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- PDB-3ze0: Integrin alphaIIB beta3 headpiece and RGD peptide complex -

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Basic information

Entry
Database: PDB / ID: 3ze0
TitleIntegrin alphaIIB beta3 headpiece and RGD peptide complex
Components
  • 10E5 FAB HEAVY CHAIN
  • 10E5 FAB LIGHT CHAIN
  • INTEGRIN ALPHA-IIB
  • INTEGRIN BETA-3Integrin beta 3
  • RGD PEPTIDEArginylglycylaspartic acid
KeywordsCELL ADHESION/IMMUNE SYSTEM/PEPTIDE / CELL ADHESION-IMMUNE SYSTEM-PEPTIDE 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 / positive regulation of glomerular mesangial cell proliferation / regulation of extracellular matrix organization ...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 / positive regulation of glomerular mesangial cell proliferation / regulation of extracellular matrix organization / platelet alpha granule membrane / 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 / cell-substrate junction assembly / regulation of release of sequestered calcium ion into cytosol / mesodermal cell differentiation / alphav-beta3 integrin-IGF-1-IGF1R complex / angiogenesis involved in wound healing / 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 / integrin complex / positive regulation of cell adhesion mediated by integrin / Molecules associated with elastic fibres / cellular response to insulin-like growth factor stimulus / positive regulation of leukocyte migration / positive regulation of cell-matrix adhesion / cell adhesion mediated by integrin / 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 / protein disulfide isomerase activity / cell-substrate adhesion / 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 T cell migration / positive regulation of bone resorption / 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 / protein kinase C binding / positive regulation of endothelial cell migration / 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 / wound healing / MAP2K and MAPK activation / cell-cell adhesion / platelet aggregation / ruffle membrane / platelet activation / 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
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) / Integrin alpha cytoplasmic 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 2. / EGF-like domain signature 1. / Immunoglobulins / Immunoglobulin-like / Sandwich / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
: / Integrin beta-3 / Integrin alpha-IIb
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å
AuthorsZhu, J.H. / Zhu, J.Q. / Springer, T.A.
CitationJournal: J.Cell Biol. / Year: 2013
Title: Complete Integrin Headpiece Opening in Eight Steps.
Authors: Zhu, J. / Zhu, J. / Springer, T.A.
History
DepositionDec 3, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 5, 2013Provider: repository / Type: Initial release
Revision 1.1Jul 10, 2013Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / 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 / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_asym / struct_conn / struct_conn_type / 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_database_status.status_code_sf / _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 / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _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 / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 20, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms / 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-IIB
B: INTEGRIN BETA-3
C: INTEGRIN ALPHA-IIB
D: INTEGRIN BETA-3
E: 10E5 FAB HEAVY CHAIN
F: 10E5 FAB LIGHT CHAIN
H: 10E5 FAB HEAVY CHAIN
I: RGD PEPTIDE
J: RGD PEPTIDE
L: 10E5 FAB LIGHT CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)302,53836
Polymers298,58310
Non-polymers3,95526
Water5,891327
1
A: INTEGRIN ALPHA-IIB
B: INTEGRIN BETA-3
H: 10E5 FAB HEAVY CHAIN
I: RGD PEPTIDE
L: 10E5 FAB LIGHT CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,39519
Polymers149,2925
Non-polymers2,10414
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11780 Å2
ΔGint-60.1 kcal/mol
Surface area68050 Å2
MethodPISA
2
C: INTEGRIN ALPHA-IIB
D: INTEGRIN BETA-3
E: 10E5 FAB HEAVY CHAIN
F: 10E5 FAB LIGHT CHAIN
J: RGD PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)151,14317
Polymers149,2925
Non-polymers1,85112
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11910 Å2
ΔGint-57.9 kcal/mol
Surface area68130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)259.640, 144.680, 104.590
Angle α, β, γ (deg.)90.00, 90.00, 90.00
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 / GPALPHA IIB / GPIIB / PLATELET MEMBRANE GLYCOPROTEIN IIB


Mass: 49515.965 Da / Num. of mol.: 2 / Fragment: RESIDUES 32-488
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): CHO LEC 3.2.1.8 / Production host: CRICETULUS GRISEUS (Chinese hamster) / References: UniProt: P08514
#2: Protein INTEGRIN BETA-3 / Integrin beta 3 / PLATELET MEMBRANE GLYCOPROTEIN IIIA / GPIIIA


Mass: 52087.902 Da / Num. of mol.: 2 / Fragment: RESIDUES 27-498
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): CHO LEC 3.2.1.8 / Production host: CRICETULUS GRISEUS (Chinese hamster) / References: UniProt: P05106

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Protein/peptide , 1 types, 2 molecules IJ

#5: Protein/peptide RGD PEPTIDE / Arginylglycylaspartic acid


Mass: 588.593 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human)

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Antibody , 2 types, 4 molecules EHFL

#3: Antibody 10E5 FAB HEAVY CHAIN


Mass: 23766.473 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Description: HYBRIDOMA / Production host: MUS MUSCULUS (house mouse)
#4: Antibody 10E5 FAB LIGHT CHAIN


Mass: 23332.686 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Description: HYBRIDOMA / Production host: MUS MUSCULUS (house mouse)

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Sugars , 3 types, 6 molecules

#6: 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
#7: 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-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
#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: 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 , 5 types, 347 molecules

#8: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#9: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca
#10: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#12: Chemical ChemComp-CL / CHLORIDE ION / Chloride


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


Mass: 18.015 Da / Num. of mol.: 327 / 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: 3.35 Å3/Da / Density % sol: 63 % / Description: NONE
Crystal growpH: 8.9
Details: 11% 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
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID / Wavelength: 1.0332
DetectorType: MARRESEARCH / Detector: CCD
RadiationMonochromator: DOUBLE SI CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.95→50 Å / Num. obs: 83398 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 57.81 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 9.5
Reflection shellResolution: 2.95→3.03 Å / Rmerge(I) obs: 1.12 / Mean I/σ(I) obs: 1.7 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3T3P

3t3p


Resolution: 2.95→48.312 Å / SU ML: 0.36 / σ(F): 1.44 / Phase error: 23.62 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2427 1071 1.3 %
Rwork0.1847 --
obs0.1854 83331 99.59 %
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 54.143 Å2 / ksol: 0.311 e/Å3
Displacement parametersBiso mean: 103.2 Å2
Baniso -1Baniso -2Baniso -3
1--0.3776 Å20 Å20 Å2
2--3.1076 Å20 Å2
3----2.73 Å2
Refinement stepCycle: LAST / Resolution: 2.95→48.312 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20802 0 224 327 21353
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00521678
X-RAY DIFFRACTIONf_angle_d0.56629361
X-RAY DIFFRACTIONf_dihedral_angle_d12.9467860
X-RAY DIFFRACTIONf_chiral_restr0.0373272
X-RAY DIFFRACTIONf_plane_restr0.0023812
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.95-3.08420.34141480.303910150X-RAY DIFFRACTION100
3.0842-3.24680.32811230.247710194X-RAY DIFFRACTION100
3.2468-3.45020.24771370.209910153X-RAY DIFFRACTION100
3.4502-3.71650.24571350.187210271X-RAY DIFFRACTION100
3.7165-4.09030.24451470.167310221X-RAY DIFFRACTION100
4.0903-4.68180.20691480.141710324X-RAY DIFFRACTION100
4.6818-5.89690.2168910.154810441X-RAY DIFFRACTION100
5.8969-48.31870.22381420.184910506X-RAY DIFFRACTION98
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)
10.74430.0266-0.09871.60140.20540.87470.0668-0.0977-0.06770.1661-0.22380.34680.2377-0.3588-0.02490.39270.04070.1283-0.34550.14430.294951.150390.021254.154
22.16550.089-0.69160.9372-0.01861.8777-0.11120.587-0.2397-0.3933-0.1348-0.30230.51760.34410.1520.6040.25740.18030.60730.04980.243284.125586.1006117.4014
33.2877-4.3953-0.16076.0190.41040.2762-0.29840.3949-0.26880.06670.1111-1.24250.3981.12390.20080.80720.54560.04331.9356-0.10221.1807123.420887.070234.0037
43.9363-1.5127-2.73781.61681.5455.1569-0.1343-0.27680.40550.13060.328-0.64750.2051.7593-0.09920.44290.066-0.04940.90660.03690.8107101.1547106.654252.2158
51.59940.46040.03173.02890.34561.27570.0423-0.20970.24570.25770.021-0.2002-0.3150.2005-0.03980.43230.03190.1063-0.03860.02580.297868.5457117.718663.3109
67.1581.6558-3.22621.8324-1.8722.3285-0.0452-0.0057-0.1109-0.4150.0225-0.89980.46040.693-0.02230.91750.61550.14921.94110.17680.84115.639488.090118.3161
74.60732.7284-0.13535.98490.26945.3368-0.63970.3713-0.7406-0.4052-0.06151.57361.3704-1.64060.62111.0824-0.53070.0641.2639-0.1341.31114.833271.1288141.1309
80.764-0.1518-0.4670.07490.3611.9315-0.26520.94520.2214-0.60880.34610.47120.7272-0.7688-0.02120.8935-0.3928-0.26961.07410.13910.634931.515387.9498115.7802
91.1496-0.38510.58861.3996-0.40682.1983-0.08990.90960.3572-0.5847-0.01670.17920.0159-0.34360.00030.79-0.003-0.12511.22540.28630.254360.2169102.311399.5722
103.01860.3652.07266.4644.2993.97690.1565-0.4564-1.07430.1994-0.43781.52581.3694-1.57050.27280.9856-0.32560.14330.9497-0.09331.202921.640179.2394154.964
115.11640.47-1.87872.3923-1.62043.3498-0.0367-0.6431-0.22190.6745-0.09030.48410.1202-0.55210.15560.4522-0.05660.20370.7043-0.0930.615518.135196.831982.9749
125.12381.99930.56232.29861.84727.40320.0882-0.24-2.06630.45420.2019-0.08341.20060.0895-0.27780.72630.08350.10130.8140.41051.9099-14.117681.650993.1483
135.28520.3941-0.34420.4125-0.78871.5819-0.06520.24080.17940.0405-0.10891.10760.1126-0.96470.10290.4031-0.02190.10260.8396-0.18340.84486.792296.251364.5971
144.76930.8013-1.04592.76681.46474.9492-0.37320.0437-1.21580.29560.10890.20160.4086-0.47540.26240.3854-0.07460.17280.85770.2971.136-22.392193.726786.5221
151.0524-0.4403-2.03871.48521.44684.23020.04770.73960.1718-0.1474-0.0419-0.02650.3124-0.1760.10330.8090.16690.25561.83850.21620.6315114.606589.731485.4614
162.58420.0603-1.03614.30161.64891.06680.50231.4587-0.1867-0.8437-0.1857-0.7987-0.25270.3694-0.26980.94110.32590.20982.40680.08041.0059149.881781.741479.1507
172.30650.0612-0.49983.4579-0.59823.25990.0230.61490.7855-0.0172-0.0268-0.819-0.06180.6237-0.06480.61440.10020.19591.61830.22360.8675125.153699.727101.6661
182.70820.2164-1.47862.45580.83021.17550.18340.90620.4511-1.0325-0.0092-0.8269-0.1971.0589-0.27191.02090.25560.44992.27690.37711.4251154.093697.580979.5345
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 1:454 OR RESID 2004:2007)
2X-RAY DIFFRACTION2CHAIN C AND (RESID 1:454 OR RESID 2004:2007)
3X-RAY DIFFRACTION3CHAIN B AND RESID 1:57
4X-RAY DIFFRACTION4CHAIN B AND (RESID 58:107 OR RESID 354:432 OR RESID 2001:2003)
5X-RAY DIFFRACTION5CHAIN B AND RESID 109:352
6X-RAY DIFFRACTION6CHAIN B AND RESID 433:466
7X-RAY DIFFRACTION7CHAIN D AND RESID 1:57
8X-RAY DIFFRACTION8CHAIN D AND (RESID 58:107 OR RESID 354:432 OR RESID 2001:2003)
9X-RAY DIFFRACTION9CHAIN D AND RESID 109:352
10X-RAY DIFFRACTION10CHAIN D AND RESID 433:471
11X-RAY DIFFRACTION11CHAIN H AND RESID 1:119
12X-RAY DIFFRACTION12CHAIN H AND RESID 120:221
13X-RAY DIFFRACTION13CHAIN L AND RESID 1:108
14X-RAY DIFFRACTION14CHAIN L AND RESID 109:214
15X-RAY DIFFRACTION15CHAIN E AND RESID 1:119
16X-RAY DIFFRACTION16CHAIN E AND RESID 120:221
17X-RAY DIFFRACTION17CHAIN F AND RESID 1:108
18X-RAY DIFFRACTION18CHAIN F AND RESID 109:214

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