BMRB Entry 653

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:

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:

Assembly members:
tryptophan synthase, polymer, 203 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: not available   Host organism: Escherichia coli

Data sets:
Data typeCount
1H chemical shifts28

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1tryptophan synthase1

Entities:

Entity 1, tryptophan synthase 203 residues - Formula weight is not available

1   XXXTYRXXXXXX
2   XXXXXXXXXX
3   XXXXXXXXXX
4   XXXXXXXXXX
5   XXXXXXXXGLUX
6   XXXXXXXXXX
7   XXXXXXXXXX
8   XXXXXXXXXX
9   XXXXXXXXXX
10   XXXXXXXXXX
11   XTYRXXXXXXXX
12   XXXXTYRXXXXX
13   XXXXXXXXXX
14   XXXXXXXXXX
15   XXXXXXXXXX
16   XXXXXXXXXX
17   XXXXXXXXTYRX
18   XXTYRXTYRXXXXX
19   XXXXXXXXXX
20   XXXXXXXXXX
21   XXTYR

Samples:

sample_one:

sample_condition_set_one: pH: 4.75 na; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz