BMRB Entry 25038

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

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PDB ID: 2mql
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25038
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:

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. "Structural Investigation of hnRNP L" To be Published ., .-..

Assembly members:

Assembly members:
entity, polymer, 105 residues, 11386.674 Da.

Natural source:

Natural source: Common Name: 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: GENYDDPHKTPASPVVHIRG LIDGVVEADLVEALQEFGPI SYVVVMPKKRQALVEFEDVL GACNAVNYAADNQIYIAGHP AFVNYSTSQKISRPGDSDDS RSVNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	318
15N chemical shifts	103
1H chemical shifts	677

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 105 residues - 11386.674 Da.

1

GLY

GLU

ASN

TYR

ASP

PRO

HIS

LYS

THR

2

PRO

ALA

SER

PRO

VAL

HIS

ILE

ARG

GLY

3

LEU

ILE

ASP

GLY

VAL

GLU

ALA

ASP

LEU

4

VAL

GLU

ALA

LEU

GLN

GLU

PHE

GLY

PRO

ILE

5

SER

TYR

VAL

MET

PRO

LYS

ARG

6

GLN

ALA

LEU

VAL

GLU

PHE

GLU

ASP

VAL

LEU

7

GLY

ALA

CYS

ASN

ALA

VAL

ASN

TYR

ALA

8

ASP

ASN

GLN

ILE

TYR

ILE

ALA

GLY

HIS

PRO

9

ALA

PHE

VAL

ASN

TYR

SER

THR

SER

GLN

LYS

10

ILE

SER

ARG

PRO

GLY

ASP

SER

ASP

SER

11

ARG

SER

VAL

ASN

SER

Samples:

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

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 700 MHz

PDB	2MQL 3R27
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