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

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Basic information

Entry
Database: PDB / ID: 4mmx
TitleIntegrin AlphaVBeta3 ectodomain bound to the tenth domain of Fibronectin
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-beta8 complex / integrin alphav-beta6 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / negative regulation of monocyte activation / opsonin binding / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / integrin alphav-beta1 complex ...integrin alphav-beta8 complex / integrin alphav-beta6 complex / transforming growth factor beta production / negative regulation of entry of bacterium into host cell / integrin alphav-beta5 complex / negative regulation of monocyte activation / opsonin binding / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / integrin alphav-beta1 complex / Fibronectin matrix formation / Cross-presentation of particulate exogenous antigens (phagosomes) / Extracellular matrix organization / positive regulation of substrate-dependent cell migration, cell attachment to substrate / extracellular matrix protein binding / tube development / regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / alpha9-beta1 integrin-ADAM8 complex / regulation of trophoblast cell migration / integrin alphaIIb-beta3 complex / 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 / fibrinogen complex / Laminin interactions / regulation of extracellular matrix organization / platelet alpha granule membrane / positive regulation of glomerular mesangial cell proliferation / negative regulation of lipoprotein metabolic process / integrin alphav-beta3 complex / negative regulation of low-density lipoprotein receptor activity / peptide cross-linking / fibrinogen binding / alphav-beta3 integrin-PKCalpha complex / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-HMGB1 complex / regulation of phagocytosis / blood coagulation, fibrin clot formation / mesodermal cell differentiation / vascular endothelial growth factor receptor 2 binding / negative regulation of lipid transport / integrin activation / glycinergic synapse / ALK mutants bind TKIs / angiogenesis involved in wound healing / Elastic fibre formation / regulation of release of sequestered calcium ion into cytosol / alphav-beta3 integrin-IGF-1-IGF1R complex / cell-substrate junction assembly / transforming growth factor beta binding / platelet-derived growth factor receptor binding / entry into host cell by a symbiont-containing vacuole / positive regulation of small GTPase mediated signal transduction / filopodium membrane / extracellular matrix binding / positive regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of fibroblast migration / regulation of postsynaptic neurotransmitter receptor internalization / 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 / positive regulation of intracellular signal transduction / Molecules associated with elastic fibres / extracellular matrix structural constituent / smooth muscle cell migration / cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion / MET activates PTK2 signaling / microvillus membrane / negative chemotaxis / Syndecan interactions / cellular response to insulin-like growth factor stimulus / activation of protein kinase activity / p130Cas linkage to MAPK signaling for integrins / cell-substrate adhesion / protein disulfide isomerase activity / positive regulation of smooth muscle cell migration / endodermal cell differentiation / positive regulation of osteoblast proliferation / cellular response to platelet-derived growth factor stimulus / TGF-beta receptor signaling activates SMADs / PECAM1 interactions / GRB2:SOS provides linkage to MAPK signaling for Integrins / endoplasmic reticulum-Golgi intermediate compartment / lamellipodium membrane / platelet-derived growth factor receptor signaling pathway / fibronectin binding / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / Non-integrin membrane-ECM interactions / basement membrane / ECM proteoglycans
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. ...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 / von Willebrand factor, type A domain / EGF-like domain, extracellular / EGF-like domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / : / Integrin alpha Ig-like domain 2 / 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 / Laminin / Laminin / 7 Propeller / Methylamine Dehydrogenase; Chain H / Kringle-like fold / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Ribbon / Few Secondary Structures / Irregular / Immunoglobulins / 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: 3.32 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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_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)199,90825
Polymers192,9213
Non-polymers6,98722
Water362
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16100 Å2
ΔGint49 kcal/mol
Surface area79550 Å2
MethodPISA
Unit cell
Length a, b, c (Å)129.859, 129.859, 305.831
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: alphav, 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: GP3A, ITGB3 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Hi5 / References: UniProt: P05106
#3: Protein Fibronectin / FN / Cold-insoluble globulin / CIG


Mass: 10349.573 Da / Num. of mol.: 1
Fragment: Fibronectin type-III domain 10 (UNP residues 1448-1540)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: Fibronectin, FN, FN1 / 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, 10 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.: 2 / 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: 3.85 Å3/Da / Density % sol: 68.05 %
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: Oct 13, 2012
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: 3.32→75.49 Å / Num. all: 67157 / Num. obs: 39593 / % possible obs: 88 % / Observed criterion σ(F): 5.3 / Observed criterion σ(I): 5.3 / Redundancy: 6.2 % / Rmerge(I) obs: 0.109 / Rsym value: 0.109 / Net I/σ(I): 13.9
Reflection shellResolution: 3.32→3.41 Å / Redundancy: 6.4 % / Mean I/σ(I) obs: 3.3 / Rsym value: 0.676 / % possible all: 88

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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: 3.32→42.506 Å / SU ML: 0.42 / σ(F): 1.38 / Phase error: 25.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2586 1942 4.91 %
Rwork0.2082 --
obs0.2105 39586 88 %
all-39661 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.32→42.506 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13184 0 440 2 13626
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0114004
X-RAY DIFFRACTIONf_angle_d0.86418917
X-RAY DIFFRACTIONf_dihedral_angle_d12.4765175
X-RAY DIFFRACTIONf_chiral_restr0.0352172
X-RAY DIFFRACTIONf_plane_restr0.0042445
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.32-3.4030.34421470.2823003X-RAY DIFFRACTION100
3.403-3.4950.3324850.29251356X-RAY DIFFRACTION46
3.495-3.59780.33791660.25922984X-RAY DIFFRACTION100
3.5978-3.71380.3559470.25321222X-RAY DIFFRACTION40
3.7138-3.84650.28791270.24943018X-RAY DIFFRACTION100
3.8465-4.00040.3271820.23111431X-RAY DIFFRACTION47
4.0004-4.18230.23181520.21323046X-RAY DIFFRACTION100
4.1823-4.40260.22551380.19153033X-RAY DIFFRACTION100
4.4026-4.67810.21871730.16743029X-RAY DIFFRACTION100
4.6781-5.03880.22141750.16773027X-RAY DIFFRACTION100
5.0388-5.54490.24321840.18913037X-RAY DIFFRACTION100
5.5449-6.34490.27681590.21883077X-RAY DIFFRACTION100
6.3449-7.98530.28661680.22723125X-RAY DIFFRACTION100
7.9853-42.50990.23171390.19413256X-RAY DIFFRACTION99
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)
14.39060.88840.69573.0593-0.59392.1627-0.35520.26450.2765-0.22350.2243-0.0609-0.46530.1520.14250.6904-0.2076-0.02710.35330.0160.42317.670456.022722.3377
25.29810.19332.1397-0.26650.00270.894-0.15310.73510.178-0.27550.11110.225-0.03980.07240.05940.9959-0.3319-0.21240.76450.1530.8212-27.346248.12631.3003
32.7018-0.76381.26823.2187-1.31989.0208-0.2405-0.15660.0558-0.05110.19710.33810.26840.4128-0.07590.7898-0.0566-0.1890.5470.06770.7545-51.824942.508421.8435
44.9222-2.07893.26053.2128-2.12246.7644-0.155-0.4131-0.06150.43570.0949-0.03310.0388-0.03160.03210.85930.23950.04730.4727-0.0590.614-26.157936.541271.6901
58.1396-2.30665.55882.4857-2.37526.17470.29570.3559-1.289-0.59870.30980.38270.4292-0.5509-0.50621.3274-0.3053-0.13770.7164-0.0131.283-33.1362.39811.797
62.93811.4970.29893.6621-0.98720.9410.2982-0.2075-1.20580.5488-0.2607-1.00190.30110.1458-0.14280.8462-0.0059-0.01950.38710.02510.80276.771515.518734.8628
71.28740.2862-0.56934.6073-1.54022.790.09840.0834-0.8833-0.12560.157-0.81960.27550.4518-0.23550.691-0.0766-0.0120.4161-0.00941.062518.391727.144831.7473
83.84183.39520.07654.78990.85940.0008-0.0753-0.2195-0.50220.0282-0.0898-0.280.3084-0.09670.16670.9226-0.0438-0.01310.38130.07950.7074-3.833118.65133.7582
92.18-3.26911.68453.2293-2.70612.10990.68092.6311-0.2506-1.6997-0.64010.43641.30270.2625-0.01452.0135-0.3861-0.12962.032-0.07131.0894-30.5697.8594-2.3379
106.0040.25622.83392.6982.0843.5831-0.65970.7280.9211-0.9438-0.14951.0887-0.171-0.02590.80491.2157-0.2304-0.25020.86460.06571.3107-38.530124.407115.2156
114.3504-6.79944.58942.2259-6.56264.3707-0.1708-0.335-0.007-0.41410.2678-1.37930.1384-0.4051-0.16120.9494-0.0260.03840.5691-0.03821.0607-18.548217.32858.9574
123.2282.30510.87591.69691.94665.7685-0.0670.1901-0.070.14720.1623-0.70190.01350.6996-0.17421.32790.2755-0.04870.58090.08421.2316-7.549415.236268.4775
130.1995-0.4275-1.37641.18153.56861.99720.63490.46840.18020.8019-0.339-0.2921-0.21920.8305-0.12973.05410.6199-0.87021.8254-0.44012.123427.436947.189961.8913
140.55141.0101-0.12492.0306-0.3060.05020.0147-2.03551.38811.3349-1.56112.1458-1.51021.54511.28855.26851.3106-0.80644.1225-1.61952.730915.933146.435478.4304
159.2787-4.19878.90622.066-6.53892.0855-0.2749-1.80380.71751.9619-1.0808-1.11842.79970.85851.37042.3062-0.0045-0.03171.6258-0.12151.096818.644546.668860.1587
162.0047-1.54764.34227.5854.47419.3371-0.86022.18213.784-1.6325-1.8395-0.3513-2.61040.56922.54972.8450.3147-0.1911.79210.2552.397816.317828.873268.6822
176.658-6.7997-1.63077.60714.01538.55130.5768-1.3693-0.69122.2399-1.69172.71451.51241.72171.11221.9604-0.17820.47991.4019-0.02121.162713.278548.299662.6235
186.87844.408-0.67433.8529-3.45569.03280.4175-0.4821-0.0227-1.2215-1.4617-1.51834.04372.97251.10772.13610.47410.34133.05730.91161.962314.596336.336876.4496
196.0018-3.1645-5.80471.66283.04845.6361-0.1676-3.373-0.21992.73050.6362-1.07772.94590.4031-0.52293.0997-0.9451-0.06372.5867-0.36141.07519.630940.149961.7817
207.0362-5.0136-7.14674.76476.56569.1199-0.2013-1.86191.18582.088-0.4101-2.74863.65071.08010.43151.5795-0.1504-0.37930.74290.13591.219420.823541.561648.3461
21-0.0149-0.0151-0.0129-0.0195-0.0095-0.00541.8068-2.1859-0.11721.17080.30770.0987-5.36890.7216-1.84472.48790.14580.79883.61460.6441.681423.869238.868873.2168
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 320 )
2X-RAY DIFFRACTION2chain 'A' and (resid 321 through 590 )
3X-RAY DIFFRACTION3chain 'A' and (resid 591 through 729 )
4X-RAY DIFFRACTION4chain 'A' and (resid 730 through 956 )
5X-RAY DIFFRACTION5chain 'B' and (resid 5 through 75 )
6X-RAY DIFFRACTION6chain 'B' and (resid 76 through 169 )
7X-RAY DIFFRACTION7chain 'B' and (resid 170 through 278 )
8X-RAY DIFFRACTION8chain 'B' and (resid 279 through 423 )
9X-RAY DIFFRACTION9chain 'B' and (resid 424 through 462 )
10X-RAY DIFFRACTION10chain 'B' and (resid 463 through 588 )
11X-RAY DIFFRACTION11chain 'B' and (resid 589 through 630 )
12X-RAY DIFFRACTION12chain 'B' and (resid 631 through 690 )
13X-RAY DIFFRACTION13chain 'C' and (resid 1417 through 1425 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1426 through 1433 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1434 through 1452 )
16X-RAY DIFFRACTION16chain 'C' and (resid 1453 through 1461 )
17X-RAY DIFFRACTION17chain 'C' and (resid 1462 through 1473 )
18X-RAY DIFFRACTION18chain 'C' and (resid 1474 through 1483 )
19X-RAY DIFFRACTION19chain 'C' and (resid 1484 through 1490 )
20X-RAY DIFFRACTION20chain 'C' and (resid 1491 through 1502 )
21X-RAY DIFFRACTION21chain 'C' and (resid 1503 through 1509 )

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