BMRB Entry 1846
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR1846
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Title: NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site
Deposition date: 1995-07-31 Original release date: 1999-06-14
Authors: Fairbrother, Wayne; Walker, Philip; Minard, Phillipe; Littlechild, Jennifer; Watson, Herman; Williams, Robert
Citation: Fairbrother, Wayne; Walker, Philip; Minard, Phillipe; Littlechild, Jennifer; Watson, Herman; Williams, Robert. "NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site" Eur. J. Biochem. 183, 57-67 (1989).
Assembly members:
phosphoglycerate kinase, polymer, 394 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: not available
Entity Sequences (FASTA):
phosphoglycerate kinase: XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXRXX
XXXXXXXXXXXXXXXXXXXX
XHXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXHXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXHMXHXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXHXXTGGG
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 3 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | phosphoglycerate kinase | 1 |
Entities:
Entity 1, phosphoglycerate kinase 394 residues - Formula weight is not available
1 | X | X | X | X | X | X | X | X | X | X | ||||
2 | X | X | X | X | X | X | X | X | X | X | ||||
3 | X | X | X | X | X | X | X | X | X | X | ||||
4 | X | X | X | X | X | X | X | ARG | X | X | ||||
5 | X | X | X | X | X | X | X | X | X | X | ||||
6 | X | X | X | X | X | X | X | X | X | X | ||||
7 | X | HIS | X | X | X | X | X | X | X | X | ||||
8 | X | X | X | X | X | X | X | X | X | X | ||||
9 | X | X | X | X | X | X | X | X | X | X | ||||
10 | X | X | X | X | X | X | X | X | X | X | ||||
11 | X | X | X | X | X | X | X | X | X | X | ||||
12 | X | X | X | X | X | X | X | X | X | X | ||||
13 | X | X | HIS | X | X | X | X | X | X | X | ||||
14 | X | X | X | X | X | X | X | X | X | X | ||||
15 | X | X | X | X | X | X | X | X | X | X | ||||
16 | X | X | X | X | X | X | X | X | X | X | ||||
17 | X | X | X | X | X | X | HIS | MET | X | HIS | ||||
18 | X | X | X | X | X | X | X | X | X | X | ||||
19 | X | X | X | X | X | X | X | X | X | X | ||||
20 | X | X | X | X | X | X | X | X | X | X | ||||
21 | X | X | X | X | X | X | X | X | X | X | ||||
22 | X | X | X | X | X | X | X | X | X | X | ||||
23 | X | X | X | X | X | X | X | X | X | X | ||||
24 | X | X | X | X | X | X | X | X | X | X | ||||
25 | X | X | X | X | X | X | X | X | X | X | ||||
26 | X | X | X | X | X | X | X | X | X | X | ||||
27 | X | X | X | X | X | X | X | X | X | X | ||||
28 | X | X | X | X | X | X | X | X | X | X | ||||
29 | X | X | X | X | X | X | X | X | X | X | ||||
30 | X | X | X | X | X | X | X | X | X | X | ||||
31 | X | X | X | X | X | X | X | X | X | X | ||||
32 | X | X | X | X | X | X | X | X | X | X | ||||
33 | X | X | X | X | X | X | X | X | X | X | ||||
34 | X | X | X | X | X | X | X | X | X | X | ||||
35 | X | X | X | X | X | X | X | X | X | X | ||||
36 | X | X | X | X | X | X | X | X | X | X | ||||
37 | X | X | X | X | X | X | X | X | X | X | ||||
38 | X | X | X | X | X | X | X | X | X | X | ||||
39 | X | X | X | X | X | X | X | HIS | X | X | ||||
40 | THR | GLY | GLY | GLY |
Samples:
sample_one:
sample_condition_set_one: pH: 7.1 na; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
unknown | sample_one | isotropic | sample_condition_set_one |
Software:
No software information available
NMR spectrometers:
- unknown unknown 0 MHz