BMRB Entry 34532

Title:
NMR structure of water-soluble domain of human Lynx2 (Lypd1) protein
Deposition date:
2020-07-16
Original release date:
2021-01-06
Authors:
Kocharovskaya, M.; Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.
Citation:

Citation: Paramonov, Alexander; Kocharovskaya, Milita; Tsarev, Andrey; Kulbatskii, Dmitrii; Loktyushov, Eugene; Shulepko, Mikhail; Kirpichnikov, Mikhail; Lyukmanova, Ekaterina; Shenkarev, Zakhar. "Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors"  Int. J. Mol. Sci. 21, 7280-7280 (2020).
PubMed: 33019770

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, 9390.756 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):

Data sets:
Data typeCount
13C chemical shifts313
15N chemical shifts86
1H chemical shifts512

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 86 residues - 9390.756 Da.

1   METILEGLNCYSTYRGLNCYSGLUGLUPHE
2   GLNLEUASNASNASPCYSSERSERPROGLU
3   PHEILEVALASNCYSTHRVALASNVALGLN
4   ASPMETCYSGLNLYSGLUVALMETGLUGLN
5   SERALAGLYILEMETTYRARGLYSSERCYS
6   ALASERSERALAALACYSLEUILEALASER
7   ALAGLYTYRGLNSERPHECYSSERPROGLY
8   LYSLEUASNSERVALCYSILESERCYSCYS
9   ASNTHRPROLEUCYSASN

Samples:

sample_1: Lynx2, [U-98% 13C; U-98% 15N], 0.25 ± 0.03 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.7; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N-TOCSY-HSQCsample_1isotropicsample_conditions_1
3D 1H-15N-NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C-HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
2D 1H-13C TROSY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement

TopSpin, Bruker Biospin - collection

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

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

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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