BMRB Entry 15351
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15351
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Title: Solution structure of first SH3 domain of adaptor Nck PubMed: 18269246
Deposition date: 2007-06-29 Original release date: 2008-02-29
Authors: Hake, Michael; Choowongkomon, Kiattawee; Carlin, Cathleen; Sonnichsen, Frank
Citation: Hake, Michael; Choowongkomon, Kiattawee; Kostenko, Olga; Carlin, Cathleen; Sonnichsen, Frank. "Specificity Determinants of a Novel Nck Interaction with the Juxtamembrane Domain of the Epidermal Growth Factor Receptor" Biochemistry 47, 3096-3108 (2008).
Assembly members:
Nck1-1, polymer, 63 residues, 7461.453 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Nck1-1: GSMAEEVVVVAKFDYVAQQE
QELDIKKNERLWLLDDSKSW
WRVRNSMNKTGFVPSNYVER
KNS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 441 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Nck1-1 SH3 | 1 |
Entities:
Entity 1, Nck1-1 SH3 63 residues - 7461.453 Da.
| 1 | GLY | SER | MET | ALA | GLU | GLU | VAL | VAL | VAL | VAL | ||||
| 2 | ALA | LYS | PHE | ASP | TYR | VAL | ALA | GLN | GLN | GLU | ||||
| 3 | GLN | GLU | LEU | ASP | ILE | LYS | LYS | ASN | GLU | ARG | ||||
| 4 | LEU | TRP | LEU | LEU | ASP | ASP | SER | LYS | SER | TRP | ||||
| 5 | TRP | ARG | VAL | ARG | ASN | SER | MET | ASN | LYS | THR | ||||
| 6 | GLY | PHE | VAL | PRO | SER | ASN | TYR | VAL | GLU | ARG | ||||
| 7 | LYS | ASN | SER |
Samples:
sample_1: Nck1-1, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.1; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRView v5.2.1, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - water refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG35571 BAG73433 BAK63238 |
| EMBL | CAA35599 |
| GB | AAD13752 AAH02015 AAH06403 AAI16110 AAI67009 |
| REF | NP_001069540 NP_001100321 NP_001131102 NP_001159671 NP_001233509 |
| SP | P16333 Q99M51 |
| TPG | DAA33097 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts