BMRB Entry 50004

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Leptin
Published: 2020-09-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50004

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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, 13C, and 15N Chemical Shift Assignments for human Leptin

Deposition date:

2019-08-21

Original release date:

2020-09-21

Authors:

Danielsson, Jens; Noel, Jeffrey; Duggan, Brendan; Oliveberg, Mikael; Onuchic, Jose; Jennings, Patricia; Haglund, Ellinor

Citation:

Citation: Danielsson, Jens; Noel, Jeffrey Kenneth; Simien, Jennifer Michelle; Duggan, Brendan Michael; Oliveberg, Mikael; Onuchic, Jose Nelson; Jennings, Patricia Ann; Haglund, Ellinor. "The Pierced Lasso Topology Leptin has a Bolt on Dynamic Domain Composed by the Disordered Loops I and III" J. Mol. Biol. 432, 3050-3063 (2020).
PubMed: 32081588

Assembly members:

Assembly members:
entity_1, polymer, 146 residues, 15912.08 Da.

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: pET-3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VPIQKVQDDTKTLIKTIVTR INDISHTQSVSSKQKVTGLD FIPGLHPILTLSKMDQTLAV YQQILTSMPSRNVIQISNDL ENLRDLLHVLAFSKSCHLPE ASGLETLDSLGGVLEASGYS TEVVALSRLQGSLQDMLEQL DLSPGC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	395
15N chemical shifts	137
1H chemical shifts	138

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	leptin monomer	1

Entities:

Entity 1, leptin monomer 146 residues - 15912.08 Da.

1

VAL

PRO

ILE

GLN

LYS

VAL

GLN

ASP

THR

2

LYS

THR

LEU

ILE

LYS

THR

ILE

VAL

THR

ARG

3

ILE

ASN

ASP

ILE

SER

HIS

THR

GLN

SER

VAL

4

SER

LYS

GLN

LYS

VAL

THR

GLY

LEU

ASP

5

PHE

ILE

PRO

GLY

LEU

HIS

PRO

ILE

LEU

THR

6

LEU

SER

LYS

MET

ASP

GLN

THR

LEU

ALA

VAL

7

TYR

GLN

ILE

LEU

THR

SER

MET

PRO

SER

8

ARG

ASN

VAL

ILE

GLN

ILE

SER

ASN

ASP

LEU

9

GLU

ASN

LEU

ARG

ASP

LEU

HIS

VAL

LEU

10

ALA

PHE

SER

LYS

SER

CYS

HIS

LEU

PRO

GLU

11

ALA

SER

GLY

LEU

GLU

THR

LEU

ASP

SER

LEU

12

GLY

VAL

LEU

GLU

ALA

SER

GLY

TYR

SER

13

THR

GLU

VAL

ALA

LEU

SER

ARG

LEU

GLN

14

GLY

SER

LEU

GLN

ASP

MET

LEU

GLU

GLN

LEU

15

ASP

LEU

SER

PRO

GLY

CYS

Samples:

sample_1: leptin monomer, [U-13C; U-15N], 0.4 mM; MES 10 mM; D2O 10%; DSS 40 uM

sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - NMR assignment

NMR spectrometers:

Bruker Avance 950 MHz

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