BMRB Entry 27904

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Fis1 residues 1-125
Published: 2019-06-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27904

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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 Fis1 residues 1-125

Deposition date:

2019-05-13

Original release date:

2019-06-13

Authors:

Egner, John; Peterson, Francis

Citation:

Citation: Egner, John; Jensen, Davin; Olp, Michael; Kennedy, Nolan; Volkman, Brian; Peterson, Francis; Smith, Brian; Hill, R. "Development and Validation of 2D Difference Intensity Analysis for Chemical Library Screening by Protein- Detected NMR Spectroscopy" ChemBioChem 19, 448-458 (2018).
PubMed: 29239081

Assembly members:

Assembly members:
hFis1, polymer, 125 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: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hFis1: MEAVLNELVSVEDLLKFEKK FQSEKAAGSVSKSTQFEYAW CLVRSKYNDDIRKGIVLLEE LLPKGSKEEQRDYVFYLAVG NYRLKEYEKALKYVRGLLQT EPQNNQAKELERLIDKAMKK DGLVG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	465
15N chemical shifts	118
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hFis1	1

Entities:

Entity 1, hFis1 125 residues - Formula weight is not available

1

MET

GLU

ALA

VAL

LEU

ASN

GLU

LEU

VAL

SER

2

VAL

GLU

ASP

LEU

LYS

PHE

GLU

LYS

3

PHE

GLN

SER

GLU

LYS

ALA

GLY

SER

VAL

4

SER

LYS

SER

THR

GLN

PHE

GLU

TYR

ALA

TRP

5

CYS

LEU

VAL

ARG

SER

LYS

TYR

ASN

ASP

6

ILE

ARG

LYS

GLY

ILE

VAL

LEU

GLU

7

LEU

PRO

LYS

GLY

SER

LYS

GLU

GLN

8

ARG

ASP

TYR

VAL

PHE

TYR

LEU

ALA

VAL

GLY

9

ASN

TYR

ARG

LEU

LYS

GLU

TYR

GLU

LYS

ALA

10

LEU

LYS

TYR

VAL

ARG

GLY

LEU

GLN

THR

11

GLU

PRO

GLN

ASN

GLN

ALA

LYS

GLU

LEU

12

GLU

ARG

LEU

ILE

ASP

LYS

ALA

MET

LYS

13

ASP

GLY

LEU

VAL

GLY

Samples:

sample_1: HEPES 20 mM; sodium chloride 175 mM; DTT 2 mM; sodium azide 0.02%; hFis1, [U-98% 13C; U-98% 15N], 0.96 mM

sample_conditions_1: ionic strength: 0.175 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

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

GARANT, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance III 500 MHz

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