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- PDB-2f54: Directed evolution of human T cell receptor CDR2 residues by phag... -

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Basic information

Entry
Database: PDB / ID: 2f54
TitleDirected evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity
Components
  • (T-cell receptor ...) x 2
  • Beta-2-microglobulin
  • Cancer/testis antigen 1B
  • HLA class I histocompatibility antigen
KeywordsIMMUNE SYSTEM / T-cell receptor / CDR2 / Phage display / wild type sequence / high affinity / NY-ESO-1
Function / homology
Function and homology information


tRNA threonylcarbamoyladenosine metabolic process / alpha-beta T cell receptor complex / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / 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 ...tRNA threonylcarbamoyladenosine metabolic process / alpha-beta T cell receptor complex / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / 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 / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / antigen processing and presentation of exogenous peptide antigen via MHC class I / beta-2-microglobulin binding / endoplasmic reticulum exit site / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / TAP binding / alpha-beta T cell activation / protection from natural killer cell mediated cytotoxicity / Generation of second messenger molecules / Co-inhibition by PD-1 / 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 receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / negative regulation of receptor binding / DAP12 interactions / cellular response to iron ion / lumenal side of endoplasmic reticulum membrane / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / response to bacterium / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / 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 / MHC class I peptide loading complex / response to molecule of bacterial origin / 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 / MHC class I protein complex / positive regulation of immune response / peptide antigen binding / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / positive regulation of receptor-mediated endocytosis / multicellular organismal-level iron ion homeostasis / positive regulation of T cell activation / cellular response to nicotine / positive regulation of type II interferon production / specific granule lumen / recycling endosome membrane / phagocytic vesicle membrane / positive regulation of cellular senescence / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / negative regulation of epithelial cell proliferation / Interferon gamma signaling / Interferon alpha/beta signaling / MHC class II protein complex binding / positive regulation of protein binding / Modulation by Mtb of host immune system / antibacterial humoral response / late endosome membrane / sensory perception of smell / tertiary granule lumen / DAP12 signaling / Downstream TCR signaling / E3 ubiquitin ligases ubiquitinate target proteins / T cell receptor signaling pathway / negative regulation of neuron projection development / iron ion transport / T cell differentiation in thymus / ER-Phagosome pathway / protein refolding / early endosome membrane / protein homotetramerization / adaptive immune response / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / defense response to Gram-positive bacterium / immune response / Amyloid fiber formation / endoplasmic reticulum lumen / Golgi membrane / external side of plasma membrane / signaling receptor binding
Similarity search - Function
CTAG/Pcc1 family / Transcription factor Pcc1 / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / : / 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 ...CTAG/Pcc1 family / Transcription factor Pcc1 / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / : / 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 / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
T cell receptor alpha chain constant / T cell receptor beta constant 1 / 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: 2.7 Å
AuthorsRizkallah, P.J. / Jakobsen, B.K. / Dunn, S.M. / Sami, M.
CitationJournal: Protein Sci. / Year: 2006
Title: Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity.
Authors: Dunn, S.M. / Rizkallah, P.J. / Baston, E. / Mahon, T. / Cameron, B. / Moysey, R. / Gao, F. / Sami, M. / Boulter, J. / Li, Y. / Jakobsen, B.K.
History
DepositionNov 25, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 25, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Oct 20, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Aug 23, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id
Revision 1.5Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 999SEQUENCE Currently there is no aminoacid sequence database reference available for T cell receptor ...SEQUENCE Currently there is no aminoacid sequence database reference available for T cell receptor alpha and beta chains (entities 4 and 5)

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


Theoretical massNumber of molelcules
Total (without water)188,11710
Polymers188,11710
Non-polymers00
Water54030
1
A: HLA class I histocompatibility antigen
B: Beta-2-microglobulin
C: Cancer/testis antigen 1B
D: T-cell receptor alpha chain
E: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)94,0595
Polymers94,0595
Non-polymers00
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10550 Å2
ΔGint-55 kcal/mol
Surface area37850 Å2
MethodPISA
2
F: HLA class I histocompatibility antigen
G: Beta-2-microglobulin
H: Cancer/testis antigen 1B
K: T-cell receptor alpha chain
L: T-cell receptor beta chain


Theoretical massNumber of molelcules
Total (without water)94,0595
Polymers94,0595
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10590 Å2
ΔGint-54 kcal/mol
Surface area38030 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.020, 53.592, 152.831
Angle α, β, γ (deg.)90.00, 96.04, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21F
12B
22G
13C
23H
14D
24K
15E
25L

NCS domain segments:

Component-ID: 1 / Refine code: 4

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYTRPTRPAA1 - 2741 - 274
21GLYGLYTRPTRPFF1 - 2741 - 274
12METMETMETMETBB0 - 991 - 100
22METMETMETMETGG0 - 991 - 100
13SERSERCYSCYSCC1 - 91 - 9
23SERSERCYSCYSHH1 - 91 - 9
14GLNGLNGLUGLUDD1 - 2052 - 206
24GLNGLNGLUGLUKI1 - 2052 - 206
15GLYGLYASPASPEE1 - 2411 - 241
25GLYGLYASPASPLJ1 - 2411 - 241

NCS ensembles :
ID
1
2
3
4
5

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Components

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Protein , 2 types, 4 molecules AFBG

#1: Protein HLA class I histocompatibility antigen / MHC class I antigen A*2


Mass: 31725.088 Da / Num. of mol.: 2 / Fragment: alpha 1, alpha 2, alpha 3, residues 25-298
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Plasmid: pEX078 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P01892, UniProt: P04439*PLUS
#2: Protein Beta-2-microglobulin


Mass: 11793.288 Da / Num. of mol.: 2 / Fragment: Beta-2-microglobulin, residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M / Plasmid: pEX050 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P61769

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T-cell receptor ... , 2 types, 4 molecules DKEL

#4: Protein T-cell receptor alpha chain


Mass: 22439.789 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGMT7 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q6PIZ8, UniProt: P01848*PLUS
#5: Protein T-cell receptor beta chain


Mass: 27005.988 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGMT7 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q6NS87, UniProt: P01850*PLUS

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Protein/peptide / Non-polymers , 2 types, 32 molecules CH

#3: Protein/peptide Cancer/testis antigen 1B / L antigen family member 2 / LAGE-2 protein / Autoimmunogenic cancer/testis antigen NY-ESO-1


Mass: 1094.347 Da / Num. of mol.: 2 / Fragment: residues 157-165 / Mutation: Y67C, K91C / Source method: obtained synthetically
Details: This sequence occurs naturally in Homo sapiens (humans)
References: UniProt: P78358
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 30 / 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: 2.6 Å3/Da / Density % sol: 52.64 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 85 mM HEPES, 8.5% iso-propanol, 17% PEG 4000, 15% glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.978 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 28, 2002 / Details: Mirror
RadiationMonochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 2.7→50.66 Å / Num. obs: 53950 / % possible obs: 100 % / Redundancy: 3.5 % / Biso Wilson estimate: 57.2 Å2 / Rmerge(I) obs: 0.134 / Rsym value: 0.134 / Net I/σ(I): 5.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allRsym value% possible all
2.7-2.853.50.5951.278040.595100
2.85-3.023.50.4181.873490.418100
3.02-3.233.50.2742.769690.274100
3.23-3.493.50.1774.164710.177100
3.49-3.823.50.1255.760220.125100
3.82-4.273.50.0957.454200.095100
4.27-4.933.40.0778.648090.077100
4.93-6.043.50.088.340870.08100
6.04-8.543.40.0758.532040.075100
8.54-50.6630.0529.518150.05299.2

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Processing

Software
NameVersionClassificationNB
SCALAdata scaling
REFMACrefinement
PDB_EXTRACT1.701data extraction
MOSFLMdata reduction
CCP4(SCALA)data scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BNR

2bnr


Resolution: 2.7→50.66 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.864 / WRfactor Rfree: 0.256 / WRfactor Rwork: 0.194 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic = TLS / Cross valid method: R-free / ESU R Free: 0.4 / Stereochemistry target values: Engh & Huber / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.286 2740 5.08 %Random
Rwork0.2214 ---
all0.225 ---
obs0.225 53938 99.944 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 16.979 Å2
Baniso -1Baniso -2Baniso -3
1--2.215 Å20 Å20.004 Å2
2--2.597 Å20 Å2
3----0.381 Å2
Refinement stepCycle: LAST / Resolution: 2.7→50.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13229 0 0 30 13259
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.02113589
X-RAY DIFFRACTIONr_bond_other_d0.0020.0211632
X-RAY DIFFRACTIONr_angle_refined_deg1.3371.93318483
X-RAY DIFFRACTIONr_angle_other_deg0.698327129
X-RAY DIFFRACTIONr_dihedral_angle_1_deg2.84751649
X-RAY DIFFRACTIONr_dihedral_angle_2_deg24.99723.9682
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.098152170
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.3611594
X-RAY DIFFRACTIONr_chiral_restr0.1020.21955
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0215321
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022867
X-RAY DIFFRACTIONr_nbd_refined0.2340.33107
X-RAY DIFFRACTIONr_nbd_other0.2120.312778
X-RAY DIFFRACTIONr_nbtor_refined0.1950.56528
X-RAY DIFFRACTIONr_nbtor_other0.0930.58143
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2050.5669
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.150.517
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2490.367
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2480.3154
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3590.511
X-RAY DIFFRACTIONr_mcbond_it1.375210416
X-RAY DIFFRACTIONr_mcbond_other0.26823354
X-RAY DIFFRACTIONr_mcangle_it1.828313374
X-RAY DIFFRACTIONr_mcangle_other0.8311363
X-RAY DIFFRACTIONr_scbond_it2.56346282
X-RAY DIFFRACTIONr_scbond_other1.048410903
X-RAY DIFFRACTIONr_scangle_it3.74765109
X-RAY DIFFRACTIONr_scangle_other1.658615766
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A4196MEDIUM POSITIONAL0.5310.5
1A4196MEDIUM THERMAL0.7942
2B1557MEDIUM POSITIONAL0.3420.5
2B1557MEDIUM THERMAL0.7472
3C149MEDIUM POSITIONAL0.4410.5
3C149MEDIUM THERMAL0.4442
4D2939MEDIUM POSITIONAL0.7760.5
4D2939MEDIUM THERMAL0.6762
5E3577MEDIUM POSITIONAL0.5310.5
5E3577MEDIUM THERMAL0.6942
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.7-2.770.421870.3183719390999.923
2.77-2.8460.3761940.3136953889100
2.846-2.9290.3711950.29435423737100
2.929-3.0190.3091960.27434163612100
3.019-3.1180.331980.26333703568100
3.118-3.2270.3191650.25232323397100
3.227-3.3490.2961810.2543165334799.97
3.349-3.4850.3231700.26929583128100
3.485-3.640.331390.25129383077100
3.64-3.8180.2751200.22128122932100
3.818-4.0240.2841440.21726422786100
4.024-4.2680.2371460.1842493264099.962
4.268-4.5630.2071410.16423352476100
4.563-4.9280.2111100.1572223233599.914
4.928-5.3980.2441100.16120322142100
5.398-6.0340.2631050.19418431948100
6.034-6.9660.358830.2091635171999.942
6.966-8.5270.199740.17814071481100
8.527-12.0420.223560.1511001156100
12.042-158.1140.432260.24364168996.807
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)
13.21980.8085-1.07151.485-0.45882.6976-0.1002-0.2368-0.0443-0.01680.0388-0.03-0.07060.20930.0613-0.04650.01610.08220.06060.0820.05913.74646.77754.699
26.1271-0.7593.18722.77630.8175.4158-0.3550.05690.2324-0.2254-0.18890.4658-0.7158-0.14980.5439-0.0381-0.03780.04150.0164-0.03580.2133-21.17653.99452.4
33.8259-0.4336-2.02732.62970.12872.75210.1631-0.1740.04840.092-0.1453-0.0556-0.20520.0065-0.0178-0.0141-0.06640.06220.0737-0.04690.0434-4.49465.06463.134
48.92769.6475-3.04613.8407-3.86861.13670.4587-0.96490.58320.61210.37280.4171-0.59451.1475-0.83150.0857-0.14830.10550.44460.02720.164921.92543.95554.071
58.6208-1.4601-0.61262.94550.58183.9862-0.0145-0.2827-1.1329-0.22010.4981-0.0690.72730.0209-0.48370.1067-0.0739-0.02550.0518-0.01640.263340.59128.78651.113
65.3894-1.2030.40645.32472.13593.6999-0.1726-0.2192-1.00620.41110.1712-0.37810.94290.73180.0013-0.01850.05920.17630.22360.09940.494276.08425.53655.221
75.0724-1.28673.49742.151-1.64734.0188-0.3127-0.79640.12580.23850.4068-0.1009-0.3256-0.1211-0.0941-0.07010.04380.1030.407-0.06930.046941.91846.04966.023
81.8592-0.7797-0.84442.41450.80014.9658-0.1053-0.5772-0.0094-0.07880.0137-0.142-0.10960.34190.0916-0.162-0.06980.04660.219-0.08550.228772.44842.00958.209
93.7961-0.1646-0.89991.83220.06931.70290.11310.05010.1326-0.08690.07690.0769-0.1642-0.0952-0.190.07760.02480.1759-0.07810.05410.18275.03347.606129.867
108.8047-0.92830.39952.22770.96312.869-0.18580.85120.1508-0.54780.00650.085-0.3462-0.09260.17930.0862-0.04990.10360.00840.02810.2387-29.94656.127129.399
118.1796-0.0898-3.75143.31980.77442.78730.2855-0.56340.58420.003-0.2349-0.3377-0.15480.0702-0.05060.0568-0.02830.1641-0.0211-0.07610.3054-12.56165.814139.683
1218.283-1.6223-5.45830.1440.48431.62960.4846-1.45770.6212-0.1865-0.20960.78510.29420.7413-0.2750.18680.05840.17040.15690.06680.328713.14144.514128.71
134.62690.0089-0.82491.96810.8472.46350.1064-0.0336-0.39910.11010.16810.12520.28610.1837-0.27450.04550.07940.11550.0031-0.02530.164131.95930.085124.074
144.5609-0.65340.11444.05611.37066.0787-0.0997-0.483-0.3920.34530.1021-0.18910.3420.0117-0.0024-0.07540.10970.14180.0277-0.02860.123968.03527.653127.305
155.0735-0.87342.36932.084-0.23483.14310.0574-0.47930.39090.28660.04480.0468-0.10490.1941-0.10220.06080.02350.24510.1203-0.02090.078433.07644.896140.937
163.4846-0.4177-1.18352.78180.15774.21060.0727-0.29760.0150.156-0.2191-0.0179-0.36170.13420.1464-0.02310.05120.05930.051-0.08590.099163.56243.244133.204
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11AA1 - 1801 - 180
22AA185 - 274185 - 274
33BB0 - 991 - 100
44CC1 - 91 - 9
55DD1 - 1102 - 111
66DD115 - 205116 - 206
77EE1 - 1101 - 110
88EE120 - 241120 - 241
99FF1 - 1801 - 180
1010FF185 - 274185 - 274
1111GG0 - 991 - 100
1212HH1 - 91 - 9
1313KI1 - 1102 - 111
1414KI115 - 205116 - 206
1515LJ1 - 1101 - 110
1616LJ120 - 241120 - 241

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