BMRB Entry 393

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR393

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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:

NMR Assignments for the Amino-Terminal Residues of trp Repressor and Their Role in DNA Binding

Deposition date:

1995-07-31

Original release date:

1999-06-14

Authors:

Arrowsmith, Cheryl; Carey, Jannette; Treat-Clemons, Lynda; Jardetzky, Oleg

Citation:

Citation: Arrowsmith, Cheryl; Carey, Jannette; Treat-Clemons, Lynda; Jardetzky, Oleg. "NMR Assignments for the Amino-Terminal Residues of trp Repressor and Their Role in DNA Binding" Biochemistry 28, 3875-3879 (1989).

Assembly members:

Assembly members:
trp repressor, polymer, 6 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
trp repressor: AQQSPY

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment_data_set_one

Data type	Count
1H chemical shifts	31

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	trp repressor	1

Entities:

Entity 1, trp repressor 6 residues - Formula weight is not available

1

ALA

GLN

SER

PRO

TYR

Samples:

sample_one:

sample_condition_set_one: pH: 7.3 na; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

unknown unknown 0 MHz