BMRB Entry 27757

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27757

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Title:
Backbone assignment of SQT-1N
Deposition date:
2019-01-17
Original release date:
2019-06-27
Authors:
Zalar, Matja; Indrakumar, Sowmya; Levy, Colin; Tunnicliffe, Richard; Peters, G nther; Golovanov, Alexander
Citation:

Citation: Zalar, Matja; Indrakumar, Sowmya; Levy, Colin; Tunnicliffe, Richard; Peters, Gunther; Golovanov, Alexander. "Studies of the oligomerisation mechanism of a cystatin-based engineered protein scaffold."  Sci. Rep. 9, 9067-9067 (2019).
PubMed: 31227800

Assembly members:

Assembly members:
SQT-1N, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SQT-1N: MGSSHHHHHHSSGLVPRGSM IPRGLSEAKPATPEIQEIVD KVKPQLEEKTNETYGKLEAV QYKTQVLDTYRYILASTNYY IKVRAGDNKYMHLKVFNGPE QKLISEEDLADRVLTGYQVD KNKDDELTGF

Data sets:
Data typeCount
13C chemical shifts290
15N chemical shifts93
1H chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SQT-1N monomer1

Entities:

Entity 1, SQT-1N monomer 130 residues - Formula weight is not available

Residues 1-19 represent a non-native affinity tag. Residues 68-73 represent the inserted AU1 peptide. Residues 100-109 represent the inserted c-Myc peptide.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERMET
3   ILEPROARGGLYLEUSERGLUALALYSPRO
4   ALATHRPROGLUILEGLNGLUILEVALASP
5   LYSVALLYSPROGLNLEUGLUGLULYSTHR
6   ASNGLUTHRTYRGLYLYSLEUGLUALAVAL
7   GLNTYRLYSTHRGLNVALLEUASPTHRTYR
8   ARGTYRILELEUALASERTHRASNTYRTYR
9   ILELYSVALARGALAGLYASPASNLYSTYR
10   METHISLEULYSVALPHEASNGLYPROGLU
11   GLNLYSLEUILESERGLUGLUASPLEUALA
12   ASPARGVALLEUTHRGLYTYRGLNVALASP
13   LYSASNLYSASPASPGLULEUTHRGLYPHE

Samples:

sample_1: SQT-1N, [U-100% 13C; U-100% 15N], 4.5 mM; L-Arginine 50 mM; L-Glutamate 50 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.2; 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 HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY v1.414, Goddard, NMRFAM - chemical shift assignment

TOPSPIN v3.5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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