BMRB Entry 16566
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16566
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Citation: Xu, Yimin; Lorieau, Justin; McDermott, Ann. "Triosephosphate Isomerase: (15)N and (13)C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy." J. Mol. Biol. 397, 233-248 (2010).
PubMed: 19854202
Assembly members:
WT_yeast_TIM_homodimer, polymer, 248 residues, Formula weight is not available
G3P, non-polymer, 172.074 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pKK223-3
Entity Sequences (FASTA):
WT_yeast_TIM_homodimer: MARTFFVGGNFKLNGSKQSI
KEIVERLNTASIPENVEVVI
CPPATYLDYSVSLVKKPQVT
VGAQNAYLKASGAFTGENSV
DQIKDVGAKWVILGHSERRS
YFHEDDKFIADKTKFALGQG
VGVILCIGETLEEKKAGKTL
DVVERQLNAVLEEVKDWTNV
VVAYEPVWAIGTGLAATPED
AQDIHASIRKFLASKLGDKA
ASELRILYGGSANGSNAVTF
KDKADVDGFLVGGASLKPEF
VDIINSRN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 296 |
| 15N chemical shifts | 20 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | WT TIM chain 1 | 1 |
| 2 | WT TIM chain 2 | 1 |
| 3 | G3P, 1 | 2 |
| 4 | G3P, 2 | 2 |
Entities:
Entity 1, WT TIM chain 1 248 residues - Formula weight is not available
| 1 | MET | ALA | ARG | THR | PHE | PHE | VAL | GLY | GLY | ASN | ||||
| 2 | PHE | LYS | LEU | ASN | GLY | SER | LYS | GLN | SER | ILE | ||||
| 3 | LYS | GLU | ILE | VAL | GLU | ARG | LEU | ASN | THR | ALA | ||||
| 4 | SER | ILE | PRO | GLU | ASN | VAL | GLU | VAL | VAL | ILE | ||||
| 5 | CYS | PRO | PRO | ALA | THR | TYR | LEU | ASP | TYR | SER | ||||
| 6 | VAL | SER | LEU | VAL | LYS | LYS | PRO | GLN | VAL | THR | ||||
| 7 | VAL | GLY | ALA | GLN | ASN | ALA | TYR | LEU | LYS | ALA | ||||
| 8 | SER | GLY | ALA | PHE | THR | GLY | GLU | ASN | SER | VAL | ||||
| 9 | ASP | GLN | ILE | LYS | ASP | VAL | GLY | ALA | LYS | TRP | ||||
| 10 | VAL | ILE | LEU | GLY | HIS | SER | GLU | ARG | ARG | SER | ||||
| 11 | TYR | PHE | HIS | GLU | ASP | ASP | LYS | PHE | ILE | ALA | ||||
| 12 | ASP | LYS | THR | LYS | PHE | ALA | LEU | GLY | GLN | GLY | ||||
| 13 | VAL | GLY | VAL | ILE | LEU | CYS | ILE | GLY | GLU | THR | ||||
| 14 | LEU | GLU | GLU | LYS | LYS | ALA | GLY | LYS | THR | LEU | ||||
| 15 | ASP | VAL | VAL | GLU | ARG | GLN | LEU | ASN | ALA | VAL | ||||
| 16 | LEU | GLU | GLU | VAL | LYS | ASP | TRP | THR | ASN | VAL | ||||
| 17 | VAL | VAL | ALA | TYR | GLU | PRO | VAL | TRP | ALA | ILE | ||||
| 18 | GLY | THR | GLY | LEU | ALA | ALA | THR | PRO | GLU | ASP | ||||
| 19 | ALA | GLN | ASP | ILE | HIS | ALA | SER | ILE | ARG | LYS | ||||
| 20 | PHE | LEU | ALA | SER | LYS | LEU | GLY | ASP | LYS | ALA | ||||
| 21 | ALA | SER | GLU | LEU | ARG | ILE | LEU | TYR | GLY | GLY | ||||
| 22 | SER | ALA | ASN | GLY | SER | ASN | ALA | VAL | THR | PHE | ||||
| 23 | LYS | ASP | LYS | ALA | ASP | VAL | ASP | GLY | PHE | LEU | ||||
| 24 | VAL | GLY | GLY | ALA | SER | LEU | LYS | PRO | GLU | PHE | ||||
| 25 | VAL | ASP | ILE | ILE | ASN | SER | ARG | ASN |
Entity 2, G3P, 1 - C3 H9 O6 P - 172.074 Da.
| 1 | G3P |
Samples:
sample_1: WT yeast TIM homodimer, [U-100% 13C; U-100% 15N], 7 mM; D-glycerol 3-phosphate 35 mM; Tris-HCl 50 mM; NaCl 50 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 277 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 13C-13C DARR | sample_1 | solid | sample_conditions_1 |
| 2D 15N-13C DCP | sample_1 | solid | sample_conditions_1 |
| 3D 15N-13C-13C DCP-DARR | sample_1 | solid | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMR spectrometers:
- Bruker DRX 750 MHz
- Bruker DRX 900 MHz