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- PDB-1az6: THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDIN... -

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Basic information

Entry
Database: PDB / ID: 1az6
TitleTHREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 23 STRUCTURES
ComponentsCELLOBIOHYDROLASE ICellulose 1,4-beta-cellobiosidase
KeywordsCELLULASE / NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY / PROTEIN-CARBOHYDRATE INTERACTION
Function / homology
Function and homology information


cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region
Similarity search - Function
Glycoside hydrolase, family 7 / Glycoside hydrolase family 7, catalytic domain superfamily / Glycosyl hydrolase family 7 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain / CBM1 (carbohydrate binding type-1) domain profile. / Fungal-type cellulose-binding domain / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Biological speciesHypocrea jecorina (fungus)
MethodSOLUTION NMR / distance geometry
AuthorsMattinen, M.-L.
CitationJournal: Protein Sci. / Year: 1997
Title: Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Authors: Mattinen, M.L. / Kontteli, M. / Kerovuo, J. / Linder, M. / Annila, A. / Lindeberg, G. / Reinikainen, T. / Drakenberg, T.
History
DepositionNov 25, 1997Processing site: BNL
Revision 1.0Apr 8, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: 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_ref_seq_dif
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_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CELLOBIOHYDROLASE I


Theoretical massNumber of molelcules
Total (without water)3,6541
Polymers3,6541
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)23 / 60LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide CELLOBIOHYDROLASE I / Cellulose 1,4-beta-cellobiosidase / CBD


Mass: 3654.030 Da / Num. of mol.: 1 / Fragment: CELLULOSE-BINDING DOMAIN / Mutation: Y5A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hypocrea jecorina (fungus)
References: UniProt: P62694, cellulose 1,4-beta-cellobiosidase (non-reducing end)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111TOCSY
121COSY
131NOESY
141RELAY-COSY

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Sample preparation

Sample conditionspH: 3.9 / Temperature: 288 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian VARIAN UNITY 600 / Manufacturer: Varian / Model: VARIAN UNITY 600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
SA/MDCLORE,NILGESrefinement
BIOSYM TECHNOLOGIESTECHNOLOGIESstructure solution
Felixstructure solution
Insight IIstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 60 / Conformers submitted total number: 23

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