BMRB Entry 20055

Title:
Tetramer of KIA7H peptide
Deposition date:
2008-11-17
Original release date:
2010-09-02
Authors:
Lopez-Alonso, Jorge; Pardo-Cea, Miguel; Lopez de la Osa, Jaime; Chakrabartty, Avijit; Gonzalez, Carlos; Laurents, Douglas
Citation:

Citation: Lopez-Alonso, Jorge; Pardo-Cea, Miguel; Gomez-Pinto, Irene; Fernandez, Irene; Chakrabartty, Avijit; Pedroso, Enrique; Gonzalez, Carlos; Laurents, Douglas. "Putative one-pot prebiotic polypeptides with ribonucleolytic activity"  Chem. Eur. J. 16, 5314-5323 (2010).
PubMed: 20232309

Assembly members:

Assembly members:
KIA7H, polymer, 22 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KIA7H: XAKAAAAAIKAIAAIIKAGG HX

Data sets:
Data typeCount
13C chemical shifts22
1H chemical shifts139

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KIA7H peptide, chain 11
2KIA7H peptide, chain 21
3KIA7H peptide, chain 31
4KIA7H peptide, chain 41

Entities:

Entity 1, KIA7H peptide, chain 1 22 residues - Formula weight is not available

1   ACEALALYSALAALAALAALAALAILELYS
2   ALAILEALAALAILEILELYSALAGLYGLY
3   HISNH2

Samples:

H2O: KIA7H tetramer 2.8 mM; sodium chloride 200 mM; sodium phosphate 1 mM; boric acid 1 mM; H2O 90%; D2O 10%

D2O: KIA7H tetramer 1 mM; sodium chloride 200 mM; sodium phosphate 1 mM; boric acid 1 mM; D2O 100%

sample_conditions_H2O: pH: 7.45; pressure: 1 atm; temperature: 278 K

sample_conditions_D2O: pH*: 7.6; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCH2Oisotropicsample_conditions_H2O
2D 1H-1H TOCSYH2Oisotropicsample_conditions_H2O
2D 1H-1H NOESYH2Oisotropicsample_conditions_H2O
2D 1H-13C HSQCD2Oisotropicsample_conditions_D2O
2D 1H-1H NOESYD2Oisotropicsample_conditions_D2O

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

DYANA, Guntert, Braun and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz