BMRB Entry 653

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR653

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
tryptophan synthase: XXXYXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXEXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XYXXXXXXXXXXXXYXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXYXXXYXYXXXXX XXXXXXXXXXXXXXXXXXXX XXY

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_data_set_one

Data type	Count
1H chemical shifts	28

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

TYR

X

2

X

3

X

4

X

5

X

GLU

X

6

X

7

X

8

X

9

X

10

X

11

X

TYR

X

12

X

TYR

X

13

X

14

X

15

X

16

X

17

X

TYR

X

18

X

TYR

X

TYR

X

19

X

20

X

21

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