BMRB Entry 18458

Name: 1H, 13C, 15N Chemical shift assignment of HIRAN domain of human HLTF
Published: 2012-06-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18458

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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:

1H, 13C, 15N Chemical shift assignment of HIRAN domain of human HLTF

Deposition date:

2012-05-11

Original release date:

2012-06-12

Authors:

Bezsonova, Irina; Neculai, Dante; Arrowsmith, Cheryl; Dhe-Paganon, Sirano

Citation:

Citation: Neculai, Dante; Bezsonova, Irina; Weigelt, J.; Bountra, C.; Edwards, A.; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "NMR structure of the HLTF HIRAN domain" .

Assembly members:

Assembly members:
HLTF-HIRAN, polymer, 122 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HLTF-HIRAN: GSDEEVDSVLFGSLRGHVVG LRYYTGVVNNNEMVALQRDP NNPYDKNAIKVNNVNGNQVG HLKKELAGALAYIMDNKLAQ IEGVVPFGANNAFTMPLHMT FWGKEENRKAVSDQLKKHGF KL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	354
15N chemical shifts	118
1H chemical shifts	831

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIRAN domain	1

Entities:

Entity 1, HIRAN domain 122 residues - Formula weight is not available

1

GLY

SER

ASP

GLU

VAL

ASP

SER

VAL

LEU

2

PHE

GLY

SER

LEU

ARG

GLY

HIS

VAL

GLY

3

LEU

ARG

TYR

THR

GLY

VAL

ASN

4

ASN

GLU

MET

VAL

ALA

LEU

GLN

ARG

ASP

PRO

5

ASN

PRO

TYR

ASP

LYS

ASN

ALA

ILE

LYS

6

VAL

ASN

VAL

ASN

GLY

ASN

GLN

VAL

GLY

7

HIS

LEU

LYS

GLU

LEU

ALA

GLY

ALA

LEU

8

ALA

TYR

ILE

MET

ASP

ASN

LYS

LEU

ALA

GLN

9

ILE

GLU

GLY

VAL

PRO

PHE

GLY

ALA

ASN

10

ASN

ALA

PHE

THR

MET

PRO

LEU

HIS

MET

THR

11

PHE

TRP

GLY

LYS

GLU

ASN

ARG

LYS

ALA

12

VAL

SER

ASP

GLN

LEU

LYS

HIS

GLY

PHE

13

LYS

LEU

Samples:

sample_1: HLTF-HIRAN, [U-100% 13C; U-100% 15N], 1-1.6 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CC-TOCSY	sample_1	isotropic	sample_conditions_1
3D aro-NOESY	sample_1	isotropic	sample_conditions_1
3D aro-TOCSY	sample_1	isotropic	sample_conditions_1
2D aro-HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	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
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis

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

ABACUS, Lemak, Steren et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	17085 25492
PDB	2L1I 2MZN 4S0N 4XZF 4XZG
DBJ	BAD92289 BAF83920
EMBL	CAA86571 CAD10805
GB	AAA67436 AAB27691 AAH05260 AAH15498 AAH30976
REF	NP_003062 NP_620636 XP_001138277 XP_002814205 XP_003256297
SP	Q14527
AlphaFold	Q14527