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- PDB-9bty: Structure of human MAIT A-F7 TCR in complex with human MR1-veratr... -

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Open data

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Basic information

Entry

Database: PDB / ID: 9bty

Title

Structure of human MAIT A-F7 TCR in complex with human MR1-veratraldehyde

Components

Beta-2-microglobulin
Human TCR TRAV1-2_ALPHA
Human TCR TRBV6-1_BETA
Major histocompatibility complex class I-related gene protein

Keywords

IMMUNE SYSTEM / antigen presentation / MAIT cells / T cell receptor / MR1

Function / homology

Function and homology information

positive regulation of T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of exogenous antigen / MHC class I receptor activity / antigen processing and presentation of peptide antigen via MHC class I / beta-2-microglobulin binding / T cell receptor binding / : / : / negative regulation of receptor binding / positive regulation of receptor binding ...positive regulation of T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of exogenous antigen / MHC class I receptor activity / antigen processing and presentation of peptide antigen via MHC class I / beta-2-microglobulin binding / T cell receptor binding / : / : / negative regulation of receptor binding / positive regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / cellular response to iron ion / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide antigen assembly with MHC class II protein complex / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / MHC class II protein complex / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / regulation of iron ion transport / response to molecule of bacterial origin / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / MHC class I protein complex / positive regulation of T cell activation / peptide antigen binding / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / cellular response to nicotine / multicellular organismal-level iron ion homeostasis / positive regulation of protein binding / specific granule lumen / phagocytic vesicle membrane / recycling endosome membrane / positive regulation of cellular senescence / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon gamma signaling / negative regulation of epithelial cell proliferation / MHC class II protein complex binding / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / tertiary granule lumen / DAP12 signaling / T cell differentiation in thymus / negative regulation of neuron projection development / iron ion transport / ER-Phagosome pathway / protein refolding / early endosome membrane / defense response to Gram-negative bacterium / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / defense response to Gram-positive bacterium / immune response / endoplasmic reticulum lumen / Amyloid fiber formation / external side of plasma membrane / Golgi membrane / lysosomal membrane / innate immune response / focal adhesion / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.85 Å

Authors

Awad, W. / Rossjohn, J.

Funding support

Australia, 2items

Citation

Journal: J.Exp.Med. / Year: 2025
Title: Cigarette smoke components modulate the MR1-MAIT axis.
Authors: Awad, W. / Mayall, J.R. / Xu, W. / Johansen, M.D. / Patton, T. / Lim, X.Y. / Galvao, I. / Howson, L.J. / Brown, A.C. / Haw, T.J. / Donovan, C. / Das, S. / Albers, G.J. / Pai, T.Y. / Hortle, ...

History

Deposition	May 15, 2024	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Dec 25, 2024	Provider: repository / Type: Initial release
Revision 1.1	Jan 29, 2025	Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewer	Molecule: MolmilJmol/JSmol

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Downloads & links

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Download

PDBx/mmCIF format	9bty.cif.gz	772.1 KB	Display	PDBx/mmCIF format
PDB format	pdb9bty.ent.gz	529.7 KB	Display	PDB format
PDBx/mmJSON format	9bty.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	9bty_validation.pdf.gz	1.1 MB	Display	wwPDB validaton report
Full document	9bty_full_validation.pdf.gz	1.1 MB	Display
Data in XML	9bty_validation.xml.gz	65.3 KB	Display
Data in CIF	9bty_validation.cif.gz	85.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/bt/9bty ftp://data.pdbj.org/pub/pdb/validation_reports/bt/9bty	HTTPS FTP

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Related structure data

Related structure data	9btxC 9btzC 9bu0C 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
Related items in Molecule of the Month	#62 - Feb 2005 Major Histocompatibility Complex similarity (1) #63 - Mar 2005 T-Cell Receptor similarity (1)

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Assembly

Deposited unit

A: Major histocompatibility complex class I-related gene protein

B: Beta-2-microglobulin

C: Major histocompatibility complex class I-related gene protein

D: Human TCR TRAV1-2_ALPHA

E: Human TCR TRBV6-1_BETA

F: Beta-2-microglobulin

G: Human TCR TRAV1-2_ALPHA

H: Human TCR TRBV6-1_BETA

hetero molecules

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

Idetical with deposited unit
defined by author&software
Evidence: surface plasmon resonance

Unit cell

Length a, b, c (Å)	216.843, 70.281, 143.207
Angle α, β, γ (deg.)	90.000, 104.120, 90.000
Int Tables number	5
Space group name H-M	C121
Space group name Hall	C2y

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Components

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Protein , 4 types, 8 molecules ACBFDGEH

#1: Protein	Major histocompatibility complex class I-related gene protein / MHC class I-related gene protein / Class I histocompatibility antigen-like protein Mass: 31711.670 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MR1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q95460
#2: Protein	Beta-2-microglobulin Mass: 11879.356 Da / Num. of mol.: 2 / Fragment: UNP residues 21-119 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / References: UniProt: P61769
#3: Protein	Human TCR TRAV1-2_ALPHA Mass: 22781.268 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#4: Protein	Human TCR TRBV6-1_BETA Mass: 27677.760 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)

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Non-polymers , 4 types, 206 molecules

#5: Chemical	ChemComp-XIK / 3,4-dimethoxybenzaldehyde Mass: 166.174 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₉H₁₀O₃ / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical	ChemComp-ACT / ACETATE ION Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₃O₂
#7: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C₃H₈O₃
#8: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 198 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
Has protein modification	Y

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Experimental details

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.81 Å³/Da / Density % sol: 56.27 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, Na acetate, BTP

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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: 0.9537 Å
Detector	Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 16, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection	Resolution: 2.85→39.91 Å / Num. obs: 222966 / % possible obs: 98.36 % / Redundancy: 4.6 % / B_iso Wilson estimate: 56.05 Å² / CC_1/2: 0.995 / R_merge(I) obs: 0.124 / Net I/σ(I): 11.65
Reflection shell	Resolution: 2.853→2.955 Å / Num. unique obs: 20545 / CC_1/2: 0.772

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Processing

Software

Name	Version	Classification
PHENIX	1.20.1_4487	refinement
XDS		data reduction
XDS		data scaling
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.85→39.91 Å / SU ML: 0.3911 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 23.6031
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2

	R_factor	Num. reflection	% reflection
R_free	0.2233	3864	4.14 %
R_work	0.161	89515	-
obs	0.1635	93379	97.87 %

Solvent computation

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

Displacement parameters

B_iso mean: 51.53 Å²

Refinement step

Cycle: LAST / Resolution: 2.85→39.91 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12545	0	56	198	12799

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.0076	12965
X-RAY DIFFRACTION	f_angle_d	0.9661	17648
X-RAY DIFFRACTION	f_chiral_restr	0.0521	1894
X-RAY DIFFRACTION	f_plane_restr	0.0079	2293
X-RAY DIFFRACTION	f_dihedral_angle_d	16.0696	4566

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 (%)
2.85-2.89	0.4042	107	0.3113	2434	X-RAY DIFFRACTION	76.1
2.89-2.92	0.336	139	0.2792	3312	X-RAY DIFFRACTION	98.6
2.92-2.96	0.3308	137	0.2766	3146	X-RAY DIFFRACTION	98.38
2.96-3	0.326	138	0.2536	3261	X-RAY DIFFRACTION	98.92
3-3.05	0.32	140	0.2548	3230	X-RAY DIFFRACTION	98.6
3.05-3.09	0.367	141	0.2365	3216	X-RAY DIFFRACTION	98.59
3.09-3.14	0.3074	141	0.2199	3182	X-RAY DIFFRACTION	98.78
3.14-3.19	0.3157	134	0.2125	3299	X-RAY DIFFRACTION	98.56
3.19-3.25	0.2091	134	0.2054	3118	X-RAY DIFFRACTION	97.13
3.25-3.31	0.2806	138	0.1868	3146	X-RAY DIFFRACTION	97.16
3.31-3.37	0.2779	140	0.1889	3282	X-RAY DIFFRACTION	98.5
3.37-3.44	0.3145	138	0.1802	3208	X-RAY DIFFRACTION	98.76
3.44-3.51	0.2373	142	0.1759	3239	X-RAY DIFFRACTION	98.83
3.51-3.59	0.2456	141	0.1702	3217	X-RAY DIFFRACTION	98.94
3.59-3.68	0.2041	142	0.1559	3300	X-RAY DIFFRACTION	99.14
3.68-3.78	0.189	139	0.1491	3184	X-RAY DIFFRACTION	99.16
3.78-3.89	0.2622	139	0.1494	3268	X-RAY DIFFRACTION	98.95
3.89-4.02	0.1957	139	0.137	3161	X-RAY DIFFRACTION	98.71
4.02-4.16	0.188	141	0.1324	3259	X-RAY DIFFRACTION	99.21
4.16-4.33	0.1541	139	0.1246	3231	X-RAY DIFFRACTION	99.09
4.33-4.53	0.1503	136	0.1152	3232	X-RAY DIFFRACTION	99.15
4.53-4.77	0.1815	141	0.1112	3243	X-RAY DIFFRACTION	99.27
4.77-5.06	0.1771	136	0.118	3263	X-RAY DIFFRACTION	99.07
5.06-5.45	0.2091	139	0.1294	3177	X-RAY DIFFRACTION	97.47
5.45-6	0.2216	141	0.1557	3213	X-RAY DIFFRACTION	98.36
6-6.87	0.2228	142	0.1728	3248	X-RAY DIFFRACTION	99.41
6.87-8.64	0.2401	144	0.1479	3259	X-RAY DIFFRACTION	99.62
8.65-39.91	0.1586	136	0.1502	3187	X-RAY DIFFRACTION	97.56

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	0.892665664264	-0.478772249468	0.179997568235	0.603959620903	0.46462307217	0.868313100075	0.0028945183622	0.0643848768861	0.048430179561	-0.149204861483	0.0572997908357	-0.0168090296555	0.050667554531	0.0781825215776	1.07041674406E-8	0.258817918952	-0.00285531774597	-0.000490338721319	0.266684631046	0.00882179320503	0.313982734516	51.3193951929	77.5848938415	224.255318819
2	0.54649313332	-0.0679514563127	-0.0163079666505	0.323891494659	-0.287380895879	0.186793718284	0.0138633821612	-0.0731190582884	0.0991894038813	0.0370284094353	-0.0117579576609	0.130510038344	0.0431602199367	0.0690542941511	2.41426255039E-8	0.226815263439	-0.000968179247804	0.0181079578564	0.221751313204	-0.0161261024443	0.29273881507	38.8025153985	81.4274203012	235.004019175
3	0.345092247787	-1.79314089373	0.616644341754	-0.0625866827566	1.06180414675	0.0422609313872	-0.329044497717	0.136961322438	-0.106488551905	-0.136030830981	0.424545389073	-0.203651139163	0.284869490396	0.023846472702	3.87800674113E-8	0.21585601848	0.0622391309978	-0.0644190812177	0.294679996535	0.0190777657937	0.278333385312	64.3759961523	72.0172575967	245.947383222
4	0.967947180938	0.000647946017534	-0.0972649695368	0.473588296188	-0.55834753682	0.604858949127	0.000523633670647	-0.00177413059185	0.146222793373	0.104842183046	-0.110338632676	0.115373118304	0.0301993616699	-0.248176882892	1.43781447767E-7	0.26339660987	0.0752262100871	-0.0857746161178	0.360809338506	-0.153871274122	0.34373197792	69.0126988368	81.0052646748	257.447578385
5	0.00464500050063	-0.00145965198172	-0.011037224839	-0.0588398421028	-0.0528619511393	0.00352989670613	-0.474504083231	0.225480744876	-0.252701527766	0.500355645602	-0.070009636562	0.360833999314	-0.324067344687	0.21941741533	1.64387245038E-8	0.401156216135	0.0166735228961	-0.112785888187	0.448694680031	-0.0844776731751	0.698403178536	64.3527600926	91.7173306768	239.38497186
6	0.00263511583777	0.0286397011731	-0.00862984117972	-0.00989985040976	-0.0712091219377	0.00736158920749	-0.611131881203	0.268820855704	-0.261106960588	0.147693590706	0.245623566045	-0.0362324127464	0.537680901789	0.415798361092	3.56356017629E-6	0.394188236524	-0.00242139036105	-0.152381761557	0.872684300962	-0.0464945069113	0.647958773166	83.8848421092	80.0022518112	241.660581745
7	0.0149917372747	0.0607570520524	0.0473423369439	0.0233262112991	0.19420939236	0.238069367253	0.196724343635	-0.22208525466	0.262691357609	-0.0673134378415	-0.0772211691132	-0.00930329390492	-0.0822742166603	0.0966519263379	7.04469119624E-7	0.29885116558	-0.0881707216141	-0.0136203369629	0.413476867463	0.0823243559858	0.478218479981	69.2746147938	89.4277985496	232.997253107
8	0.0123788660429	0.0162081292006	0.00388024962162	0.00964901640982	0.00565464414862	0.0131565442381	0.403123148049	-0.207730533271	0.260870662064	-0.0536360887874	0.135400343381	-0.163988640825	-0.146944301231	0.214082582424	0.000115225496616	0.603914058189	-0.0314260569415	-0.0533793138467	0.95587375337	0.0625171138501	0.847081566757	81.8547128561	94.5501552171	229.496531593
9	0.00771049952407	-0.00264989691675	-0.0173165676254	0.000280430626418	-0.0169789513128	0.00641333005726	0.158202685658	0.0496302076561	-0.316235772722	-0.308728546717	0.0754208918335	0.206878101378	0.370253644697	-0.288512417379	-2.52503945376E-5	0.574154656249	-0.112258248341	0.0503485719768	0.694910072699	-0.0911062288901	0.700503522632	74.1806403383	84.8284113584	225.874102499
10	0.0374755166133	0.0600837743675	-0.00917282489068	-0.0529774108586	-0.0248220721168	-0.0437257018751	-0.220063528559	0.154167974489	-0.032100823946	-0.0988657717524	-0.0612950542319	0.247155869736	-0.187488301096	0.198969581872	2.44244016346E-6	0.252282709358	-0.0339590588101	0.0554864243719	0.291788448192	-0.0141406468935	0.36530469084	56.1204388075	84.2714928935	233.73603737
11	0.0170734759746	0.0683407733457	0.0277954648203	0.0388169738073	-0.195147346414	0.0329224977698	-0.208360755082	0.347191535424	-0.637922025463	-0.294574458081	0.111155949148	0.108644609272	-0.180013357534	0.198367910192	2.25585535022E-8	0.180038881804	-0.0465001606899	0.0403497887986	0.406913849494	-0.0755088996607	0.474075331195	71.8926307593	84.2536977807	232.70363946
12	0.00112564841303	-0.00645360640779	0.0201932442685	-0.00906804306017	-0.00537388317141	-0.016117468851	0.210194765	0.249832095483	-0.163661116588	-0.188493027844	0.341868602383	0.132399570496	-0.193801235469	-0.196926183575	-6.51769541614E-6	0.539378560717	-0.0671912662284	-0.0495696690207	1.22405989494	-0.0024117961864	1.07568877006	88.4797990717	90.4165599263	238.412445327
13	0.0141964721184	0.00287767299404	0.00682056548251	-0.00469945847343	0.0582008185405	0.043815929784	-0.0539488192539	0.345774104239	-0.152124039537	-0.435846401612	0.265302848753	-0.531442388536	-0.11851420524	0.0334768496745	4.03217004681E-7	0.522685230603	-0.155440631219	-0.0558265605853	0.54491004817	0.119315388592	0.86014855424	73.9388815564	95.026018506	233.089763469
14	0.00121296642455	0.00818153934834	0.00495364177534	0.00819978816114	-0.00623271120069	0.0119111088278	0.222101302938	0.164880294934	-0.0980648089793	-0.332861629428	-0.20906135707	0.104276719085	-0.308774335454	-0.34381487369	1.63013578299E-5	0.544654380983	-0.0425015200781	-0.0816550873148	0.455776365808	-0.0269521282854	0.803507558637	63.078043758	101.576513731	232.503768575
15	0.0600177869455	0.0678728344777	-0.00991585772621	0.0556384483864	0.00862645291279	-0.0392688329184	-0.373083823302	0.147977150337	-0.0468893108031	0.359502773985	0.118680637245	-0.0418354473173	0.078679012755	-0.369629878838	4.26001440318E-6	0.381039403046	-0.0785197118002	-0.0862802478872	0.528793719113	-0.0375578983559	0.618840287017	77.1772136845	93.466822247	241.036234764
16	0.820746110959	0.0152215596632	-0.0654303429075	0.67684312346	-0.432862678589	0.536158366695	-0.00448624250161	0.151234111639	0.0815437659459	-0.0204274636155	0.0313445232556	0.084326516695	-0.0116276944898	0.0623726397821	-7.13473790968E-9	0.332443041516	-0.0257359004088	0.0322309139138	0.26044486648	-0.0127021328137	0.280871628865	-3.87113486763	63.5824309591	160.439611342
17	0.923811845107	-0.673140474994	0.257336297585	0.997561603629	-0.254443014784	0.0527414180131	0.0579112843083	0.0531268771647	-0.0578020254656	0.123339034999	-0.0784277360003	-0.0972200764912	-0.0187638470144	0.0760415496846	-1.10514157496E-8	0.32421229171	-0.040082751538	0.0253561495021	0.303744734896	-0.0148939272027	0.254466964863	3.815994117	55.839679448	170.696186547
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54	0.0288439707379	0.0197967308084	0.0379895783066	-0.0378260541305	0.0172797394349	0.0347020914111	-0.194288617884	0.622363192805	0.180255325307	0.409896588498	-0.00999942903859	0.180432471041	0.295682140457	0.490303583979	2.53406204179E-6	0.375286228458	-0.0071288607163	-0.0151444996865	0.375554857881	-0.0109947104178	0.293432999376	26.9913621178	53.9105076714	188.34023794
55	0.180814282226	-0.439932816442	-0.321400832093	0.717377464076	-0.526890513245	0.153828435001	0.0527930570579	-0.16278463421	0.0260059402613	-0.0202071372672	-0.0528433777051	0.080246219608	-0.0519160850075	0.0961521228266	-1.59544659996E-7	0.31786735905	-0.0574418521579	-0.0151363096445	0.303644376192	-0.0171829594608	0.267348287948	2.85859891024	53.7909193227	194.314335067
56	0.386108450724	0.266914136576	-0.585552650233	-0.0854452864068	-0.217182185618	0.319553698778	-0.0347105416558	-0.116573864853	-0.0174986186441	0.18033828167	-0.234206595784	-0.068683844429	-0.12225810726	0.199349364152	1.86363297186E-8	0.340978043621	-0.0109622223691	-0.00334104134795	0.291528696312	0.00596674083919	0.280088054774	12.3142638554	52.6156600796	196.503038144
57	0.105160625756	0.472244397435	-0.174643435742	0.663519534518	-0.171996930405	0.385212428828	0.0389559728366	-0.0488193228849	0.0998426294108	-0.0258728855473	0.026850103078	0.096932504358	-0.18028221946	0.0727277620332	-6.82737511323E-8	0.286128820471	-0.0631098483767	-0.0254139312358	0.239689738552	-0.0116779572973	0.23513273339	-1.09472600867	58.9331126291	193.733382813
58	0.281905441722	0.152873916381	0.197290621927	0.654681404574	-0.520326378572	0.300855611971	0.035089531477	-0.0159849058439	0.0639973597055	0.0549416350654	-0.0325646866676	-0.0887403739015	0.0824303858943	-0.00494536446568	-2.38494525224E-7	0.308545751754	-0.0528495705936	-0.0174948523195	0.320710180578	0.0116327100973	0.234597768809	15.9302272688	58.9509798495	182.402887101

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

ID	Refine TLS-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	chain 'A' and (resid 0 through 83 )	A	A	0 - 83	1 - 84
2	2	chain 'A' and (resid 84 through 158 )	A	A	84 - 158	85 - 159
3	3	chain 'A' and (resid 159 through 216 )	A	A	159 - 216	160 - 211
4	4	chain 'A' and (resid 217 through 269 )	A	A	217 - 269	212 - 264
5	5	chain 'B' and (resid 1 through 11 )	B	D	1 - 11	1 - 11
6	6	chain 'B' and (resid 12 through 19 )	B	D	12 - 19	12 - 19
7	7	chain 'B' and (resid 20 through 41 )	B	D	20 - 41	20 - 41
8	8	chain 'B' and (resid 42 through 46 )	B	D	42 - 46	42 - 46
9	9	chain 'B' and (resid 47 through 51 )	B	D	47 - 51	47 - 51
10	10	chain 'B' and (resid 52 through 61 )	B	D	52 - 61	52 - 61
11	11	chain 'B' and (resid 62 through 71 )	B	D	62 - 71	62 - 71
12	12	chain 'B' and (resid 72 through 77 )	B	D	72 - 77	72 - 77
13	13	chain 'B' and (resid 78 through 83 )	B	D	78 - 83	78 - 83
14	14	chain 'B' and (resid 84 through 90 )	B	D	84 - 90	84 - 90
15	15	chain 'B' and (resid 91 through 97 )	B	D	91 - 97	91 - 97
16	16	chain 'C' and (resid 0 through 83 )	C	E	0 - 83	1 - 84
17	17	chain 'C' and (resid 84 through 171 )	C	E	84 - 171	85 - 172
18	18	chain 'C' and (resid 172 through 270 )	C	E	172 - 270	173 - 266
19	19	chain 'D' and (resid 1 through 13 )	D	G	1 - 13	1 - 13
20	20	chain 'D' and (resid 14 through 25 )	D	G	14 - 25	14 - 25
21	21	chain 'D' and (resid 26 through 52 )	D	G	26 - 52	26 - 52
22	22	chain 'D' and (resid 53 through 75 )	D	G	53 - 75	53 - 75
23	23	chain 'D' and (resid 76 through 102 )	D	G	76 - 102	76 - 102
24	24	chain 'D' and (resid 103 through 135 )	D	G	103 - 135	103 - 129
25	25	chain 'D' and (resid 136 through 150 )	D	G	136 - 150	130 - 144
26	26	chain 'D' and (resid 151 through 165 )	D	G	151 - 165	145 - 159
27	27	chain 'D' and (resid 166 through 198 )	D	G	166 - 198	160 - 189
28	28	chain 'E' and (resid 3 through 73 )	E	H	3 - 73	1 - 71
29	29	chain 'E' and (resid 74 through 109 )	E	H	74 - 109	72 - 107
30	30	chain 'E' and (resid 110 through 140 )	E	H	110 - 140	108 - 138
31	31	chain 'E' and (resid 141 through 188 )	E	H	141 - 188	139 - 186
32	32	chain 'E' and (resid 189 through 215 )	E	H	189 - 215	187 - 213
33	33	chain 'E' and (resid 216 through 244 )	E	H	216 - 244	214 - 242
34	34	chain 'F' and (resid 1 through 11 )	F	I	1 - 11	1 - 11
35	35	chain 'F' and (resid 12 through 30 )	F	I	12 - 30	12 - 30
36	36	chain 'F' and (resid 31 through 46 )	F	I	31 - 46	31 - 46
37	37	chain 'F' and (resid 47 through 56 )	F	I	47 - 56	47 - 56
38	38	chain 'F' and (resid 57 through 71 )	F	I	57 - 71	57 - 71
39	39	chain 'F' and (resid 72 through 77 )	F	I	72 - 77	72 - 77
40	40	chain 'F' and (resid 78 through 90 )	F	I	78 - 90	78 - 90
41	41	chain 'F' and (resid 91 through 99 )	F	I	91 - 99	91 - 99
42	42	chain 'G' and (resid 1 through 17 )	G	J	1 - 17	1 - 17
43	43	chain 'G' and (resid 18 through 52 )	G	J	18 - 52	18 - 52
44	44	chain 'G' and (resid 53 through 75 )	G	J	53 - 75	53 - 75
45	45	chain 'G' and (resid 76 through 91 )	G	J	76 - 91	76 - 91
46	46	chain 'G' and (resid 92 through 103 )	G	J	92 - 103	92 - 103
47	47	chain 'G' and (resid 104 through 120 )	G	J	104 - 120	104 - 120
48	48	chain 'G' and (resid 121 through 150 )	G	J	121 - 150	121 - 150
49	49	chain 'G' and (resid 151 through 165 )	G	J	151 - 165	151 - 165
50	50	chain 'G' and (resid 166 through 201 )	G	J	166 - 201	166 - 201
51	51	chain 'H' and (resid 1 through 25 )	H	K	1 - 25	1 - 25
52	52	chain 'H' and (resid 26 through 94 )	H	K	26 - 94	26 - 94
53	53	chain 'H' and (resid 95 through 109 )	H	K	95 - 109	95 - 109
54	54	chain 'H' and (resid 110 through 124 )	H	K	110 - 124	110 - 124
55	55	chain 'H' and (resid 125 through 162 )	H	K	125 - 162	125 - 162
56	56	chain 'H' and (resid 163 through 188 )	H	K	163 - 188	163 - 188
57	57	chain 'H' and (resid 189 through 215 )	H	K	189 - 215	189 - 215
58	58	chain 'H' and (resid 216 through 244 )	H	K	216 - 244	216 - 244

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