BMRB Entry 18662
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18662
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Title: Solution NMR structure of SH3 domain of growth arrest-specific protein 7 (GAS7)(fragment 1-60)from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8574A
Deposition date: 2012-08-15 Original release date: 2012-10-09
Authors: Yang, Yunhuang; Ramelot, Theresa; Dan, Lee; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Yang, Yunhuang; Ramelot, Theresa; Dan, Lee; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of SH3 domain of growth arrest-specific protein 7 (GAS7) (fragment 1-60)from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8574A" To be published ., .-..
Assembly members:
SH3_domain_of_GAS7, polymer, 60 residues, 6718.633 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):
SH3_domain_of_GAS7: MSGARCRTLYPFSGERHGQG
LRFAAGELITLLQVPDGGWW
EGEKEDGLRGWFPASYVQLL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 266 |
| 15N chemical shifts | 64 |
| 1H chemical shifts | 413 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SH3_domain_of_GAS7 | 1 |
Entities:
Entity 1, SH3_domain_of_GAS7 60 residues - 6718.633 Da.
| 1 | MET | SER | GLY | ALA | ARG | CYS | ARG | THR | LEU | TYR | |
| 2 | PRO | PHE | SER | GLY | GLU | ARG | HIS | GLY | GLN | GLY | |
| 3 | LEU | ARG | PHE | ALA | ALA | GLY | GLU | LEU | ILE | THR | |
| 4 | LEU | LEU | GLN | VAL | PRO | ASP | GLY | GLY | TRP | TRP | |
| 5 | GLU | GLY | GLU | LYS | GLU | ASP | GLY | LEU | ARG | GLY | |
| 6 | TRP | PHE | PRO | ALA | SER | TYR | VAL | GLN | LEU | LEU |
Samples:
NC_sample: SH3_domain_of_GAS7, [U-100% 13C; U-100% 15N], 0.26 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; D2O 10 ± 0.005 %; DSS 50 ± 0.025 uM; H2O 90 ± 0.005 %
NC5_sample: SH3_domain_of_GAS7, [U-10% 13C; U-100% 15N], 0.45 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; D2O 10 ± 0.005 %; DSS 50 ± 0.025 uM; H2O 90 ± 0.005 %
NC_sample_in_D2O: SH3_domain_of_GAS7, [U-100% 13C; U-100% 15N], 0.26 ± 0.02 mM; NaN3 0.02 ± 0.001 %; DTT 10 ± 0.05 mM; CaCL2 5 ± 0.025 mM; NaCL 100 ± 0.5 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 ± 0.01 mM; DSS 50 ± 0.025 uM; D2O 100 ± 0.005 %
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | NC_sample | isotropic | sample_conditions_1 |
| 4D CC-NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | NC_sample | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HNHA | NC_sample | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC-arom | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-Histidine | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC - NC5 | NC5_sample | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Bruker Avance 850 MHz
- Varian INOVA 600 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAC21639 BAE89369 |
| GB | AAP92798 EAW90011 ELK03871 ELW53078 |
| REF | NP_958839 XP_002747958 XP_002827074 XP_003274725 XP_003315707 |
| SP | O60861 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts