BMRB Entry 27585

Name: Backbone 1H, 15N, 13C chemical shift assignments for MAK33 EV-CH2-SK antibody domain extended variant
Published: 2018-09-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27585

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EV-CH2-SK: EVSSVFIFPPKPKDVLTITL TPKVTCVVVDISKDDPEVQF SWFVDDVEVHTAQTQPREEQ FNSTFRSVSELPIMHQDWLN GKEFKCRVNSAAFPAPIEKT ISK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	150
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EV-CH2-SK	1

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

GLU

VAL

SER

VAL

PHE

ILE

PHE

PRO

2

LYS

PRO

LYS

ASP

VAL

LEU

THR

ILE

THR

LEU

3

THR

PRO

LYS

VAL

THR

CYS

VAL

ASP

4

ILE

SER

LYS

ASP

PRO

GLU

VAL

GLN

PHE

5

SER

TRP

PHE

VAL

ASP

VAL

GLU

VAL

HIS

6

THR

ALA

GLN

THR

GLN

PRO

ARG

GLU

GLN

7

PHE

ASN

SER

THR

PHE

ARG

SER

VAL

SER

GLU

8

LEU

PRO

ILE

MET

HIS

GLN

ASP

TRP

LEU

ASN

9

GLY

LYS

GLU

PHE

LYS

CYS

ARG

VAL

ASN

SER

10

ALA

PHE

PRO

ALA

PRO

ILE

GLU

LYS

THR

11

ILE

SER

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_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