BMRB Entry 6785

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6785

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Title:
Backbone resonance assignments for the Fv fragment of the catalytic antibody 6D9 complexed with a transition state analogue
Deposition date:
2005-08-20
Original release date:
2005-12-20
Authors:
Sakakura, Masayoshi; Takahashi, Hideo; Terasawa, Hiroaki; Takeuchi, Kou; Fujii, Ikuo; Shimada, Ichio
Citation:

Citation: Sakakura, Masayoshi; Takahashi, Hideo; Terasawa, Hiroaki; Takeuchi, Kou; Fujii, Ikuo; Shimada, Ichio. "Backbone Resonance Assignments for the Fv Fragment of Catalytic Antibody 6D9 Complexed with a Transition State Analogue"  J. Biomol. NMR 33, 282-282 (2005).
PubMed: 16341758

Assembly members:

Assembly members:
variable light chain, polymer, 115 residues, 12500 Da.
variable heavy chain, polymer, 134 residues, 14900 Da.
TSA, non-polymer, 228.199 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
variable light chain: MELVMTQTPLSLPVSLGDQA SISCRSSQTIVHSNGDTYLD WFLQKPGQSPKLLIYKVSNR FSGVPDRFSGSGSGTDFTLK ISRVEAEDLGVYYCFQGSHV PPTFGGGTKLEIKRA
variable heavy chain: MQVQLLESGGGLVKPGGSLK LSCAASGFTFSNYAMSWVRQ TPEKRLEWVVSISSGGSIYY LDSVKGRFTVSRDNARNILY LQMTSLRSEDTAMYFCARVS HYDGSRDWYFDVWGAGTSVT VSSAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts639
15N chemical shifts214
1H chemical shifts216

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1variable light chain1
2variable heavy chain2
3TSA3

Entities:

Entity 1, variable light chain 115 residues - 12500 Da.

1   METGLULEUVALMETTHRGLNTHRPROLEU
2   SERLEUPROVALSERLEUGLYASPGLNALA
3   SERILESERCYSARGSERSERGLNTHRILE
4   VALHISSERASNGLYASPTHRTYRLEUASP
5   TRPPHELEUGLNLYSPROGLYGLNSERPRO
6   LYSLEULEUILETYRLYSVALSERASNARG
7   PHESERGLYVALPROASPARGPHESERGLY
8   SERGLYSERGLYTHRASPPHETHRLEULYS
9   ILESERARGVALGLUALAGLUASPLEUGLY
10   VALTYRTYRCYSPHEGLNGLYSERHISVAL
11   PROPROTHRPHEGLYGLYGLYTHRLYSLEU
12   GLUILELYSARGALA

Entity 2, variable heavy chain 134 residues - 14900 Da.

1   METGLNVALGLNLEULEUGLUSERGLYGLY
2   GLYLEUVALLYSPROGLYGLYSERLEULYS
3   LEUSERCYSALAALASERGLYPHETHRPHE
4   SERASNTYRALAMETSERTRPVALARGGLN
5   THRPROGLULYSARGLEUGLUTRPVALVAL
6   SERILESERSERGLYGLYSERILETYRTYR
7   LEUASPSERVALLYSGLYARGPHETHRVAL
8   SERARGASPASNALAARGASNILELEUTYR
9   LEUGLNMETTHRSERLEUARGSERGLUASP
10   THRALAMETTYRPHECYSALAARGVALSER
11   HISTYRASPGLYSERARGASPTRPTYRPHE
12   ASPVALTRPGLYALAGLYTHRSERVALTHR
13   VALSERSERALAALAALALEUGLUHISHIS
14   HISHISHISHIS

Entity 3, TSA - C10 H12 O6 - 228.199 Da.

1   TSA

Samples:

sample_1: variable light chain, [U-13C; U-15N], 0.6 mM; variable heavy chain 0.6 mM; TSA 2.7 mM; sodium phosphate 5 mM; sodium chloride 200 mM

sample_2: variable light chain, [U-80% 2H; U-13C; U-15N], 0.5 mM; variable heavy chain, [U-80% 2H], 0.5 mM; TSA 1 mM; sodium phosphate 5 mM; sodium chloride 200 mM

sample_3: variable light chain, [U-80% 2H], 0.6 mM; variable heavy chain, [U-80% 2H; U-13C; U-15N], 0.6 mM; TSA 0.8 mM; sodium phosphate 5 mM; sodium chloride 200 mM

sample_4: variable light chain, [U-98% 2H; U-13C; U-15N], 0.25 mM; variable heavy chain, [U-98% 2H; U-13C; U-15N], 0.25 mM; TSA 0.3 mM; sodium phosphate 5 mM; sodium chloride 50 mM

conditions_1: pH: 6.0; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCnot availablenot availableconditions_1
HNCAsample_1not availableconditions_1
HNCOCAsample_1not availableconditions_1
TROSY-HNCAsample_3not availableconditions_1
TROSY-HNCOCAsample_3not availableconditions_1
TROSY-HNCACBnot availablenot availableconditions_1
TROSY-HNCOCACBnot availablenot availableconditions_1
TROSY-HNCOsample_4not availableconditions_1

Software:

xwinnmr v2.6, Bruker - data collection, FT

xwinnmr v3.5, Bruker - data collection, FT

SPARKY v3.106, T. D. Goddard and D. G. Kneller - peak assignments

NMR spectrometers:

  • Bruker DRX600 600 MHz
  • Bruker Avance600 600 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