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Open data
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Basic information
Entry | Database: PDB / ID: 1kvf | ||||||
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Title | EMP-18 Erythropoietin Receptor Agonist Peptide | ||||||
![]() | PROTEIN: EMP-18 Receptor Agonist | ||||||
![]() | DE NOVO PROTEIN / BETA HAIRPIN PEPTIDE | ||||||
Method | SOLUTION NMR / distance geometry, restrained molecular dynamics | ||||||
![]() | Skelton, N.J. / Russell, S. / de Sauvage, F. / Cochran, A.G. | ||||||
![]() | ![]() Title: Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library Authors: Skelton, N.J. / Russell, S. / de Sauvage, F. / Cochran, A.G. #1: ![]() Title: Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1 Authors: Johnson, D.L. / Farrell, F.X. / Barbone, F.P. / McMahon, F.J. / Tullai, J. / Hoey, K. / Livnah, O. / Wrighton, N.C. / Middleton, S.A. / Loughney, D.A. / Dower, W.J. / Mulcahy, L.S. / Wilson, ...Authors: Johnson, D.L. / Farrell, F.X. / Barbone, F.P. / McMahon, F.J. / Tullai, J. / Hoey, K. / Livnah, O. / Wrighton, N.C. / Middleton, S.A. / Loughney, D.A. / Dower, W.J. / Mulcahy, L.S. / Wilson, I.A. / Jolliffe, L.K. | ||||||
History |
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Remark 999 | SEQUENCE AN APPROPRIATE DATABASE MATCH WAS NOT AVAILABLE AT THE TIME OF PROCESSING. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 93.3 KB | Display | ![]() |
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PDB format | ![]() | 71.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 331.7 KB | Display | ![]() |
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Full document | ![]() | 380.4 KB | Display | |
Data in XML | ![]() | 6.2 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 1867.177 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. It is a novel sequence derived from phage-display selection. |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. The sample contains a mixture of cis and trans isomers about the Gly7-Pro8 peptide bond. Both sets of resonances were ...Text: This structure was determined using standard 2D homonuclear techniques. The sample contains a mixture of cis and trans isomers about the Gly7-Pro8 peptide bond. Both sets of resonances were assigned. The trans isoform is not well ordered in solution. The cis isoform is structured, especially within the disulfide cycle. Structures were calculated on the basis of restraints generated only from the cis isoform. |
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Sample preparation
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: distance geometry, restrained molecular dynamics / Software ordinal: 1 Details: The structures are based on 52 NOE distance restraints, 11 phi and 4 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. The mean backbone atom RMSD to the mean ...Details: The structures are based on 52 NOE distance restraints, 11 phi and 4 chi-1 dihedral angle restraints. No hydrogen bond restraints were employed. The mean backbone atom RMSD to the mean structure within the disulfide cycle is 0.43 +/- 0.12 Angstoms. | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 80 / Conformers submitted total number: 20 |