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- PDB-1hic: THE NMR SOLUTION STRUCTURE OF HIRUDIN(1-51) AND COMPARISON WITH C... -

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Entry
Database: PDB / ID: 1hic
TitleTHE NMR SOLUTION STRUCTURE OF HIRUDIN(1-51) AND COMPARISON WITH CORRESPONDING THREE-DIMENSIONAL STRUCTURES DETERMINED USING THE COMPLETE 65-RESIDUE HIRUDIN POLYPEPTIDE CHAIN
ComponentsHIRUDIN VARIANT
KeywordsHIRUDIN
Function / homology
Function and homology information


negative regulation of serine-type peptidase activity / serine-type endopeptidase inhibitor activity / toxin activity / extracellular space
Similarity search - Function
Thrombin Inhibitor (Hirudin); Chain I / Thrombin Inhibitor (Hirudin), subunit I / Hirudin / Proteinase inhibitor I14, hirudin / Thrombin inhibitor hirudin / Hirudin/antistatin / Distorted Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesHirudo medicinalis (medicinal leech)
MethodSOLUTION NMR
AuthorsSzyperski, T. / Guntert, P. / Stone, S.R. / Wuthrich, K.
Citation
Journal: J.Mol.Biol. / Year: 1992
Title: Nuclear magnetic resonance solution structure of hirudin(1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain.
Authors: Szyperski, T. / Guntert, P. / Stone, S.R. / Wuthrich, K.
#1: Journal: J.Mol.Biol. / Year: 1992
Title: Impact of Protein-Protein Contacts on the Conformation of Thrombin-Bound Hirudin Studied by Comparison with the NMR Solution Structure of Hirudin(1-51)
Authors: Szyperski, T. / Guntert, P. / Tulinsky, A. / Bode, W. / Huber, R. / Wuthrich, K.
#2: Journal: Biochemistry / Year: 1989
Title: Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance
Authors: Haruyama, H. / Wuthrich, K.
#3: Journal: Biochemistry / Year: 1989
Title: Solution Structure of Recombinant Hirudin and the Lys 47-Glu Mutant: A Nuclear Magnetic Resonance and Hybrid Geometry-Dynamical Simulated Annealing Study
Authors: Folkers, P.J.M. / Clore, G.M. / Driscoll, P.C. / Dodt, J. / Kohler, S. / Gronenborn, A.M.
History
DepositionApr 30, 1992Processing site: BNL
Revision 1.0Jan 31, 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
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
Revision 1.4Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HIRUDIN VARIANT


Theoretical massNumber of molelcules
Total (without water)5,2941
Polymers5,2941
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: SER 32 - ASP 33 MODEL 1 OMEGA =218.49 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
2: SER 32 - ASP 33 MODEL 10 OMEGA =215.83 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: SER 32 - ASP 33 MODEL 15 OMEGA =219.86 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein HIRUDIN VARIANT


Mass: 5293.813 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hirudo medicinalis (medicinal leech) / References: UniProt: P01050
Has protein modificationY

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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

NMR software
NameVersionDeveloperClassification
DIANAGUNTERT,BRAUN,WUTHRICHrefinement
Amber3SINGH,WEINER,CALDWELL,KOLLMANrefinement
NMR ensembleConformers submitted total number: 20

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