BMRB Entry 25039

Name: Structural Investigation of hnRNP L
Published: 2015-05-04

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PDB ID: 2mqm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25039
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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:

Structural Investigation of hnRNP L

Deposition date:

2014-06-24

Original release date:

2015-05-04

Authors:

Blatter, Markus; Allain, Frederic

Citation:

Citation: Blatter, Markus; Allain, Frederic. "Second RNA Recognition Motif Domain of hnRNP L" To be Published ., .-..

Assembly members:

Assembly members:
entity, polymer, 118 residues, 13079.807 Da.

Natural source:

Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTYB11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QKISRPGDSDDSRSVNSVLL FTILNPIYSITTDVLYTICN PCGPVQRIVIFRKNGVQAMV EFDSVQSAQRAKASLNGADI YSGCCTLKIEYAKPTRLNVF KNDQDTWDYTNPNLSGQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	129
1H chemical shifts	792

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 118 residues - 13079.807 Da.

1

GLN

LYS

ILE

SER

ARG

PRO

GLY

ASP

SER

ASP

2

ASP

SER

ARG

SER

VAL

ASN

SER

VAL

LEU

3

PHE

THR

ILE

LEU

ASN

PRO

ILE

TYR

SER

ILE

4

THR

ASP

VAL

LEU

TYR

THR

ILE

CYS

ASN

5

PRO

CYS

GLY

PRO

VAL

GLN

ARG

ILE

VAL

ILE

6

PHE

ARG

LYS

ASN

GLY

VAL

GLN

ALA

MET

VAL

7

GLU

PHE

ASP

SER

VAL

GLN

SER

ALA

GLN

ARG

8

ALA

LYS

ALA

SER

LEU

ASN

GLY

ALA

ASP

ILE

9

TYR

SER

GLY

CYS

THR

LEU

LYS

ILE

GLU

10

TYR

ALA

LYS

PRO

THR

ARG

LEU

ASN

VAL

PHE

11

LYS

ASN

ASP

GLN

ASP

THR

TRP

ASP

TYR

THR

12

ASN

PRO

ASN

LEU

SER

GLY

GLN

GLY

Samples:

sample_1: entity, [U-100% 15N], 1 – 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_2: entity, [U-100% 13C; U-100% 15N], 1 – 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_3: entity, [U-100% 15N], 1 – 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 310.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 700 MHz

PDB	2MQM
DBJ	BAB18649 BAC39565 BAE02304 BAE26011 BAF84804
EMBL	CAA34261
GB	AAH27206 AAH69184 AAH99683 AAI69048 EAW56826
PRF	1604358A
REF	NP_001005335 NP_001128232 NP_001178959 NP_001252929 NP_001267082
SP	P14866 Q8R081
TPG	DAA19831
AlphaFold	P14866 Q8R081