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- PDB-7axm: Structure of SARS-CoV-2 Main Protease bound to Pelitinib -

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Entry
Database: PDB / ID: 7axm
TitleStructure of SARS-CoV-2 Main Protease bound to Pelitinib
Components3C-like proteinase
KeywordsPEPTIDE BINDING PROTEIN / inhibitor / complex / screen / sars-cov-2
Function / homology
Function and homology information


Maturation of replicase proteins / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Transcription of SARS-CoV-2 sgRNAs / host cell endosome / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Translation of Replicase and Assembly of the Replication Transcription Complex / exoribonuclease activity / modulation by virus of host autophagy / RNA phosphodiester bond hydrolysis, exonucleolytic / mRNA methylation ...Maturation of replicase proteins / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Transcription of SARS-CoV-2 sgRNAs / host cell endosome / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Translation of Replicase and Assembly of the Replication Transcription Complex / exoribonuclease activity / modulation by virus of host autophagy / RNA phosphodiester bond hydrolysis, exonucleolytic / mRNA methylation / double membrane vesicle viral factory outer membrane / suppression by virus of host translation / ISG15-specific protease activity / host cell Golgi apparatus / Replication of the SARS-CoV-2 genome / suppression by virus of host type I interferon production / host cell endoplasmic reticulum / induction by virus of catabolism of host mRNA / SARS coronavirus main proteinase / cytoplasmic viral factory / G-quadruplex RNA binding / suppression by virus of host ISG15-protein conjugation / suppression by virus of host toll-like receptor signaling pathway / protein K48-linked deubiquitination / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-exoribonuclease activity / host cell endoplasmic reticulum-Golgi intermediate compartment / suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / suppression by virus of host NF-kappaB cascade / modulation by virus of host protein ubiquitination / transcription, RNA-templated / protein K63-linked deubiquitination / positive stranded viral RNA replication / protein autoprocessing / viral genome replication / cysteine-type peptidase activity / suppression by virus of host TRAF activity / mRNA (nucleoside-2'-O-)-methyltransferase activity / helicase activity / ubiquitinyl hydrolase 1 / Transferases; Transferring one-carbon groups; Methyltransferases / viral transcription / DNA helicase / methyltransferase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / thiol-dependent deubiquitinase / DNA helicase activity / single-stranded RNA binding / host cell perinuclear region of cytoplasm / methylation / RNA helicase / induction by virus of host autophagy / endonuclease activity / RNA-directed RNA polymerase / suppression by virus of host type I interferon-mediated signaling pathway / viral protein processing / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / RNA helicase activity / transcription, DNA-templated / Hydrolases; Acting on ester bonds / host cell cytoplasm / protein dimerization activity / protein homodimerization activity / zinc ion binding / integral component of membrane / ATP binding / identical protein binding / cytosol
Similarity search - Function
RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nonstructural protein 14, betacoronavirus / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. ...RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nonstructural protein 14, betacoronavirus / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Sarbecovirus Nsp3c-N domain profile. / Betacoronavirus replicase NSP3, N-terminal / Betacoronavirus SUD-C domain / Non-structural protein NSP3, N-terminal, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, coronavirus / DPUP/SUD, C-terminal, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Non-structural protein NSP1 superfamily, betacoronavirus / Viral (Superfamily 1) RNA helicase / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP15, NendoU domain, coronavirus / Nonstructural protein 13, 1B domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, middle domain / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronaviral / Coronavirus replicase NSP15, N-terminal oligomerisation / Coronavirus replicase NSP15, N-terminal oligomerisation / Coronavirus RNA-dependent RNA polymerase, N-terminal / Coronavirus proofreading exoribonuclease / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Coronavirus 2'-O-methyltransferase / Non-structural protein NSP15, middle domain superfamily / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Betacoronavirus Nsp3c-M domain profile. / Betacoronavirus Nsp3c-C domain profile. / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / NendoU domain, nidovirus / Endoribonuclease EndoU-like / Carbamoyl-phosphate synthase subdomain signature 2. / Coronavirus (CoV) Nsp1 globular domain profile. / Betacoronavirus single-stranded poly(A) binding domain / Replicase polyprotein, nucleic acid-binding domain superfamily / Non-structural protein NSP1, betacoronavirus / Betacoronavirus replicase NSP1 / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein 6, betacoronavirus / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Papain-like protease, N-terminal domain superfamily, coronavirus / Betacoronavirus nucleic acid-binding (NAR) / Coronavirus Nsp3a Ubl domain profile. / Non-structural protein NSP3A domain-like superfamily / Coronavirus Nsp4 C-terminal (Nsp4C) 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. / Papain-like protease, thumb domain superfamily, coronavirus / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / Coronavirus Nsp3d Ubl domain profile. / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Lipocalin signature. / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus replicase NSP7 / Non-structural protein NSP7, coronavirus / Peptidase family C16 domain profile. / Non-structural protein NSP7 superfamily, coronavirus / Coronavirus papain-like peptidase / Coronavirus RNA synthesis protein NSP10 / Coronavirus replicase NSP8 / Coronavirus replicase NSP4, N-terminal / Coronavirus replicase NSP3, C-terminal / Non-structural protein 6, coronavirus / Non-structural protein NSP8 superfamily, coronavirus / Coronavirus replicase NSP4, C-terminal / Non-structural protein NSP4, C-terminal, coronavirus / Peptidase C30, coronavirus / Peptidase C16, coronavirus / Non-structural protein NSP9, coronavirus / Non-structural protein NSP8, coronavirus-like / RNA synthesis protein NSP10, coronavirus / Coronavirus main protease (M-pro) domain profile. / RNA synthesis protein NSP10 superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / Non-structural protein NSP9 superfamily, coronavirus / Coronavirus endopeptidase C30 / Non-structural protein NSP4, C-terminal superfamily, coronavirus / Coronavirus replicase NSP3, C-terminal
Similarity search - Domain/homology
Chem-93J / IMIDAZOLE / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.4 Å
AuthorsGuenther, S. / Reinke, P.Y.A. / Oberthuer, D. / Yefanov, O. / Gelisio, L. / Ginn, H. / Lieske, J. / Domaracky, M. / Brehm, W. / Rahmani Mashour, A. ...Guenther, S. / Reinke, P.Y.A. / Oberthuer, D. / Yefanov, O. / Gelisio, L. / Ginn, H. / Lieske, J. / Domaracky, M. / Brehm, W. / Rahmani Mashour, A. / White, T.A. / Knoska, J. / Pena Esperanza, G. / Koua, F. / Tolstikova, A. / Groessler, M. / Fischer, P. / Hennicke, V. / Fleckenstein, H. / Trost, F. / Galchenkova, M. / Gevorkov, Y. / Li, C. / Awel, S. / Paulraj, L.X. / Ullah, N. / Falke, S. / Alves Franca, B. / Schwinzer, M. / Brognaro, H. / Werner, N. / Perbandt, M. / Tidow, H. / Seychell, B. / Beck, T. / Meier, S. / Doyle, J.J. / Giseler, H. / Melo, D. / Lane, T.J. / Dunkel, I. / Peck, A. / Saouane, S. / Hakanpaeae, J. / Meyer, J. / Noei, H. / Gribbon, P. / Ellinger, B. / Kuzikov, M. / Wolf, M. / Zhang, L. / Ehrt, C. / Pletzer-Zelgert, J. / Wollenhaupt, J. / Feiler, C. / Weiss, M. / Schulz, E.C. / Mehrabi, P. / Norton-Baker, B. / Schmidt, C. / Lorenzen, K. / Schubert, R. / Han, H. / Chari, A. / Fernandez Garcia, Y. / Turk, D. / Hilgenfeld, R. / Rarey, M. / Zaliani, A. / Chapman, H.N. / Pearson, A. / Betzel, C. / Meents, A.
Funding support Germany, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
European Commission Germany
Citation
Journal: Science / Year: 2021
Title: X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease.
Authors: Gunther, S. / Reinke, P.Y.A. / Fernandez-Garcia, Y. / Lieske, J. / Lane, T.J. / Ginn, H.M. / Koua, F.H.M. / Ehrt, C. / Ewert, W. / Oberthuer, D. / Yefanov, O. / Meier, S. / Lorenzen, K. / ...Authors: Gunther, S. / Reinke, P.Y.A. / Fernandez-Garcia, Y. / Lieske, J. / Lane, T.J. / Ginn, H.M. / Koua, F.H.M. / Ehrt, C. / Ewert, W. / Oberthuer, D. / Yefanov, O. / Meier, S. / Lorenzen, K. / Krichel, B. / Kopicki, J.D. / Gelisio, L. / Brehm, W. / Dunkel, I. / Seychell, B. / Gieseler, H. / Norton-Baker, B. / Escudero-Perez, B. / Domaracky, M. / Saouane, S. / Tolstikova, A. / White, T.A. / Hanle, A. / Groessler, M. / Fleckenstein, H. / Trost, F. / Galchenkova, M. / Gevorkov, Y. / Li, C. / Awel, S. / Peck, A. / Barthelmess, M. / Schlunzen, F. / Lourdu Xavier, P. / Werner, N. / Andaleeb, H. / Ullah, N. / Falke, S. / Srinivasan, V. / Franca, B.A. / Schwinzer, M. / Brognaro, H. / Rogers, C. / Melo, D. / Zaitseva-Doyle, J.J. / Knoska, J. / Pena-Murillo, G.E. / Mashhour, A.R. / Hennicke, V. / Fischer, P. / Hakanpaa, J. / Meyer, J. / Gribbon, P. / Ellinger, B. / Kuzikov, M. / Wolf, M. / Beccari, A.R. / Bourenkov, G. / von Stetten, D. / Pompidor, G. / Bento, I. / Panneerselvam, S. / Karpics, I. / Schneider, T.R. / Garcia-Alai, M.M. / Niebling, S. / Gunther, C. / Schmidt, C. / Schubert, R. / Han, H. / Boger, J. / Monteiro, D.C.F. / Zhang, L. / Sun, X. / Pletzer-Zelgert, J. / Wollenhaupt, J. / Feiler, C.G. / Weiss, M.S. / Schulz, E.C. / Mehrabi, P. / Karnicar, K. / Usenik, A. / Loboda, J. / Tidow, H. / Chari, A. / Hilgenfeld, R. / Uetrecht, C. / Cox, R. / Zaliani, A. / Beck, T. / Rarey, M. / Gunther, S. / Turk, D. / Hinrichs, W. / Chapman, H.N. / Pearson, A.R. / Betzel, C. / Meents, A.
#1: Journal: Biorxiv / Year: 2020
Title: Inhibition of SARS-CoV-2 main protease by allosteric drug-binding
Authors: Guenther, S. / Reinke, P.Y.A., / Fernandez-Garcia, Y., / Lieske, J., / Lane, T.J., / Ginn, H.M., / Koua, F.H.M., / Ehrt, C., / Ewert, W., / Oberthuer, D., / Yefanov, O., / Meier, S., / ...Authors: Guenther, S. / Reinke, P.Y.A., / Fernandez-Garcia, Y., / Lieske, J., / Lane, T.J., / Ginn, H.M., / Koua, F.H.M., / Ehrt, C., / Ewert, W., / Oberthuer, D., / Yefanov, O., / Meier, S., / Lorenzen, K., / Krichel, B., / Kopicki, J.D., / Gelisio, L., / Brehm, W., / Dunkel , I., / Seychell , B., / Gieseler , H., / Norton-Baker , B., / Escudero-Perez, B., / Domaracky , M., / Saouane, S., / Tolstikova , A., / White, T.A., / Hanle, A., / Groessler , M., / Fleckenstein , H., / Trost , F., / Galchenkova , M., / Gevorkov , Y., / Li , C., / Awel , S., / Peck, A. / Barthelmess , M., / Schluenzen , F., / Paulraj , L.X., / Werner , N., / Andaleeb , H., / Ullah , N., / Falke , S., / Srinivasan, V., / Franca , B., / Schwinzer , M., / Brognaro , H., / Rogers , C., / Melo , D., / Doyle , J.J., / Knoska , J., / Pena Murillo, G.E., / Rahmani Mashhour, A., / Guicking , F., / Hennicke , V., / Fischer , P., / Hakanpaeae , J., / Meyer , J., / Gribbon , P., / Ellinger , B., / Kuzikov , M., / Wolf , M., / Burenkov, G., / von Stetten, D., / Pompidor, G., / Bento, I., / Panneerselvam, S., / Karpics, I., / Schneider , T.R., / Garcia Alai, M., / Niebling, S., / Guenther , C., / Schmidt , C., / Schubert , R., / Han , H., / Boger, J., / Monteiro , D., / Zhang, L., / Sun, X., / Pletzer-Zelgert , J., / Wollenhaupt , J., / Feiler , C., / Weiss , M., / Schulz , E.C., / Mehrabi , P., / Karnicar , K., / Usenik, A., / Loboda , J., / Tidow , H., / Chari , A., / Hilgenfeld , R., / Uetrecht , C., / Cox , R., / Zaliani , A., / Beck , T., / Rarey , M., / Guenther , S., / Turk , D., / Hinrichs , W., / Chapman , H.N., / Pearson , A., / Betzel , C., / Meents , A.
History
DepositionNov 9, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 2, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 9, 2020Group: Database references / Derived calculations
Category: citation_author / pdbx_struct_assembly ...citation_author / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details ..._pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.oper_expression / _pdbx_struct_assembly_prop.value
Revision 1.2Apr 14, 2021Group: Database references / Source and taxonomy / Structure summary
Category: citation / citation_author ...citation / citation_author / entity / entity_name_com / entity_src_gen
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity_name_com.name / _entity_src_gen.gene_src_common_name
Revision 1.3May 19, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 3C-like proteinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,6757
Polymers33,8261
Non-polymers8506
Water6,521362
1
A: 3C-like proteinase
hetero molecules

A: 3C-like proteinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,35014
Polymers67,6512
Non-polymers1,69912
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area4800 Å2
ΔGint0 kcal/mol
Surface area26260 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)113.400, 53.200, 44.776
Angle α, β, γ (deg.)90.000, 103.054, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Components on special symmetry positions
IDModelComponents
11A-847-

HOH

21A-928-

HOH

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Components

#1: Protein 3C-like proteinase / 3CL-PRO / 3CLp / Main protease / Mpro / Non-structural protein 5 / nsp5 / SARS coronavirus main proteinase


Mass: 33825.547 Da / Num. of mol.: 1
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-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#3: Chemical ChemComp-93J / (2E)-N-{4-[(3-chloro-4-fluorophenyl)amino]-3-cyano-7-ethoxyquinolin-6-yl}-4-(dimethylamino)but-2-enamide


Mass: 467.923 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H23ClFN5O2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C3H5N2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 362 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 1.93 Å3/Da / Density % sol: 36.31 %
Crystal growTemperature: 291 K / Method: vapor diffusion / pH: 7.5 / Details: 0.1 M MIB pH 7.5, 25% PEG1500, 5% DMSO

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.033 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 28, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 1.4→26.6 Å / Num. obs: 50456 / % possible obs: 98.59 % / Redundancy: 3.8 % / Biso Wilson estimate: 18.59 Å2 / CC1/2: 0.998 / Net I/σ(I): 10.07
Reflection shellResolution: 1.4→1.45 Å / Num. unique obs: 4883 / CC1/2: 0.43

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PHENIX1.17.1_3660refinement
DIALSdata reduction
DIALSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6nyq
Resolution: 1.4→26.6 Å / SU ML: 0.1908 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.8036
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2095 2000 3.97 %
Rwork0.1428 48427 -
obs0.1454 50427 98.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 27.29 Å2
Refinement stepCycle: LAST / Resolution: 1.4→26.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2368 0 54 362 2784
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01022600
X-RAY DIFFRACTIONf_angle_d1.17213545
X-RAY DIFFRACTIONf_chiral_restr0.0865386
X-RAY DIFFRACTIONf_plane_restr0.008467
X-RAY DIFFRACTIONf_dihedral_angle_d18.5938960
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.4-1.440.36071360.31263283X-RAY DIFFRACTION95.32
1.44-1.470.35081410.27593420X-RAY DIFFRACTION97.64
1.47-1.520.26311410.23443395X-RAY DIFFRACTION97.84
1.52-1.570.31161420.21933450X-RAY DIFFRACTION98.01
1.57-1.620.28991420.20093434X-RAY DIFFRACTION98.49
1.62-1.690.25561410.18453437X-RAY DIFFRACTION98.46
1.69-1.760.24191430.15973447X-RAY DIFFRACTION98.71
1.76-1.860.23671430.14783457X-RAY DIFFRACTION98.71
1.86-1.970.19541420.13233465X-RAY DIFFRACTION98.79
1.97-2.130.21021460.1253507X-RAY DIFFRACTION99.54
2.13-2.340.17971430.11883495X-RAY DIFFRACTION99.75
2.34-2.680.19871450.12743519X-RAY DIFFRACTION99.75
2.68-3.370.18561460.13193528X-RAY DIFFRACTION99.86
3.37-26.60.19231490.12923590X-RAY DIFFRACTION99.57

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