BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25830

Title: Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum   PubMed: 27137920

Deposition date: 2015-09-30 Original release date: 2016-05-23

Authors: Paramonov, Alexander; Rumynskiy, Eugene; Bogdanov, Ivan; Ovchinnikova, Tatiana; Shenkarev, Zakhar

Citation: Bogdanov, Ivan; Shenkarev, Zakhar; Paramonov, Alexander; Rumynskiy, Eugene; Finkina, Ekaterina; Melnikova, Daria; Arseniev, Alexander; Ovchinnikova, Tatiana. "A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties"  BMC Plant Biol. 16, 107-107 (2016).

Assembly members:
Ps-LTP1, polymer, 95 residues, 9546.055 Da.

Natural source:   Common Name: pea   Taxonomy ID: 3888   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Pisum sativum

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

Entity Sequences (FASTA):
Ps-LTP1: ALSCGTVSADLAPCVTYLQA PNNASPPPPCCAGVKKLLAA ATTTPDRQAACNCLKSAAGS IPKLNTNNAAALPGKCGVSI PYKISTSTNCNTVRF

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts96
1H chemical shifts623

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PS-LTP11

Entities:

Entity 1, PS-LTP1 95 residues - 9546.055 Da.

1   ALALEUSERCYSGLYTHRVALSERALAASP
2   LEUALAPROCYSVALTHRTYRLEUGLNALA
3   PROASNASNALASERPROPROPROPROCYS
4   CYSALAGLYVALLYSLYSLEULEUALAALA
5   ALATHRTHRTHRPROASPARGGLNALAALA
6   CYSASNCYSLEULYSSERALAALAGLYSER
7   ILEPROLYSLEUASNTHRASNASNALAALA
8   ALALEUPROGLYLYSCYSGLYVALSERILE
9   PROTYRLYSILESERTHRSERTHRASNCYS
10   ASNTHRVALARGPHE

Samples:

sample_1: PS-LTP1, [U-98% 13C; U-98% 15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 10 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

GB KJ569141

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts