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- PDB-7q5w: The tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM ... -

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Basic information

Entry
Database: PDB / ID: 7q5w
TitleThe tandem SH2 domains of SYK with a bound TYROBP diphospho-ITAM peptide
Components
  • TYRO protein tyrosine kinase-binding protein
  • Tyrosine-protein kinase SYK
KeywordsTRANSFERASE / Signalling / kinase
Function / homology
Function and homology information


myeloid leukocyte activation / positive regulation of receptor localization to synapse / stimulatory killer cell immunoglobulin-like receptor signaling pathway / natural killer cell mediated immunity / positive regulation of macrophage fusion / microglial cell activation involved in immune response / positive regulation of osteoclast development / negative regulation of transforming growth factor beta1 production / positive regulation of natural killer cell activation / positive regulation of microglial cell mediated cytotoxicity ...myeloid leukocyte activation / positive regulation of receptor localization to synapse / stimulatory killer cell immunoglobulin-like receptor signaling pathway / natural killer cell mediated immunity / positive regulation of macrophage fusion / microglial cell activation involved in immune response / positive regulation of osteoclast development / negative regulation of transforming growth factor beta1 production / positive regulation of natural killer cell activation / positive regulation of microglial cell mediated cytotoxicity / Other semaphorin interactions / T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell / interleukin-15 receptor binding / regulation of superoxide anion generation / regulation of neutrophil degranulation / regulation of arachidonate secretion / positive regulation of interleukin-3 production / cellular response to lectin / B cell receptor complex / Toll-like receptor binding / regulation of platelet aggregation / positive regulation of alpha-beta T cell proliferation / serotonin secretion by platelet / leukocyte activation involved in immune response / neutrophil activation involved in immune response / lymph vessel development / positive regulation of mast cell degranulation / gamma-delta T cell differentiation / positive regulation of mast cell cytokine production / collagen-activated tyrosine kinase receptor signaling pathway / positive regulation of gamma-delta T cell differentiation / cell surface pattern recognition receptor signaling pathway / regulation of platelet activation / cell activation / beta selection / cellular response to molecule of fungal origin / FLT3 signaling through SRC family kinases / early phagosome / leukotriene biosynthetic process / regulation of phagocytosis / regulation of DNA-binding transcription factor activity / regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of protein localization to cell surface / macrophage activation involved in immune response / interleukin-3-mediated signaling pathway / positive regulation of bone resorption / positive regulation of monocyte chemotactic protein-1 production / cellular response to lipid / Fc epsilon receptor (FCERI) signaling / Interleukin-2 signaling / positive regulation of granulocyte macrophage colony-stimulating factor production / positive regulation of alpha-beta T cell differentiation / blood vessel morphogenesis / positive regulation of cell adhesion mediated by integrin / Signal regulatory protein family interactions / apoptotic cell clearance / positive regulation of B cell differentiation / negative regulation of type I interferon production / leukocyte cell-cell adhesion / T cell receptor complex / mast cell degranulation / negative regulation of interleukin-10 production / negative regulation of B cell proliferation / Dectin-2 family / positive regulation of interleukin-4 production / Fc-epsilon receptor signaling pathway / stimulatory C-type lectin receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / forebrain development / amyloid-beta clearance / semaphorin-plexin signaling pathway / positive regulation of interleukin-10 production / negative regulation of long-term synaptic potentiation / positive regulation of receptor internalization / FCGR activation / cellular response to low-density lipoprotein particle stimulus / Role of LAT2/NTAL/LAB on calcium mobilization / positive regulation of type I interferon production / Role of phospholipids in phagocytosis / cellular defense response / phosphatase binding / regulation of ERK1 and ERK2 cascade / response to axon injury / phospholipase binding / GPVI-mediated activation cascade / Signaling by CSF3 (G-CSF) / positive regulation of superoxide anion generation / phosphotyrosine residue binding / neutrophil chemotaxis / positive regulation of interleukin-12 production / Integrin signaling / positive regulation of TORC1 signaling / FCERI mediated Ca+2 mobilization / SH2 domain binding / positive regulation of calcium-mediated signaling / FCGR3A-mediated IL10 synthesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / osteoclast differentiation / peptidyl-tyrosine phosphorylation / secretory granule membrane
Similarity search - Function
TYRO protein tyrosine kinase-binding protein / Tyrosine-protein kinase, non-receptor SYK/ZAP-70 / Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily / SYK/ZAP-70, N-terminal SH2 domain / : / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily ...TYRO protein tyrosine kinase-binding protein / Tyrosine-protein kinase, non-receptor SYK/ZAP-70 / Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily / SYK/ZAP-70, N-terminal SH2 domain / : / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE / DI(HYDROXYETHYL)ETHER / PHOSPHATE ION / TYRO protein tyrosine kinase-binding protein / Tyrosine-protein kinase SYK
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsBradshaw, W.J. / Katis, V.L. / Chen, Z. / Bountra, C. / von Delft, F. / Gileadi, O. / Brennan, P.E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)5U54AG065187-03 United States
CitationJournal: Structure / Year: 2024
Title: The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures.
Authors: Bradshaw, W.J. / Harris, G. / Gileadi, O. / Katis, V.L.
History
DepositionNov 4, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 24, 2021Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Derived calculations / Refinement description
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z ..._atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Oct 30, 2024Group: Database references / Structure summary
Category: citation / citation_author ...citation / citation_author / pdbx_entry_details / pdbx_modification_feature
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _pdbx_entry_details.has_protein_modification
Revision 1.3Jan 29, 2025Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AAA: Tyrosine-protein kinase SYK
BBB: Tyrosine-protein kinase SYK
CCC: Tyrosine-protein kinase SYK
DDD: Tyrosine-protein kinase SYK
EEE: Tyrosine-protein kinase SYK
FFF: Tyrosine-protein kinase SYK
GGG: TYRO protein tyrosine kinase-binding protein
HHH: TYRO protein tyrosine kinase-binding protein
III: TYRO protein tyrosine kinase-binding protein
JJJ: TYRO protein tyrosine kinase-binding protein
KKK: TYRO protein tyrosine kinase-binding protein
LLL: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)195,40823
Polymers194,38412
Non-polymers1,02411
Water5,459303
1
AAA: Tyrosine-protein kinase SYK
JJJ: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5544
Polymers32,3972
Non-polymers1572
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2280 Å2
ΔGint-13 kcal/mol
Surface area14620 Å2
MethodPISA
2
BBB: Tyrosine-protein kinase SYK
LLL: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5544
Polymers32,3972
Non-polymers1572
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2680 Å2
ΔGint-9 kcal/mol
Surface area14950 Å2
MethodPISA
3
CCC: Tyrosine-protein kinase SYK
KKK: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5984
Polymers32,3972
Non-polymers2012
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2250 Å2
ΔGint-12 kcal/mol
Surface area14580 Å2
MethodPISA
4
DDD: Tyrosine-protein kinase SYK
GGG: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5544
Polymers32,3972
Non-polymers1572
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2500 Å2
ΔGint-12 kcal/mol
Surface area14610 Å2
MethodPISA
5
EEE: Tyrosine-protein kinase SYK
III: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6554
Polymers32,3972
Non-polymers2572
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2280 Å2
ΔGint-14 kcal/mol
Surface area14360 Å2
MethodPISA
6
FFF: Tyrosine-protein kinase SYK
HHH: TYRO protein tyrosine kinase-binding protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4923
Polymers32,3972
Non-polymers951
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2310 Å2
ΔGint-14 kcal/mol
Surface area14710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)117.949, 131.928, 141.526
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11AAA
21BBB
32AAA
42CCC
53AAA
63DDD
74AAA
84EEE
95AAA
105FFF
116BBB
126CCC
137BBB
147DDD
158BBB
168EEE
179BBB
189FFF
1910CCC
2010DDD
2111CCC
2211EEE
2312CCC
2412FFF
2513DDD
2613EEE
2714DDD
2814FFF
2915EEE
3015FFF
3116GGG
3216HHH
3317GGG
3417III
3518GGG
3618JJJ
3719GGG
3819KKK
3920GGG
4020LLL
4121HHH
4221III
4322HHH
4422JJJ
4523HHH
4623KKK
4724HHH
4824LLL
4925III
5025JJJ
5126III
5226KKK
5327III
5427LLL
5528JJJ
5628KKK
5729JJJ
5829LLL
5930KKK
6030LLL

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSERILEILEAAAA9 - 2625 - 258
221SERSERILEILEBBBB9 - 2625 - 258
332SERSERGLNGLNAAAA9 - 2605 - 256
442SERSERGLNGLNCCCC9 - 2605 - 256
553SERSERLYSLYSAAAA9 - 2615 - 257
663SERSERLYSLYSDDDD9 - 2615 - 257
774SERSERILEILEAAAA9 - 2625 - 258
884SERSERILEILEEEEE9 - 2625 - 258
995SERSERLYSLYSAAAA9 - 2615 - 257
10105SERSERLYSLYSFFFF9 - 2615 - 257
11116SERSERGLNGLNBBBB9 - 2605 - 256
12126SERSERGLNGLNCCCC9 - 2605 - 256
13137SERSERLYSLYSBBBB9 - 2615 - 257
14147SERSERLYSLYSDDDD9 - 2615 - 257
15158SERSERILEILEBBBB9 - 2625 - 258
16168SERSERILEILEEEEE9 - 2625 - 258
17179SERSERLYSLYSBBBB9 - 2615 - 257
18189SERSERLYSLYSFFFF9 - 2615 - 257
191910ASPASPGLNGLNCCCC8 - 2604 - 256
202010ASPASPGLNGLNDDDD8 - 2604 - 256
212111SERSERGLNGLNCCCC9 - 2605 - 256
222211SERSERGLNGLNEEEE9 - 2605 - 256
232312ASPASPGLNGLNCCCC8 - 2604 - 256
242412ASPASPGLNGLNFFFF8 - 2604 - 256
252513SERSERLYSLYSDDDD9 - 2615 - 257
262613SERSERLYSLYSEEEE9 - 2615 - 257
272714ASPASPLYSLYSDDDD8 - 2614 - 257
282814ASPASPLYSLYSFFFF8 - 2614 - 257
292915SERSERLYSLYSEEEE9 - 2615 - 257
303015SERSERLYSLYSFFFF9 - 2615 - 257
313116PROPROLEULEUGGGG90 - 1053 - 18
323216PROPROLEULEUHHHH90 - 1053 - 18
333317PROPROLEULEUGGGG90 - 1053 - 18
343417PROPROLEULEUIIII90 - 1053 - 18
353518PROPROLEULEUGGGG90 - 1053 - 18
363618PROPROLEULEUJJJJ90 - 1053 - 18
373719PROPROLEULEUGGGG90 - 1053 - 18
383819PROPROLEULEUKKKK90 - 1053 - 18
393920PROPROASNASNGGGG90 - 1063 - 19
404020PROPROASNASNLLLL90 - 1063 - 19
414121PROPROASNASNHHHH90 - 1063 - 19
424221PROPROASNASNIIII90 - 1063 - 19
434322PROPROLEULEUHHHH90 - 1053 - 18
444422PROPROLEULEUJJJJ90 - 1053 - 18
454523PROPROASNASNHHHH90 - 1063 - 19
464623PROPROASNASNKKKK90 - 1063 - 19
474724PROPROLEULEUHHHH90 - 1053 - 18
484824PROPROLEULEULLLL90 - 1053 - 18
494925PROPROLEULEUIIII90 - 1053 - 18
505025PROPROLEULEUJJJJ90 - 1053 - 18
515126PROPROASNASNIIII90 - 1063 - 19
525226PROPROASNASNKKKK90 - 1063 - 19
535327PROPROLEULEUIIII90 - 1053 - 18
545427PROPROLEULEULLLL90 - 1053 - 18
555528PROPROLEULEUJJJJ90 - 1053 - 18
565628PROPROLEULEUKKKK90 - 1053 - 18
575729SERSERLEULEUJJJJ89 - 1052 - 18
585829SERSERLEULEULLLL89 - 1052 - 18
595930PROPROLEULEUKKKK90 - 1053 - 18
606030PROPROLEULEULLLL90 - 1053 - 18

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42
22Local NCS retraints between domains: 43 44
23Local NCS retraints between domains: 45 46
24Local NCS retraints between domains: 47 48
25Local NCS retraints between domains: 49 50
26Local NCS retraints between domains: 51 52
27Local NCS retraints between domains: 53 54
28Local NCS retraints between domains: 55 56
29Local NCS retraints between domains: 57 58
30Local NCS retraints between domains: 59 60

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Components

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Protein / Protein/peptide , 2 types, 12 molecules AAABBBCCCDDDEEEFFFGGGHHHIIIJJJKKKLLL

#1: Protein
Tyrosine-protein kinase SYK / Spleen tyrosine kinase / p72-Syk


Mass: 29906.971 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SYK / Plasmid: pNIC28-Bsa7 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P43405, non-specific protein-tyrosine kinase
#2: Protein/peptide
TYRO protein tyrosine kinase-binding protein / DNAX-activation protein 12 / Killer-activating receptor-associated protein / KAR-associated protein


Mass: 2490.357 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: O43914

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Non-polymers , 5 types, 314 molecules

#3: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: C2H6O2
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical ChemComp-P4G / 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE


Mass: 162.227 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 303 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.93 Å3/Da / Density % sol: 58.01 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jun 27, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.2→65.96 Å / Num. obs: 112454 / % possible obs: 100 % / Redundancy: 24.2 % / CC1/2: 0.999 / Rmerge(I) obs: 0.132 / Rpim(I) all: 0.039 / Rrim(I) all: 0.137 / Χ2: 0.69 / Net I/σ(I): 14
Reflection shellResolution: 2.2→2.24 Å / Redundancy: 25.8 % / Rmerge(I) obs: 4.191 / Mean I/σ(I) obs: 0.8 / Num. unique obs: 5513 / CC1/2: 0.571 / Rpim(I) all: 1.195 / Rrim(I) all: 4.259 / Χ2: 0.51 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1A81

1a81


Resolution: 2.2→65.96 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.931 / SU B: 9.193 / SU ML: 0.214 / Cross valid method: FREE R-VALUE / ESU R: 0.253 / ESU R Free: 0.206
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2663 2018 1.796 %
Rwork0.2336 110340 -
all0.234 --
obs-112358 99.986 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 61.064 Å2
Baniso -1Baniso -2Baniso -3
1-1.15 Å2-0 Å2-0 Å2
2---3.288 Å20 Å2
3---2.138 Å2
Refinement stepCycle: LAST / Resolution: 2.2→65.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13148 0 60 303 13511
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01313498
X-RAY DIFFRACTIONr_bond_other_d0.0010.01512666
X-RAY DIFFRACTIONr_angle_refined_deg1.421.64818215
X-RAY DIFFRACTIONr_angle_other_deg1.2071.58429210
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.0951625
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.02722.592737
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.967152367
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8331584
X-RAY DIFFRACTIONr_chiral_restr0.0610.21654
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0215252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023152
X-RAY DIFFRACTIONr_nbd_refined0.2030.22258
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1730.211077
X-RAY DIFFRACTIONr_nbtor_refined0.1610.26217
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0740.26778
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.170.2363
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.1260.26
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1330.233
X-RAY DIFFRACTIONr_nbd_other0.2130.2156
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1490.27
X-RAY DIFFRACTIONr_mcbond_it5.0766.226530
X-RAY DIFFRACTIONr_mcbond_other5.0746.2196529
X-RAY DIFFRACTIONr_mcangle_it7.5779.3168142
X-RAY DIFFRACTIONr_mcangle_other7.5779.3178143
X-RAY DIFFRACTIONr_scbond_it5.1546.6846968
X-RAY DIFFRACTIONr_scbond_other5.1546.6856969
X-RAY DIFFRACTIONr_scangle_it7.9339.80810072
X-RAY DIFFRACTIONr_scangle_other7.9339.80910073
X-RAY DIFFRACTIONr_lrange_it10.65569.87514099
X-RAY DIFFRACTIONr_lrange_other10.66169.87514070
X-RAY DIFFRACTIONr_ncsr_local_group_10.0840.057873
X-RAY DIFFRACTIONr_ncsr_local_group_20.090.057708
X-RAY DIFFRACTIONr_ncsr_local_group_30.0850.057807
X-RAY DIFFRACTIONr_ncsr_local_group_40.0980.057717
X-RAY DIFFRACTIONr_ncsr_local_group_50.090.057737
X-RAY DIFFRACTIONr_ncsr_local_group_60.0880.057697
X-RAY DIFFRACTIONr_ncsr_local_group_70.0940.057789
X-RAY DIFFRACTIONr_ncsr_local_group_80.0940.057763
X-RAY DIFFRACTIONr_ncsr_local_group_90.0910.057770
X-RAY DIFFRACTIONr_ncsr_local_group_100.0710.057918
X-RAY DIFFRACTIONr_ncsr_local_group_110.0940.057695
X-RAY DIFFRACTIONr_ncsr_local_group_120.0980.057732
X-RAY DIFFRACTIONr_ncsr_local_group_130.0950.057753
X-RAY DIFFRACTIONr_ncsr_local_group_140.0970.057759
X-RAY DIFFRACTIONr_ncsr_local_group_150.0910.057820
X-RAY DIFFRACTIONr_ncsr_local_group_160.1360.05343
X-RAY DIFFRACTIONr_ncsr_local_group_170.1060.05353
X-RAY DIFFRACTIONr_ncsr_local_group_180.140.05345
X-RAY DIFFRACTIONr_ncsr_local_group_190.1170.05335
X-RAY DIFFRACTIONr_ncsr_local_group_200.1470.05361
X-RAY DIFFRACTIONr_ncsr_local_group_210.1610.05367
X-RAY DIFFRACTIONr_ncsr_local_group_220.1360.05345
X-RAY DIFFRACTIONr_ncsr_local_group_230.1920.05340
X-RAY DIFFRACTIONr_ncsr_local_group_240.1640.05335
X-RAY DIFFRACTIONr_ncsr_local_group_250.130.05345
X-RAY DIFFRACTIONr_ncsr_local_group_260.1590.05350
X-RAY DIFFRACTIONr_ncsr_local_group_270.1290.05343
X-RAY DIFFRACTIONr_ncsr_local_group_280.1590.05328
X-RAY DIFFRACTIONr_ncsr_local_group_290.1970.05354
X-RAY DIFFRACTIONr_ncsr_local_group_300.1230.05334
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AAAX-RAY DIFFRACTIONLocal ncs0.084110.05009
12BBBX-RAY DIFFRACTIONLocal ncs0.084110.05009
23AAAX-RAY DIFFRACTIONLocal ncs0.089510.05009
24CCCX-RAY DIFFRACTIONLocal ncs0.089510.05009
35AAAX-RAY DIFFRACTIONLocal ncs0.08470.05009
36DDDX-RAY DIFFRACTIONLocal ncs0.08470.05009
47AAAX-RAY DIFFRACTIONLocal ncs0.09820.05009
48EEEX-RAY DIFFRACTIONLocal ncs0.09820.05009
59AAAX-RAY DIFFRACTIONLocal ncs0.089940.05009
510FFFX-RAY DIFFRACTIONLocal ncs0.089940.05009
611BBBX-RAY DIFFRACTIONLocal ncs0.087640.05009
612CCCX-RAY DIFFRACTIONLocal ncs0.087640.05009
713BBBX-RAY DIFFRACTIONLocal ncs0.094030.05009
714DDDX-RAY DIFFRACTIONLocal ncs0.094030.05009
815BBBX-RAY DIFFRACTIONLocal ncs0.093660.05009
816EEEX-RAY DIFFRACTIONLocal ncs0.093660.05009
917BBBX-RAY DIFFRACTIONLocal ncs0.091020.05009
918FFFX-RAY DIFFRACTIONLocal ncs0.091020.05009
1019CCCX-RAY DIFFRACTIONLocal ncs0.070570.05009
1020DDDX-RAY DIFFRACTIONLocal ncs0.070570.05009
1121CCCX-RAY DIFFRACTIONLocal ncs0.093710.05009
1122EEEX-RAY DIFFRACTIONLocal ncs0.093710.05009
1223CCCX-RAY DIFFRACTIONLocal ncs0.097960.05009
1224FFFX-RAY DIFFRACTIONLocal ncs0.097960.05009
1325DDDX-RAY DIFFRACTIONLocal ncs0.094970.05009
1326EEEX-RAY DIFFRACTIONLocal ncs0.094970.05009
1427DDDX-RAY DIFFRACTIONLocal ncs0.097190.05009
1428FFFX-RAY DIFFRACTIONLocal ncs0.097190.05009
1529EEEX-RAY DIFFRACTIONLocal ncs0.091130.05009
1530FFFX-RAY DIFFRACTIONLocal ncs0.091130.05009
1631GGGX-RAY DIFFRACTIONLocal ncs0.135670.05008
1632HHHX-RAY DIFFRACTIONLocal ncs0.135670.05008
1733GGGX-RAY DIFFRACTIONLocal ncs0.105890.05008
1734IIIX-RAY DIFFRACTIONLocal ncs0.105890.05008
1835GGGX-RAY DIFFRACTIONLocal ncs0.140040.05007
1836JJJX-RAY DIFFRACTIONLocal ncs0.140040.05007
1937GGGX-RAY DIFFRACTIONLocal ncs0.117270.05006
1938KKKX-RAY DIFFRACTIONLocal ncs0.117270.05006
2039GGGX-RAY DIFFRACTIONLocal ncs0.146760.05007
2040LLLX-RAY DIFFRACTIONLocal ncs0.146760.05007
2141HHHX-RAY DIFFRACTIONLocal ncs0.161230.05008
2142IIIX-RAY DIFFRACTIONLocal ncs0.161230.05008
2243HHHX-RAY DIFFRACTIONLocal ncs0.136360.05008
2244JJJX-RAY DIFFRACTIONLocal ncs0.136360.05008
2345HHHX-RAY DIFFRACTIONLocal ncs0.1920.05007
2346KKKX-RAY DIFFRACTIONLocal ncs0.1920.05007
2447HHHX-RAY DIFFRACTIONLocal ncs0.164370.05008
2448LLLX-RAY DIFFRACTIONLocal ncs0.164370.05008
2549IIIX-RAY DIFFRACTIONLocal ncs0.130330.05008
2550JJJX-RAY DIFFRACTIONLocal ncs0.130330.05008
2651IIIX-RAY DIFFRACTIONLocal ncs0.159490.05006
2652KKKX-RAY DIFFRACTIONLocal ncs0.159490.05006
2753IIIX-RAY DIFFRACTIONLocal ncs0.128660.05007
2754LLLX-RAY DIFFRACTIONLocal ncs0.128660.05007
2855JJJX-RAY DIFFRACTIONLocal ncs0.159330.05006
2856KKKX-RAY DIFFRACTIONLocal ncs0.159330.05006
2957JJJX-RAY DIFFRACTIONLocal ncs0.196590.05007
2958LLLX-RAY DIFFRACTIONLocal ncs0.196590.05007
3059KKKX-RAY DIFFRACTIONLocal ncs0.122790.05006
3060LLLX-RAY DIFFRACTIONLocal ncs0.122790.05006
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.2570.3961180.3858066X-RAY DIFFRACTION99.9756
2.257-2.3190.381550.3627879X-RAY DIFFRACTION99.9751
2.319-2.3860.3561390.3297680X-RAY DIFFRACTION99.9872
2.386-2.460.3781350.3027449X-RAY DIFFRACTION99.9736
2.46-2.540.3231030.2917213X-RAY DIFFRACTION99.9727
2.54-2.6290.2951230.2927014X-RAY DIFFRACTION100
2.629-2.7280.321270.2636749X-RAY DIFFRACTION100
2.728-2.840.2851170.2476482X-RAY DIFFRACTION99.9848
2.84-2.9660.3431040.2696255X-RAY DIFFRACTION100
2.966-3.110.319930.296007X-RAY DIFFRACTION100
3.11-3.2790.317840.2685734X-RAY DIFFRACTION100
3.279-3.4770.3211130.2615386X-RAY DIFFRACTION100
3.477-3.7170.2981160.255046X-RAY DIFFRACTION100
3.717-4.0140.291100.2234730X-RAY DIFFRACTION100
4.014-4.3970.184920.1834378X-RAY DIFFRACTION100
4.397-4.9140.184880.173969X-RAY DIFFRACTION100
4.914-5.6720.247720.193520X-RAY DIFFRACTION100
5.672-6.9410.226580.1933019X-RAY DIFFRACTION100
6.941-9.790.174470.1512373X-RAY DIFFRACTION100
9.79-65.960.196240.1961391X-RAY DIFFRACTION99.5778

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