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- PDB-4quy: yCP beta5-A49S-mutant -

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Basic information

Entry
Database: PDB / ID: 4quy
TitleyCP beta5-A49S-mutant
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis
Function / homology
Function and homology information


proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / Cross-presentation of soluble exogenous antigens (endosomes) / TNFR2 non-canonical NF-kB pathway / proteasomal ubiquitin-independent protein catabolic process / Ub-specific processing proteases / proteasome storage granule / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
Similarity search - Function
Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. ...Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 ...Probable proteasome subunit alpha type-7 / Proteasome subunit alpha type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-2 / Proteasome subunit beta type-6 / Proteasome subunit beta type-2 / Proteasome subunit beta type-3 / Proteasome subunit beta type-5 / Proteasome subunit beta type-7 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHuber, E.M. / Heinemeyer, W. / Groll, M.
CitationJournal: Structure / Year: 2015
Title: Bortezomib-Resistant Mutant Proteasomes: Structural and Biochemical Evaluation with Carfilzomib and ONX 0914.
Authors: Huber, E.M. / Heinemeyer, W. / Groll, M.
History
DepositionJul 14, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_auth_asym_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 / _struct_conn.pdbx_dist_value / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-2
B: Proteasome subunit alpha type-3
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-5
E: Proteasome subunit alpha type-6
F: Probable proteasome subunit alpha type-7
G: Proteasome subunit alpha type-1
H: Proteasome subunit beta type-2
I: Proteasome subunit beta type-3
J: Proteasome subunit beta type-4
K: Proteasome subunit beta type-5
L: Proteasome subunit beta type-6
M: Proteasome subunit beta type-7
N: Proteasome subunit beta type-1
O: Proteasome subunit alpha type-2
P: Proteasome subunit alpha type-3
Q: Proteasome subunit alpha type-4
R: Proteasome subunit alpha type-5
S: Proteasome subunit alpha type-6
T: Probable proteasome subunit alpha type-7
U: Proteasome subunit alpha type-1
V: Proteasome subunit beta type-2
W: Proteasome subunit beta type-3
X: Proteasome subunit beta type-4
Y: Proteasome subunit beta type-5
Z: Proteasome subunit beta type-6
a: Proteasome subunit beta type-7
b: Proteasome subunit beta type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)731,34838
Polymers731,08328
Non-polymers26510
Water6,900383
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119670 Å2
ΔGint-462 kcal/mol
Surface area212600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.500, 300.140, 144.190
Angle α, β, γ (deg.)90.00, 112.83, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999572, -0.002132, 0.029168), (-0.002955, -0.984876, -0.173237), (0.029096, -0.173249, 0.984448)67.22161, -288.95029, -26.0135

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Components

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Proteasome subunit alpha type- ... , 6 types, 12 molecules AOBPCQDRESGU

#1: Protein Proteasome subunit alpha type-2 / / Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / ...Macropain subunit Y7 / Multicatalytic endopeptidase complex subunit Y7 / Proteasome component Y7 / Proteinase YSCE subunit 7


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: A49S / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-3 / / Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 ...Macropain subunit Y13 / Multicatalytic endopeptidase complex subunit Y13 / Proteasome component Y13 / Proteinase YSCE subunit 13


Mass: 28748.230 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23638, proteasome endopeptidase complex
#3: Protein Proteasome subunit alpha type-4 / / Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component ...Macropain subunit PRE6 / Multicatalytic endopeptidase complex subunit PRE6 / Proteasome component PRE6 / Proteinase YSCE subunit PRE6


Mass: 28478.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40303, proteasome endopeptidase complex
#4: Protein Proteasome subunit alpha type-5 / / Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component ...Macropain subunit PUP2 / Multicatalytic endopeptidase complex subunit PUP2 / Proteasome component PUP2 / Proteinase YSCE subunit PUP2


Mass: 28649.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P32379, proteasome endopeptidase complex
#5: Protein Proteasome subunit alpha type-6 / / Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component ...Macropain subunit PRE5 / Multicatalytic endopeptidase complex subunit PRE5 / Proteasome component PRE5 / Proteinase YSCE subunit PRE5


Mass: 25634.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40302, proteasome endopeptidase complex
#7: Protein Proteasome subunit alpha type-1 / / Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7- ...Macropain subunit C7-alpha / Multicatalytic endopeptidase complex C7 / Proteasome component C7-alpha / Proteasome component Y8 / Proteinase YSCE subunit 7 / SCL1 suppressor protein


Mass: 28033.830 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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Protein , 1 types, 2 molecules FT

#6: Protein Probable proteasome subunit alpha type-7 / Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / ...Macropain subunit C1 / Multicatalytic endopeptidase complex subunit C1 / Proteasome component C1 / Proteinase YSCE subunit 1


Mass: 31575.068 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21242, proteasome endopeptidase complex

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Proteasome subunit beta type- ... , 7 types, 14 molecules HVIWJXKYLZMaNb

#8: Protein Proteasome subunit beta type-2 / PSMB2 / Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component ...Macropain subunit PUP1 / Multicatalytic endopeptidase complex subunit PUP1 / Proteasome component PUP1 / Proteinase YSCE subunit PUP1


Mass: 25114.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-3 / PSMB3 / Macropain subunit PUP3 / Multicatalytic endopeptidase complex subunit PUP3 / Proteasome component PUP3


Mass: 22627.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25451, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-4 / PSMB4 / Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 ...Macropain subunit C11 / Multicatalytic endopeptidase complex subunit C11 / Proteasome component C11 / Proteinase YSCE subunit 11


Mass: 22545.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P22141, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-5 / PSMB5 / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component ...Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component PRE2 / Proteinase YSCE subunit PRE2


Mass: 23341.248 Da / Num. of mol.: 2 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast)
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-6 / / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-7 / / Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component ...Macropain subunit PRE4 / Multicatalytic endopeptidase complex subunit PRE4 / Proteasome component PRE4 / Proteinase YSCE subunit PRE4


Mass: 27200.893 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-1 / PSMB1 / Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component ...Macropain subunit PRE3 / Multicatalytic endopeptidase complex subunit PRE3 / Proteasome component PRE3 / Proteinase YSCE subunit PRE3


Mass: 21517.186 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 3 types, 393 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#16: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#17: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 383 / 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: 3.67 Å3/Da / Density % sol: 66.52 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 14, 2013
RadiationMonochromator: LN2 COOLED FIXED-EXIT. SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→30 Å / Num. all: 257937 / Num. obs: 250973 / % possible obs: 97.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 11.7
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.481 / Mean I/σ(I) obs: 2.6 / % possible all: 97.8

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Processing

Software
NameClassification
XDSdata scaling
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 1RYP
Resolution: 2.8→15 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.933 / SU B: 31.502 / SU ML: 0.258 / Cross valid method: THROUGHOUT / ESU R Free: 0.297 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22597 12549 5 %RANDOM
Rwork0.19102 ---
obs0.19275 238424 97.39 %-
all-250973 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 65.059 Å2
Baniso -1Baniso -2Baniso -3
1-4.72 Å20 Å2-2.4 Å2
2---6.79 Å2-0 Å2
3---2.27 Å2
Refinement stepCycle: LAST / Resolution: 2.8→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49368 0 10 383 49761
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950276
X-RAY DIFFRACTIONr_bond_other_d0.0010.0248050
X-RAY DIFFRACTIONr_angle_refined_deg0.8451.96368012
X-RAY DIFFRACTIONr_angle_other_deg0.6683110652
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.14956314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.33924.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.111158760
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.67315284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27662
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0257108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211268
X-RAY DIFFRACTIONr_mcbond_it2.5855.48225346
X-RAY DIFFRACTIONr_mcbond_other2.5855.48225345
X-RAY DIFFRACTIONr_mcangle_it3.4368.20831630
X-RAY DIFFRACTIONr_mcangle_other3.4368.20831631
X-RAY DIFFRACTIONr_scbond_it2.5825.86124930
X-RAY DIFFRACTIONr_scbond_other2.5825.86124930
X-RAY DIFFRACTIONr_scangle_other3.2018.64336382
X-RAY DIFFRACTIONr_long_range_B_refined3.98242.78454389
X-RAY DIFFRACTIONr_long_range_B_other3.97142.78654346
X-RAY DIFFRACTIONr_rigid_bond_restr0.951398326
X-RAY DIFFRACTIONr_sphericity_free34.4275241
X-RAY DIFFRACTIONr_sphericity_bonded17.669597580
LS refinement shellResolution: 2.8→2.87 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.325 901 -
Rwork0.303 17117 -
obs--97.9 %
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)
10.0039-0.0095-0.00780.03220.02460.0196-0.0020.0061-0.00570.00260.0096-0.00810.0029-0.0026-0.00760.0833-0.00660.02570.1261-0.00370.129166.251-91.7645.883
20.0244-0.00880.02030.0107-0.00380.0347-0.0066-0.0084-0.0244-0.0137-0.0080.0172-0.00450.01160.01460.0815-0.00110.03740.124900.110858.803-87.46716.339
30.02550.0296-0.00190.0377-0.00230.0002-0.0044-0.0094-0.01080.00060.0039-0.00090.003-0.00030.00060.10010.00190.01160.11530.00360.12231.688-87.1061.086
40.0039-0.0008-0.0090.00030.00210.02290.0028-0.01650.0018-0.0020.00110.0044-0.02250.0327-0.00390.07350.01520.00510.09080.00910.1412.597-90.11613.622
50.0625-0.02090.01890.0107-0.01080.01390.0089-0.0119-0.01120.0067-0.0010.0191-0.00990.009-0.00790.04110.01230.04430.1174-0.00270.1259-3.656-94.57445.534
60.0073-0.00020.010.0007-0.00120.0226-0.0171-0.0006-0.0039-0.0001-0.0083-0.0001-0.01180.00650.02540.06520.00360.05660.127-0.01410.114414.771-95.16469.603
70.0036-0.0011-00.0051-0.00120.0004-0.00140.01950.00060.0147-0.0021-0.0162-0.0053-0.0010.00350.114-0.00050.01790.1084-0.0060.113747.09-93.30470.877
80.00440.00950.00430.02560.01410.00950.01660.0027-0.00350.0197-0.0042-0.02760.0029-0.0149-0.01240.07350.00330.0140.11950.00090.124967.449-129.01647.274
90.006-0.0044-0.00050.00320.0010.00560.01990.00440.0047-0.01190.001-0.0064-0.0095-0.0093-0.02090.05360.00230.05820.1451-0.00750.139368.001-126.71820.746
100.0143-0.01240.01640.1681-0.0430.0325-0.0016-0.01340.0025-0.02780.0099-0.0008-0.00760.0118-0.00820.0835-0.00090.03060.12140.00040.119344.401-126.242-0.793
110.0136-0.03490.03750.0899-0.09550.10720.001700.0029-0.0003-0.0014-0.0146-0.0150.0115-0.00030.07990.00420.00920.11470.00140.125710.755-130.7552.455
120.0036-0.0002-0.00320.0003-0.00020.00450.0102-0.01750.00650.00140.0060.0049-0.00470.0153-0.01620.0526-0.00020.03130.12650.0050.1398-4.567-134.58228.241
130.007-0.00490.00630.169-0.02170.01050.00620.00790.01150.0152-0.00560.00380.01610.0044-0.00060.05850.00230.04360.1298-0.00380.1197.677-138.00860.027
140.0012-0.0005-00.0348-0.01430.00660.01020.00790.00650.0222-0.0098-0.003-0.00370.0033-0.00040.1227-0.00530.00470.1215-0.00330.12139.608-133.88870.488
150.0044-0.0021-0.00360.00220.00210.0079-0.00820.00970.0028-0.0030.0012-0.00110.01620.010.0070.0879-0.01280.0090.10990.00340.13662.481-206.66236.589
160.0091-0.00480.02110.0043-0.01530.0596-0.00990.0126-0.00020.00160.0044-0.0027-0.0050.00490.00550.0962-0.0017-0.00040.1101-0.00310.1399.044-205.6226.575
170.00790.0004-0.00160.00090.00010.00460.005-0.0254-0.0048-0.00960.0072-0.00250.00260.0103-0.01220.11150.02220.00750.0882-0.00940.118636.032-203.5-9.214
180.0067-0.01160.00350.0484-0.0080.00230.0134-0.00940.0056-0.0466-0.0234-0.03850.0092-0.00560.01010.04720.00790.04350.1019-0.01670.104265.382-202.6463.171
190.01030.00530.00380.00390.00250.00980.0234-0.0099-0.00060.009-0.002-0.01130.0068-0.0109-0.02140.05950.01370.00850.1077-0.00710.145272.368-203.67235.112
200.00140.0004-0.00060.00030.00030.00370.00710.0024-0.00230.0034-0.0075-0.0046-0.0017-0.01660.00040.09830.0083-0.01230.08480.01140.12254.476-207.32559.291
210.0023-0-0.00020.0003-0.00050.00110.00580.01480.00440.00090.00180.00580.00320.0002-0.00760.127-0.00890.00120.10380.00420.120722.265-209.58360.867
220.0320.00140.04590.0031-0.00090.07310.0042-0.01690.01260.0013-0.00820.01780.00670.00010.0040.064-0.00310.03130.11320.00520.12381.414-170.21244.434
230.01650.0040.00920.0127-0.00030.00790.0050.0063-0.00580.01190.0005-0.00350.00630.0174-0.00550.0875-0.00040.00370.11390.00250.13890.269-167.86717.906
240.0016-0.0022-0.00020.00450.0020.00190.0016-0.0058-0.0118-0.0170.00750.0087-0.01250.0029-0.00910.10570.0032-0.00430.1096-0.0010.126223.314-164.563-3.947
250.0078-0.02350.00530.1027-0.03280.01370.0208-0.0156-0.0023-0.0651-0.00110.02990.01350.0145-0.01970.0730.00960.03730.1227-0.00870.111357.046-160.619-0.68
260.00010.0003-0.00040.0172-0.00080.0021-0.00380.00280.00120.00710.0145-0.0314-0.004-0.0158-0.01070.03290.01570.03980.1484-0.01470.150372.968-161.30925.018
270.01330.02020.00020.03290.00220.00250.00510.0075-0.00450.0127-0.0027-0.0148-0.0025-0.0164-0.00240.09670.00480.00620.11480.00130.129861.5-163.46357.167
280.00820.0249-0.00160.1434-0.00080.00070.00630.0193-0.00560.0161-0.0067-0.01110.0018-0.00840.00030.1094-0.00160.00770.11680.0040.113329.832-169.4167.517
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 310
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 312
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 312
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 316
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 309
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 310
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 421
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301 - 312
18X-RAY DIFFRACTION9I1 - 204
19X-RAY DIFFRACTION9I301
20X-RAY DIFFRACTION9I401 - 413
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 213
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301 - 302
25X-RAY DIFFRACTION11K401 - 420
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 319
28X-RAY DIFFRACTION13M1 - 233
29X-RAY DIFFRACTION13M301 - 319
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201 - 202
32X-RAY DIFFRACTION14N301 - 309
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301 - 306
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 310
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 319
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301 - 310
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301 - 308
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 312
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 413
48X-RAY DIFFRACTION22V1 - 226
49X-RAY DIFFRACTION22V301 - 310
50X-RAY DIFFRACTION23W1 - 204
51X-RAY DIFFRACTION23W301 - 315
52X-RAY DIFFRACTION24X1 - 195
53X-RAY DIFFRACTION24X201 - 212
54X-RAY DIFFRACTION25Y1 - 212
55X-RAY DIFFRACTION25Y301
56X-RAY DIFFRACTION25Y401 - 420
57X-RAY DIFFRACTION26Z1 - 222
58X-RAY DIFFRACTION26Z301
59X-RAY DIFFRACTION26Z401 - 415
60X-RAY DIFFRACTION27a1 - 233
61X-RAY DIFFRACTION27a301 - 320
62X-RAY DIFFRACTION28b1 - 196
63X-RAY DIFFRACTION28b201 - 218

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