[English] 日本語
Yorodumi
- PDB-2yw7: Crystal structure of C-terminal deletion mutant of Mycobacterium ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2yw7
TitleCrystal structure of C-terminal deletion mutant of Mycobacterium smegmatis Dps
ComponentsStarvation-induced DNA protecting protein
KeywordsDNA BINDING PROTEIN / DNA-BINDING PROTEIN / Quarternary assebmly
Function / homology
Function and homology information


Oxidoreductases; Oxidizing metal ions / oxidoreductase activity, acting on metal ions / nucleoid / ferric iron binding / intracellular iron ion homeostasis / DNA binding / cytoplasm
Similarity search - Function
Dps protein family signature 1. / DNA-binding protein Dps, conserved site / DNA-binding protein Dps / Ferritin, core subunit, four-helix bundle / Ferritin / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA protection during starvation protein / DNA protection during starvation protein
Similarity search - Component
Biological speciesMycobacterium smegmatis (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsRoy, S. / Saraswathi, R. / Gupta, S. / Sekar, K. / Chatterji, D. / Vijayan, M.
CitationJournal: J.Mol.Biol. / Year: 2007
Title: Role of N and C-terminal Tails in DNA Binding and Assembly in Dps: Structural Studies of Mycobacterium smegmatis Dps Deletion Mutants
Authors: Roy, S. / Saraswathi, R. / Gupta, S. / Sekar, K. / Chatterji, D. / Vijayan, M.
History
DepositionApr 19, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 17, 2007Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 25, 2023Group: 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: Starvation-induced DNA protecting protein
B: Starvation-induced DNA protecting protein
C: Starvation-induced DNA protecting protein
D: Starvation-induced DNA protecting protein
E: Starvation-induced DNA protecting protein
F: Starvation-induced DNA protecting protein
G: Starvation-induced DNA protecting protein
H: Starvation-induced DNA protecting protein
I: Starvation-induced DNA protecting protein
J: Starvation-induced DNA protecting protein


Theoretical massNumber of molelcules
Total (without water)202,98810
Polymers202,98810
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21210 Å2
ΔGint-85 kcal/mol
Surface area60890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.516, 83.940, 111.911
Angle α, β, γ (deg.)90.00, 105.89, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Starvation-induced DNA protecting protein


Mass: 20298.809 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium smegmatis (bacteria) / Plasmid: pRSET-msdpsdeltaC26 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21DE3 / References: UniProt: A0R692, UniProt: P0C558*PLUS

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.15 Å3/Da / Density % sol: 42.72 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 30% PEG1140, 100mM CaCl2, 0.1M Tris-HCl pH8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Jan 20, 2006
RadiationMonochromator: OSMIC MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 3.3→30 Å / Num. obs: 24653 / % possible obs: 100 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.0108 / Net I/σ(I): 11.7
Reflection shellResolution: 3.3→3.382 Å / Rmerge(I) obs: 0.0331 / Mean I/σ(I) obs: 3.3 / Num. unique all: 2467 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
HKL-2000data collection
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1VEI
Resolution: 3.3→28.54 Å / Cor.coef. Fo:Fc: 0.903 / Cor.coef. Fo:Fc free: 0.874 / SU B: 23.764 / SU ML: 0.399 / Cross valid method: THROUGHOUT / ESU R Free: 0.598 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25878 1320 5.1 %RANDOM
Rwork0.22179 ---
obs0.22367 24653 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 43.228 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å2-0.02 Å2
2--0 Å20 Å2
3----0.01 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.42 Å0.36 Å
Luzzati d res low-5 Å
Luzzati sigma a0.34 Å0.4 Å
Refinement stepCycle: LAST / Resolution: 3.3→28.54 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11597 0 0 0 11597
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.02111837
X-RAY DIFFRACTIONr_angle_refined_deg1.0681.95216082
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.36351445
X-RAY DIFFRACTIONr_dihedral_angle_2_deg42.35324.983578
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.755152069
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.2391560
X-RAY DIFFRACTIONr_chiral_restr0.0720.21842
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.028922
X-RAY DIFFRACTIONr_nbd_refined0.260.26864
X-RAY DIFFRACTIONr_nbtor_refined0.3120.28041
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1610.2575
X-RAY DIFFRACTIONr_metal_ion_refined0.210.25
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2950.266
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.030.23
X-RAY DIFFRACTIONr_mcbond_it4.721.57409
X-RAY DIFFRACTIONr_mcangle_it6.052211678
X-RAY DIFFRACTIONr_scbond_it1.3634966
X-RAY DIFFRACTIONr_scangle_it2.344.54404
LS refinement shellResolution: 3.297→3.382 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.328 97 -
Rwork0.291 1690 -
obs--100 %

+
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