BMRB Entry 19210
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19210
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Title: The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins
Deposition date: 2013-05-01 Original release date: 2013-05-14
Authors: Chuang, Woei-Jer; Chang, Yao-Tsung; Shiu, Jia-Hau
Citation: Chuang, Woei-Jer; Chang, Yao-Tsung; Shiu, Jia-Hau; Chen, Chiu-Yueh; Chen, Yi-Chun. "The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins" Not known ., .-..
Assembly members:
rhodostomin, polymer, 76 residues, 7387.333 Da.
Natural source: Common Name: Malayan pit viper Taxonomy ID: 8717 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Calloselasma rhodostoma
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
rhodostomin: EFHHHHHHGKECDCSSPENP
CCDAATCKLRPGAQCGEGLC
CEQCKFSRAGKICRIARGDW
NDDRCTGQSADCPRYH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 381 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rhodostomin | 1 |
Entities:
Entity 1, rhodostomin 76 residues - 7387.333 Da.
| 1 | GLU | PHE | HIS | HIS | HIS | HIS | HIS | HIS | GLY | LYS | ||||
| 2 | GLU | CYS | ASP | CYS | SER | SER | PRO | GLU | ASN | PRO | ||||
| 3 | CYS | CYS | ASP | ALA | ALA | THR | CYS | LYS | LEU | ARG | ||||
| 4 | PRO | GLY | ALA | GLN | CYS | GLY | GLU | GLY | LEU | CYS | ||||
| 5 | CYS | GLU | GLN | CYS | LYS | PHE | SER | ARG | ALA | GLY | ||||
| 6 | LYS | ILE | CYS | ARG | ILE | ALA | ARG | GLY | ASP | TRP | ||||
| 7 | ASN | ASP | ASP | ARG | CYS | THR | GLY | GLN | SER | ALA | ||||
| 8 | ASP | CYS | PRO | ARG | TYR | HIS |
Samples:
sample_1: Rhodostomin P48A/M52W/P53N mutant 2 mM
sample_2: Rhodostomin P48A/M52W/P53N mutant 2 mM
sample_3: Rhodostomin P48A/M52W/P53N mutant, [U-15N], 2 mM
sample_4: Rhodostomin P48A/M52W/P53N mutant, [U-15N], 2 mM
sample_conditions_1: ionic strength: 0 M; pH: 6.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
Software:
xwinnmr v2.6, Bruker Biospin - collection
AURELIA v3.1.7, Neidig, Geyer, Gorler, Antz, Saffrich, Beneicke, Kalbitzer - data analysis
X-PLOR v3.185, Brunger - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts