+Open data
-Basic information
Entry | Database: PDB / ID: 1rzs | ||||||
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Title | Solution structure of P22 Cro | ||||||
Components | Regulatory protein cro | ||||||
Keywords | TRANSCRIPTION / HELIX-TURN-HELIX / DNA-BINDING PROTEIN / STRUCTURAL EVOLUTION | ||||||
Function / homology | DNA-binding transcriptional regulator Cro / lambda repressor-like DNA-binding domains / 434 Repressor (Amino-terminal Domain) / Lambda repressor-like, DNA-binding domain superfamily / DNA binding / Orthogonal Bundle / Mainly Alpha / Regulatory protein cro Function and homology information | ||||||
Biological species | Enterobacteria phage P22 (virus) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Newlove, T. / Konieczka, J.H. / Cordes, M.H. | ||||||
Citation | Journal: STRUCTURE / Year: 2004 Title: Secondary structure switching in Cro protein evolution. Authors: Newlove, T. / Konieczka, J.H. / Cordes, M.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rzs.cif.gz | 393.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rzs.ent.gz | 330.2 KB | Display | PDB format |
PDBx/mmJSON format | 1rzs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rzs_validation.pdf.gz | 339.6 KB | Display | wwPDB validaton report |
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Full document | 1rzs_full_validation.pdf.gz | 466.7 KB | Display | |
Data in XML | 1rzs_validation.xml.gz | 21 KB | Display | |
Data in CIF | 1rzs_validation.cif.gz | 34.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rz/1rzs ftp://data.pdbj.org/pub/pdb/validation_reports/rz/1rzs | 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 | Mass: 6837.767 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage P22 (virus) / Genus: P22-like viruses / Gene: CRO / Plasmid: pET21b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: P09964 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: 30 structures were calculated using 916 NOE-derived distance restraints, 10 hydrogen bond distance restraints, 41 phi angle restraints and 5 chi1 angle restraints. 23 of 30 calculated ...Details: 30 structures were calculated using 916 NOE-derived distance restraints, 10 hydrogen bond distance restraints, 41 phi angle restraints and 5 chi1 angle restraints. 23 of 30 calculated structures were initially accepted based on no distance restraint violations greater than 0.4 angstroms and no angle restraint violations greater than 5 degrees. Of the 23, 2 were eliminated for having significantly higher energy than the others, leaving 21 structures in the final ensemble. The ordered region of the structure includes residues 1-57. Pairwise RMSDs for the ordered region were 0.53 A (backbone atoms) and 1.29 A (all heavy atoms). None of the backbone angles in the ordered region of any ensemble member fell outside the most favorable and additionally allowed regions of a Ramachandran plot. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: agreement with distance and angle restraints; two structures were also eliminated due to high energy Conformers calculated total number: 30 / Conformers submitted total number: 21 |