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- PDB-9c97: Yeast 20S proteasome soaked with BRA-346 fraction -

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Basic information

Entry
Database: PDB / ID: 9c97
TitleYeast 20S proteasome soaked with BRA-346 fraction
Components
  • (Proteasome subunit ...) x 3
  • (proteasome endopeptidase ...) x 2
  • PRE10 isoform 1
  • PRE5 isoform 1
  • PRE6 isoform 1
  • PRE7 isoform 1
  • PRE8 isoform 1
  • PRE9 isoform 1
  • PUP2 isoform 1
  • PUP3 isoform 1
  • SCL1 isoform 1
KeywordsHYDROLASE
Function / homology
Function and homology information


proteasome core complex / Proteasome assembly / 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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway ...proteasome core complex / Proteasome assembly / 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 / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / proteasome storage granule / Antigen processing: Ubiquitination & Proteasome degradation / Ub-specific processing proteases / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / proteasome complex / endopeptidase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / nucleus / cytosol / cytoplasm
Similarity search - Function
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 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 B-type subunit / Proteasome beta-type subunit profile. / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
PRE5 isoform 1 / PRE9 isoform 1 / PUP2 isoform 1 / SCL1 isoform 1 / PRE7 isoform 1 / Proteasome subunit beta / PRE6 isoform 1 / proteasome endopeptidase complex / PRE10 isoform 1 / proteasome endopeptidase complex ...PRE5 isoform 1 / PRE9 isoform 1 / PUP2 isoform 1 / SCL1 isoform 1 / PRE7 isoform 1 / Proteasome subunit beta / PRE6 isoform 1 / proteasome endopeptidase complex / PRE10 isoform 1 / proteasome endopeptidase complex / PUP3 isoform 1 / PRE8 isoform 1 / Proteasome subunit beta / Proteasome subunit beta type-1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.33 Å
AuthorsMeneghello, R. / Rustiguel, J.K.
Funding support Brazil, 3items
OrganizationGrant numberCountry
Sao Paulo Research Foundation (FAPESP)2019/17721-9 Brazil
Sao Paulo Research Foundation (FAPESP)2014/10753-9 Brazil
Other private1709-19681 Brazil
Citation
Journal: Acta Crystallogr.,Sect.F / Year: 2025
Title: High-throughput protein crystallography to empower natural product-based drug discovery.
Authors: Meneghello, R. / Rustiguel, J.K. / de Araujo, E.A. / de Felicio, R. / Fernandes, A.Z.N. / Ferreira, E.L.F. / Gubiani, J.R. / Takeda, A.A.S. / Araujo, A. / de Lima Silva, C.C. / Bertonha, A.F. ...Authors: Meneghello, R. / Rustiguel, J.K. / de Araujo, E.A. / de Felicio, R. / Fernandes, A.Z.N. / Ferreira, E.L.F. / Gubiani, J.R. / Takeda, A.A.S. / Araujo, A. / de Lima Silva, C.C. / Bertonha, A.F. / Urano, R.P.M. / Trindade, D.M. / Cunha, T.M. / Cardoso, A.C. / Berlinck, R.G.S. / Nascimento, A.F.Z. / Trivella, D.B.B.
#1: Journal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionJun 13, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 30, 2025Provider: repository / Type: Initial release
Revision 1.1May 7, 2025Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PRE8 isoform 1
B: PRE9 isoform 1
C: PRE6 isoform 1
D: PUP2 isoform 1
E: PRE5 isoform 1
F: PRE10 isoform 1
G: SCL1 isoform 1
O: PRE8 isoform 1
P: PRE9 isoform 1
Q: PRE6 isoform 1
R: PUP2 isoform 1
S: PRE5 isoform 1
T: PRE10 isoform 1
U: SCL1 isoform 1
H: proteasome endopeptidase complex
I: PUP3 isoform 1
J: Proteasome subunit beta
K: proteasome endopeptidase complex
L: PRE7 isoform 1
M: Proteasome subunit beta
N: Proteasome subunit beta type-1
V: proteasome endopeptidase complex
W: PUP3 isoform 1
X: Proteasome subunit beta
Y: proteasome endopeptidase complex
Z: PRE7 isoform 1
a: Proteasome subunit beta
b: Proteasome subunit beta type-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)732,72381
Polymers728,27828
Non-polymers4,44653
Water5,693316
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)117.511, 299.917, 143.913
Angle α, β, γ (deg.)90.000, 108.458, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1chain "A"
d_2ens_1chain "O"
d_1ens_2chain "B"
d_2ens_2(chain "P" and (resid 1 through 217 or resid 221...
d_1ens_3chain "C"
d_2ens_3(chain "Q" and resid 1 through 238)
d_1ens_4chain "D"
d_2ens_4(chain "R" and (resid 0 through 117 or resid 124 through 242))
d_1ens_5chain "E"
d_2ens_5(chain "S" and (resid 3 through 201 or (resid 202...
d_1ens_6(chain "F" and (resid 1 through 50 or (resid 51...
d_2ens_6chain "T"
d_1ens_7chain "G"
d_2ens_7(chain "U" and resid 2 through 242)
d_1ens_8(chain "H" and (resid 1 through 220 or (resid 221...
d_2ens_8chain "V"
d_1ens_9chain "I"
d_2ens_9chain "W"
d_1ens_10(chain "J" and resid 1 through 195)
d_2ens_10chain "X"
d_1ens_11chain "K"
d_2ens_11chain "Y"
d_1ens_12chain "L"
d_2ens_12chain "Z"
d_1ens_13chain "M"
d_2ens_13chain "a"
d_1ens_14(chain "N" and resid 1 through 196)
d_2ens_14chain "b"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1THRTHRLEULEUAA2 - 2502 - 250
d_21ens_1THRTHRLEULEUOH2 - 2502 - 250
d_11ens_2GLYGLYLYSLYSBB1 - 2452 - 246
d_21ens_2GLYGLYLYSLYSPI1 - 2172 - 218
d_22ens_2ASPASPLYSLYSPI221 - 245222 - 246
d_11ens_3GLYGLYLYSLYSCC1 - 2383 - 240
d_21ens_3GLYGLYLYSLYSQJ1 - 2383 - 240
d_11ens_4TYRTYRGLUGLUDD0 - 2428 - 250
d_21ens_4TYRTYRGLUGLURK0 - 1178 - 125
d_22ens_4ARGARGGLUGLURK124 - 242132 - 250
d_11ens_5ASNASNILEILEEE3 - 2334 - 234
d_21ens_5ASNASNILEILESL3 - 2334 - 234
d_11ens_6GLYGLYASNASNFF1 - 2444 - 247
d_21ens_6GLYGLYASNASNTM1 - 2444 - 247
d_11ens_7GLYGLYGLNGLNGG2 - 24211 - 251
d_21ens_7GLYGLYGLNGLNUN2 - 24211 - 251
d_11ens_8THRTHRASPASPHO1 - 2221 - 222
d_21ens_8THRTHRASPASPVV1 - 2221 - 222
d_11ens_9SERSERASPASPIP1 - 2042 - 205
d_21ens_9SERSERASPASPWW1 - 2042 - 205
d_11ens_10METMETPHEPHEJQ1 - 1951 - 195
d_21ens_10METMETPHEPHEXX1 - 1951 - 195
d_11ens_11THRTHRGLYGLYKR1 - 2121 - 212
d_21ens_11THRTHRGLYGLYYY1 - 2121 - 212
d_11ens_12GLNGLNASPASPLS1 - 2221 - 222
d_21ens_12GLNGLNASPASPZZ1 - 2221 - 222
d_11ens_13THRTHRILEILEMT1 - 2331 - 233
d_21ens_13THRTHRILEILEaAA1 - 2331 - 233
d_11ens_14THRTHRLEULEUNU1 - 1961 - 196
d_21ens_14THRTHRLEULEUbBA1 - 1961 - 196

NCS ensembles :
ID
ens_1
ens_2
ens_3
ens_4
ens_5
ens_6
ens_7
ens_8
ens_9
ens_10
ens_11
ens_12
ens_13
ens_14

NCS oper:
IDCodeMatrixVector
1given(-0.997232114539, -0.012662239067, -0.0732651174406), (-0.000543095268404, -0.984124936561, 0.177476235835), (-0.0743492755802, 0.177024791881, 0.981394114655)-67.375951062, 9.18241736718, -2.9368850983
2given(-0.996570612293, -0.0162661044855, -0.0811321672257), (0.00167491461303, -0.984252851593, 0.17675836272), (-0.0827297369445, 0.176016300312, 0.9809047113)-67.2550980024, 9.1514511566, -3.43388392861
3given(-0.99729325484, -0.00415870211855, -0.0734089166699), (-0.00844882697445, -0.985304183345, 0.1705997761), (-0.0730395863399, 0.170758225217, 0.982602079861)-67.6833119163, 8.77207919525, -2.83387058851
4given(-0.997168991496, -0.0142988009167, -0.0738210450407), (0.000534916613037, -0.983077020157, 0.183191938424), (-0.0751911980405, 0.182633832385, 0.980301569419)-67.1293620854, 9.02105456759, -3.67632998297
5given(-0.996909198287, -0.0104003752336, -0.0778709353109), (-0.0040764895628, -0.983015328588, 0.183478189424), (-0.0784565650793, 0.183228534777, 0.979934626105)-67.6941327742, 9.11631514561, -3.84706998625
6given(-0.997037832344, -0.00663316919469, -0.076626117873), (-0.00732833531342, -0.983548505044, 0.180495522736), (-0.0765627610225, 0.180522406622, 0.980586459386)-67.9126746508, 9.00656628068, -3.50348522426
7given(-0.997098517588, -0.00830149327573, -0.0756679022603), (-0.00613617370907, -0.982035419391, 0.188596878112), (-0.0758741958461, 0.18851397898, 0.979135121489)-67.8119195076, 9.40075905765, -3.81350396399
8given(-0.997394174422, -0.00570371528563, -0.0719189019745), (-0.00708288723892, -0.984312576041, 0.176291194775), (-0.0717961944509, 0.176341204144, 0.981707230382)-67.6151388257, 8.75027128125, -2.82917167695
9given(-0.997020445057, -0.00729327459887, -0.0767921889511), (-0.00671358270306, -0.983538200012, 0.180575571228), (-0.0768450385227, 0.180553087104, 0.980558729904)-67.5758731387, 8.88911876831, -3.3109468013
10given(-0.997360177156, -0.0110853584969, -0.0717620502056), (-0.00224431977151, -0.983100086058, 0.183055138748), (-0.0725785095705, 0.182732962599, 0.980479996904)-67.3646770692, 9.07600112577, -3.30432088342
11given(-0.997517335218, -0.0069706709278, -0.0700754999061), (-0.00594570799154, -0.983199194548, 0.182439010075), (-0.0701698973689, 0.182402723629, 0.98071679496)-67.4374952544, 8.8661591545, -3.52186840874
12given(-0.997206280116, -0.00780977376559, -0.0742875651229), (-0.00585063351431, -0.983297850451, 0.18190961323), (-0.0744674760257, 0.181836038045, 0.98050509957)-67.5772575746, 8.91590899281, -3.66328191814
13given(-0.996804644253, -0.00872114139779, -0.0794005219672), (-0.00574034186486, -0.983630753064, 0.180104386683), (-0.0796715110389, 0.179984675236, 0.980437640551)-68.0176570219, 8.94790680603, -3.66849617922
14given(-0.996708747097, -0.00792379459231, -0.0806776731146), (-0.00672729291931, -0.983694011205, 0.179724332937), (-0.0807862425782, 0.179675557044, 0.980403119748)-68.2197753126, 8.92754941366, -3.57068910366

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Components

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Protein , 9 types, 18 molecules AOBPCQDRESFTGUIWLZ

#1: Protein PRE8 isoform 1


Mass: 27191.828 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6L1BIF8
#2: Protein PRE9 isoform 1


Mass: 28748.230 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5PXC6
#3: Protein PRE6 isoform 1


Mass: 28478.111 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q273
#4: Protein PUP2 isoform 1


Mass: 28649.086 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5PXN2
#5: Protein PRE5 isoform 1


Mass: 25634.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5PTH4
#6: Protein PRE10 isoform 1


Mass: 31443.875 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q4M4
#7: Protein SCL1 isoform 1


Mass: 28033.830 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5PYC9
#9: Protein PUP3 isoform 1


Mass: 22627.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6L0YA22
#12: Protein PRE7 isoform 1


Mass: 24883.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q0P3

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Proteasome endopeptidase ... , 2 types, 4 molecules HVKY

#8: Protein proteasome endopeptidase complex


Mass: 25114.459 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: A0A6A5Q449, proteasome endopeptidase complex
#11: Protein proteasome endopeptidase complex


Mass: 23325.248 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast)
References: UniProt: A0A6A5Q5W3, proteasome endopeptidase complex

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Proteasome subunit ... , 3 types, 6 molecules JXMaNb

#10: Protein Proteasome subunit beta


Mass: 22545.676 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A6A5Q0W2
#13: Protein Proteasome subunit beta


Mass: 25945.496 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: A0A8H8ULD3
#14: Protein Proteasome subunit beta type-1 / 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)
References: UniProt: P38624, proteasome endopeptidase complex

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Non-polymers , 3 types, 369 molecules

#15: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 44 / Source method: obtained synthetically / Formula: SO4
#16: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Mg
#17: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 316 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationN

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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: 3.3 Å3/Da / Density % sol: 62.76 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.9
Details: MES 100 mM pH 6.9, MPD 25% and magnesium acetate 20 mM

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: LNLS SIRIUS / Beamline: MANACA / Wavelength: 0.9772 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Apr 30, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9772 Å / Relative weight: 1
ReflectionResolution: 3.33→49.11 Å / Num. obs: 132592 / % possible obs: 96.5 % / Redundancy: 3 % / Biso Wilson estimate: -9.9 Å2 / CC1/2: 0.754 / Rmerge(I) obs: 0.395 / Rpim(I) all: 0.274 / Rrim(I) all: 0.483 / Χ2: 0.45 / Net I/σ(I): 3
Reflection shellResolution: 3.33→3.39 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.793 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 6605 / CC1/2: 0.526 / Rpim(I) all: 0.556 / Rrim(I) all: 0.973 / Χ2: 0.4 / % possible all: 97.4

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Processing

Software
NameVersionClassification
PHENIX1.21_5207refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.33→49.11 Å / SU ML: 0.4003 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.2991
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.252 6630 5.02 %
Rwork0.2001 125400 -
obs0.2028 132030 96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 38.34 Å2
Refinement stepCycle: LAST / Resolution: 3.33→49.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms49321 0 229 316 49866
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00250393
X-RAY DIFFRACTIONf_angle_d0.477468179
X-RAY DIFFRACTIONf_chiral_restr0.04257647
X-RAY DIFFRACTIONf_plane_restr0.00388761
X-RAY DIFFRACTIONf_dihedral_angle_d11.394718486
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS0.668426060821
ens_2d_2BBX-RAY DIFFRACTIONTorsion NCS0.77376612594
ens_3d_2CCX-RAY DIFFRACTIONTorsion NCS0.879535579674
ens_4d_2DDX-RAY DIFFRACTIONTorsion NCS0.880095384186
ens_5d_2EEX-RAY DIFFRACTIONTorsion NCS0.64116496777
ens_6d_2FFX-RAY DIFFRACTIONTorsion NCS0.746460773379
ens_7d_2GGX-RAY DIFFRACTIONTorsion NCS0.731087726007
ens_8d_2OHX-RAY DIFFRACTIONTorsion NCS0.670433284471
ens_9d_2PIX-RAY DIFFRACTIONTorsion NCS0.566535209651
ens_10d_2QJX-RAY DIFFRACTIONTorsion NCS0.729342053094
ens_11d_2RKX-RAY DIFFRACTIONTorsion NCS0.632846233496
ens_12d_2SLX-RAY DIFFRACTIONTorsion NCS0.69360990402
ens_13d_2TMX-RAY DIFFRACTIONTorsion NCS0.533886005507
ens_14d_2UNX-RAY DIFFRACTIONTorsion NCS0.50415371355
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.33-3.370.29122310.24484102X-RAY DIFFRACTION94.59
3.37-3.410.28452220.23174113X-RAY DIFFRACTION95.3
3.41-3.450.30532250.23294164X-RAY DIFFRACTION95.79
3.45-3.490.28252000.23814200X-RAY DIFFRACTION95.84
3.49-3.540.32382390.23334153X-RAY DIFFRACTION96
3.54-3.590.26732330.22254116X-RAY DIFFRACTION95.23
3.59-3.640.27562140.21484140X-RAY DIFFRACTION96.24
3.64-3.690.27552230.22114279X-RAY DIFFRACTION97.17
3.69-3.750.26022300.21884222X-RAY DIFFRACTION97.52
3.75-3.810.2672410.21224208X-RAY DIFFRACTION97.63
3.81-3.880.2432310.20454277X-RAY DIFFRACTION97.89
3.88-3.950.27381990.20384253X-RAY DIFFRACTION97.38
3.95-4.020.27652100.20854261X-RAY DIFFRACTION97.68
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