BMRB Entry 18837

Name: 15N, 13C and 1H Resonance Assignments and Secondary Structure Determination of a Variable Heavy Chain Antibody
Published: 2013-02-28

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18837

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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:

15N, 13C and 1H Resonance Assignments and Secondary Structure Determination of a Variable Heavy Chain Antibody

Deposition date:

2012-11-13

Original release date:

2013-02-28

Authors:

Prosser, Christine; Waters, Lorna; Muskett, Frederick; Veverka, Vaclav; Addis, Philip; Griffin, Laura; Baker, Terry; Lawson, Alastair; Wernery, Ulrich; Kinne, Jorg; Henry, Alistair; Taylor, Richard; Carr, Mark

Citation:

Citation: Prosser, Christine; Waters, Lorna; Muskett, Frederick; Veverka, Vaclav; Addis, Philip; Griffin, Laura; Baker, Alastair; Lawson, Alastair; Wernery, Ulrich; Kinne, Jorg; Henry, Alistair; Taylor, Richard; Carr, Mark. "(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody" Biomol. NMR Assignments ., .-..
PubMed: 23359223

Assembly members:

Assembly members:
VHH_18, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Camelidae Taxonomy ID: 9835 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VHH_18: MHHHHHHENLYFQGEVQLVE SGGGSVQAGGSLRLSCAASG LRISECTTGWYRQAPGKERE LVSKFSNLGTTWYTGSVKGR FTISQDSAKNTVYLQMNSLS PGDTAMYYCNTDLCPWYYEN TWGQGTQVTVSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	422
15N chemical shifts	124
1H chemical shifts	731

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VHH 18	1

Entities:

Entity 1, VHH 18 132 residues - Formula weight is not available

Residues -13 to 0 are the histidine tag and TEV cleavage site. Residues 1-118 are the native sequence

1

MET

HIS

GLU

ASN

LEU

2

TYR

PHE

GLN

GLY

GLU

VAL

GLN

LEU

VAL

GLU

3

SER

GLY

SER

VAL

GLN

ALA

GLY

4

SER

LEU

ARG

LEU

SER

CYS

ALA

SER

GLY

5

LEU

ARG

ILE

SER

GLU

CYS

THR

GLY

TRP

6

TYR

ARG

GLN

ALA

PRO

GLY

LYS

GLU

ARG

GLU

7

LEU

VAL

SER

LYS

PHE

SER

ASN

LEU

GLY

THR

8

THR

TRP

TYR

THR

GLY

SER

VAL

LYS

GLY

ARG

9

PHE

THR

ILE

SER

GLN

ASP

SER

ALA

LYS

ASN

10

THR

VAL

TYR

LEU

GLN

MET

ASN

SER

LEU

SER

11

PRO

GLY

ASP

THR

ALA

MET

TYR

CYS

ASN

12

THR

ASP

LEU

CYS

PRO

TRP

TYR

GLU

ASN

13

THR

TRP

GLY

GLN

GLY

THR

GLN

VAL

THR

VAL

14

SER

Samples:

15N_13C: VHH 18, [U-99% 13C; U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N: VHH 18, [U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

13C_UnlabelledAromatics: VHH 18, [U-99% 13C], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

13C: VHH 18, [U-99% 13C], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N_13C_D2O: VHH 18, [U-99% 13C; U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

15N_D2O: VHH 18, [U-99% 15N], 300-400 uM; sodium phosphate 25 mM; sodium chloride 100 mM; EDTA 10 uM; sodium azide 0.02%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 312 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	15N_13C_D2O	isotropic	sample_conditions_1
2D 1H-1H NOESY	15N_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_13C	isotropic	sample_conditions_1
3D 1H-15N TOCSY-HSQC	15N	isotropic	sample_conditions_1
3D 1H-15N NOESY-HSQC	15N	isotropic	sample_conditions_1
2D 1H-13C HSQC	15N_13C_D2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	15N_13C_D2O	isotropic	sample_conditions_1
3D HNCACB	15N_13C	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C	isotropic	sample_conditions_1
3D HNCO	15N_13C	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C_UnlabelledAromatics	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection

SPARKY, Goddard - data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker DRX 600 MHz
Bruker Avance 800 MHz

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