BMRB Entry 16305

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16305

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Title:
1H, 13C and 15N assignments of a camelid nanobody directed against human alpha-synuclein
Deposition date:
2009-05-18
Original release date:
2009-10-14
Authors:
Vuchelen, Anneleen; O'Day, Elizabeth; Hsu, Danny; De Genst, Erwin
Citation:

Citation: Vuchelen, Anneleen; O'Day, Elizabeth; De Genst, Erwin; Pardon, Els; Wyns, Lode; Dumoulin, Mireille; Dobson, Chris; Christodoulou, John; Hsu, Danny. "1H, 13C and 15N assignments of a camelid nanobody directed against human alpha-synuclein"  Biomol. NMR Assignments 3, 231-233 (2009).
PubMed: 19763886

Assembly members:

Assembly members:
NbSyn2, polymer, 132 residues, 14440.9 Da.

Natural source:

Natural source:   Common Name: even-toed ungulates   Taxonomy ID: 9844   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lama glama

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NbSyn2: QGQLVESGGGSVQAGGSLRL SCAASGIDSSSYCMGWFRQR PGKEREGVARINGLGGVKTA YADSVKDRFTISRDNAENTV YLQMNSLKPEDTAIYYCAAK FSPGYCGGSWSNFGYWGQGT QVTVSSHHHHHH

Data sets:
Data typeCount
13C chemical shifts432
15N chemical shifts130
1H chemical shifts703

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NbSyn21

Entities:

Entity 1, NbSyn2 132 residues - 14440.9 Da.

1   GLNGLYGLNLEUVALGLUSERGLYGLYGLY
2   SERVALGLNALAGLYGLYSERLEUARGLEU
3   SERCYSALAALASERGLYILEASPSERSER
4   SERTYRCYSMETGLYTRPPHEARGGLNARG
5   PROGLYLYSGLUARGGLUGLYVALALAARG
6   ILEASNGLYLEUGLYGLYVALLYSTHRALA
7   TYRALAASPSERVALLYSASPARGPHETHR
8   ILESERARGASPASNALAGLUASNTHRVAL
9   TYRLEUGLNMETASNSERLEULYSPROGLU
10   ASPTHRALAILETYRTYRCYSALAALALYS
11   PHESERPROGLYTYRCYSGLYGLYSERTRP
12   SERASNPHEGLYTYRTRPGLYGLNGLYTHR
13   GLNVALTHRVALSERSERHISHISHISHIS
14   HISHIS

Samples:

sample_1: NbSyn2, [U-95% 13C; U-95% 15N], 300 uM; H2O 90%; D2O 10%; sodium acetate 10%

NbSyn2_conditions: ionic strength: 20 mM; pH: 4.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicNbSyn2_conditions
3D NOESY HSQCsample_1isotropicNbSyn2_conditions
3D TOCSY HSQCsample_1isotropicNbSyn2_conditions
2D 1H-15N HSQCsample_1isotropicNbSyn2_conditions
2D 1H-13C HSQCsample_1isotropicNbSyn2_conditions
3D HCCH-TOCSYsample_1isotropicNbSyn2_conditions
3D HNCAsample_1isotropicNbSyn2_conditions
3D HNCACBsample_1isotropicNbSyn2_conditions
3D CBCA(CO)NHsample_1isotropicNbSyn2_conditions

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - processing

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

MARS, Jung, YS and Zweckstetter, M - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

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