+Open data
-Basic information
Entry | Database: PDB / ID: 1lb7 | ||||||
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Title | IGF-F1-1, A PEPTIDE ANTAGONIST OF IGF-1 | ||||||
Components | IGF-1 ANTAGONIST F1-1 | ||||||
Keywords | DE NOVO PROTEIN / loop-helix / disulfide | ||||||
Method | SOLUTION NMR / distance geometry, molecular dynamics | ||||||
Authors | Deshayes, K. / Schaffer, M.L. / Skelton, N.J. / Nakamura, G.R. / Kadkhodayan, S. / Sidhu, S.S. | ||||||
Citation | Journal: Chem.Biol. / Year: 2002 Title: Rapid identification of small binding motifs with high-throughput phage display: discovery of peptidic antagonists of IGF-1 function. Authors: Deshayes, K. / Schaffer, M.L. / Skelton, N.J. / Nakamura, G.R. / Kadkhodayan, S. / Sidhu, S.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lb7.cif.gz | 91.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lb7.ent.gz | 70.2 KB | Display | PDB format |
PDBx/mmJSON format | 1lb7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lb7_validation.pdf.gz | 332.8 KB | Display | wwPDB validaton report |
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Full document | 1lb7_full_validation.pdf.gz | 391.8 KB | Display | |
Data in XML | 1lb7_validation.xml.gz | 5.9 KB | Display | |
Data in CIF | 1lb7_validation.cif.gz | 9.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lb/1lb7 ftp://data.pdbj.org/pub/pdb/validation_reports/lb/1lb7 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1879.216 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: De novo sequence derived from phage display library |
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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 to generate distance (ROESY) and dihederal angle (DQF-COSY, COSY-35)restraints. Additional dihedral angle restraints were ...Text: This structure was determined using standard 2D homonuclear techniques to generate distance (ROESY) and dihederal angle (DQF-COSY, COSY-35)restraints. Additional dihedral angle restraints were derived from chemical shift information using the program TALOS |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0 / pH: 5.1 / Pressure: atm / Temperature: 303 K | |||||||||
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 |
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-Processing
NMR software |
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Refinement | Method: distance geometry, molecular dynamics / Software ordinal: 1 Details: The structures are based on 91 distance restraints and 26 dihedral angle restraints. None of the final structures have violations > 0.07A or 1.0 degrees. The mean rmsd to the mean ...Details: The structures are based on 91 distance restraints and 26 dihedral angle restraints. None of the final structures have violations > 0.07A or 1.0 degrees. The mean rmsd to the mean coordinates for heavy atoms of residues Cys3 to Tyr15 is 0.31+/-0.06 A. | ||||||||||||||||
NMR representative | Selection criteria: closest to the average,fewest violations,lowest energy,minimized average structure | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 80 / Conformers submitted total number: 20 |