PDB-6x6h: Structure of Shiga toxin 2 with a C-terminal peptide of ribosomal...

ID or keywords:

Entry

Database: PDB / ID: 6x6h

Title

Structure of Shiga toxin 2 with a C-terminal peptide of ribosomal P stalk proteins

Components

(rRNA N-glycosylase) x 2
P11 peptide
Shiga toxin 2 B subunit

Keywords

TOXIN / Shiga toxin / ribosome-inactivating protein / C-terminal peptide of ribosomal P stalk proteins

Function / homology

Function and homology information

hemolysis by symbiont of host erythrocytes / rRNA N-glycosylase / rRNA N-glycosylase activity / toxin activity / negative regulation of translation / extracellular region
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.88 Å

Authors

Rudolph, M.J.

Citation

Journal: J.Biol.Chem. / Year: 2020
Title: Structural basis for the interaction of Shiga toxin 2a with a C-terminal peptide of ribosomal P stalk proteins.
Authors: Rudolph, M.J. / Davis, S.A. / Tumer, N.E. / Li, X.P.

History

Deposition	May 28, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 9, 2020	Provider: repository / Type: Initial release
Revision 2.0	Sep 16, 2020	Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Structure summary Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / citation / citation_author / entity_poly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_validate_close_contact / pdbx_validate_torsion / struct_conf / struct_conn / struct_ref_seq / struct_sheet_range Item: _atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id ..._atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id / _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _entity_poly.pdbx_strand_id / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.pdb_strand_id / _pdbx_struct_sheet_hbond.range_1_auth_asym_id / _pdbx_struct_sheet_hbond.range_2_auth_asym_id / _pdbx_struct_special_symmetry.auth_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_torsion.auth_asym_id / _struct_conf.beg_auth_asym_id / _struct_conf.end_auth_asym_id / _struct_conn.ptnr1_auth_asym_id / _struct_ref_seq.pdbx_strand_id / _struct_sheet_range.beg_auth_asym_id / _struct_sheet_range.end_auth_asym_id
Revision 2.1	Nov 25, 2020	Group: Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.2	Oct 18, 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 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

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Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/x6/6x6h ftp://data.pdbj.org/pub/pdb/validation_reports/x6/6x6h	HTTPS FTP

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Related structure data

Related structure data	1r4pS S: Starting model for refinement
Similar structure data	1r4q-2 3k1g-10 3kum-4 7d6q-d 1dm0-2 3k1g-9 1djx-1 6smd-d 4bfx-d 4v06-d 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	#161 - May 2013 Ricin similarity (8) #69 - Sep 2005 Cholera Toxin similarity (9) #4 - Apr 2000 Collagen similarity (1) #116 - Aug 2009 Sulfotransferases similarity (1)

Deposited unit

A1: rRNA N-glycosylase

A2: rRNA N-glycosylase

B: Shiga toxin 2 B subunit

C: Shiga toxin 2 B subunit

D: Shiga toxin 2 B subunit

E: Shiga toxin 2 B subunit

F: Shiga toxin 2 B subunit

P: P11 peptide

hetero molecules

72 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	82.148, 85.226, 98.841
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	18
Space group name H-M	P22₁2₁

Components on special symmetry positions

ID	Model	Components
1	1	A1-401- HOH

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Protein , 2 types, 6 molecules A1BCDEF

#1: Protein	rRNA N-glycosylase / Stx2A Mass: 27061.381 Da / Num. of mol.: 1 Fragment: N-terminal portion, disulfide linked to C-terminal fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_29255, DOT81_27455, DOY22_27375, DQG35_26865, ED607_26125, ED648_25265, EHV81_26780, EHV90_26725, EHW09_26775, F7G01_26395, GJD97_09695, GN312_26720 Production host: Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase
#3: Protein	Shiga toxin 2 B subunit / Shiga toxin 2 subunit B / Shiga toxin 2B / Shiga toxin 2v subunit A / Shiga toxin Stx2 subunit B / ...Shiga toxin 2 subunit B / Shiga toxin 2B / Shiga toxin 2v subunit A / Shiga toxin Stx2 subunit B / Shiga toxin Stx2a subunit B / Stx2 holotoxin B subunit / Stx2 holotoxin subunit B / Stx2B / Stx2B protein Mass: 7824.590 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: stxII, stx2B, stx2b, stx2B_2, stx2dB, stx2vB, stxB2, vtx2B, BvCmsHHP019_02074, BvCmsNSP072_02053, BvCmsOUP014_04264, C9098_23370, C9Z37_23105, C9Z78_24425, D6004_26885, D7K33_26370, D9X77_ ...Gene: stxII, stx2B, stx2b, stx2B_2, stx2dB, stx2vB, stxB2, vtx2B, BvCmsHHP019_02074, BvCmsNSP072_02053, BvCmsOUP014_04264, C9098_23370, C9Z37_23105, C9Z78_24425, D6004_26885, D7K33_26370, D9X77_26970, DAH30_25515, DM155_24460, DNR35_15450, EBM08_12130, F7F11_25580, HW43_14770, UN91_26180 Production host: Escherichia coli (E. coli) / References: UniProt: Q7DJJ2

#1: Protein

rRNA N-glycosylase / Stx2A

Mass: 27061.381 Da / Num. of mol.: 1
Fragment: N-terminal portion, disulfide linked to C-terminal fragment
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli)
Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...
Production host:

Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase

#3: Protein

Shiga toxin 2 B subunit / Shiga toxin 2 subunit B / Shiga toxin 2B / Shiga toxin 2v subunit A / Shiga toxin Stx2 subunit B / ...

Mass: 7824.590 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli)
Gene: stxII, stx2B, stx2b, stx2B_2, stx2dB, stx2vB, stxB2, vtx2B, BvCmsHHP019_02074, BvCmsNSP072_02053, BvCmsOUP014_04264, C9098_23370, C9Z37_23105, C9Z78_24425, D6004_26885, D7K33_26370, D9X77_ ...
Production host:

Escherichia coli (E. coli) / References: UniProt: Q7DJJ2

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Protein/peptide , 2 types, 2 molecules A2P

#2: Protein/peptide	rRNA N-glycosylase / Stx2A Mass: 4532.119 Da / Num. of mol.: 1 Fragment: C-terminal fragment, disulfide linked to N-terminal portion Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_29255, DOT81_27455, DOY22_27375, DQG35_26865, ED607_26125, ED648_25265, EHV81_26780, EHV90_26725, EHW09_26775, F7G01_26395, GJD97_09695, GN312_26720 Production host: Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase
#4: Protein/peptide	P11 peptide Mass: 654.712 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Escherichia coli (E. coli)

#2: Protein/peptide

rRNA N-glycosylase / Stx2A

Mass: 4532.119 Da / Num. of mol.: 1
Fragment: C-terminal fragment, disulfide linked to N-terminal portion
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli)
Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...
Production host:

Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase

#4: Protein/peptide

P11 peptide

Mass: 654.712 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)

Escherichia coli (E. coli)

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Non-polymers , 4 types, 489 molecules

#5: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C₂H₆O₂
#7: Chemical	ChemComp-ACY / ACETIC ACID Mass: 60.052 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₄O₂
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 476 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	N

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.43 Å³/Da / Density % sol: 49.33 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: 100 mM Sodium Acetate pH 4.5, 100 mM NaCl, 30% PEG 200

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

NSLS-II

/ Beamline: 19-ID / Wavelength: 0.979 Å

Detector

Type: ADSC HF-4M / Detector: PIXEL / Date: Sep 6, 2019

Radiation

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

Radiation wavelength

Wavelength: 0.979 Å / Relative weight: 1

Reflection

Resolution: 1.875→50 Å / Num. obs: 57068 / % possible obs: 99.7 % / Redundancy: 28.1 % / B_iso Wilson estimate: 23.38 Å² / R_merge(I) obs: 0.38 / R_pim(I) all: 0.072 / R_rim(I) all: 0.387 / Χ²: 0.786 / Net I/σ(I): 2

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Χ²	% possible all
1.88-1.91	22.5	3.065	2805	0.339	0.656	3.138	0.639	99.4
1.91-1.95	25.1	2.476	2820	0.451	0.498	2.528	0.692	99.6
1.95-1.98	30.1	2.337	2809	0.617	0.426	2.376	0.669	99.9
1.98-2.03	30.7	2.172	2799	0.712	0.39	2.207	0.666	100
2.03-2.07	30.3	1.878	2846	0.788	0.34	1.909	0.687	100
2.07-2.12	30.6	1.472	2839	0.843	0.266	1.496	0.727	100
2.12-2.17	29.1	1.434	2816	0.857	0.265	1.458	0.71	100
2.17-2.23	26.5	1.18	2833	0.878	0.231	1.203	0.737	99.9
2.23-2.29	28.6	1.063	2848	0.913	0.199	1.082	0.769	99.8
2.29-2.37	30	0.915	2836	0.943	0.166	0.93	0.721	99.9
2.37-2.45	28.9	0.819	2814	0.951	0.152	0.833	0.731	99.9
2.45-2.55	27.2	0.705	2846	0.965	0.135	0.718	0.748	99.9
2.55-2.67	24.1	0.576	2845	0.908	0.118	0.589	0.769	99
2.67-2.81	23.9	0.469	2821	0.974	0.096	0.479	0.802	99.1
2.81-2.98	31	0.384	2861	0.99	0.069	0.39	0.825	99.8
2.98-3.21	31.4	0.276	2879	0.994	0.049	0.28	0.873	100
3.21-3.54	28.4	0.196	2884	0.996	0.037	0.199	0.974	99.9
3.54-4.05	29.9	0.125	2913	0.998	0.023	0.127	1.005	100
4.05-5.1	26.1	0.089	2892	0.999	0.017	0.091	0.981	98.6
5.1-50	27.6	0.098	3062	0.999	0.019	0.1	0.95	98.6

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing
PHENIX	1.11.1_2575	refinement
PDB_EXTRACT	3.25	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1R4P

1r4p

Resolution: 1.88→42.753 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.47 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2056	2793	4.9 %
R_work	0.1677	54209	-
obs	0.1696	57002	99 %

Solvent computation

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

Displacement parameters

B_iso max: 94.44 Å² / B_iso mean: 28.531 Å² / B_iso min: 12.63 Å²

Refinement step

Cycle: final / Resolution: 1.88→42.753 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5005	0	34	476	5515
B_iso mean	-	-	40.81	38.95	-
Num. residues	-	-	-	-	637

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.006	5200
X-RAY DIFFRACTION	f_angle_d	0.671	7040
X-RAY DIFFRACTION	f_chiral_restr	0.052	787
X-RAY DIFFRACTION	f_plane_restr	0.004	910
X-RAY DIFFRACTION	f_dihedral_angle_d	11.019	3090

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	% reflection obs (%)
1.88-1.9074	0.3331	138	0.3006	2337	87
1.9074-1.9421	0.3004	131	0.2727	2678	100
1.9421-1.9794	0.2903	125	0.2506	2727	100
1.9794-2.0198	0.2949	132	0.2287	2696	100
2.0198-2.0638	0.2688	172	0.2152	2652	100
2.0638-2.1118	0.2287	138	0.2	2736	100
2.1118-2.1646	0.2176	133	0.1867	2689	100
2.1646-2.2231	0.2088	142	0.1754	2730	100
2.2231-2.2885	0.2157	129	0.1746	2716	100
2.2885-2.3624	0.2212	148	0.1665	2693	100
2.3624-2.4468	0.2231	139	0.1606	2715	100
2.4468-2.5447	0.2426	129	0.1648	2713	100
2.5447-2.6605	0.1973	132	0.1657	2746	99
2.6605-2.8008	0.2055	137	0.1652	2699	99
2.8008-2.9762	0.1967	137	0.16	2732	100
2.9762-3.2059	0.1674	133	0.1611	2766	100
3.2059-3.5284	0.2103	161	0.1554	2735	100
3.5284-4.0387	0.1786	157	0.1349	2769	100
4.0387-5.087	0.1612	149	0.1274	2760	99
5.087-42.753	0.1894	131	0.1785	2920	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	4.5585	-2.8985	-0.809	3.2036	0.8214	0.8485	0.0214	-0.0335	0.4204	0.0098	0.0116	-0.3823	-0.175	0.1954	-0.0293	0.1941	-0.0525	0.0008	0.194	0.009	0.2621	28.8597	62.9577	130.9505
2	4.2889	-1.7891	-1.564	1.8838	1.0753	2.8851	0.0462	-0.0311	0.304	0.0247	0.0573	-0.2429	-0.2411	0.0771	-0.1014	0.1367	-0.0709	-0.0284	0.1452	0.0078	0.1973	27.5944	58.8765	134.7661
3	1.3325	-0.1743	0.0723	1.9506	-0.0882	1.9814	0.02	-0.2504	-0.0185	0.2319	0.0077	0.0376	0.1121	-0.191	-0.0056	0.183	-0.036	0.0046	0.2236	-0.0012	0.1502	13.8759	54.7208	142.5354
4	2.3466	-1.6479	-0.9708	2.6257	1.2096	1.6205	0.0959	0.2364	-0.0321	-0.0718	-0.1124	-0.0218	-0.0058	-0.138	-0.0032	0.1405	-0.032	-0.0184	0.184	0.016	0.1309	21.5335	50.8413	122.133
5	4.1345	3.2396	1.4343	6.3865	0.1599	2.1757	0.118	-0.0294	-0.1349	0.0155	-0.0891	0.0052	0.118	0.5071	0.0426	0.1485	0.0582	0.0312	0.1961	-0.0103	0.1722	29.8527	48.14	120.9887
6	5.4066	2.8683	2.0776	5.9017	2.1181	2.8532	0.2405	-0.2397	-0.0913	0.5732	-0.1047	-0.2305	0.1926	-0.0839	-0.1399	0.2299	0.0346	-0.0083	0.163	0.0346	0.1619	22.9676	27.551	117.0601
7	7.5861	-4.0817	4.7396	3.4118	-2.1708	4.953	0.0241	0.4356	-0.0028	-0.1251	-0.1754	-0.2553	0.1232	0.6899	0.1481	0.1365	0.0051	0.028	0.23	0.0086	0.1481	33.8993	17.1781	103.1935
8	9.0807	5.7467	4.4249	6.7861	4.1103	5.1901	-0.0581	0.1583	-0.1799	-0.2509	-0.094	0.0917	0.0986	0.0911	0.1711	0.1935	0.0353	0.0069	0.162	0.014	0.1542	25.4804	15.3848	97.935
9	9.2936	5.7019	-3.1571	3.8765	-0.5907	7.1756	0.1886	0.0105	-0.5043	0.0005	-0.1607	-0.2342	0.1479	0.4079	0.0445	0.1993	0.0482	-0.0274	0.1358	0.0345	0.25	31.719	11.8841	100.3852
10	3.6759	1.4876	0.5061	1.8447	1.7894	2.2585	0.1227	-0.1635	0.0105	0.1012	-0.0564	0.0425	0.0872	0.0276	-0.0513	0.1641	0.0025	-0.0125	0.1342	0.044	0.1468	28.4185	17.8615	108.7589
11	9.3691	1.6715	2.7332	9.4009	-6.6906	6.4575	0.4092	1.5863	-0.9808	-0.891	-0.5863	-0.6233	1.0417	0.9426	0.3417	0.3704	0.0982	-0.0366	0.4032	-0.1024	0.3378	34.5681	6.6312	100.2939
12	4.8867	0.9651	-0.9099	3.623	3.4873	4.0733	0.45	-0.7542	-0.2926	0.1577	-0.0002	-0.5749	0.0792	0.7533	-0.388	0.2422	0.0199	-0.0415	0.2656	-0.0266	0.3025	34.2682	15.0746	113.6994
13	6.3491	1.9514	1.739	2.6318	-2.2831	8.1299	0.0578	-0.3521	-0.0768	0.5882	-0.0662	-0.0169	0.1328	0.8064	0.0765	0.2812	0.0439	-0.0265	0.1376	0.0417	0.2034	30.9183	13.6917	125.2411
14	6.2453	4.4004	5.1623	6.9305	5.9395	7.7667	0.1523	0.0032	-0.5058	0.0671	0.0459	-0.2725	0.7244	0.2931	-0.1458	0.2618	0.037	-0.0089	0.152	0.057	0.2582	28.0479	7.8086	117.4489
15	7.6343	0.7367	2.0517	8.509	-1.3618	4.813	0.1239	-0.6557	-0.7189	0.3926	0.0377	-0.1732	0.3378	0.1404	-0.0851	0.2764	0.0315	0.0201	0.2226	0.0659	0.2053	27.8031	7.5983	124.816
16	3.9969	0.5005	1.2819	5.9627	-1.8736	4.4618	-0.1412	-0.2618	-0.079	0.3246	0.0192	0.1881	-0.0765	0.0036	0.0036	0.154	0.0203	0.0439	0.1641	0.0107	0.1744	24.1329	17.6689	122.2463
17	6.218	2.525	-1.4901	4.8098	-1.0001	8.4578	0.0836	-0.965	-1.2765	1.0986	0.2317	0.3775	1.0031	0.3296	-0.0745	0.4713	0.0639	-0.0293	0.2775	0.1337	0.4246	26.7366	3.9637	129.2815
18	7.8614	4.4595	2.249	3.1379	3.1856	6.7684	0.1147	-0.6006	-0.0085	1.1444	-0.0314	-0.1471	-0.1088	-0.0513	-0.2245	0.314	0.0436	0.004	0.2619	0.039	0.2138	22.4052	19.5419	130.7938
19	2.8889	-1.0274	0.2591	3.552	1.7983	2.0034	-0.1666	-0.5418	-0.3076	0.5711	0.1428	0.2729	0.0055	-0.0436	0.0308	0.3461	0.0011	0.1041	0.3057	0.0838	0.209	12.234	20.882	130.935
20	4.8138	4.351	4.2466	7.171	4.4542	3.8866	-0.0239	-0.4066	0.3266	0.7135	-0.1115	0.9585	-0.3875	-0.455	0.0225	0.4997	0.0548	0.1793	0.3839	0.1563	0.4174	7.9976	20.0895	132.4812
21	2.1873	-0.4017	0.8887	3.1144	1.4792	1.4289	-0.0311	-0.5877	-0.2112	0.4081	-0.091	0.3348	0.1166	-0.2995	0.1229	0.3016	0.005	0.0655	0.3087	0.051	0.1817	8.8775	23.9904	127.0683
22	6.0099	5.9637	-5.5384	5.7975	-5.4417	5.0669	0.2682	-0.7004	0.2265	0.6952	-0.5483	0.1839	-0.5021	0.0069	0.2089	0.3063	0.0149	0.0106	0.2647	0.0017	0.2683	7.2189	32.5117	124.6977
23	4.0582	1.8016	1.1268	4.9779	-0.1915	2.8025	0.0448	-0.2768	-0.0237	0.357	-0.1821	0.1389	-0.127	-0.0592	0.0376	0.1719	0.0587	0.0915	0.1912	-0.0195	0.1587	2.6596	32.4691	115.5144
24	6.6057	0.3188	0.8281	5.9604	2.1046	3.7772	-0.1059	-0.0168	0.0953	0.134	0.0609	0.3062	-0.1266	-0.3315	0.0808	0.1618	0.0067	0.0322	0.1848	0.02	0.1577	0.3492	33.2331	113.6658
25	5.8827	1.1257	-0.4805	2.4601	0.0524	2.6589	-0.0796	0.061	0.0669	-0.0965	0.0266	0.1508	0.0165	-0.1607	0.0156	0.141	0.0033	0.0094	0.1044	0.0007	0.1178	5.9714	33.0131	109.1874
26	5.8229	1.5107	-4.1273	4.203	-0.6386	6.0975	0.2273	0.1472	0.1809	-0.0146	-0.0647	0.1949	-0.0825	-0.0543	-0.2027	0.1436	0.0271	-0.0636	0.1357	0.0582	0.084	14.0018	29.5134	96.6081
27	3.295	-0.3667	1.1073	3.4763	-0.1017	5.7041	0.0415	0.2286	-0.0796	-0.185	-0.0258	0.1349	-0.0019	-0.0712	-0.0168	0.1043	0.0129	0.0072	0.1164	0.0012	0.1418	16.5757	27.0281	96.3071
28	6.9238	0.7062	0.9897	6.4765	-0.1488	6.7356	0.0791	-0.1257	0.0975	-0.1312	-0.1821	-0.7016	-0.2437	0.6998	-0.0714	0.1565	0.0009	0.008	0.2192	0.0181	0.2346	27.3747	26.0795	98.3322
29	6.9934	-1.4327	-2.29	0.7794	-0.7223	6.6801	0.1591	-0.0645	1.3878	-1.5896	0.605	-0.6913	-1.3208	0.7558	-0.6501	0.536	-0.0774	0.0804	0.2779	0.0148	0.4614	27.1424	62.886	116.9258

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 27 )	A	1 - 27
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 28 through 76 )	A	28 - 76
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 77 through 164 )	A	77 - 164
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 165 through 225 )	A	165 - 225
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 226 through 242 )	A	226 - 242
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 258 through 297 )	A	258 - 297
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 1 through 13 )	B	1 - 13
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 14 through 23 )	B	14 - 23
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 24 through 32 )	B	24 - 32
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 33 through 52 )	B	33 - 52
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 53 through 63 )	B	53 - 63
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 64 through 70 )	B	64 - 70
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 1 through 13 )	C	1 - 13
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 14 through 23 )	C	14 - 23
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 24 through 32 )	C	24 - 32
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 33 through 52 )	C	33 - 52
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 53 through 63 )	C	53 - 63
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 64 through 70 )	C	64 - 70
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 1 through 23 )	D	1 - 23
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 24 through 32 )	D	24 - 32
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 33 through 63 )	D	33 - 63
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 64 through 70 )	D	64 - 70
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 1 through 18 )	E	1 - 18
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 19 through 32 )	E	19 - 32
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 33 through 70 )	E	33 - 70
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 1 through 18 )	F	1 - 18
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 19 through 63 )	F	19 - 63
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 64 through 70 )	F	64 - 70
29	X-RAY DIFFRACTION	29	chain 'P' and (resid 6 through 11 )	P	6 - 11

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