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- PDB-2vj1: A Structural View of the Inactivation of the SARS-Coronavirus Mai... -

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Basic information

Entry
Database: PDB / ID: 2vj1
TitleA Structural View of the Inactivation of the SARS-Coronavirus Main Proteinase by Benzotriazole Esters
ComponentsSARS CORONAVIRUS MAIN PROTEINASE3C-like protease
KeywordsHYDROLASE / SARS / PROTEASE / POLYPROTEIN / THIOL PROTEASE / RIBOSOMAL FRAMESHIFT / SARS CORONAVIRUS MAIN PROTEINASE
Function / homology
Function and homology information


cysteine-type deubiquitinase activity => GO:0004843 / positive regulation of ubiquitin-specific protease activity / Maturation of replicase proteins / Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Transcription of SARS-CoV-1 sgRNAs / Lys48-specific deubiquitinase activity / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-1 genome / host cell membrane / viral genome replication ...cysteine-type deubiquitinase activity => GO:0004843 / positive regulation of ubiquitin-specific protease activity / Maturation of replicase proteins / Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) / Transcription of SARS-CoV-1 sgRNAs / Lys48-specific deubiquitinase activity / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-1 genome / host cell membrane / viral genome replication / mRNA (guanine-N7-)-methyltransferase activity / Transferases; Transferring one-carbon groups; Methyltransferases / exoribonuclease complex / viral RNA-directed RNA polymerase complex / endoribonuclease complex / endopeptidase complex / 5'-3' RNA helicase activity / mRNA cap methyltransferase complex / RNA phosphodiester bond hydrolysis, exonucleolytic / positive regulation of RNA biosynthetic process / Lyases; Phosphorus-oxygen lyases / mRNA methylation / double membrane vesicle viral factory outer membrane / suppression by virus of host translation / ISG15-specific peptidase activity / SARS coronavirus main proteinase / suppression by virus of host type I interferon production / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-exoribonuclease activity / host cell endosome / host cell endoplasmic reticulum-Golgi intermediate compartment / induction by virus of catabolism of host mRNA / cytoplasmic viral factory / protein K48-linked deubiquitination / G-quadruplex RNA binding / suppression by virus of host ISG15-protein conjugation / 7-methylguanosine mRNA capping / transcription, RNA-templated / viral transcription / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / suppression by virus of host toll-like receptor signaling pathway / host cell Golgi apparatus / host cell endoplasmic reticulum / suppression by virus of host NF-kappaB cascade / modulation by virus of host protein ubiquitination / protein K63-linked deubiquitination / methyltransferase cap1 / mRNA (nucleoside-2'-O-)-methyltransferase activity / positive stranded viral RNA replication / suppression by virus of host TRAF activity / protein autoprocessing / helicase activity / double-stranded RNA binding / ubiquitinyl hydrolase 1 / DNA helicase / DNA helicase activity / cysteine-type deubiquitinase activity / single-stranded RNA binding / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / protein processing / host cell perinuclear region of cytoplasm / transferase activity / viral protein processing / RNA helicase / lyase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / suppression by virus of host gene expression / endonuclease activity / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / transcription, DNA-templated / suppression by virus of host type I interferon-mediated signaling pathway / host cell cytoplasm / protein dimerization activity / ATP hydrolysis activity / zinc ion binding / integral component of membrane / ATP binding / identical protein binding
Similarity search - Function
Non-structural protein 3, SUD-N macrodomain, SARS-CoV / main proteinase (3clpro) structure, domain 3 / main proteinase (3clpro) structure, domain 3 / RNA-dependent RNA polymerase, SARS-CoV-like / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 14, betacoronavirus / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. ...Non-structural protein 3, SUD-N macrodomain, SARS-CoV / main proteinase (3clpro) structure, domain 3 / main proteinase (3clpro) structure, domain 3 / RNA-dependent RNA polymerase, SARS-CoV-like / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 14, betacoronavirus / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Viral (Superfamily 1) RNA helicase / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP15, NendoU domain, coronavirus / Nonstructural protein 13, 1B domain, coronavirus / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerisation / RNA polymerase, N-terminal, coronavirus / Non-structural protein 14, coronavirus / Nonstructural protein 15, middle domain, coronavirus / Non-structural protein NSP16, coronavirus-like / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Coronaviridae zinc-binding (CV ZBD) domain profile. / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / NendoU domain, nidovirus / Endoribonuclease EndoU-like / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Non-structural protein NSP1 superfamily, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Betacoronavirus replicase NSP3, N-terminal / Non-structural protein NSP3, N-terminal, betacoronavirus / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus SUD-C domain / (+)RNA virus helicase core domain profile. / (+) RNA virus helicase core domain / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Betacoronavirus Nsp3c-M domain profile. / Betacoronavirus replicase NSP1 / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Betacoronavirus single-stranded poly(A) binding domain / Non-structural protein NSP1, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / Betacoronavirus Nsp3c-C domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3A domain-like superfamily / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, N-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / Coronavirus Nsp4 C-terminal (Nsp4C) domain profile. / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Papain-like protease, thumb domain superfamily, coronavirus / Coronavirus replicase NSP7 / Peptidase family C16 domain profile. / Non-structural protein NSP7, coronavirus / Non-structural protein NSP4, N-terminal, coronavirus / Non-structural protein NSP7 superfamily, coronavirus / Coronavirus endopeptidase C30 / Coronavirus papain-like peptidase / Non-structural protein NSP9 superfamily, coronavirus / Non-structural protein 6, coronavirus / Coronavirus replicase NSP8 / Coronavirus RNA synthesis protein NSP10 / Coronavirus replicase NSP4, C-terminal / Coronavirus replicase NSP6 / Coronavirus replicase NSP4, N-terminal / Coronavirus replicase NSP3, C-terminal / Coronavirus main protease (M-pro) domain profile. / Coronavirus replicase NSP3, C-terminal / Peptidase C16, coronavirus / Peptidase C30, coronavirus / Non-structural protein NSP9, coronavirus / Peptidase C30, domain 3, coronavirus
Similarity search - Domain/homology
3C-like proteinase / BENZOIC ACID / 4-(DIMETHYLAMINO)BENZOIC ACID / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesHUMAN SARS CORONAVIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsVerschueren, K.H.G. / Pumpor, K. / Anemueller, S. / Mesters, J.R. / Hilgenfeld, R.
CitationJournal: Chem.Biol. / Year: 2008
Title: A Structural View of the Inactivation of the Sars Coronavirus Main Proteinase by Benzotriazole Esters.
Authors: Verschueren, K.H.G. / Pumpor, K. / Anemueller, S. / Chen, S. / Mesters, J.R. / Hilgenfeld, R.
History
DepositionDec 6, 2007Deposition site: PDBE / Processing site: PDBE
SupersessionJul 1, 2008ID: 2CGG
Revision 1.0Jul 1, 2008Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 24, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SARS CORONAVIRUS MAIN PROTEINASE
B: SARS CORONAVIRUS MAIN PROTEINASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,2087
Polymers68,6862
Non-polymers5225
Water5,441302
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2810 Å2
ΔGint-22 kcal/mol
Surface area30630 Å2
MethodPQS
Unit cell
Length a, b, c (Å)52.231, 97.760, 67.709
Angle α, β, γ (deg.)90.00, 103.01, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein SARS CORONAVIRUS MAIN PROTEINASE / 3C-like protease


Mass: 34343.129 Da / Num. of mol.: 2 / Fragment: RESIDUES 3242-3544
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HUMAN SARS CORONAVIRUS / Production host: ESCHERICHIA COLI (E. coli)
References: UniProt: A7J8L3, UniProt: P0C6X7*PLUS, EC: 3.4.34.-
#2: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-BEZ / BENZOIC ACID / Benzoic acid


Mass: 122.121 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H6O2
#4: Chemical ChemComp-XP1 / 4-(DIMETHYLAMINO)BENZOIC ACID


Mass: 165.189 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H11NO2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 302 / 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: 2.5 Å3/Da / Density % sol: 50.2 % / Description: NONE
Crystal growpH: 6.5
Details: 5% PEG10000, 0.1M MES PH6.5, 3% ETHYLNE GLYCOL, 50MM NH4-ACETATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.8157
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 7, 2005 / Details: BENT MIRROR
RadiationMonochromator: TRIANGULAR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8157 Å / Relative weight: 1
ReflectionResolution: 2.25→39.27 Å / Num. obs: 31422 / % possible obs: 99.7 % / Observed criterion σ(I): 2 / Redundancy: 3.2 % / Biso Wilson estimate: 38.14 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 12.9
Reflection shellResolution: 2.25→2.34 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 1.91 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.3.0037refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1UJ1
Resolution: 2.25→65.94 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.919 / SU B: 13.502 / SU ML: 0.175 / Cross valid method: THROUGHOUT / ESU R: 0.302 / ESU R Free: 0.241 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.256 1575 5 %RANDOM
Rwork0.183 ---
obs0.187 29847 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 43.84 Å2
Baniso -1Baniso -2Baniso -3
1-1.52 Å20 Å21.28 Å2
2--0.84 Å20 Å2
3----1.78 Å2
Refinement stepCycle: LAST / Resolution: 2.25→65.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4652 0 29 302 4983
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0224845
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5741.9536586
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.5185613
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.73224.292219
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.44415787
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.6081525
X-RAY DIFFRACTIONr_chiral_restr0.1070.2742
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.023705
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2160.22167
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.310.23245
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.210.2289
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2150.259
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1590.214
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.8671.53077
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.48124872
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.17331988
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.1714.51708
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.25→2.31 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.379 102
Rwork0.237 2213
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)
131.396519.1582-13.810416.758-13.082310.351-1.02570.1294-3.7348-0.9618-0.7414-1.44770.3738-0.43041.767100.0560.1746-0.1205-0.01020.4584-14.7183-7.991924.3341
21.9794-0.192-1.38593.51361.3932.47310.3460.11350.3668-0.8171-0.0245-0.327-0.8035-0.048-0.32150.1833-0.00510.1105-0.17730.01650.0113-4.771423.511317.4577
31.7725-0.953-0.88613.66991.45412.24970.13350.0678-0.0139-0.3039-0.0227-0.0838-0.2526-0.0226-0.1108-0.0575-0.0242-0.0071-0.13730.0169-0.075-4.28797.186217.2176
42.33756.4137-2.494626.0876-10.797513.736-0.18090.18190.1904-2.91180.58030.39420.1367-0.172-0.39940.3313-0.01010.0654-0.109-0.0209-0.04890.35110.32824.179
52.81861.4558-2.0152.8668-2.76683.6531-0.3809-0.0384-0.2443-0.35470.0508-0.20070.48810.10870.33-0.0575-0.02790.02-0.1513-0.00020.0031.7083-19.950820.399
64.35142.03860.51547.0451-1.89834.3403-0.07470.2850.13160.02980.15390.75790.1484-0.6584-0.0792-0.1621-0.0205-0.0249-0.09110.0149-0.0342-7.7853-16.224519.8816
730.80752.7199.66852.9091-2.04226.17550.82942.8444-0.9884-0.5322-0.5644-0.8577-0.58870.0955-0.265-0.06520.0108-0.07180.1897-0.0886-0.0548-16.5305-0.741214.8189
83.14751.7423-1.17441.7653-1.56564.19520.277-0.93220.25840.3281-0.24220-0.4257-0.3462-0.0348-0.128-0.0269-0.00040.2746-0.0912-0.1835-28.50040.289745.8922
93.60341.52961.29592.4697-0.5063.79830.064-0.2955-0.07260.0419-0.0898-0.09480.0508-0.2540.0258-0.1415-0.0225-0.0174-0.01-0.0157-0.1208-28.0215-3.76629.8549
104.06390.3978-5.59061.5696-9.11355.6248-0.4649-0.3896-0.5505-0.38080.14420.29414.4562-0.26650.32070.6055-0.00980.02590.18430.00420.1315-31.9523-17.980126.1493
116.50070.3496-2.04262.8218-0.06243.7713-0.06810.87870.1225-0.12850.17810.0613-0.0302-0.1801-0.11-0.1526-0.0246-0.02380.1120.0086-0.1863-31.2759-7.84272.1272
124.7496-0.2172-1.46063.24590.06244.6452-0.0520.3927-0.00230.06720.0646-0.4244-0.06230.3183-0.0127-0.1634-0.0486-0.04810.0579-0.0003-0.1438-22.4552-7.44927.232
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 7
2X-RAY DIFFRACTION2A8 - 98
3X-RAY DIFFRACTION3A99 - 188
4X-RAY DIFFRACTION4A189 - 200
5X-RAY DIFFRACTION5A201 - 269
6X-RAY DIFFRACTION6A270 - 301
7X-RAY DIFFRACTION7B2 - 7
8X-RAY DIFFRACTION8B8 - 98
9X-RAY DIFFRACTION9B99 - 188
10X-RAY DIFFRACTION10B189 - 200
11X-RAY DIFFRACTION11B201 - 269
12X-RAY DIFFRACTION12B270 - 301

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