+Open data
-Basic information
Entry | Database: PDB / ID: 2rlt | ||||||
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Title | phosphorylated CPI-17 (22-120) | ||||||
Components | Protein phosphatase 1 regulatory subunit 14A | ||||||
Keywords | HYDROLASE / phosphorylation / PP1 inhibitor / Cytoplasm / Protein phosphatase inhibitor | ||||||
Function / homology | Function and homology information RHO GTPases activate PKNs / protein serine/threonine phosphatase inhibitor activity / cytoplasm Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | SOLUTION NMR | ||||||
Model type details | minimized average | ||||||
Authors | Eto, M. | ||||||
Citation | Journal: Structure / Year: 2007 Title: Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor. Authors: Eto, M. / Kitazawa, T. / Matsuzawa, F. / Aikawa, S. / Kirkbride, J.A. / Isozumi, N. / Nishimura, Y. / Brautigan, D.L. / Ohki, S.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rlt.cif.gz | 42.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rlt.ent.gz | 34.8 KB | Display | PDB format |
PDBx/mmJSON format | 2rlt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rlt_validation.pdf.gz | 255.9 KB | Display | wwPDB validaton report |
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Full document | 2rlt_full_validation.pdf.gz | 255.6 KB | Display | |
Data in XML | 2rlt_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 2rlt_validation.cif.gz | 11 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/2rlt ftp://data.pdbj.org/pub/pdb/validation_reports/rl/2rlt | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11626.057 Da / Num. of mol.: 1 / Fragment: residues 22-120 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: CPI17 / Production host: Escherichia coli (E. coli) References: UniProt: O18734, Hydrolases; Acting on ester bonds |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM [U-100% 15N] H2O, 1 mM [U-100% 13C; U-100% 15N] H2O, 1 mM [U-100% 13C; U-100% 15N] D2O, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | pH: 6.7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Software ordinal: 1 / Details: DGSA-distance geometry simulated annealing | |||||||||
NMR representative | Selection criteria: minimized average structure | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 1 / Representative conformer: 20 |