BMRB Entry 30098

Name: NMR structure of the HLTF HIRAN domain
Published: 2016-06-06

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PDB ID: 5k5f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30098
MolProbity Validation Chart

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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:

2016-05-23

Original release date:

2016-06-06

Authors:

Bezsonova, I.; Neculai, D.; Korzhnev, D.; Weigelt, J.; Bountra, C.; Edwards, A.; Arrowsmith, C.; Dhe-Paganon, S.; Structural Genomics Consortium (SGC), SGC

Citation:

Citation: Korzhnev, Dmitry; Neculai, Dante; Dhe-Paganon, Sirano; Arrowsmith, Cheryl; Bezsonova, Irina. "Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins" J. Biomol. NMR 66, 209-219 (2016).
PubMed: 27771863

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 13532.326 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDEEVDSVLFGSLRGHVVG LRYYTGVVNNNEMVALQRDP NNPYDKNAIKVNNVNGNQVG HLKKELAGALAYIMDNKLAQ IEGVVPFGANNAFTMPLHMT FWGKEENRKAVSDQLKKHGF KL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	487
15N chemical shifts	129
1H chemical shifts	808

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 122 residues - 13532.326 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

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

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

BMRB Entry 30098

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: