BMRB Entry 17508

Name: Solution NMR Structure of RRM domain of RNA-binding protein FUS from homo sapiens, Northeast Structural Genomics onsortium Target HR6430A
Published: 2011-05-02

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PDB ID: 2la6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17508
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of RRM domain of RNA-binding protein FUS from homo sapiens, Northeast Structural Genomics onsortium Target HR6430A

Deposition date:

2011-03-04

Original release date:

2011-05-02

Authors:

Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Lee, Hsiau-Wei; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Lee, Hsiau-Wei; Ciccosanti, Colleen; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR6430A" To be published ., .-..

Assembly members:

Assembly members:
HR6430A, polymer, 99 residues, 10970.295 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 Vector: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR6430A: MGHHHHHHSHSDNNTIFVQG LGENVTIESVADYFKQIGII KTNKKTGQPMINLYTDRETG KLKGEATVSFDDPPSAKAAI DWFDGKEFSGNPIKVSFAT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1

Data type	Count
13C chemical shifts	391
15N chemical shifts	90
1H chemical shifts	620
residual dipolar couplings	69

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR6430A	1

Entities:

Entity 1, HR6430A 99 residues - 10970.295 Da.

1

MET

GLY

HIS

SER

HIS

2

SER

ASP

ASN

THR

ILE

PHE

VAL

GLN

GLY

3

LEU

GLY

GLU

ASN

VAL

THR

ILE

GLU

SER

VAL

4

ALA

ASP

TYR

PHE

LYS

GLN

ILE

GLY

ILE

5

LYS

THR

ASN

LYS

THR

GLY

GLN

PRO

MET

6

ILE

ASN

LEU

TYR

THR

ASP

ARG

GLU

THR

GLY

7

LYS

LEU

LYS

GLY

GLU

ALA

THR

VAL

SER

PHE

8

ASP

PRO

SER

ALA

LYS

ALA

ILE

9

ASP

TRP

PHE

ASP

GLY

LYS

GLU

PHE

SER

GLY

10

ASN

PRO

ILE

LYS

VAL

SER

PHE

ALA

THR

Samples:

sample_NC: HR6430A, [U-100% 13C; U-100% 15N], 0.83 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%

sample_NC5: HR6430A, [U-5% 13C; U-100% 15N], 0.794 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC5	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_NC	isotropic	sample_conditions_1
3D C(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz
Varian INOVA 600 MHz

PDB	2LA6 2LCW
GB	EDL17618 EDM17203 EGW03250 ELK10995
REF	XP_004323165