+
Open data
-
Basic information
Entry | Database: PDB / ID: 2lhc | ||||||
---|---|---|---|---|---|---|---|
Title | Ga98 solution structure | ||||||
![]() | Ga98 | ||||||
![]() | DE NOVO PROTEIN | ||||||
Function / homology | Albumin-binding domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha![]() | ||||||
Biological species | artificial gene (others) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | He, Y. / Chen, Y. / Alexander, P. / Bryan, P. / Orban, J. | ||||||
![]() | ![]() Title: Mutational tipping points for switching protein folds and functions. Authors: He, Y. / Chen, Y. / Alexander, P.A. / Bryan, P.N. / Orban, J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 356.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 300.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 533.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 701.5 KB | Display | |
Data in XML | ![]() | 37.3 KB | Display | |
Data in CIF | ![]() | 48.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2lhdC ![]() 2lheC ![]() 2lhgC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 6355.346 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) artificial gene (others) / Gene: PGA98 / Production host: ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: 0.1-0.3 mM [U-100% 13C; U-100% 15N] Ga98, 100 mM potassium phosphate, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||
Sample conditions | Ionic strength: 100 / pH: 7.0 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 816 / NOE intraresidue total count: 507 / NOE long range total count: 66 / NOE medium range total count: 78 / NOE sequential total count: 165 | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 500 / Conformers submitted total number: 20 |