BMRB Entry 25901

Name: Structure of SUMO-2 bound to phosphorylated RAP80 SIM.
Published: 2016-01-19

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PDB ID: 2n9e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25901
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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:

Structure of SUMO-2 bound to phosphorylated RAP80 SIM.

Deposition date:

2016-01-19

Original release date:

2016-01-19

Authors:

Anamika, Anamika; Spyracopoulos, Leo

Citation:

Citation: Anamika, Anamika; Spyracopoulos, Leo. "Molecular Basis for Phosphorylation Dependent SUMO Recognition by the DNA Repair Protein RAP80" J. Biol. Chem. 291, 4417-4428 (2016).
PubMed: 26719330

Assembly members:

Assembly members:
entity_1, polymer, 15 residues, 1745.656 Da.
entity_2, polymer, 95 residues, 11502.955 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XEDAFIVIXDXDGEX
entity_2: MADEKPKEGVKTENNDHINL KVAGQDGSVVQFKIKRHTPL SKLMKAYCERQGLSMRQIRF RFDGQPINETDTPAQLEMED EDTIDVFQQQTGGVY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	230
15N chemical shifts	81
1H chemical shifts	81

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 15 residues - 1745.656 Da.

The polypeptide belongs to residues 37-49 of human RAP80.

1

ACE

GLU

ASP

ALA

PHE

ILE

VAL

ILE

SEP

ASP

2

SEP

ASP

GLY

GLU

NH2

Entity 2, entity_2 95 residues - 11502.955 Da.

1

MET

ALA

ASP

GLU

LYS

PRO

LYS

GLU

GLY

VAL

2

LYS

THR

GLU

ASN

ASP

HIS

ILE

ASN

LEU

3

LYS

VAL

ALA

GLY

GLN

ASP

GLY

SER

VAL

4

GLN

PHE

LYS

ILE

LYS

ARG

HIS

THR

PRO

LEU

5

SER

LYS

LEU

MET

LYS

ALA

TYR

CYS

GLU

ARG

6

GLN

GLY

LEU

SER

MET

ARG

GLN

ILE

ARG

PHE

7

ARG

PHE

ASP

GLY

GLN

PRO

ILE

ASN

GLU

THR

8

ASP

THR

PRO

ALA

GLN

LEU

GLU

MET

GLU

ASP

9

GLU

ASP

THR

ILE

ASP

VAL

PHE

GLN

10

THR

GLY

VAL

TYR

Samples:

sample_1: entity_1 1.2 mM; entity_2, [U-100% 13C; U-100% 15N], 0.4 mM

sample_conditions_1: ionic strength: 25 mM; pH: 7.3; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

AMBER v14, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure solution

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

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz