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

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Basic information

Entry
Database: PDB / ID: 3zdy
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 / CELL ADHESION
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 / apoptotic cell clearance / heterotypic cell-cell adhesion / integrin complex / positive regulation of cell adhesion mediated by integrin / Molecules associated with elastic fibres / positive regulation of leukocyte migration / cellular response to insulin-like growth factor stimulus / 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 / TGF-beta receptor signaling activates SMADs / positive regulation of osteoblast proliferation / 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 / cell-matrix adhesion / Integrin signaling / substrate adhesion-dependent cell spreading / response to activity / positive regulation of endothelial cell migration / Signal transduction by L1 / integrin-mediated signaling pathway / protein kinase C binding / 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 / VEGFA-VEGFR2 Pathway / ruffle membrane / cellular response to mechanical stimulus / Signaling by RAF1 mutants / positive regulation of angiogenesis / 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 / positive regulation of fibroblast proliferation
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 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: 2.45 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 2.0Oct 25, 2017Group: Advisory / Atomic model / Derived calculations
Category: atom_site / pdbx_struct_assembly_gen ...atom_site / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_unobs_or_zero_occ_atoms
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 / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.value
Revision 3.0Jul 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_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_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 3.1Dec 20, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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)303,82350
Polymers298,58310
Non-polymers5,23940
Water15,979887
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)152,29629
Polymers149,2925
Non-polymers3,00424
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13200 Å2
ΔGint-214 kcal/mol
Surface area56980 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)151,52721
Polymers149,2925
Non-polymers2,23516
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12430 Å2
ΔGint-166 kcal/mol
Surface area56970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)257.760, 145.250, 106.060
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 , 4 types, 921 molecules

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


Mass: 96.063 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: SO4
#9: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca
#10: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#12: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 887 / 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: 23ID / Wavelength: 0.97934
DetectorType: MARRESEARCH / Detector: CCD
RadiationMonochromator: DOUBLE SI CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 2.45→50 Å / Num. obs: 146427 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 45.59 Å2 / Rmerge(I) obs: 0.2 / Net I/σ(I): 7
Reflection shellResolution: 2.45→2.51 Å / Rmerge(I) obs: 1.39 / Mean I/σ(I) obs: 1.6 / % possible all: 99.5

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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
Resolution: 2.45→49.15 Å / SU ML: 0.35 / σ(F): 1.33 / Phase error: 21.59 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2156 1015 0.7 %
Rwork0.182 --
obs0.1823 146295 99.81 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 54.514 Å2 / ksol: 0.336 e/Å3
Displacement parametersBiso mean: 77.3 Å2
Baniso -1Baniso -2Baniso -3
1-5.4654 Å20 Å20 Å2
2--2.2087 Å20 Å2
3----7.6741 Å2
Refinement stepCycle: LAST / Resolution: 2.45→49.15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20778 0 298 887 21963
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00521810
X-RAY DIFFRACTIONf_angle_d0.5729536
X-RAY DIFFRACTIONf_dihedral_angle_d12.987889
X-RAY DIFFRACTIONf_chiral_restr0.0383278
X-RAY DIFFRACTIONf_plane_restr0.0023825
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.45-2.57920.28581360.265320485X-RAY DIFFRACTION100
2.5792-2.74070.33781320.258520545X-RAY DIFFRACTION100
2.7407-2.95230.29531510.230820597X-RAY DIFFRACTION100
2.9523-3.24940.2561310.200720660X-RAY DIFFRACTION100
3.2494-3.71940.23971500.181520726X-RAY DIFFRACTION100
3.7194-4.68550.16781650.146320883X-RAY DIFFRACTION100
4.6855-49.15990.17841500.15821384X-RAY DIFFRACTION100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.5564-0.0659-0.10990.83950.26070.65080.0084-0.0179-0.04030.1082-0.03030.08390.1786-0.095-0.02150.27910.00460.0745-0.00570.0580.152250.969590.437154.7385
21.26760.0308-0.38110.6921-0.04371.5431-0.07830.0982-0.1418-0.14770.0549-0.17070.33570.40480.01470.2090.06720.07870.2445-0.02870.147884.527787.1546119.4334
34.1788-2.0559-1.78194.2741-0.34491.2173-0.09520.5302-0.4902-0.1176-0.0914-1.12860.23110.60250.27220.53120.3502-0.06911.4957-0.19340.8316123.568489.382835.1357
44.5657-1.104-2.23143.91393.62517.6004-0.0243-0.0830.21880.080.2625-0.23780.22920.8065-0.19060.17360.0569-0.08390.4778-0.080.3818101.2858108.198353.4242
50.93360.25730.09261.58910.34660.60670.0239-0.09240.18220.1320.0721-0.0679-0.18280.0647-0.03490.32130.030.0572-0.0550.00530.187667.6653118.773864.3397
62.66712.2025-1.63414.1397-1.27711.00350.28230.08-0.2975-0.79140.0213-1.1176-0.26140.3885-0.33380.59940.29450.09821.677-0.10710.6815116.008489.943519.4222
76.51422.1569-2.14965.4127-1.33912.823-0.4758-0.0445-0.7126-0.12890.0280.66050.8288-0.83140.33360.9178-0.56990.14991.1551-0.09040.569215.271270.525142.732
82.731-0.103-0.58861.9574-1.16886.5103-0.14720.5181-0.0706-0.12760.10560.06830.4874-0.98970.05610.3341-0.1923-0.02330.65880.03190.249131.20887.424117.3885
91.4381-0.42990.60570.8591-0.29812.348-0.04020.29440.2166-0.16720.06660.0297-0.1223-0.2457-0.0590.2773-0.06240.03490.28670.08780.085260.359102.6816100.6281
105.46992.4387-0.62025.92422.09285.1612-0.25070.0607-0.59760.27750.08290.38241.0904-1.12610.16730.5511-0.21460.19310.5592-0.09910.494321.624278.9521156.6558
114.10970.7522-2.01130.68930.42783.848-0.2019-0.7585-0.06330.90850.13290.25850.3731-0.10590.11230.59850.11830.19760.576-0.00880.3518.001796.537783.6955
124.42620.2042-0.82440.0507-0.29081.6905-0.3839-0.6196-1.72210.13430.10660.03090.5519-0.18220.3190.60470.17720.39090.78880.481.3877-13.708680.709994.5229
136.32511.0771-0.4050.5392-0.54021.2542-0.0630.2727-0.12150.1489-0.20390.84720.1711-0.64040.18880.29980.00660.14570.6398-0.1280.5496.367595.661565.3048
143.53010.1392-1.20521.38761.11296.3528-0.5161-0.2021-0.90720.2649-0.00770.36130.3217-0.39770.39610.34060.11950.28580.680.10580.8833-22.01492.872187.8553
152.7953-0.4782-1.66960.6173-0.16837.2664-0.01680.4165-0.0626-0.7611-0.1078-0.3281.1432-0.20610.18850.8013-0.11620.32630.7732-0.04510.5082114.812290.462387.2259
162.8510.5969-0.88792.14040.73190.69430.11790.5691-0.6374-0.14660.1743-0.92080.63861.6267-0.22561.07320.62660.20971.65910.07090.8706150.68582.436580.5665
173.40421.39070.10260.86130.1311.37490.0181-0.1160.7598-0.0239-0.2527-1.0727-0.04740.82980.15170.3518-0.11340.17290.9748-0.08640.9101125.6631100.6998103.1462
180.62530.1451-1.15022.21490.87092.710.17121.050.1833-1.03450.1869-0.976-0.62520.5884-0.4770.84220.03990.37862.00810.46651.2543154.412798.31980.9234
190.4903-0.311.60690.8696-1.11315.75250.1617-0.16030.01040.9887-0.07750.0646-0.3134-0.4684-0.03870.524-0.17880.031.143-0.18110.343553.1377110.244975.2552
207.5794-5.2984-6.59944.02034.76245.81620.49450.75470.3627-1.6915-0.7173-0.6740.59520.29490.23751.0885-0.37840.15341.42360.12590.508977.720194.950893.5591
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
19X-RAY DIFFRACTION19CHAIN I
20X-RAY DIFFRACTION20CHAIN J

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