BMRB Entry 17280
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17280
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR Structure of BVU_3817 from , Northeast Structural Genomics Consortium Target BvR159
Deposition date: 2010-11-03 Original release date: 2010-11-15
Authors: Mills, J.; Eletsky, A.; Lee, H.; Wang, D.; Ciccosanti, C.; Hamilton, K.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, J.; Montelione, G.; Szyperski, T.
Citation: Mills, J.; Eletsky, A.; Lee, H.; Wang, D.; Ciccosanti, C.; Hamilton, K.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, J.; Montelione, G.; Szyperski, T.. "Northeast Structural Genomics Consortium Target BvR159" To be published ., .-..
Assembly members:
BvR159, polymer, 142 residues, 15895.376 Da.
Natural source: Common Name: Bacteroides vulgatus Taxonomy ID: 821 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides vulgatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BvR159: MLKTILSIAGKPGLYKLISQ
GKNMLIVETVDAAKKRVPAY
AHDKVISLADIAMYTDAEEV
PLSEVLEAVKKKENGAVASI
NYKKASADELHAYFAEVLPN
YDRDRVHNGDIKKLISWYNI
LVNNGITEFVEAPALEHHHH
HH
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 551 |
15N chemical shifts | 125 |
1H chemical shifts | 890 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BvR159 | 1 |
Entities:
Entity 1, BvR159 142 residues - 15895.376 Da.
1 | MET | LEU | LYS | THR | ILE | LEU | SER | ILE | ALA | GLY | ||||
2 | LYS | PRO | GLY | LEU | TYR | LYS | LEU | ILE | SER | GLN | ||||
3 | GLY | LYS | ASN | MET | LEU | ILE | VAL | GLU | THR | VAL | ||||
4 | ASP | ALA | ALA | LYS | LYS | ARG | VAL | PRO | ALA | TYR | ||||
5 | ALA | HIS | ASP | LYS | VAL | ILE | SER | LEU | ALA | ASP | ||||
6 | ILE | ALA | MET | TYR | THR | ASP | ALA | GLU | GLU | VAL | ||||
7 | PRO | LEU | SER | GLU | VAL | LEU | GLU | ALA | VAL | LYS | ||||
8 | LYS | LYS | GLU | ASN | GLY | ALA | VAL | ALA | SER | ILE | ||||
9 | ASN | TYR | LYS | LYS | ALA | SER | ALA | ASP | GLU | LEU | ||||
10 | HIS | ALA | TYR | PHE | ALA | GLU | VAL | LEU | PRO | ASN | ||||
11 | TYR | ASP | ARG | ASP | ARG | VAL | HIS | ASN | GLY | ASP | ||||
12 | ILE | LYS | LYS | LEU | ILE | SER | TRP | TYR | ASN | ILE | ||||
13 | LEU | VAL | ASN | ASN | GLY | ILE | THR | GLU | PHE | VAL | ||||
14 | GLU | ALA | PRO | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
15 | HIS | HIS |
Samples:
NC: BvR159, [U-98% 13C; U-98% 15N], 0.78 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; D2O 5%; H2O 95%
NC5: BvR159, [5% U-98% 13C; U-98% 15N], 0.66 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; D2O 5%; H2O 95%
NC5-RDC: BvR159, [5% U-98% 13C; U-98% 15N], 0.61 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; D2O 5%; H2O 95%; PAGE 7%
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
3D HNCO | NC | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
3D HNCACB | NC | isotropic | sample_conditions_1 |
3D (H)CCH-COSY | NC | isotropic | sample_conditions_1 |
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | NC5 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | NC5-RDC | anisotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, 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
CARA, Keller 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
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PROSA, Guntert - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
PDB | |
EMBL | CDF18897 CUO88664 CUQ05140 CUQ47765 |
GB | ABR41428 AII63846 AII69760 ALA75532 ALK85904 |
REF | WP_005841613 WP_007833211 WP_007844300 WP_008671167 WP_012055911 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts