BMRB Entry 27533

Name: NBPF-15 HLS2-domain
Published: 2019-07-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27533

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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:

NBPF-15 HLS2-domain

Deposition date:

2018-07-05

Original release date:

2019-07-02

Authors:

Issaian, Aaron; Hansen, Kirk; Sikela, James; Vogeli, Beat; Henen, Morkos

Citation:

Citation: Issaian, Aaron; Schmitt, Lauren; Born, Alexandra; Nichols, Parker; Sikela, James; Hansen, Kirk; Vogeli, Beat; Henen, Morkos. "Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains" Biomol. NMR Assign. 13, 339-343 (2019).
PubMed: 31264103

Assembly members:

Assembly members:
HLS-2, polymer, 106 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: pET-21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HLS-2: SAAAASSASLEIDMDEIEKY QEVEEDQDPSCPRLSRELLD EKEPEVLQDSLDRCYSTPSD YLELPDLGQPYSSAVYSLEE QYLGLALDVDRIKKDQEELE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	229
15N chemical shifts	77
1H chemical shifts	77

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HLS2	1

Entities:

Entity 1, HLS2 106 residues - Formula weight is not available

The numbering goes from 1-106 where 1-11 and 100-106 are cloning artifact and tags while actual protein is 12-99.

1

SER

ALA

SER

ALA

SER

LEU

2

GLU

ILE

ASP

MET

ASP

GLU

ILE

GLU

LYS

TYR

3

GLN

GLU

VAL

GLU

ASP

GLN

ASP

PRO

SER

4

CYS

PRO

ARG

LEU

SER

ARG

GLU

LEU

ASP

5

GLU

LYS

GLU

PRO

GLU

VAL

LEU

GLN

ASP

SER

6

LEU

ASP

ARG

CYS

TYR

SER

THR

PRO

SER

ASP

7

TYR

LEU

GLU

LEU

PRO

ASP

LEU

GLY

GLN

PRO

8

TYR

SER

ALA

VAL

TYR

SER

LEU

GLU

9

GLN

TYR

LEU

GLY

LEU

ALA

LEU

ASP

VAL

ASP

10

ARG

ILE

LYS

ASP

GLN

GLU

LEU

GLU

11

HIS

Samples:

sample_1: HLS-2, [U-99% 13C; U-99% 15N], 320 uM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Varian INOVA 900 MHz
Varian INOVA 600 MHz

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