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 30679

Title: Gypsy Moth Pheromone-binding protein 1 (LdisPBP1) NMR Structure at pH 4.5   PubMed: 32877603

Deposition date: 2019-10-09 Original release date: 2020-09-18

Authors: Terrado, M.; Plettner, E.

Citation: Terrado, Mailyn; Okon, Mark; McIntosh, Lawrence; Plettner, Erika. "Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1)"  Biochemistry ., .-. (2020).

Assembly members:
entity_1, polymer, 143 residues, 16165.910 Da.

Natural source:   Common Name: Gypsy moth   Taxonomy ID: 13123   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lymantria dispar

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

Entity Sequences (FASTA):
entity_1: SKEVMKQMTINFAKPMEACK QELNVPDAVMQDFFNFWKEG YQITNREAGCVILCLAKKLE LLDQDMNLHHGKAMEFAMKH GADEAMAKQLLDIKHSCEKV ITIVADDPCQTMLNLAMCFK AEIHKLDWAPTLDVAVGELL ADT

Data sets:
Data typeCount
13C chemical shifts610
15N chemical shifts156
1H chemical shifts980

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 143 residues - 16165.910 Da.

1   SERLYSGLUVALMETLYSGLNMETTHRILE
2   ASNPHEALALYSPROMETGLUALACYSLYS
3   GLNGLULEUASNVALPROASPALAVALMET
4   GLNASPPHEPHEASNPHETRPLYSGLUGLY
5   TYRGLNILETHRASNARGGLUALAGLYCYS
6   VALILELEUCYSLEUALALYSLYSLEUGLU
7   LEULEUASPGLNASPMETASNLEUHISHIS
8   GLYLYSALAMETGLUPHEALAMETLYSHIS
9   GLYALAASPGLUALAMETALALYSGLNLEU
10   LEUASPILELYSHISSERCYSGLULYSVAL
11   ILETHRILEVALALAASPASPPROCYSGLN
12   THRMETLEUASNLEUALAMETCYSPHELYS
13   ALAGLUILEHISLYSLEUASPTRPALAPRO
14   THRLEUASPVALALAVALGLYGLULEULEU
15   ALAASPTHR

Samples:

sample_1: LdisPBP1, [U-99% 13C; U-99% 15N], 1.2 M; sodium acetate 50 mM; EDTA 1 mM; sodium azide 0.05 % w/v

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRe, Ryu H, Lim GT, Sung BH, Lee J - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 850 MHz

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