BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16136

Title: NMR assignment of jerdostatin from Trimeresurus jerdonii   PubMed: 21656569

Authors: Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Calvete, Juan Jose; Pineda-Lucena, Antonio

Citation: Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Perez, Alicia; Marcinkiewicz, Cezary; Pineda-Lucena, Antonio; Calvete, Juan. "NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin (1) (1)."  Proteins ., .-. (2011).

Assembly members:
jerdostatin, polymer, 46 residues, Formula weight is not available

Natural source:   Common Name: Trimeresurus jerdonii   Taxonomy ID: 135726   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Trimeresurus jerdonii

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

Entity Sequences (FASTA):
jerdostatin: AMDCTTGPCCRQCKLKPAGT TCWRTSVSSHYCTGRSCECP SYPGNG

Data sets:
Data typeCount
13C chemical shifts102
15N chemical shifts45
1H chemical shifts257

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1jerdostatin polypeptide1

Entities:

Entity 1, jerdostatin polypeptide 46 residues - Formula weight is not available

Residues 1-3 represent a non-native tag

1   ALAMETASPCYSTHRTHRGLYPROCYSCYS
2   ARGGLNCYSLYSLEULYSPROALAGLYTHR
3   THRCYSTRPARGTHRSERVALSERSERHIS
4   TYRCYSTHRGLYARGSERCYSGLUCYSPRO
5   SERTYRPROGLYASNGLY

Samples:

sample_1: jerdostatin, [U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16150 16151 16152
PDB
EMBL CAJ34936 CAK12627 CAL18287
GB AAP20878
SP Q3BK17 Q7ZZM2