BMRB Entry 34548

Title:
Structure of the cis-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1)
Deposition date:
2020-08-04
Original release date:
2021-01-06
Authors:
Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.
Citation:

Citation: Shulepko, Mikhail; Bychkov, Maxim; Shenkarev, Zakhar; Kulbatskii, Dmitrii; Makhonin, Alexey; Paramonov, Alexander; Chugunov, Anton; Kirpichnikov, Mikhail; Lyukmanova, Ekaterina. "Biochemical Basis of Skin Disease Mal de Meleda: SLURP-1 Mutants Differently Affect Keratinocyte Proliferation and Apoptosis"  J. Invest. Dermatol. 141, 2229-2237 (2021).
PubMed: 33741389

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, 8992.360 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 BL21(DE3)   Vector: pET-22b(+)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts82
1H chemical shifts535

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 82 residues - 8992.360 Da.

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

Samples:

sample_1: SLURP-1, [U-15N], 0.3 ± 0.03 mM

sample_2: SLURP-1, [U-13C; U-15N], 0.3 ± 0.03 mM

sample_3: SLURP-1, [U-13C; U-15N], 0.3 ± 0.03 mM

sample_conditions_1: ionic strength: 10 mM; 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
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.8, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - collection

MddNMR, V. Orekhov, V. Jaravine, M. Mayzel, K. Kazimierczuk, Swedish NMR Center, University of Gothenburg - processing

CARA, Keller and Wuthrich - peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE 700 MHz

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