BMRB Entry 18477
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18477
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Title: NMR dynamics in the C-terminal globular domain of oligosaccharyltransferase PubMed: 23177926
Deposition date: 2012-05-23 Original release date: 2012-11-26
Authors: Nyirenda, James; Matsumoto, Shunsuke; Takashi, Saitoh; Kohda, Daisuke
Citation: Nyirenda, James; Matsumoto, Shunsuke; Saitoh, Takashi; Maita, Nobuo; Noda, Nobuo; Inagaki, Fuyuhiko; Kohda, Daisuke. "Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance." Structure 21, 32-41 (2013).
Assembly members:
AfAglB-S2, polymer, 180 residues, Formula weight is not available
Natural source: Common Name: euryarchaeotes Taxonomy ID: 2234 Superkingdom: Archae Kingdom: not available Genus/species: Archaeoglobus fulgidus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET47b+
Entity Sequences (FASTA):
AfAglB-S2: MAHHHHHHSAALEVLFQGPE
MTMDWKEALNWMKENLEAQD
YLKAYEKPDYAVLSWWDYGN
WILYVAKKAVVCNNFQAGAD
DAAKFFTAQSEEEAMKIVEK
RKVRYVVTVEELTVKPETNK
TKFIPIMQIAGYSPEYMKNK
EIIDFFNKTMLYKLHVENAT
NLTHFRLLKNFGTVKIFEVK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
Data type | Count |
15N chemical shifts | 151 |
1H chemical shifts | 151 |
heteronuclear NOE values | 264 |
order parameters | 130 |
T1 relaxation values | 264 |
T2 relaxation values | 264 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | AfAglB-S2 | 1 |
Entities:
Entity 1, AfAglB-S2 180 residues - Formula weight is not available
Residues 1-19 are plasmid derived and part of the sequence in the assigned residues is labeled 10-18 from Alanine number 10 and the target sequence starts from 433.
1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | SER | ALA | |
2 | ALA | LEU | GLU | VAL | LEU | PHE | GLN | GLY | PRO | GLU | |
3 | MET | THR | MET | ASP | TRP | LYS | GLU | ALA | LEU | ASN | |
4 | TRP | MET | LYS | GLU | ASN | LEU | GLU | ALA | GLN | ASP | |
5 | TYR | LEU | LYS | ALA | TYR | GLU | LYS | PRO | ASP | TYR | |
6 | ALA | VAL | LEU | SER | TRP | TRP | ASP | TYR | GLY | ASN | |
7 | TRP | ILE | LEU | TYR | VAL | ALA | LYS | LYS | ALA | VAL | |
8 | VAL | CYS | ASN | ASN | PHE | GLN | ALA | GLY | ALA | ASP | |
9 | ASP | ALA | ALA | LYS | PHE | PHE | THR | ALA | GLN | SER | |
10 | GLU | GLU | GLU | ALA | MET | LYS | ILE | VAL | GLU | LYS | |
11 | ARG | LYS | VAL | ARG | TYR | VAL | VAL | THR | VAL | GLU | |
12 | GLU | LEU | THR | VAL | LYS | PRO | GLU | THR | ASN | LYS | |
13 | THR | LYS | PHE | ILE | PRO | ILE | MET | GLN | ILE | ALA | |
14 | GLY | TYR | SER | PRO | GLU | TYR | MET | LYS | ASN | LYS | |
15 | GLU | ILE | ILE | ASP | PHE | PHE | ASN | LYS | THR | MET | |
16 | LEU | TYR | LYS | LEU | HIS | VAL | GLU | ASN | ALA | THR | |
17 | ASN | LEU | THR | HIS | PHE | ARG | LEU | LEU | LYS | ASN | |
18 | PHE | GLY | THR | VAL | LYS | ILE | PHE | GLU | VAL | LYS |
Samples:
sample_1: AfAglB-S2, [U-99% 13C; U-99% 15N], 1.0 mM; AfAglB-S2, [U-99% 15N], 1.0 mM; H2O 90%; D2O 10%
Sample_2: AfAglB-S2, [U-99% 15N], 0.5-1.0 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
sample_conditions_2: ionic strength: 5 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
1H-15N heteronuclear noe | Sample_2 | isotropic | sample_conditions_2 |
1H-15N heteronuclear noe | Sample_2 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC | Sample_2 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC | Sample_2 | isotropic | sample_conditions_2 |
Software:
TOPSPIN v2, Bruker Biospin - collection
NMRPipe, Delaglio, Zhengrong and Bax - processing
SPARKY, Goddard - chemical shift assignment
ModelFree v4.16, Palmer - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts