BMRB Entry 28043

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28043

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Title:
Backbone 13C and 15N assignment of lambdaQ
Deposition date:
2019-11-13
Original release date:
2021-07-16
Authors:
Dudenhoeffer, Benjamin; Knauer, Stefan
Citation:

Citation: Dudenhoeffer, Benjamin; Borggraefe, Jan; Schweimer, Kristian; Knauer, Stefan. "NusA directly interacts with antitermination factor Q from phage lambda"  Sci. Rep. 10, 6607-6607 (2020).
PubMed: 32313022

Assembly members:

Assembly members:
lambdaQ, polymer, 172 residues, 18722 Da.

Natural source:

Natural source:   Common Name: Bacteriophage lambda   Taxonomy ID: 10710   Superkingdom: Virus   Kingdom: not available   Genus/species: Bacteriophage lambda

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETGb1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lambdaQ: GAMGMAQSQAGFGMAAFCGK HELSQNDKQKAINYLMQFAH KVSGKYRGVAKLEGNTKAKV LQVLATFAYADYCRSAATPG ARCRDCHGTGRAVDIAKTEL WGRVVEKECGRCKGVGYSRM PASAAYRAVTMLIPNLTQPT WSRTVKPLYDALVVQCHKEE SIADNILNAVTR

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lambdaQ1

Entities:

Entity 1, lambdaQ 172 residues - 18722 Da.

Residue 0 represents a leftover of TEV-cleavage site

1   GLYALAMETGLYMETALAGLNSERGLNALA
2   GLYPHEGLYMETALAALAPHECYSGLYLYS
3   HISGLULEUSERGLNASNASPLYSGLNLYS
4   ALAILEASNTYRLEUMETGLNPHEALAHIS
5   LYSVALSERGLYLYSTYRARGGLYVALALA
6   LYSLEUGLUGLYASNTHRLYSALALYSVAL
7   LEUGLNVALLEUALATHRPHEALATYRALA
8   ASPTYRCYSARGSERALAALATHRPROGLY
9   ALAARGCYSARGASPCYSHISGLYTHRGLY
10   ARGALAVALASPILEALALYSTHRGLULEU
11   TRPGLYARGVALVALGLULYSGLUCYSGLY
12   ARGCYSLYSGLYVALGLYTYRSERARGMET
13   PROALASERALAALATYRARGALAVALTHR
14   METLEUILEPROASNLEUTHRGLNPROTHR
15   TRPSERARGTHRVALLYSPROLEUTYRASP
16   ALALEUVALVALGLNCYSHISLYSGLUGLU
17   SERILEALAASPASNILELEUASNALAVAL
18   THRARG

Samples:

sample_1: lambdaQ, [U-80% 2H; U-98% 13C; U-98% 15N], 270 uM; NaCl 100 mM

sample_2: lambdaQ, [U-98% 13C; U-98% 15N], 500 uM; NaCl 100 mM

lambdaQ_conditions: ionic strength: 0.1 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

lambdaQ_N-Terminus_conditions: ionic strength: 0.3 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropiclambdaQ_conditions
3D HNCAsample_1isotropiclambdaQ_conditions
3D HNCACBsample_1isotropiclambdaQ_conditions
3D HNCOsample_1isotropiclambdaQ_conditions
3D HN(CA)COsample_1isotropiclambdaQ_conditions
3D HN(CO)CAsample_1isotropiclambdaQ_conditions
3D HN(COCA)CBsample_1isotropiclambdaQ_conditions
2D 1H-15N HSQCsample_2isotropiclambdaQ_N-Terminus_conditions
3D HNCAsample_2isotropiclambdaQ_N-Terminus_conditions
3D HNCACBsample_2isotropiclambdaQ_N-Terminus_conditions
3D HNCOsample_2isotropiclambdaQ_N-Terminus_conditions
3D HCACOsample_2isotropiclambdaQ_N-Terminus_conditions
3D HN(CO)CAsample_2isotropiclambdaQ_N-Terminus_conditions
3D HN(COCA)CBsample_2isotropiclambdaQ_N-Terminus_conditions

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks