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- PDB-1dep: MEMBRANE PROTEIN, NMR, 1 STRUCTURE -

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Basic information

Entry
Database: PDB / ID: 1dep
TitleMEMBRANE PROTEIN, NMR, 1 STRUCTURE
ComponentsT345-359
KeywordsMEMBRANE PROTEIN / BETA-ADRENOCEPTOR / MICELLE-BOUND PEPTIDE
Function / homology
Function and homology information


beta1-adrenergic receptor activity / positive regulation of heart contraction / regulation of circadian sleep/wake cycle, sleep / adenylate cyclase-activating adrenergic receptor signaling pathway / early endosome / identical protein binding / membrane / plasma membrane
Similarity search - Function
Beta 1 adrenoceptor / Adrenoceptor family / Serpentine type 7TM GPCR chemoreceptor Srsx / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family)
Similarity search - Domain/homology
Beta-1 adrenergic receptor
Similarity search - Component
Biological speciesMeleagris gallopavo (turkey)
MethodSOLUTION NMR
AuthorsJung, H. / Schnackerz, K.D.
Citation
Journal: FEBS Lett. / Year: 1995
Title: NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.
Authors: Jung, H. / Windhaber, R. / Palm, D. / Schnackerz, K.D.
#1: Journal: Eur.J.Biochem. / Year: 1991
Title: Multisite Contacts Involved in Coupling of the Beta-Adrenergic Receptor with the Stimulatory Guanine-Nucleotide-Binding Regulatory Protein. Structural and Functional Studies by Beta-Receptor- ...Title: Multisite Contacts Involved in Coupling of the Beta-Adrenergic Receptor with the Stimulatory Guanine-Nucleotide-Binding Regulatory Protein. Structural and Functional Studies by Beta-Receptor-Site-Specific Synthetic Peptides
Authors: Munch, G. / Dees, C. / Hekman, M. / Palm, D.
History
DepositionAug 23, 1995Processing site: BNL
Revision 1.0Oct 14, 1996Provider: 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 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: T345-359


Theoretical massNumber of molelcules
Total (without water)1,8891
Polymers1,8891
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)1 / -
Representative

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Components

#1: Protein/peptide T345-359


Mass: 1889.294 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: THE PEPTIDE T345-359 REPRESENTS THE FOURTH INTRACELLULAR LOOP OF THE BETA-ADRENOCEPTOR FROM TURKEY
Source: (gene. exp.) Meleagris gallopavo (turkey) / References: UniProt: P07700

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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: EREF / Developer: JACK,LEVITT / Classification: refinement
NMR ensembleConformers submitted total number: 1

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