[English] 日本語
Yorodumi
- PDB-7prz: Crystal structure of the receptor binding domain of SARS-CoV-2 be... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7prz
TitleCrystal structure of the receptor binding domain of SARS-CoV-2 beta variant spike glycoprotein in complex with beta-22 Fabs
Components
  • Beta-22 Fab heavy chain
  • Beta-22 Fab light chain
  • Spike protein S1
KeywordsVIRAL PROTEIN / SARS-CoV-2 alpha variant / beta variant / gamma variant / delta variant / B.1.1.7 / B.1.351 / P.1 / B.1.617.2 / antibody / receptor-binding-domain / spike / neutralisation / VIRAL PROTEIN/IMMUNE SYSTEM
Function / homology
Function and homology information


Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell ...Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / membrane fusion / Attachment and Entry / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / symbiont-mediated suppression of host innate immune response / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane
Similarity search - Function
Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal / Spike glycoprotein, betacoronavirus / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus ...Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal / Spike glycoprotein, betacoronavirus / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Severe acute respiratory syndrome coronavirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsZhou, D. / Ren, J. / Stuart, D.I.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/ N00065X/1 United Kingdom
CAMS Innovation Fund for Medical Sciences (CIFMS)2018-I2M-2-002 United Kingdom
CitationJournal: Cell Host Microbe / Year: 2022
Title: The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants.
Authors: Chang Liu / Daming Zhou / Rungtiwa Nutalai / Helen M E Duyvesteyn / Aekkachai Tuekprakhon / Helen M Ginn / Wanwisa Dejnirattisai / Piyada Supasa / Alexander J Mentzer / Beibei Wang / James ...Authors: Chang Liu / Daming Zhou / Rungtiwa Nutalai / Helen M E Duyvesteyn / Aekkachai Tuekprakhon / Helen M Ginn / Wanwisa Dejnirattisai / Piyada Supasa / Alexander J Mentzer / Beibei Wang / James Brett Case / Yuguang Zhao / Donal T Skelly / Rita E Chen / Sile Ann Johnson / Thomas G Ritter / Chris Mason / Tariq Malik / Nigel Temperton / Neil G Paterson / Mark A Williams / David R Hall / Daniel K Clare / Andrew Howe / Philip J R Goulder / Elizabeth E Fry / Michael S Diamond / Juthathip Mongkolsapaya / Jingshan Ren / David I Stuart / Gavin R Screaton /
Abstract: Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape ...Alpha-B.1.1.7, Beta-B.1.351, Gamma-P.1, and Delta-B.1.617.2 variants of SARS-CoV-2 express multiple mutations in the spike protein (S). These may alter the antigenic structure of S, causing escape from natural or vaccine-induced immunity. Beta is particularly difficult to neutralize using serum induced by early pandemic SARS-CoV-2 strains and is most antigenically separated from Delta. To understand this, we generated 674 mAbs from Beta-infected individuals and performed a detailed structure-function analysis of the 27 most potent mAbs: one binding the spike N-terminal domain (NTD), the rest the receptor-binding domain (RBD). Two of these RBD-binding mAbs recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 18 target mutated residues in Beta: K417N, E484K, and N501Y. There is a major response to N501Y, including a public IgVH4-39 sequence, with E484K and K417N also targeted. Recognition of these key residues underscores why serum from Beta cases poorly neutralizes early pandemic and Delta viruses.
History
DepositionSep 22, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 15, 2021Provider: repository / Type: Initial release
Revision 1.1Dec 22, 2021Group: Data collection / Database references ...Data collection / Database references / Source and taxonomy / Structure summary
Category: entity / entity_src_gen ...entity / entity_src_gen / reflns / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity_src_gen.gene_src_common_name ..._entity.pdbx_description / _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_gene / _reflns.d_resolution_low / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_db_accession
Revision 1.2Dec 29, 2021Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Jan 26, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.year
Revision 1.4Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.5Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
H: Beta-22 Fab heavy chain
E: Spike protein S1
L: Beta-22 Fab light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,68920
Polymers72,3103
Non-polymers2,37917
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9140 Å2
ΔGint-173 kcal/mol
Surface area30070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)199.378, 199.378, 202.444
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number155
Space group name H-MH32
Space group name HallR32"
Symmetry operation#1: x,y,z
#2: -y,x-y,z
#3: -x+y,-x,z
#4: x-y,-y,-z
#5: -x,-x+y,-z
#6: y,x,-z
#7: x+1/3,y+2/3,z+2/3
#8: -y+1/3,x-y+2/3,z+2/3
#9: -x+y+1/3,-x+2/3,z+2/3
#10: x-y+1/3,-y+2/3,-z+2/3
#11: -x+1/3,-x+y+2/3,-z+2/3
#12: y+1/3,x+2/3,-z+2/3
#13: x+2/3,y+1/3,z+1/3
#14: -y+2/3,x-y+1/3,z+1/3
#15: -x+y+2/3,-x+1/3,z+1/3
#16: x-y+2/3,-y+1/3,-z+1/3
#17: -x+2/3,-x+y+1/3,-z+1/3
#18: y+2/3,x+1/3,-z+1/3

-
Components

-
Antibody , 2 types, 2 molecules HL

#1: Antibody Beta-22 Fab heavy chain


Mass: 24457.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#3: Antibody Beta-22 Fab light chain


Mass: 24205.961 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)

-
Protein / Non-polymers , 2 types, 16 molecules E

#2: Protein Spike protein S1


Mass: 23646.551 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2
#6: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: SO4

-
Sugars , 2 types, 2 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE
#5: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE

-
Details

Has ligand of interestN
Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 5.35 Å3/Da / Density % sol: 77.03 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: containing 0.2 M Lithium sulfate, 0.1 M MES pH 6.0 and 20% (w/v) PEG 4000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97626 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jun 26, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97626 Å / Relative weight: 1
ReflectionResolution: 3.2→87.32 Å / Num. obs: 25724 / % possible obs: 99.8 % / Redundancy: 57.5 % / Biso Wilson estimate: 121.27 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.473 / Rpim(I) all: 0.063 / Net I/σ(I): 9.4
Reflection shellResolution: 3.2→3.25 Å / Mean I/σ(I) obs: 0.5 / Num. unique obs: 1210 / CC1/2: 0.549

-
Processing

Software
NameVersionClassification
GDA1.19_4092data collection
PHENIX1.19_4092refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7NXA
Resolution: 3.2→87.32 Å / SU ML: 0.4803 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.5351
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2229 1326 5.17 %
Rwork0.1904 24332 -
obs0.1922 25658 99.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 131.38 Å2
Refinement stepCycle: LAST / Resolution: 3.2→87.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4950 0 137 0 5087
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00345205
X-RAY DIFFRACTIONf_angle_d0.60127096
X-RAY DIFFRACTIONf_chiral_restr0.0448786
X-RAY DIFFRACTIONf_plane_restr0.0053892
X-RAY DIFFRACTIONf_dihedral_angle_d11.75351839
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.320.3591390.33832627X-RAY DIFFRACTION97.7
3.32-3.480.26061410.27032682X-RAY DIFFRACTION99.93
3.48-3.660.26321510.2362669X-RAY DIFFRACTION99.89
3.66-3.890.27631390.21572705X-RAY DIFFRACTION99.96
3.89-4.190.22311490.19272697X-RAY DIFFRACTION99.96
4.19-4.610.17591280.15062728X-RAY DIFFRACTION100
4.61-5.280.19141470.15082708X-RAY DIFFRACTION100
5.28-6.650.24111460.19492747X-RAY DIFFRACTION100
6.65-87.320.21121860.18492769X-RAY DIFFRACTION99.66
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)
18.21992070493-1.057264027354.257389704143.021402229541.419441051226.311407633120.7652413326651.2954287314-0.178027073145-0.976528348593-0.878971785184-0.309101691381-0.310850571316-0.2290577308280.1778252592281.358368277970.6441093571580.2584316300411.30346647090.0633086891380.97748698976462.0296712332-31.059168687433.6522982132
23.1707025382-0.7511975888891.213921555531.905516277020.7042183055631.180196471710.3300159602870.414846430624-0.0583018486762-0.251927269907-0.3011148442160.0308619047061-0.285698353314-0.449602484776-0.1284905064971.214137374370.544168560020.1035261133381.370807238740.05080318443590.96096274838259.0978472885-31.469334984332.1471560893
32.368761077732.017329692.030986972512.367435313542.268654352032.159567078481.609924321760.314594701042-0.4506605360760.133816098603-1.234950342680.929346709842-1.348969825660.00974271508204-2.37310363241.204995116140.4040247908350.1725725908421.88626304931-0.1479243854631.2463232889223.6542549768-15.280719030549.7178712591
44.94677473317-2.64356298222-1.187060596795.06460953767-3.853921866244.062837107550.9377639463860.946946886950.359034522441-0.564863085449-0.9902465539010.316339919214-0.419075111548-0.0365438623260.09931024505011.033442723010.3138051285770.008234188994311.50659542209-0.3873085647051.1286359030733.6641216144-13.635686071246.5030395424
51.196075043611.74808676538-0.6999121251014.330819559340.459703488021.479653936520.3402844588290.0463994496277-0.4210329015470.4159151001310.024268193099-0.722345206431-0.9590799578150.448125294149-0.05990098589871.260208392340.1348844320730.2478081629060.9448092937710.09127700709671.2511360989998.6921932776-38.506964432860.826280463
65.96696877737-1.921814840271.37991949033.27274860972-1.118559097596.42723231274-0.0930228698087-0.2201401917060.5188072048150.6073719350030.576952513949-0.22754602984-0.891260652214-0.374122963922-0.6014616356980.9131125609730.2537552580540.1074952164650.899004133104-0.02302982451891.0040583644290.3889597999-42.509831016869.3977475935
73.14096970732-0.0007584973607343.241317002372.61686519381-3.867741637298.69315871456-0.651918795441-0.5035686023750.3969124470560.6420446523761.098768057670.232460465502-1.34642666532-1.02445913967-0.3331324692240.7966338972040.2601284744270.26253618910.8017164291360.07534001424971.0445093416785.769021841-42.858891978257.4416697057
80.84760831099-0.7398170247141.872717201861.80841653659-0.6954947984345.740635854730.2258238606820.06499092566360.191630521852-0.1125039951670.00510978154275-0.126150575788-0.335855096293-0.616985795199-0.3932333928210.8378005309620.2106842323060.2403380601550.8443793021660.1447558532791.0350572639183.7991517016-42.823583204250.4781699355
94.418904073941.561868848830.8953588729924.869713243281.406443921559.64869471741-0.2792752090630.306487706085-0.895647323704-0.1592793331890.6929727946510.2277129661320.521673596771-0.714621656758-0.616230304891.516647301130.3794076260380.2431075133211.267481807440.04781457251931.1190073680581.7044100313-48.402426785728.2760009396
101.94112602123-1.790126992632.943603592561.47436098964-1.470123030584.982150345640.0917970769015-0.2184333733940.2543906316780.1764568888220.3137523041450.0336185945822-0.889786664331-0.567232495915-0.2568308478850.9645502534840.1693146232780.261340375340.8985464599750.07177495813610.97519165437685.594608283-41.033382608156.9045201283
117.57372751743-1.40083659906-0.427464520896.56579835016-0.4882436062976.034465440350.0565144525994-0.084893529088-0.7156989288820.534408762455-0.2074189619640.2559660063370.530288987371-0.1057038390960.2491946540061.225649942180.187132013509-0.01409658815830.932419487654-0.1109448868220.92095286542955.7602403139-45.191216598750.1144016477
125.38918483109-4.72673393210.1790917935043.164038585850.982932470318-0.4516906971230.5337356165661.1801964263-0.775562732754-0.497723388654-0.9585980608891.053531742850.423289965123-0.5388661702280.4708567379621.003877858140.09578022316530.03164110705781.66202911175-0.410848420441.3693068916829.1878761405-30.209040007846.3153591189
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'H' and (resid 1 through 60 )HA1 - 601 - 60
22chain 'H' and (resid 61 through 130 )HA61 - 13061 - 130
33chain 'H' and (resid 131 through 145 )HA131 - 145131 - 143
44chain 'H' and (resid 146 through 227 )HA146 - 227144 - 225
55chain 'E' and (resid 329 through 353 )EB329 - 3531 - 25
66chain 'E' and (resid 354 through 391 )EB354 - 39126 - 63
77chain 'E' and (resid 392 through 409 )EB392 - 40964 - 81
88chain 'E' and (resid 410 through 469 )EB410 - 46982 - 141
99chain 'E' and (resid 470 through 489 )EB470 - 489142 - 161
1010chain 'E' and (resid 490 through 526 )EB490 - 526162 - 198
1111chain 'L' and (resid 1 through 96 )LC1 - 961 - 96
1212chain 'L' and (resid 97 through 217)LC97 - 40197

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more