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- PDB-1bku: EFFECTS OF GLYCOSYLATION ON THE STRUCTURE AND DYNAMICS OF EEL CAL... -

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Basic information

Entry
Database: PDB / ID: 1bku
TitleEFFECTS OF GLYCOSYLATION ON THE STRUCTURE AND DYNAMICS OF EEL CALCITONIN, NMR, 10 STRUCTURES
ComponentsCALCITONIN
KeywordsHORMONE / CALCIUM-REGULATING HORMONE
Function / homology
Function and homology information


hormone activity / extracellular region
Similarity search - Function
Calcitonin / Calcitonin peptide-like / Calcitonin, conserved site / Calcitonin / CGRP / IAPP family signature. / calcitonin / Calcitonin/adrenomedullin / Calcitonin / CGRP / IAPP family
Similarity search - Domain/homology
Biological speciesAnguilla japonica (Japanese eel)
MethodSOLUTION NMR / distance geometry
AuthorsHashimoto, Y. / Nishikido, J. / Toma, K. / Yamamoto, K. / Haneda, K. / Inazu, T. / Valentine, K. / Opella, S.J.
CitationJournal: Biochemistry / Year: 1999
Title: Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy.
Authors: Hashimoto, Y. / Toma, K. / Nishikido, J. / Yamamoto, K. / Haneda, K. / Inazu, T. / Valentine, K.G. / Opella, S.J.
History
DepositionJul 13, 1998Processing site: BNL
Revision 1.0Jan 13, 1999Provider: 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: 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_conn / struct_site
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_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CALCITONIN


Theoretical massNumber of molelcules
Total (without water)3,4201
Polymers3,4201
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 20LEATEST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide CALCITONIN /


Mass: 3419.906 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Anguilla japonica (Japanese eel) / References: UniProt: P01262

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TWO DIMENSIONAL NMR SPECTROSCOPY.

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Sample preparation

Sample conditionspH: 4.0 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX750 / Manufacturer: Bruker / Model: DMX750 / Field strength: 750 MHz

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Processing

NMR software
NameDeveloperClassification
DGIIHAVELrefinement
Felixstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEATEST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 10

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