BMRB Entry 15386
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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/BMR15386
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Title: Solution NMR structure of PefI protein from Salmonella typhimurium. Northeast Structural Genomics target StR82. PubMed: 20979070
Deposition date: 2007-07-17 Original release date: 2007-08-13
Authors: Aramini, James; Rossi, Paolo; Wang, Huang; Nwosu, Chioma; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Aramini, James; Rossi, Paolo; Cort, John; Ma, Li-Chung; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI from Salmonella enterica serovar Typhimurium." Proteins 79, 335-339 (2011).
Assembly members:
Str82, polymer, 77 residues, 8689.014 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):
Str82: MSESIVTKIISIVQERQNMD
DGAPVKTRDIADAAGLSIYQ
VRLYLEQLHDVGVLEKVNAG
KGVPGLWRLLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 317 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | str82 | 1 |
Entities:
Entity 1, str82 77 residues - 8689.014 Da.
C-terminal EHHHHHH tag starting at residue 71.
| 1 | MET | SER | GLU | SER | ILE | VAL | THR | LYS | ILE | ILE | ||||
| 2 | SER | ILE | VAL | GLN | GLU | ARG | GLN | ASN | MET | ASP | ||||
| 3 | ASP | GLY | ALA | PRO | VAL | LYS | THR | ARG | ASP | ILE | ||||
| 4 | ALA | ASP | ALA | ALA | GLY | LEU | SER | ILE | TYR | GLN | ||||
| 5 | VAL | ARG | LEU | TYR | LEU | GLU | GLN | LEU | HIS | ASP | ||||
| 6 | VAL | GLY | VAL | LEU | GLU | LYS | VAL | ASN | ALA | GLY | ||||
| 7 | LYS | GLY | VAL | PRO | GLY | LEU | TRP | ARG | LEU | LEU | ||||
| 8 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Str82, [U-100% 13C; U-100% 15N], 0.72 mM; ammonium acetate 20 mM; sodium chloride 450 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_2: Str82, [U-5% 13C; U-100% 15N], 0.46 mM; ammonium acetate 20 mM; sodium chloride 450 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 450 mM; pH: 5.5; 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 (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous CN-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC stereospecific Leu/Val methyl | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
PDBStat v5.0, Tejero and Montelione - PDB analysis
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - structure validation
MolProbity, Richardson - structure validation
Molmol v2K-2, Koradi, Billeter and Wuthrich - structure visualization
SPARKY v3.110, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAJ39680 |
| EMBL | CAQ51408 CBA11337 CCF76797 CCW77296 CDM74116 |
| GB | AAC36964 AAL23517 ACY86448 ADX20475 AEF10470 |
| REF | NP_490505 WP_000004313 WP_050195597 YP_003264374 YP_008997526 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts