[English] 日本語
Yorodumi
- PDB-2hvf: Crystal Structure of N-terminal Domain of Ribosomal Protein L9 (N... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2hvf
TitleCrystal Structure of N-terminal Domain of Ribosomal Protein L9 (NTL9), G34dA
Components50S ribosomal protein L9
KeywordsSTRUCTURAL PROTEIN / L9 / ribosomal protein / NTL9 / G34dA
Function / homology
Function and homology information


cytosolic large ribosomal subunit / rRNA binding / structural constituent of ribosome / translation
Similarity search - Function
Ribosomal protein L9, N-terminal domain / Ribosomal Protein L9; domain 1 / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal ...Ribosomal protein L9, N-terminal domain / Ribosomal Protein L9; domain 1 / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal / Ribosomal protein L9, N-terminal domain / Ribosomal protein L9/RNase H1, N-terminal / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETIC ACID / IMIDAZOLE / Large ribosomal subunit protein bL9
Similarity search - Component
MethodX-RAY DIFFRACTION / SYNCHROTRON / Phase from wild type NTL9 / Resolution: 1.57 Å
AuthorsAnil, B. / Kim, E.Y. / Cho, J.H. / Schindelin, H. / Raleigh, D.P.
CitationJournal: To be Published
Title: Detecting and quantifying strain in protein folding
Authors: Anil, B. / Kim, E.Y. / Cho, J.H. / Schindelin, H. / Raleigh, D.P.
History
DepositionJul 28, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr2_label_alt_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.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 / _struct_conn.ptnr2_symmetry / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 50S ribosomal protein L9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)6,23411
Polymers5,7021
Non-polymers53310
Water1,15364
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
A: 50S ribosomal protein L9
hetero molecules

A: 50S ribosomal protein L9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,46922
Polymers11,4032
Non-polymers1,06520
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z1
Buried area3640 Å2
ΔGint-348 kcal/mol
Surface area6220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.517, 53.517, 36.178
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-423-

HOH

-
Components

-
Protein , 1 types, 1 molecules A

#1: Protein 50S ribosomal protein L9 / BL17


Mass: 5701.719 Da / Num. of mol.: 1 / Fragment: N-terminal domain / Mutation: G34(DAL) / Source method: obtained synthetically
Details: This sequence naturally occurs in Bacillus stearothermophilus(Geobacillus stearothermophilus) with gene name rplI. It was chemically synthesized by FMOC solid-phase peptide synthesis method.
References: UniProt: P02417

-
Non-polymers , 5 types, 74 molecules

#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#5: Chemical ChemComp-ACY / ACETIC ACID


Mass: 60.052 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H4O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 64 / 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: 2.27 Å3/Da / Density % sol: 45.84 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 10 mM Imidazole (pH 8.0), 300 mM Zn Acetate, 3 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 291K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1.1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 7, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 1.57→50 Å / Num. all: 7705 / Num. obs: 7705 / % possible obs: 99.2 % / Redundancy: 9.9 % / Rmerge(I) obs: 0.062 / Χ2: 1.23 / Net I/σ(I): 15.5
Reflection shellResolution: 1.57→1.63 Å / Redundancy: 9.3 % / Rmerge(I) obs: 0.286 / Num. unique all: 684 / Χ2: 0.787 / % possible all: 92.8

-
Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACT2data extraction
HKL-2000data reduction
REFMACphasing
RefinementMethod to determine structure: Phase from wild type NTL9 / Resolution: 1.57→20 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.94 / SU B: 2.776 / SU ML: 0.046 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.106 / ESU R Free: 0.086 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.208 355 4.6 %RANDOM
Rwork0.159 ---
all0.162 7670 --
obs0.162 7670 99.93 %-
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: 14.741 Å2
Baniso -1Baniso -2Baniso -3
1-0.02 Å20 Å20 Å2
2--0.02 Å20 Å2
3----0.04 Å2
Refinement stepCycle: LAST / Resolution: 1.57→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms400 0 17 64 481
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.022422
X-RAY DIFFRACTIONr_bond_other_d0.0010.02402
X-RAY DIFFRACTIONr_angle_refined_deg1.6222561
X-RAY DIFFRACTIONr_angle_other_deg2.8713950
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.449552
X-RAY DIFFRACTIONr_dihedral_angle_2_deg43.88727.64717
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.8281589
X-RAY DIFFRACTIONr_chiral_restr0.0920.263
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02455
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0275
X-RAY DIFFRACTIONr_nbd_refined0.2690.286
X-RAY DIFFRACTIONr_nbd_other0.1730.2367
X-RAY DIFFRACTIONr_nbtor_refined0.1850.2200
X-RAY DIFFRACTIONr_nbtor_other0.1020.2256
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.3870.237
X-RAY DIFFRACTIONr_metal_ion_refined0.1910.28
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1080.25
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1420.225
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3920.218
X-RAY DIFFRACTIONr_mcbond_it1.9741.5335
X-RAY DIFFRACTIONr_mcbond_other0.5681.5110
X-RAY DIFFRACTIONr_mcangle_it2.2262415
X-RAY DIFFRACTIONr_scbond_it3.6393185
X-RAY DIFFRACTIONr_scangle_it4.4614.5146
X-RAY DIFFRACTIONr_rigid_bond_restr1.7323962
X-RAY DIFFRACTIONr_sphericity_free8.58376
X-RAY DIFFRACTIONr_sphericity_bonded2.4543820
LS refinement shellResolution: 1.57→1.615 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.303 27 -
Rwork0.124 514 -
obs-541 100 %

+
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