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- PDB-1pih: THE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP... -

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Basic information

Entry
Database: PDB / ID: 1pih
TitleTHE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP I FROM E.HALOPHILA THROUGH NUCLEAR MAGNETIC RESONANCE
ComponentsHIGH POTENTIAL IRON SULFUR PROTEIN
KeywordsELECTRON TRANSFER(IRON-SULFUR PROTEIN)
Function / homology
Function and homology information


aerobic electron transport chain / 4 iron, 4 sulfur cluster binding / electron transfer activity / metal ion binding
Similarity search - Function
High potential iron-sulphur protein / High-Potential Iron-Sulfur Protein; Chain A / High potential iron-sulfur protein / High potential iron-sulphur protein / High potential iron-sulphur protein superfamily / High potential iron-sulfur proteins family profile. / Few Secondary Structures / Irregular
Similarity search - Domain/homology
IRON/SULFUR CLUSTER / High-potential iron-sulfur protein isozyme 1
Similarity search - Component
Biological speciesHalorhodospira halophila (bacteria)
MethodSOLUTION NMR
AuthorsBanci, L. / Bertini, I. / Eltis, L.D. / Felli, I. / Kastrau, D.H.W. / Luchinat, C. / Piccioli, M. / Pierattelli, R. / Smith, M.
Citation
Journal: Eur.J.Biochem. / Year: 1994
Title: The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance.
Authors: Banci, L. / Bertini, I. / Eltis, L.D. / Felli, I.C. / Kastrau, D.H. / Luchinat, C. / Piccioli, M. / Pierattelli, R. / Smith, M.
#1: Journal: Eur.J.Biochem. / Year: 1994
Title: Sequence Specific Assignment of the 1H and 15N Nuclear Magnetic Resonance Spectra of the Reduced Recombinant High Potential Iron Sulfur Protein (Hipip) I from Ectothiorhodospira Halophila
Authors: Bertini, I. / Felli, I. / Kastrau, D.H.W. / Luchinat, C. / Piccioli, M. / Viezzoli, M.S.
History
DepositionAug 3, 1994Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HIGH POTENTIAL IRON SULFUR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)8,3552
Polymers8,0041
Non-polymers3521
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: GLN 44 - ASP 45 MODEL 5 OMEGA = 148.94 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
2: ARG 49 - CYS 50 MODEL 8 OMEGA = 141.06 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: SER 2 - GLU 3 MODEL 9 OMEGA = 211.11 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: PRO 71 - ALA 72 MODEL 11 OMEGA = 142.48 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / -
Representative

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Components

#1: Protein HIGH POTENTIAL IRON SULFUR PROTEIN


Mass: 8003.524 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Halorhodospira halophila (bacteria) / Gene: POTENTIAL / References: UniProt: P04168
#2: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe4S4

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

SoftwareName: AMBER / Classification: refinement
NMR software
NameDeveloperClassification
DIANAGUNTERT,BRAUN,WUTHRICHrefinement
AmberPEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMANrefinement
NMR ensembleConformers submitted total number: 15

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