[English] 日本語
Yorodumi
- PDB-7sej: Structure-based design of prefusion-stabilized human metapneumovi... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7sej
TitleStructure-based design of prefusion-stabilized human metapneumovirus fusion proteins
Components
  • Fusion glycoprotein F1 subunit
  • Fusion glycoprotein F2 subunit
KeywordsVIRAL PROTEIN / human metapneumovirus / fusion protein
Function / homologyPrecursor fusion glycoprotein F0, Paramyxoviridae / Fusion glycoprotein F0 / fusion of virus membrane with host plasma membrane / host cell plasma membrane / virion membrane / plasma membrane / Fusion glycoprotein F0
Function and homology information
Biological speciesHuman metapneumovirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.51 Å
AuthorsHsieh, C.-L. / Rush, S.A. / McLellan, J.S.
Funding support United States, 2items
OrganizationGrant numberCountry
Robert A. Welch FoundationF-0003-19620604 United States
Department of Energy (DOE, United States)DE-AC02-06CH11357 United States
CitationJournal: Nat Commun / Year: 2022
Title: Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins.
Authors: Hsieh, C.L. / Rush, S.A. / Palomo, C. / Chou, C.W. / Pickens, W. / Mas, V. / McLellan, J.S.
History
DepositionSep 30, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 9, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 30, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Fusion glycoprotein F2 subunit
F: Fusion glycoprotein F1 subunit
C: Fusion glycoprotein F2 subunit
A: Fusion glycoprotein F1 subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,8298
Polymers120,9444
Non-polymers8854
Water2,450136
1
B: Fusion glycoprotein F2 subunit
F: Fusion glycoprotein F1 subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,9144
Polymers60,4722
Non-polymers4422
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9220 Å2
ΔGint-47 kcal/mol
Surface area20800 Å2
MethodPISA
2
C: Fusion glycoprotein F2 subunit
A: Fusion glycoprotein F1 subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,9144
Polymers60,4722
Non-polymers4422
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8780 Å2
ΔGint-49 kcal/mol
Surface area20550 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.379, 105.809, 90.990
Angle α, β, γ (deg.)90.000, 105.260, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

-
Components

#1: Protein Fusion glycoprotein F2 subunit


Mass: 11015.444 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human metapneumovirus / Cell (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: H6X1Z0
#2: Protein Fusion glycoprotein F1 subunit


Mass: 49456.418 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: the protein is cleaved into the two subunits (entities 1 and 2) as it transported through ER-Golgi
Source: (gene. exp.) Human metapneumovirus / Cell (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: H6X1Z0
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 136 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49.49 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 500 nl of hMPV F (10 mg/ml) with 500 nl of reservoir solution containing 0.1 M MES pH 6.0 and 12%(v/v) PEK 20k.

-
Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 1, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.5→45.4 Å / Num. obs: 35650 / % possible obs: 97.6 % / Redundancy: 3.2 % / Biso Wilson estimate: 40.37 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.078 / Rpim(I) all: 0.073 / Net I/σ(I): 8.3
Reflection shellResolution: 2.51→2.6 Å / Rmerge(I) obs: 0.038 / Mean I/σ(I) obs: 15.5 / Num. unique obs: 801 / CC1/2: 0.994 / Rpim(I) all: 0.037

-
Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
PDB_EXTRACTdata extraction
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5wb0
Resolution: 2.51→45.31 Å / SU ML: 0.3247 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.5753
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2527 1802 5.06 %
Rwork0.209 33814 -
obs0.2113 35616 97.35 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 42.77 Å2
Refinement stepCycle: LAST / Resolution: 2.51→45.31 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6562 0 56 136 6754
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00526707
X-RAY DIFFRACTIONf_angle_d0.70019073
X-RAY DIFFRACTIONf_chiral_restr0.04731088
X-RAY DIFFRACTIONf_plane_restr0.0061155
X-RAY DIFFRACTIONf_dihedral_angle_d23.04472470
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.51-2.580.30861580.26242576X-RAY DIFFRACTION98.03
2.58-2.650.33331650.25772608X-RAY DIFFRACTION98.33
2.65-2.740.2831200.23732612X-RAY DIFFRACTION98.03
2.74-2.840.31591130.24172587X-RAY DIFFRACTION96.77
2.84-2.950.31431200.2522561X-RAY DIFFRACTION94.63
2.95-3.080.2841220.26142625X-RAY DIFFRACTION98.39
3.08-3.250.29011660.2372633X-RAY DIFFRACTION98.59
3.25-3.450.30051510.21982562X-RAY DIFFRACTION97.31
3.45-3.720.2481250.21432545X-RAY DIFFRACTION95.46
3.72-4.090.23391420.20032631X-RAY DIFFRACTION98.58
4.09-4.680.20781240.17452602X-RAY DIFFRACTION96.98
4.68-5.90.23441350.18152652X-RAY DIFFRACTION97.65
5.9-45.310.18721610.17482620X-RAY DIFFRACTION96.8

+
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