BMRB Entry 17085

Name: NMR structure of the HLTF HIRAN domain
Published: 2012-05-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17085

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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:

NMR structure of the HLTF HIRAN domain

Deposition date:

2010-07-28

Original release date:

2012-05-14

Authors:

Bezsonova, Irina; Neculai, Dante; Weigelt, Johan; Bountra, Chas; Edwards, Aled; Arrowsmith, Cheryl; Dhe-Paganon, Sirano

Citation:

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

Assembly members:

Assembly members:
HLTF, polymer, 122 residues, 13532.442 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: pET28a-LIC

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	453
15N chemical shifts	116
1H chemical shifts	750

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HLTF	1

Entities:

Entity 1, HLTF 122 residues - 13532.442 Da.

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

sample_conditions_1: ionic strength: 0.1 M; 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
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
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

Software:

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

MDDNMR, Jaravine and Orekhov - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

BMRB	18458 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