[English] 日本語
![](img/lk-miru.gif)
- PDB-1kco: Structure of e131 Zeta Peptide, a Potent Antagonist of the High-A... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1kco | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of e131 Zeta Peptide, a Potent Antagonist of the High-Affinity IgE Receptor | ||||||
![]() | e131 Zeta Peptide | ||||||
![]() | PROTEIN BINDING / disulfide-bonded / HELICAL / "zeta" structure | ||||||
Method | SOLUTION NMR / hybrid distance geometry, simulated annealing, then further refined by restrained molecular dynamics | ||||||
![]() | Nakamura, G.R. / Reynolds, M.E. / Chen, Y.M. / Starovasnik, M.A. / Lowman, H.B. | ||||||
![]() | ![]() Title: Stable "zeta" peptides that act as potent antagonists of the high-affinity IgE receptor. Authors: Nakamura, G.R. / Reynolds, M.E. / Chen, Y.M. / Starovasnik, M.A. / Lowman, H.B. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 112.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 93.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 331.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 394.8 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Data in CIF | ![]() | 12 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 2537.906 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Solid-phase peptide synthesis of a novel peptide based ON A NAIVE PHAGE-PEPTIDE LIBRARY THAT WAS SORTED FOR BINDING TO THE HIGH-AFFINITY IGE RECEPTOR |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||
NMR details | Text: This structure was determined using standard 2D homonuclear techniques. 3JHNHA WERE OBTAINED BY FITTING LORENTZIAN LINES TO THE ANTIPHASE DOUBLETS OF HN-HA PEAKS IN A 2QF-COSY SPECTRUM ...Text: This structure was determined using standard 2D homonuclear techniques. 3JHNHA WERE OBTAINED BY FITTING LORENTZIAN LINES TO THE ANTIPHASE DOUBLETS OF HN-HA PEAKS IN A 2QF-COSY SPECTRUM PROCESSED TO HIGH DIGITAL RESOLUTION IN F2. 3JHAHB WERE EXTRACTED FROM A COSY-35 SPECTRUM ACQUIRED IN D2O |
-
Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | pH: 6.0 / Pressure: ambient / Temperature: 308 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: hybrid distance geometry, simulated annealing, then further refined by restrained molecular dynamics Software ordinal: 1 Details: The structures are based on a total of 143 NOE-derived distance restraints and 24 dihedral angle restraints. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 20 |