BMRB Entry 25225

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25225

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Title:
Structure of the trans-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1)
Deposition date:
2014-09-15
Original release date:
2015-12-07
Authors:
Paramonov, Alexander; Shenkarev, Zakhar; Lyukmanova, Ekaterina; Arseniev, Alexander
Citation:

Citation: Lyukmanova, Ekaterina; Shenkarev, Zakhar; Shulepko, Mikhail; Paramonov, Alexander; Kudryavsev, Denis; Astapova, Maria; Tompsen, Morten; Kasheverov, Igor; Feofanov, Alexey; Arseniev, Alexander; Tsetlin, Vikor; Dolgikh, Dmitrii; Kirpichnikov, Mikhail. "Structural and Functional Properties of Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1) Imply a Non-Canonical Mode of Interaction with 7 nAChR"  FEBS Lett. ., .-..

Assembly members:

Assembly members:
Slurp1, polymer, 82 residues, 8992.387 Da.

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: pET-22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Slurp1: MLKCYTCKEPMTSASCRTIT RCKPEDTACMTTLVTVEAEY PFNQSPVVTRSCSSSCVATD PDSIGAAHLIFCCFRDLCNS EL

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts81
1H chemical shifts529

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Slurp11

Entities:

Entity 1, Slurp1 82 residues - 8992.387 Da.

Residue 100 is non-native Methionine introdused due to recombinant production

1   METLEULYSCYSTYRTHRCYSLYSGLUPRO
2   METTHRSERALASERCYSARGTHRILETHR
3   ARGCYSLYSPROGLUASPTHRALACYSMET
4   THRTHRLEUVALTHRVALGLUALAGLUTYR
5   PROPHEASNGLNSERPROVALVALTHRARG
6   SERCYSSERSERSERCYSVALALATHRASP
7   PROASPSERILEGLYALAALAHISLEUILE
8   PHECYSCYSPHEARGASPLEUCYSASNSER
9   GLULEU

Samples:

sample_1: Slurp1, [U-100% 15N], 0.3 mM; H2O 95%; D2O 5%

sample_2: Slurp1, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 95%; D2O 5%

sample_3: Slurp1, [U-100% 13C; U-100% 15N], 0.3 mM; D2O 100%

sample_conditions_1: ionic strength: 0.001 M; pH: 4.7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CARA v1.8, Keller R. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

UNP P55000
AlphaFold Q92483

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