+Open data
-Basic information
Entry | Database: PDB / ID: 1imw | ||||||
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Title | Peptide Antagonist of IGFBP-1 | ||||||
Components | IGFBP-1 antagonist | ||||||
Keywords | ANTAGONIST / loop-turn-helix / DE NOVO PROTEIN | ||||||
Method | SOLUTION NMR / restrained molecular dynamics | ||||||
Authors | Lowman, H.B. / Chen, Y.M. / Skelton, N.J. / Mortensen, D.L. / Tomlinson, E.E. / Sadick, M.D. / Robinson, I.C. / Clark, R.G. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1. Authors: Skelton, N.J. / Chen, Y.M. / Dubree, N. / Quan, C. / Jackson, D.Y. / Cochran, A. / Zobel, K. / Deshayes, K. / Baca, M. / Pisabarro, M.T. / Lowman, H.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1imw.cif.gz | 85.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1imw.ent.gz | 66.3 KB | Display | PDB format |
PDBx/mmJSON format | 1imw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1imw_validation.pdf.gz | 338.1 KB | Display | wwPDB validaton report |
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Full document | 1imw_full_validation.pdf.gz | 420.2 KB | Display | |
Data in XML | 1imw_validation.xml.gz | 5.9 KB | Display | |
Data in CIF | 1imw_validation.cif.gz | 9.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/im/1imw ftp://data.pdbj.org/pub/pdb/validation_reports/im/1imw | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1771.094 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. |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: restrained molecular dynamics / Software ordinal: 1 Details: The structures were detemined on the basis of 149 NOE distance restraints and 15 dihedral angle restraints. The resulting ensemble had no restraint violations greater than 0.07 Angstroms or ...Details: The structures were detemined on the basis of 149 NOE distance restraints and 15 dihedral angle restraints. The resulting ensemble had no restraint violations greater than 0.07 Angstroms or 1.4 deg. The mean restraint violation energy was 0.17+/- 0.06 kcal/mol. | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |