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- PDB-2mh8: GA-79-MBP cs-rosetta structures -

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Basic information

Entry
Database: PDB / ID: 2mh8
TitleGA-79-MBP cs-rosetta structures
ComponentsGA-79-MBP, maltose binding protein
KeywordsPROTEIN BINDING / MBP / maltose binding protein / GA / human serum albumin binding protein
Function / homologyAlbumin-binding domain / GA-like domain / GA-like domain / Immunoglobulin/albumin-binding domain superfamily / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha / GA-79-MBP, maltose binding protein
Function and homology information
Biological speciesStreptococcus dysgalactiae (bacteria)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model1
AuthorsHe, Y. / Chen, Y. / Porter, L. / Bryan, P. / Orban, J.
CitationJournal: Biophys.J. / Year: 2015
Title: Subdomain interactions foster the design of two protein pairs with 80% sequence identity but different folds.
Authors: Porter, L.L. / He, Y. / Chen, Y. / Orban, J. / Bryan, P.N.
History
DepositionNov 19, 2013Deposition site: BMRB / Processing site: RCSB
Revision 1.0Apr 8, 2015Provider: repository / Type: Initial release
Revision 1.1May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer
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

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Assembly

Deposited unit
A: GA-79-MBP, maltose binding protein


Theoretical massNumber of molelcules
Total (without water)6,3121
Polymers6,3121
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 3000structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein GA-79-MBP, maltose binding protein


Mass: 6312.251 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus dysgalactiae (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0J9X1W7*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D CBCA(CO)NH
1313D HN(CA)CB
1413D HNHA
1513D HNCO

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Sample preparation

DetailsContents: 0.27 mM [U-100% 13C; U-100% 15N] GA-79-MBP, 100 mM potassium phosphate, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.27 mMGA-79-MBP-1[U-100% 13C; U-100% 15N]1
100 mMpotassium phosphate-21
Sample conditionsIonic strength: 0.1 / pH: 7 / Pressure: ambient / Temperature: 283 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX6001
Bruker Avance IIIBrukerAVANCE III6002

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Processing

NMR software
NameDeveloperClassification
CS-ROSETTAShen, Vernon, Baker and Baxstructure solution
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
SparkyGoddardchemical shift assignment
MOLMOLKoradi, Billeter and Wuthrichdata analysis
TopSpinBruker Biospinstructure solution
ProcheckLaskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thorntondata analysis
CSIDavid Wishart, Brian Sykesdata analysis
CS-ROSETTAShen, Vernon, Baker and Baxrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 3000 / Conformers submitted total number: 10

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