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- PDB-4wk0: Metal Ion and Ligand Binding of Integrin -

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Basic information

Entry
Database: PDB / ID: 4wk0
TitleMetal Ion and Ligand Binding of Integrin
Components
  • ARG-GLY-ASP
  • Integrin alpha-5Integrin alpha 5
  • Integrin beta-1
KeywordsCELL ADHESION/IMMUNE SYSTEM / CELL ADHESION-FIBRONECTIN RECEPTOR / CELL ADHESION-IMMUNE SYSTEM complex
Function / homology
Function and homology information


integrin alpha8-beta1 complex / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / myoblast fate specification / positive regulation of glutamate uptake involved in transmission of nerve impulse / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process ...integrin alpha8-beta1 complex / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / myoblast fate specification / positive regulation of glutamate uptake involved in transmission of nerve impulse / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process / integrin alpha9-beta1 complex / cell-cell adhesion mediated by integrin / integrin alpha4-beta1 complex / cardiac cell fate specification / integrin binding involved in cell-matrix adhesion / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / integrin alpha2-beta1 complex / regulation of synapse pruning / formation of radial glial scaffolds / Localization of the PINCH-ILK-PARVIN complex to focal adhesions / reactive gliosis / cerebellar climbing fiber to Purkinje cell synapse / Other semaphorin interactions / CD40 signaling pathway / positive regulation of vascular endothelial growth factor signaling pathway / calcium-independent cell-matrix adhesion / integrin alphav-beta1 complex / positive regulation of fibroblast growth factor receptor signaling pathway / Fibronectin matrix formation / basement membrane organization / myelin sheath abaxonal region / alphav-beta3 integrin-vitronectin complex / CHL1 interactions / cardiac muscle cell myoblast differentiation / Laminin interactions / RUNX2 regulates genes involved in cell migration / germ cell migration / MET interacts with TNS proteins / leukocyte tethering or rolling / cardiac muscle cell differentiation / cell projection organization / Platelet Adhesion to exposed collagen / vascular endothelial growth factor receptor 2 binding / myoblast fusion / Elastic fibre formation / cell-substrate junction assembly / mesodermal cell differentiation / platelet-derived growth factor receptor binding / axon extension / positive regulation of fibroblast migration / cell migration involved in sprouting angiogenesis / positive regulation of vascular endothelial growth factor receptor signaling pathway / wound healing, spreading of epidermal cells / regulation of spontaneous synaptic transmission / heterotypic cell-cell adhesion / positive regulation of cell-substrate adhesion / myoblast differentiation / integrin complex / dendrite morphogenesis / Basigin interactions / muscle organ development / Molecules associated with elastic fibres / sarcomere organization / lamellipodium assembly / cell adhesion mediated by integrin / negative regulation of Rho protein signal transduction / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / MET activates PTK2 signaling / maintenance of blood-brain barrier / Syndecan interactions / negative regulation of vasoconstriction / leukocyte cell-cell adhesion / positive regulation of neuroblast proliferation / epidermal growth factor receptor binding / positive regulation of wound healing / cell-substrate adhesion / positive regulation of sprouting angiogenesis / homophilic cell adhesion via plasma membrane adhesion molecules / endodermal cell differentiation / TGF-beta receptor signaling activates SMADs / establishment of mitotic spindle orientation / glial cell projection / cleavage furrow / cellular response to low-density lipoprotein particle stimulus / fibronectin binding / neuroblast proliferation / RHOG GTPase cycle / negative regulation of anoikis / negative regulation of neuron differentiation / ECM proteoglycans / intercalated disc / RAC3 GTPase cycle / RAC2 GTPase cycle / laminin binding / Integrin cell surface interactions / cellular defense response / coreceptor activity / phagocytosis / ruffle
Similarity search - Function
ligand-binding face of the semaphorins, domain 2 / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / ligand-binding face of the semaphorins, domain 2 / Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : ...ligand-binding face of the semaphorins, domain 2 / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / ligand-binding face of the semaphorins, domain 2 / Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin alpha Ig-like domain 3 / Integrin beta tail domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain cysteine-rich domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / EGF-like domain, extracellular / EGF-like domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / von Willebrand factor, type A domain / : / Integrin alpha Ig-like domain 2 / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / Integrins alpha chain signature. / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin domain superfamily / Integrin alpha, N-terminal / PSI domain / domain found in Plexins, Semaphorins and Integrins / 7 Propeller / Methylamine Dehydrogenase; Chain H / von Willebrand factor A-like domain superfamily / EGF-like domain signature 1. / Immunoglobulin-like / Sandwich / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Integrin beta-1 / Integrin alpha-5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.78 Å
AuthorsXia, W. / Springer, T.A.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: Metal ion and ligand binding of integrin alpha 5 beta 1.
Authors: Xia, W. / Springer, T.A.
History
DepositionOct 1, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 3, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 17, 2014Group: Database references
Revision 1.2Dec 24, 2014Group: Database references
Revision 2.0Nov 22, 2017Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Other / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / citation / entity / entity_src_gen / pdbx_database_status / pdbx_entity_src_syn / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_oper_list / software / struct_conn / struct_site_gen
Item: _atom_site.label_asym_id / _atom_site.label_entity_id ..._atom_site.label_asym_id / _atom_site.label_entity_id / _atom_site_anisotrop.pdbx_label_asym_id / _citation.journal_id_CSD / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_oper_list.symmetry_operation / _software.classification / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_site_gen.label_asym_id
Revision 3.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Refinement description / 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_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / refine_hist / 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 / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.conn_type_id / _struct_conn.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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.1Dec 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrin alpha-5
B: Integrin beta-1
C: ARG-GLY-ASP
hetero molecules


Theoretical massNumber of molelcules
Total (without water)101,88719
Polymers97,9673
Non-polymers3,92016
Water11,331629
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8650 Å2
ΔGint-23 kcal/mol
Surface area36350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.060, 117.070, 167.090
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein Integrin alpha-5 / Integrin alpha 5 / CD49 antigen-like family member E / Fibronectin receptor subunit alpha / Integrin alpha-F / VLA-5


Mass: 48116.863 Da / Num. of mol.: 1 / Fragment: UNP residues 42-493 / Mutation: I451V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGA5, FNRA / Cell line (production host): HEK 293 / Production host: Homo sapiens (human) / References: UniProt: P08648
#2: Protein Integrin beta-1 / Fibronectin receptor subunit beta / Glycoprotein IIa / GPIIA / VLA-4 subunit beta


Mass: 49502.852 Da / Num. of mol.: 1 / Fragment: UNP residues 21-465
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB1, FNRB, MDF2, MSK12 / Cell line (production host): HEK 293 / Production host: Homo sapiens (human) / References: UniProt: P05556

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Protein/peptide , 1 types, 1 molecules C

#3: Protein/peptide ARG-GLY-ASP


Mass: 347.349 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

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Sugars , 3 types, 9 molecules

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


Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#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.: 4 / Source method: obtained synthetically
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
#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.: 4 / Source method: obtained synthetically / 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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Non-polymers , 3 types, 636 molecules

#6: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 629 / 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: 3.06 Å3/Da / Density % sol: 59.79 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.2 / Details: 0.1 M HEPES 7.2, 16% PEG 6000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.97934 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 25, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 1.78→47.9 Å / Num. obs: 113328 / % possible obs: 98.2 % / Redundancy: 3.6 % / Biso Wilson estimate: 28.32 Å2 / Net I/σ(I): 7.17

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Processing

Software
NameVersionClassification
XDSdata scaling
PHENIX(phenix.refine: dev_1760)refinement
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.78→47.9 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.65 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2231 1997 1.76 %
Rwork0.1865 111322 -
obs0.1872 113319 98.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 206.19 Å2 / Biso mean: 50.2932 Å2 / Biso min: 15.95 Å2
Refinement stepCycle: final / Resolution: 1.78→47.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6725 0 516 629 7870
Biso mean--88.63 45.56 -
Num. residues----876
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0077156
X-RAY DIFFRACTIONf_angle_d1.0869724
X-RAY DIFFRACTIONf_chiral_restr0.0421104
X-RAY DIFFRACTIONf_plane_restr0.0051260
X-RAY DIFFRACTIONf_dihedral_angle_d14.0762608
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.78-1.82460.48211430.432179348077100
1.8246-1.87390.42811430.386379858128100
1.8739-1.9290.40751430.35317947809099
1.929-1.99130.36351430.318580198162100
1.9913-2.06250.34091440.293179768120100
2.0625-2.14510.29531430.256979798122100
2.1451-2.24270.24081440.22918009815399
2.2427-2.36090.2351430.21147971811499
2.3609-2.50880.24591420.19467953809599
2.5088-2.70250.21151440.18317960810498
2.7025-2.97450.17681410.17017932807398
2.9745-3.40480.20681420.1567864800696
3.4048-4.28920.17211390.12537796793595
4.2892-47.95670.16021430.13437997814094
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)
13.1684-1.5715-0.59624.30781.46123.3718-0.0195-0.0658-0.17380.2885-0.09870.50680.3591-0.50810.02110.2225-0.07140.05620.28240.00770.2854-6.4467-17.895-25.7064
21.7511-0.02210.32522.66310.09151.9090.1351-0.20660.25760.4623-0.14740.5933-0.3547-0.39310.16060.33830.05020.15810.3544-0.04320.3629-5.9882-0.7445-14.334
31.27050.251-0.19972.6098-0.32961.64820.0821-0.23960.15420.6567-0.0830.2551-0.242-0.10380.03030.4117-0.00570.0630.3047-0.04330.20995.9067-0.9661-10.7288
41.18110.5072-0.78132.0957-0.32122.94650.0769-0.3110.04650.533-0.1006-0.0153-0.19620.06450.02260.2819-0.0095-0.02460.3059-0.00440.188314.0344-6.1114-11.0187
54.49882.4313-3.09044.813-4.66254.6994-0.1174-0.14490.0830.6279-0.0355-0.317-0.37720.08350.40180.28630.0042-0.01160.2545-0.02970.256121.7763-10.2911-20.4335
61.2442-0.78370.70624.4138-1.11861.6249-0.02780.038-0.1305-0.1824-0.0242-0.02020.14480.10070.09470.15560.03630.04420.2080.00450.186119.0289-15.4977-29.8441
71.2629-1.07550.85863.7179-2.77754.29290.00390.2056-0.0511-0.2974-0.1473-0.15030.21820.33960.14190.21770.01530.03130.2049-0.010.209119.0072-16.59-37.73
83.3281-1.18321.68073.2763-3.10934.2724-0.03240.1471-0.1327-0.1292-0.0884-0.08130.2324-0.01850.01430.2165-0.01480.04830.2273-0.03540.20497.5569-22.8424-35.0249
91.30520.955-0.74772.7283-1.91355.0358-0.05350.0722-0.041-0.00220.12090.3560.1809-0.2204-0.21190.2015-0.0407-0.0060.2506-0.02340.2343-2.1637-19.1375-33.5862
101.5032-1.6906-0.48392.2365-0.2231.8830.0140.1089-0.1696-0.0055-0.02660.49250.1862-0.2442-0.00810.1895-0.05170.00150.2545-0.02910.2971-4.7853-21.1958-31.7362
116.1494-1.5342-1.43039.42413.77927.59860.39050.8897-1.8979-0.70630.2031-1.06721.19020.0921-0.51411.3406-0.1372-0.02940.7271-0.32341.401420.7038-36.2657-77.4267
121.12090.1688-0.60964.00962.71574.48-0.180.3715-0.1828-0.66470.2224-0.07730.2497-0.0206-0.08870.4138-0.0618-0.02550.38160.00640.266423.4576-1.1176-69.2728
132.96370.8175-2.62381.6956-1.13633.93450.363-0.28810.54380.449-0.010.1136-0.66850.3051-0.37290.3564-0.02660.0310.2172-0.0480.338318.227222.0783-35.5877
140.93390.1116-0.71371.0072-0.77841.45970.06460.02810.1790.12780.01870.0141-0.1884-0.0035-0.08320.26310.00090.00260.23740.00220.258616.917212.1107-41.247
151.35631.85631.2177.62725.72586.2260.1389-0.0073-0.19670.17990.0831-0.5130.4330.1062-0.25320.24740.0071-0.00870.24220.06140.236127.69841.4407-56.1943
169.14514.39231.71813.86672.13515.84370.40220.0726-0.52450.3204-0.008-0.54760.810.1783-0.40550.39740.0692-0.02190.3194-0.0090.347329.0761-6.2061-63.4755
175.40023.03463.47324.29356.03828.77590.11570.131-0.3410.2840.05570.2190.7214-0.50.04390.4981-0.1235-0.03030.35860.04580.27617.0624-6.41-67.6637
185.3381-3.40174.35753.56380.40552.0006-1.0011-1.19060.73214.40221.1614-1.1156-2.5987-0.5738-0.00750.81630.1048-0.04170.6295-0.00440.505521.858412.3444-21.3407
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 39 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 40 through 116 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 117 through 177 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 178 through 246 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 247 through 271 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 272 through 312 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 313 through 350 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 351 through 397 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 398 through 431 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 432 through 452 )A0
11X-RAY DIFFRACTION11chain 'B' and (resid 5 through 53 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 54 through 132 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 133 through 199 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 200 through 346 or resid 449)B0
15X-RAY DIFFRACTION15chain 'B' and (resid 347 through 380 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 381 through 420 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 421 through 444 )B0
18X-RAY DIFFRACTION18chain 'C' and (resid 1524 through 1526 )D0

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