BMRB Entry 30469

Name: NMR structure of the second qRRM2 domain of human hnRNP H
Published: 2018-08-31

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PDB ID: 6dg1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30469
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the second qRRM2 domain of human hnRNP H

Deposition date:

2018-05-16

Original release date:

2018-08-31

Authors:

Srinivasa, R.

Citation:

Citation: Penumutchu, Srinivasa; Chiu, Liang-Yuan; Meagher, Jennifer; Hansen, Alexandar; Stuckey, Jeanne; Tolbert, Blanton. "Differential Conformational Dynamics Encoded by the Linker between Quasi RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein H." J. Am. Chem. Soc. 140, 11661-11673 (2018).
PubMed: 30122033

Assembly members:

Assembly members:
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2, polymer, 105 residues, 11791.324 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):
qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2: SNAMDWVLKHTGPNSPDTAN DGFVRLRGLPFGCSKEEIVQ FFSGLEIVPNGITLPVDFQG RSTGEAFVQFASQEIAEKAL KKHKERIGHRYIEIFKSSRA EVRTH

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	380
15N chemical shifts	97
1H chemical shifts	617

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_1 105 residues - 11791.324 Da.

1

SER

ASN

ALA

MET

ASP

TRP

VAL

LEU

LYS

HIS

2

THR

GLY

PRO

ASN

SER

PRO

ASP

THR

ALA

ASN

3

ASP

GLY

PHE

VAL

ARG

LEU

ARG

GLY

LEU

PRO

4

PHE

GLY

CYS

SER

LYS

GLU

ILE

VAL

GLN

5

PHE

SER

GLY

LEU

GLU

ILE

VAL

PRO

ASN

6

GLY

ILE

THR

LEU

PRO

VAL

ASP

PHE

GLN

GLY

7

ARG

SER

THR

GLY

GLU

ALA

PHE

VAL

GLN

PHE

8

ALA

SER

GLN

GLU

ILE

ALA

GLU

LYS

ALA

LEU

9

LYS

HIS

LYS

GLU

ARG

ILE

GLY

HIS

ARG

10

TYR

ILE

GLU

ILE

PHE

LYS

SER

ARG

ALA

11

GLU

VAL

ARG

THR

HIS

Samples:

sample_1: qRRM2 domain of hnRNP H, C13_N15, 1.5 ± 0.1 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6.2; pressure: 760 mmHg; temperature: 305 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

Bruker AvanceIII 900 MHz
Bruker AvanceIII 800 MHz

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