BMRB Entry 19963

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19963
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structure of Bitistatin_B
Deposition date:
2014-05-11
Original release date:
2014-11-10
Authors:
Carbajo, Rodrigo; Calvete, Juan Jose; Sanz, Libia; Perez, Alicia
Citation:

Citation: Carbajo, Rodrigo; Calvete, Juan Jose; Sanz, Libia; Perez, Alicia. "NMR structure of bitistatin, a missing piece in the evolutionary pathway of snake venom disintegrins"  FEBS J. ., .-. (2014).
PubMed: 25363287

Assembly members:

Assembly members:
Bitistatin_B, polymer, 83 residues, 9014.037 Da.

Natural source:

Natural source:   Common Name: puff adder   Taxonomy ID: 8692   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bitis arietans

Experimental source:

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bitistatin_B: SPPVCGNKILEQGEDCDCGS PANCQDRCCNAATCKLTPGS QCNYGECCDQCRFKKAGTVC RIARGDWNDDYCTGKSSDCP WNH

Data sets:
Data typeCount
1H chemical shifts507
13C chemical shifts172
15N chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 83 residues - 9014.037 Da.

Seven S-S covalent bonds between cysteine residues: 5-34, 16-29, 18-24, 28-51, 42-48, 47-72, 60-79

1   SERPROPROVALCYSGLYASNLYSILELEU
2   GLUGLNGLYGLUASPCYSASPCYSGLYSER
3   PROALAASNCYSGLNASPARGCYSCYSASN
4   ALAALATHRCYSLYSLEUTHRPROGLYSER
5   GLNCYSASNTYRGLYGLUCYSCYSASPGLN
6   CYSARGPHELYSLYSALAGLYTHRVALCYS
7   ARGILEALAARGGLYASPTRPASNASPASP
8   TYRCYSTHRGLYLYSSERSERASPCYSPRO
9   TRPASNHIS

Samples:

sample_1: Bitistatin B, [U-99% 2H], 1 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM

sample_2: Bitistatin_B, [U-100% 15N], 1 mM; H2O 90%; D2O, [U-99% 2H], 10%; sodium phosphate 50 mM

sample_conditions_1: temperature: 300 K; pH: 5; pressure: 1 atm; ionic strength: 50 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19947
PDB
GB AAY43681 AAY43684
SP P17497
AlphaFold P17497

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