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- PDB-6rp9: Crystal structure of the T-cell receptor NYE_S3 bound to HLA A2*0... -

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Basic information

Entry
Database: PDB / ID: 6rp9
TitleCrystal structure of the T-cell receptor NYE_S3 bound to HLA A2*01-SLLMWITQV
Components
  • Beta-2-microglobulinBeta-2 microglobulin
  • Cancer/testis antigen 1
  • HLA class I histocompatibility antigen, A-2 alpha chain
  • T-cell receptor alpha chain
  • T-cell receptor beta chain
KeywordsIMMUNE SYSTEM / T-cell receptor / peptide-Human leukocyte antigen complex / NY-ESO-1 / cancer testis antigen
Function / homology
Function and homology information


tRNA threonylcarbamoyladenosine metabolic process / T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / positive regulation of memory T cell activation / TAP complex binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation ...tRNA threonylcarbamoyladenosine metabolic process / T cell mediated cytotoxicity directed against tumor cell target / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / positive regulation of memory T cell activation / TAP complex binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / CD8 receptor binding / endoplasmic reticulum exit site / beta-2-microglobulin binding / TAP binding / protection from natural killer cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / detection of bacterium / 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 / lumenal side of endoplasmic reticulum membrane / 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 / peptide antigen assembly with MHC class I protein complex / 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 / MHC class II protein complex / positive regulation of receptor-mediated endocytosis / cellular response to nicotine / recycling endosome membrane / phagocytic vesicle membrane / specific granule lumen / 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 / Interferon alpha/beta signaling / positive regulation of type II interferon production / sensory perception of smell / negative regulation of neuron projection development / E3 ubiquitin ligases ubiquitinate target proteins / 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 / antibacterial humoral response / iron ion transport / T cell receptor signaling pathway / protein refolding / early endosome membrane / protein homotetramerization / intracellular iron ion homeostasis / 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 / signaling receptor binding / focal adhesion / innate immune response / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / Golgi apparatus / cell surface
Similarity search - Function
CTAG/Pcc1 family / Transcription factor Pcc1 / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / 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 ...CTAG/Pcc1 family / Transcription factor Pcc1 / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / 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
HLA class I histocompatibility antigen, A alpha chain / HLA class I histocompatibility antigen, A alpha chain / Beta-2-microglobulin / Cancer/testis antigen 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.12 Å
AuthorsColes, C.H. / Mulvaney, R. / Malla, S. / Lloyd, A. / Smith, K. / Chester, F. / Knox, A. / Stacey, A.R. / Dukes, J. / Baston, E. ...Coles, C.H. / Mulvaney, R. / Malla, S. / Lloyd, A. / Smith, K. / Chester, F. / Knox, A. / Stacey, A.R. / Dukes, J. / Baston, E. / Griffin, S. / Vuidepot, A. / Jakobsen, B.K. / Harper, S.
CitationJournal: J Immunol. / Year: 2020
Title: TCRs with Distinct Specificity Profiles Use Different Binding Modes to Engage an Identical Peptide-HLA Complex.
Authors: Coles, C.H. / Mulvaney, R.M. / Malla, S. / Walker, A. / Smith, K.J. / Lloyd, A. / Lowe, K.L. / McCully, M.L. / Martinez Hague, R. / Aleksic, M. / Harper, J. / Paston, S.J. / Donnellan, Z. / ...Authors: Coles, C.H. / Mulvaney, R.M. / Malla, S. / Walker, A. / Smith, K.J. / Lloyd, A. / Lowe, K.L. / McCully, M.L. / Martinez Hague, R. / Aleksic, M. / Harper, J. / Paston, S.J. / Donnellan, Z. / Chester, F. / Wiederhold, K. / Robinson, R.A. / Knox, A. / Stacey, A.R. / Dukes, J. / Baston, E. / Griffin, S. / Jakobsen, B.K. / Vuidepot, A. / Harper, S.
History
DepositionMay 14, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 15, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 11, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Apr 8, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 24, 2024Group: 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 / refine
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine.pdbx_diffrn_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: Cancer/testis antigen 1
D: T-cell receptor alpha chain
E: T-cell receptor beta chain
F: HLA class I histocompatibility antigen, A-2 alpha chain
G: Beta-2-microglobulin
H: Cancer/testis antigen 1
I: T-cell receptor alpha chain
J: T-cell receptor beta chain
K: T-cell receptor alpha chain
L: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)241,50112
Polymers241,50112
Non-polymers00
Water0
1
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: Cancer/testis antigen 1
D: T-cell receptor alpha chain
E: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)95,5185
Polymers95,5185
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: HLA class I histocompatibility antigen, A-2 alpha chain
G: Beta-2-microglobulin
H: Cancer/testis antigen 1
I: T-cell receptor alpha chain
J: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)95,5185
Polymers95,5185
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
K: T-cell receptor alpha chain
L: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)50,4662
Polymers50,4662
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)106.570, 85.610, 171.920
Angle α, β, γ (deg.)90.00, 91.78, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21F
12B
22G
13D
23I
14D
24K
15E
25J
16E
26L
17I
27K
18J
28L
19J
29L
110E
210L
111I
211K
112D
212I
113D
213K
114E
214J

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 275
2114F1 - 275
1124B0 - 99
2124G0 - 99
1134D3 - 107
2134I3 - 107
1144D7 - 107
2144K7 - 107
1154E1 - 64
2154J1 - 64
1164E2 - 64
2164L2 - 64
1174I7 - 107
2174K7 - 107
1184J2 - 64
2184L2 - 64
1194J72 - 243
2194L72 - 243
11104E72 - 243
21104L72 - 243
11114I116 - 199
21114K116 - 199
11124D116 - 198
21124I116 - 198
11134D116 - 199
21134K116 - 199
11144E72 - 244
21144J72 - 244

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.735114, -0.032576, -0.677161), (-0.013889, 0.999359, -0.032998), (0.677801, -0.014852, -0.735095)50.02382, -4.26145, 85.59537
3given(1), (1), (1)
4given(-0.733984, -0.027087, -0.678626), (-0.005665, 0.999414, -0.033764), (0.679143, -0.020938, -0.733707)50.07603, -4.31286, 85.45335
5given(1), (1), (1)
6given(-0.73471, 0.056708, -0.676007), (0.020196, 0.997887, 0.061759), (0.67808, 0.031722, -0.734303)48.8544, -3.78238, 85.10164
7given(1), (1), (1)
8given(-0.547093, -0.273854, -0.791008), (-0.293396, -0.822288, 0.487607), (-0.78397, 0.498845, 0.36952)124.72198, 31.80466, -1.35619
9given(1), (1), (1)
10given(-0.734919, 0.047543, -0.676487), (0.017259, 0.998528, 0.051426), (0.677936, 0.026119, -0.734657)49.07241, -3.868, 85.18219
11given(1), (1), (1)
12given(-0.635231, -0.214844, -0.741838), (-0.30472, -0.812885, 0.49635), (-0.709667, 0.54135, 0.450902)115.17016, 30.41178, -6.18807
13given(1), (1), (1)
14given(-0.135136, 0.523322, 0.841352), (-0.349182, -0.819817, 0.453842), (0.92726, -0.232454, 0.293522)-113.643, 37.00259, 14.42074
15given(1), (1), (1)
16given(-0.019482, 0.510732, 0.859519), (-0.352954, -0.807845, 0.472027), (0.935438, -0.294175, 0.196003)-109.92369, 34.99571, 24.17966
17given(1), (1), (1)
18given(-0.031233, 0.504808, 0.862667), (-0.315026, -0.82407, 0.470816), (0.948569, -0.257057, 0.184766)-109.94206, 36.80414, 22.68023
19given(1), (1), (1)
20given(-0.638274, -0.230168, -0.734595), (-0.261097, -0.832965, 0.487851), (-0.724179, 0.503183, 0.471563)115.71024, 32.96675, -5.06232
21given(1), (1), (1)
22given(-0.062031, 0.505789, 0.860424), (-0.300223, -0.831614, 0.46721), (0.95185, -0.229338, 0.203436)-111.33941, 38.0867, 20.77706
23given(1), (1), (1)
24given(-0.73119, 0.044299, -0.680734), (0.01063, 0.998508, 0.053561), (0.682091, 0.031927, -0.73057)49.27967, -4.10373, 85.34093
25given(1), (1), (1)
26given(-0.615625, -0.250692, -0.7471), (-0.250283, -0.836764, 0.487016), (-0.747238, 0.486806, 0.452389)118.25117, 33.78144, -4.55277
27given(1), (1), (1)
28given(-0.729908, 0.044849, -0.682072), (0.008422, 0.99836, 0.056633), (0.683493, 0.035593, -0.729088)49.27406, -4.12585, 85.30721

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Components

#1: Protein HLA class I histocompatibility antigen, A-2 alpha chain / MHC class I antigen A*2


Mass: 32082.512 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: Escherichia coli (E. coli) / References: UniProt: P01892, UniProt: P04439*PLUS
#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 / Production host: Escherichia coli (E. coli) / References: UniProt: P61769
#3: Protein/peptide Cancer/testis antigen 1 / Autoimmunogenic cancer/testis antigen NY-ESO-1 / Cancer/testis antigen 6.1 / CT6.1 / L antigen ...Autoimmunogenic cancer/testis antigen NY-ESO-1 / Cancer/testis antigen 6.1 / CT6.1 / L antigen family member 2 / LAGE-2


Mass: 1090.335 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P78358
#4: Protein T-cell receptor alpha chain


Mass: 22844.078 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#5: Protein T-cell receptor beta chain


Mass: 27621.572 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)

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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: 3.25 Å3/Da / Density % sol: 62.11 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.2 M ammonium sulphate, 15 % PEG8k, 0.1 M Tris pH7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.91587 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 25, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91587 Å / Relative weight: 1
ReflectionResolution: 3.12→85.61 Å / Num. obs: 52792 / % possible obs: 100 % / Redundancy: 6.76 % / CC1/2: 0.999 / Rmerge(I) obs: 0.117 / Rpim(I) all: 0.047 / Net I/σ(I): 10.99
Reflection shellResolution: 3.12→3.2 Å / Redundancy: 3.97 % / Rmerge(I) obs: 0.999 / Mean I/σ(I) obs: 1.25 / Num. unique obs: 2717 / CC1/2: 0.627 / Rpim(I) all: 0.567 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
xia20.5.436-g557f8872-dials-1.7data reduction
xia20.5.436-g557f8872-dials-1.7data scaling
PHASERVersion 2.7.17phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5e00 (chains A and B), 3QDJ (chain D) and 5D2N (chain E)

5e00

3qdj

5d2n


Resolution: 3.12→68.01 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.927 / SU B: 62.726 / SU ML: 0.441 / Cross valid method: THROUGHOUT / ESU R Free: 0.446 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25046 2717 4.9 %RANDOM
Rwork0.22349 ---
obs0.22481 52792 99.94 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 117.682 Å2
Baniso -1Baniso -2Baniso -3
1--3.55 Å2-0 Å2-2.27 Å2
2---1.37 Å2-0 Å2
3---5.05 Å2
Refinement stepCycle: LAST / Resolution: 3.12→68.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16633 0 0 0 16633
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01917088
X-RAY DIFFRACTIONr_bond_other_d0.0010.0214837
X-RAY DIFFRACTIONr_angle_refined_deg0.9291.92923203
X-RAY DIFFRACTIONr_angle_other_deg0.796334509
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.95352068
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.05723.763877
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.213152718
X-RAY DIFFRACTIONr_dihedral_angle_4_deg9.83915128
X-RAY DIFFRACTIONr_chiral_restr0.060.22423
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02119251
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023737
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6296.4288309
X-RAY DIFFRACTIONr_mcbond_other0.6296.4288308
X-RAY DIFFRACTIONr_mcangle_it1.1669.64110364
X-RAY DIFFRACTIONr_mcangle_other1.1669.64110365
X-RAY DIFFRACTIONr_scbond_it0.4186.4328779
X-RAY DIFFRACTIONr_scbond_other0.4186.4328780
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other0.7929.63112840
X-RAY DIFFRACTIONr_long_range_B_refined1.85971.0517663
X-RAY DIFFRACTIONr_long_range_B_other1.85971.05117664
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Auth asym-ID: A / Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDNumberTypeRms dev position (Å)Weight position
114240medium positional0.180.5
221600medium positional0.130.5
331309medium positional0.10.5
441249medium positional0.240.5
55807medium positional0.120.5
66798medium positional0.290.5
771249medium positional0.240.5
88798medium positional0.290.5
992566medium positional0.20.5
10102566medium positional0.230.5
11111141medium positional0.230.5
12121219medium positional0.190.5
13131141medium positional0.260.5
14142582medium positional0.160.5
114240medium thermal2.822
221600medium thermal3.262
331309medium thermal2.42
441249medium thermal3.042
55807medium thermal3.62
66798medium thermal2.932
771249medium thermal3.062
88798medium thermal1.622
992566medium thermal2.82
10102566medium thermal3.142
11111141medium thermal2.372
12121219medium thermal3.132
13131141medium thermal4.642
14142582medium thermal2.032
LS refinement shellResolution: 3.12→3.201 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.415 193 -
Rwork0.369 3877 -
obs--99.83 %
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)
16.33131.22770.61931.9734-0.52192.93350.2076-0.1640.58940.0656-0.02670.5545-0.4076-0.2849-0.18090.08110.01020.02960.1379-0.02560.42835.13833.048271.5446
25.65112.42571.29714.29140.21566.01260.03820.4859-0.4404-0.4332-0.04260.25380.9649-0.36010.00440.2155-0.0481-0.09160.1178-0.04480.453730.7075-15.762370.3928
36.2096-0.09017.58485.46691.766723.240.4853-0.02240.2178-0.0296-0.4117-0.5303-0.6625-0.498-0.07360.2227-0.09780.02280.3048-0.02180.380154.53558.330973.6034
47.40330.2268-1.91962.2384-0.2892.38820.0840.3140.4789-0.24070.1042-0.7635-0.42140.3777-0.18820.2967-0.07810.05240.209-0.00790.617988.210732.202469.9875
55.21571.1644-0.46342.41230.62581.62270.1169-0.18340.3307-0.13760.0517-0.4773-0.0740.4019-0.16860.0364-0.0242-0.04230.1484-0.00260.574492.559713.285268.0313
63.3668-1.39470.83812.025-0.72951.6726-0.3256-0.7520.47320.44820.2701-0.4706-0.333-0.13860.05550.66370.1428-0.28931.1126-0.02030.65631.32187.997620.1681
74.0164-1.24540.44243.2117-0.43363.0343-0.486-1.0953-0.58170.74130.55090.37190.4334-0.2915-0.06490.79940.1444-0.24451.11550.25760.59034.0579-10.601724.5798
84.89292.1756-10.16380.9706-4.53421.2082-0.2686-0.059-0.1426-0.09010.0174-0.06960.5085-0.15910.25120.590.1204-0.17980.8520.06980.4516-11.694912.63835.3299
94.8534-0.99512.46372.0181-0.11252.0826-0.0773-0.37880.59860.0027-0.02490.4038-0.3375-0.25530.10230.74070.0003-0.18580.7763-0.00310.7603-38.561337.5194-13.427
103.3194-0.631.75431.3997-0.59492.6171-0.094-0.39990.03730.02770.00810.0855-0.029-0.14030.08590.5097-0.022-0.23430.6697-0.02080.4315-43.25318.7295-15.9459
113.37780.89582.38832.47610.71295.8646-0.0140.3147-0.2341-0.26050.22170.07310.5013-0.2221-0.20770.4698-0.0062-0.09420.2110.06480.6753-36.867645.159556.4771
123.27371.70021.74822.77590.47262.73090.11230.485-0.1868-0.57210.2452-0.250.25950.0218-0.35750.34010.0351-0.1010.3917-0.02080.5087-33.011958.450941.8696
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 275
2X-RAY DIFFRACTION2B0 - 99
3X-RAY DIFFRACTION3C1 - 9
4X-RAY DIFFRACTION4D4 - 217
5X-RAY DIFFRACTION5E1 - 256
6X-RAY DIFFRACTION6F1 - 275
7X-RAY DIFFRACTION7G0 - 99
8X-RAY DIFFRACTION8H1 - 9
9X-RAY DIFFRACTION9I4 - 218
10X-RAY DIFFRACTION10J1 - 256
11X-RAY DIFFRACTION11K8 - 218
12X-RAY DIFFRACTION12L2 - 256

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