[English] 日本語
![](img/lk-miru.gif)
- PDB-1bf9: N-TERMINAL EGF-LIKE DOMAIN FROM HUMAN FACTOR VII, NMR, 23 STRUCTURES -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1bf9 | ||||||
---|---|---|---|---|---|---|---|
Title | N-TERMINAL EGF-LIKE DOMAIN FROM HUMAN FACTOR VII, NMR, 23 STRUCTURES | ||||||
![]() | FACTOR VII | ||||||
![]() | BLOOD COAGULATION / EGF / HYDROLASE / SERINE PROTEASE | ||||||
Function / homology | ![]() coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / response to vitamin K / response to carbon dioxide ...coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / response to vitamin K / response to carbon dioxide / response to thyroxine / response to cholesterol / response to growth hormone / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of leukocyte chemotaxis / positive regulation of TOR signaling / positive regulation of blood coagulation / animal organ regeneration / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Removal of aminoterminal propeptides from gamma-carboxylated proteins / serine-type peptidase activity / BMAL1:CLOCK,NPAS2 activates circadian gene expression / protein processing / Golgi lumen / circadian rhythm / response to estrogen / blood coagulation / response to estradiol / collagen-containing extracellular matrix / vesicle / response to hypoxia / positive regulation of cell migration / endoplasmic reticulum lumen / serine-type endopeptidase activity / signaling receptor binding / calcium ion binding / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY EMBEDDING WITHOUT METRIZATION, RESTRAINED SIMULATED ANNEALING, SIMULATED ANNEALING REFINEMENT | ||||||
![]() | Muranyi, A. / Finn, B.E. / Gippert, G.P. / Forsen, S. / Stenflo, J. / Drakenberg, T. | ||||||
![]() | ![]() Title: Solution structure of the N-terminal EGF-like domain from human factor VII. Authors: Muranyi, A. / Finn, B.E. / Gippert, G.P. / Forsen, S. / Stenflo, J. / Drakenberg, T. #1: ![]() Title: The Crystal Structure of the Complex of Blood Coagulation Factor Viia with Soluble Tissue Factor Authors: Banner, D.W. / D'Arcy, A. / Chene, C. / Winkler, F.K. / Guha, A. / Konigsberg, W.H. / Nemerson, Y. / Kirchhofer, D. #2: ![]() Title: The Three-Dimensional Structure of the First Egf-Like Module of Human Factor Ix: Comparison with Egf and Tgf-Alpha Authors: Baron, M. / Norman, D.G. / Harvey, T.S. / Handford, P.A. / Mayhew, M. / Tse, A.G. / Brownlee, G.G. / Campbell, I.D. #3: ![]() Title: Three-Dimensional Structure of the Apo Form of the N-Terminal Egf-Like Module of Blood Coagulation Factor X as Determined by NMR Spectroscopy and Simulated Folding Authors: Ullner, M. / Selander, M. / Persson, E. / Stenflo, J. / Drakenberg, T. / Teleman, O. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 256.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 220.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 349.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 518 KB | Display | |
Data in XML | ![]() | 24.7 KB | Display | |
Data in CIF | ![]() | 37.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 4432.865 Da / Num. of mol.: 1 / Fragment: N-TERMINAL EGF-LIKE DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: H2O AND D2O |
---|---|
Sample conditions | Ionic strength: NO SALT ADDED / pH: 5.6 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| ||||||||||||
Refinement | Method: DISTANCE GEOMETRY EMBEDDING WITHOUT METRIZATION, RESTRAINED SIMULATED ANNEALING, SIMULATED ANNEALING REFINEMENT Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: NO DISTANCE RESTRAINT VIOLATED BY MORE THAN 0.2 ANGSTROM AND NO DIHEDRAL ANGLE RESTRAINTS VIOLATED BY MORE THAN 2 DEGREES Conformers calculated total number: 100 / Conformers submitted total number: 23 |