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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 proteinTYROBP
  • Tyrosine-protein kinase SYK
KeywordsTRANSFERASE / Signalling / kinase
Function / homology
Function and homology information


myeloid leukocyte activation / stimulatory killer cell immunoglobulin-like receptor signaling pathway / positive regulation of receptor localization to synapse / positive regulation of macrophage fusion / positive regulation of osteoclast development / microglial cell activation involved in immune response / negative regulation of transforming growth factor beta1 production / Other semaphorin interactions / positive regulation of microglial cell mediated cytotoxicity / positive regulation of natural killer cell activation ...myeloid leukocyte activation / stimulatory killer cell immunoglobulin-like receptor signaling pathway / positive regulation of receptor localization to synapse / positive regulation of macrophage fusion / positive regulation of osteoclast development / microglial cell activation involved in immune response / negative regulation of transforming growth factor beta1 production / Other semaphorin interactions / positive regulation of microglial cell mediated cytotoxicity / positive regulation of natural killer cell activation / serotonin secretion by platelet / interleukin-15 receptor binding / positive regulation of interleukin-3 production / regulation of superoxide anion generation / regulation of neutrophil degranulation / regulation of arachidonic acid secretion / cellular response to lectin / gamma-delta T cell differentiation / positive regulation of gamma-delta T cell differentiation / B cell receptor complex / Toll-like receptor binding / neutrophil activation involved in immune response / regulation of platelet aggregation / positive regulation of alpha-beta T cell proliferation / leukocyte activation involved in immune response / positive regulation of mast cell cytokine production / regulation of platelet activation / lymph vessel development / collagen-activated tyrosine kinase receptor signaling pathway / cell activation / positive regulation of mast cell degranulation / positive regulation of protein localization to cell surface / positive regulation of killing of cells of another organism / regulation of phagocytosis / beta selection / macrophage activation involved in immune response / leukotriene biosynthetic process / cellular response to molecule of fungal origin / early phagosome / FLT3 signaling through SRC family kinases / regulation of tumor necrosis factor-mediated signaling pathway / interleukin-3-mediated signaling pathway / cellular response to lipid / positive regulation of monocyte chemotactic protein-1 production / regulation of DNA-binding transcription factor activity / apoptotic cell clearance / positive regulation of granulocyte macrophage colony-stimulating factor production / positive regulation of cell adhesion mediated by integrin / Fc epsilon receptor (FCERI) signaling / Interleukin-2 signaling / positive regulation of alpha-beta T cell differentiation / blood vessel morphogenesis / Signal regulatory protein family interactions / negative regulation of type I interferon production / T cell receptor complex / positive regulation of B cell differentiation / leukocyte cell-cell adhesion / mast cell degranulation / negative regulation of interleukin-10 production / Fc-gamma receptor signaling pathway involved in phagocytosis / positive regulation of interleukin-4 production / Dectin-2 family / negative regulation of B cell proliferation / Fc-epsilon receptor signaling pathway / stimulatory C-type lectin receptor signaling pathway / phospholipase binding / positive regulation of interleukin-10 production / positive regulation of receptor internalization / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / cellular response to low-density lipoprotein particle stimulus / negative regulation of long-term synaptic potentiation / FCGR activation / response to axon injury / positive regulation of type I interferon production / phosphatase binding / positive regulation of bone resorption / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / cellular defense response / positive regulation of calcium-mediated signaling / Signaling by CSF3 (G-CSF) / forebrain development / negative regulation of inflammatory response to antigenic stimulus / GPVI-mediated activation cascade / positive regulation of TORC1 signaling / positive regulation of interleukin-12 production / phosphotyrosine residue binding / SH2 domain binding / Integrin signaling / FCERI mediated Ca+2 mobilization / B cell differentiation / neutrophil chemotaxis / FCGR3A-mediated IL10 synthesis / osteoclast differentiation / regulation of ERK1 and ERK2 cascade / positive regulation of superoxide anion generation / secretory granule membrane / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / DAP12 interactions / positive regulation of interleukin-1 beta production
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 / Tyrosine-protein kinase, catalytic domain ...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 / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / 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: To Be Published
Title: The tandem SH2 domains of SYK
Authors: Bradshaw, W.J. / Katis, V.L. / Chen, Z. / Bountra, C. / von Delft, F. / Gileadi, O. / Brennan, P.E.
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

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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 / TYROBP / 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 / Phosphate


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


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


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

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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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