BMRB Entry 25634

Title:
Fusion to a Highly Stable Consensus Albumin Binding Domain Allows for Tunable Pharmacokinetics
Deposition date:
2015-05-21
Original release date:
2015-08-31
Authors:
Gibbs, Alan; Jacobs, Steven
Citation:

Citation: Jacobs, Steven; Gibbs, Alan; Conk, Michelle; Yi, Fang; Maguire, Diane; O'Neil, Karyn. "Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokinetics"  Protein Eng. Des. Sel. 28, 385-393 (2015).
PubMed: 26275855

Assembly members:

Assembly members:
ABD, polymer, 52 residues, 5863.789 Da.

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   Host organism: Escherichia coli   Vector: pET26

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts53
1H chemical shifts375

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ABD1

Entities:

Entity 1, ABD 52 residues - 5863.789 Da.

1   GLYTHRILEASPGLUTRPLEULEULYSGLU
2   ALALYSGLULYSALAILEGLUGLULEULYS
3   LYSALAGLYILETHRSERASPTYRTYRPHE
4   ASPLEUILEASNLYSALALYSTHRVALGLU
5   GLYVALASNALALEULYSASPGLUILELEU
6   LYSALA

Samples:

sample_1: ABD, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 90%

sample_2: ABD, [U-10% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CS-Rosetta, Yang Shen, Oliver Lange, Frank Delaglio, et al. - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

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