[English] 日本語
Yorodumi
- PDB-2vut: Crystal structure of NAD-bound NmrA-AreA zinc finger complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2vut
TitleCrystal structure of NAD-bound NmrA-AreA zinc finger complex
Components
  • NITROGEN METABOLITE REPRESSION REGULATOR NMRA
  • NITROGEN REGULATORY PROTEIN AREA
KeywordsTRANSCRIPTION / TRANSCRIPTION REGULATION / PROTEIN-PROTEIN INTERACTIONS / METAL-BINDING / NITRATE ASSIMILATION / ZINC-FINGER / DNA-BINDING / ZINC FINGERS / ZINC / AREA / NMRA / NUCLEUS / ACTIVATOR / GATA-TYPE
Function / homology
Function and homology information


nitrogen catabolite repression of transcription from RNA polymerase II promoter / regulation of amide catabolic process / nitrogen catabolite repression of transcription / regulation of arginine metabolic process / regulation of nitrogen utilization / NADP+ binding / NAD+ binding / nitrate assimilation / NAD binding / regulation of gene expression ...nitrogen catabolite repression of transcription from RNA polymerase II promoter / regulation of amide catabolic process / nitrogen catabolite repression of transcription / regulation of arginine metabolic process / regulation of nitrogen utilization / NADP+ binding / NAD+ binding / nitrate assimilation / NAD binding / regulation of gene expression / sequence-specific DNA binding / oxidoreductase activity / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Nitrogen regulatory AreA, N-terminal / Nitrogen regulatory protein AreA N terminus / Nitrogen regulatory protein areA, GATA-like domain / Fungal protein of unknown function (DUF1752) / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type ...Nitrogen regulatory AreA, N-terminal / Nitrogen regulatory protein AreA N terminus / Nitrogen regulatory protein areA, GATA-like domain / Fungal protein of unknown function (DUF1752) / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type / NmrA-like domain / NmrA-like family / Erythroid Transcription Factor GATA-1, subunit A / Erythroid Transcription Factor GATA-1; Chain A / UDP-galactose 4-epimerase, domain 1 / UDP-galactose 4-epimerase; domain 1 / Zinc finger, NHR/GATA-type / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Alpha-Beta Complex / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Nitrogen metabolite repression protein nmrA / Nitrogen regulatory protein areA / Nitrogen metabolite repression protein nmrA
Similarity search - Component
Biological speciesEmericella nidulans (mold)
EMERICELLA NIDULANS (mold)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsKotaka, M. / Johnson, C. / Lamb, H.K. / Hawkins, A.R. / Ren, J. / Stammers, D.K.
CitationJournal: J.Mol.Biol. / Year: 2008
Title: Structural Analysis of the Recognition of the Negative Regulator Nmra and DNA by the Zinc Finger from the Gata-Type Transcription Factor Area.
Authors: Kotaka, M. / Johnson, C. / Lamb, H.K. / Hawkins, A.R. / Ren, J. / Stammers, D.K.
History
DepositionMay 30, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 29, 2008Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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.ptnr1_label_seq_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 / _struct_conn.ptnr2_label_seq_id
Revision 1.4May 8, 2024Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.gene_src_common_name / _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id / _entity_src_gen.pdbx_gene_src_scientific_name

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
B: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
C: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
D: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
E: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
F: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
G: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
H: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
I: NITROGEN REGULATORY PROTEIN AREA
J: NITROGEN REGULATORY PROTEIN AREA
K: NITROGEN REGULATORY PROTEIN AREA
L: NITROGEN REGULATORY PROTEIN AREA
M: NITROGEN REGULATORY PROTEIN AREA
N: NITROGEN REGULATORY PROTEIN AREA
O: NITROGEN REGULATORY PROTEIN AREA
P: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)355,35442
Polymers348,99916
Non-polymers6,35526
Water35,2551957
1
A: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
I: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3895
Polymers43,6252
Non-polymers7643
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1770 Å2
ΔGint-10.2 kcal/mol
Surface area18300 Å2
MethodPQS
2
B: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
J: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3544
Polymers43,6252
Non-polymers7292
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1810 Å2
ΔGint-8.5 kcal/mol
Surface area18550 Å2
MethodPQS
3
C: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
K: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,4816
Polymers43,6252
Non-polymers8564
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1740 Å2
ΔGint-8.7 kcal/mol
Surface area18040 Å2
MethodPQS
4
D: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
L: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3895
Polymers43,6252
Non-polymers7643
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1800 Å2
ΔGint-9.8 kcal/mol
Surface area18300 Å2
MethodPQS
5
E: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
M: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,4816
Polymers43,6252
Non-polymers8564
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1850 Å2
ΔGint-8.9 kcal/mol
Surface area18050 Å2
MethodPQS
6
F: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
N: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3895
Polymers43,6252
Non-polymers7643
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1760 Å2
ΔGint-6.9 kcal/mol
Surface area17980 Å2
MethodPQS
7
G: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
O: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,4816
Polymers43,6252
Non-polymers8564
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1800 Å2
ΔGint-7.3 kcal/mol
Surface area18290 Å2
MethodPQS
8
H: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
P: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,3895
Polymers43,6252
Non-polymers7643
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1760 Å2
ΔGint-8.9 kcal/mol
Surface area18230 Å2
MethodPQS
9
A: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5343
Polymers38,8351
Non-polymers6992
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
10
B: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,4992
Polymers38,8351
Non-polymers6631
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
11
C: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,6264
Polymers38,8351
Non-polymers7913
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
12
D: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5343
Polymers38,8351
Non-polymers6992
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
13
E: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5343
Polymers38,8351
Non-polymers6992
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
14
F: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5343
Polymers38,8351
Non-polymers6992
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
15
G: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,6264
Polymers38,8351
Non-polymers7913
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
16
H: NITROGEN METABOLITE REPRESSION REGULATOR NMRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5343
Polymers38,8351
Non-polymers6992
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
17
I: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
18
J: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
19
K: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
20
L: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
21
M: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,9473
Polymers4,7901
Non-polymers1582
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
22
N: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
23
O: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
24
P: NITROGEN REGULATORY PROTEIN AREA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,8552
Polymers4,7901
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)227.520, 227.520, 222.570
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3
Components on special symmetry positions
IDModelComponents
11B-2023-

HOH

-
Components

-
Protein / Protein/peptide , 2 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein
NITROGEN METABOLITE REPRESSION REGULATOR NMRA / NMRA


Mass: 38835.238 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (mold)
Plasmid: PET / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O59919, UniProt: Q5AU62*PLUS
#2: Protein/peptide
NITROGEN REGULATORY PROTEIN AREA / AREA


Mass: 4789.604 Da / Num. of mol.: 8 / Fragment: ZINC FINGER DOMAIN, RESIDUES 670-712
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) EMERICELLA NIDULANS (mold) / Plasmid: PET3A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P17429

-
Non-polymers , 5 types, 1983 molecules

#3: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE


Mass: 663.425 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Comment: NAD*YM
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1957 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.1 Å3/Da / Density % sol: 60 % / Description: NONE
Crystal growpH: 6.4
Details: 0.2M LI2SO4, 0.1M BIS-TRIS PH 6.4, 15% - 17% PEG3350

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 2.3→30 Å / Num. obs: 180785 / % possible obs: 94.8 % / Observed criterion σ(I): -1 / Redundancy: 6 % / Biso Wilson estimate: 22.6 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.7
Reflection shellResolution: 2.3→2.38 Å / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 1.6 / % possible all: 71.3

-
Processing

Software
NameVersionClassification
CNS1.1refinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 1K6J AND 4GAT
Resolution: 2.3→29.86 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 2465599.64 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
Details: A SELF PATTERSON FUNCTION SHOWED A SIGNIFICANT PEAK INDICATIVE OF PSEUDO-TRANSLATION.
RfactorNum. reflection% reflectionSelection details
Rfree0.274 17971 9.9 %RANDOM
Rwork0.215 ---
obs0.215 180780 94.6 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 56.8585 Å2 / ksol: 0.35 e/Å3
Displacement parametersBiso mean: 35.5 Å2
Baniso -1Baniso -2Baniso -3
1-3.2 Å20 Å20 Å2
2--3.2 Å20 Å2
3----6.39 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.38 Å0.29 Å
Luzzati d res low-5 Å
Luzzati sigma a0.41 Å0.33 Å
Refinement stepCycle: LAST / Resolution: 2.3→29.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22892 0 385 1957 25234
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d22.5
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.87
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it5.44
X-RAY DIFFRACTIONc_mcangle_it7.418
X-RAY DIFFRACTIONc_scbond_it9.678
X-RAY DIFFRACTIONc_scangle_it10.9810
LS refinement shellResolution: 2.3→2.44 Å / Rfactor Rfree error: 0.007 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.35 2467 10 %
Rwork0.293 22290 -
obs--77.9 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2NAD.PARNAD.TOP
X-RAY DIFFRACTION3WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION4GOL.PARGOL.TOP
X-RAY DIFFRACTION5ION.PARAM

+
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://pdbjlvh1.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