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- PDB-5d5m: Structure of human MR1-5-OP-RU in complex with human MAIT M33.64 TCR -

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Basic information

Entry
Database: PDB / ID: 5d5m
TitleStructure of human MR1-5-OP-RU in complex with human MAIT M33.64 TCR
Components
  • Beta-2-microglobulin
  • M33.64 TCR Alpha Chain
  • M33.64 TCR Beta Chain
  • Major histocompatibility complex class I-related gene protein
KeywordsIMMUNE SYSTEM / Antigen
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 / beta-2-microglobulin binding / antigen processing and presentation of peptide antigen via MHC class I / T cell receptor binding / negative regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions ...positive regulation of T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of exogenous antigen / MHC class I receptor activity / beta-2-microglobulin binding / antigen processing and presentation of peptide antigen via MHC class I / T cell receptor binding / negative regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / transferrin transport / 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 / cellular response to iron(III) ion / MHC class II protein complex / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of iron ion transport / regulation of erythrocyte differentiation / HFE-transferrin receptor complex / response to molecule of bacterial origin / MHC class I peptide loading complex / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / 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 / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / multicellular organismal-level iron ion homeostasis / specific granule lumen / phagocytic vesicle membrane / recycling endosome membrane / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / 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 / positive regulation of cellular senescence / tertiary granule lumen / DAP12 signaling / T cell differentiation in thymus / negative regulation of neuron projection development / 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 / Golgi membrane / lysosomal membrane / innate immune response / external side of plasma membrane / 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
MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : ...MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-2LJ / ACETATE ION / Beta-2-microglobulin / Major histocompatibility complex class I-related protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.2 Å
AuthorsKeller, A.N. / Birkinshaw, R.W. / Rossjohn, J.
CitationJournal: Immunity / Year: 2016
Title: Diversity of T Cells Restricted by the MHC Class I-Related Molecule MR1 Facilitates Differential Antigen Recognition.
Authors: Gherardin, N.A. / Keller, A.N. / Woolley, R.E. / Le Nours, J. / Ritchie, D.S. / Neeson, P.J. / Birkinshaw, R.W. / Eckle, S.B. / Waddington, J.N. / Liu, L. / Fairlie, D.P. / Uldrich, A.P. / ...Authors: Gherardin, N.A. / Keller, A.N. / Woolley, R.E. / Le Nours, J. / Ritchie, D.S. / Neeson, P.J. / Birkinshaw, R.W. / Eckle, S.B. / Waddington, J.N. / Liu, L. / Fairlie, D.P. / Uldrich, A.P. / Pellicci, D.G. / McCluskey, J. / Godfrey, D.I. / Rossjohn, J.
History
DepositionAug 11, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 27, 2016Provider: repository / Type: Initial release
Revision 1.1Feb 3, 2016Group: Database references
Revision 2.0Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Non-polymer description / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / citation / database_2 / diffrn_radiation_wavelength / diffrn_source / entity / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_struct_oper_list / struct_conn
Item: _chem_comp.formula / _chem_comp.formula_weight ..._chem_comp.formula / _chem_comp.formula_weight / _chem_comp.name / _citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.pdbx_leaving_atom_flag
Revision 2.1Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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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: Beta-2-microglobulin
E: M33.64 TCR Alpha Chain
F: M33.64 TCR Beta Chain
G: M33.64 TCR Alpha Chain
H: M33.64 TCR Beta Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)188,23216
Polymers187,1138
Non-polymers1,1198
Water13,601755
1
A: Major histocompatibility complex class I-related gene protein
B: Beta-2-microglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,9073
Polymers43,5912
Non-polymers3161
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2560 Å2
ΔGint-9 kcal/mol
Surface area18980 Å2
MethodPISA
2
C: Major histocompatibility complex class I-related gene protein
D: Beta-2-microglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,0585
Polymers43,5912
Non-polymers4673
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2640 Å2
ΔGint-9 kcal/mol
Surface area19020 Å2
MethodPISA
3
E: M33.64 TCR Alpha Chain
F: M33.64 TCR Beta Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,0583
Polymers49,9662
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4230 Å2
ΔGint-28 kcal/mol
Surface area20520 Å2
MethodPISA
4
G: M33.64 TCR Alpha Chain
H: M33.64 TCR Beta Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,2095
Polymers49,9662
Non-polymers2433
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4640 Å2
ΔGint-30 kcal/mol
Surface area20540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)216.197, 70.260, 142.379
Angle α, β, γ (deg.)90.000, 104.150, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Protein , 4 types, 8 molecules ACBDEGFH

#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 / Fragment: Extracellular domain residues 23-291
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MR1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q95460
#2: Protein Beta-2-microglobulin


Mass: 11879.356 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P61769
#3: Protein M33.64 TCR Alpha Chain


Mass: 22783.283 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli BL21(DE3) (bacteria)
#4: Protein M33.64 TCR Beta Chain


Mass: 27182.260 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli BL21(DE3) (bacteria)

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Non-polymers , 4 types, 763 molecules

#5: Chemical ChemComp-2LJ / 1-deoxy-1-({2,6-dioxo-5-[(E)-propylideneamino]-1,2,3,6-tetrahydropyrimidin-4-yl}amino)-D-ribitol / 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil


Mass: 316.310 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H20N4O6
#6: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 755 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.84 Å3/Da / Density % sol: 56.73 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: BTP, PEG 3350, NaAc

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.953 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 22, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.953 Å / Relative weight: 1
ReflectionResolution: 2.2→75.11 Å / Num. obs: 105471 / % possible obs: 99.9 % / Redundancy: 3.7 % / Biso Wilson estimate: 34.25 Å2 / CC1/2: 0.991 / Rmerge(I) obs: 0.111 / Rpim(I) all: 0.068 / Net I/σ(I): 7.4 / Num. measured all: 387238 / Scaling rejects: 16
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) all% possible all
2.2-2.243.70.66321915051510.7650.39899.9
12.05-75.113.50.06915.424347020.9870.04399.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIXrefinement
Aimless0.5.7data scaling
PHASERphasing
PDB_EXTRACT3.15data extraction
iMOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4L4T

4l4t


Resolution: 2.2→47.739 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.59 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2221 5253 4.98 %Random selection
Rwork0.1706 100169 --
obs0.1731 105422 99.89 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 146.95 Å2 / Biso mean: 47.8493 Å2 / Biso min: 16.14 Å2
Refinement stepCycle: final / Resolution: 2.2→47.739 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12918 0 83 755 13756
Biso mean--38.04 43.69 -
Num. residues----1607
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00813396
X-RAY DIFFRACTIONf_angle_d1.09918176
X-RAY DIFFRACTIONf_chiral_restr0.0451921
X-RAY DIFFRACTIONf_plane_restr0.0052380
X-RAY DIFFRACTIONf_dihedral_angle_d15.2124861
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.2250.29291670.243933403507100
2.225-2.25120.29481810.24632713452100
2.2512-2.27860.26931570.238833393496100
2.2786-2.30750.27951950.229832913486100
2.3075-2.33780.2941890.230833323521100
2.3378-2.36990.29621810.230133283509100
2.3699-2.40370.2861700.224933163486100
2.4037-2.43960.30061910.221632703461100
2.4396-2.47770.29231670.215333713538100
2.4777-2.51830.25291650.211533133478100
2.5183-2.56180.26421590.199433143473100
2.5618-2.60830.281520.200633613513100
2.6083-2.65850.29181790.208233033482100
2.6585-2.71280.3021660.204333693535100
2.7128-2.77170.31091700.204833213491100
2.7717-2.83620.261780.200333263504100
2.8362-2.90710.24941790.188533403519100
2.9071-2.98570.25871620.186533143476100
2.9857-3.07360.24441640.186633703534100
3.0736-3.17280.24421860.185333253511100
3.1728-3.28610.22961880.184132923480100
3.2861-3.41770.23191820.16833403522100
3.4177-3.57320.22172000.161733253525100
3.5732-3.76150.18721630.15333653528100
3.7615-3.9970.19081720.15333483520100
3.997-4.30550.18131660.131133753541100
4.3055-4.73840.14561940.114233473541100
4.7384-5.42320.16171920.124333713563100
5.4232-6.82950.20891660.15633993565100
6.8295-47.75030.18461720.15323493366599
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°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)
11.50120.0283-0.28983.0569-0.17311.98940.05860.21030.044-0.1243-0.05420.26620.0287-0.03510.01960.1957-0.0085-0.01620.1861-0.00740.2108-3.577365.122159.0408
22.0023-0.102-0.1692.0577-0.23681.32860.0392-0.0913-0.09460.1624-0.1008-0.02410.02530.0650.07110.2606-0.0430.00150.1823-0.00980.17493.992957.7895169.7157
31.7424-0.4250.20412.43070.87061.87540.3563-0.36080.28970.1514-0.10910.5329-0.2306-0.2286-0.22980.35950.02730.00220.27880.0010.3725-20.779677.9001186.3828
43.75090.2180.16663.33190.42964.68080.0082-0.5284-0.35420.1593-0.15390.14210.541-0.23960.14090.3447-0.01060.0620.25440.00660.3418-18.493673.492191.1413
54.0666-0.80170.46144.6049-0.7162.8534-0.1087-0.09390.22450.3246-0.08070.4255-0.3147-0.2930.21160.2524-0.00230.01430.2705-0.02850.3283-26.25270.1409174.921
62.6407-2.4621-1.17156.15062.24041.91670.04980.29060.4674-0.2782-0.2810.0031-0.3715-0.3220.18110.37350.0442-0.05830.2959-0.0530.4058-24.20971.259171.3014
79.166-6.1672-0.75056.89450.40782.76850.21340.8143-0.2578-0.7403-0.33350.7572-0.2701-0.61070.09970.40640.0018-0.12710.4541-0.08660.5054-29.158765.7548163.2853
86.755-0.10112.98642.0252-1.12218.71450.15271.22060.5204-0.73110.10940.1841-0.5042-0.3528-0.20980.78380.0925-0.17790.738-0.01640.6342-26.244975.3256160.09
96.2114-4.43531.23524.3775-3.07774.283-0.16450.01670.1174-0.04690.12060.23920.01690.12360.0670.3226-0.05010.01620.2717-0.05970.2858-11.202962.7663168.7277
103.0996-4.9216-0.05467.86980.42074.6814-0.19810.61810.4525-0.30220.08610.1669-0.8177-0.47380.09220.38920.0234-0.04970.3731-0.0090.4391-23.753472.9138167.8004
116.55891.4101-0.48594.18481.80473.21990.207-0.1829-0.12170.6403-0.1820.59290.2693-0.6305-0.06940.59590.1891-0.1360.7494-0.0971.0332-41.646977.0485173.3914
124.0567-2.2794-0.67845.3311.39253.11050.07790.7055-0.8332-0.6292-0.32271.44980.1452-0.16870.26860.3207-0.0199-0.06180.3467-0.1150.5335-29.950959.6996166.1601
138.6633-1.0117-0.48965.68711.54725.8012-0.1492-0.65780.59750.3827-0.17360.6143-0.3229-0.73840.3640.3258-0.01840.08330.5946-0.08930.5043-34.111168.5367175.344
142.2396-0.22320.19682.727-0.27281.8429-0.0178-0.5090.25120.26050.0340.0944-0.1197-0.30080.00460.24470.1011-0.0230.5746-0.06670.3535-46.86644.6476191.053
152.167-0.26910.32842.47-0.32411.09960.0023-0.08610.3422-0.0745-0.0254-0.2528-0.1045-0.09110.02150.25480.0541-0.0180.3941-0.02830.3451-36.745544.7944180.228
162.7331-0.9561.43663.3195-1.97575.813-0.25410.1280.6636-0.3584-0.0575-0.0455-0.60940.07360.27430.4048-0.1054-0.16940.45790.10710.6059-65.591546.1041160.1077
171.2060.4901-1.26972.1582-0.76041.62710.0883-0.50970.5242-0.237-0.36750.5901-0.4499-0.62420.17020.39380.1898-0.07110.51080.03340.6778-58.674959.2819176.9228
188.617-3.5262-2.10922.68220.22050.8666-0.39630.3007-0.4552-0.6786-0.25451.5889-0.493-1.720.59260.47550.0216-0.26810.9818-0.04161.2062-79.794146.0729173.6675
195.4988-0.1603-1.51020.9538-0.79771.45380.2372-0.88290.36010.1215-0.14390.9056-0.7059-0.6598-0.08360.26180.3881-0.17790.8064-0.2540.994-65.259455.6247182.3283
206.7593-5.68040.60354.7946-0.51020.0764-0.2388-1.12780.35030.86270.01610.9506-0.321-0.38340.0760.59520.30720.05841.2971-0.18851.0891-73.805855.9024188.7006
213.20190.1207-3.24171.10030.18433.38890.0419-0.44970.2305-0.0228-0.08820.3686-0.1649-0.35650.13820.25130.0551-0.03360.5647-0.00560.4353-52.05750.7574181.6097
228.0887-1.38220.60930.5878-0.88171.8115-0.2272-0.9349-0.04710.46460.16860.95720.165-0.87970.06940.32340.15150.02760.8834-0.11660.832-67.7850.4878182.7225
234.69972.35730.82313.7655-1.25311.22420.31530.15710.0264-0.48430.4890.5742-0.2055-0.4798-0.56930.56670.1669-0.13961.54850.08961.5358-84.406457.0709176.7911
243.440.94140.92051.65950.39161.3277-0.1369-0.25051.15490.25430.1470.7416-0.2849-0.5147-0.12050.58560.2709-0.09250.7825-0.26161.1351-64.575464.8672182.4933
253.30424.3906-0.54026.62960.10992.2283-0.6398-0.08330.3141-0.42150.42160.1630.3036-0.40050.02930.52640.2062-0.29170.69870.00151.1349-73.25759.8821174.2716
263.4244-1.8882.371.6258-1.38262.2178-0.0937-0.13960.10470.04130.0472-0.05580.0778-0.06160.05920.21640.04240.01370.2559-0.05110.2407-16.749323.8392193.9697
273.2283-0.1898-0.6142.7192-0.3765.9536-0.04240.134-0.230.4002-0.0371-0.04860.5231-0.11380.090.44090.07230.02340.2486-0.03870.30640.925811.5916216.259
289.29242.50851.13385.98651.30426.8699-0.06710.2776-0.83880.69240.088-0.03631.3170.30150.02360.63110.15150.03250.3937-0.10480.44566.73952.877211.7559
291.5384-0.09640.39622.1491-1.37722.4848-0.0493-0.5980.12150.30940.07810.1152-0.3144-0.6151-0.03050.32690.1127-0.01790.7093-0.09220.2895-31.10734.1707211.9601
300.6977-0.21980.66460.4688-0.33422.2862-0.0633-0.0811-0.10740.12420.088-0.0202-0.0234-0.2236-0.02860.2846-0.0016-0.00760.2947-0.07360.2885-11.878624.5276216.9413
314.6804-0.7384-3.33850.75351.15694.5420.19360.29870.1577-0.1099-0.08520.025-0.3181-0.3547-0.12590.45550.1106-0.01910.3239-0.01340.2869-6.019823.5754224.0882
323.51580.0617-1.39651.2010.04283.3828-0.0184-0.0673-0.05860.0736-0.0561-0.16460.17120.38470.08550.264-0.0107-0.03110.20710.04660.246930.699363.2719158.7787
334.0657-0.6777-2.3711.15880.51362.60250.0635-0.01690.0912-0.2771-0.0475-0.33970.13270.65490.0180.42340.05870.03540.52690.0850.380346.334163.0405141.6192
345.12460.2253-0.26183.20120.5145.3308-0.1378-0.21010.32950.0040.1247-0.3691-0.28721.03350.05090.41320.02520.06360.61990.01930.549556.248365.8765138.4282
352.32320.1776-0.69131.0774-0.51144.0204-0.06160.18-0.0848-0.21860.0186-0.02080.2085-0.32110.06390.3219-0.0208-0.0050.2095-0.02990.263915.659562.8529139.8123
364.0017-2.1306-5.1281.8532.71816.6990.2938-0.1170.7498-0.32150.0629-0.1328-0.19950.151-0.23820.4645-0.03190.03670.2540.0350.355629.355868.7527123.4973
371.3259-0.25930.63922.3812-0.81743.2115-0.1041-0.0272-0.27890.06980.1111-0.09780.54590.6462-0.04180.55260.15630.12150.38580.03820.410148.201956.3414130.2918
386.1281-1.76471.03214.7115-1.18034.45110.30070.5389-0.0739-0.7146-0.07140.23520.26750.1356-0.20080.63750.0270.12620.3064-0.0740.307535.964158.6723117.999
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 83 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 84 through 171 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 172 through 195 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 196 through 269 )A0
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 19 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 20 through 30 )B0
7X-RAY DIFFRACTION7chain 'B' and (resid 31 through 46 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 47 through 51 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 52 through 61 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 62 through 71 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 72 through 77 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 78 through 90 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 91 through 98 )B0
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 84 )C0
15X-RAY DIFFRACTION15chain 'C' and (resid 85 through 171 )C0
16X-RAY DIFFRACTION16chain 'C' and (resid 172 through 269 )C0
17X-RAY DIFFRACTION17chain 'D' and (resid 0 through 11 )D0
18X-RAY DIFFRACTION18chain 'D' and (resid 12 through 19 )D0
19X-RAY DIFFRACTION19chain 'D' and (resid 20 through 41 )D0
20X-RAY DIFFRACTION20chain 'D' and (resid 42 through 51 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 52 through 61 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 62 through 71 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 72 through 77 )D0
24X-RAY DIFFRACTION24chain 'D' and (resid 78 through 90 )D0
25X-RAY DIFFRACTION25chain 'D' and (resid 91 through 97 )D0
26X-RAY DIFFRACTION26chain 'E' and (resid 1 through 120 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 121 through 185 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 186 through 200 )E0
29X-RAY DIFFRACTION29chain 'F' and (resid 3 through 94 )F0
30X-RAY DIFFRACTION30chain 'F' and (resid 95 through 139 )F0
31X-RAY DIFFRACTION31chain 'F' and (resid 140 through 242 )F0
32X-RAY DIFFRACTION32chain 'G' and (resid 1 through 91 )G0
33X-RAY DIFFRACTION33chain 'G' and (resid 92 through 135 )G0
34X-RAY DIFFRACTION34chain 'G' and (resid 136 through 198 )G0
35X-RAY DIFFRACTION35chain 'H' and (resid 3 through 108 )H0
36X-RAY DIFFRACTION36chain 'H' and (resid 109 through 123 )H0
37X-RAY DIFFRACTION37chain 'H' and (resid 124 through 214 )H0
38X-RAY DIFFRACTION38chain 'H' and (resid 215 through 243 )H0

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