BMRB Entry 17622

Name: Solution structure of the closed conformation of human U2AF65 tandem RRM1 and RRM2 domains
Published: 2011-08-03

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PDB ID: 2yh0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17622
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the closed conformation of human U2AF65 tandem RRM1 and RRM2 domains

Deposition date: 2011-05-04 Original release date: 2011-08-03

Authors: Mackereth, C.; Madl, T.; Simon, B.; Zanier, K.; Gasch, A.; Sattler, Michael

Citation: Mackereth, C.; Madl, T.; Bonnal, S.; Simon, B.; Zanier, K.; Gasch, A.; Rybin, V.; Valcarcel, J.; Sattler, Michael. "Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF" Nature ., .-..

Assembly members:
HUMAN_U2AF65, polymer, 198 residues, 21491.534 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
HUMAN_U2AF65: GAMARRLYVGNIPFGITEEA MMDFFNAQMRLGGLTQAPGN PVLAVQINQDKNFAFLEFRS VDETTQAMAFDGIIFQGQSL KIRRPHDYQPLPGMSENPSV YVPGVVSTVVPDSAHKLFIG GLPNYLNDDQVKELLTSFGP LKAFNLVKDSATGLSKGYAF CEYVDINVTDQAIAGLNGMQ LGDKKLLVQRASVGAKNA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	497
15N chemical shifts	187
1H chemical shifts	939

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HUMAN U2AF65	1

Entities:

Entity 1, HUMAN U2AF65 198 residues - 21491.534 Da.

1

GLY

ALA

MET

ALA

ARG

LEU

TYR

VAL

GLY

2

ASN

ILE

PRO

PHE

GLY

ILE

THR

GLU

ALA

3

MET

ASP

PHE

ASN

ALA

GLN

MET

ARG

4

LEU

GLY

LEU

THR

GLN

ALA

PRO

GLY

ASN

5

PRO

VAL

LEU

ALA

VAL

GLN

ILE

ASN

GLN

ASP

6

LYS

ASN

PHE

ALA

PHE

LEU

GLU

PHE

ARG

SER

7

VAL

ASP

GLU

THR

GLN

ALA

MET

ALA

PHE

8

ASP

GLY

ILE

PHE

GLN

GLY

GLN

SER

LEU

9

LYS

ILE

ARG

PRO

HIS

ASP

TYR

GLN

PRO

10

LEU

PRO

GLY

MET

SER

GLU

ASN

PRO

SER

VAL

11

TYR

VAL

PRO

GLY

VAL

SER

THR

VAL

12

PRO

ASP

SER

ALA

HIS

LYS

LEU

PHE

ILE

GLY

13

GLY

LEU

PRO

ASN

TYR

LEU

ASN

ASP

GLN

14

VAL

LYS

GLU

LEU

THR

SER

PHE

GLY

PRO

15

LEU

LYS

ALA

PHE

ASN

LEU

VAL

LYS

ASP

SER

16

ALA

THR

GLY

LEU

SER

LYS

GLY

TYR

ALA

PHE

17

CYS

GLU

TYR

VAL

ASP

ILE

ASN

VAL

THR

ASP

18

GLN

ALA

ILE

ALA

GLY

LEU

ASN

GLY

MET

GLN

19

LEU

GLY

ASP

LYS

LEU

VAL

GLN

ARG

20

ALA

SER

VAL

GLY

ALA

LYS

ASN

ALA

Samples:

sample_1: HUMAN_U2AF65, [U-13C; U-15N], 0.2 mM; H2O 90%; D2O 10%; sodium phosphate 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 70.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 295.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H	sample_1	solution	sample_conditions_1
15N HSQC (PRE)	sample_1	solution	sample_conditions_1

Software:

AutoDep v4.3, PDBe - collection

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - chemical shift assignment

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

UNP	U2AF2_HUMAN
BMRB	17623
PDB	2YH0 2YH1
DBJ	BAC37309 BAG70075 BAG70201 BAI45669
EMBL	CAA45409 CAA45874 CAA45875 CAF97922
GB	AAH07487 AAH08740 AAH30574 AAH43071 AAH44032
PRF	1805352A
REF	NP_001001217 NP_001012496 NP_001025127 NP_001068804 NP_001080595
SP	P26368 P26369
TPG	DAA19368

Biological Magnetic Resonance Data Bank