[English] 日本語
![](img/lk-miru.gif)
- PDB-4cwe: Structural studies of rolling circle replication initiation prote... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4cwe | ||||||
---|---|---|---|---|---|---|---|
Title | Structural studies of rolling circle replication initiation protein from Staphylococcus aureus | ||||||
![]() | REPLICATION INITIATION PROTEIN, REPLICATION INITIATION PROTEIN | ||||||
![]() | ISOMERASE / ANTIBIOTIC RESISTANCE / PCRA HELICASE / DNA RELAXASE / CHIMERA | ||||||
Function / homology | Replication initiation factor / Replication initiation factor / DNA topoisomerase activity / DNA replication initiation / DNA replication / DNA binding / Replication initiation protein / Replication initiation protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Carr, S.B. / Phillips, S.E.V. / Thomas, C.D. | ||||||
![]() | ![]() Title: Structures of Replication Initiation Proteins from Staphylococcal Antibiotic Resistance Plasmids Reveal Protein Asymmetry and Flexibility are Necessary for Replication. Authors: Carr, S.B. / Phillips, S.E. / Thomas, C.D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 124.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 99.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 445.2 KB | Display | |
Data in XML | ![]() | 21.3 KB | Display | |
Data in CIF | ![]() | 28.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cijSC ![]() 4cwcC C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 34236.105 Da / Num. of mol.: 2 Fragment: REPLICATION INITIATION PROTEIN RESIDUES 32-216, REPLICATION INITIATION PROTEIN RESIDUES 220-314 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P03065, UniProt: P19529, DNA topoisomerase Sequence details | PROTEIN WAS CONSTRUCTED BY FUSING THE N-TERMINAL DOMAIN OF REPD - BASES 1295-1849 FROM PLASMID ...PROTEIN WAS CONSTRUCTE | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.8 % / Description: NONE |
---|---|
Crystal grow | pH: 5.5 / Details: 0.1 M SODIUM CITRATE PH 5.5, 2.5 M 1,6-HEXANEDIOL |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||
Detector | Type: ADSC Q4 / Detector: CCD / Date: Jun 7, 2002 / Details: MIRRORS | |||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 | |||||||||||||||
Reflection twin |
| |||||||||||||||
Reflection | Resolution: 3→39.7 Å / Num. obs: 15902 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 10.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 23.7 | |||||||||||||||
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 2.3 / % possible all: 100 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4CIJ Resolution: 3→39.66 Å / Cor.coef. Fo:Fc: 0.891 / Cor.coef. Fo:Fc free: 0.844 / SU B: 19.145 / SU ML: 0.376 / Cross valid method: THROUGHOUT / ESU R Free: 0.106 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 82.066 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→39.66 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|