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- PDB-4qv7: yCP beta5-A50V mutant -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4qv7
TitleyCP beta5-A50V 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 / endopeptidase activator activity / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / proteasome core complex / proteasome core complex, beta-subunit complex / proteasome endopeptidase complex / proteasome core complex, alpha-subunit complex / proteasome assembly ...proteasome core complex assembly / nuclear outer membrane-endoplasmic reticulum membrane network / endopeptidase activator activity / proteasomal ubiquitin-independent protein catabolic process / proteasome storage granule / proteasome core complex / proteasome core complex, beta-subunit complex / proteasome endopeptidase complex / proteasome core complex, alpha-subunit complex / proteasome assembly / threonine-type endopeptidase activity / proteasomal protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol / cytoplasm
Proteasome subunit alpha5 / Proteasome subunit alpha6 / Nucleophile aminohydrolases, N-terminal / Proteasome beta subunit, C-terminal / Proteasome B-type subunit / Proteasome alpha-type subunit / Proteasome subunit beta 4 / Proteasome beta-type subunit, conserved site / Proteasome, subunit alpha/beta / Proteasome alpha-subunit, N-terminal domain ...Proteasome subunit alpha5 / Proteasome subunit alpha6 / Nucleophile aminohydrolases, N-terminal / Proteasome beta subunit, C-terminal / Proteasome B-type subunit / Proteasome alpha-type subunit / Proteasome subunit beta 4 / Proteasome beta-type subunit, conserved site / Proteasome, subunit alpha/beta / Proteasome alpha-subunit, N-terminal domain / Peptidase T1A, proteasome beta-subunit / Proteasome subunit alpha2 / Proteasome subunit alpha 1 / Proteasome beta 3 subunit / Proteasome subunit beta 2 / Proteasome subunit beta 1 / Proteasome subunit beta 7 / Proteasome subunit alpha 3 / Proteasome subunit beta Pre3 / Proteasome subunit / Proteasome subunit A N-terminal signature / Proteasome beta subunits C terminal / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / 4-Layer Sandwich / Alpha Beta
Proteasome subunit alpha type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4 / Proteasome subunit beta type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-7 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Probable proteasome subunit alpha type-7 ...Proteasome subunit alpha type-1 / Proteasome subunit alpha type-6 / Proteasome subunit alpha type-4 / Proteasome subunit beta type-1 / Proteasome subunit beta type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-7 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Probable proteasome subunit alpha type-7 / Proteasome subunit beta type-6 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit beta type-2
Biological speciesSaccharomyces cerevisiae (baker's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 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.
Validation Report
SummaryFull reportAbout validation report
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

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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)731,42140
Polymers731,10728
Non-polymers31412
Water11,638646
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area119950 Å2
ΔGint-481 kcal/mol
Surface area214310 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)135.110, 301.030, 144.330
Angle α, β, γ (deg.)90.00, 113.18, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:

Code: given

IDMatrixVector
1(1), (1), (1)
2(-0.999647, -0.001514, 0.026519), (-0.003067, -0.985115, -0.171867), (0.026385, -0.171887, 0.984763)67.49856, -289.88406, -25.94564

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Components

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

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


Mass: 27191.828 Da / Num. of mol.: 2 / Mutation: A50V / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23639, proteasome endopeptidase complex
#2: Protein/peptide Proteasome subunit alpha type-3 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23638, proteasome endopeptidase complex
#3: Protein/peptide Proteasome subunit alpha type-4 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40303, proteasome endopeptidase complex
#4: Protein/peptide Proteasome subunit alpha type-5 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P32379, proteasome endopeptidase complex
#5: Protein/peptide Proteasome subunit alpha type-6 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P40302, proteasome endopeptidase complex
#7: Protein/peptide Proteasome subunit alpha type-1 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P21243, proteasome endopeptidase complex

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Protein/peptide , 1 types, 2 molecules FT

#6: Protein/peptide Probable proteasome subunit alpha type-7 / 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 (baker'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/peptide Proteasome subunit beta type-2 / PSMB2 / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25043, proteasome endopeptidase complex
#9: Protein/peptide 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P25451, proteasome endopeptidase complex
#10: Protein/peptide Proteasome subunit beta type-4 / PSMB4 / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P22141, proteasome endopeptidase complex
#11: Protein/peptide Proteasome subunit beta type-5 / PSMB5 / Macropain subunit PRE2 / Multicatalytic endopeptidase complex subunit PRE2 / Proteasome component PRE2 / Proteinase YSCE subunit PRE2


Mass: 23353.303 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Strain: ATCC 204508 / S288c / Gene: PRE2, DOA3, PRG1, YPR103W, P8283.10 / Production host: SACCHAROMYCES CEREVISIAE (baker's yeast)
References: UniProt: P30656, proteasome endopeptidase complex
#12: Protein/peptide 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P23724, proteasome endopeptidase complex
#13: Protein/peptide Proteasome subunit beta type-7 / / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P30657, proteasome endopeptidase complex
#14: Protein/peptide Proteasome subunit beta type-1 / PSMB1 / 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 (baker's yeast) / Strain: ATCC 204508 / S288c
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 3 types, 658 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Mg / Magnesium
#16: Chemical ChemComp-CL / CHLORIDE ION


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


Mass: 18.015 Da / Num. of mol.: 646 / Source method: isolated from a natural source / Formula: H2O / Water

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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: Oct 20, 2012
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: 2.6→30 Å / Num. all: 324147 / Num. obs: 317016 / % possible obs: 97.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 11.7
Reflection shellResolution: 2.6→2.7 Å / Rmerge(I) obs: 0.495 / Mean I/σ(I) obs: 2.7 / % possible all: 99

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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: 2.6→15 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.945 / SU B: 21.033 / SU ML: 0.191 / Cross valid method: THROUGHOUT / ESU R Free: 0.232 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21396 15851 5 %RANDOM
Rwork0.18811 ---
Obs0.1894 301165 97.96 %-
All-317016 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.698 Å2
Baniso -1Baniso -2Baniso -3
1-4.2 Å2-0 Å2-1.23 Å2
2---5.7 Å2-0 Å2
3---1.48 Å2
Refinement stepCycle: LAST / Resolution: 2.6→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49370 0 12 646 50028
Refine LS restraints

Refinement-ID: X-RAY DIFFRACTION

TypeDev idealDev ideal targetNumber
r_bond_refined_d0.0040.01950278
r_bond_other_d0.0010.0248060
r_angle_refined_deg0.8521.96368016
r_angle_other_deg0.6823110672
r_dihedral_angle_1_deg5.03556314
r_dihedral_angle_2_deg34.0224.4232252
r_dihedral_angle_3_deg13.769158760
r_dihedral_angle_4_deg13.1315284
r_chiral_restr0.0480.27664
r_gen_planes_refined0.0020.0257108
r_gen_planes_other0.0010.0211268
r_mcbond_it2.1535.30925346
r_mcbond_other2.1535.30925345
r_mcangle_it2.8477.94731630
r_mcangle_other2.8477.94731631
r_scbond_it2.0855.70824932
r_scbond_other2.0845.70824932
r_scangle_other2.5388.40736386
r_long_range_B_refined3.27741.4154400
r_long_range_B_other3.23641.40654304
r_rigid_bond_restr1.185398338
r_sphericity_free28.945334
r_sphericity_bonded16.163597764
LS refinement shellResolution: 2.6→2.665 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.338 1150 -
Rwork0.309 21860 -
Obs--98.98 %
Refinement TLS params.

Method: refined / Refinement-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)
10.01860.00110.00910.01740.01580.0224-0.00590.00870.00020.00370.0093-0.0094-0.0066-0.004-0.00340.0905-0.00780.00220.0669-0.00570.114766.2943-92.021945.7103
20.04860.00830.01170.00470.00360.0059-0.0007-0.0088-0.025-0.013-0.00570.0038-0.00260.00440.00640.0956-0.00240.01540.0619-0.00150.093758.9168-87.785616.1052
30.02120.0243-0.02010.0298-0.02360.0198-0.0039-0.007-0.0049-0.00830.00510.00160.00760.0062-0.00120.11270.0036-0.00610.05780.00550.101631.7401-87.52370.7845
40.0005-0.0015-0.00230.01080.00920.0234-0.0045-0.0032-0.0057-0.0192-0.00340.0298-0.02510.01810.0080.07920.0151-0.01510.0370.01280.11682.5104-90.546613.3529
50.04260.02610.02670.02050.01690.01780.0004-0.0055-0.00870.002-0.00190.0169-0.00130.00290.00150.03610.01890.01310.0592-0.00430.1144-3.8248-95.008745.2902
60.0008-0.00130.00050.00460.0010.002-0.00490.00480.00250.0198-0.00570.00290.00710.00260.01060.09790.00570.01920.0595-0.01280.098214.5996-95.522869.4303
70.0055-0.0042-0.0010.0114-0.00540.0052-0.00440.0158-0.00050.0099-0.0051-0.0043-0.0039-0.00840.00950.1163-0.00010.00060.0524-0.01070.097746.9776-93.559670.7609
80.0026-0.0009-0.00330.02170.01340.01280.01240.00790.00770.0179-0.0034-0.0245-0.0037-0.0144-0.0090.0841-0.0022-0.00730.0625-0.00210.110267.5503-129.338447.2129
90.0078-0.003-0.00030.09670.01640.00970.01530.0057-0.0039-0.0112-0.0132-0.016-0.0221-0.0054-0.00210.0872-0.00380.01150.0657-0.00410.113368.1305-127.121520.6147
100.0037-0.0002-0.00040.05360.00180.0010.0094-0.0127-0.0001-0.02520.0018-0.0079-0.0020.0019-0.01120.1118-0.00120.01010.06610.00050.099444.5332-126.6683-1.0368
110.0033-0.00910.00310.0668-0.03540.02580.0032-0.01080.0012-0.01280.00450.0145-0.01350.0079-0.00770.09230.0074-0.01820.05730.00280.10610.8003-131.27232.1665
120.0439-0.00980.03690.0169-0.00260.04360.0073-0.01210.0014-0.00350.00210.0176-0.0050.008-0.00940.07050.0026-0.00410.06740.0060.1268-4.6345-135.096728.0745
130.0055-0.0145-0.00260.09640.02130.00490.0070.00870.01020.0215-0.01230.01950.00640.00030.00530.0865-0.00190.01590.0656-0.00460.10557.5768-138.447459.9533
140.05470.0246-0.00970.0384-0.02430.01670.00890.0129-0.00370.0143-0.00140.0101-0.00220.005-0.00750.1164-0.0021-0.00230.062-0.00290.094239.5644-134.24670.4652
150.01080.00820.0010.02810.00840.0096-0.00780.01480.0099-0.00030.00120.01070.0220.0040.00660.088-0.0133-0.01280.05640.00590.11572.4865-207.232936.5267
160.0216-0.00010.00910.0004-0.00050.0062-0.01050.0032-0.00380.00280.0013-0.00670.00380.00270.00920.0984-0.0015-0.02080.0581-0.00680.10999.1499-206.25816.4731
170.00470.00090.00730.01320.00090.06650.0079-0.0069-0.0056-0.03080.0060.02050.00330.0213-0.01390.10940.0279-0.00730.0324-0.01720.095336.3231-204.0699-9.3461
180.0047-0.02150.00330.1154-0.02050.0043-0.0019-0.00330.0066-0.0348-0.0046-0.03080.01220.00270.00650.07270.03140.02060.0249-0.02190.091265.7237-203.17053.1888
190.00320.00320.00020.00430.0010.00140.0091-0.0006-0.00160.01110.0023-0.0128-0.0021-0.0032-0.01140.04620.0261-0.00760.0472-0.0150.121672.6166-204.073235.0999
200.01710.00190.01340.00260.00080.01060.003-0.0170.00390.0103-0.0064-0.01350.0022-0.0130.00350.10510.0171-0.02980.02970.01380.093454.632-207.745959.3079
210.00060.00040.00060.0011-0.00030.00110.00120.00530.00290.0040.00150.0096-0.00320.0068-0.00270.13-0.0057-0.01080.05060.00540.099622.2769-210.100760.8922
220.00030.00150.00060.01130.00090.00380.0067-0.00010.00110.0216-0.00080.02530.01180.0079-0.00590.0824-0.00540.00080.0560.00550.11511.3645-170.715144.3664
230.003-0.01720.00310.142-0.01860.00610.0076-0.00090.0028-0.0041-0.00660.01220.01210.0116-0.0010.0826-0.0029-0.01490.06170.00360.11580.3184-168.379917.7637
240.01980.00940.00750.0070.00460.00420.00320.0022-0.0044-0.00820.00340.0086-0.00180.0093-0.00670.11180.0025-0.01470.06310.00170.105423.4843-165.1269-4.1662
250.0151-0.01380.02020.0176-0.02090.03130.0208-0.0115-0.0089-0.0321-0.00050.0010.0267-0.0027-0.02040.08310.0120.03020.0603-0.01230.084357.2732-161.0997-0.866
260.0126-0.03520.00090.13140.00550.00240.0081-0.0078-0.00260.00510.0038-0.01970.0051-0.0072-0.01190.07120.00350.00260.073-0.00930.117773.1869-161.687724.9855
270.0063-0.0046-0.00110.03270.00030.00250.00860.0134-0.01330.0105-0.003-0.01780.0039-0.0105-0.00550.10080.003-0.01510.0579-0.00190.111161.5769-163.821557.2
280.0246-0.04090.00150.0768-0.00250.00320.01270.00170.00190.00250.00250.00610.0099-0.0065-0.01520.1162-0.0052-0.00420.06440.00220.097429.7962-169.809667.5353
Refinement TLS group

Refinement-ID: X-RAY DIFFRACTION

IDRefine TLS-IDAuth asym-IDAuth seq-ID
11A1 - 250
21A301 - 315
32B1 - 244
42B301 - 318
53C1 - 240
63C301 - 321
74D1 - 242
84D301 - 319
95E3 - 233
105E301 - 315
116F2 - 244
126F301 - 331
137G2 - 242
147G301 - 302
157G401 - 431
168H1 - 226
178H301 - 320
189I1 - 204
199I301
209I401 - 436
2110J1 - 195
2210J201
2310J301 - 328
2411K1 - 212
2511K301 - 302
2611K401 - 426
2712L1 - 222
2812L301 - 331
2913M1 - 233
3013M301 - 333
3114N1 - 196
3214N201 - 202
3314N301 - 328
3415O1 - 250
3515O301 - 311
3616P1 - 244
3716P301 - 316
3817Q1 - 240
3917Q301 - 317
4018R1 - 242
4118R301 - 316
4219S3 - 233
4319S301 - 308
4420T2 - 244
4520T301 - 320
4621U2 - 242
4721U301
4821U401 - 425
4922V1 - 226
5022V301
5122V401 - 420
5223W1 - 204
5323W301 - 327
5424X1 - 195
5524X201 - 224
5625Y1 - 212
5725Y301
5825Y401 - 427
5926Z1 - 222
6026Z301
6126Z401 - 421
6227a1 - 233
6327a301 - 335
6428b1 - 196
6528b201 - 227

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