BMRB Entry 34442

Name: Solution structure of the HRP2 IBD
Published: 2020-11-12

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PDB ID: 6t3i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34442
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:

Solution structure of the HRP2 IBD

Deposition date:

2019-10-11

Original release date:

2020-11-12

Authors:

Veverka, V.

Citation:

Citation: Van Belle, Siska; El Ashkar, Sara; Cermakova, Katerina; Matthijssens, Filip; Goossens, Steven; Canella, Alessandro; Hodges, Courtney; Christ, Frauke; De Rijck, Jan; Van Vlierberghe, Pieter; Veverka, Vaclav; Debyser, Zeger. "Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R Leukemogenesis but Important for Leukemic Cell Survival" Cells 10, 192-192 (2021).
PubMed: 33477970

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, 9675.237 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: AASPSVEEKLQKLHSEIKFA LKVDSPDVKRCLNALEELGT LQVTSQILQKNTDVVATLKK IRRYKANKDVMEKAAEVYTR LKSRGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	85
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 86 residues - 9675.237 Da.

1

ALA

SER

PRO

SER

VAL

GLU

LYS

LEU

2

GLN

LYS

LEU

HIS

SER

GLU

ILE

LYS

PHE

ALA

3

LEU

LYS

VAL

ASP

SER

PRO

ASP

VAL

LYS

ARG

4

CYS

LEU

ASN

ALA

LEU

GLU

LEU

GLY

THR

5

LEU

GLN

VAL

THR

SER

GLN

ILE

LEU

GLN

LYS

6

ASN

THR

ASP

VAL

ALA

THR

LEU

LYS

7

ILE

ARG

TYR

LYS

ALA

ASN

LYS

ASP

VAL

8

MET

GLU

LYS

ALA

GLU

VAL

TYR

THR

ARG

9

LEU

LYS

SER

ARG

GLY

SER

Samples:

sample_1: HRP2, [U-13C; U-15N], 0.5 mM; TRIS 25 mM; NaCl 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 175 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, Yasara - refinement

NMR spectrometers:

Bruker AVANCE 850 MHz

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