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

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Basic information

Entry
Database: PDB / ID: 3zdz
TitleIntegrin alphaIIB beta3 headpiece and RGD peptide complex
Components
  • 10E5 FAB HEAVY CHAIN
  • 10E5 FAB LIGHT CHAIN
  • INTEGRIN ALPHA-IIB
  • INTEGRIN BETA-3
  • RGD PEPTIDE
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 / regulation of extracellular matrix organization / platelet alpha granule membrane / positive regulation of glomerular mesangial cell proliferation ...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 / 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 / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-HMGB1 complex / blood coagulation, fibrin clot formation / negative regulation of lipid transport / vascular endothelial growth factor receptor 2 binding / glycinergic synapse / negative regulation of low-density lipoprotein receptor activity / angiogenesis involved in wound healing / 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 / platelet-derived growth factor receptor binding / filopodium membrane / 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 / Molecules associated with elastic fibres / positive regulation of leukocyte migration / positive regulation of cell-matrix adhesion / cellular response to insulin-like growth factor stimulus / smooth muscle cell migration / microvillus membrane / 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 / 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 / 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 / cell adhesion molecule binding / positive regulation of endothelial cell proliferation / embryo implantation / positive regulation of endothelial cell migration / Integrin signaling / substrate adhesion-dependent cell spreading / cell-matrix adhesion / response to activity / Signal transduction by L1 / integrin-mediated signaling pathway / regulation of actin cytoskeleton organization / protein kinase C binding / positive regulation of smooth muscle cell proliferation / Signaling by high-kinase activity BRAF mutants / wound healing / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / MAP2K and MAPK activation / platelet activation / platelet aggregation / ruffle membrane / VEGFA-VEGFR2 Pathway / cell-cell adhesion / 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 / 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 / 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: 2.75 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 / _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_2 / _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)302,50834
Polymers298,58310
Non-polymers3,92524
Water9,728540
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)151,36517
Polymers149,2925
Non-polymers2,07412
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11720 Å2
ΔGint-58.7 kcal/mol
Surface area68200 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 area11680 Å2
ΔGint-57.7 kcal/mol
Surface area68230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)259.620, 144.470, 104.750
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 / 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


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) / 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) / Production host: MUS MUSCULUS (house mouse)

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Sugars , 4 types, 6 molecules

#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-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
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}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
#8: 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.: 1
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
#12: 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


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, 558 molecules

#9: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#10: Chemical
ChemComp-CA / CALCIUM ION


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


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


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


Mass: 18.015 Da / Num. of mol.: 540 / 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: 2.75→50 Å / Num. obs: 102899 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Biso Wilson estimate: 52.25 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 10.1
Reflection shellResolution: 2.75→2.82 Å / Rmerge(I) obs: 1 / Mean I/σ(I) obs: 1.8 / % possible all: 100

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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: 2.75→48.279 Å / SU ML: 0.34 / σ(F): 1.44 / Phase error: 21.88 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2211 1032 1 %
Rwork0.1844 --
obs0.1848 102822 99.81 %
Solvent computationShrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 50.516 Å2 / ksol: 0.318 e/Å3
Displacement parametersBiso mean: 91.9 Å2
Baniso -1Baniso -2Baniso -3
1--1.7084 Å20 Å20 Å2
2--2.8223 Å20 Å2
3----1.1139 Å2
Refinement stepCycle: LAST / Resolution: 2.75→48.279 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20787 0 225 540 21552
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00521662
X-RAY DIFFRACTIONf_angle_d0.59129341
X-RAY DIFFRACTIONf_dihedral_angle_d13.2737864
X-RAY DIFFRACTIONf_chiral_restr0.0383275
X-RAY DIFFRACTIONf_plane_restr0.0023807
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.75-2.8950.33861430.296514401X-RAY DIFFRACTION100
2.895-3.07630.29881470.265114432X-RAY DIFFRACTION100
3.0763-3.31380.26291550.22414383X-RAY DIFFRACTION100
3.3138-3.64720.21681510.184614486X-RAY DIFFRACTION100
3.6472-4.17470.16941410.155814552X-RAY DIFFRACTION100
4.1747-5.25860.15921420.132114648X-RAY DIFFRACTION100
5.2586-48.28630.24271530.182614888X-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)
10.5190.0508-0.03921.33940.20360.6940.0179-0.0542-0.07480.1568-0.09860.24510.1809-0.1315-0.03720.38130.03560.1297-0.07420.07930.220851.100489.920354.1631
21.61290.0014-0.38560.8020.06761.2436-0.21690.4418-0.2184-0.3239-0.0305-0.2560.42590.31390.01880.42720.13780.21250.45850.03510.153984.115685.9926117.5764
33.5276-3.8907-0.66764.29120.73640.1263-0.4052-0.2764-0.46960.14120.2862-1.36350.3761.0490.17280.75890.47170.06791.9328-0.12631.2191123.24186.901734.0174
44.48-1.0065-2.70983.5823.33927.2056-0.0038-0.22220.30830.00840.2218-0.24620.13641.2055-0.20450.26080.0742-0.05970.8060.06310.7803101.6129106.25352.1734
51.01140.279-0.0062.22030.1460.67960.0608-0.11020.20480.2643-0.0173-0.1591-0.22590.0567-0.00950.35730.00710.0949-0.00560.02270.228868.4779117.482363.4869
66.92590.7243-2.46662.0434-2.00652.43240.054-0.42840.1421-0.36880.0196-0.81850.50780.6929-0.07760.7460.4680.12321.80750.14750.723115.620587.873618.4247
76.251.2936-3.90521.9331-1.38944.2491-0.3333-0.1026-0.98470.0303-0.15761.16971.0241-1.04960.45550.9918-0.55210.17131.2339-0.09731.190914.92871.0125141.1803
81.6345-0.48640.9580.4046-0.10457.089-0.33931.04550.1863-0.3550.34030.23270.7123-0.7904-0.00130.7122-0.4513-0.12631.14840.12240.605231.155387.6757116.1529
91.2269-0.43410.46660.5168-0.28751.1485-0.21431.04130.4134-0.3310.18250.1282-0.0542-0.3675-0.12830.4929-0.1853-0.07121.09620.2840.342360.3925102.391699.6952
109.12.80843.02925.09333.53337.14880.0775-0.1869-1.05830.49520.02580.47291.1759-1.2771-0.07310.688-0.27640.13780.6868-0.05630.795721.673979.1476155.0072
114.9778-0.1314-1.69041.6506-0.92562.4496-0.0574-0.5515-0.1230.67830.02190.40020.0355-0.49210.07250.45-0.04440.21270.6301-0.10890.543618.198496.688283.0177
125.50650.75170.47990.21380.90116.31870.0691-0.2645-1.94280.33860.1141-0.03971.1772-0.0143-0.11580.65170.07920.17680.77010.36791.8206-14.044781.505993.1804
133.390.6408-0.57020.3709-0.5150.7614-0.02730.2453-0.09350.0315-0.16120.85090.1013-0.8260.03830.333-0.00580.12480.8283-0.19860.73726.84596.119264.6276
142.87780.2428-0.20741.21980.59322.4105-0.24350.0443-0.97730.1920.01270.22610.3111-0.25960.24650.3004-0.06460.16530.75940.16891.0012-22.35393.59386.5755
151.8783-0.417-2.41110.78850.74873.1613-0.01041.01640.1247-0.35890.0034-0.0950.305-0.10390.24960.69360.10330.21891.72830.1690.6586114.606189.637885.652
163.21150.4754-0.93323.53761.1390.74160.2421.0058-0.3493-0.91210.0156-0.8827-0.23610.1763-0.19230.8940.25780.2622.22990.08840.9844149.828181.624279.3824
174-0.2706-1.73772.55890.27520.9276-0.07630.0530.7098-0.14370.0619-0.86950.05330.71-0.06750.51540.04140.14651.520.22640.8326125.104799.5332101.9005
181.83040.3682-0.57792.67260.92810.6020.21040.74870.3757-1.1176-0.0349-0.9175-0.35070.6697-0.27240.94060.23460.42792.14440.40931.3099154.035497.569579.8483
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)
5X-RAY DIFFRACTION5CHAIN B AND (RESID 109:352 OR RESID 2001:2003)
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)
9X-RAY DIFFRACTION9CHAIN D AND (RESID 109:352 OR RESID 2001:2003)
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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