BMRB Entry 6940
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6940
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Title: NMR assignment of the 2H, 13C, 15N labeled amino-terminal domain of apo-pantothenate synthetase from E.coli. PubMed: 16705359
Deposition date: 2006-01-16 Original release date: 2006-06-26
Authors: Chakrabarti, Kalyan Sundar; Sarma, Siddhartha
Citation: Chakrabarti, Kalyan Sundar; Sarma, Siddhartha. "NMR Assignment of 2H, 13C and 15N Labeled Amino-Terminal Domain of Apo-Pantothenate Synthetase from E. coli" J. Biomol. NMR 36, 38-38 (2006).
Assembly members:
panc, polymer, 176 residues, 19830 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
panc: MLIIETLPLLRQQIRRLRME
GKRVALVPTMGNLHDGHMKL
VDEAKARADVVAVSIFVNPM
QFDRPEDLARYPRTLQEDCE
KLNKRKVDLVFAPSVKEIYP
NGTETHTYVDVPGLSTMLEG
ASRPGHFRGVSTIVSKLFNL
VQPDIACFGEKDFQQLALIR
KMVADMGFDIEIVGVP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 470 |
15N chemical shifts | 152 |
1H chemical shifts | 152 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | amino-terminal pantothenate synthetase, chain 1 | 1 |
2 | amino-terminal pantothenate synthetase, chain 2 | 1 |
Entities:
Entity 1, amino-terminal pantothenate synthetase, chain 1 176 residues - 19830 Da.
1 | MET | LEU | ILE | ILE | GLU | THR | LEU | PRO | LEU | LEU | ||||
2 | ARG | GLN | GLN | ILE | ARG | ARG | LEU | ARG | MET | GLU | ||||
3 | GLY | LYS | ARG | VAL | ALA | LEU | VAL | PRO | THR | MET | ||||
4 | GLY | ASN | LEU | HIS | ASP | GLY | HIS | MET | LYS | LEU | ||||
5 | VAL | ASP | GLU | ALA | LYS | ALA | ARG | ALA | ASP | VAL | ||||
6 | VAL | ALA | VAL | SER | ILE | PHE | VAL | ASN | PRO | MET | ||||
7 | GLN | PHE | ASP | ARG | PRO | GLU | ASP | LEU | ALA | ARG | ||||
8 | TYR | PRO | ARG | THR | LEU | GLN | GLU | ASP | CYS | GLU | ||||
9 | LYS | LEU | ASN | LYS | ARG | LYS | VAL | ASP | LEU | VAL | ||||
10 | PHE | ALA | PRO | SER | VAL | LYS | GLU | ILE | TYR | PRO | ||||
11 | ASN | GLY | THR | GLU | THR | HIS | THR | TYR | VAL | ASP | ||||
12 | VAL | PRO | GLY | LEU | SER | THR | MET | LEU | GLU | GLY | ||||
13 | ALA | SER | ARG | PRO | GLY | HIS | PHE | ARG | GLY | VAL | ||||
14 | SER | THR | ILE | VAL | SER | LYS | LEU | PHE | ASN | LEU | ||||
15 | VAL | GLN | PRO | ASP | ILE | ALA | CYS | PHE | GLY | GLU | ||||
16 | LYS | ASP | PHE | GLN | GLN | LEU | ALA | LEU | ILE | ARG | ||||
17 | LYS | MET | VAL | ALA | ASP | MET | GLY | PHE | ASP | ILE | ||||
18 | GLU | ILE | VAL | GLY | VAL | PRO |
Samples:
sample_1: panc, [U-90% 2H; U->98% 13C; U->98% 15N], 0.6 ± 0.05 mM; K2HPO4/KH2PO4 buffer 10 mM; NaCl 10 mM; DTT (Dithiothreitol) 1 mM
conditions_1: ionic strength: 10 mM; pH: 6.8; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
TROSY_1H15N_HSQC | sample_1 | not available | conditions_1 |
TROSY_HNCA | sample_1 | not available | conditions_1 |
TROSY_HN(CO)CA | sample_1 | not available | conditions_1 |
TROSY_HNCACB | sample_1 | not available | conditions_1 |
TROSY_HN(CO)CACB | sample_1 | not available | conditions_1 |
TROSY-HNCO | sample_1 | not available | conditions_1 |
3D_NOE_HSQC | sample_1 | not available | conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
PDB | |
DBJ | BAB33560 BAE76042 BAG75657 BAI23496 BAI29011 |
EMBL | CAP74704 CAQ30648 CAQ87737 CAQ97020 CAR01508 |
GB | AAA24272 AAC73244 AAG54437 AAN41793 AAN78658 |
REF | NP_285829 NP_308164 NP_414675 NP_706086 NP_752114 |
SP | A1A7H9 A7ZHM3 A7ZW82 B1IQK7 B1LGT5 |
AlphaFold | A7ZW82 A1A7H9 A7ZHM3 B1IQK7 B1LGT5 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts