BMRB Entry 27585

Title:
Backbone 1H, 15N, 13C chemical shift assignments for MAK33 EV-CH2-SK antibody domain extended variant
Deposition date:
2018-08-23
Original release date:
2018-09-18
Authors:
Weber, Benedikt; Berner, Carolin; Feind, Gina; Buchner, Johannes; Brandl, Matthias; Pradhan, Tejaswini; Reif, Bernd; Pulido Cendales, Maria Daniela; Zacharias, Martin
Citation:

Citation: Weber, Benedikt; Brandl, Matthias; Pulido Cendales, Maria Daniela; Berner, Carolin; Pradhan, Tejaswini; Feind, Gina Maria; Zacharias, Martin; Reif, Bernd; Buchner, Johannes. "A single residue switch reveals principles of antibody domain integrity."  J. Biol. Chem. 293, 17107-17118 (2018).
PubMed: 30228183

Assembly members:

Assembly members:
EV-CH2-SK, polymer, 103 residues, Formula weight is not available

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: pET28b

Data sets:
Data typeCount
13C chemical shifts150
15N chemical shifts69
1H chemical shifts69

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EV-CH2-SK1

Entities:

Entity 1, EV-CH2-SK 103 residues - Formula weight is not available

CH2 domain with N-terminal EV and C-terminal SK extensions that are both part of the native linker sequences to the neighboring domains.

1   GLUVALSERSERVALPHEILEPHEPROPRO
2   LYSPROLYSASPVALLEUTHRILETHRLEU
3   THRPROLYSVALTHRCYSVALVALVALASP
4   ILESERLYSASPASPPROGLUVALGLNPHE
5   SERTRPPHEVALASPASPVALGLUVALHIS
6   THRALAGLNTHRGLNPROARGGLUGLUGLN
7   PHEASNSERTHRPHEARGSERVALSERGLU
8   LEUPROILEMETHISGLNASPTRPLEUASN
9   GLYLYSGLUPHELYSCYSARGVALASNSER
10   ALAALAPHEPROALAPROILEGLULYSTHR
11   ILESERLYS

Samples:

sample_1: EV-CH2-SK, [U-98% 13C; U-98% 15N], 500 ± 30 uM; sodium phosphate 9.1 mM; potassium phosphate 1.6 mM; sodium chloride 125 mM; potassium chloride 2.5 mM

sample_conditions_1: ionic strength: 148 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CCPNMR_Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

TOPSPIN v4.0.1, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 500 MHz

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