[English] 日本語
Yorodumi
- PDB-9udu: Single-chain Fv antibody of E11 complex with NNP-Cap -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9udu
TitleSingle-chain Fv antibody of E11 complex with NNP-Cap
ComponentsSingle-chain Fv antibody of E11
KeywordsIMMUNE SYSTEM / ANTIGEN BINDING / AFFINITY MATURATION / SOMATIC HYPERMUTATION
Function / homology: / DI(HYDROXYETHYL)ETHER
Function and homology information
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.06 Å
AuthorsYoshida, M. / Hanazono, Y. / Numoto, N. / Ito, N. / Oda, M.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Structural basis of anti-(4-hydroxy-3-nitrophenyl)acetyl antibodies during affinity maturation
Authors: Yoshida, M. / Hanazono, Y. / Numoto, N. / Yabuno, S. / Ito, N. / Azuma, T. / Oda, M.
History
DepositionApr 7, 2025Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 5, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Single-chain Fv antibody of E11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,8976
Polymers26,1571
Non-polymers7405
Water6,179343
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)33.650, 41.820, 162.450
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

-
Components

#1: Antibody Single-chain Fv antibody of E11


Mass: 26157.059 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli)
#2: Chemical ChemComp-A1L81 / 6-[2-(3,5-dinitro-4-oxidanyl-phenyl)ethanoylamino]hexanoic acid


Mass: 357.316 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H19N3O8 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 343 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.18 Å3/Da / Density % sol: 43.71 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.1 M HEPES sodium pH 7.5, 10% v/v 2-propanol, 20% w/v polyethylene glycol 4,000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 0.8 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Oct 25, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8 Å / Relative weight: 1
ReflectionResolution: 1.06→50 Å / Num. obs: 105351 / % possible obs: 100 % / Redundancy: 16.5 % / Biso Wilson estimate: 8.7 Å2 / Rmerge(I) obs: 0.181 / Net I/σ(I): 10
Reflection shellResolution: 1.06→1.12 Å / Redundancy: 15.9 % / Rmerge(I) obs: 2.467 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 15852 / CC1/2: 0.588 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX1.21.2_5419refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.06→37.18 Å / SU ML: 0.1179 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 12.69
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1433 5262 5 %
Rwork0.1242 99968 -
obs0.1252 105230 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 13 Å2
Refinement stepCycle: LAST / Resolution: 1.06→37.18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1790 0 50 343 2183
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00862296
X-RAY DIFFRACTIONf_angle_d1.18363184
X-RAY DIFFRACTIONf_chiral_restr0.0974345
X-RAY DIFFRACTIONf_plane_restr0.013418
X-RAY DIFFRACTIONf_dihedral_angle_d14.4516884
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.06-1.070.35991740.35573304X-RAY DIFFRACTION99.63
1.07-1.080.35131730.32313280X-RAY DIFFRACTION100
1.08-1.10.29021720.26763275X-RAY DIFFRACTION100
1.1-1.110.24931730.23613278X-RAY DIFFRACTION100
1.11-1.130.21741740.20373316X-RAY DIFFRACTION100
1.13-1.140.17861720.17623264X-RAY DIFFRACTION100
1.14-1.160.19111730.15433296X-RAY DIFFRACTION99.97
1.16-1.180.1821730.14693270X-RAY DIFFRACTION100
1.18-1.190.17241750.14413339X-RAY DIFFRACTION100
1.19-1.210.15881720.14323280X-RAY DIFFRACTION100
1.21-1.230.17361740.14873285X-RAY DIFFRACTION100
1.23-1.260.17171740.14873313X-RAY DIFFRACTION100
1.26-1.280.17281740.15053300X-RAY DIFFRACTION100
1.28-1.310.17491750.14423338X-RAY DIFFRACTION99.97
1.31-1.340.1591720.11693261X-RAY DIFFRACTION100
1.34-1.370.14761760.1093325X-RAY DIFFRACTION100
1.37-1.40.12021750.10743329X-RAY DIFFRACTION100
1.4-1.440.15161730.09963306X-RAY DIFFRACTION100
1.44-1.480.13411740.09883314X-RAY DIFFRACTION100
1.48-1.530.13291760.09373340X-RAY DIFFRACTION99.97
1.53-1.580.12641750.09293333X-RAY DIFFRACTION100
1.58-1.650.11011750.09473297X-RAY DIFFRACTION100
1.65-1.720.12621760.09773360X-RAY DIFFRACTION99.97
1.72-1.810.12511760.09873339X-RAY DIFFRACTION100
1.81-1.930.11161770.10053374X-RAY DIFFRACTION100
1.93-2.070.11321780.09493361X-RAY DIFFRACTION100
2.07-2.280.12131770.10283383X-RAY DIFFRACTION100
2.28-2.610.13521810.11473430X-RAY DIFFRACTION100
2.61-3.290.13421810.12213439X-RAY DIFFRACTION100
3.29-37.180.13211920.13223639X-RAY DIFFRACTION99.9

+
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