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Yorodumi- PDB-1ctl: STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RI... -
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-Basic information
Entry | Database: PDB / ID: 1ctl | ||||||
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Title | STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP | ||||||
Components | AVIAN CYSTEINE RICH PROTEIN | ||||||
Keywords | METAL BINDING PROTEIN / LIM DOMAIN CONTAINING PROTEINS / METAL-BINDING PROTEIN | ||||||
Function / homology | Function and homology information muscle tissue development / actinin binding / structural constituent of muscle / sarcomere organization / cell leading edge / alpha-actinin binding / stress fiber / phosphoprotein binding / Z disc / focal adhesion ...muscle tissue development / actinin binding / structural constituent of muscle / sarcomere organization / cell leading edge / alpha-actinin binding / stress fiber / phosphoprotein binding / Z disc / focal adhesion / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Perez-Alvarado, G.C. / Miles, C. / Michelsen, J.W. / Louis, H.A. / Winge, D.R. / Beckerle, M.C. / Summers, M.F. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1994 Title: Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP. Authors: Perez-Alvarado, G.C. / Miles, C. / Michelsen, J.W. / Louis, H.A. / Winge, D.R. / Beckerle, M.C. / Summers, M.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ctl.cif.gz | 430.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ctl.ent.gz | 357.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ctl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ctl_validation.pdf.gz | 354.1 KB | Display | wwPDB validaton report |
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Full document | 1ctl_full_validation.pdf.gz | 486.4 KB | Display | |
Data in XML | 1ctl_validation.xml.gz | 30.7 KB | Display | |
Data in CIF | 1ctl_validation.cif.gz | 49 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ct/1ctl ftp://data.pdbj.org/pub/pdb/validation_reports/ct/1ctl | 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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Atom site foot note | 1: GLU 56 - ILE 57 MODEL 1 OMEGA = 216.87 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: LYS 23 - VAL 24 MODEL 2 OMEGA = 212.09 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: GLU 56 - ILE 57 MODEL 2 OMEGA = 217.75 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: GLU 56 - ILE 57 MODEL 3 OMEGA = 217.70 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: TYR 58 - CYS 59 MODEL 3 OMEGA = 210.32 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: GLU 56 - ILE 57 MODEL 4 OMEGA = 217.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: GLU 56 - ILE 57 MODEL 5 OMEGA = 217.12 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 8: GLU 56 - ILE 57 MODEL 6 OMEGA = 217.24 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 9: GLU 56 - ILE 57 MODEL 7 OMEGA = 217.78 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 10: GLU 22 - LYS 23 MODEL 8 OMEGA = 213.73 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 11: GLU 56 - ILE 57 MODEL 8 OMEGA = 216.95 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 12: GLU 56 - ILE 57 MODEL 9 OMEGA = 217.36 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 13: GLU 56 - ILE 57 MODEL 10 OMEGA = 217.20 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 14: LYS 23 - VAL 24 MODEL 11 OMEGA = 210.89 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 15: GLU 56 - ILE 57 MODEL 11 OMEGA = 216.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 16: TYR 58 - CYS 59 MODEL 11 OMEGA = 210.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 17: GLU 56 - ILE 57 MODEL 12 OMEGA = 217.10 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 18: GLU 56 - ILE 57 MODEL 13 OMEGA = 217.31 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 19: LYS 23 - VAL 24 MODEL 14 OMEGA = 210.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 20: GLU 56 - ILE 57 MODEL 14 OMEGA = 217.54 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 21: GLU 56 - ILE 57 MODEL 15 OMEGA = 217.11 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 22: TYR 58 - CYS 59 MODEL 15 OMEGA = 218.10 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 23: GLU 56 - ILE 57 MODEL 16 OMEGA = 217.53 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 24: LYS 23 - VAL 24 MODEL 17 OMEGA = 212.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 25: GLU 56 - ILE 57 MODEL 17 OMEGA = 216.97 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 26: GLU 56 - ILE 57 MODEL 18 OMEGA = 217.12 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 8839.138 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Organ: GIZZARD / Plasmid: PAED4-LIM2 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P67966 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other |
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-Processing
NMR software | Name: DSPACE / Developer: HARE RESEARCH INC. / Classification: refinement |
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NMR ensemble | Conformers submitted total number: 18 |