[English] 日本語
Yorodumi
- PDB-7rxj: Fab236 in complex with the C-terminal alpha-TSR domain of P. falc... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7rxj
TitleFab236 in complex with the C-terminal alpha-TSR domain of P. falciparum
Components
  • Circumsporozoite protein
  • Fab236 heavy chain
  • Fab236 light chain
KeywordsIMMUNE SYSTEM / Malaria / Antibody / Sporozoite / Circumsporozoite protein / alpha-TSR domain
Function / homology
Function and homology information


host cell surface binding / symbiont entry into host / entry into host cell by a symbiont-containing vacuole / heparan sulfate proteoglycan binding / side of membrane / cell surface / plasma membrane / cytoplasm
Similarity search - Function
Plasmodium circumsporozoite protein / Thrombospondin type 1 domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat
Similarity search - Domain/homology
Circumsporozoite protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Plasmodium falciparum (malaria parasite P. falciparum)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.345 Å
AuthorsPholcharee, T. / Oyen, D. / Wilson, I.A.
Funding support United States, 1items
OrganizationGrant numberCountry
Bill & Melinda Gates FoundationOPP1170236 United States
CitationJournal: Plos Pathog. / Year: 2022
Title: A novel CSP C-terminal epitope targeted by an antibody with protective activity against Plasmodium falciparum.
Authors: Beutler, N. / Pholcharee, T. / Oyen, D. / Flores-Garcia, Y. / MacGill, R.S. / Garcia, E. / Calla, J. / Parren, M. / Yang, L. / Volkmuth, W. / Locke, E. / Regules, J.A. / Dutta, S. / ...Authors: Beutler, N. / Pholcharee, T. / Oyen, D. / Flores-Garcia, Y. / MacGill, R.S. / Garcia, E. / Calla, J. / Parren, M. / Yang, L. / Volkmuth, W. / Locke, E. / Regules, J.A. / Dutta, S. / Emerling, D. / Early, A.M. / Neafsey, D.E. / Winzeler, E. / King, C.R. / Zavala, F. / Burton, D.R. / Wilson, I.A. / Rogers, T.F.
History
DepositionAug 23, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2022Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2022Group: 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_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Apr 3, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Fab236 light chain
A: Fab236 heavy chain
L: Fab236 light chain
H: Fab236 heavy chain
I: Circumsporozoite protein
G: Circumsporozoite protein


Theoretical massNumber of molelcules
Total (without water)108,5116
Polymers108,5116
Non-polymers00
Water2,504139
1
B: Fab236 light chain
A: Fab236 heavy chain
G: Circumsporozoite protein


Theoretical massNumber of molelcules
Total (without water)54,2563
Polymers54,2563
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
L: Fab236 light chain
H: Fab236 heavy chain
I: Circumsporozoite protein


Theoretical massNumber of molelcules
Total (without water)54,2563
Polymers54,2563
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)130.137, 45.564, 201.087
Angle α, β, γ (deg.)90.00, 94.04, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Antibody Fab236 light chain


Mass: 22792.162 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)
#2: Antibody Fab236 heavy chain


Mass: 24009.908 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)
#3: Protein Circumsporozoite protein


Mass: 7453.486 Da / Num. of mol.: 2
Fragment: C-terminal alpha-TSR domain (UNP residues 310-375)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (isolate 3D7) (eukaryote)
Strain: isolate 3D7 / Gene: PF3D7_0304600 / Production host: Escherichia coli (E. coli) / References: UniProt: Q7K740
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 139 / 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: 2.82 Å3/Da / Density % sol: 56.35 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: 30% PEG2000 MME, 0.2 M ammonium sulfate, 0.1 M acetate, pH 4.6

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 28, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.345→50 Å / Num. obs: 46380 / % possible obs: 96.7 % / Redundancy: 5.2 % / CC1/2: 0.946 / Rpim(I) all: 0.055 / Rsym value: 0.12 / Net I/σ(I): 13.7
Reflection shellResolution: 2.345→2.44 Å / Redundancy: 3.1 % / Mean I/σ(I) obs: 1.6 / Num. unique obs: 1678 / CC1/2: 0.828 / Rpim(I) all: 0.254 / Rsym value: 0.463 / % possible all: 71.1

-
Processing

Software
NameVersionClassification
PHENIX(1.16_3549: ???)refinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Homology model

Resolution: 2.345→42.24 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.21 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2486 2436 5.26 %
Rwork0.2175 --
obs0.2193 46326 92.31 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.345→42.24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7260 0 0 139 7399
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0067437
X-RAY DIFFRACTIONf_angle_d0.75210168
X-RAY DIFFRACTIONf_dihedral_angle_d11.2764408
X-RAY DIFFRACTIONf_chiral_restr0.0491166
X-RAY DIFFRACTIONf_plane_restr0.0051304
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.345-2.39270.261310.2762681X-RAY DIFFRACTION24
2.3927-2.44470.3223980.28991907X-RAY DIFFRACTION70
2.4447-2.50160.34091070.29632409X-RAY DIFFRACTION87
2.5016-2.56410.34671280.31082669X-RAY DIFFRACTION94
2.5641-2.63340.42881470.31092676X-RAY DIFFRACTION98
2.6334-2.71090.37251400.29022759X-RAY DIFFRACTION99
2.7109-2.79840.33151360.27932764X-RAY DIFFRACTION99
2.7984-2.89840.28871670.27352768X-RAY DIFFRACTION100
2.8984-3.01440.33011510.27122787X-RAY DIFFRACTION100
3.0144-3.15160.30681480.2852787X-RAY DIFFRACTION100
3.1516-3.31770.31331480.24672767X-RAY DIFFRACTION100
3.3177-3.52540.26471610.222810X-RAY DIFFRACTION100
3.5254-3.79750.23451750.20362787X-RAY DIFFRACTION100
3.7975-4.17930.22511870.18392757X-RAY DIFFRACTION100
4.1793-4.78340.1641720.14362792X-RAY DIFFRACTION100
4.7834-6.02380.1771750.16772829X-RAY DIFFRACTION100
6.0238-42.240.21921650.18672941X-RAY DIFFRACTION99

+
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