BMRB Entry 26936

Name: 1H, 13C, and 15N Backbone Chemical Shift Assignments of camelid single-domain antibodies against active state of mu-opioid receptor.
Published: 2017-04-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26936

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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:

1H, 13C, and 15N Backbone Chemical Shift Assignments of camelid single-domain antibodies against active state of mu-opioid receptor.

Deposition date:

2016-11-08

Original release date:

2017-04-26

Authors:

Sounier, Remy; Yang, Yinshan; Hagelberger, Joanna; Granier, Sebastien; Demene, Helene

Citation:

Citation: Sounier, Remy; Yang, Yinshan; Hagelberger, Joanna; Granier, Sebastien; Demene, Helene. "1H, 13C, and 15N Backbone Chemical Shift Assignments of camelid single-domain antibodies against active state of mu-opioid receptor." Biomol. NMR Assign. 11, 117-121 (2017).
PubMed: 28239762

Assembly members:

Assembly members:
Nb33, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Llama Taxonomy ID: 9844 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lama Glama

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMalp2x

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nb33: SQVQLVESGGGLVRPGGSRR LSCVDSERTSYPMGWFRRAP GKEREFVASITWSGIDPTYA DSVADRFTISRDVANNTLYL QMNSLKHEDTAVYYCAARAP VGQSSSPYDYDYWGQGTQVT VSSLEVLFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	369
15N chemical shifts	133
1H chemical shifts	279

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nanobody 33	1

Entities:

Entity 1, nanobody 33 129 residues - Formula weight is not available

1

SER

GLN

VAL

GLN

LEU

VAL

GLU

SER

GLY

2

GLY

LEU

VAL

ARG

PRO

GLY

SER

ARG

3

LEU

SER

CYS

VAL

ASP

SER

GLU

ARG

THR

SER

4

TYR

PRO

MET

GLY

TRP

PHE

ARG

ALA

PRO

5

GLY

LYS

GLU

ARG

GLU

PHE

VAL

ALA

SER

ILE

6

THR

TRP

SER

GLY

ILE

ASP

PRO

THR

TYR

ALA

7

ASP

SER

VAL

ALA

ASP

ARG

PHE

THR

ILE

SER

8

ARG

ASP

VAL

ALA

ASN

THR

LEU

TYR

LEU

9

GLN

MET

ASN

SER

LEU

LYS

HIS

GLU

ASP

THR

10

ALA

VAL

TYR

CYS

ALA

ARG

ALA

PRO

11

VAL

GLY

GLN

SER

PRO

TYR

ASP

TYR

12

ASP

TYR

TRP

GLY

GLN

GLY

THR

GLN

VAL

THR

13

VAL

SER

LEU

GLU

VAL

LEU

PHE

GLN

Samples:

sample_1: Nb33, [U-99% 13C; U-99% 15N], 1.2 mM; D2O 10%; H2O 90%; HEPES 20 mM; sodium chloride 40 mM; LMNG 0.01%; Cholesteryl Hemisuccinate 0.001%

sample_conditions_1: ionic strength: 40 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

GIFA, Delsuc - processing

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

CCPNMR, CCPN - data analysis

NMR spectrometers:

Bruker Avance 700 MHz

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