BMRB Entry 16379

Name: Solution structure of Interleukin 1a
Published: 2010-03-10

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16379

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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:

Solution structure of Interleukin 1a

Deposition date:

2009-06-30

Original release date:

2010-03-10

Authors:

Mohan, Sepuru; Chang, Hsuan-Kuo; Chin, Yu

Citation:

Citation: Chang, Hsuan-Kuo; Mohan, Sepuru; Chin, Yu. "1H, 13C and 15N backbone and side chain resonance assignments of human interleukin 1alpha." Biomol. NMR Assignments 4, 59-60 (2010).
PubMed: 20108067

Assembly members:

Assembly members:
human interleukin 1alpha, polymer, 151 residues, 17227.705 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(20b)+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human interleukin 1alpha: NVKYNFMRIIKYEFILNDAL NQSIIRANDQYLTAAALHNL DEAVKFDMGAYKSSKDDAKI TVILRISKTQLYVTAQDEDQ PVLLKEMPEIPKTITGSETN LLFFWETHGTKNYFTSVAHP NLFIATKQDYWVCLAGGPPS ITDFQILENQA

Data sets:

assigned_chemical_shifts
- chemical_shift_set

Data type	Count
13C chemical shifts	493
15N chemical shifts	129
1H chemical shifts	759

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 151 residues - 17227.705 Da.

1

ASN

VAL

LYS

TYR

ASN

PHE

MET

ARG

ILE

2

LYS

TYR

GLU

PHE

ILE

LEU

ASN

ASP

ALA

LEU

3

ASN

GLN

SER

ILE

ARG

ALA

ASN

ASP

GLN

4

TYR

LEU

THR

ALA

LEU

HIS

ASN

LEU

5

ASP

GLU

ALA

VAL

LYS

PHE

ASP

MET

GLY

ALA

6

TYR

LYS

SER

LYS

ASP

ALA

LYS

ILE

7

THR

VAL

ILE

LEU

ARG

ILE

SER

LYS

THR

GLN

8

LEU

TYR

VAL

THR

ALA

GLN

ASP

GLU

ASP

GLN

9

PRO

VAL

LEU

LYS

GLU

MET

PRO

GLU

ILE

10

PRO

LYS

THR

ILE

THR

GLY

SER

GLU

THR

ASN

11

LEU

PHE

TRP

GLU

THR

HIS

GLY

THR

12

LYS

ASN

TYR

PHE

THR

SER

VAL

ALA

HIS

PRO

13

ASN

LEU

PHE

ILE

ALA

THR

LYS

GLN

ASP

TYR

14

TRP

VAL

CYS

LEU

ALA

GLY

PRO

SER

15

ILE

THR

ASP

PHE

GLN

ILE

LEU

GLU

ASN

GLN

16

ALA

Samples:

sample_1: TRIS 10 mM; sodium chloride 100 mM; human interleukin 1alpha 1.4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - dihedral angles

VNMRJ vVNMRJ_2.2C, Varian - processing

NMR spectrometers:

Varian VNMRS 700 MHz

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