BMRB Entry 16498
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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/BMR16498
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Title: Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A.
Deposition date: 2009-09-15 Original release date: 2009-10-16
Authors: Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of CLOLEP_01837 (fragment 61-160) from Clostridium leptum. Northeast Structural Genomics Consortium Target QlR8A." Not known ., .-..
Assembly members:
QlR8A, polymer, 108 residues, 13000 Da.
Natural source: Common Name: Clostridium leptum Taxonomy ID: 1535 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium leptum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
QlR8A: RDSFGDWAEKFLKSKEADGV
SVSQLNSYKNYCRNHLSPLY
MKSLSEILPADIQSIINETK
LAKNTLKAIRNTASQIFRLA
IENRAIDFNPADYVRIPKIA
LEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 475 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 746 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | QlR8A | 1 |
Entities:
Entity 1, QlR8A 108 residues - 13000 Da.
8 non-native residues at C-terminus (LEHHHHHH)
| 1 | ARG | ASP | SER | PHE | GLY | ASP | TRP | ALA | GLU | LYS | ||||
| 2 | PHE | LEU | LYS | SER | LYS | GLU | ALA | ASP | GLY | VAL | ||||
| 3 | SER | VAL | SER | GLN | LEU | ASN | SER | TYR | LYS | ASN | ||||
| 4 | TYR | CYS | ARG | ASN | HIS | LEU | SER | PRO | LEU | TYR | ||||
| 5 | MET | LYS | SER | LEU | SER | GLU | ILE | LEU | PRO | ALA | ||||
| 6 | ASP | ILE | GLN | SER | ILE | ILE | ASN | GLU | THR | LYS | ||||
| 7 | LEU | ALA | LYS | ASN | THR | LEU | LYS | ALA | ILE | ARG | ||||
| 8 | ASN | THR | ALA | SER | GLN | ILE | PHE | ARG | LEU | ALA | ||||
| 9 | ILE | GLU | ASN | ARG | ALA | ILE | ASP | PHE | ASN | PRO | ||||
| 10 | ALA | ASP | TYR | VAL | ARG | ILE | PRO | LYS | ILE | ALA | ||||
| 11 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; H2O 95%; D2O 5%
NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 200 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; D2O 100%
sample_conditions_1: ionic strength: 200 mM; 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 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliph | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 4D HCCH NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY arom | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC edHN2 | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC swN | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC arom ct | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC arom no ct | NC_sample | isotropic | sample_conditions_1 |
Software:
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1.4, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts