BMRB Entry 19033
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19033
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1
Deposition date: 2013-02-12 Original release date: 2013-03-21
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1" Not known ., .-..
Assembly members:
RAS_GAP_1, polymer, 62 residues, 7268.292 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RAS_GAP_1: GRRRVRAILPYTKVPDTDEI
SFLKGDMFIVHNELEDGWMW
VTNLRTDEQGLIVEDLVEEV
GR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 214 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 450 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SH3 domain of human RAS GAP 1 | 1 |
Entities:
Entity 1, SH3 domain of human RAS GAP 1 62 residues - 7268.292 Da.
| 1 | GLY | ARG | ARG | ARG | VAL | ARG | ALA | ILE | LEU | PRO | ||||
| 2 | TYR | THR | LYS | VAL | PRO | ASP | THR | ASP | GLU | ILE | ||||
| 3 | SER | PHE | LEU | LYS | GLY | ASP | MET | PHE | ILE | VAL | ||||
| 4 | HIS | ASN | GLU | LEU | GLU | ASP | GLY | TRP | MET | TRP | ||||
| 5 | VAL | THR | ASN | LEU | ARG | THR | ASP | GLU | GLN | GLY | ||||
| 6 | LEU | ILE | VAL | GLU | ASP | LEU | VAL | GLU | GLU | VAL | ||||
| 7 | GLY | ARG |
Samples:
sample_1: RAS_GAP_1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D-HACANH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D-CBCACONH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D-HACACONH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, G ntert P. - structure solution
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAD92343 BAE21614 BAG35610 BAG62024 BAG62030 |
| EMBL | CAA31122 CAH18488 CAH90505 |
| GB | AAA16319 AAA35865 AAA52517 AAH13637 AAH20761 |
| PRF | 1411306A 1615347A 1615347B |
| REF | NP_001125265 NP_002881 NP_037267 NP_072179 NP_663427 |
| SP | P09851 P20936 P50904 |
| TPG | DAA27162 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts