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Basic information

Entry
Database: PDB / ID: 6ey3
Titlemf2
ComponentsCYS-ARG-PRO-LEU-TRP-THR-ALA-CYS-GLY
KeywordsPEPTIDE BINDING PROTEIN / STRUCTURE FROM CYANA 2.1
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry
AuthorsCalvanese, L. / Falcigno, L. / D'Auria, G. / Coppola, F.
CitationJournal: To Be Published
Title: mf2
Authors: Calvanese, L.
History
DepositionNov 10, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 17, 2018Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Database references / Derived calculations / Other / Category: database_2 / pdbx_database_status / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _struct_conn.pdbx_dist_value
Revision 1.2Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CYS-ARG-PRO-LEU-TRP-THR-ALA-CYS-GLY


Theoretical massNumber of molelcules
Total (without water)1,0071
Polymers1,0071
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area1100 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)40 / 100structures with the least restraint violations
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide CYS-ARG-PRO-LEU-TRP-THR-ALA-CYS-GLY


Mass: 1007.210 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111anisotropic12D 1H-1H TOCSY
121anisotropic12D 1H-1H NOESY
131anisotropic12D 1H-1H ROESY

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Sample preparation

DetailsType: solution / Contents: 1.4 mM 1H mf2, 90% H2O/10% D2O / Label: mf2 / Solvent system: 90% H2O/10% D2O
SampleConc.: 1.4 mM / Component: mf2 / Isotopic labeling: 1H
Sample conditionsIonic strength: NULL Not defined / Label: conditions / pH: 4.7 / Pressure: AMBIENT Pa / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
CARAKeller and Wuthrichchemical shift calculation
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
CARAKeller and Wuthrichchemical shift assignment
CARAKeller and Wuthrichpeak picking
RefinementMethod: distance geometry / Software ordinal: 2 / Details: 88 NOE-derived
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 40

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