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- PDB-7tct: Integrin alaphIIBbeta3 complex with UR2922 -

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Basic information

Entry
Database: PDB / ID: 7tct
TitleIntegrin alaphIIBbeta3 complex with UR2922
Components
  • Fab heavy chainFragment antigen-binding
  • Fab light chainFragment antigen-binding
  • Integrin alpha-IIb heavy chain
  • Isoform Beta-3C of Integrin beta-3
KeywordsBLOOD CLOTTING/INHIBITOR / Complex / Inhibitor / BLOOD CLOTTING / BLOOD CLOTTING-INHIBITOR complex
Function / homology
Function and homology information


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 / regulation of postsynaptic neurotransmitter receptor diffusion trapping / alphav-beta3 integrin-vitronectin complex / maintenance of postsynaptic specialization structure / regulation of extracellular matrix organization / platelet alpha granule membrane ...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 / regulation of postsynaptic neurotransmitter receptor diffusion trapping / alphav-beta3 integrin-vitronectin complex / maintenance of postsynaptic specialization structure / regulation of extracellular matrix organization / platelet alpha granule membrane / positive regulation of glomerular mesangial cell proliferation / integrin alphav-beta3 complex / negative regulation of lipoprotein metabolic process / alphav-beta3 integrin-PKCalpha complex / fibrinogen binding / glycinergic synapse / alphav-beta3 integrin-HMGB1 complex / vascular endothelial growth factor receptor 2 binding / blood coagulation, fibrin clot formation / negative regulation of lipid transport / negative regulation of low-density lipoprotein receptor activity / Elastic fibre formation / regulation of release of sequestered calcium ion into cytosol / cell-substrate junction assembly / mesodermal cell differentiation / angiogenesis involved in wound healing / alphav-beta3 integrin-IGF-1-IGF1R complex / platelet-derived growth factor receptor binding / filopodium membrane / extracellular matrix binding / positive regulation of fibroblast migration / positive regulation of vascular endothelial growth factor receptor signaling pathway / regulation of postsynaptic neurotransmitter receptor internalization / apolipoprotein A-I-mediated signaling pathway / regulation of bone resorption / wound healing, spreading of epidermal cells / apoptotic cell clearance / heterotypic cell-cell adhesion / positive regulation of cell adhesion mediated by integrin / integrin complex / Molecules associated with elastic fibres / cellular response to insulin-like growth factor stimulus / positive regulation of leukocyte migration / cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion / smooth muscle cell migration / microvillus membrane / Syndecan interactions / negative chemotaxis / p130Cas linkage to MAPK signaling for integrins / cellular response to platelet-derived growth factor stimulus / cell-substrate adhesion / protein disulfide isomerase activity / positive regulation of smooth muscle cell migration / activation of protein kinase activity / 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 / negative regulation of lipid storage / platelet-derived growth factor receptor signaling pathway / fibronectin binding / ECM proteoglycans / positive regulation of bone resorption / positive regulation of T cell migration / Integrin cell surface interactions / coreceptor activity / negative regulation of endothelial cell apoptotic process / positive regulation of substrate adhesion-dependent cell spreading / embryo implantation / positive regulation of endothelial cell proliferation / cell adhesion molecule binding / Integrin signaling / substrate adhesion-dependent cell spreading / cell-matrix adhesion / positive regulation of endothelial cell migration / protein kinase C binding / response to activity / Signal transduction by L1 / integrin-mediated signaling pathway / regulation of actin cytoskeleton organization / positive regulation of smooth muscle cell proliferation / Signaling by high-kinase activity BRAF mutants / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / MAP2K and MAPK activation / wound healing / cell-cell adhesion / platelet aggregation / platelet activation / ruffle membrane / VEGFA-VEGFR2 Pathway / cellular response to mechanical stimulus / positive regulation of angiogenesis / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / regulation of protein localization
Similarity search - Function
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 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) / Integrin alpha cytoplasmic region / EGF-like domain, extracellular / EGF-like 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 domain superfamily / Integrin alpha, N-terminal / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1.
Similarity search - Domain/homology
Chem-I1F / Integrin beta-3 / Integrin alpha-IIb
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.501 Å
AuthorsZhu, J. / Lin, F.-Y. / Zhu, J. / Springer, T.A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL-103526 United States
CitationJournal: Cell / Year: 2022
Title: A general chemical principle for creating closure-stabilizing integrin inhibitors.
Authors: Lin, F.Y. / Li, J. / Xie, Y. / Zhu, J. / Huong Nguyen, T.T. / Zhang, Y. / Zhu, J. / Springer, T.A.
History
DepositionDec 28, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 17, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 8, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrin alpha-IIb heavy chain
B: Isoform Beta-3C of Integrin beta-3
C: Integrin alpha-IIb heavy chain
D: Isoform Beta-3C of Integrin beta-3
E: Fab heavy chain
F: Fab light chain
H: Fab heavy chain
L: Fab light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)302,72939
Polymers297,4068
Non-polymers5,32331
Water17,979998
1
A: Integrin alpha-IIb heavy chain
B: Isoform Beta-3C of Integrin beta-3
H: Fab heavy chain
L: Fab light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,52420
Polymers148,7034
Non-polymers2,82116
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Integrin alpha-IIb heavy chain
D: Isoform Beta-3C of Integrin beta-3
E: Fab heavy chain
F: Fab light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,20519
Polymers148,7034
Non-polymers2,50215
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)259.160, 143.840, 104.910
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Integrin alpha-IIb heavy chain


Mass: 49515.965 Da / Num. of mol.: 2 / Fragment: UNP Residues 32-488
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGA2B, GP2B, ITGAB / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P08514
#2: Protein Isoform Beta-3C of Integrin beta-3 / Platelet membrane glycoprotein IIIa / GPIIIa


Mass: 52087.902 Da / Num. of mol.: 2 / Fragment: UNP Residues 27-498
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB3, GP3A / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P05106

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Antibody , 2 types, 4 molecules EHFL

#3: Antibody Fab heavy chain / Fragment antigen-binding


Mass: 23766.473 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
#4: Antibody Fab light chain / Fragment antigen-binding


Mass: 23332.686 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)

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Sugars , 4 types, 6 molecules

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


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpb1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: 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: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-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.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#11: 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
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 , 6 types, 1023 molecules

#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca
#9: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: SO4
#10: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#12: Chemical ChemComp-I1F / {5-[N-(4-carbamimidoylbenzoyl)-4-nitro-L-phenylalanyl]-4,5,6,7-tetrahydro-2H-pyrazolo[4,3-c]pyridin-2-yl}acetic acid


Mass: 519.509 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H25N7O6 / Feature type: SUBJECT OF INVESTIGATION
#13: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#14: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 998 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 3.32 Å3/Da / Density % sol: 62.96 %
Crystal growTemperature: 297 K / Method: vapor diffusion, hanging drop
Details: 11-13% PEG 8000, 0.2 M Ammonium Sulfate, 0.1 M Tris-HCl, pH 8.9

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 23, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. obs: 134985 / % possible obs: 99.4 % / Redundancy: 4.7 % / Biso Wilson estimate: 42.4032868899 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 14.61
Reflection shellResolution: 2.5→2.57 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.888 / Mean I/σ(I) obs: 1.63 / Num. unique obs: 9487 / % possible all: 95.4

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NIG

3nig


Resolution: 2.501→49.28 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 23.87 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2271 2000 1.48 %
Rwork0.1951 132972 -
obs0.1955 134972 99.38 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 176.57 Å2 / Biso mean: 62.6399 Å2 / Biso min: 16.12 Å2
Refinement stepCycle: final / Resolution: 2.501→49.28 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20708 0 326 998 22032
Biso mean--79.47 46.03 -
Num. residues----2701
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00421748
X-RAY DIFFRACTIONf_angle_d0.55529533
X-RAY DIFFRACTIONf_chiral_restr0.0433278
X-RAY DIFFRACTIONf_plane_restr0.0043826
X-RAY DIFFRACTIONf_dihedral_angle_d8.75512948
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5012-2.56370.39321360.3415900295
2.5637-2.6330.33011400.30959386100
2.633-2.71050.30571430.28859505100
2.7105-2.7980.29841420.26249407100
2.798-2.8980.25411430.24699474100
2.898-3.0140.27921420.23289481100
3.014-3.15110.27661430.22469508100
3.1511-3.31720.25731430.20959467100
3.3172-3.5250.24251430.19359556100
3.525-3.79710.24471430.18069535100
3.7971-4.1790.17741450.15989575100
4.179-4.78330.16251430.13939590100
4.7833-6.02470.181460.15869649100
6.0247-49.280.19641480.1759983798
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)
11.38380.51510.53330.853-0.18671.29880.05330.18240.0894-0.1667-0.09460.3465-0.0105-0.20650.00440.35060.06960.06450.19360.01170.271246.117788.791138.8074
21.4103-0.23920.05751.06560.34170.99910.1199-0.07140.03170.2941-0.19170.22450.1517-0.201-0.03170.4501-0.01480.15050.09080.01110.24544.255492.48763.2507
30.9463-0.41710.05061.2348-0.06271.22830.0959-0.2094-0.23260.4402-0.0433-0.30270.33710.16570.89050.59620.15120.0465-0.07380.17490.199167.09980.236755.226
40.68570.13120.20160.58650.25790.5312-0.06250.0569-0.1408-0.0708-0.0791-0.11070.29680.1403-0.10320.47280.18850.1276-0.05650.06580.241660.582782.416341.3571
51.03970.7837-0.38080.6509-0.52281.22950.04710.171-0.0109-0.06620.1273-0.61860.34271.0220.00010.65290.2131-0.12071.2935-0.07460.9704113.322297.94842.7705
61.02740.75020.36042.61880.54581.18940.1587-0.17040.25150.3208-0.1163-0.0049-0.17320.3458-0.0030.5014-0.03540.10590.01430.02550.256467.5748115.765963.6563
70.5394-0.2136-0.48080.25430.23760.4258-0.02810.1055-0.17680.2456-0.0166-0.27390.38630.6296-0.00440.62220.0929-0.10330.8213-0.04440.771797.0368103.557956.2812
80.0760.0228-0.00030.0588-0.06670.08680.01760.0636-0.1271-0.2026-0.1841-0.56460.41090.12880.00010.87530.23430.07891.25980.04351.0196114.882586.976218.6823
91.5726-0.1456-0.18190.71520.32041.2601-0.2778-0.17350.14820.14980.08-0.1909-0.04190.5489-0.03880.2577-0.0099-0.03640.45290.05470.384889.901595.8419125.7651
102.00470.1999-0.03510.8131-0.11731.1524-0.25370.5181-0.2091-0.17620.0142-0.12150.26980.44390.00760.3959-0.03640.1140.53580.0230.358587.683685.3789107.8554
112.1049-0.1004-0.0631.61360.20772.06-0.4016-0.0046-0.5517-0.06050.0972-0.0130.61880.0806-0.04280.42960.01710.17810.26010.05590.382972.223778.8367126.9439
120.12140.10250.07830.12880.00430.1684-0.5591-0.0359-0.66360.03790.15560.80770.4389-0.5625-0.00020.9123-0.36430.20051.10640.05460.941814.349169.357142.2259
130.4688-0.15860.11910.34070.00420.81480.21060.21110.19740.09960.07360.27590.0449-0.6340.00680.4756-0.1405-0.12410.85020.14010.565530.164693.7917114.5711
141.4286-0.32670.91841.3697-0.24712.07410.01080.28690.2835-0.1054-0.1298-0.0062-0.286-0.0507-0.01490.3444-0.0546-0.04340.47640.09230.38360.6476103.24101.3183
150.23120.0698-0.40210.029-0.14830.7768-0.27580.1595-0.1183-0.2741-0.02-0.01761.1746-0.5167-0.02550.6983-0.3047-0.05090.91120.03290.537735.67285.957108.0534
160.3926-0.0723-0.11060.26790.30980.35940.01330.0101-0.10140.1358-0.14040.13540.13350.2258-0.00010.5755-0.1808-0.05360.71740.06090.559632.681588.2464126.1321
170.21630.15840.07290.15550.10780.0937-0.0587-0.0609-0.2840.3899-0.00450.10010.61710.091800.9516-0.13430.18010.7779-0.02380.821921.489977.7572155.9035
180.11610.108-0.23750.2176-0.17060.49910.08940.5453-0.0774-0.1291-0.04770.14380.0469-0.01680.07050.5077-0.11150.17041.54830.00510.6867118.871582.685981.9622
190.4607-0.211-0.05310.24510.11130.1592-0.0850.6545-0.0199-0.14450.0435-0.07560.0110.17991.00980.2926-0.25660.12641.34810.2060.6283111.433191.648986.9574
200.207-0.07220.08370.08750.04530.1167-0.07991.04850.0408-0.2021-0.0419-0.0467-0.02870.0816-0.06210.4367-0.13960.1331.49720.16080.5221113.10789.496486.5885
210.02230.00640.01480.01440.00960.02560.36540.1178-0.0542-0.22410.28430.08780.09660.08190.00080.71310.16520.09432.1457-0.0110.7105130.012184.164271.8601
220.0164-0.0280.00010.08540.03910.03630.04880.35860.2489-0.28790.073-0.4727-0.1581-0.30740.00010.7318-0.1180.12541.86860.17261.1079153.556784.279477.3083
230.1099-0.1234-0.18580.15320.22040.32390.1620.27580.0606-0.032-0.2157-0.1554-0.0208-0.3387-0.01750.4778-0.1896-0.00571.64780.19230.9349145.308278.513183.9041
240.1110.0398-0.0150.25020.14340.17930.19710.3602-0.2353-0.675-0.089-0.371-0.4256-0.17110.00190.683-0.001-0.0451.7640.16661.0759149.680182.109580.5536
250.003-0.00450.00130.0077-0.00190.0538-0.22060.15130.0895-0.1926-0.4556-0.1446-0.2162-0.2891-0.00010.7591-0.06880.03941.8544-0.19731.1286150.085375.246974.445
260.21870.14040.20010.82780.61380.51280.1071-0.13620.1225-0.03920.359-0.3108-0.06070.27230.97210.4431-0.2316-0.07621.37560.34260.8866130.0331102.8076100.6072
271.5047-1.1869-0.45052.48250.56370.8005-0.19280.13240.51530.08580.092-0.268-0.04290.4707-0.18660.3232-0.2269-0.06661.1920.25240.7497120.895898.3125103.8072
280.1155-0.0009-0.10760.04050.02920.1162-0.1254-0.22430.1618-0.03420.1138-0.3926-0.06530.2224-0.00010.4892-0.1822-0.00551.17070.21760.7285123.426797.568298.8691
290.1119-0.0084-0.1420.1340.11770.2669-0.08740.12920.1221-0.10590.0332-0.1128-0.0632-0.0576-0.0810.3804-0.1337-0.00491.38270.11061.1412145.447897.174699.4231
301.0091-0.96680.50913.9432-0.78490.2852-0.07080.89560.4769-1.0234-0.3664-0.59340.22930.0287-0.01960.6789-0.20680.24831.83390.33311.134152.615491.62479.646
310.15430.0872-0.02390.0495-0.01370.0037-0.06490.12620.0407-0.17520.03350.01610.0026-0.0404-0.11961.1597-0.07940.38461.9330.84211.5616153.4192104.220574.7927
320.0906-0.4927-0.23463.26980.66751.22120.21860.34420.2252-0.60720.0331-0.3086-0.2557-0.14390.04350.5232-0.16530.08651.57010.37591.202144.99593.515187.6912
330.00420.0277-0.00450.1535-0.02230.0024-0.02770.34750.0818-0.79520.1995-0.4426-0.43680.013-0.07481.1433-0.05910.40022.52420.52051.2098154.461997.18270.4459
340.018-0.0160.01840.0314-0.01350.0182-0.19480.58270.0523-0.72240.0883-0.04530.10870.2748-0.00070.99690.04530.40482.03180.33991.869160.485598.998180.6636
350.47520.1810.16170.567-0.36050.6969-0.0806-0.341-0.240.2244-0.07140.0280.1731-0.3182-0.00010.46070.11830.15560.6595-0.04910.484918.882695.29983.8595
360.10430.06230.06420.03950.03010.11050.1083-0.66160.04710.2773-0.2203-0.0872-0.19670.041800.54480.14540.12980.7751-0.04250.461124.007795.730189.0138
370.4243-0.06010.12190.2414-0.17690.1457-0.044-0.40170.04180.17150.15120.18080.0045-0.352-0.00110.43810.08420.19270.7749-0.02950.503912.657893.844884.7725
380.0534-0.0069-0.03620.04910.07670.21970.0777-0.2355-1.0420.0694-0.06860.35810.9610.3206-0.00370.88020.25550.13240.83730.21371.3513-16.00180.751792.1895
390.1950.0123-0.19350.1188-0.15760.3675-0.197-0.6708-0.44880.2582-0.150.41340.44580.0536-0.00010.67320.19090.18460.74660.12351.0972-12.057386.911489.9737
400.0839-0.04390.00760.04280.04530.1175-0.10030.0456-0.5020.10070.11880.21931.10990.32970.00351.14950.02090.16360.93540.42431.6108-17.60875.504796.1118
410.7580.0364-0.1460.008-0.0170.53-0.04880.1411-0.1145-0.1402-0.16530.4041-0.0273-0.6022-0.00380.40460.04460.10170.6867-0.15750.67356.160294.674865.7946
420.6622-0.08970.47561.20.61651.1437-0.2405-0.0762-0.51480.38440.08360.1240.35520.06680.17350.40020.06640.26050.70890.23190.9657-20.260493.022988.1516
430.1315-0.23590.05940.89420.58892.0754-0.06210.3219-0.85840.2518-0.06780.57790.6269-0.72620.19420.4235-0.00640.24680.93320.04780.9926-30.071194.693785.6715
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 67 )A1 - 67
2X-RAY DIFFRACTION2chain 'A' and (resid 68 through 296 )A68 - 296
3X-RAY DIFFRACTION3chain 'A' and (resid 297 through 373 )A297 - 373
4X-RAY DIFFRACTION4chain 'A' and (resid 374 through 453 )A374 - 453
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 111 )B1 - 111
6X-RAY DIFFRACTION6chain 'B' and (resid 112 through 339 )B112 - 339
7X-RAY DIFFRACTION7chain 'B' and (resid 340 through 431 )B340 - 431
8X-RAY DIFFRACTION8chain 'B' and (resid 432 through 466 )B432 - 466
9X-RAY DIFFRACTION9chain 'C' and (resid 1 through 92 )C1 - 92
10X-RAY DIFFRACTION10chain 'C' and (resid 93 through 304 )C93 - 304
11X-RAY DIFFRACTION11chain 'C' and (resid 305 through 453 )C305 - 453
12X-RAY DIFFRACTION12chain 'D' and (resid 1 through 53 )D1 - 53
13X-RAY DIFFRACTION13chain 'D' and (resid 54 through 121 )D54 - 121
14X-RAY DIFFRACTION14chain 'D' and (resid 122 through 339 )D122 - 339
15X-RAY DIFFRACTION15chain 'D' and (resid 340 through 403 )D340 - 403
16X-RAY DIFFRACTION16chain 'D' and (resid 404 through 432 )D404 - 432
17X-RAY DIFFRACTION17chain 'D' and (resid 433 through 471 )D433 - 471
18X-RAY DIFFRACTION18chain 'E' and (resid 1 through 17 )E1 - 17
19X-RAY DIFFRACTION19chain 'E' and (resid 18 through 64 )E18 - 64
20X-RAY DIFFRACTION20chain 'E' and (resid 65 through 112 )E65 - 112
21X-RAY DIFFRACTION21chain 'E' and (resid 113 through 125 )E113 - 125
22X-RAY DIFFRACTION22chain 'E' and (resid 126 through 151 )E126 - 151
23X-RAY DIFFRACTION23chain 'E' and (resid 152 through 171 )E152 - 171
24X-RAY DIFFRACTION24chain 'E' and (resid 172 through 205 )E172 - 205
25X-RAY DIFFRACTION25chain 'E' and (resid 206 through 219 )E206 - 219
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 18 )F1 - 18
27X-RAY DIFFRACTION27chain 'F' and (resid 19 through 75 )F19 - 75
28X-RAY DIFFRACTION28chain 'F' and (resid 76 through 102 )F76 - 102
29X-RAY DIFFRACTION29chain 'F' and (resid 103 through 113 )F103 - 113
30X-RAY DIFFRACTION30chain 'F' and (resid 114 through 144 )F114 - 144
31X-RAY DIFFRACTION31chain 'F' and (resid 145 through 155 )F145 - 155
32X-RAY DIFFRACTION32chain 'F' and (resid 156 through 174 )F156 - 174
33X-RAY DIFFRACTION33chain 'F' and (resid 175 through 197 )F175 - 197
34X-RAY DIFFRACTION34chain 'F' and (resid 198 through 214 )F198 - 214
35X-RAY DIFFRACTION35chain 'H' and (resid 1 through 64 )H1 - 64
36X-RAY DIFFRACTION36chain 'H' and (resid 65 through 83 )H65 - 83
37X-RAY DIFFRACTION37chain 'H' and (resid 84 through 125 )H84 - 125
38X-RAY DIFFRACTION38chain 'H' and (resid 126 through 168 )H126 - 168
39X-RAY DIFFRACTION39chain 'H' and (resid 169 through 190 )H169 - 190
40X-RAY DIFFRACTION40chain 'H' and (resid 191 through 219 )H191 - 219
41X-RAY DIFFRACTION41chain 'L' and (resid 1 through 113 )L1 - 113
42X-RAY DIFFRACTION42chain 'L' and (resid 114 through 188 )L114 - 188
43X-RAY DIFFRACTION43chain 'L' and (resid 189 through 214 )L189 - 214

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