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- PDB-1tus: SOLUTION STRUCTURE OF REACTIVE-SITE HYDROLYZED TURKEY OVOMUCOID T... -

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Basic information

Entry
Database: PDB / ID: 1tus
TitleSOLUTION STRUCTURE OF REACTIVE-SITE HYDROLYZED TURKEY OVOMUCOID THIRD DOMAIN BY NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY METHODS
ComponentsOVOMUCOID
KeywordsSERINE PROTEINASE INHIBITOR
Function / homology
Function and homology information


molecular function inhibitor activity / serine-type endopeptidase inhibitor activity / extracellular region
Similarity search - Function
Proteinase inhibitor I1, Kazal-type, metazoa / : / Kazal serine protease inhibitors family signature. / Kazal-type serine protease inhibitor domain / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #30 / Kazal type serine protease inhibitors / Kazal domain superfamily / Kazal domain / Kazal domain profile. / Wheat Germ Agglutinin (Isolectin 2); domain 1 ...Proteinase inhibitor I1, Kazal-type, metazoa / : / Kazal serine protease inhibitors family signature. / Kazal-type serine protease inhibitor domain / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #30 / Kazal type serine protease inhibitors / Kazal domain superfamily / Kazal domain / Kazal domain profile. / Wheat Germ Agglutinin (Isolectin 2); domain 1 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesMeleagris gallopavo (turkey)
MethodSOLUTION NMR
AuthorsWalkenhorst, W.F. / Krezel, A.M. / Rhyu, G.I. / Markley, J.L.
CitationJournal: J.Mol.Biol. / Year: 1994
Title: Solution structure of reactive-site hydrolyzed turkey ovomucoid third domain by nuclear magnetic resonance and distance geometry methods.
Authors: Walkenhorst, W.F. / Krezel, A.M. / Rhyu, G.I. / Markley, J.L.
History
DepositionJul 6, 1994Processing site: BNL
Revision 1.0Oct 15, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: OVOMUCOID


Theoretical massNumber of molelcules
Total (without water)6,0271
Polymers6,0271
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Atom site foot note1: CIS PROLINE - PRO 12 MODEL 1
2: TYR 20 - ARG 21 MODEL 1 OMEGA = 214.18 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: CIS PROLINE - PRO 12 MODEL 2
4: TYR 20 - ARG 21 MODEL 2 OMEGA = 215.32 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
5: CIS PROLINE - PRO 12 MODEL 3
6: TYR 20 - ARG 21 MODEL 3 OMEGA = 213.03 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
7: ARG 21 - PRO 22 MODEL 3 OMEGA = 217.32 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
8: CIS PROLINE - PRO 12 MODEL 4 / 9: CIS PROLINE - PRO 12 MODEL 5 / 10: CIS PROLINE - PRO 12 MODEL 6 / 11: CIS PROLINE - PRO 12 MODEL 7 / 12: CIS PROLINE - PRO 12 MODEL 8
13: TYR 20 - ARG 21 MODEL 8 OMEGA = 214.47 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
14: ARG 21 - PRO 22 MODEL 8 OMEGA = 211.07 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
15: CIS PROLINE - PRO 12 MODEL 9 / 16: CIS PROLINE - PRO 12 MODEL 10 / 17: CIS PROLINE - PRO 12 MODEL 11 / 18: CIS PROLINE - PRO 12 MODEL 12
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)12 / -
Representative

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Components

#1: Protein OVOMUCOID


Mass: 6026.811 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Meleagris gallopavo (turkey) / References: UniProt: P68390
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Processing

NMR softwareName: DSPACE / Version: 4 / Classification: refinement
NMR ensembleConformers submitted total number: 12

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