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- PDB-1a90: RECOMBINANT MUTANT CHICKEN EGG WHITE CYSTATIN, NMR, 31 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1a90
TitleRECOMBINANT MUTANT CHICKEN EGG WHITE CYSTATIN, NMR, 31 STRUCTURES
ComponentsCYSTATIN
KeywordsTHIOL PROTEASE INHIBITOR / PROTEINASE INHIBITOR / THIOL PROTEINASE / STEFFINS / KININOGENS
Function / homology
Function and homology information


cysteine-type endopeptidase inhibitor activity / vesicle / extracellular space / cytoplasm
Similarity search - Function
Proteinase inhibitor I25, cystatin, conserved site / Cysteine proteases inhibitors signature. / Cystatin domain / Cystatin-like domain / Cystatin domain / Nuclear Transport Factor 2; Chain: A, - #10 / Cystatin superfamily / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta
Similarity search - Domain/homology
Biological speciesGallus gallus (chicken)
MethodSOLUTION NMR
AuthorsDieckmann, T. / Mitschang, L. / Hofmann, M. / Kos, J. / Turk, V. / Auerswald, E.A. / Jaenicke, R. / Oschkinat, H.
Citation
Journal: J.Mol.Biol. / Year: 1993
Title: The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.
Authors: Dieckmann, T. / Mitschang, L. / Hofmann, M. / Kos, J. / Turk, V. / Auerswald, E.A. / Jaenicke, R. / Oschkinat, H.
#1: Journal: J.Mol.Biol. / Year: 1993
Title: Conformational Variability of Chicken Cystatin. Comparison of Structures Determined by X-Ray Diffraction and NMR Spectroscopy
Authors: Engh, R.A. / Dieckmann, T. / Bode, W. / Auerswald, E.A. / Turk, V. / Huber, R. / Oschkinat, H.
History
DepositionApr 14, 1998Processing site: BNL
Revision 1.0Jun 17, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
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: CYSTATIN


Theoretical massNumber of molelcules
Total (without water)12,1691
Polymers12,1691
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)31 / -
Representative

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Components

#1: Protein CYSTATIN


Mass: 12168.792 Da / Num. of mol.: 1 / Mutation: M29I, M89L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Cell: EGG / Cellular location: CYTOPLASM (WHITE) / Organ: EGG / Production host: Escherichia coli (E. coli) / References: UniProt: P01038
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

Software
NameVersionClassification
X-PLOR3model building
X-PLOR3refinement
X-PLOR3phasing
NMR softwareName: X-PLOR / Version: 3 / Developer: BRUNGER / Classification: refinement
RefinementSoftware ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformers submitted total number: 31

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