[English] 日本語
![](img/lk-miru.gif)
- PDB-6nm1: The crystal structure of the Staphylococcus aureus Fatty acid Kin... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6nm1 | ||||||
---|---|---|---|---|---|---|---|
Title | The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein A158L mutant to 2.33 Angstrom resolution exhibits a conformation change compared to the wild type form | ||||||
![]() | Fatty acid Kinase (Fak) B1 protein | ||||||
![]() | TRANSFERASE / Staphylococcus aureus / FakB1 / mutant / conformation change | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cuypers, M.G. / Gullett, J.M. / Subramanian, C. / Ericson, M. / White, S.W. / Rock, C.O. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Identification of structural transitions in bacterial fatty acid binding proteins that permit ligand entry and exit at membranes. Authors: Gullett, J.M. / Cuypers, M.G. / Grace, C.R. / Pant, S. / Subramanian, C. / Tajkhorshid, E. / Rock, C.O. / White, S.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 128.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 98.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 463.1 KB | Display | |
Data in XML | ![]() | 24.1 KB | Display | |
Data in CIF | ![]() | 32.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6mh9SC ![]() 7sclC ![]() 7sg3C S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 32143.584 Da / Num. of mol.: 2 / Mutation: A158L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: BTN44_08795, CV021_09110, EP54_02745, EQ90_03735, ERS072840_01626, HMPREF3211_01094, NCTC10654_00855, NCTC11940_00723, NCTC13131_00828, NCTC13196_00435, NCTC13812_00781, NCTC6133_00899, ...Gene: BTN44_08795, CV021_09110, EP54_02745, EQ90_03735, ERS072840_01626, HMPREF3211_01094, NCTC10654_00855, NCTC11940_00723, NCTC13131_00828, NCTC13196_00435, NCTC13812_00781, NCTC6133_00899, NCTC7878_03402, NCTC9944_00829, SAMEA1469870_00860, SAMEA1531701_00562 Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.71 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: PH 6.5 0.1M MES/IMIDAZOLE, 12.5%, PEG1000, 12.5% PEG3350, 12.5% MPD, 0.03M NANO3, 0.03M NA2HPO4, 0.03M (NH4)2 SO4 Temp details: controlled temp room |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Feb 26, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.33→83.74 Å / Num. obs: 23124 / % possible obs: 98.2 % / Redundancy: 3.9 % / Biso Wilson estimate: 38 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.086 / Rpim(I) all: 0.051 / Rrim(I) all: 0.1 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 2.33→2.41 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.813 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 2250 / CC1/2: 0.748 / Rpim(I) all: 0.475 / Rrim(I) all: 0.942 / % possible all: 97.7 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 6MH9 Resolution: 2.33→31.709 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 36.52 / Details: high disorder for residues B178-B185
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.33→31.709 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|