BMRB Entry 18837

Title:
15N, 13C and 1H Resonance Assignments and Secondary Structure Determination of a Variable Heavy Chain Antibody
Deposition date:
2012-11-13
Original release date:
2013-02-28
Authors:
Prosser, Christine; Waters, Lorna; Muskett, Frederick; Veverka, Vaclav; Addis, Philip; Griffin, Laura; Baker, Terry; Lawson, Alastair; Wernery, Ulrich; Kinne, Jorg; Henry, Alistair; Taylor, Richard; Carr, Mark
Citation:

Citation: Prosser, Christine; Waters, Lorna; Muskett, Frederick; Veverka, Vaclav; Addis, Philip; Griffin, Laura; Baker, Alastair; Lawson, Alastair; Wernery, Ulrich; Kinne, Jorg; Henry, Alistair; Taylor, Richard; Carr, Mark. "(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody"  Biomol. NMR Assignments ., .-..
PubMed: 23359223

Assembly members:

Assembly members:
VHH_18, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Camelidae   Taxonomy ID: 9835   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts124
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VHH 181

Entities:

Entity 1, VHH 18 132 residues - Formula weight is not available

Residues -13 to 0 are the histidine tag and TEV cleavage site. Residues 1-118 are the native sequence

1   METHISHISHISHISHISHISGLUASNLEU
2   TYRPHEGLNGLYGLUVALGLNLEUVALGLU
3   SERGLYGLYGLYSERVALGLNALAGLYGLY
4   SERLEUARGLEUSERCYSALAALASERGLY
5   LEUARGILESERGLUCYSTHRTHRGLYTRP
6   TYRARGGLNALAPROGLYLYSGLUARGGLU
7   LEUVALSERLYSPHESERASNLEUGLYTHR
8   THRTRPTYRTHRGLYSERVALLYSGLYARG
9   PHETHRILESERGLNASPSERALALYSASN
10   THRVALTYRLEUGLNMETASNSERLEUSER
11   PROGLYASPTHRALAMETTYRTYRCYSASN
12   THRASPLEUCYSPROTRPTYRTYRGLUASN
13   THRTRPGLYGLNGLYTHRGLNVALTHRVAL
14   SERSER

Samples:

15N_13C: VHH 18, [U-99% 13C; U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N: VHH 18, [U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

13C_UnlabelledAromatics: VHH 18, [U-99% 13C], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

13C: VHH 18, [U-99% 13C], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N_13C_D2O: VHH 18, [U-99% 13C; U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N_D2O: VHH 18, [U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 312 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSY15N_13C_D2Oisotropicsample_conditions_1
2D 1H-1H NOESY15N_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC15N_13Cisotropicsample_conditions_1
3D 1H-15N TOCSY-HSQC15Nisotropicsample_conditions_1
3D 1H-15N NOESY-HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC15N_13C_D2Oisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C_D2Oisotropicsample_conditions_1
3D HNCACB15N_13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N_13Cisotropicsample_conditions_1
3D HNCO15N_13Cisotropicsample_conditions_1
3D 1H-13C NOESY13C_UnlabelledAromaticsisotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

SPARKY, Goddard - data analysis, peak picking

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DRX 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