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- PDB-1trl: NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THER... -

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Entry
Database: PDB / ID: 1trl
TitleNMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS HAVING THE NATIVE STRUCTURE
ComponentsTHERMOLYSIN FRAGMENT 255 - 316
KeywordsHYDROLASE (METALLOPROTEASE)
Function / homology
Function and homology information


thermolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding
Similarity search - Function
PepSY domain / Peptidase propeptide and YPEB domain / : / Peptidase M4, C-terminal / FTP domain / Peptidase M4 domain / Peptidase M4 / Thermolysin metallopeptidase, catalytic domain / Thermolysin metallopeptidase, alpha-helical domain / Fungalysin/Thermolysin Propeptide Motif ...PepSY domain / Peptidase propeptide and YPEB domain / : / Peptidase M4, C-terminal / FTP domain / Peptidase M4 domain / Peptidase M4 / Thermolysin metallopeptidase, catalytic domain / Thermolysin metallopeptidase, alpha-helical domain / Fungalysin/Thermolysin Propeptide Motif / Neutral Protease Domain 2 / Neutral Protease; domain 2 / Peptidase M4/M1, CTD superfamily / Neutral zinc metallopeptidases, zinc-binding region signature. / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesBacillus thermoproteolyticus (bacteria)
MethodSOLUTION NMR
AuthorsRico, M. / Jimenez, M.A. / Gonzalez, C. / De Filippis, V. / Fontana, A.
Citation
Journal: Biochemistry / Year: 1994
Title: NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.
Authors: Rico, M. / Jimenez, M.A. / Gonzalez, C. / De Filippis, V. / Fontana, A.
#1: Journal: Eur.J.Biochem. / Year: 1993
Title: Cd and H-NMR Studies on the Conformational Properties of Peptide Fragments from the C-Terminal Domain of Thermolysin
Authors: Jimenez, M.A. / Bruix, M. / Gonzalez, C. / Blanco, F.J. / Nieto, J.L. / Herranz, J. / Rico, M.
#2: Journal: J.Mol.Biol. / Year: 1985
Title: Folding of Thermolysin Fragments: Identification of the Minimum Size of a Carboxyl-Terminal Fragment that Can Fold Into a Stable Native-Like Structure
Authors: Dalzoppo, D. / Vita, C. / Fontana, A.
History
DepositionSep 2, 1994Processing site: BNL
Revision 1.0Feb 7, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Assembly

Deposited unit
A: THERMOLYSIN FRAGMENT 255 - 316
B: THERMOLYSIN FRAGMENT 255 - 316


Theoretical massNumber of molelcules
Total (without water)13,2632
Polymers13,2632
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)8 / -
Representative

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Components

#1: Protein THERMOLYSIN FRAGMENT 255 - 316


Mass: 6631.481 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus thermoproteolyticus (bacteria)
References: UniProt: P00800, thermolysin

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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 softwareName: GROMOS / Developer: VAN GUNSTEREN,BERENDSEN / Classification: refinement
NMR ensembleConformers submitted total number: 8

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