BMRB Entry 17038
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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/BMR17038
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Title: Solution NMR Structure of protein STY4237 (residues 36-120) from Salmonella enterica, Northeast Structural Genomics Consortium Target SlR115
Deposition date: 2010-06-30 Original release date: 2010-08-24
Authors: Cort, John; Lee, D.; Ciccosanti, C.; Janjua, H.; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Ramelot, T.; KENNEDY, M.
Citation: Cort, John; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; KENNEDY, M.. "Northeast Structural Genomics Consortium Target SlR115" To be published ., .-..
Assembly members:
SlR115, polymer, 97 residues, 11129.551 Da.
Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SlR115: MAPLQQKQVVVSNKREKPVN
DRRSRQQEVSPAGTSMRYEA
SFKPLNGGLEKTFRLQAQQY
HALTVGDQGTLSYKGTRFVG
FVSRTPDNELEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 390 |
15N chemical shifts | 96 |
1H chemical shifts | 582 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SlR115 | 1 |
Entities:
Entity 1, SlR115 97 residues - 11129.551 Da.
residue 2 of the structure corresponds to residue 36 of the sequence.
1 | MET | ALA | PRO | LEU | GLN | GLN | LYS | GLN | VAL | VAL | ||||
2 | VAL | SER | ASN | LYS | ARG | GLU | LYS | PRO | VAL | ASN | ||||
3 | ASP | ARG | ARG | SER | ARG | GLN | GLN | GLU | VAL | SER | ||||
4 | PRO | ALA | GLY | THR | SER | MET | ARG | TYR | GLU | ALA | ||||
5 | SER | PHE | LYS | PRO | LEU | ASN | GLY | GLY | LEU | GLU | ||||
6 | LYS | THR | PHE | ARG | LEU | GLN | ALA | GLN | GLN | TYR | ||||
7 | HIS | ALA | LEU | THR | VAL | GLY | ASP | GLN | GLY | THR | ||||
8 | LEU | SER | TYR | LYS | GLY | THR | ARG | PHE | VAL | GLY | ||||
9 | PHE | VAL | SER | ARG | THR | PRO | ASP | ASN | GLU | LEU | ||||
10 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SlR115, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; DTT 10 mM; H2O 95%; D2O 5%
sample_2: SlR115, [U-100% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; D2O 100%
sample_3: SlR115, [5% 13C; U-100% 15N], 1.1 mM; NaCl 100 mM; MES 20 mM; CaCl2 5 mM; NaN3 0.05%; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 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 |
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 |
3D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C aliph NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
4D 1H-13C-13C-1H HMQC NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen, rgeometry optimization, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinemen, rgeometry optimization, 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
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
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
PALES, PALES (Zweckstetter, Bax) - geometry optimization
REDCAT, Valafar, Prestegard - geometry optimization
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
PDB | |
DBJ | BAJ38571 BAP09540 |
EMBL | CAD08056 CAR34973 CAR39639 CAR61453 CBG26565 |
GB | AAL22434 AAO71419 AAV79236 AAX67409 ACF62437 |
PIR | AD0991 |
REF | NP_458347 NP_462475 WP_000042846 WP_000042847 WP_000042849 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts