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- PDB-8drv: Product structure of SARS-CoV-2 Mpro C145A mutant in complex with... -

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Basic information

Entry
Database: PDB / ID: 8drv
TitleProduct structure of SARS-CoV-2 Mpro C145A mutant in complex with nsp8-nsp9 (C8) cut site sequence
ComponentsFusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
KeywordsVIRAL PROTEIN / Viral protease / SARS-CoV-2
Function / homology
Function and homology information


protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs ...protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / TRAF3-dependent IRF activation pathway / snRNP Assembly / Replication of the SARS-CoV-2 genome / double membrane vesicle viral factory outer membrane / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / SARS coronavirus main proteinase / host cell endosome / 3'-5'-RNA exonuclease activity / : / host cell endoplasmic reticulum-Golgi intermediate compartment / symbiont-mediated suppression of host toll-like receptor signaling pathway / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / SARS-CoV-2 modulates host translation machinery / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / copper ion binding / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. ...RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / NSP12 RNA-dependent RNA polymerase, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidovirus 2-O-methyltransferase / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nonstructural protein 13, 1B domain, coronavirus / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerization / Nonstructural protein 15, middle domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Lipocalin signature. / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein NSP3, N-terminal, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus SUD-C domain / Betacoronavirus replicase NSP3, N-terminal / NSP1 globular domain superfamily, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Carbamoyl-phosphate synthase subdomain signature 2. / Coronavirus 3Ecto domain profile. / : / Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile. / NSP1, C-terminal domain, betacoronavirus / Betacoronavirus Nsp3c-M domain profile. / NSP1, globular domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Betacoronavirus replicase NSP1 / Betacoronavirus single-stranded poly(A) binding domain / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Betacoronavirus Nsp3c-C domain profile. / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Non-structural protein NSP3A domain-like superfamily / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / : / Coronavirus (CoV) Nsp2 middle domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / NSP1, globular domain, alpha/betacoronavirus / : / Coronavirus (CoV) Nsp3 Y domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus
Similarity search - Domain/homology
Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsLee, J. / Kenward, C. / Worrall, L.J. / Vuckovic, M. / Paetzel, M. / Strynadka, N.C.J.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR) Canada
CitationJournal: Nat Commun / Year: 2022
Title: X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation.
Authors: Lee, J. / Kenward, C. / Worrall, L.J. / Vuckovic, M. / Gentile, F. / Ton, A.T. / Ng, M. / Cherkasov, A. / Strynadka, N.C.J. / Paetzel, M.
History
DepositionJul 21, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 21, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
B: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
C: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
D: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,4455
Polymers135,2064
Non-polymers2381
Water4,450247
1
A: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
C: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site


Theoretical massNumber of molelcules
Total (without water)67,6032
Polymers67,6032
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2590 Å2
ΔGint-13 kcal/mol
Surface area26030 Å2
MethodPISA
2
B: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
D: Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,8413
Polymers67,6032
Non-polymers2381
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2600 Å2
ΔGint-11 kcal/mol
Surface area25860 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.788, 117.202, 121.381
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

#1: Protein
Fusion protein of 3C-like proteinase nsp5 and nsp8-nsp9 (C8) cut site / / 3CL-PRO / 3CLp / Main protease / Mpro / Non-structural protein 5 / nsp5 / SARS coronavirus main ...3CL-PRO / 3CLp / Main protease / Mpro / Non-structural protein 5 / nsp5 / SARS coronavirus main proteinase / nsp8


Mass: 33801.570 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: rep, 1a-1b / Production host: Escherichia coli (E. coli)
References: UniProt: P0DTD1, SARS coronavirus main proteinase
#2: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 247 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.27 Å3/Da / Density % sol: 45.87 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1M Tris pH 8.5, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 10, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 2.2→60.69 Å / Num. obs: 62720 / % possible obs: 99.9 % / Redundancy: 12.5 % / Biso Wilson estimate: 46.08 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.181 / Net I/σ(I): 9.9
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Net I/σ(I) obs% possible all
2.2-2.2611.32.8525155545460.384199.6
9.84-49.5511.40.04791758060.99938.199.3

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7JOY
Resolution: 2.4→60.69 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.28 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2398 2441 5.04 %
Rwork0.1776 46032 -
obs0.1808 48473 99.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 140.24 Å2 / Biso mean: 53.7053 Å2 / Biso min: 26.75 Å2
Refinement stepCycle: final / Resolution: 2.4→60.69 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9376 0 10 247 9633
Biso mean--55.52 48.31 -
Num. residues----1217
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 17

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.450.32121410.281726682809100
2.45-2.50.38951160.259427022818100
2.5-2.560.29181530.235226722825100
2.56-2.620.30021270.230926682795100
2.62-2.70.31251330.22927082841100
2.7-2.770.31331250.226526962821100
2.77-2.860.31091330.244726982831100
2.86-2.970.30791420.251726962838100
2.97-3.090.33891270.225326892816100
3.09-3.230.29081560.2122656281299
3.23-3.40.26161420.19862675281799
3.4-3.610.22931360.186527152851100
3.61-3.890.25651830.169326782861100
3.89-4.280.2231500.140627362886100
4.28-4.90.17521550.125827402895100
4.9-6.170.18571690.144227582927100
6.17-60.690.17661530.13382877303099
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)
12.7862.9014-0.42744.7859-0.6972.59340.1411-0.2468-0.0803-0.1479-0.18-0.09020.14550.03530.04650.26890.0477-0.01420.31820.01830.227-2.41429.11516.1989
29.4116-0.65165.29264.8631-2.10617.2489-0.0610.24510.49220.1616-0.4785-0.6073-0.20370.30230.57680.35540.00030.03970.33650.10090.354412.254641.701416.7608
32.2351.8076-0.08716.0326-0.75122.06040.0896-0.10420.1679-0.1081-0.05780.2043-0.1451-0.2362-0.04550.21180.06130.02620.2906-0.02160.2495-3.852334.409518.6781
41.27641.2122-1.27534.9428-0.56994.5076-0.02530.1605-0.15720.087-0.1562-0.13920.06110.01510.20290.2056-0.008-0.01550.34210.04020.2911-1.316421.368722.691
54.052-0.38253.07934.349-1.153.2454-0.1468-0.2926-0.12590.2021-0.0824-0.43240.10520.24460.23150.2403-0.00020.02530.29460.08950.24412.680726.962625.2905
62.18911.6148-0.62731.2632-0.38720.13170.4122-0.6778-0.76670.7482-0.7899-0.8136-0.36760.48880.41310.44-0.1519-0.15130.60140.22660.531410.675724.446931.7152
72.76550.82080.83666.53722.06044.0268-0.10080.0656-0.14580.10550.61840.60240.9439-0.3505-0.55840.5403-0.1218-0.06690.43590.14190.4436-8.99220.838338.5151
84.53081.5985-3.0147.8828-0.8954.64040.0725-1.1319-0.22250.9598-0.3022-0.1319-0.68941.02280.31270.4943-0.0959-0.07250.60860.12140.38981.31578.815946.6759
99.4136-0.3675-0.45994.4255-0.81985.93390.2527-0.5236-0.34940.38770.37820.51310.0296-1.301-0.55370.35390.02430.08470.59230.19230.4118-9.6174.743843.0222
105.08131.8578-3.25310.9195-0.76493.5372-0.10630.77130.4842-0.03480.22330.1230.221-0.0674-0.13960.4589-0.0163-0.07360.45330.09580.3692-10.16824.784331.379
111.7803-2.94521.61667.0699-1.94812.5026-0.12030.07190.15350.4162-0.0378-0.154-0.2729-0.01370.15250.27170.02870.02420.30960.02630.245540.73572.098342.714
125.328-0.3648-1.14125.444-0.87299.13760.12380.00980.0696-0.0959-0.1649-0.22480.31550.56490.02110.32080.0617-0.03820.29930.05050.385650.5198-10.62344.226
134.58140.5158-2.73936.1947-4.29156.1909-0.09790.3759-0.339-0.29750.48870.74470.2112-1.2582-0.36390.26320.0552-0.05030.40790.02280.358633.2874-1.939537.4671
141.935-0.97920.9195.0889-0.94266.1762-0.0798-0.06580.1320.1746-0.03350.0464-0.0954-0.25020.11710.29360.0428-0.0290.33790.02110.330241.23548.305836.129
153.1688-0.25050.51233.7462-1.53014.35460.2340.1469-0.0487-0.3394-0.4102-0.35340.01940.53960.15450.31350.09830.01160.40330.09260.315747.99892.718229.5676
164.4578-0.6308-2.0742.92942.03982.6678-0.1060.07980.3249-0.46680.06680.1697-0.9006-0.02720.03860.4860.0511-0.02320.31920.05170.342230.987525.497115.6806
172.5697-2.0752-1.86625.96521.77514.05540.11410.316-0.3906-0.5239-0.25640.22750.03610.13020.12150.40840.0417-0.03680.38370.05680.393333.616218.141810.9678
185.2539-1.51640.91161.38270.75352.9763-0.2019-0.529-0.39450.19270.36490.2578-0.18920.2768-0.18830.4616-0.0176-0.01570.34480.03490.41231.557523.432823.5164
196.65570.83082.46711.82790.25072.2475-0.0521-0.15740.0057-0.10090.03760.029-0.0488-0.26560.00560.32980.0276-0.01090.278-0.00690.2164-18.858212.29178.0298
205.8417-0.27781.13532.1457-0.44071.99340.0389-0.2653-0.2635-0.22960.04090.31590.2934-0.3407-0.08130.3881-0.017-0.02970.33040.00720.1967-26.62167.79191.8118
213.2782-0.48050.58592.95461.11541.83350.0995-0.1934-0.38010.1781-0.02940.13080.2646-0.096-0.07180.39330.02110.00260.30870.04110.334-13.83652.538310.5028
221.2769-0.6901-0.23280.99691.45772.7214-0.2571-0.34960.13140.5520.7204-0.88950.45440.7823-0.36220.52930.2363-0.07320.5943-0.12540.825215.20720.235115.3791
235.4151-1.542-1.07184.85192.7785.06590.0158-0.32130.11730.22480.1319-0.47960.57250.6632-0.14390.42660.1420.04950.45830.06190.499810.1914-2.244912.8497
245.9071-2.7772-2.86481.8490.87122.121-0.034-0.32740.11660.26740.16520.0482-0.1565-0.1045-0.110.47080.0628-0.03310.5289-0.01060.414924.058220.140248.3634
253.20040.57780.54318.8298-2.68522.65830.2111-0.46950.5077-0.19890.13860.6128-0.5137-0.6536-0.39690.63250.220.03350.79140.07450.73158.035930.23250.5084
264.6854-2.208-2.28027.4591-0.51942.0725-0.3907-0.6951-0.25550.65420.32830.3843-0.1923-0.06120.06080.51290.1235-0.00680.66360.00840.268116.907919.708457.5989
274.60852.0046-0.5663.7520.56131.7973-0.0041-0.08020.4191-0.00640.02080.0382-0.36860.171-0.02630.58650.0836-0.06830.4605-0.00730.467229.561929.302845.0926
283.6948-0.67921.44248.96232.17823.33060.212-0.3936-0.05270.2432-0.0782-0.7532-0.15980.0374-0.11880.4976-0.16-0.07780.60960.04680.536754.993934.952239.1137
297.87351.29310.0888.250.88438.32840.25420.32760.0669-0.82060.16680.2791-0.30640.591-0.38970.4816-0.0388-0.05410.3889-0.03890.41752.572729.792635.3561
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 43 )A1 - 43
2X-RAY DIFFRACTION2chain 'A' and (resid 44 through 70 )A44 - 70
3X-RAY DIFFRACTION3chain 'A' and (resid 71 through 120 )A71 - 120
4X-RAY DIFFRACTION4chain 'A' and (resid 121 through 155 )A121 - 155
5X-RAY DIFFRACTION5chain 'A' and (resid 156 through 180 )A156 - 180
6X-RAY DIFFRACTION6chain 'A' and (resid 181 through 200 )A181 - 200
7X-RAY DIFFRACTION7chain 'A' and (resid 201 through 226 )A201 - 226
8X-RAY DIFFRACTION8chain 'A' and (resid 227 through 243 )A227 - 243
9X-RAY DIFFRACTION9chain 'A' and (resid 244 through 274 )A244 - 274
10X-RAY DIFFRACTION10chain 'A' and (resid 275 through 306 )A275 - 306
11X-RAY DIFFRACTION11chain 'B' and (resid 1 through 43 )B1 - 43
12X-RAY DIFFRACTION12chain 'B' and (resid 44 through 91 )B44 - 91
13X-RAY DIFFRACTION13chain 'B' and (resid 92 through 110 )B92 - 110
14X-RAY DIFFRACTION14chain 'B' and (resid 111 through 155 )B111 - 155
15X-RAY DIFFRACTION15chain 'B' and (resid 156 through 200 )B156 - 200
16X-RAY DIFFRACTION16chain 'B' and (resid 201 through 226 )B201 - 226
17X-RAY DIFFRACTION17chain 'B' and (resid 227 through 274 )B227 - 274
18X-RAY DIFFRACTION18chain 'B' and (resid 275 through 306 )B275 - 306
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 43 )C1 - 43
20X-RAY DIFFRACTION20chain 'C' and (resid 44 through 110 )C44 - 110
21X-RAY DIFFRACTION21chain 'C' and (resid 111 through 200 )C111 - 200
22X-RAY DIFFRACTION22chain 'C' and (resid 201 through 226 )C201 - 226
23X-RAY DIFFRACTION23chain 'C' and (resid 227 through 302 )C227 - 302
24X-RAY DIFFRACTION24chain 'D' and (resid 1 through 43 )D1 - 43
25X-RAY DIFFRACTION25chain 'D' and (resid 44 through 70 )D44 - 70
26X-RAY DIFFRACTION26chain 'D' and (resid 71 through 100 )D71 - 100
27X-RAY DIFFRACTION27chain 'D' and (resid 101 through 200 )D101 - 200
28X-RAY DIFFRACTION28chain 'D' and (resid 201 through 257 )D201 - 257
29X-RAY DIFFRACTION29chain 'D' and (resid 258 through 302 )D258 - 302

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