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- PDB-4qvn: yCP beta5-M45V mutant in complex with bortezomib -

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Basic information

Entry
Database: PDB / ID: 4qvn
TitleyCP beta5-M45V mutant in complex with bortezomib
Components
  • (Proteasome subunit alpha type- ...) x 6
  • (Proteasome subunit beta type- ...) x 7
  • Probable proteasome subunit alpha type-7
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Cancer / Proteasome / Bortezomib / Drug Resistance / Binding Analysis / HYDROLASE-HYDROLASE INHIBITOR complex
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
Chem-BO2 / 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 ...Chem-BO2 / 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: 2.9 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 15, 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_auth_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 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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)733,60445
Polymers730,98728
Non-polymers2,61717
Water3,603200
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area124760 Å2
ΔGint-476 kcal/mol
Surface area213280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.900, 300.780, 145.160
Angle α, β, γ (deg.)90.00, 113.09, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999853, -0.00093, 0.017122), (-0.002037, -0.985016, -0.172452), (0.017025, -0.172461, 0.984869)67.53764, -289.41272, -25.62625

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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: A49T / 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: 23293.186 Da / Num. of mol.: 2
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) / Strain (production host): 4932
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 , 4 types, 217 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Mg
#16: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-BO2 / N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / BORTEZOMIB / Bortezomib


Mass: 384.237 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C19H25BN4O4 / Comment: medication, anticancer*YM
#18: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 200 / 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: Sep 7, 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: 2.9→30 Å / Num. all: 234652 / Num. obs: 225031 / % possible obs: 95.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 12.6
Reflection shellResolution: 2.9→3 Å / Rmerge(I) obs: 0.535 / Mean I/σ(I) obs: 2 / % possible all: 97.4

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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: 2.9→15 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.94 / SU B: 32.341 / SU ML: 0.255 / Cross valid method: THROUGHOUT / ESU R Free: 0.307 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21271 11252 5 %RANDOM
Rwork0.17529 ---
obs0.17716 213779 96.02 %-
all-225031 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 78.791 Å2
Baniso -1Baniso -2Baniso -3
1-5.86 Å2-0 Å20.5 Å2
2---9.12 Å2-0 Å2
3---2.23 Å2
Refinement stepCycle: LAST / Resolution: 2.9→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49364 0 179 200 49743
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01950452
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248196
X-RAY DIFFRACTIONr_angle_refined_deg0.8321.96768262
X-RAY DIFFRACTIONr_angle_other_deg0.6793.001110964
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.97256314
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.66824.4232252
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.428158748
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.71915284
X-RAY DIFFRACTIONr_chiral_restr0.0480.27688
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257252
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211322
X-RAY DIFFRACTIONr_mcbond_it3.4386.87425346
X-RAY DIFFRACTIONr_mcbond_other3.4386.87425345
X-RAY DIFFRACTIONr_mcangle_it4.61210.29531630
X-RAY DIFFRACTIONr_mcangle_other4.61210.29531631
X-RAY DIFFRACTIONr_scbond_it3.287.32525106
X-RAY DIFFRACTIONr_scbond_other3.287.32525106
X-RAY DIFFRACTIONr_scangle_other4.17210.81236632
X-RAY DIFFRACTIONr_long_range_B_refined5.22553.80554295
X-RAY DIFFRACTIONr_long_range_B_other5.22353.80854282
X-RAY DIFFRACTIONr_rigid_bond_restr0.996398648
X-RAY DIFFRACTIONr_sphericity_free29.0135152
X-RAY DIFFRACTIONr_sphericity_bonded21.155597797
LS refinement shellResolution: 2.9→2.972 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.35 816 -
Rwork0.312 15500 -
obs--97.5 %
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)
10.0492-0.0096-0.02590.00340.00640.0153-0.00910.0027-0.0107-0.00430.0065-0.0058-0.00680.00550.00260.1106-0.0091-0.01540.1039-0.00230.110966.536-92.02846.161
20.0005-0.00070.00040.0027-0.00020.00120.00260.0013-0.0067-0.0138-0.00310.00780.00170.00270.00050.1041-0.0060.00150.10180.00180.112959.365-87.89416.455
30.0027-0.001-0.00040.0015-0.00120.0017-0.0062-0.0113-0.0041-0.00130.01130.01120.0080.0022-0.0050.12680.0069-0.01040.09790.00150.097732.247-87.5391
40.0278-0.00940.03680.0118-0.01090.0598-0.00920.0004-0.0063-0.0107-0.00190.0282-0.02580.0260.0110.08870.014-0.01780.07350.0090.10572.993-90.28113.395
50.0113-0.0047-0.03060.00550.01250.0857-0.00470.0098-0.00550.0082-0.00410.02070.009-0.01150.00870.07890.012-0.0020.09650.00270.1249-3.521-94.6445.328
60.0003-0.0007-0.00010.0024-0.00040.001-0.00240.001-0.00420.0144-0.00290.0063-0.00220.00710.00530.10380.00330.01350.0932-0.010.084414.723-95.13669.636
70.0095-0.00210.00290.00190.00510.03800.02460.01070.0044-0.01010.0035-0.0046-0.00810.01010.129-0.009-0.0110.0837-0.00580.096947.106-93.40271.158
80.00250.0027-0.00330.0114-0.00190.00660.01240.0078-0.00160.0165-0.004-0.0181-0.0093-0.0181-0.00840.1024-0.0034-0.02360.0981-0.00430.108167.293-129.53947.665
90.0015-0.0116-0.00430.13460.03340.01520.00630.00680.0022-0.0187-0.0106-0.0225-0.0264-0.01280.00430.0984-0.00470.00350.10230.00070.116368.17-127.49821.056
100.0173-0.01-0.00550.0560.03040.01830.0115-0.02240.014-0.02360.0042-0.0183-0.00680.0131-0.01570.122-0.0011-0.00520.09680.00370.093444.777-126.668-0.6
110.02760.06930.02460.21230.08450.03960.0071-0.00040.0016-0.0190.0080.014-0.01430.0183-0.01510.10180.0043-0.02710.08960.0120.085310.993-131.0542.271
120.01420.01930.01920.02930.03230.05060.003-0.01160.00680.00830.00010.0077-0.01470.0182-0.00320.0850.0095-0.01590.09220.00590.1284-4.57-134.57728.319
130.0044-0.0115-0.00660.09880.03330.01390.0097-0.0040.00970.0239-0.00980.0158-0.00540.00350.00010.09920.00090.00740.0983-0.00260.11277.575-138.0760.224
140.005-0.01770.00040.09690.00280.00060.01380.0095-00.0056-0.013-0.01610.00470.0045-0.00080.125-0.0083-0.01270.1009-0.0060.076739.456-134.16170.728
150.05130.04-0.04190.0334-0.03540.0398-0.01130.01950.0004-0.01830.00630.00030.01150.00490.0050.0959-0.0113-0.02360.09110.00490.1131.819-206.80736.645
160.06640.02310.02820.0110.00720.0144-0.01370.0005-0.0012-0.014-0.0005-0.0105-0.00410.00410.01420.0971-0.0014-0.03640.0969-0.00480.10018.488-205.6916.649
170.00590.000900.00020.00010.00260.0119-0.0196-0.005-0.0013-0.0008-0.00220.0070.0066-0.01110.12230.0168-0.01640.091-0.00980.088635.85-203.604-9.113
180.0014-0.00440.00240.0141-0.00640.00830.00050.00130.0097-0.0182-0.0135-0.02540.0207-0.00110.01290.08520.02680.00460.032-0.02680.110765.096-202.9993.565
190.01630.02020.01280.02590.01780.01540.026-0.0014-0.00650.0333-0.0081-0.01590.0145-0.0165-0.01790.06750.0314-0.02410.0639-0.01580.124871.853-204.0835.5
200.00990.0043-0.00070.00260.00090.00610.02170.0013-0.01680.0134-0.0118-0.0123-0.0036-0.0192-0.010.09690.0085-0.05480.0619-0.00330.074553.833-207.79959.663
210.00310.002-0.00250.0111-0.01730.0294-0.00080.01510.00680.00820.00820.00190.0009-0.0037-0.00750.133-0.0086-0.01980.08350.00660.101821.51-209.8961.137
220.00330.0030.0040.00820.00330.00650.01520.00460.00180.0138-0.00860.0160.01620.0093-0.00660.113-0.005-0.00270.08960.01730.11311.157-170.12544.536
230.01170.0214-0.01320.1033-0.00640.04490.01280.00260.0119-0.02010.00650.01420.0130.0142-0.01930.0886-0.0029-0.0320.09570.00620.11530.037-167.55617.913
240.0034-0.00080.00080.00390.00010.00090.003-0.0046-0.0173-0.02030.00290-0.004-0.008-0.00590.13010.0061-0.02430.0948-0.00340.096623.24-164.674-3.808
250.0710.1223-0.0030.2298-0.01760.01550.0089-0.0018-0.0161-0.01830.0166-0.02590.0204-0.0079-0.02550.10980.00390.00850.0959-0.01160.078657.048-160.874-0.496
260.0170.0188-0.01910.0235-0.0270.03480.0084-0.0071-0.01750.0042-0.0056-0.00980.0043-0.012-0.00280.09470.005-0.01510.1023-0.00950.124572.804-161.82925.628
270.0217-0.0454-0.01690.10170.03820.0147-0.00390.0101-0.00340.02440.001-0.00010.01360.00030.00280.10250.0064-0.02710.09140.00380.106660.989-163.8357.741
280.0074-0.0027-0.00420.00290.00310.0040.01820.02290.00280.0059-0.0085-0.011-0.0031-0.0134-0.00970.1264-0.0115-0.00930.1031-0.00040.097729.23-169.49967.763
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 305
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 309
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 305
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 304
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301 - 306
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 304
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 406
16X-RAY DIFFRACTION8H1 - 226
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 409
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION9I401 - 404
22X-RAY DIFFRACTION10J1 - 195
23X-RAY DIFFRACTION10J201
24X-RAY DIFFRACTION10J301 - 308
25X-RAY DIFFRACTION11K1 - 212
26X-RAY DIFFRACTION11K301 - 303
27X-RAY DIFFRACTION11K401 - 409
28X-RAY DIFFRACTION12L1 - 222
29X-RAY DIFFRACTION12L301 - 314
30X-RAY DIFFRACTION13M1 - 233
31X-RAY DIFFRACTION13M301 - 313
32X-RAY DIFFRACTION14N1 - 196
33X-RAY DIFFRACTION14N201 - 203
34X-RAY DIFFRACTION14N301 - 307
35X-RAY DIFFRACTION15O1 - 250
36X-RAY DIFFRACTION15O301 - 302
37X-RAY DIFFRACTION16P1 - 244
38X-RAY DIFFRACTION16P301 - 303
39X-RAY DIFFRACTION17Q1 - 240
40X-RAY DIFFRACTION17Q301 - 310
41X-RAY DIFFRACTION18R1 - 242
42X-RAY DIFFRACTION18R301 - 305
43X-RAY DIFFRACTION19S3 - 233
44X-RAY DIFFRACTION19S301 - 302
45X-RAY DIFFRACTION20T2 - 244
46X-RAY DIFFRACTION20T301 - 303
47X-RAY DIFFRACTION21U2 - 242
48X-RAY DIFFRACTION21U301
49X-RAY DIFFRACTION21U401 - 407
50X-RAY DIFFRACTION22V1 - 226
51X-RAY DIFFRACTION22V301
52X-RAY DIFFRACTION22V401 - 413
53X-RAY DIFFRACTION23W1 - 204
54X-RAY DIFFRACTION23W301 - 304
55X-RAY DIFFRACTION24X1 - 195
56X-RAY DIFFRACTION24X201 - 209
57X-RAY DIFFRACTION25Y1 - 212
58X-RAY DIFFRACTION25Y301
59X-RAY DIFFRACTION25Y401 - 412
60X-RAY DIFFRACTION26Z1 - 222
61X-RAY DIFFRACTION26Z301
62X-RAY DIFFRACTION26Z401 - 409
63X-RAY DIFFRACTION27a1 - 233
64X-RAY DIFFRACTION27a301 - 311
65X-RAY DIFFRACTION28b1 - 196
66X-RAY DIFFRACTION28b201 - 202
67X-RAY DIFFRACTION28b301 - 307

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