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- PDB-4qz4: yCP beta5-A49S mutant in complex with the epoxyketone inhibitor O... -

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Basic information

Entry
Database: PDB / ID: 4qz4
TitleyCP beta5-A49S mutant in complex with the epoxyketone inhibitor ONX 0914
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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation ...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 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / KEAP1-NFE2L2 pathway / CDK-mediated phosphorylation and removal of Cdc6 / Neddylation / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / endopeptidase activator activity / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / Ub-specific processing proteases / threonine-type endopeptidase activity / Neutrophil degranulation / proteasome complex / peroxisome / proteasome-mediated ubiquitin-dependent protein catabolic process / endopeptidase activity / mRNA binding / endoplasmic reticulum membrane / mitochondrion / nucleus / cytosol
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
1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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 ...1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL / Chem-04C / 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: 3 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 27, 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.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)735,22345
Polymers731,08328
Non-polymers4,14017
Water3,117173
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area118590 Å2
ΔGint-434 kcal/mol
Surface area211850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.970, 298.960, 145.340
Angle α, β, γ (deg.)90.00, 112.78, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.999669, -0.001609, 0.025663), (-0.002854, -0.984931, -0.172923), (0.025555, -0.172939, 0.984601)67.41818, -287.09756, -25.55111

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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


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


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


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


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


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


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


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


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


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


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


Mass: 23341.248 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


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


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


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 , 5 types, 190 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


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#17: Chemical
ChemComp-04C / 1,2,4-trideoxy-4-methyl-2-{[N-(morpholin-4-ylacetyl)-L-alanyl-O-methyl-L-tyrosyl]amino}-1-phenyl-D-xylitol


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 584.704 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C31H44N4O7
References: 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
#18: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#19: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 173 / 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: 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: 3→30 Å / Num. all: 211609 / Num. obs: 202933 / % possible obs: 95.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 12
Reflection shellResolution: 3→3.1 Å / Rmerge(I) obs: 0.446 / Mean I/σ(I) obs: 3.4 / % possible all: 99.5

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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: 3→15 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.913 / SU B: 36.39 / SU ML: 0.276 / Cross valid method: THROUGHOUT / ESU R Free: 0.343 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21843 10147 5 %RANDOM
Rwork0.18251 ---
obs0.18429 192786 96.04 %-
all-201933 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 71.787 Å2
Baniso -1Baniso -2Baniso -3
1-3.57 Å20 Å20.51 Å2
2---8.08 Å2-0 Å2
3---3.17 Å2
Refinement stepCycle: LAST / Resolution: 3→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49172 0 285 173 49630
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.01950376
X-RAY DIFFRACTIONr_bond_other_d0.0020.0248130
X-RAY DIFFRACTIONr_angle_refined_deg0.9171.96968172
X-RAY DIFFRACTIONr_angle_other_deg0.8273.003110834
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.19156290
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.61524.4072242
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.617158710
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.50715284
X-RAY DIFFRACTIONr_chiral_restr0.0520.27670
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0257066
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0211294
X-RAY DIFFRACTIONr_mcbond_it3.1176.24625250
X-RAY DIFFRACTIONr_mcbond_other3.1176.24625249
X-RAY DIFFRACTIONr_mcangle_it4.2189.35731510
X-RAY DIFFRACTIONr_mcangle_other4.2189.35731511
X-RAY DIFFRACTIONr_scbond_it3.0476.64625126
X-RAY DIFFRACTIONr_scbond_other3.0476.64625126
X-RAY DIFFRACTIONr_scangle_other3.9079.80636663
X-RAY DIFFRACTIONr_long_range_B_refined4.8248.6953986
X-RAY DIFFRACTIONr_long_range_B_other4.81548.69353975
X-RAY DIFFRACTIONr_rigid_bond_restr1.008398506
X-RAY DIFFRACTIONr_sphericity_free33.1035119
X-RAY DIFFRACTIONr_sphericity_bonded20.977597650
LS refinement shellResolution: 3→3.075 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.325 747 -
Rwork0.271 14187 -
obs--99.63 %
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)
10.0325-0.0420.00710.0662-0.00510.00950.00710.0114-0.0202-0.0038-0.0018-0.002-0.0084-0.0027-0.00530.0905-0.01020.00380.0873-0.00430.114366.844-91.312546.312
20.01970.005-0.02470.03380.01030.0407-0.00760.0011-0.0168-0.0343-0.02030.0246-0.0176-0.0060.02790.0849-0.00750.01680.09260.00850.10759.674-87.163916.6906
30.02880.0293-0.01960.0322-0.02210.01580.0076-0.0055-0.0008-0.00130.00430.01210.00230.0031-0.01190.10650.00750.00020.08470.00490.111432.4882-86.68891.2705
40.03570.01180.02170.02540.03010.04890.0034-0.0039-0.0026-0.0078-0.00750.0306-0.01180.01620.0040.08130.0060.00080.06580.01390.11993.2581-89.337213.7293
50.0032-0.00280.00620.0053-0.00050.0297-0.0061-0.0011-0.01570.0060.00850.0204-0.0057-0.0051-0.00240.02830.0150.04210.0874-0.00410.1168-3.176-93.563345.6573
60.0010.0007-0.00050.0049-0.00310.00280.0125-0.00120.00450.0018-0.01110.0157-0.00120.0144-0.00130.07750.0070.03270.0759-0.01310.089715.1236-94.203969.9075
70.01240.00780.02670.0180.03840.11240.00250.0150.00940.0164-0.019-0.00640.0073-0.01340.01650.1179-0.00550.00690.0689-0.00950.099247.5466-92.642371.3287
80.0122-0.014-0.01420.05430.01430.0180.01270.0105-0.00010.033-0.0125-0.0377-0.0155-0.0167-0.00020.0756-0.00710.00060.0796-0.00940.108567.2892-129.230448.3583
90.10570.045-0.00030.1816-0.01360.0175-0.0024-0.0162-0.0069-0.0467-0.0096-0.0145-0.0237-0.01830.01210.0877-0.00430.0150.0907-0.00080.125568.3657-126.686421.1447
100.00410.002-0.00370.1395-0.0620.02990.0058-0.01240.0151-0.023-0.0031-0.0070.00240.0131-0.00280.1075-0.00110.00960.08750.00140.108744.8831-125.7192-0.3206
110.0129-0.0215-0.00380.0650.0090.00330.0197-0.0096-0.0055-0.031-0.01010.04740.00240.0041-0.00950.11220.0044-0.01120.08450.01170.107411.0646-129.91552.6773
120.02950.00120.05320.0145-0.00690.13460.0118-0.0160.00750.01320.00340.0115-0.01380.0059-0.01530.06160.00540.0080.08780.00460.1331-4.4161-133.340328.7298
130.0237-0.0550.00070.1524-0.00460.00050.00760.00550.0130.0239-0.00240.0057-0.0025-0.0001-0.00530.08530.00190.02390.09280.00040.11497.3664-135.434760.3714
140.00120.0019-0.00050.0057-0.00110.00030.00320.0077-0.00470.0252-0.0003-0.0108-0.0057-0.002-0.00290.1321-0.0123-0.01140.0914-0.00380.104139.7887-133.220270.7107
150.0140.0039-0.0010.010.00180.00740.00540.01690.0135-0.00840.0016-0.0060.01550.0054-0.00690.0984-0.0146-0.00820.08250.00830.11961.8498-205.261936.8866
160.0011-0.00040.00070.0009-0.00030.0004-0.00860.00160.0078-0.00110.003-0.0095-0.00460.00130.00550.1056-0.0043-0.01720.0865-0.00140.11948.3051-204.08016.8339
170.0076-0.0008-0.00290.0025-0.00030.00150.0153-0.01340.001-0.0077-0.00820.0132-0.00290.009-0.00720.12160.01740.00220.0656-0.00570.089835.5217-202.0391-8.9992
180.0238-0.0228-0.02610.02640.02140.03130.0109-0.01620.0127-0.02940.0004-0.0204-0.01030.0232-0.01130.06120.02550.00110.0405-0.02420.095664.8979-201.52293.4578
190.01550.0099-0.02260.0098-0.01320.03580.00480.0021-0.00190.0115-0.0005-0.0213-0.0102-0.0137-0.00430.05130.0245-0.0170.0625-0.01750.139171.8741-202.802135.2189
200.00950.0104-0.01080.0211-0.01760.01690.00530.0017-0.01360.0064-0.0225-0.0376-0.00410.00420.01720.0880.0166-0.03150.04490.01220.112754.0697-206.472659.5064
210.0044-0.00170.00330.0049-0.00890.01680.0060.0133-0.0110.00530.00170.0088-0.00970.0049-0.00770.1273-0.0109-0.00930.07440.01420.114721.6946-208.459761.211
220.00390.00110.00220.0073-0.0040.0090.0161-0.0122-0.00360.0041-0.00240.02580.02020.0071-0.01370.0818-0.007-0.00220.07250.01330.10871.5578-168.315745.5305
230.06720.0842-0.02350.1398-0.05450.0291-0.00270.0121-0.0003-0.01270.00910.0292-0.00180.0167-0.00640.08970.0016-0.01350.08470.00250.1225-0.0231-166.063418.2532
240.01350.01880.01450.0350.0250.0183-0.0077-0.0019-0.0148-0.03550.00820.0025-0.02070.0053-0.00050.10440.0042-0.02180.0903-0.00490.106623.1203-163.2268-3.4874
250.0026-0.00090.00090.00050.00020.00180.0109-0.01040.0011-0.00560.0018-0.00460.0007-0.0042-0.01270.11160.00180.01480.0928-0.01650.104856.9625-159.5941-0.3333
260.00040.00110.00150.0130.01380.01530.01060.001-0.00140.0111-0.0084-0.01230.0166-0.0133-0.00220.06420.00840.01260.0931-0.00330.126872.8824-160.7325.6096
270.0167-0.0152-0.0060.05530.00830.00310.00670.02-0.02850.0051-0.0125-0.0042-0.0004-0.01270.00580.10420.0023-0.01370.06790.00690.112561.6986-164.188257.3383
280.0093-0.015-0.00530.11430.03720.01330.016-0.002-0.00470.0221-0.00060.0160.00460.0058-0.01540.1234-0.00810.00010.0890.00390.09929.4681-168.231367.7308
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 250
2X-RAY DIFFRACTION1A301 - 306
3X-RAY DIFFRACTION2B1 - 244
4X-RAY DIFFRACTION2B301 - 304
5X-RAY DIFFRACTION3C1 - 240
6X-RAY DIFFRACTION3C301 - 302
7X-RAY DIFFRACTION4D1 - 242
8X-RAY DIFFRACTION4D301 - 303
9X-RAY DIFFRACTION5E3 - 233
10X-RAY DIFFRACTION5E301
11X-RAY DIFFRACTION6F2 - 244
12X-RAY DIFFRACTION6F301 - 307
13X-RAY DIFFRACTION7G2 - 242
14X-RAY DIFFRACTION7G301 - 302
15X-RAY DIFFRACTION7G401 - 405
16X-RAY DIFFRACTION8H1 - 222
17X-RAY DIFFRACTION8H301
18X-RAY DIFFRACTION8H401 - 410
19X-RAY DIFFRACTION9I1 - 204
20X-RAY DIFFRACTION9I301
21X-RAY DIFFRACTION10J1 - 195
22X-RAY DIFFRACTION10J201 - 213
23X-RAY DIFFRACTION11K1 - 212
24X-RAY DIFFRACTION11K301 - 303
25X-RAY DIFFRACTION11K401 - 408
26X-RAY DIFFRACTION12L1 - 222
27X-RAY DIFFRACTION12L301 - 305
28X-RAY DIFFRACTION13M1 - 225
29X-RAY DIFFRACTION13M301 - 308
30X-RAY DIFFRACTION14N1 - 196
31X-RAY DIFFRACTION14N201 - 202
32X-RAY DIFFRACTION14N301 - 308
33X-RAY DIFFRACTION15O1 - 250
34X-RAY DIFFRACTION15O301 - 303
35X-RAY DIFFRACTION16P1 - 244
36X-RAY DIFFRACTION16P301 - 303
37X-RAY DIFFRACTION17Q1 - 240
38X-RAY DIFFRACTION17Q301 - 311
39X-RAY DIFFRACTION18R1 - 242
40X-RAY DIFFRACTION18R301
41X-RAY DIFFRACTION19S3 - 233
42X-RAY DIFFRACTION19S301
43X-RAY DIFFRACTION20T2 - 244
44X-RAY DIFFRACTION20T301 - 311
45X-RAY DIFFRACTION21U2 - 242
46X-RAY DIFFRACTION21U301
47X-RAY DIFFRACTION21U401 - 406
48X-RAY DIFFRACTION22V1 - 222
49X-RAY DIFFRACTION22V301 - 302
50X-RAY DIFFRACTION22V401 - 409
51X-RAY DIFFRACTION23W1 - 204
52X-RAY DIFFRACTION23W301 - 305
53X-RAY DIFFRACTION24X1 - 195
54X-RAY DIFFRACTION24X201
55X-RAY DIFFRACTION24X301 - 310
56X-RAY DIFFRACTION25Y1 - 212
57X-RAY DIFFRACTION25Y301 - 302
58X-RAY DIFFRACTION25Y401 - 405
59X-RAY DIFFRACTION26Z1 - 222
60X-RAY DIFFRACTION26Z301
61X-RAY DIFFRACTION26Z401 - 405
62X-RAY DIFFRACTION27a1 - 225
63X-RAY DIFFRACTION27a301 - 308
64X-RAY DIFFRACTION28b1 - 196
65X-RAY DIFFRACTION28b201
66X-RAY DIFFRACTION28b301 - 315

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