BMRB Entry 4349

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4349

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Title:
Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol
Deposition date:
1999-05-19
Original release date:
2007-07-13
Authors:
Kroon, Gerard; Martinez-Yamout, Maria; Krebs, Joseph; Chung, John; Dyson, H.; Wright, Peter
Citation:

Citation: Kroon, Gerard; Martinez-Yamout, Maria; Krebs, Joseph; Chung, John; Dyson, H.; Wright, Peter. "Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol"  J. Biomol. NMR 15, 83-84 (1999).

Assembly members:

Assembly members:
Variable light chain, polymer, 113 residues, Formula weight is not available
Variable heavy chain, polymer, 117 residues, Formula weight is not available
NPO, non-polymer, 139.109 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   Host organism: Escherichia coli   Vector: pJK34

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Variable light chain: DVVMTQTPSSLAMSVGQKVT MSCKSSQSLLNISNQKNYLA WYQQKPGQSPKLLVYFASTR ESGVPDRFIGSGSGTDFTLT ISSVQAEDQADYFCQQHYRA PRTFGGGTKLEIK
Variable heavy chain: QVQLVESGPGLVAPSQSLSI TCTVSGISLSRYNVHWVRQS PGKGLEWLGMIWGGGSIEYN PALKSRLSISKDNSKSQIFL KMNSLQTDDSAMYYCVSYGY GGDRFSYWGQGTLVTVS

Data sets:
Data typeCount
13C chemical shifts564
15N chemical shifts195
1H chemical shifts385

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Vh2
2Vl1
3p-nitrophenol3

Entities:

Entity 2, Vh 117 residues - Formula weight is not available

1   GLNVALGLNLEUVALGLUSERGLYPROGLY
2   LEUVALALAPROSERGLNSERLEUSERILE
3   THRCYSTHRVALSERGLYILESERLEUSER
4   ARGTYRASNVALHISTRPVALARGGLNSER
5   PROGLYLYSGLYLEUGLUTRPLEUGLYMET
6   ILETRPGLYGLYGLYSERILEGLUTYRASN
7   PROALALEULYSSERARGLEUSERILESER
8   LYSASPASNSERLYSSERGLNILEPHELEU
9   LYSMETASNSERLEUGLNTHRASPASPSER
10   ALAMETTYRTYRCYSVALSERTYRGLYTYR
11   GLYGLYASPARGPHESERTYRTRPGLYGLN
12   GLYTHRLEUVALTHRVALSER

Entity 1, Vl 113 residues - Formula weight is not available

1   ASPVALVALMETTHRGLNTHRPROSERSER
2   LEUALAMETSERVALGLYGLNLYSVALTHR
3   METSERCYSLYSSERSERGLNSERLEULEU
4   ASNILESERASNGLNLYSASNTYRLEUALA
5   TRPTYRGLNGLNLYSPROGLYGLNSERPRO
6   LYSLEULEUVALTYRPHEALASERTHRARG
7   GLUSERGLYVALPROASPARGPHEILEGLY
8   SERGLYSERGLYTHRASPPHETHRLEUTHR
9   ILESERSERVALGLNALAGLUASPGLNALA
10   ASPTYRPHECYSGLNGLNHISTYRARGALA
11   PROARGTHRPHEGLYGLYGLYTHRLYSLEU
12   GLUILELYS

Entity 3, p-nitrophenol - C6 H5 N O3 - 139.109 Da.

1   NPO

Samples:

sample_1: Variable heavy chain, [U-90% 15N; U-90% 13C, U-70% 2H], 0.5 mM; Variable light chain, [U-90% 15N; U-90% 13C, U-70% 2H], 0.5 mM; d11Tris 10 mM; NaCl 100 mM; p-nitrophenol 80 uM

conditions_1: pH: 6.8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availableconditions_1
3D 1H-1H-15N NOESYsample_1not availableconditions_1
3D 1H-1H-15N TOCSYsample_1not availableconditions_1
3D HNCAsample_1not availableconditions_1
3D HN(CO)CAsample_1not availableconditions_1
3D HNCACBsample_1not availableconditions_1
3D HN(CO)CACBsample_1not availableconditions_1
3D HNCOsample_1not availableconditions_1

Software:

NMRPipe - data processing

NMRView vNMRView3.1.2. - data analysis

seq_prob - assignments

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB AAA73053

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