BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18126

Title: Backbone Chemical Shifts of the designed protein Z-L2LBT   PubMed: 22851279

Deposition date: 2011-12-08 Original release date: 2012-09-10

Authors: Barb, Adam; Ho, Tienhuei; Prestegard, James

Citation: Barb, Adam; Ho, Tienhuei Grace; Flanagan-Steet, Heather; Prestegard, James. "Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy."  Protein Sci. 21, 1456-1466 (2012).

Assembly members:
Z-L2LBT, polymer, 88 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Z-L2LBT: MGSSHHHHHHSSGVDNKFNK EQQNAFYEILHLPNLNEEQR NAFIQSLKDDSYIDTNNDGA YEGDELSGSQSANLLAEAKK LNDAQAPK

Data sets:
Data typeCount
13C chemical shifts223
15N chemical shifts73
1H chemical shifts73

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Z-L2LBT1

Entities:

Entity 1, Z-L2LBT 88 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYVALASPASNLYSPHEASNLYS
3   GLUGLNGLNASNALAPHETYRGLUILELEU
4   HISLEUPROASNLEUASNGLUGLUGLNARG
5   ASNALAPHEILEGLNSERLEULYSASPASP
6   SERTYRILEASPTHRASNASNASPGLYALA
7   TYRGLUGLYASPGLULEUSERGLYSERGLN
8   SERALAASNLEULEUALAGLUALALYSLYS
9   LEUASNASPALAGLNALAPROLYS

Samples:

sample_1: Z-L2LBT, [U-98% 13C; U-98% 15N], 100 – 800 uM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian VXRS 900 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts