[English] 日本語
Yorodumi
- PDB-2wr1: structure of influenza H2 hemagglutinin with human receptor -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2wr1
Titlestructure of influenza H2 hemagglutinin with human receptor
ComponentsHEMAGGLUTININ
KeywordsVIRAL PROTEIN / GLYCOPROTEIN / LIPOPROTEIN / ENVELOPE PROTEIN
Function / homology
Function and homology information


sialate O-acetylesterase activity / sialate O-acetylesterase / viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / membrane
Similarity search - Function
Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
6'-sialyl-N-acetyllactosamine / Hemagglutinin-esterase-fusion glycoprotein
Similarity search - Component
Biological speciesUNIDENTIFIED INFLUENZA VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsLiu, J. / Stevens, D.J. / Haire, L.F. / Walker, P.A. / Coombs, P.J. / Russell, R.J. / Gamblin, S.J. / Skehel, J.J.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2009
Title: From the Cover: Structures of Receptor Complexes Formed by Hemagglutinins from the Asian Influenza Pandemic of 1957.
Authors: Liu, J. / Stevens, D.J. / Haire, L.F. / Walker, P.A. / Coombs, P.J. / Russell, R.J. / Gamblin, S.J. / Skehel, J.J.
History
DepositionAug 29, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 29, 2009Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_seq_id_1 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Apr 9, 2025Group: Advisory / Data collection ...Advisory / Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_unobs_or_zero_occ_atoms
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 3.0Oct 1, 2025Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / pdbx_distant_solvent_atoms ...atom_site / pdbx_distant_solvent_atoms / pdbx_modification_feature / pdbx_nonpoly_scheme / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_conn
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HEMAGGLUTININ
B: HEMAGGLUTININ
C: HEMAGGLUTININ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)176,71611
Polymers172,7813
Non-polymers3,9358
Water22,2851237
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18610 Å2
ΔGint-13.94 kcal/mol
Surface area59570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.565, 141.457, 199.505
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

-
Protein / Non-polymers , 2 types, 1240 molecules ABC

#1: Protein HEMAGGLUTININ


Mass: 57593.816 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) UNIDENTIFIED INFLUENZA VIRUS / References: UniProt: D0VWP8*PLUS
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1237 / Source method: isolated from a natural source / Formula: H2O

-
Sugars , 5 types, 8 molecules

#2: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / 6'-sialyl-N-acetyllactosamine


Type: oligosaccharide, Oligosaccharide / Class: Glycan component / Mass: 674.604 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: 6'-sialyl-N-acetyllactosamine
DescriptorTypeProgram
DNeup5Aca2-6DGalpb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,3,2/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-3/a4-b1_b6-c2WURCSPDB2Glycan 1.1.0
[][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(6+2)][a-D-Neup5Ac]{}}}LINUCSPDB-CARE
#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#4: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp3Me]{}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

-
Details

Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.68 Å3/Da / Density % sol: 53.7 % / Description: NONE

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.979
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.1→30 Å / Num. obs: 115302 / % possible obs: 99.8 % / Observed criterion σ(I): 3.7 / Redundancy: 6.4 % / Biso Wilson estimate: 41.4 Å2 / Rmerge(I) obs: 0.08

-
Processing

SoftwareName: PHENIX / Version: (PHENIX.REFINE) / Classification: refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→30 Å / SU ML: 0.3 / σ(F): 1.33 / Phase error: 24.02 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2297 5780 5 %
Rwork0.1958 --
obs0.1975 115302 99.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 69.61 Å2 / ksol: 0.356 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.8908 Å2-0 Å20 Å2
2---0.3299 Å20 Å2
3---1.2207 Å2
Refinement stepCycle: LAST / Resolution: 2.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11605 0 252 1237 13094
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02112169
X-RAY DIFFRACTIONf_angle_d1.60816475
X-RAY DIFFRACTIONf_dihedral_angle_d17.7074503
X-RAY DIFFRACTIONf_chiral_restr0.1251820
X-RAY DIFFRACTIONf_plane_restr0.0092113
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12390.29781920.27053576X-RAY DIFFRACTION100
2.1239-2.14880.33072150.25523575X-RAY DIFFRACTION100
2.1488-2.1750.28851750.24663670X-RAY DIFFRACTION100
2.175-2.20260.33141900.24553576X-RAY DIFFRACTION100
2.2026-2.23150.26881780.22923649X-RAY DIFFRACTION100
2.2315-2.26210.26291880.21573595X-RAY DIFFRACTION100
2.2621-2.29440.26491880.2173634X-RAY DIFFRACTION100
2.2944-2.32860.25391870.21453644X-RAY DIFFRACTION100
2.3286-2.3650.26071910.2223591X-RAY DIFFRACTION100
2.365-2.40380.2532080.21553648X-RAY DIFFRACTION100
2.4038-2.44520.30771840.22333598X-RAY DIFFRACTION100
2.4452-2.48960.2691990.2173645X-RAY DIFFRACTION100
2.4896-2.53750.26981660.21973630X-RAY DIFFRACTION100
2.5375-2.58930.25711880.223637X-RAY DIFFRACTION100
2.5893-2.64550.31721970.22293630X-RAY DIFFRACTION100
2.6455-2.7070.27911990.21583608X-RAY DIFFRACTION100
2.707-2.77470.24861880.20763667X-RAY DIFFRACTION100
2.7747-2.84970.24391880.19863604X-RAY DIFFRACTION100
2.8497-2.93340.26871890.21063671X-RAY DIFFRACTION100
2.9334-3.0280.27052000.20733670X-RAY DIFFRACTION100
3.028-3.13620.22891660.20013657X-RAY DIFFRACTION100
3.1362-3.26160.22042160.19033627X-RAY DIFFRACTION100
3.2616-3.40980.2071750.18513666X-RAY DIFFRACTION100
3.4098-3.58930.21872060.17643663X-RAY DIFFRACTION100
3.5893-3.81380.182110.16353664X-RAY DIFFRACTION100
3.8138-4.10760.1731990.15793681X-RAY DIFFRACTION100
4.1076-4.51970.18312140.1613677X-RAY DIFFRACTION100
4.5197-5.17080.1971930.16423713X-RAY DIFFRACTION100
5.1708-6.50370.22082050.1883763X-RAY DIFFRACTION100
6.5037-30.0030.21181850.20113893X-RAY DIFFRACTION98
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.8060.8591.54560.97031.57083.35280.04140.0406-0.09650.03510.0752-0.1227-0.04520.262-0.08710.2454-0.04490.00510.3538-0.02950.281329.842224.402442.657
20.56020.48710.96431.34372.04093.3344-0.0602-0.14330.0421-0.0113-0.05750.0841-0.1005-0.23370.10190.28660.01220.02340.25970.01440.23699.653626.012949.4425
30.7380.86970.88031.82031.57291.729-0.05150.02120.0439-0.02270.0484-0.0034-0.22520.06520.02170.3378-0.02630.00840.20810.00530.224717.809740.284736.7141
4-0.65530.3895-0.00591.35711.56331.6250.01510.0373-0.1658-0.0660.3298-0.3831-0.08740.5363-0.32490.2884-0.066-0.00820.5186-0.09270.3734.98321.032631.2568
50.01760.16150.45670.27690.87431.30320.0967-0.1595-0.02850.1554-0.0703-0.01020.2339-0.3514-0.0280.415-0.06160.01250.37780.01910.23756.095813.259948.1574
60.19310.48690.68580.93211.08771.421-0.12180.01120.0544-0.2820.06930.1245-0.53210.00860.03020.52970.0135-0.0190.276-0.00530.36446.9641.243827.8756
7-0.36260.37750.3530.48520.30681.3179-0.03780.0442-0.0311-0.00390.0629-0.1987-0.10870.2882-0.03620.1948-0.00560.02040.3061-0.03450.283422.3204-8.6297-0.3255
81.49660.70811.21430.59130.47460.79270.0279-0.32740.15430.1047-0.1358-0.07970.1015-0.18510.10140.2093-0.05520.02270.29480.02180.2954-14.4507-7.533713.4746
90.99780.39641.15630.03230.75082.9039-0.1148-0.18540.1229-0.09360.00020.0628-0.5048-0.07740.07870.41140.0021-0.00650.27860.00960.2847-1.941221.3487-10.9166
100.78760.00320.08211.29690.09372.10520.02530.0916-0.093-0.02280.0024-0.04770.1040.0975-0.01010.1709-0.02010.03960.2161-0.01370.236812.0416-18.8624-13.1933
111.12930.31860.05751.0561-0.13111.5355-0.02510.121-0.054-0.0468-0.04470.28840.1655-0.33950.05880.1627-0.06350.02750.2479-0.00460.2884-19.9271-13.4389-4.3385
121.6517-0.169-0.37940.9866-0.16511.59530.08290.1468-0.0947-0.2245-0.0530.057-0.0718-0.0512-0.03230.29240.01680.0060.21990.02710.2232-3.7347.6007-24.4523
130.14160.14890.08550.43510.50560.75560.0477-0.0743-0.07540.01310.1312-0.1789-0.02620.1418-0.15030.2109-0.02260.00910.2823-0.04440.270523.70480.46712.3455
140.41410.41980.70420.62990.82371.55860.0973-0.12830.0270.1071-0.12660.06290.0934-0.34660.01750.2079-0.05170.00570.2863-0.00970.278-7.53982.499623.4239
150.1920.11680.40071.04331.22332.516-0.1044-0.03530.0125-0.2316-0.03020.0386-0.5054-0.00890.11380.312-0.0120.00270.23370.00920.21374.282826.41792.8209
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 330:492
2X-RAY DIFFRACTION2CHAIN B AND RESID 330:492
3X-RAY DIFFRACTION3CHAIN C AND RESID 330:492
4X-RAY DIFFRACTION4CHAIN A AND RESID 5:49
5X-RAY DIFFRACTION5CHAIN B AND RESID 5:49
6X-RAY DIFFRACTION6CHAIN C AND RESID 6:49
7X-RAY DIFFRACTION7CHAIN A AND RESID 50:113
8X-RAY DIFFRACTION8CHAIN B AND RESID 50:113
9X-RAY DIFFRACTION9CHAIN C AND RESID 50:113
10X-RAY DIFFRACTION10CHAIN A AND RESID 114-240
11X-RAY DIFFRACTION11CHAIN B AND RESID 114-240
12X-RAY DIFFRACTION12CHAIN C AND RESID 114-240
13X-RAY DIFFRACTION13CHAIN A AND RESID 241-323
14X-RAY DIFFRACTION14CHAIN B AND RESID 241-323
15X-RAY DIFFRACTION15CHAIN C AND RESID 241-323

+
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