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- PDB-5d7i: Structure of human MR1-Ac-6-FP in complex with human MAIT M33.64 TCR -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5d7i
TitleStructure of human MR1-Ac-6-FP in complex with human MAIT M33.64 TCR
Components
  • Beta-2-microglobulinBeta-2 microglobulin
  • M33.64 TCR Alpha Chain
  • M33.64 TCR Beta Chain
  • Major histocompatibility complex class I-related gene protein
KeywordsIMMUNE SYSTEM / Antigen / receptor
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 / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / early endosome lumen / 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 / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / early endosome lumen / positive regulation of receptor binding / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / negative regulation of receptor binding / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / response to molecule of bacterial origin / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / cellular response to iron ion / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / recycling endosome membrane / specific granule lumen / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon gamma signaling / positive regulation of immune response / negative regulation of epithelial cell proliferation / Modulation by Mtb of host immune system / positive regulation of T cell activation / sensory perception of smell / negative regulation of neuron projection development / tertiary granule lumen / DAP12 signaling / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / positive regulation of protein binding / ER-Phagosome pathway / iron ion transport / protein refolding / early endosome membrane / protein homotetramerization / intracellular iron ion homeostasis / defense response to Gram-negative bacterium / amyloid fibril formation / learning or memory / defense response to Gram-positive bacterium / immune response / Amyloid fiber formation / lysosomal membrane / endoplasmic reticulum lumen / external side of plasma membrane / Golgi membrane / focal adhesion / innate immune response / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / Golgi apparatus / endoplasmic reticulum / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / membrane / identical protein binding / 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 / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. ...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 / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-30W / PROLINE / Beta-2-microglobulin / Major histocompatibility complex class I-related gene protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsKeller, A.N. / Woolley, R.E. / 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 14, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 27, 2016Provider: repository / Type: Initial release
Revision 1.1Feb 3, 2016Group: Database references
Revision 1.2Feb 10, 2016Group: Refinement description
Revision 1.3Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength / diffrn_source / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _pdbx_struct_oper_list.symmetry_operation

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


Theoretical massNumber of molelcules
Total (without water)188,73122
Polymers187,1138
Non-polymers1,61814
Water23,2571291
1
A: Major histocompatibility complex class I-related gene protein
B: Beta-2-microglobulin
G: M33.64 TCR Alpha Chain
H: M33.64 TCR Beta Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,55013
Polymers93,5574
Non-polymers9939
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10330 Å2
ΔGint-46 kcal/mol
Surface area36060 Å2
MethodPISA
2
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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,1819
Polymers93,5574
Non-polymers6255
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9360 Å2
ΔGint-45 kcal/mol
Surface area37020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)214.300, 69.660, 141.190
Angle α, β, γ (deg.)90.000, 103.990, 90.000
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11H-637-

HOH

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Components

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Protein , 4 types, 8 molecules ACBDGEHF

#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 23-292
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MR1 / Plasmid: pET30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q95460
#2: Protein Beta-2-microglobulin / 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 / Plasmid: pET30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / 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) / Gene: TRAV/TRAV / Plasmid: pET30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
#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) / Gene: TRBV/TRBC / Plasmid: pET30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)

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Non-polymers , 4 types, 1305 molecules

#5: Chemical ChemComp-PRO / PROLINE / Proline


Type: L-peptide linking / Mass: 115.130 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H9NO2
#6: Chemical ChemComp-30W / N-(6-formyl-4-oxo-3,4-dihydropteridin-2-yl)acetamide / Acetyl 6-formylpterin


Mass: 233.184 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H7N5O3
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1291 / Source method: isolated from a natural source / Formula: H2O

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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: 2.74 Å3/Da / Density % sol: 55.05 %
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: 0.954 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: 0.954 Å / Relative weight: 1
ReflectionResolution: 2→51.74 Å / Num. obs: 133791 / % possible obs: 98.1 % / Redundancy: 3.7 % / Net I/σ(I): 8.7
Reflection shellResolution: 2→2.07 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 1.2 / % possible all: 97

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
Aimlessdata scaling
PHASERphasing
PDB_EXTRACT3.15data extraction
iMOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4L4T

4l4t


Resolution: 2→51.74 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 23.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2201 6637 4.96 %
Rwork0.1777 127122 -
obs0.1798 133759 97.81 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 132.71 Å2 / Biso mean: 39.9361 Å2 / Biso min: 12.84 Å2
Refinement stepCycle: final / Resolution: 2→51.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12761 0 106 1291 14158
Biso mean--45.36 42.82 -
Num. residues----1611
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00713296
X-RAY DIFFRACTIONf_angle_d1.08618068
X-RAY DIFFRACTIONf_chiral_restr0.0461920
X-RAY DIFFRACTIONf_plane_restr0.0042379
X-RAY DIFFRACTIONf_dihedral_angle_d13.7854761
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 (%)
2-2.02270.33882140.29734182439697
2.0227-2.04650.35812200.28254236445697
2.0465-2.07150.31942250.27524052427797
2.0715-2.09770.27291780.25134252443097
2.0977-2.12530.25351990.23234215441497
2.1253-2.15440.29732240.24044140436497
2.1544-2.18520.30181930.23024240443397
2.1852-2.21780.28352330.22494142437597
2.2178-2.25250.28732500.22844240449098
2.2525-2.28940.27832350.2184097433297
2.2894-2.32890.24272160.21124247446398
2.3289-2.37120.26782300.20774207443798
2.3712-2.41690.26032270.19914206443398
2.4169-2.46620.24832250.1994224444998
2.4662-2.51980.23972280.19814194442298
2.5198-2.57840.25612130.19114276448998
2.5784-2.64290.23792320.19154151438398
2.6429-2.71440.24082240.19274292451698
2.7144-2.79420.22562390.19384212445198
2.7942-2.88440.24432320.18694270450298
2.8844-2.98750.22782360.17954205444198
2.9875-3.10710.20922140.17564263447798
3.1071-3.24850.21362040.17454296450098
3.2485-3.41970.20822210.16654274449598
3.4197-3.63390.19092140.15294286450098
3.6339-3.91440.19412210.14924291451299
3.9144-4.30820.17372340.14024290452498
4.3082-4.93110.14552100.12094315452598
4.9311-6.2110.18062040.15384375457999
6.211-51.76040.21022420.17174452469499
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)
11.2526-0.0418-0.02642.8062-0.96561.58130.06460.00680.01590.0298-0.0550.18690.00730.00850.00780.1312-0.01240.02680.1273-0.03490.161177.06162.389297.4714
21.3168-0.3218-0.61860.91750.34431.10780.0387-0.206-0.0101-0.0144-0.0112-0.0027-0.02690.0363-0.02890.2007-0.0631-0.04190.2130.00420.1613177.614663.5087311.1486
32.71540.55250.02033.52480.28792.44170.0578-0.4131-0.13950.2141-0.1198-0.03670.1671-0.01620.06640.21610.00730.03650.2262-0.00820.2134163.089672.8006326.1739
422-0.1019222-2.6981-0.61164.68293.45160.377-1.2781-1.82981.10852.34440.24210.18230.47450.9783-0.18741.1237153.52978.9011338.938
51.7524-1.53560.61562.2121-1.57431.47980.04370.107-0.16450.0552-0.35340.0093-0.0111-0.24480.24810.188-0.0157-0.01840.2737-0.03790.325157.591560.3835308.9888
62.6376-0.35671.64561.3948-1.00071.4714-0.2153-0.31421.34330.4672-0.20030.3848-1.1457-0.85940.27470.51240.1379-0.06280.4359-0.17810.6982148.962181.8096313.3178
73.1127-1.6416-1.0256.30781.98592.69360.00750.08910.3055-0.5224-0.10430.432-0.4063-0.2540.09350.2437-0.0035-0.02870.2221-0.0270.3148156.026170.3452307.0697
88.8966-6.1782-1.6427.7291.63852.60530.23060.6068-0.5117-0.667-0.46270.4793-0.2219-0.59690.21070.2297-0.0504-0.03660.3409-0.07330.2559154.666662.2641299.5921
95.72340.8886-4.28886.71421.01313.6547-0.22780.76330.3682-1.1229-0.25270.81860.2893-1.33870.40060.5230.0847-0.20180.6405-0.05390.5164143.026269.9526298.3283
102.0687-1.93482.06177.1691-1.43433.92950.07091.35040.6905-1.260.18970.4692-0.9142-0.4373-0.1030.77570.0686-0.05660.69050.08440.5081153.748374.3055296.1311
113.2514-2.82691.97393.1302-1.66381.27080.0310.04940.1717-0.3822-0.0614-0.20290.2339-0.1517-0.00730.2859-0.03260.05460.2373-0.06360.2389168.740462.0037303.8762
128.284-4.31820.08294.96480.41642.9853-0.01550.68750.7021-0.3871-0.28820.0684-0.4076-0.4290.29820.30330.0207-0.04940.2928-0.00420.2834156.451671.9925303.6044
137.30450.3271-1.92874.9941-1.19467.27980.17620.1706-0.13020.4509-0.0910.48530.2262-1.0481-0.12540.39440.1087-0.01750.5197-0.10670.9959139.037775.5335309.2533
142.9424-2.4744-0.37395.9667-0.70981.74950.12920.303-0.2351-0.6705-0.36780.82990.1128-0.64330.27150.2643-0.0207-0.06510.4267-0.150.3612150.347458.6947302.0728
156.83680.97591.07852.49143.1026.7581-0.19-0.01520.71570.4542-0.60231.0455-0.0047-0.64140.64390.2626-0.0460.03570.4375-0.10440.4111146.282867.7252311.7725
161.54540.20130.09072.2963-0.45361.46690.07-0.3880.1760.2559-0.0230.14650.0406-0.1021-0.04920.2230.0402-0.0070.4943-0.0490.2735133.82443.8597327.063
171.6580.07550.07862.3761-0.4250.71760.0827-0.02120.1495-0.145-0.0315-0.17890.08150.0343-0.04690.19720.036-0.01950.3531-0.03840.2243143.77243.9851316.2365
182.1277-0.27711.25932.4951-1.44325.1168-0.09990.15160.441-0.1641-0.12340.0744-0.51610.21840.21330.27-0.0559-0.11340.33430.04180.4084115.472545.184296.2173
192.000122.00021.99991.99991.9999-1.1444-1.2585-5.1437-0.50691.3883-19.6242.7490.749-0.28580.82450.1584-0.26441.05570.01941.3237105.615745.9209282.819
203.35590.7324-1.79550.3582-0.59591.1279-0.0696-0.45430.6299-0.0157-0.01990.3404-0.2609-0.00280.09370.26710.0435-0.09610.3613-0.01920.6727120.65957.8391312.1238
213.494-2.3551.10011.8273-1.03210.7136-0.60030.5141-0.2822-0.4979-0.16820.6552-0.2566-1.06480.18090.37620.0122-0.30610.7312-0.17480.9483101.072345.8784309.3696
220.441-0.73540.15351.2094-0.12681.88920.1684-0.40190.14590.0601-0.0670.42130.1425-0.1527-0.10510.19650.0459-0.04210.4616-0.12330.554113.384651.2384314.7365
234.0509-0.2619-0.35030.1961-0.46191.578-0.3793-1.12720.92250.2344-0.08171.1074-0.7281-0.39640.2130.31210.13640.01020.5746-0.30711.0439117.381559.0326321.4141
240.64070.54150.81411.41010.81691.6120.0756-0.31330.54230.28210.32910.0045-0.4181-0.3195-0.12460.00530.3981-0.27091.1446-0.64061.6232103.444460.5529322.1729
252.5423.0703-2.17253.87-3.19563.85520.4329-1.35190.66211.48870.46220.735-0.6432-0.4141-0.85410.5706-0.01580.16341.087-0.18640.7271109.851451.0634325.5725
262.92522.1543-3.12622.7926-1.89873.53350.0995-0.17630.03430.0283-0.06450.52080.1854-0.4090.03490.2656-0.0255-0.01440.5105-0.07880.3851128.634649.7894317.2107
275.4234-1.3784-0.65790.7415-0.351.64680.0437-0.89050.15160.1045-0.02410.65740.2003-0.5726-0.08690.23840.00010.01260.5913-0.12060.5868112.736149.9562318.4033
281.66610.3035-1.74788.4862.89353.07220.1491-0.1190.4148-0.5890.27130.0089-0.533-0.4391-0.31260.51340.1612-0.17041.0873-0.23941.379396.541956.9456312.138
293.79370.4273-1.71272.2719-1.1811.24520.2358-0.22330.30280.1173-0.0610.85070.09090.1014-0.19870.38540.1002-0.00550.562-0.26520.9525110.761960.7141317.9557
301.46481.1365-0.97850.9491-0.36462.866-0.21650.04280.66630.07250.30090.9089-0.7931-0.8589-0.10380.43570.2084-0.11970.5643-0.34361.3852121.091767.5492318.458
313.59621.429-1.90748.6499-1.04711.024-0.30730.57330.7213-0.93870.07010.37980.02420.10080.12850.63390.1812-0.36630.5544-0.08280.8738107.913459.5947309.2803
322.89020.2728-0.58890.88080.36191.75960.0131-0.0586-0.12020.0743-0.0111-0.09630.09970.31190.01430.16010.005-0.01240.16120.03120.1739212.367862.5231293.2637
334.46550.00840.40363.7173-0.13245.06960.00320.04070.5423-0.26710.0593-0.4065-0.15250.7349-0.06680.24180.01750.06650.34940.00690.4636237.133563.5466272.3131
341.78620.0461-0.80351.0392-0.43753.1036-0.01320.1572-0.0316-0.1472-0.0563-0.01180.1566-0.20930.06870.1936-0.0045-0.00670.1271-0.01820.1869196.072962.2711275.6006
355.8258-1.2785-3.23981.42521.7282.76080.21550.38710.4913-0.1955-0.0513-0.258-0.5856-0.0434-0.14990.4257-0.0220.05390.22120.03320.3217209.983467.8556259.5251
361.630.12350.93141.848-0.62283.28410.0182-0.0094-0.14670.02830.0575-0.20420.42490.3531-0.08230.33410.06540.08340.2023-0.01370.3139228.682855.4346266.4636
374.0024-1.31691.16454.567-0.64923.8216-0.09710.4748-0.2045-0.58760.10470.28230.273-0.0382-0.08580.3658-0.0610.04630.2103-0.03960.2654216.815257.3251254.3896
382.8332-1.80430.68512.1428-0.86961.4215-0.0001-0.08740.1308-0.0751-0.0168-0.05580.0354-0.05080.01820.22920.032-0.02670.2634-0.05830.214161.985124.5182327.3161
392.381-1.11020.62871.382-0.32030.75750.04590.234-0.11120.2135-0.0378-0.10520.07280.14710.00590.29610.001-0.01460.2277-0.02510.1875175.784116.3452344.4406
405.67282.0905-0.89418.5487-4.20772.54060.04910.51630.1072-0.4024-0.33260.56540.6186-0.74670.34360.4667-0.0017-0.02060.5389-0.17440.3995178.13726.2443342.2957
413.8203-0.0047-1.16562.08651.22623.5238-0.04420.1509-0.43020.3798-0.0436-0.01190.6187-0.07690.07910.4420.0131-0.00440.2931-0.05640.2633183.17119.0414349.8634
421.5209-0.51140.50771.6398-1.28742.2658-0.0571-0.46990.08090.36990.0561-0.04-0.2526-0.2931-0.0060.34540.0817-0.06390.623-0.10720.2434150.348633.9343345.984
434.5348-1.21352.66012.2158-1.48223.86570.1730.3385-0.3186-0.36730.15550.31150.5274-0.7838-0.29910.3713-0.0307-0.04420.5299-0.0310.2843157.564520.5205362.1017
444.2780.5548-1.54262.13940.92233.54160.1920.4779-0.01960.1533-0.12040.1303-0.1422-0.4021-0.06590.34550.0622-0.02010.2989-0.00940.1753179.03219.7775355.1795
455.94910.1994-3.71430.6555-0.15443.13050.40920.38340.1674-0.0526-0.1690.0024-0.4313-0.3112-0.20250.4040.0645-0.02050.3492-0.09890.2779173.679326.1144365.6655
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 114 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 115 through 203 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 204 through 269 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 301 through 301 )A0
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 11 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 12 through 19 )B0
7X-RAY DIFFRACTION7chain 'B' and (resid 20 through 30 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 31 through 41 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 42 through 46 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 47 through 51 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 52 through 61 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 62 through 71 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 72 through 77 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 78 through 90 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 91 through 99 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 84 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 85 through 171 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 172 through 269 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 301 through 301 )C0
20X-RAY DIFFRACTION20chain 'D' and (resid 1 through 11 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 12 through 19 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 20 through 30 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 31 through 41 )D0
24X-RAY DIFFRACTION24chain 'D' and (resid 42 through 46 )D0
25X-RAY DIFFRACTION25chain 'D' and (resid 47 through 51 )D0
26X-RAY DIFFRACTION26chain 'D' and (resid 52 through 61 )D0
27X-RAY DIFFRACTION27chain 'D' and (resid 62 through 71 )D0
28X-RAY DIFFRACTION28chain 'D' and (resid 72 through 77 )D0
29X-RAY DIFFRACTION29chain 'D' and (resid 78 through 83 )D0
30X-RAY DIFFRACTION30chain 'D' and (resid 84 through 90 )D0
31X-RAY DIFFRACTION31chain 'D' and (resid 91 through 98 )D0
32X-RAY DIFFRACTION32chain 'G' and (resid 1 through 116 )G0
33X-RAY DIFFRACTION33chain 'G' and (resid 117 through 198 )G0
34X-RAY DIFFRACTION34chain 'H' and (resid 3 through 108 )H0
35X-RAY DIFFRACTION35chain 'H' and (resid 109 through 123 )H0
36X-RAY DIFFRACTION36chain 'H' and (resid 124 through 214 )H0
37X-RAY DIFFRACTION37chain 'H' and (resid 215 through 243 )H0
38X-RAY DIFFRACTION38chain 'E' and (resid 1 through 91 )E0
39X-RAY DIFFRACTION39chain 'E' and (resid 92 through 137 )E0
40X-RAY DIFFRACTION40chain 'E' and (resid 138 through 147 )E0
41X-RAY DIFFRACTION41chain 'E' and (resid 148 through 200 )E0
42X-RAY DIFFRACTION42chain 'F' and (resid 1 through 108 )F0
43X-RAY DIFFRACTION43chain 'F' and (resid 109 through 123 )F0
44X-RAY DIFFRACTION44chain 'F' and (resid 124 through 201 )F0
45X-RAY DIFFRACTION45chain 'F' and (resid 202 through 243 )F0

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