BMRB Entry 16136

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16136
MolProbity Validation Chart

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Title:
NMR assignment of jerdostatin from Trimeresurus jerdonii
Deposition date:
2009-01-27
Original release date:
2011-07-18
Authors:
Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Calvete, Juan Jose; Pineda-Lucena, Antonio
Citation:

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 alpha(1)beta(1)."  Proteins 79, 2530-2542 (2011).
PubMed: 21656569

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32a

Entity Sequences (FASTA):

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
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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:

UNP Q7ZZM2
AlphaFold Q7ZZM2

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