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- PDB-1jem: NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARR... -

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Basic information

Entry
Database: PDB / ID: 1jem
TitleNMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES
ComponentsHISTIDINE CONTAINING PROTEIN
KeywordsPHOSPHOTRANSFERASE / HISTIDINE CONTAINING PROTEIN / PHOSPHOHISTIDINE / PTS
Function / homology
Function and homology information


regulation of carbohydrate utilization / phosphoenolpyruvate-dependent sugar phosphotransferase system / cytoplasm
Similarity search - Function
Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / HPr-like / Phosphocarrier protein HPr-like / HPr-like superfamily / : / PTS HPr component phosphorylation site / PTS HPR domain profile. / Histidine-containing Protein; Chain: A; ...Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / HPr-like / Phosphocarrier protein HPr-like / HPr-like superfamily / : / PTS HPr component phosphorylation site / PTS HPR domain profile. / Histidine-containing Protein; Chain: A; / PTS HPR domain serine phosphorylation site signature. / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphocarrier protein HPr
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR
AuthorsJones, B.E. / Rajagopal, P. / Klevit, R.E.
Citation
Journal: Protein Sci. / Year: 1997
Title: Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.
Authors: Jones, B.E. / Rajagopal, P. / Klevit, R.E.
#1: Journal: Biochemistry / Year: 1994
Title: Structural Consequences of Histidine Phosphorylation: NMR Characterization of the Phosphohistidine Form of Histidine-Containing Protein from Bacillus Subtilis and Escherichia Coli
Authors: Rajagopal, P. / Waygood, E.B. / Klevit, R.E.
#2: Journal: Protein Sci. / Year: 1992
Title: Solution Structure of the Phosphocarrier Protein Hpr from Bacillus Subtilis by Two-Dimensional NMR Spectroscopy
Authors: Wittekind, M. / Rajagopal, P. / Branchini, B.R. / Reizer, J. / Saier Junior, M.H. / Klevit, R.E.
#3: Journal: Biochemistry / Year: 1990
Title: Sequence-Specific 1H NMR Resonance Assignments of Bacillus Subtilis Hpr: Use of Spectra Obtained from Mutants to Resolve Spectral Overlap
Authors: Wittekind, M. / Reizer, J. / Klevit, R.E.
History
DepositionApr 1, 1997Processing site: BNL
Revision 1.0Jul 23, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HISTIDINE CONTAINING PROTEIN


Theoretical massNumber of molelcules
Total (without water)9,1151
Polymers9,1151
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 50LOWEST ENERGY
Representative

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Components

#1: Protein HISTIDINE CONTAINING PROTEIN / HPR


Mass: 9115.053 Da / Num. of mol.: 1 / Mutation: M51V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / Strain (production host): GM-1 / References: UniProt: P08877

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 6.9 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX 500 / Manufacturer: Bruker / Model: DMX 500 / Field strength: 500.13 MHz

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Processing

Software
NameVersionClassification
X-PLOR3model building
X-PLOR3refinement
X-PLOR3phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3BRUNGERrefinement
X-PLORstructure solution
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 25

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