[English] 日本語
Yorodumi
- PDB-5nyj: Anbu from Hyphomicrobium sp. strain MC1 - SG: C2 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5nyj
TitleAnbu from Hyphomicrobium sp. strain MC1 - SG: C2
ComponentsAnbu
KeywordsHYDROLASE / Ntn-hydrolase-fold / proteasome / evolution
Function / homologyUncharacterised conserved protein UCP009120, proteasome-type protease, Sll0069 / proteasome core complex / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / proteolysis involved in protein catabolic process / Peptidase
Function and homology information
Biological speciesHyphomicrobium sp.
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsVielberg, M.-T. / Groll, M.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationSFB1035 Germany
CitationJournal: J. Mol. Biol. / Year: 2018
Title: On the Trails of the Proteasome Fold: Structural and Functional Analysis of the Ancestral beta-Subunit Protein Anbu.
Authors: Vielberg, M.T. / Bauer, V.C. / Groll, M.
History
DepositionMay 11, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 24, 2017Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2018Group: Author supporting evidence / Database references / Category: citation / citation_author / pdbx_audit_support
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name / _pdbx_audit_support.funding_organization
Revision 1.2Mar 7, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Anbu
B: Anbu
C: Anbu
D: Anbu
E: Anbu
F: Anbu
G: Anbu
H: Anbu
I: Anbu
J: Anbu
K: Anbu
L: Anbu
M: Anbu
N: Anbu
O: Anbu
P: Anbu


Theoretical massNumber of molelcules
Total (without water)439,66316
Polymers439,66316
Non-polymers00
Water0
1
J: Anbu

B: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
2
H: Anbu

G: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_556x,y,z+11
3
A: Anbu
I: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3690 Å2
ΔGint-21 kcal/mol
Surface area21630 Å2
MethodPISA
4


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area48570 Å2
ΔGint-150 kcal/mol
Surface area154530 Å2
MethodPISA
5
B: Anbu

J: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_556x,y,z+11
Buried area4050 Å2
ΔGint-20 kcal/mol
Surface area21170 Å2
MethodPISA
6
C: Anbu
N: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4180 Å2
ΔGint-26 kcal/mol
Surface area21160 Å2
MethodPISA
7
D: Anbu
O: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4180 Å2
ΔGint-27 kcal/mol
Surface area21250 Å2
MethodPISA
8
E: Anbu
P: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3980 Å2
ΔGint-24 kcal/mol
Surface area21330 Å2
MethodPISA
9
F: Anbu
L: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3880 Å2
ΔGint-26 kcal/mol
Surface area21560 Å2
MethodPISA
10
G: Anbu

H: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area4260 Å2
ΔGint-23 kcal/mol
Surface area21380 Å2
MethodPISA
11
K: Anbu
M: Anbu


Theoretical massNumber of molelcules
Total (without water)54,9582
Polymers54,9582
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4280 Å2
ΔGint-27 kcal/mol
Surface area21120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)240.220, 242.150, 107.320
Angle α, β, γ (deg.)90.00, 90.77, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein
Anbu


Mass: 27478.965 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hyphomicrobium sp. (strain MC1) (bacteria)
Gene: HYPMC_4374 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: F8JB59

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.55 Å3/Da / Density % sol: 65.35 %
Crystal growTemperature: 298.15 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.01 M cobalt(II) chloride, 0.1 M Tris, 20 % PVP K15. The protein crystallized in presence of the proteasome inhibitor bortezomib.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 19, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→40 Å / Num. obs: 99540 / % possible obs: 98.8 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 9.7
Reflection shellResolution: 3.2→3.3 Å / Rmerge(I) obs: 0.562 / Mean I/σ(I) obs: 2 / % possible all: 98.6

-
Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5NYF

5nyf


Resolution: 3.2→20 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.906 / SU B: 28.845 / SU ML: 0.464 / Cross valid method: THROUGHOUT / ESU R Free: 0.514 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2787 4957 5 %RANDOM
Rwork0.23502 ---
obs0.23715 94184 98.4 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 112.126 Å2
Baniso -1Baniso -2Baniso -3
1--2.78 Å2-0 Å20.48 Å2
2---5.34 Å20 Å2
3---8.1 Å2
Refinement stepCycle: 1 / Resolution: 3.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29869 0 0 0 29869
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01930412
X-RAY DIFFRACTIONr_bond_other_d0.0010.0228120
X-RAY DIFFRACTIONr_angle_refined_deg0.921.94841099
X-RAY DIFFRACTIONr_angle_other_deg0.797364724
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.71853703
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.43223.3641614
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.726155133
X-RAY DIFFRACTIONr_dihedral_angle_4_deg10.12915320
X-RAY DIFFRACTIONr_chiral_restr0.0520.24540
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0234274
X-RAY DIFFRACTIONr_gen_planes_other0.0010.026850
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_it1.60711.42314908
X-RAY DIFFRACTIONr_mcbond_other1.60711.42314907
X-RAY DIFFRACTIONr_mcangle_it2.94817.12718579
X-RAY DIFFRACTIONr_mcangle_other2.94717.12718580
X-RAY DIFFRACTIONr_scbond_it1.02811.5215504
X-RAY DIFFRACTIONr_scbond_other1.02811.5215504
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.97117.2522520
X-RAY DIFFRACTIONr_long_range_B_refined4.49532519
X-RAY DIFFRACTIONr_long_range_B_other4.49532520
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3.2→3.281 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.376 358 -
Rwork0.357 6809 -
obs--98.83 %

+
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