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- PDB-2wbj: TCR complex -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 2wbj
TitleTCR complex
Components
  • (HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, ...) x 2
  • (OB TCR) x 2
KeywordsIMMUNE SYSTEM / TRANSMEMBRANE / IMMUNE RESPONSE / T CELL RECEPTOR / MHC II / MEMBRANE / RECEPTOR / MOLECULAR MIMICRY / MULTIPLE SCLEROSIS / AUTOIMMUNITY / GLYCOPROTEIN / MHC CLASS II
Function / homology
Function and homology information


regulation of interleukin-4 production / regulation of interleukin-10 production / myeloid dendritic cell antigen processing and presentation / antigen processing and presentation of endogenous peptide antigen via MHC class II / autolysosome membrane / regulation of T-helper cell differentiation / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / MHC class II receptor activity / positive regulation of CD4-positive, alpha-beta T cell activation / antigen processing and presentation of peptide or polysaccharide antigen via MHC class II ...regulation of interleukin-4 production / regulation of interleukin-10 production / myeloid dendritic cell antigen processing and presentation / antigen processing and presentation of endogenous peptide antigen via MHC class II / autolysosome membrane / regulation of T-helper cell differentiation / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / MHC class II receptor activity / positive regulation of CD4-positive, alpha-beta T cell activation / antigen processing and presentation of peptide or polysaccharide antigen via MHC class II / positive regulation of T cell mediated immune response to tumor cell / positive regulation of kinase activity / positive regulation of memory T cell differentiation / positive regulation of monocyte differentiation / inflammatory response to antigenic stimulus / CD4 receptor binding / intermediate filament / T-helper 1 type immune response / transport vesicle membrane / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / polysaccharide binding / negative regulation of type II interferon production / humoral immune response / macrophage differentiation / Generation of second messenger molecules / immunological synapse / Co-inhibition by PD-1 / epidermis development / positive regulation of insulin secretion involved in cellular response to glucose stimulus / detection of bacterium / T cell receptor binding / negative regulation of T cell proliferation / MHC class II antigen presentation / trans-Golgi network membrane / lumenal side of endoplasmic reticulum membrane / protein tetramerization / peptide antigen assembly with MHC class II protein complex / negative regulation of inflammatory response to antigenic stimulus / MHC class II protein complex / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / positive regulation of T cell activation / peptide antigen binding / structural constituent of cytoskeleton / positive regulation of T cell mediated cytotoxicity / cognition / positive regulation of protein phosphorylation / Interferon gamma signaling / MHC class II protein complex binding / endocytic vesicle membrane / late endosome membrane / Downstream TCR signaling / T cell receptor signaling pathway / early endosome membrane / adaptive immune response / positive regulation of viral entry into host cell / lysosome / positive regulation of ERK1 and ERK2 cascade / positive regulation of canonical NF-kappaB signal transduction / positive regulation of MAPK cascade / immune response / Golgi membrane / lysosomal membrane / external side of plasma membrane / positive regulation of DNA-templated transcription / cell surface / signal transduction / extracellular space / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / MHC classes I/II-like antigen recognition protein ...Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / 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 / Roll / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
HLA class II histocompatibility antigen, DR alpha chain / HLA class II histocompatibility antigen, DRB1 beta chain
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsHarkiolaki, M. / Holmes, S.L. / Svendsen, P. / Gregersen, J.W. / Jensen, L.T. / McMahon, R. / Friese, M.A. / van Boxel, G. / Etzensperger, R. / Tzartos, J.S. ...Harkiolaki, M. / Holmes, S.L. / Svendsen, P. / Gregersen, J.W. / Jensen, L.T. / McMahon, R. / Friese, M.A. / van Boxel, G. / Etzensperger, R. / Tzartos, J.S. / Kranc, K. / Sainsbury, S. / Harlos, K. / Mellins, E.D. / Palace, J. / Esiri, M.M. / van der Merwe, P.A. / Jones, E.Y. / Fugger, L.
CitationJournal: Immunity / Year: 2009
Title: T Cell-Mediated Autoimmune Disease due to Low-Affinity Crossreactivity to Common Microbial Peptides.
Authors: Harkiolaki, M. / Holmes, S.L. / Svendsen, P. / Gregersen, J.W. / Jensen, L.T. / Mcmahon, R. / Friese, M.A. / Van Boxel, G. / Etzensperger, R. / Tzartos, J.S. / Kranc, K. / Sainsbury, S. / ...Authors: Harkiolaki, M. / Holmes, S.L. / Svendsen, P. / Gregersen, J.W. / Jensen, L.T. / Mcmahon, R. / Friese, M.A. / Van Boxel, G. / Etzensperger, R. / Tzartos, J.S. / Kranc, K. / Sainsbury, S. / Harlos, K. / Mellins, E.D. / Palace, J. / Esiri, M.M. / Van Der Merwe, P.A. / Jones, E.Y. / Fugger, L.
History
DepositionMar 2, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 7, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Aug 22, 2012Group: Database references / Derived calculations
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN
B: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN
C: OB TCR
D: OB TCR
E: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN
F: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN
G: OB TCR
H: OB TCR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)203,97016
Polymers201,8868
Non-polymers2,0848
Water00
1
A: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN
B: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN
C: OB TCR
D: OB TCR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)101,5788
Polymers100,9434
Non-polymers6354
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14130 Å2
ΔGint-90.9 kcal/mol
Surface area38360 Å2
MethodPISA
2
E: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN
F: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN
G: OB TCR
H: OB TCR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,3938
Polymers100,9434
Non-polymers1,4494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14410 Å2
ΔGint-48.1 kcal/mol
Surface area38930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.706, 130.271, 180.220
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21E
12B
22F
13C
23G
14D
24H

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1112A5 - 180
2112E5 - 180
1122B3 - 104
2122F3 - 104
1222B114 - 164
2222F114 - 164
1322B172 - 188
2322F172 - 188
1132C10 - 36
2132G10 - 36
1232C59 - 124
2232G59 - 124
1332C134 - 199
2332G134 - 199
1142D1 - 12
2142H1 - 12
1242D24 - 72
2242H24 - 72
1342D88 - 268
2342H88 - 268

NCS ensembles :
ID
1
2
3
4

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Components

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HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, ... , 2 types, 4 molecules AEBF

#1: Protein HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN / MHC CLASS II ANTIGEN DRA


Mass: 22436.246 Da / Num. of mol.: 2 / Fragment: MHC CLASS II, RESIDUES 26-218
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): S2 CELLS / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: P01903
#2: Protein HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-15 BETA CHAIN / MHC CLASS I ANTIGEN DRB1*15 / DW2.2/DR2.2 / HLA-DR2


Mass: 23205.834 Da / Num. of mol.: 2 / Fragment: MHC CLASS II, RESIDUES 29-227
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): S2 CELLS / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: P01911

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Antibody / Protein / Non-polymers , 3 types, 7 molecules CGDH

#3: Antibody OB TCR


Mass: 24474.988 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: E. COLI ENGA PEPTIDE COVALENTLY BOUND / Source: (gene. exp.) HOMO SAPIENS (human) / Description: PATIENT DERIVED SEQUENCE / Plasmid: PET22 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
#4: Protein OB TCR


Mass: 30826.158 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: E. COLI ENGA PEPTIDE COVALENTLY BOUND / Source: (gene. exp.) HOMO SAPIENS (human) / Description: PATIENT DERIVED SEQUENCE / Plasmid: PET22 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
#7: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4

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Sugars , 2 types, 5 molecules

#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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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: 3.47 Å3/Da / Density % sol: 64.3 % / Description: NONE
Crystal growpH: 6.3
Details: 0.2 M LISO4, 0.8 M K2HPO4, 1.2 M NAH2PO4, 0.1 M CAPS PH 10.5, 8 % 1,1,1,3,3, 3-HEXAFLUORO-2-PROPANOL

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726
DetectorType: MARRESEARCH / Detector: CCD / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 3.15→30 Å / Num. obs: 45361 / % possible obs: 100 % / Observed criterion σ(I): 1 / Redundancy: 16.9 % / Rmerge(I) obs: 0.23 / Net I/σ(I): 10.3
Reflection shellResolution: 3.15→3.26 Å / Redundancy: 16.6 % / Rmerge(I) obs: 1 / Mean I/σ(I) obs: 2.1 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1YMM

1ymm


Resolution: 3→105.41 Å / Cor.coef. Fo:Fc: 0.895 / Cor.coef. Fo:Fc free: 0.864 / SU B: 45.999 / SU ML: 0.408 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.455 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.28778 2659 5.1 %RANDOM
Rwork0.24697 ---
obs0.24909 49485 99.47 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 64.111 Å2
Baniso -1Baniso -2Baniso -3
1--1.07 Å20 Å20 Å2
2---3.29 Å20 Å2
3---4.36 Å2
Refinement stepCycle: LAST / Resolution: 3→105.41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13103 0 132 0 13235
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.02213601
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg11.94218491
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.40751624
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.2923.89671
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.277152176
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8791590
X-RAY DIFFRACTIONr_chiral_restr0.070.22023
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0210446
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1910.25079
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3020.28961
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1150.2320
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1590.254
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1520.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.01938338
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.672413282
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.94445940
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.08865209
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A704tight positional0.020.05
12E704tight positional0.020.05
21B680tight positional0.020.05
22F680tight positional0.020.05
31C636tight positional0.030.05
32G636tight positional0.030.05
41D964tight positional0.030.05
42H964tight positional0.030.05
11A744medium positional0.350.5
12E744medium positional0.350.5
21B719medium positional0.270.5
22F719medium positional0.270.5
31C600medium positional0.40.5
32G600medium positional0.40.5
41D959medium positional0.40.5
42H959medium positional0.40.5
11A704tight thermal0.030.5
12E704tight thermal0.030.5
21B680tight thermal0.030.5
22F680tight thermal0.030.5
31C636tight thermal0.030.5
32G636tight thermal0.030.5
41D964tight thermal0.030.5
42H964tight thermal0.030.5
11A744medium thermal0.352
12E744medium thermal0.352
21B719medium thermal0.342
22F719medium thermal0.342
31C600medium thermal0.322
32G600medium thermal0.322
41D959medium thermal0.332
42H959medium thermal0.332
LS refinement shellResolution: 3→3.078 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.407 184 -
Rwork0.329 3493 -
obs--96.41 %
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)
13.30250.1372-0.0412.84430.2262.78790.0704-0.01250.04430.1216-0.12380.1453-0.0994-0.0450.0533-0.2696-0.0101-0.0602-0.18060.0954-0.220328.372434.287289.6618
212.07982.02352.8052.90410.37263.51380.2911-0.6145-0.03160.4739-0.2486-0.27460.0128-0.0839-0.04250.0473-0.0643-0.0703-0.11450.1322-0.21942.062931.0141113.7133
33.89920.4208-0.35939.4955-6.579810.4636-0.0872-0.2905-0.83340.2263-0.7559-0.54390.65130.7580.8431-0.2917-0.0925-0.0492-0.04740.21260.126857.475314.8849103.3966
44.8342-3.24834.53624.4668-3.810910.56430.1140.39790.1226-0.7467-0.0735-0.14940.14330.3081-0.0406-0.1422-0.0312-0.05-0.1530.0542-0.105128.626745.533759.796
52.86481.0028-0.844310.745-4.27264.3933-0.0819-0.00030.06250.2066-0.1066-0.424-0.29220.03590.1886-0.28590.0365-0.0881-0.11370.0723-0.169735.995962.213873.2093
67.67894.00581.341514.38382.01286.427-0.2690.2660.4115-0.76620.3148-0.08-0.74320.498-0.0458-0.03360.0389-0.024-0.01980.0364-0.295219.655370.55436.4614
77.83133.2145.01463.74732.66267.1432-0.04580.06360.1628-0.2317-0.17540.1622-0.3252-0.12670.2212-0.0420.11150.0437-0.29790.0243-0.191418.131877.612951.7834
83.0056-0.39990.16621.85150.0172.46260.129-0.1084-0.18060.0886-0.18940.0387-0.24060.01640.0604-0.12820.01930.0281-0.17020.0003-0.269123.14460.663711.6742
94.6951-3.7135-1.32678.44843.51385.22440.38130.6095-0.2442-0.8857-0.4973-0.1084-0.0195-0.28870.116-0.02280.01280.0838-0.09730.0388-0.234834.4267-14.8606-22.4295
104.00930.3061-3.33463.2376-1.75318.4529-0.072-0.1311-0.3336-0.2073-0.0697-0.1903-0.16690.50610.1417-0.24170.0273-0.0033-0.282-0.0219-0.081546.4561-4.8186-2.1938
113.0041-2.94620.472911.15250.74971.67750.12690.15980.3035-0.40820.0256-0.4988-0.24070.1774-0.1526-0.10320.00120.0966-0.1013-0.0821-0.189714.174832.857410.9634
125.80771.9437-3.54524.5873-1.9996.00730.2325-0.582-0.06320.5019-0.29320.07750.0494-0.01440.06070.0518-0.0228-0.0477-0.1765-0.0885-0.3005-3.076248.662332.2875
139.4122-2.4705-5.94291.82351.5124.21180.1470.05440.2085-0.2232-0.14790.3907-0.3024-0.16390.0009-0.08950.0247-0.022-0.1362-0.0159-0.1254-3.352518.962414.201
1411.16722.3451.009510.0759-1.15954.03860.02090.01810.58140.6706-0.07571.4877-0.1213-0.1880.0548-0.04760.05740.15580.05060.002-0.0259-20.402545.729629.6471
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A7 - 79
2X-RAY DIFFRACTION1B8 - 92
3X-RAY DIFFRACTION2A84 - 180
4X-RAY DIFFRACTION3B94 - 108
5X-RAY DIFFRACTION3B111 - 165
6X-RAY DIFFRACTION3B171 - 188
7X-RAY DIFFRACTION4C8 - 111
8X-RAY DIFFRACTION5D25 - 140
9X-RAY DIFFRACTION6C114 - 200
10X-RAY DIFFRACTION7D146 - 269
11X-RAY DIFFRACTION8E4 - 80
12X-RAY DIFFRACTION8F5 - 92
13X-RAY DIFFRACTION9F95 - 190
14X-RAY DIFFRACTION10E85 - 180
15X-RAY DIFFRACTION11H23 - 139
16X-RAY DIFFRACTION12H146 - 268
17X-RAY DIFFRACTION13G10 - 111
18X-RAY DIFFRACTION14G113 - 125
19X-RAY DIFFRACTION14G129 - 202

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