BMRB Entry 19684
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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/BMR19684
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Title: Solution NMR Structure of SH3 Domain 1 of Rho GTPase-activating Protein 10 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target: HR9129A
Deposition date: 2013-12-13 Original release date: 2013-12-20
Authors: Xu, Xianzhong; Eletsky, Alexander; Pulavarti, Surya; Wang, Huang; O'Connell, Patrick; Janjua, Haleema; Xiao, Rong; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas
Citation: Xu, Xianzhong; Eletsky, Alexander; Pulavarti, Surya; Wang, Huang; O'Connell, Patrick; Janjua, Haleema; Xiao, Rong; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of SH3 Domain 1 of Rho GTPase-activating Protein 10 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target: HR9129A" To be published ., .-..
Assembly members:
HR9129A, polymer, 70 residues, 8044.164 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):
HR9129A: MGHHHHHHSHMIRSRKARAV
YPCEAEHSSELSFEIGAIFE
DVQTSREPGWLEGTLNGKRG
LIPQNYVKLL
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 270 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 437 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR9129A | 1 |
Entities:
Entity 1, HR9129A 70 residues - 8044.164 Da.
Residues 12-70 correspond to the residues 728-786 of the native protein. Residues 1-11 are the un-cleaved his-tag.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | |
| 2 | MET | ILE | ARG | SER | ARG | LYS | ALA | ARG | ALA | VAL | |
| 3 | TYR | PRO | CYS | GLU | ALA | GLU | HIS | SER | SER | GLU | |
| 4 | LEU | SER | PHE | GLU | ILE | GLY | ALA | ILE | PHE | GLU | |
| 5 | ASP | VAL | GLN | THR | SER | ARG | GLU | PRO | GLY | TRP | |
| 6 | LEU | GLU | GLY | THR | LEU | ASN | GLY | LYS | ARG | GLY | |
| 7 | LEU | ILE | PRO | GLN | ASN | TYR | VAL | LYS | LEU | LEU |
Samples:
sample_1: HR9129A, [U-99% 13C; U-98% 15N], 0.72 mM
sample_2: HR9129A, [U-99% 13C; U-98% 15N], 0.72 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D(H)CCH-TOCSY ali | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY ali | sample_1 | isotropic | sample_conditions_1 |
| GFT-43D (H)CCH-COSY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| gNfHSQC_His | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C ct-HSQC methyl(28ms) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC-methyl (42ms) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC-methyl (56ms) | sample_2 | isotropic | sample_conditions_1 |
| 2D J-modulation 1H-15N HSQC | sample_2 | Aligned in poly acrylamide | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
VNMRJ, Varian - collection
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya, Montelione, Guntert - processing, structure validation
CSI, David Wishart,Leigh Willard,Tim Jellard,Brian Sykes - data analysis
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| HUGO | ARHGAP10 |
| NCBI | 79658 |
| UNP | A1A4S6 |
| PDB | |
| DBJ | BAB14924 BAB61771 BAG65274 |
| EMBL | CAD39024 CAG33609 |
| GB | AAH11920 AAH47914 AAI06019 AAI09030 AAI09031 |
| REF | NP_001070298 NP_001102971 NP_078881 XP_002815242 XP_003258064 |
| SP | A1A4S6 Q08DP6 |
| TPG | DAA20889 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts