BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50139

Title: Backbone 1H,13C, and 15N Chemical Shift Assignments for the S. typhimurium tryptophan synthase alpha subunit   PubMed: 32415580

Deposition date: 2019-12-20 Original release date: 2020-06-09

Authors: Mueller, Leonard; Sakhrani, Varun

Citation: Sakhrani, Varun; Hilario, Eduardo; Caulkins, Bethany; Hatcher-Skeers, Mary; Fan, Li; Dunn, Michael; Mueller, Leonard. "Backbone Assignments and Conformational Dynamics in the S. Typhimurium Tryptophan Synthase alpha-Subunit From Solution-State NMR"  J. Biomol. NMR ., .-. (2020).

Assembly members:
entity_1, polymer, 268 residues, 28500 Da.

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 28901   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella enterica

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: MERYENLFAQLNDRREGAFV PFVTLGDPGIEQSLKIIDTL IDAGADALELGVPFSDPLAD GPTIQNANLRAFAAGVTPAQ CFEMLALIREKHPTIPIGLL MYANLVFNNGIDAFYARCEQ VGVDSVLVADVPVEESAPFR QAALRHNIAPIFICPPNADD DLLRQVASYGRGYTYLLSRS GVTGAENRGALPLHHLIEKL KEYHAAPALQGFGISSPEQV SAAVRAGAAGAISGSAIVKI IEKNLASPKQMLAELRSFVS AMKAASRA

Data sets:
Data typeCount
13C chemical shifts634
15N chemical shifts233
1H chemical shifts233

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TS_alpha_subunit1

Entities:

Entity 1, TS_alpha_subunit 268 residues - 28500 Da.

1   METGLUARGTYRGLUASNLEUPHEALAGLN
2   LEUASNASPARGARGGLUGLYALAPHEVAL
3   PROPHEVALTHRLEUGLYASPPROGLYILE
4   GLUGLNSERLEULYSILEILEASPTHRLEU
5   ILEASPALAGLYALAASPALALEUGLULEU
6   GLYVALPROPHESERASPPROLEUALAASP
7   GLYPROTHRILEGLNASNALAASNLEUARG
8   ALAPHEALAALAGLYVALTHRPROALAGLN
9   CYSPHEGLUMETLEUALALEUILEARGGLU
10   LYSHISPROTHRILEPROILEGLYLEULEU
11   METTYRALAASNLEUVALPHEASNASNGLY
12   ILEASPALAPHETYRALAARGCYSGLUGLN
13   VALGLYVALASPSERVALLEUVALALAASP
14   VALPROVALGLUGLUSERALAPROPHEARG
15   GLNALAALALEUARGHISASNILEALAPRO
16   ILEPHEILECYSPROPROASNALAASPASP
17   ASPLEULEUARGGLNVALALASERTYRGLY
18   ARGGLYTYRTHRTYRLEULEUSERARGSER
19   GLYVALTHRGLYALAGLUASNARGGLYALA
20   LEUPROLEUHISHISLEUILEGLULYSLEU
21   LYSGLUTYRHISALAALAPROALALEUGLN
22   GLYPHEGLYILESERSERPROGLUGLNVAL
23   SERALAALAVALARGALAGLYALAALAGLY
24   ALAILESERGLYSERALAILEVALLYSILE
25   ILEGLULYSASNLEUALASERPROLYSGLN
26   METLEUALAGLULEUARGSERPHEVALSER
27   ALAMETLYSALAALASERARGALA

Samples:

sample_1: entity_1, [U-2H; U-13C; U-15N], 750 uM; sodium phosphate 50 ± 0 mM; EDTA 1 ± 0 mM; sodium azide 0.05 ± 0 %; DTT 1 ± 0 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts