2266	256	0.1844	4867	X-RAY DIFFRACTION	98
1.9666-1.9959	0.2584	260	0.1777	4940	X-RAY DIFFRACTION	98
1.9959-2.0271	0.2399	260	0.1784	4934	X-RAY DIFFRACTION	98
2.0271-2.0603	0.2253	260	0.1702	4938	X-RAY DIFFRACTION	98
2.0603-2.0957	0.1979	258	0.1637	4909	X-RAY DIFFRACTION	98
2.0957-2.1338	0.1978	262	0.1613	4965	X-RAY DIFFRACTION	98
2.1338-2.1748	0.2163	261	0.1557	4967	X-RAY DIFFRACTION	98
2.1748-2.2191	0.1877	261	0.1536	4955	X-RAY DIFFRACTION	99
2.2191-2.2673	0.1961	260	0.1537	4950	X-RAY DIFFRACTION	99
2.2673-2.32	0.1942	261	0.1489	4961	X-RAY DIFFRACTION	99
2.32-2.3779	0.2219	263	0.1533	4988	X-RAY DIFFRACTION	99
2.3779-2.4421	0.1754	264	0.1438	5024	X-RAY DIFFRACTION	99
2.4421-2.5138	0.1766	261	0.1465	4947	X-RAY DIFFRACTION	99
2.5138-2.5948	0.2001	261	0.1514	4969	X-RAY DIFFRACTION	99
2.5948-2.6874	0.2126	265	0.1575	5026	X-RAY DIFFRACTION	99
2.6874-2.7947	0.2123	263	0.1584	4989	X-RAY DIFFRACTION	99
2.7947-2.9215	0.2046	263	0.1531	4997	X-RAY DIFFRACTION	99
2.9215-3.075	0.1794	265	0.1511	5052	X-RAY DIFFRACTION	99
3.075-3.2669	0.1642	265	0.1516	5021	X-RAY DIFFRACTION	99
3.2669-3.5179	0.1848	265	0.1518	5044	X-RAY DIFFRACTION	99
3.5179-3.8696	0.1627	266	0.1443	5053	X-RAY DIFFRACTION	99
3.8696-4.4242	0.1516	266	0.1305	5050	X-RAY DIFFRACTION	100
4.4242-5.5542	0.182	268	0.138	5085	X-RAY DIFFRACTION	99
5.5542-19.9932	0.1914	267	0.1761	5132	X-RAY DIFFRACTION	99

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	0.705	0.0271	-0.047	0.3944	-0.04	0.4782	-0.0088	-0.1829	0.1392	0.0405	0.0313	0.0141	-0.1003	-0.048	-0.0319	0.1088	0.0201	-0.0068	0.1405	-0.03	0.1141	76.0038	1.6608	75.2835
2	0.3724	-0.1196	0.1185	0.1352	-0.1229	0.4165	0.0813	0.1997	-0.2416	-0.1612	0.0434	0.0602	0.0537	0.0908	0.056	0.1697	0.0147	-0.0331	0.1116	-0.0242	0.2138	94.613	-12.2209	47.3947
3	0.1328	-0.2218	0.1168	0.2636	0.065	0.4501	-0.0053	-0.0783	-0.1462	0.1217	0.024	0.094	-0.0315	-0.0196	0.0001	0.1195	0.0094	0.0095	0.0993	0.0115	0.1633	93.0874	-8.4903	56.851
4	0.7336	-0.0328	0.246	0.2967	-0.0605	0.6453	-0.0037	-0.2041	-0.0136	0.0288	0.0424	0.0574	-0.0077	-0.1666	0.0009	0.1075	0.0146	0.0079	0.1639	-0.006	0.0964	73.9882	-6.2859	82.8058
5	0.924	0.0528	-0.1783	0.3429	-0.0213	0.3677	-0.0391	-0.152	0.1112	-0.0573	0.0299	-0.106	0.0177	0.1555	-0.0238	0.1313	-0.0178	-0.0094	0.1384	-0.0244	0.1421	97.2648	-0.1111	71.6195
6	0.631	-0.0441	-0.347	0.4136	-0.4825	0.3984	0.0091	-0.1489	-0.0278	-0.0493	0.0406	-0.0242	0.0689	-0.0258	0.0833	0.1216	-0.0163	-0.0032	0.1048	-0.0063	0.0985	80.0894	-7.8821	72.8408
7	0.8084	0.1204	-0.3126	0.3592	-0.1575	0.8676	0.0406	0.0485	-0.013	-0.0113	-0.0143	0.0125	0.0105	0.114	0.0002	0.1101	0.0196	-0.0132	0.1427	0.0083	0.1181	94.982	-2.5473	116.9227
8	0.175	0.1935	0.1589	0.3128	-0.123	0.334	-0.0066	-0.0277	-0.255	-0.1169	0.0083	-0.0733	0.0796	0.0696	0.003	0.1434	0.0104	0.0095	0.1053	0.0048	0.1866	83.6436	-8.9233	127.2505
9	0.7783	0.0903	-0.3892	0.396	0.0091	1.1857	0.0143	0.1335	0.0647	-0.0086	-0.0065	0.0528	0.0528	-0.0543	-0.0015	0.1372	0.0271	-0.0093	0.1335	0.0224	0.0938	89.3368	-3.1209	107.5884
10	0.2346	0.0336	-0.244	0.1056	0.0186	0.9839	-0.0041	0.0235	-0.0066	0.0067	0.0479	0.0107	0.1265	0.107	0.0952	0.1716	0.0592	0.0052	0.1543	0.0019	0.1106	96.4176	-8.5566	111.086
11	0.3754	0.2497	-0.1187	0.1923	0.1789	0.3853	0.0627	-0.0681	0.0483	0.047	0.0244	0.0344	-0.0839	-0.1493	0.0095	0.1278	0.0058	0.0091	0.169	0.0185	0.1345	56.5715	-45.1185	111.834
12	1.2999	-0.5113	-0.3384	0.2659	0.2183	0.4393	0.0077	0.1007	-0.0901	-0.0207	0.0401	0.0408	0.0431	-0.0257	0.0122	0.1371	-0.0003	-0.0087	0.1034	-0.0064	0.1402	72.6289	-51.4407	88.0685
13	0.7056	0.0901	-0.0196	0.1647	-0.1293	1.2623	0.0323	-0.1104	-0.0439	-0.0168	0.0395	0.0114	0.1293	-0.1764	0.0468	0.1029	-0.0095	-0.0116	0.0518	0.0047	0.0953	60.0405	-51.7332	113.5922
14	0.9084	-0.1222	-0.1616	0.6824	-0.1876	0.9186	0.0384	-0.064	0.1361	-0.0349	0.0122	-0.1939	-0.0996	0.1179	0.0239	0.1262	-0.0169	0.0022	0.077	-0.0218	0.1644	84.652	-36.5421	99.8282
15	0.3408	0.3132	-0.3204	0.1719	-0.163	0.7939	-0.0016	0.0096	-0.0823	-0.0464	0.0663	-0.0008	0.1312	-0.1252	0.0172	0.1588	-0.0245	-0.0256	0.1142	0.0217	0.1401	58.8947	-55.6737	106.2833
16	0.1437	-0.1169	0.0608	0.4101	-0.0491	0.1319	0.0055	0.0304	0.0604	0.089	-0.0914	0.1703	-0.0205	-0.1522	-0.086	0.1232	-0.0038	0.0298	0.2173	-0.063	0.2006	95.5618	-6.2528	155.8653
17	0.4898	-0.1091	-0.4416	0.0422	0.1529	0.2461	0.0944	0.0117	0.1577	0.0402	0.0489	-0.019	-0.1635	-0.0025	0.0161	0.146	-0.0134	0.0055	0.14	-0.0311	0.1541	113.1711	4.6203	145.8575
18	1.1774	0.0533	-0.1819	0.2535	-0.1804	0.2379	0.0036	0.3688	-0.0557	-0.1159	0.0141	-0.0156	-0.0074	-0.1363	0.0182	0.1401	0.0011	-0.0068	0.2156	-0.0268	0.1728	118.1537	-5.0715	126.7252
19	0.3327	0.2232	0.0877	0.2333	0.2772	0.1842	0.011	-0.0017	-0.2706	-0.0609	-0.0031	0.0463	0.0563	-0.163	0.0002	0.1683	-0.0128	0.0012	0.1889	-0.0037	0.1772	123.1082	-10.286	129.7259
20	0.6264	0.2784	0.159	0.5341	-0.0524	0.4255	0.013	0.0372	0.057	0.0308	-0.0304	0.0807	-0.0709	-0.059	-0.0005	0.0916	0.0246	0.0022	0.1	-0.0338	0.1217	105.1183	-0.7219	148.6886
21	0.1137	-0.1406	0.1532	0.4346	-0.0462	0.1836	0.0073	-0.11	-0.0683	0.1678	-0.1154	0.0913	0.1626	-0.072	-0.0321	0.1671	-0.0416	0.0283	0.1802	-0.0329	0.1689	104.5748	-13.1245	162.903
22	0.5017	-0.252	-0.1007	0.1531	0.0522	0.2109	0.0309	0.0607	-0.2229	0.1556	-0.0337	-0.177	0.0081	0.0714	-0.0279	0.1439	0.008	0.0014	0.1018	-0.0263	0.141	115.9232	-13.2597	148.3735
23	0.5648	0.493	-0.2778	0.6817	-0.2558	0.5078	0.0515	-0.1254	0.1008	-0.0082	-0.0883	-0.0487	-0.0405	0.0565	-0.0015	0.13	-0.0156	-0.0028	0.1446	-0.0026	0.1638	131.8452	7.9052	139.4795
24	0.4707	0.0424	-0.7162	0.3254	-0.1783	0.8598	-0.0511	0.1584	-0.1353	-0.0407	0.006	0.0342	0.0891	-0.1046	0.0007	0.1193	-0.0178	-0.0057	0.128	-0.0372	0.1444	106.6156	-11.6454	146.1746

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN 'A' AND (RESID 3 THROUGH 96 )
2	X-RAY DIFFRACTION	2	CHAIN 'A' AND (RESID 97 THROUGH 130 )
3	X-RAY DIFFRACTION	3	CHAIN 'A' AND (RESID 131 THROUGH 170 )
4	X-RAY DIFFRACTION	4	CHAIN 'A' AND (RESID 171 THROUGH 248 )
5	X-RAY DIFFRACTION	5	CHAIN 'A' AND (RESID 249 THROUGH 341 )
6	X-RAY DIFFRACTION	6	CHAIN 'A' AND (RESID 342 THROUGH 418 )
7	X-RAY DIFFRACTION	7	CHAIN 'B' AND (RESID 3 THROUGH 130 )
8	X-RAY DIFFRACTION	8	CHAIN 'B' AND (RESID 131 THROUGH 170 )
9	X-RAY DIFFRACTION	9	CHAIN 'B' AND (RESID 171 THROUGH 341 )
10	X-RAY DIFFRACTION	10	CHAIN 'B' AND (RESID 342 THROUGH 418 )
11	X-RAY DIFFRACTION	11	CHAIN 'C' AND (RESID 1 THROUGH 70 )
12	X-RAY DIFFRACTION	12	CHAIN 'C' AND (RESID 71 THROUGH 169 )
13	X-RAY DIFFRACTION	13	CHAIN 'C' AND (RESID 170 THROUGH 273 )
14	X-RAY DIFFRACTION	14	CHAIN 'C' AND (RESID 274 THROUGH 352 )
15	X-RAY DIFFRACTION	15	CHAIN 'C' AND (RESID 353 THROUGH 418 )
16	X-RAY DIFFRACTION	16	CHAIN 'D' AND (RESID 3 THROUGH 38 )
17	X-RAY DIFFRACTION	17	CHAIN 'D' AND (RESID 39 THROUGH 70 )
18	X-RAY DIFFRACTION	18	CHAIN 'D' AND (RESID 71 THROUGH 130 )
19	X-RAY DIFFRACTION	19	CHAIN 'D' AND (RESID 131 THROUGH 169 )
20	X-RAY DIFFRACTION	20	CHAIN 'D' AND (RESID 170 THROUGH 214 )
21	X-RAY DIFFRACTION	21	CHAIN 'D' AND (RESID 215 THROUGH 248 )
22	X-RAY DIFFRACTION	22	CHAIN 'D' AND (RESID 249 THROUGH 273 )
23	X-RAY DIFFRACTION	23	CHAIN 'D' AND (RESID 274 THROUGH 352 )
24	X-RAY DIFFRACTION	24	CHAIN 'D' AND (RESID 353 THROUGH 418 )

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