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- PDB-1hzn: NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHO... -

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Basic information

Entry
Database: PDB / ID: 1hzn
TitleNMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR
ComponentsCHOLECYSTOKININ TYPE A RECEPTOR
KeywordsHORMONE/GROWTH FACTOR / HORMONE-GROWTH FACTOR complex
Function / homology
Function and homology information


cholecystokinin receptor activity / cholecystokinin signaling pathway / regulation of hormone secretion / forebrain development / peptide hormone binding / cellular response to hormone stimulus / axonogenesis / Peptide ligand-binding receptors / neuron migration / phospholipase C-activating G protein-coupled receptor signaling pathway ...cholecystokinin receptor activity / cholecystokinin signaling pathway / regulation of hormone secretion / forebrain development / peptide hormone binding / cellular response to hormone stimulus / axonogenesis / Peptide ligand-binding receptors / neuron migration / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / G protein-coupled receptor signaling pathway / nucleoplasm / membrane / plasma membrane / cytosol
Similarity search - Function
Cholecystokinin receptor type A / Cholecystokinin A receptor, N-terminal / Cholecystokinin A receptor, N-terminal domain superfamily / Cholecystokinin A receptor, N-terminal / Cholecystokinin receptor / 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
Cholecystokinin receptor type A
Similarity search - Component
MethodSOLUTION NMR / Metric matrix DG calculations, NOE-restrained MD simulations in a water, decane simulation cell
AuthorsGiragossian, C. / Mierke, D.F.
CitationJournal: Biochemistry / Year: 2001
Title: Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin A receptor.
Authors: Giragossian, C. / Mierke, D.F.
History
DepositionJan 25, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 25, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_spectrometer ...database_2 / pdbx_nmr_spectrometer / 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_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 20, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Assembly

Deposited unit
A: CHOLECYSTOKININ TYPE A RECEPTOR


Theoretical massNumber of molelcules
Total (without water)3,2551
Polymers3,2551
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 / 100structures with the least restraint violations
Representative

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Components

#1: Protein/peptide CHOLECYSTOKININ TYPE A RECEPTOR / CCK-A RECEPTOR


Mass: 3254.699 Da / Num. of mol.: 1 / Fragment: RESIDUES 329-357 / Source method: obtained synthetically
Details: The peptide was synthesized using Solid-phase synthesis
References: UniProt: P32238
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: NOESY,ROESY,COSY,TOCSY

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Sample preparation

DetailsContents: Peptides, DPC
Sample conditionspH: 4.5 / Pressure: 1 atm / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE4001
Bruker AVANCEBrukerAVANCE6002

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Processing

NMR software
NameDeveloperClassification
HOMEWRITTEN METRIC MATRIX DISTANCE GEOMETRYMIERKE, D.F.refinement
MOLECULAR DYNAMICS with GROMACSBERENDSEN, H.J.C.refinement
HOMEWRITTEN DGstructure solution
GROMACS-MDstructure solution
RefinementMethod: Metric matrix DG calculations, NOE-restrained MD simulations in a water, decane simulation cell
Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 1

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