BMRB Entry 4969

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4969

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Title:
Backbone 1H, 13C and 15N chemical shift assignments for the Brucella D4.4 VH antibody fragment
Deposition date:
2001-03-07
Original release date:
2002-12-23
Authors:
Vranken, Wim
Citation:

Citation: Vranken, Wim; Tolkatchev, Dmitri; Xu, Ping; Tanha, Jamshid; Chen, Zhigang; Narang, Saran; Ni, Feng. "Solution Structure of a Llama Single-domain Antibody with Hydrophobic Residues typical of the VH/VL Interface"  Biochemistry 41, 8570-8579 (2002).
PubMed: 12093273

Assembly members:

Assembly members:
VH antibody fragment, polymer, 135 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VH antibody fragment: DVQLQASGGGLVQPGGSLRV SCAASGFTFSSYHMAWVRQA PGKGLEWVSTINPGDGSTYY ADSVKGRFTISRDNAKNTLY LQMNSLKSEDTAVYYCAKYS GGALDAWGQGTQVTVSSQSE QKLISEEDLNHHHHH

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts140
1H chemical shifts861

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bruc D4.4 VH fragment1

Entities:

Entity 1, Bruc D4.4 VH fragment 135 residues - Formula weight is not available

1   ASPVALGLNLEUGLNALASERGLYGLYGLY
2   LEUVALGLNPROGLYGLYSERLEUARGVAL
3   SERCYSALAALASERGLYPHETHRPHESER
4   SERTYRHISMETALATRPVALARGGLNALA
5   PROGLYLYSGLYLEUGLUTRPVALSERTHR
6   ILEASNPROGLYASPGLYSERTHRTYRTYR
7   ALAASPSERVALLYSGLYARGPHETHRILE
8   SERARGASPASNALALYSASNTHRLEUTYR
9   LEUGLNMETASNSERLEULYSSERGLUASP
10   THRALAVALTYRTYRCYSALALYSTYRSER
11   GLYGLYALALEUASPALATRPGLYGLNGLY
12   THRGLNVALTHRVALSERSERGLNSERGLU
13   GLNLYSLEUILESERGLUGLUASPLEUASN
14   HISHISHISHISHIS

Samples:

sample1: VH antibody fragment, [U-13C; U-15N], 0.4 – 0.6 mM; sodium phosphate buffer 10 mM; NaCl 150 mM; EDTA 0.2 mM

cond1: ionic strength: 0.095 M; pH: 6.8; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
15N HSQCnot availablenot availablenot available
13C HSQCnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNcoCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCAcoNHnot availablenot availablenot available
HBHAcoNHnot availablenot availablenot available
13C TOCSYnot availablenot availablenot available
combined 15N/13C 3D NOESYnot availablenot availablenot available

Software:

NMRview v4.1.3 - Data analysis, Data visualization

NMRPipe v1.7 - Data processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GenBank AAL35875

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