[English] 日本語
Yorodumi
- PDB-5apz: Thermosinus carboxydivorans Nor1 Tcar0761 residues 68-101 and 191... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5apz
TitleThermosinus carboxydivorans Nor1 Tcar0761 residues 68-101 and 191-211 fused to GCN4 adaptors
ComponentsGENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4
KeywordsDNA BINDING PROTEIN / ALPHA/BETA COILED COIL / BETA LAYER / TRIMER
Function / homology
Function and homology information


protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding ...protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / amino acid biosynthetic process / cellular response to amino acid starvation / RNA polymerase II transcription regulator complex / : / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / regulation of cell cycle / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus
Similarity search - Function
Basic region leucine zipper / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. / basic region leucin zipper / Basic-leucine zipper domain superfamily / Basic-leucine zipper domain
Similarity search - Domain/homology
Uncharacterized protein / General control transcription factor GCN4
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
THERMOSINUS CARBOXYDIVORANS NOR1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsHartmann, M.D. / Deiss, S. / Lupas, A.N. / Hernandez Alvarez, B.
CitationJournal: Elife / Year: 2016
Title: alpha / beta coiled coils.
Authors: Hartmann, M.D. / Mendler, C.T. / Bassler, J. / Karamichali, I. / Ridderbusch, O. / Lupas, A.N. / Hernandez Alvarez, B.
History
DepositionSep 17, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 27, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 15, 2017Group: Database references / Source and taxonomy
Revision 1.2Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: GENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4


Theoretical massNumber of molelcules
Total (without water)13,9251
Polymers13,9251
Non-polymers00
Water1,874104
1
A: GENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4

A: GENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4

A: GENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4


Theoretical massNumber of molelcules
Total (without water)41,7763
Polymers41,7763
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_565-x+y,-x+1,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
Buried area15510 Å2
ΔGint-146.7 kcal/mol
Surface area18890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)37.920, 37.920, 179.150
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number173
Space group name H-MP63

-
Components

#1: Protein GENERAL CONTROL PROTEIN GCN4, NOR1 TCAR0761, GENERAL CONTROL PROTEIN GCN4


Mass: 13925.276 Da / Num. of mol.: 1 / Fragment: RESIDUES 250-279,68-101,191-211,250-279
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast), (gene. exp.) THERMOSINUS CARBOXYDIVORANS NOR1 (bacteria)
Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P03069, UniProt: A1HT30
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 104 / 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: 2.8 Å3/Da / Density % sol: 55 % / Description: NONE
Crystal growDetails: 0.1 M TRI-SODIUM CITRATE PH 4.0, 30 %(V/V) MPD

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1
DetectorType: DECTRIS PILATUS / Detector: PIXEL / Date: Aug 22, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.6→32.3 Å / Num. obs: 19111 / % possible obs: 99.2 % / Observed criterion σ(I): -3 / Redundancy: 3.69 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 20.3
Reflection shellResolution: 1.6→1.69 Å / Redundancy: 3.65 % / Rmerge(I) obs: 0.6 / Mean I/σ(I) obs: 2.23 / % possible all: 96.9

-
Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2WPQ
Resolution: 1.6→30.83 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.965 / SU B: 4.204 / SU ML: 0.068 / Cross valid method: THROUGHOUT / ESU R: 0.077 / ESU R Free: 0.082 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.21312 993 5.2 %RANDOM
Rwork0.17694 ---
obs0.17872 18113 99.23 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 38.659 Å2
Baniso -1Baniso -2Baniso -3
1-1.05 Å20.53 Å20 Å2
2--1.05 Å20 Å2
3----3.42 Å2
Refinement stepCycle: LAST / Resolution: 1.6→30.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms888 0 0 104 992
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.019916
X-RAY DIFFRACTIONr_bond_other_d0.0010.02950
X-RAY DIFFRACTIONr_angle_refined_deg1.9181.9961232
X-RAY DIFFRACTIONr_angle_other_deg0.87932202
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.7375118
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.3927.17939
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.98715207
X-RAY DIFFRACTIONr_dihedral_angle_4_deg7.829153
X-RAY DIFFRACTIONr_chiral_restr0.1070.2149
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.021002
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02169
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.2742.674455
X-RAY DIFFRACTIONr_mcbond_other2.2652.671454
X-RAY DIFFRACTIONr_mcangle_it2.884.002569
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.6693.375461
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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: 1.598→1.64 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.285 68 -
Rwork0.317 1293 -
obs--94.51 %
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)
16.6090.0026-1.35844.5232-1.3131.22460.1131-0.18540.13570.2739-0.06170.0431-0.16760.0152-0.05140.1325-0.01530.01310.1259-0.02060.0922-6.327624.1842127.7372
20.37580.5154-0.1821.9441-0.717212.1282-0.019-0.0110.12140.1562-0.02080.2037-0.1316-0.03040.03980.0672-0.0132-0.00830.0942-0.00850.063-5.739620.5594119.41
30.464-0.4041-1.32460.8085-0.193810.02870.0114-0.03090.0333-0.0101-0.0102-0.0270.06250.0442-0.00120.0193-0.0155-0.00520.03540.00770.0388-3.333616.4057101.2718
40.7041-0.1425-0.22570.59151.0797.2909-0.0302-0.11-0.0780.0845-0.0809-0.06490.3036-0.28360.1110.0326-0.01820.00060.04070.02070.03080.593121.41359.1197
50.18390.2892-1.43890.6665-2.080411.74910.00180.00360.0150.0184-0.00550.04-0.0259-0.08120.00370.01770.00950.00070.0248-0.00570.04383.707317.79795.9464
62.71520.3919-1.27834.56361.840610.0161-0.01350.09380.0143-0.06580.0299-0.1442-0.0280.1415-0.01640.0013-0.00320.00020.02510.01480.01565.253424.4924-22.7728
78.7923-4.744810.397.2477-5.738612.63470.13560.57410.3649-0.8-0.49240.13390.22210.48640.35670.15420.0373-0.03090.16820.05950.06262.478826.8956-31.8061
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-10 - 7
2X-RAY DIFFRACTION2A8 - 14
3X-RAY DIFFRACTION3A15 - 32
4X-RAY DIFFRACTION4A33 - 69
5X-RAY DIFFRACTION5A70 - 100
6X-RAY DIFFRACTION6A101 - 108
7X-RAY DIFFRACTION7A109 - 999

+
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