BMRB Entry 26936

Title:
1H, 13C, and 15N Backbone Chemical Shift Assignments of camelid single-domain antibodies against active state of mu-opioid receptor.
Deposition date:
2016-11-08
Original release date:
2017-04-26
Authors:
Sounier, Remy; Yang, Yinshan; Hagelberger, Joanna; Granier, Sebastien; Demene, Helene
Citation:

Citation: Sounier, Remy; Yang, Yinshan; Hagelberger, Joanna; Granier, Sebastien; Demene, Helene. "1H, 13C, and 15N Backbone Chemical Shift Assignments of camelid single-domain antibodies against active state of mu-opioid receptor."  Biomol. NMR Assign. 11, 117-121 (2017).
PubMed: 28239762

Assembly members:

Assembly members:
Nb33, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Llama   Taxonomy ID: 9844   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lama Glama

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMalp2x

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts133
1H chemical shifts279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nanobody 331

Entities:

Entity 1, nanobody 33 129 residues - Formula weight is not available

1   SERGLNVALGLNLEUVALGLUSERGLYGLY
2   GLYLEUVALARGPROGLYGLYSERARGARG
3   LEUSERCYSVALASPSERGLUARGTHRSER
4   TYRPROMETGLYTRPPHEARGARGALAPRO
5   GLYLYSGLUARGGLUPHEVALALASERILE
6   THRTRPSERGLYILEASPPROTHRTYRALA
7   ASPSERVALALAASPARGPHETHRILESER
8   ARGASPVALALAASNASNTHRLEUTYRLEU
9   GLNMETASNSERLEULYSHISGLUASPTHR
10   ALAVALTYRTYRCYSALAALAARGALAPRO
11   VALGLYGLNSERSERSERPROTYRASPTYR
12   ASPTYRTRPGLYGLNGLYTHRGLNVALTHR
13   VALSERSERLEUGLUVALLEUPHEGLN

Samples:

sample_1: Nb33, [U-99% 13C; U-99% 15N], 1.2 mM; D2O 10%; H2O 90%; HEPES 20 mM; sodium chloride 40 mM; LMNG 0.01%; Cholesteryl Hemisuccinate 0.001%

sample_conditions_1: ionic strength: 40 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

GIFA, Delsuc - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPNMR, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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