[English] 日本語
Yorodumi
- PDB-6jl9: Crystal structure of a frog ependymin related protein -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6jl9
TitleCrystal structure of a frog ependymin related protein
ComponentsEpendymin-related 1
KeywordsUNKNOWN FUNCTION / Ependymin
Function / homologyEpendymin / Ependymin / Ependymins / cell-matrix adhesion / lysosome / calcium ion binding / extracellular region / Mammalian ependymin-related protein 1
Function and homology information
Biological speciesXenopus tropicalis (tropical clawed frog)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2 Å
AuthorsPark, S.Y.
Funding support Korea, Republic Of, 1items
OrganizationGrant numberCountry
National Research Foundation (Korea)2016R1D1A1A09918187 Korea, Republic Of
CitationJournal: Iucrj / Year: 2019
Title: Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder.
Authors: Park, J.K. / Kim, K.Y. / Sim, Y.W. / Kim, Y.I. / Kim, J.K. / Lee, C. / Han, J. / Kim, C.U. / Lee, J.E. / Park, S.
History
DepositionMar 4, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 10, 2019Provider: repository / Type: Initial release
Revision 1.1Jul 31, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ependymin-related 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,8772
Polymers22,8371
Non-polymers401
Water99155
1
A: Ependymin-related 1
hetero molecules

A: Ependymin-related 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,7534
Polymers45,6732
Non-polymers802
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_775-y+2,-x+2,-z+1/61
Buried area4600 Å2
ΔGint-27 kcal/mol
Surface area19940 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.208, 61.208, 236.196
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522

-
Components

#1: Protein Ependymin-related 1


Mass: 22836.588 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Xenopus tropicalis (tropical clawed frog)
Gene: epdr1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: F6VRB7
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 55 / 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: 56.02 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: 0.2M Calcium acetate hydrate, 0.1M Sodium cacodylate trihydrate pH 6.5, 18%(w/v) Polyethylene glycol 8,000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 7A (6B, 6C1) / Wavelength: 1.54 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Jul 25, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2→53.01 Å / Num. obs: 18642 / % possible obs: 99.7 % / Redundancy: 19.8 % / Net I/σ(I): 70.5
Reflection shellResolution: 2→2.03 Å

-
Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
HKL-2000data reduction
HKL-2000data scaling
ARP/wARP8model building
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2→53.01 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.903 / SU B: 9.651 / SU ML: 0.122 / Cross valid method: THROUGHOUT / ESU R: 0.287 / ESU R Free: 0.171 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27753 952 5.1 %RANDOM
Rwork0.1942 ---
obs0.19819 17685 99.67 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 55.467 Å2
Baniso -1Baniso -2Baniso -3
1-0.95 Å20.48 Å20 Å2
2--0.95 Å20 Å2
3----3.08 Å2
Refinement stepCycle: 1 / Resolution: 2→53.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1554 0 1 55 1610
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0191623
X-RAY DIFFRACTIONr_bond_other_d0.0010.021465
X-RAY DIFFRACTIONr_angle_refined_deg1.741.9342217
X-RAY DIFFRACTIONr_angle_other_deg1.47333395
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.5675191
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.91824.02482
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.54115261
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.925158
X-RAY DIFFRACTIONr_chiral_restr0.1030.2233
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0211826
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02388
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_it10.0025.114759
X-RAY DIFFRACTIONr_mcbond_other9.995.118758
X-RAY DIFFRACTIONr_mcangle_it11.3447.694947
X-RAY DIFFRACTIONr_mcangle_other11.3387.696948
X-RAY DIFFRACTIONr_scbond_it11.3615.78863
X-RAY DIFFRACTIONr_scbond_other11.3555.779864
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other12.9528.3891269
X-RAY DIFFRACTIONr_long_range_B_refined13.96742.7161808
X-RAY DIFFRACTIONr_long_range_B_other13.94142.6951800
X-RAY DIFFRACTIONr_rigid_bond_restr5.13233084
X-RAY DIFFRACTIONr_sphericity_free37.313516
X-RAY DIFFRACTIONr_sphericity_bonded28.53753072
LS refinement shellResolution: 2.001→2.053 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.345 77 -
Rwork0.237 1259 -
obs--99.26 %

+
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