BMRB Entry 15584
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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/BMR15584
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Title: NMR STRUCTURE OF PUTATIVE-tRNA HYDROLASE DOMAIN FROM SALMONELLA TYPHIMURIUM: NORTH EAST STRUCTURAL GENOMICS CONSORTIUM TARGET STR220
Deposition date: 2007-12-07 Original release date: 2008-01-18
Authors: SINGARAPU, KIRAN KUMAR; WU, YIBING; SUKUMARAN, DINESH; ELETSKY, ALEX; ZERI, ANNA; WANG, DONGYAN; JANJUA, HALEEMA; OWENS, LEAH; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; G.V.T., SWAPNA; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS
Citation: SINGARAPU, KIRAN KUMAR; WU, YIBING; SUKUMARAN, DINESH; ELETSKY, ALEX; ZERI, ANNA; WANG, DONGYAN; JANJUA, HALEEMA; OWENS, LEAH; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; G.V.T., SWAPNA; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO; SZYPERSKI, THOMAS. "NMR STRUCTURE OF PUTATIVE-tRNA HYDROLASE DOMAIN FROM SALMONELLA TYPHIMURIUM: NORTH EAST STRUCTURAL GENOMICS CONSORTIUM TARGET STR220" . ., .-..
Assembly members:
STR220, polymer, 148 residues, 16700.322 Da.
Natural source: Common Name: Salmonella typhimurium Taxonomy ID: 602 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
STR220: MIAISRTVSIADNELEITAI
RAQGAGGQHVNKTSSAIHLR
FDIRASGLPEYYKQRLLTAS
HHLISDDGVIIIKAQEFRSQ
ELNREAAIARLVAVIKELTA
EQKSRRATRPTRASKERRLS
SKAQKSSVKALRGKVRRPLD
LEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 586 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 977 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | STR220 | 1 |
Entities:
Entity 1, STR220 148 residues - 16700.322 Da.
| 1 | MET | ILE | ALA | ILE | SER | ARG | THR | VAL | SER | ILE | ||||
| 2 | ALA | ASP | ASN | GLU | LEU | GLU | ILE | THR | ALA | ILE | ||||
| 3 | ARG | ALA | GLN | GLY | ALA | GLY | GLY | GLN | HIS | VAL | ||||
| 4 | ASN | LYS | THR | SER | SER | ALA | ILE | HIS | LEU | ARG | ||||
| 5 | PHE | ASP | ILE | ARG | ALA | SER | GLY | LEU | PRO | GLU | ||||
| 6 | TYR | TYR | LYS | GLN | ARG | LEU | LEU | THR | ALA | SER | ||||
| 7 | HIS | HIS | LEU | ILE | SER | ASP | ASP | GLY | VAL | ILE | ||||
| 8 | ILE | ILE | LYS | ALA | GLN | GLU | PHE | ARG | SER | GLN | ||||
| 9 | GLU | LEU | ASN | ARG | GLU | ALA | ALA | ILE | ALA | ARG | ||||
| 10 | LEU | VAL | ALA | VAL | ILE | LYS | GLU | LEU | THR | ALA | ||||
| 11 | GLU | GLN | LYS | SER | ARG | ARG | ALA | THR | ARG | PRO | ||||
| 12 | THR | ARG | ALA | SER | LYS | GLU | ARG | ARG | LEU | SER | ||||
| 13 | SER | LYS | ALA | GLN | LYS | SER | SER | VAL | LYS | ALA | ||||
| 14 | LEU | ARG | GLY | LYS | VAL | ARG | ARG | PRO | LEU | ASP | ||||
| 15 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.4 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 100 mM; 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 HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT CABCACONHN | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D SimNOESY | sample_1 | isotropic | sample_conditions_1 |
| 4,3D HABCABCONHN | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
Molmol, Koradi, Billeter and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - validation
TALOS, Cornilescu, Delaglio and Bax - data analysis
VNMRJ, Varian - collection
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAJ35184 BAP05946 |
| EMBL | CAD08699 CAR31835 CAR36151 CAR58353 CBG23262 |
| GB | AAL19204 AAO67971 AAV76276 AAX64146 ABX22610 |
| PIR | AC0532 |
| REF | NP_454848 NP_459245 WP_000560520 WP_000560521 WP_000560522 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts