BMRB Entry 19854

Name: Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Published: 2014-10-07

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PDB ID: 2mmg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19854
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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 Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance

Deposition date:

2014-03-15

Original release date:

2014-10-07

Authors:

Bacot-Davis, Valjean; Palmenberg, Ann; Cornilescu, Claudia; Markley, John

Citation:

Citation: Bacot-Davis, Valjean; Ciomperlik, J.; Basta, H.; Cornilescu, Claudia; Palmenberg, Ann. "Solution Structures of Mengovirus Leader Protein, its Phosphorylated Derivatives, and in Complex with Nuclear Transport Protein, RanGTPase" Proc. Nat. Acad. Sci, U.S.A. ., .-. (2014).

Assembly members:

Assembly members:
entity, polymer, 216 residues, 24456.295 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: pET23A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAAQGEPQVQFKLVLVGDGG TGKTTFVKRHLTGEFEKKYV ATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYY IQAQCAIIMFDVTSRVTYKN VPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHR KKNLQYYDISAKSNYNFEKP FLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHD LEVAQTTALPDEDDDL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	899
15N chemical shifts	294
1H chemical shifts	1438

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 216 residues - 24456.295 Da.

1

MET

ALA

GLN

GLY

GLU

PRO

GLN

VAL

GLN

2

PHE

LYS

LEU

VAL

LEU

VAL

GLY

ASP

GLY

3

THR

GLY

LYS

THR

PHE

VAL

LYS

ARG

HIS

4

LEU

THR

GLY

GLU

PHE

GLU

LYS

TYR

VAL

5

ALA

THR

LEU

GLY

VAL

GLU

VAL

HIS

PRO

LEU

6

VAL

PHE

HIS

THR

ASN

ARG

GLY

PRO

ILE

LYS

7

PHE

ASN

VAL

TRP

ASP

THR

ALA

GLY

GLN

GLU

8

LYS

PHE

GLY

LEU

ARG

ASP

GLY

TYR

9

ILE

GLN

ALA

GLN

CYS

ALA

ILE

MET

PHE

10

ASP

VAL

THR

SER

ARG

VAL

THR

TYR

LYS

ASN

11

VAL

PRO

ASN

TRP

HIS

ARG

ASP

LEU

VAL

ARG

12

VAL

CYS

GLU

ASN

ILE

PRO

ILE

VAL

LEU

CYS

13

GLY

ASN

LYS

VAL

ASP

ILE

LYS

ASP

ARG

LYS

14

VAL

LYS

ALA

LYS

SER

ILE

VAL

PHE

HIS

ARG

15

LYS

ASN

LEU

GLN

TYR

ASP

ILE

SER

16

ALA

LYS

SER

ASN

TYR

ASN

PHE

GLU

LYS

PRO

17

PHE

LEU

TRP

LEU

ALA

ARG

LYS

LEU

ILE

GLY

18

ASP

PRO

ASN

LEU

GLU

PHE

VAL

ALA

MET

PRO

19

ALA

LEU

ALA

PRO

GLU

VAL

MET

ASP

20

PRO

ALA

LEU

ALA

GLN

TYR

GLU

HIS

ASP

21

LEU

GLU

VAL

ALA

GLN

THR

ALA

LEU

PRO

22

ASP

GLU

ASP

LEU

Samples:

sample_1: RAN GTPASE, [U-100% 13C; U-100% 15N], 0.5 mM; L MENGO 0.5 mM; HEPES 20 mM; potassium chloride 100 mM; magnesium chloride 2 mM; DTT 2 mM; sodium azide 0.04%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 102 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
31-P	sample_1	isotropic	sample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARTA+, Shen and Bax - geometry optimization

SPARKY, Goddard - peak picking

CARA, Kurt W. Thrich, Swiss Federal Institute of Technology ETH - peak picking

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	19852
PDB	1A2K 1BYU 1I2M 1IBR 1K5D 1K5G 1QBK 1QG2 1QG4 1RRP 1WA5 2BKU 2MMC 2MMG 3A6P 3CH5 3EA5 3GJ0 3GJ3 3GJ4 3GJ5 3GJ6 3GJ7 3GJ8 3GJX 3NBY 3NBZ 3NC0 3NC1 3RAN 3W3Z 3ZJY 4C0Q 4GMX 4GPT 4HAT 4HAU 4HAV 4HAW 4HAX 4HAY 4HAZ 4HB0 4HB2 4HB3 4HB4 4OL0 4WVF 5BXQ 5CIQ 5CIT 5CIW 5CJ2 5CLL 5CLQ 5DH9 5DHA 5DHF 5DI9 5DIF 5DIS
DBJ	BAA89696 BAB27034 BAB27105 BAB93486 BAC36040
EMBL	CAA10191 CAA47355 CAA77980 CAG29343 CAH92646
GB	AAA36546 AAA64247 AAB24940 AAB50841 AAC05840
PRF	1814339A
REF	NP_001004829 NP_001029877 NP_001080182 NP_001126549 NP_001128547
SP	P42558 P52301 P62825 P62826 P62827
TPG	DAA20795
AlphaFold	P42558 P52301 P62825 P62826 P62827