BMRB Entry 16810
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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/BMR16810
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Title: Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A
Deposition date: 2010-03-31 Original release date: 2010-04-28
Authors: Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A" To be published ., .-..
Assembly members:
PgR37A, polymer, 157 residues, 17546.934 Da.
Natural source: Common Name: Porphyromonas gingivalis Taxonomy ID: 837 Superkingdom: Bacteria Kingdom: not available Genus/species: Porphyromonas gingivalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PgR37A: MRVYKPEDVPNVQLADSTRL
VTDEAGLLSNAQEEVMNGRL
RAIRSSHAVEFAVVTLPSIG
DAPLEDFTLKLARQWGVGNE
KNNNGLLLVLVLDQRRVRFE
TGYGLEGYLPDGLLSRIIHD
RMIPHFRSGNYAEGLSEGVL
AVQQVLDGSLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 667 |
| 15N chemical shifts | 169 |
| 1H chemical shifts | 1101 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PgR37A | 1 |
Entities:
Entity 1, PgR37A 157 residues - 17546.934 Da.
| 1 | MET | ARG | VAL | TYR | LYS | PRO | GLU | ASP | VAL | PRO | ||||
| 2 | ASN | VAL | GLN | LEU | ALA | ASP | SER | THR | ARG | LEU | ||||
| 3 | VAL | THR | ASP | GLU | ALA | GLY | LEU | LEU | SER | ASN | ||||
| 4 | ALA | GLN | GLU | GLU | VAL | MET | ASN | GLY | ARG | LEU | ||||
| 5 | ARG | ALA | ILE | ARG | SER | SER | HIS | ALA | VAL | GLU | ||||
| 6 | PHE | ALA | VAL | VAL | THR | LEU | PRO | SER | ILE | GLY | ||||
| 7 | ASP | ALA | PRO | LEU | GLU | ASP | PHE | THR | LEU | LYS | ||||
| 8 | LEU | ALA | ARG | GLN | TRP | GLY | VAL | GLY | ASN | GLU | ||||
| 9 | LYS | ASN | ASN | ASN | GLY | LEU | LEU | LEU | VAL | LEU | ||||
| 10 | VAL | LEU | ASP | GLN | ARG | ARG | VAL | ARG | PHE | GLU | ||||
| 11 | THR | GLY | TYR | GLY | LEU | GLU | GLY | TYR | LEU | PRO | ||||
| 12 | ASP | GLY | LEU | LEU | SER | ARG | ILE | ILE | HIS | ASP | ||||
| 13 | ARG | MET | ILE | PRO | HIS | PHE | ARG | SER | GLY | ASN | ||||
| 14 | TYR | ALA | GLU | GLY | LEU | SER | GLU | GLY | VAL | LEU | ||||
| 15 | ALA | VAL | GLN | GLN | VAL | LEU | ASP | GLY | SER | LEU | ||||
| 16 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: PgR37A, [U-100% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%
NC5_sample: PgR37A, [U-5% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%
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 aliphatic | 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 HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aliphatic | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aromatic | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5_sample | isotropic | sample_conditions_1 |
| 2D long-range 1H-15N HSQC for histidine | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC_sample | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation
AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
TOPSPIN v2.1, Bruker Biospin - collection, processing
VNMRJ v2.1B, Varian - collection
PROSA v6.4, Guntert - processing
TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 900 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAG34119 BAK25626 GAP82223 |
| GB | AAQ65571 AIJ36374 AKV64744 ALA94086 ALJ26010 |
| REF | WP_005873820 WP_012458397 WP_013816169 WP_039417602 WP_043894154 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts