BMRB Entry 19982

Name: NPM-N (Nucleophosmin) pentamer assignment
Published: 2014-06-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19982

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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:

NPM-N (Nucleophosmin) pentamer assignment

Deposition date:

2014-05-20

Original release date:

2014-06-18

Authors:

Mitrea, Diana; Grace, Christy; Buljan, Marija; Yun, Mi-Kyung; Pytel, Nicholas; Satumba, John; Nourse, Amanda; Park, Cheon-Gil; Babu, Madan; White, Stephen; Kriwacki, Richard

Citation:

Citation: Mitrea, Diana; Grace, Christy; Buljan, Marija; Yun, Mi-Kyung; Pytel, Nicholas; Satumba, John; Nourse, Amanda; Park, Cheon-Gil; Babu, Madan; White, Stephen; Kriwacki, Richard. "Structural polymorphism in the N-terminal oligomerization domain of NPM1" Proc. Natl. Acad. Sci. U.S.A. 111, 4466-4471 (2014).
PubMed: 1321007111

Assembly members:

Assembly members:
NPM, polymer, 133 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: DE3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NPM: GSHWEDSMDMDMSPLRPQNY LFGCELKADKDYHFKVDNDE NEHQLSLRTVSLGAGAKDEL HIVEAEAMNYEGSPIKVTLA TLKMSVQPTVSLGGFEITPP VVLRLKCGSGPVHISGQHLV AVEEDAESEDEDE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	122
13C chemical shifts	300
15N chemical shifts	122

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NPM1, chain 1	1
2	NPM1, chain 2	1
3	NPM1, chain 3	1
4	NPM1, chain 4	1
5	NPM1, chain 5	1

Entities:

Entity 1, NPM1, chain 1 133 residues - Formula weight is not available

1

GLY

SER

HIS

TRP

GLU

ASP

SER

MET

ASP

MET

2

ASP

MET

SER

PRO

LEU

ARG

PRO

GLN

ASN

TYR

3

LEU

PHE

GLY

CYS

GLU

LEU

LYS

ALA

ASP

LYS

4

ASP

TYR

HIS

PHE

LYS

VAL

ASP

ASN

ASP

GLU

5

ASN

GLU

HIS

GLN

LEU

SER

LEU

ARG

THR

VAL

6

SER

LEU

GLY

ALA

GLY

ALA

LYS

ASP

GLU

LEU

7

HIS

ILE

VAL

GLU

ALA

GLU

ALA

MET

ASN

TYR

8

GLU

GLY

SER

PRO

ILE

LYS

VAL

THR

LEU

ALA

9

THR

LEU

LYS

MET

SER

VAL

GLN

PRO

THR

VAL

10

SER

LEU

GLY

PHE

GLU

ILE

THR

PRO

11

VAL

LEU

ARG

LEU

LYS

CYS

GLY

SER

GLY

12

PRO

VAL

HIS

ILE

SER

GLY

GLN

HIS

LEU

VAL

13

ALA

VAL

GLU

ASP

ALA

GLU

SER

GLU

ASP

14

GLU

ASP

GLU

Samples:

sample_1: NPM, [U-13C; U-15N; U-2H], 1.0 mM; NPM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2 mM; NaCl 200 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 200 mM

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Keller and Wuthrich - chemical shift assignment, collection, data analysis, peak picking, processing

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2P1B 4N8M
DBJ	BAA08343 BAB24014 BAB40600 BAC25844 BAC25910
EMBL	CAA34809 CAH90204
GB	AAA36380 AAA36385 AAA39801 AAA40794 AAA40795
REF	NP_001030518 NP_001032827 NP_001125077 NP_001164790 NP_001238905
SP	P06748 P13084 Q3T160 Q61937
TPG	DAA18048 DAA26330 DAA26331
AlphaFold	P06748 Q61937 Q3T160 P13084