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- PDB-3tvm: Structure of the mouse CD1d-SMC124-iNKT TCR complex -

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Basic information

Entry
Database: PDB / ID: 3tvm
TitleStructure of the mouse CD1d-SMC124-iNKT TCR complex
Components
  • Antigen-presenting glycoprotein CD1d1
  • Valpha14 (mouse variable domain, human constant domain)
  • Vbeta8.2 (mouse variable domain, human constant domain)
  • beta-2-microglobulinBeta-2 microglobulin
KeywordsIMMUNE SYSTEM / antigen presentation / glycolipid / NKT cells
Function / homology
Function and homology information


regulation of immature T cell proliferation in thymus / positive regulation of NK T cell differentiation / positive regulation of NK T cell activation / NK T cell differentiation / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding / alpha-beta T cell receptor complex ...regulation of immature T cell proliferation in thymus / positive regulation of NK T cell differentiation / positive regulation of NK T cell activation / NK T cell differentiation / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding / alpha-beta T cell receptor complex / positive thymic T cell selection / positive regulation of macrophage activation / Endosomal/Vacuolar pathway / DAP12 interactions / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / regulation of membrane depolarization / positive regulation of interleukin-4 production / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / alpha-beta T cell activation / Generation of second messenger molecules / antigen processing and presentation / PD-1 signaling / regulation of immune response / cellular defense response / T cell receptor binding / positive regulation of interleukin-2 production / Neutrophil degranulation / response to bacterium / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / negative regulation of forebrain neuron differentiation / regulation of erythrocyte differentiation / peptide antigen assembly with MHC class I protein complex / response to molecule of bacterial origin / 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 / negative regulation of neurogenesis / peptide antigen assembly with MHC class II protein complex / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / negative regulation of epithelial cell proliferation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of immune response / positive regulation of type II interferon production / antimicrobial humoral immune response mediated by antimicrobial peptide / sensory perception of smell / positive regulation of T cell activation / late endosome / Downstream TCR signaling / negative regulation of neuron projection development / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / T cell receptor signaling pathway / iron ion transport / protein refolding / antibacterial humoral response / protein homotetramerization / intracellular iron ion homeostasis / adaptive immune response / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / amyloid fibril formation / lysosome / early endosome / learning or memory / endosome membrane / defense response to Gram-positive bacterium / immune response / lysosomal membrane / external side of plasma membrane / innate immune response / structural molecule activity / Golgi apparatus / protein homodimerization activity / extracellular space / identical protein binding / plasma membrane / cytosol
Similarity search - Function
T-cell receptor alpha chain, constant domain / MHC-I family domain / Domain of unknown function (DUF1968) / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / 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 ...T-cell receptor alpha chain, constant domain / MHC-I family domain / Domain of unknown function (DUF1968) / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / 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-07P / T cell receptor beta constant 2 / T cell receptor alpha chain constant / Beta-2-microglobulin / Antigen-presenting glycoprotein CD1d1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsGirardi, E. / Li, Y. / Zajonc, D.M.
CitationJournal: Chem.Biol. / Year: 2011
Title: Glycolipids that Elicit IFN-gama-Biased Responses from Natural Killer T Cells
Authors: Tyznik, A.J. / Farber, E. / Girardi, E. / Birkholz, A. / Li, Y. / Chitale, S. / So, R. / Arora, P. / Khurana, A. / Wang, J. / Porcelli, S.A. / Zajonc, D.M. / Kronenberg, M. / Howell, A.R.
History
DepositionSep 20, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 1, 2012Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_entity_src_syn / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_ref_seq_dif / 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 / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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 / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 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 2.2Mar 13, 2024Group: Source and taxonomy / Structure summary / Category: entity / pdbx_entity_src_syn / Item: _entity.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Antigen-presenting glycoprotein CD1d1
B: beta-2-microglobulin
C: Valpha14 (mouse variable domain, human constant domain)
D: Vbeta8.2 (mouse variable domain, human constant domain)
E: Antigen-presenting glycoprotein CD1d1
F: beta-2-microglobulin
G: Valpha14 (mouse variable domain, human constant domain)
H: Vbeta8.2 (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)193,13218
Polymers188,7518
Non-polymers4,38110
Water1,08160
1
A: Antigen-presenting glycoprotein CD1d1
B: beta-2-microglobulin
C: Valpha14 (mouse variable domain, human constant domain)
D: Vbeta8.2 (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,5389
Polymers94,3764
Non-polymers2,1625
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
E: Antigen-presenting glycoprotein CD1d1
F: beta-2-microglobulin
G: Valpha14 (mouse variable domain, human constant domain)
H: Vbeta8.2 (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,5949
Polymers94,3764
Non-polymers2,2195
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)78.970, 150.570, 101.960
Angle α, β, γ (deg.)90.00, 96.35, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11B
21D
12G
22E
13H
23F

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1116B1 - 99
2116D1 - 99
1126G1 - 210
2126E1 - 210
1136H1 - 245
2136F1 - 245

NCS ensembles :
ID
1
2
3

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Components

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Protein , 3 types, 6 molecules AEBFDH

#1: Protein Antigen-presenting glycoprotein CD1d1 / T cell surface glycoprotein CD1d


Mass: 32632.668 Da / Num. of mol.: 2 / Fragment: residues 19-298
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cd1.1, CD1d, Cd1d1 / Plasmid: pBACp10pH / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P11609
#2: Protein beta-2-microglobulin / Beta-2 microglobulin


Mass: 11660.350 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: beta-2-microglobulin / Plasmid: pBACp10pH / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P01887
#4: Protein Vbeta8.2 (mouse variable domain, human constant domain)


Mass: 27026.998 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus, Homo sapiens
Gene: Vbeta8.2 (mouse variable domain, human constant domain)
Plasmid: pET30a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 / References: UniProt: A0A5B9*PLUS

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Antibody , 1 types, 2 molecules CG

#3: Antibody Valpha14 (mouse variable domain, human constant domain)


Mass: 23055.621 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus, Homo sapiens
Gene: Valpha14 (mouse variable domain, human constant domain)
Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01848*PLUS

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Sugars , 3 types, 6 molecules

#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: glycosphingolipid
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#6: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: glycosphingolipid
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#7: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6 / Details: glycosphingolipid
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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Non-polymers , 4 types, 64 molecules

#8: Chemical ChemComp-07P / N-[(2S,3R)-10-[(1R,2R)-2-decylcyclopropyl]-1-(alpha-D-galactopyranosyloxy)-3-hydroxydecan-2-yl]hexacosanamide / SMC124


Mass: 910.440 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C55H107NO8
#9: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#10: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 60 / 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: 3.19 Å3/Da / Density % sol: 61.46 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 100mM trisodium citrate pH5.6, 10% PEG3350, 2% tacsimate pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.9795 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Dec 14, 2009
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.8→75.29 Å / Num. all: 58305 / Num. obs: 58305 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.094 / Net I/σ(I): 10.9
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.577 / Mean I/σ(I) obs: 2.4 / % possible all: 100

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Processing

Software
NameVersionClassification
Blu-Icedata collection
MOLREPphasing
REFMAC5.5.0102refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2Q7Y for CD1d, 3HE6 for TCR

2q7y

3he6


Resolution: 2.8→75.29 Å / Cor.coef. Fo:Fc: 0.91 / Cor.coef. Fo:Fc free: 0.866 / SU B: 33.138 / SU ML: 0.295 / Cross valid method: THROUGHOUT / ESU R: 0.895 / ESU R Free: 0.366 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27272 2948 5.1 %RANDOM
Rwork0.22404 ---
obs0.22647 55304 99.93 %-
all-58305 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 52.28 Å2
Baniso -1Baniso -2Baniso -3
1--0.49 Å2-0 Å21.82 Å2
2---0.21 Å2-0 Å2
3---1.11 Å2
Refinement stepCycle: LAST / Resolution: 2.8→75.29 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11890 0 295 60 12245
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.02112549
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.9211.95117132
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.92251543
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.41224.045539
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.225151781
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.3421558
X-RAY DIFFRACTIONr_chiral_restr0.0580.21918
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0219570
X-RAY DIFFRACTIONr_gen_planes_other
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_it0.1091.57768
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.233212463
X-RAY DIFFRACTIONr_scbond_it0.41634781
X-RAY DIFFRACTIONr_scangle_it0.7124.54663
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1B740LOOSE POSITIONAL0.325
1B740LOOSE THERMAL0.6210
2G1468LOOSE POSITIONAL0.495
2G1468LOOSE THERMAL0.3610
3H1832LOOSE POSITIONAL0.285
3H1832LOOSE THERMAL0.3710
LS refinement shellResolution: 2.8→2.873 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.385 216 -
Rwork0.343 4064 -
obs--99.98 %
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)
13.2017-0.0807-1.78663.96950.54222.15410.0908-0.08690.20980.42920.09010.1016-0.07810.0039-0.1810.29-0.030.06250.2247-0.00740.198226.1843-0.798628.5091
28.4999-0.5745-3.0811.3003-1.21216.93090.0095-0.3992-0.44530.54430.17420.50350.5291-0.4457-0.18370.66990.03430.31570.59550.08770.4735-2.9178-2.369752.0236
36.8685-2.5716-0.82793.08460.98273.0602-0.14360.4479-0.289-0.03160.12970.7867-0.1162-0.76030.01390.34640.01120.10180.63370.1340.5205-2.2392.540230.9044
45.91161.967-2.38852.5963-1.03733.26130.0438-0.2192-0.0547-0.0111-0.1701-0.3015-0.17930.14480.12630.16760.0072-0.0270.1077-0.00970.194853.58837.06547.8702
53.05340.2227-1.39131.8064-1.58998.2429-0.06460.502-0.2195-0.41290.0267-0.12480.5627-0.43430.0380.2623-0.0223-0.00730.2623-0.10680.181540.0744-6.7149-5.2364
65.5881.21262.23514.89991.29297.1989-0.1570.12210.7732-0.77840.0588-0.493-1.04130.69570.09820.561-0.02880.2940.27640.03130.658175.66988.7532-21.206
76.1665-0.11930.87312.93670.58913.53280.09520.32630.3027-0.473-0.0176-0.2218-0.1912-0.1264-0.07760.360.05280.06720.2028-0.00060.148265.1449-4.7915-22.4397
87.5107-1.04651.13633.4153-0.42872.6698-0.0371-1.2808-1.53220.23280.07320.18210.08120.0538-0.03610.1844-0.0416-0.05240.4690.33220.540215.140238.15726.465
98.53844.8291-2.37129.10186.280810.3339-0.3005-1.61231.06621.39990.97170.88791.18722.5074-0.67120.82180.46790.13342.85070.65960.484741.829637.256143.8172
1017.9398-6.71820.06743.6598-1.76372.8611-0.1517-2.1291-0.6247-0.12850.43960.20890.1950.5117-0.28790.2209-0.0689-0.03820.91830.2290.516143.53536.313927.3941
115.84512.39382.45552.89971.0782.83860.1473-0.1641-0.1124-0.0171-0.1309-0.02790.1504-0.0392-0.01640.1640.0099-0.03030.10610.08760.295-13.171829.67988.009
123.12120.90030.671.1950.00437.3895-0.11280.42710.0126-0.22020.17060.1113-0.45450.0477-0.05780.2852-0.0039-0.00340.20210.08250.2553-0.58744.2568-5.4213
136.52160.7381-2.51474.7613-0.238.6215-0.02910.3092-0.6828-0.83110.20420.28370.9917-0.6698-0.17510.4831-0.0048-0.16070.28340.03660.5499-35.935228.0631-20.5839
146.70350.3414-0.82821.8979-0.52644.04440.00530.4276-0.3922-0.3221-0.0068-0.02440.16870.04920.00150.38560.0732-0.08920.21610.03690.2244-26.074142.0269-22.0725
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 185
2X-RAY DIFFRACTION1A508 - 513
3X-RAY DIFFRACTION1A286
4X-RAY DIFFRACTION2A186 - 279
5X-RAY DIFFRACTION3B2 - 99
6X-RAY DIFFRACTION4C1 - 114
7X-RAY DIFFRACTION5D2 - 112
8X-RAY DIFFRACTION6C115 - 206
9X-RAY DIFFRACTION7D113 - 240
10X-RAY DIFFRACTION8E7 - 185
11X-RAY DIFFRACTION8E514 - 519
12X-RAY DIFFRACTION8E286
13X-RAY DIFFRACTION9E186 - 249
14X-RAY DIFFRACTION10F2 - 98
15X-RAY DIFFRACTION11G1 - 114
16X-RAY DIFFRACTION12H1 - 112
17X-RAY DIFFRACTION13G115 - 206
18X-RAY DIFFRACTION14H113 - 240

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