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- PDB-4mmy: Integrin AlphaVBeta3 ectodomain bound to the tenth domain of Fibr... -

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Basic information

Entry
Database: PDB / ID: 4mmy
TitleIntegrin AlphaVBeta3 ectodomain bound to the tenth domain of Fibronectin with the IAKGDWND motif
Components
  • Fibronectin
  • Integrin alpha-V
  • Integrin beta-3
KeywordsCELL ADHESION / integrin / A domain / hybrid domain / PSI / EGF repeats / beta TA thigh / beta propeller / RGD motif / fibronectin / vitronectin
Function / homology
Function and homology information


integrin alphav-beta6 complex / integrin alphav-beta8 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / : / opsonin binding / negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / integrin alphav-beta1 complex ...integrin alphav-beta6 complex / integrin alphav-beta8 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / : / opsonin binding / negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / integrin alphav-beta1 complex / negative regulation of transforming growth factor beta production / Fibronectin matrix formation / Cross-presentation of particulate exogenous antigens (phagosomes) / extracellular matrix protein binding / Extracellular matrix organization / tube development / positive regulation of substrate-dependent cell migration, cell attachment to substrate / regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / alpha9-beta1 integrin-ADAM8 complex / regulation of trophoblast cell migration / neural crest cell migration involved in autonomic nervous system development / regulation of postsynaptic neurotransmitter receptor diffusion trapping / peptidase activator activity / alphav-beta3 integrin-vitronectin complex / regulation of extracellular matrix organization / Laminin interactions / platelet alpha granule membrane / positive regulation of glomerular mesangial cell proliferation / fibrinogen complex / integrin alphav-beta3 complex / negative regulation of lipoprotein metabolic process / peptide cross-linking / alphav-beta3 integrin-PKCalpha complex / entry into host cell by a symbiont-containing vacuole / fibrinogen binding / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-HMGB1 complex / blood coagulation, fibrin clot formation / negative regulation of lipid transport / integrin activation / vascular endothelial growth factor receptor 2 binding / glycinergic synapse / negative regulation of low-density lipoprotein receptor activity / ALK mutants bind TKIs / angiogenesis involved in wound healing / regulation of phagocytosis / Elastic fibre formation / regulation of release of sequestered calcium ion into cytosol / mesodermal cell differentiation / cell-substrate junction assembly / alphav-beta3 integrin-IGF-1-IGF1R complex / transforming growth factor beta binding / platelet-derived growth factor receptor binding / filopodium membrane / positive regulation of small GTPase mediated signal transduction / extracellular matrix binding / regulation of postsynaptic neurotransmitter receptor internalization / positive regulation of fibroblast migration / positive regulation of vascular endothelial growth factor receptor signaling pathway / apolipoprotein A-I-mediated signaling pathway / regulation of bone resorption / apoptotic cell clearance / positive regulation of cell adhesion mediated by integrin / wound healing, spreading of epidermal cells / heterotypic cell-cell adhesion / integrin complex / biological process involved in interaction with symbiont / proteoglycan binding / Molecules associated with elastic fibres / positive regulation of intracellular signal transduction / positive regulation of cell-matrix adhesion / cellular response to insulin-like growth factor stimulus / smooth muscle cell migration / MET activates PTK2 signaling / microvillus membrane / extracellular matrix structural constituent / negative chemotaxis / cell adhesion mediated by integrin / Syndecan interactions / p130Cas linkage to MAPK signaling for integrins / activation of protein kinase activity / cellular response to platelet-derived growth factor stimulus / cell-substrate adhesion / protein disulfide isomerase activity / positive regulation of smooth muscle cell migration / endodermal cell differentiation / positive regulation of osteoblast proliferation / TGF-beta receptor signaling activates SMADs / PECAM1 interactions / lamellipodium membrane / GRB2:SOS provides linkage to MAPK signaling for Integrins / negative regulation of macrophage derived foam cell differentiation / platelet-derived growth factor receptor signaling pathway / negative regulation of lipid storage / fibronectin binding / endoplasmic reticulum-Golgi intermediate compartment / positive regulation of cell adhesion / Non-integrin membrane-ECM interactions / basement membrane
Similarity search - Function
Hormone receptor fold - #30 / ntegrin, alpha v. Chain A, domain 4 / Integrin domains. Chain A, domain 2 / Hormone receptor fold / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / Fibronectin type I domain / Fibronectin, type I / Fibronectin type-I domain signature. / Fibronectin type-I domain profile. ...Hormone receptor fold - #30 / ntegrin, alpha v. Chain A, domain 4 / Integrin domains. Chain A, domain 2 / Hormone receptor fold / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / Fibronectin type I domain / Fibronectin, type I / Fibronectin type-I domain signature. / Fibronectin type-I domain profile. / Fibronectin type 1 domain / 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 / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. / Fibronectin type-II collagen-binding domain profile. / Fibronectin type 2 domain / 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) / Integrin alpha cytoplasmic region / EGF-like domain, extracellular / EGF-like domain / von Willebrand factor, type A domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / : / 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 alpha, N-terminal / Integrin domain superfamily / PSI domain / domain found in Plexins, Semaphorins and Integrins / Laminin / Laminin / 7 Propeller / Methylamine Dehydrogenase; Chain H / Kringle-like fold / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / Fibronectin type III domain / EGF-like domain signature 1. / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Ribbon / Few Secondary Structures / Irregular / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
: / Fibronectin / Integrin beta-3 / Integrin alpha-V
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.183 Å
Authorsvan Agthoven, J. / Xiong, J. / Arnaout, M.A.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2014
Title: Structural basis for pure antagonism of integrin alpha V beta 3 by a high-affinity form of fibronectin.
Authors: Van Agthoven, J.F. / Xiong, J.P. / Alonso, J.L. / Rui, X. / Adair, B.D. / Goodman, S.L. / Arnaout, M.A.
History
DepositionSep 9, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 26, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 9, 2014Group: Database references
Revision 1.2Apr 30, 2014Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / 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 / 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 / _chem_comp.name / _chem_comp.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_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_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 / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrin alpha-V
B: Integrin beta-3
C: Fibronectin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)200,06425
Polymers193,0773
Non-polymers6,98722
Water905
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15920 Å2
ΔGint52 kcal/mol
Surface area75180 Å2
MethodPISA
Unit cell
Length a, b, c (Å)130.018, 130.018, 308.203
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein Integrin alpha-V / Vitronectin receptor subunit alpha / Integrin alpha-V heavy chain / Integrin alpha-V light chain


Mass: 106048.359 Da / Num. of mol.: 1 / Fragment: Extracellular domain (UNP residues 31-989)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGAV, MSK8, VNRA / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Hi5 / References: UniProt: P06756
#2: Protein Integrin beta-3 / Platelet membrane glycoprotein IIIa / GPIIIa


Mass: 76523.125 Da / Num. of mol.: 1 / Fragment: Extracellular domain (UNP residues 27-718)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB3, GP3A / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Hi5 / References: UniProt: P05106
#3: Protein Fibronectin / FN / Cold-insoluble globulin / CIG


Mass: 10505.757 Da / Num. of mol.: 1
Fragment: Fibronectin type-III domain 10 (UNP residues 1448-1540)
Mutation: TGRGDSPASS to IARGDWNDG
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FN1, FN / Plasmid: pET / Production host: Escherichia coli (E. coli) / References: UniProt: P02751

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Sugars , 5 types, 14 molecules

#4: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...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: 748.682 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-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: isolated from a genetically manipulated source
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 alpha-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-4)-beta-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
DManpa1-4DManpb1-6[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]/1-1-2-3-2-3/a4-b1_b4-c1_c3-d1_c6-e1_e4-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)][b-D-Manp]{[(4+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#8: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5
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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Non-polymers , 2 types, 13 molecules

#9: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mn
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 5 / 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: 3.84 Å3/Da / Density % sol: 68.01 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 12% PEG3350, 0.8 M sodium chloride, 0.1 M sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97921 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 19, 2013
RadiationMonochromator: sagitally focused Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97921 Å / Relative weight: 1
ReflectionResolution: 3.18→50 Å / Num. all: 51260 / Num. obs: 51260 / % possible obs: 99.7 % / Observed criterion σ(F): 14.3 / Observed criterion σ(I): 14.3 / Redundancy: 5.3 % / Rsym value: 0.104 / Net I/σ(I): 12.6
Reflection shellResolution: 3.18→3.28 Å / Redundancy: 5.1 % / Mean I/σ(I) obs: 2.2 / Rsym value: 0.894 / % possible all: 99.7

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.183→41.021 Å / SU ML: 0.39 / σ(F): 1.36 / Phase error: 25.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.252 2535 4.96 %
Rwork0.2111 --
obs0.213 51144 99.39 %
all-49336 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.183→41.021 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12555 0 440 5 13000
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00713359
X-RAY DIFFRACTIONf_angle_d0.99618031
X-RAY DIFFRACTIONf_dihedral_angle_d13.734942
X-RAY DIFFRACTIONf_chiral_restr0.0392064
X-RAY DIFFRACTIONf_plane_restr0.0052332
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1829-3.24410.33411550.30692527X-RAY DIFFRACTION95
3.2441-3.31030.34791480.28192651X-RAY DIFFRACTION100
3.3103-3.38220.29411330.27032649X-RAY DIFFRACTION100
3.3822-3.46090.30271230.26142678X-RAY DIFFRACTION100
3.4609-3.54740.31981540.2462696X-RAY DIFFRACTION100
3.5474-3.64320.29281330.23462660X-RAY DIFFRACTION100
3.6432-3.75040.25811330.21992684X-RAY DIFFRACTION100
3.7504-3.87130.25291150.22412695X-RAY DIFFRACTION100
3.8713-4.00960.28021410.2162682X-RAY DIFFRACTION100
4.0096-4.170.2271370.20212707X-RAY DIFFRACTION100
4.17-4.35960.22361300.19272711X-RAY DIFFRACTION100
4.3596-4.58910.20331490.17992701X-RAY DIFFRACTION100
4.5891-4.87620.221490.17132704X-RAY DIFFRACTION100
4.8762-5.2520.23261650.18082700X-RAY DIFFRACTION100
5.252-5.77920.23191480.20842742X-RAY DIFFRACTION100
5.7792-6.61250.29031470.22822753X-RAY DIFFRACTION100
6.6125-8.31960.26011550.22422774X-RAY DIFFRACTION100
8.3196-41.02460.23361200.19842895X-RAY DIFFRACTION97
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)
15.10060.75620.87582.1819-0.61072.0999-0.41370.36760.3743-0.48620.32630.2311-0.23050.03540.06940.8556-0.2561-0.06180.42840.05530.61113.446154.037821.0785
24.01470.15070.85650.3841-0.05720.3307-0.41841.22020.7077-0.45710.32350.3711-0.26410.07380.09281.2144-0.2904-0.38160.89070.2271.0916-41.491947.0121-0.5515
33.8081-1.44571.80882.90920.4632.1086-0.42170.1941-0.0316-0.1480.35590.6634-0.13691.03270.12781.0342-0.102-0.19110.98150.20710.9535-50.137843.04522.8554
45.0923-0.55491.35613.7039-0.65916.1554-0.2209-0.5872-0.23640.650.0797-0.16930.10680.18690.13190.91440.27980.00840.5255-0.0050.7861-25.40136.275773.2419
59.77037.51256.56146.74755.80395.0062-0.08830.3319-0.6041-1.2881-0.03190.5210.1529-1.38480.11761.6242-0.1405-0.45711.29680.12981.4471-41.0864.40117.4339
63.36772.9972-0.21545.5251-0.49630.99650.452-0.5558-1.5020.6903-0.4534-1.37640.60070.0194-0.02291.1617-0.0817-0.04360.54290.16081.03364.424913.003334.4407
72.20781.0351-0.73658.7177-2.12015.18290.1368-0.2111-1.2283-0.0750.0047-1.19220.5740.6383-0.14160.6986-0.0749-0.0180.57560.11481.241817.77427.506431.4178
87.01023.2035-0.5584.54661.72244.59831.0063-1.4254-1.33630.93550.0514-0.16041.517-1.0085-1.04371.0984-0.2034-0.12310.72850.37131.02824.526725.439140.938
96.42822.42442.09794.18632.09763.0913-0.53390.13830.1251-0.30790.0762-0.356-1.10570.09740.46431.3095-0.0876-0.01210.45420.09220.9112-12.712512.347731.6404
104.68330.9235-0.01341.49432.0823.29850.35821.8108-0.1143-1.1775-0.78270.73151.5333-1.18960.43562.0399-0.34-0.37211.5723-0.16131.487-30.07647.9994-2.2448
111.77-2.4305-1.85263.31762.55391.9638-0.11531.28870.0806-0.7514-0.71620.4595-1.2477-0.80990.8491.9505-0.1292-0.79491.50180.15742.1137-52.34920.3744-2.4562
129.87855.90028.46146.24243.98682.0157-1.18710.99431.949-1.4792-0.16680.9876-1.3670.04311.38811.5104-0.1578-0.45711.21920.15761.5142-38.789227.426712.6184
130.3918-1.33941.31274.6654-4.59164.7499-0.1289-0.0118-0.1924-0.05710.1867-0.27270.4116-0.1288-0.05630.7680.05840.08840.7624-0.03761.0796-21.098520.827549.015
144.35541.7477-1.05022.11963.10368.9222-0.29450.05670.84640.34580.0444-0.5591-0.85310.5260.25751.26850.3112-0.15560.63110.08741.4314-7.963515.358568.8222
159.96861.99895.96332-5.14213.9348-0.3923-1.7517-0.92992.7281.08690.43280.29110.1667-0.67471.585-0.2546-0.14670.92430.3681.210420.370642.282944.1906
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 421 )
2X-RAY DIFFRACTION2chain 'A' and (resid 422 through 633 )
3X-RAY DIFFRACTION3chain 'A' and (resid 634 through 737 )
4X-RAY DIFFRACTION4chain 'A' and (resid 738 through 956 )
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 59 )
6X-RAY DIFFRACTION6chain 'B' and (resid 60 through 169 )
7X-RAY DIFFRACTION7chain 'B' and (resid 170 through 291 )
8X-RAY DIFFRACTION8chain 'B' and (resid 292 through 342 )
9X-RAY DIFFRACTION9chain 'B' and (resid 343 through 423 )
10X-RAY DIFFRACTION10chain 'B' and (resid 424 through 462 )
11X-RAY DIFFRACTION11chain 'B' and (resid 463 through 502 )
12X-RAY DIFFRACTION12chain 'B' and (resid 503 through 549 )
13X-RAY DIFFRACTION13chain 'B' and (resid 550 through 630 )
14X-RAY DIFFRACTION14chain 'B' and (resid 631 through 690 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1492 through 1497 )

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