[English] 日本語
Yorodumi
- PDB-7y6e: Crystal structure of sDscam FNIII23 domains, isoform Beta2v6 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7y6e
TitleCrystal structure of sDscam FNIII23 domains, isoform Beta2v6
ComponentsDscam
KeywordsCELL ADHESION / cell surface receptor
Function / homology
Function and homology information


anatomical structure morphogenesis / cell differentiation / membrane
Similarity search - Function
Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype ...Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesChelicerata (chelicerates)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.034 Å
AuthorsChen, Q. / Yu, Y. / Cheng, J.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Nat Commun / Year: 2023
Title: Structural basis for the self-recognition of sDSCAM in Chelicerata.
Authors: Cheng, J. / Yu, Y. / Wang, X. / Zheng, X. / Liu, T. / Hu, D. / Jin, Y. / Lai, Y. / Fu, T.M. / Chen, Q.
History
DepositionJun 20, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 24, 2023Provider: repository / Type: Initial release
Revision 1.1May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Dscam
B: Dscam
C: Dscam
D: Dscam
E: Dscam
F: Dscam
G: Dscam


Theoretical massNumber of molelcules
Total (without water)156,5507
Polymers156,5507
Non-polymers00
Water1629
1
A: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Dscam


Theoretical massNumber of molelcules
Total (without water)22,3641
Polymers22,3641
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)307.021, 56.219, 94.837
Angle α, β, γ (deg.)90.00, 105.38, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein
Dscam


Mass: 22364.230 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chelicerata (chelicerates) / Gene: Dscam / Production host: Escherichia coli (E. coli) / References: UniProt: A0A161FW14
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 9 / 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: 2.52 Å3/Da / Density % sol: 51.2 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop
Details: 0.2 M NaCl, 14% (w/v) PEG 8,000, 100 mM HEPES buffer pH 7.0

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97852 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 27, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97852 Å / Relative weight: 1
ReflectionResolution: 3.034→50 Å / Num. obs: 30260 / % possible obs: 98.7 % / Redundancy: 4.7 % / CC1/2: 0.989 / CC star: 0.997 / Rmerge(I) obs: 0.143 / Rpim(I) all: 0.072 / Rrim(I) all: 0.161 / Χ2: 0.926 / Net I/σ(I): 5.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2CC starRpim(I) allRrim(I) allΧ2% possible all
3.05-3.13.80.76213760.7210.9150.4330.8810.90890.9
3.1-3.1640.76714630.7860.9380.4260.8810.87794.5
3.16-3.224.10.77414480.8040.9440.4220.8860.94497.6
3.22-3.294.30.61515140.8730.9650.3310.7010.98398.8
3.29-3.364.50.56915140.9170.9780.2950.6440.93899.4
3.36-3.434.40.5314850.8990.9730.2740.5990.97199.4
3.43-3.524.60.4415410.9380.9840.2230.4951.00299.3
3.52-3.625.10.37414660.9630.990.1780.4160.95899.7
3.62-3.725.10.32115490.9710.9930.1540.3570.94499.7
3.72-3.8450.25714980.9760.9940.1240.2870.90399.7
3.84-3.9850.2515380.9770.9940.120.2790.98499.7
3.98-4.1450.1815210.9830.9960.0880.2020.95999.9
4.14-4.3350.15515350.9860.9960.0770.1730.95599.7
4.33-4.564.50.12814960.9880.9970.0670.1460.9299.4
4.56-4.8450.11715270.9870.9970.0580.1310.92699.7
4.84-5.215.10.10115560.990.9970.050.1130.90499.9
5.21-5.745.10.09515280.990.9980.0470.1070.81999.7
5.74-6.574.70.09215330.9880.9970.0470.1040.76999.5
6.57-8.274.90.08415650.9860.9960.0420.0940.79799.4
8.27-504.70.09616070.9850.9960.0490.1091.06298.1

-
Processing

Software
NameVersionClassification
PHENIX(1.15.2_3472: ???)refinement
HKL-2000data scaling
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.034→48.847 Å / SU ML: 0.43 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 30.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2724 1373 5.29 %
Rwork0.2345 --
obs0.2365 25974 84.31 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.034→48.847 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10697 0 0 9 10706
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00211006
X-RAY DIFFRACTIONf_angle_d0.64415010
X-RAY DIFFRACTIONf_dihedral_angle_d3.046475
X-RAY DIFFRACTIONf_chiral_restr0.0441652
X-RAY DIFFRACTIONf_plane_restr0.0041875
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0345-3.14290.3806650.31581298X-RAY DIFFRACTION44
3.1429-3.26870.36151020.28761699X-RAY DIFFRACTION59
3.2687-3.41750.3502980.2831995X-RAY DIFFRACTION69
3.4175-3.59760.3091390.2622310X-RAY DIFFRACTION80
3.5976-3.82290.27731630.26122723X-RAY DIFFRACTION94
3.8229-4.11790.29031560.24862901X-RAY DIFFRACTION100
4.1179-4.53210.28051620.2162877X-RAY DIFFRACTION99
4.5321-5.18730.23211630.19562919X-RAY DIFFRACTION99
5.1873-6.53290.25541630.2252900X-RAY DIFFRACTION99
6.5329-48.8470.24351620.22162979X-RAY DIFFRACTION97

+
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