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- PDB-2plp: Ultra high resolution backbone conformation of protein GB1 from r... -

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Basic information

Entry
Database: PDB / ID: 2plp
TitleUltra high resolution backbone conformation of protein GB1 from residual dipolar couplings alone
ComponentsImmunoglobulin G-binding protein G
KeywordsIMMUNE SYSTEM/PROTEIN BINDING / residual dipolar couplings / perdeuteration / NMR / ultra-high resolution / proton-proton couplings / rdc / hydrogen bonds / IMMUNE SYSTEM-PROTEIN BINDING COMPLEX
Function / homology
Function and homology information


IgG binding / extracellular region
Similarity search - Function
IgG-binding B / B domain / M protein-type anchor domain / GA-like domain / GA-like domain / Ubiquitin-like (UB roll) - #10 / Immunoglobulin/albumin-binding domain superfamily / YSIRK Gram-positive signal peptide / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. ...IgG-binding B / B domain / M protein-type anchor domain / GA-like domain / GA-like domain / Ubiquitin-like (UB roll) - #10 / Immunoglobulin/albumin-binding domain superfamily / YSIRK Gram-positive signal peptide / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain / Ubiquitin-like (UB roll) / Roll / Alpha Beta
Similarity search - Domain/homology
Immunoglobulin G-binding protein G / Immunoglobulin G-binding protein G
Similarity search - Component
Biological speciesStreptococcus sp. 'group G' (bacteria)
MethodSOLUTION NMR / dynamic meccano
AuthorsBouvignies, G. / Meier, S. / Grzesiek, S. / Blackledge, M.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2006
Title: Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment media
Authors: Bouvignies, G. / Meier, S. / Grzesiek, S. / Blackledge, M.
History
DepositionApr 20, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Immunoglobulin G-binding protein G


Theoretical massNumber of molelcules
Total (without water)5,9411
Polymers5,9411
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 1all calculated structures submitted
Representative

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Components

#1: Antibody Immunoglobulin G-binding protein G / IgG-binding protein G


Mass: 5941.474 Da / Num. of mol.: 1 / Fragment: First Immunoglobin binding domain (GB1)
Source method: isolated from a genetically manipulated source
Details: deposited only main chain atoms / Source: (gene. exp.) Streptococcus sp. 'group G' (bacteria) / Strain: group G / Gene: spg / Production host: Escherichia coli (E. coli) / References: UniProt: P19909, UniProt: P06654*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HCN-HSQC
222water flip-back 3D 15N-edited 1H-1H COSYHMQC

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Sample preparation

DetailsContents: perdeuterated (triple labelled 15N, 13C, 2D)
Solvent system: Partially aligned in bacteriophage and lyotrophic alcohol medium.
Sample conditionsIonic strength: 50mM salt / pH: 5.6 / Pressure: ambient / Temperature: 300 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Dynamic Meccano1bouvignies et alstructure solution
Dynamic Meccano1bouvignies et alrefinement
RefinementMethod: dynamic meccano / Software ordinal: 1
Details: Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment media. Angew Chem Int Ed Engl. 2006 Dec 11;45(48):8166-9.
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 1 / Conformers submitted total number: 1

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