BMRB Entry 653
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR653
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Title: Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit Monitoring conformational changes due to substitutions at position 49
Deposition date: 1995-07-31 Original release date: 1999-06-14
Authors: Sawada, Shintaro; Akutsu, Hideo; Ogasahara, Kyoko; Yutani, Katsuhide
Citation: Sawada, Shintaro; Akutsu, Hideo; Ogasahara, Kyoko; Yutani, Katsuhide. "Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit Monitoring conformational changes due to substitutions at position 49" Eur. J. Biochem. 189, 667-673 (1990).
Assembly members:
tryptophan synthase, polymer, 203 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: not available Host organism: Escherichia coli
Entity Sequences (FASTA):
tryptophan synthase: XXXYXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXEXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XYXXXXXXXXXXXXYXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXX
XXXXXXXXYXXXYXYXXXXX
XXXXXXXXXXXXXXXXXXXX
XXY
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 28 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | tryptophan synthase | 1 |
Entities:
Entity 1, tryptophan synthase 203 residues - Formula weight is not available
| 1 | X | X | X | TYR | 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 | X | X | X | ||||
| 5 | X | X | X | X | X | X | X | X | GLU | X | ||||
| 6 | X | X | X | X | X | X | X | X | X | X | ||||
| 7 | X | X | 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 | TYR | X | X | X | X | X | X | X | X | ||||
| 12 | X | X | X | X | TYR | X | X | X | X | X | ||||
| 13 | X | X | X | 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 | X | X | TYR | X | ||||
| 18 | X | X | TYR | X | TYR | 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 | TYR |
Samples:
sample_one:
sample_condition_set_one: pH: 4.75 na; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- unknown unknown 0 MHz