BMRB Entry 26579

Name: Resonance assignment of the N-terminal domain of hLCN2-R
Published: 2016-10-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26579

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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:

Resonance assignment of the N-terminal domain of hLCN2-R

Deposition date:

2015-06-01

Original release date:

2016-10-04

Authors:

Coudevylle, Nicolas; Zerko, Szymon; Kozminski, Wiktor; Konrat, Robert

Citation:

Citation: Cabedo Martinez, Ana Isabel; Weinhaupl, Katharina; Lee, Wing-Kee; Wolff, Natascha; Storch, Barbara; Zerko, Szymon; Konrat, Robert; Kozminski, Wiktor; Breuker, Kathrin; Thevenod, Frank; Coudevylle, Nicolas. "Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17" J. Biol. Chem. 291, 2917-2930 (2016).
PubMed: 26635366

Assembly members:

Assembly members:
hLCN2-R-NTD, polymer, 105 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hLCN2-R-NTD: MASDPIFTLAPPLHCHYGAF PPNASGWEQPPNASGVSVAS AALAASAASRVATSTDPSCS GFAPPDFNHCLKDWDYNGLP VLTTNAIGQWDLVCDLGWQV ILEQI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	255
15N chemical shifts	88
1H chemical shifts	342

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hLCN2-R-NTD	1

Entities:

Entity 1, hLCN2-R-NTD 105 residues - Formula weight is not available

1

MET

ALA

SER

ASP

PRO

ILE

PHE

THR

LEU

ALA

2

PRO

LEU

HIS

CYS

HIS

TYR

GLY

ALA

PHE

3

PRO

ASN

ALA

SER

GLY

TRP

GLU

GLN

PRO

4

PRO

ASN

ALA

SER

GLY

VAL

SER

VAL

ALA

SER

5

ALA

LEU

ALA

SER

ALA

SER

ARG

6

VAL

ALA

THR

SER

THR

ASP

PRO

SER

CYS

SER

7

GLY

PHE

ALA

PRO

ASP

PHE

ASN

HIS

CYS

8

LEU

LYS

ASP

TRP

ASP

TYR

ASN

GLY

LEU

PRO

9

VAL

LEU

THR

ASN

ALA

ILE

GLY

GLN

TRP

10

ASP

LEU

VAL

CYS

ASP

LEU

GLY

TRP

GLN

VAL

11

ILE

LEU

GLU

GLN

ILE

Samples:

sample_1: hLCN2-R-NTD, [U-95% 13C; U-95% 15N], 0.5 mM; H20 95%; D20 5%

sample_conditions_1: ionic strength: 70 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
5D HN(CA)CONH	sample_1	isotropic	sample_conditions_1
5D (HACA)CON(CA)CONH	sample_1	isotropic	sample_conditions_1
5D (H)NCO(NCA)CONH	sample_1	isotropic	sample_conditions_1
4D HNCACO	sample_1	isotropic	sample_conditions_1
5D HabCabCONH	sample_1	isotropic	sample_conditions_1
5D H(CC-tocsy)CONH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 700 MHz

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