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- PDB-1bzv: [D-ALAB26]-DES(B27-B30)-INSULIN-B26-AMIDE A SUPERPOTENT SINGLE-RE... -

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Basic information

Entry
Database: PDB / ID: 1bzv
Title[D-ALAB26]-DES(B27-B30)-INSULIN-B26-AMIDE A SUPERPOTENT SINGLE-REPLACEMENT INSULIN ANALOGUE, NMR, MINIMIZED AVERAGE STRUCTURE
Components(INSULIN) x 2
KeywordsHORMONE / INSULIN / SUPERPOTENCY
Function / homology
Function and homology information


hormone activity / glucose metabolic process / extracellular region
Similarity search - Function
Insulin / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily
Similarity search - Domain/homology
Insulin / Insulin / Insulin
Similarity search - Component
Biological speciessynthetic construct (others)
MethodSOLUTION NMR / distance geometry
AuthorsKurapkat, G. / Siedentopf, M. / Gattner, H.G. / Hagelstein, M. / Brandenburg, D. / Grotzinger, J. / Wollmer, A.
CitationJournal: Protein Sci. / Year: 1999
Title: The solution structure of a superpotent B-chain-shortened single-replacement insulin analogue.
Authors: Kurapkat, G. / Siedentop, M. / Gattner, H.G. / Hagelstein, M. / Brandenburg, D. / Grotzinger, J. / Wollmer, A.
History
DepositionNov 4, 1998Processing site: BNL
Revision 1.0May 18, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: INSULIN
B: INSULIN


Theoretical massNumber of molelcules
Total (without water)5,2972
Polymers5,2972
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)1 / 16LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide INSULIN /


Mass: 2383.698 Da / Num. of mol.: 1 / Mutation: CHAIN B, TYR(B26)D-ALA
Source method: isolated from a genetically manipulated source
References: UniProt: P01312, UniProt: P67974*PLUS
#2: Protein/peptide INSULIN /


Mass: 2913.355 Da / Num. of mol.: 1 / Mutation: CHAIN B, TYR(B26)D-ALA
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / References: UniProt: P30410

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: MEAN STRUCTURE.

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Sample preparation

Sample conditionspH: 2.0 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DISTANCE GEOMETRYGEOMETRYSCHEEKrefinement
NMRVIEWstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 16 / Conformers submitted total number: 1

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