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- PDB-2o8z: Bound Structure of CRF1 Extracellular Domain Antagonist -

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Basic information

Entry
Database: PDB / ID: 2o8z
TitleBound Structure of CRF1 Extracellular Domain Antagonist
ComponentscCRF(30-41) Peptide
KeywordsNEUROPEPTIDE / HELICAL / CRF / PEPTIDE LIGAND / GPCR / ECD / EXTRACELLULAR DOMAIN
MethodSOLUTION NMR / Stochastic Energy Minimization with Experimental Restraints
AuthorsMesleh, M.F. / Shirley, W.A. / Heise, C.E. / Ling, N. / Maki, R.A. / Laura, R.P.
CitationJournal: J.Biol.Chem. / Year: 2007
Title: NMR structural characterization of a minimal peptide antagonist bound to the extracellular domain of the corticotropin-releasing factor1 receptor.
Authors: Mesleh, M.F. / Shirley, W.A. / Heise, C.E. / Ling, N. / Maki, R.A. / Laura, R.P.
History
DepositionDec 12, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 26, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / 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_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_dist_value / _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
Revision 1.4Dec 27, 2023Group: 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: cCRF(30-41) Peptide


Theoretical massNumber of molelcules
Total (without water)1,5101
Polymers1,5101
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)20 / 50structures with the lowest energy
RepresentativeModel #4closest to the average

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Components

#1: Protein/peptide cCRF(30-41) Peptide


Mass: 1509.838 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence can be naturally found in Homo sapiens (human)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D NOESY
NMR detailsText: This structure was determined using transferred NOE techniques

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Sample preparation

DetailsContents: 2 mM cCRF(30-41), 50 microM trx-ECD of CRF1, 50 mM NaAc-d3, pH=4.5, 0.01% NaN3, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 0 / pH: 4.5 / Pressure: ambient / Temperature: 310 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.5Brukercollection
XwinNMR3.5Brukerprocessing
MOEv2006.08ChemCompGroupstructure solution
MOEv2006.08ChemCompGrouprefinement
RefinementMethod: Stochastic Energy Minimization with Experimental Restraints
Software ordinal: 1
Details: Model: Structure from 134 NOE restraints, 89 Intra-Residual, 23 Sequential, 22 Long Range
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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