BMRB Entry 11504

Name: Structure of SPOC domain of the human transcriptional corepressor SHARP
Published: 2013-12-02

Click here to enlarge.

PDB ID: 2rt5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11504
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Structure of SPOC domain of the human transcriptional corepressor SHARP PubMed: 24268649

Deposition date: 2012-05-22 Original release date: 2013-12-02

Authors: Mikami, Suzuka; Kanaba, Teppei; Mishima, Masaki

Citation: Mikami, Suzuka; Kanaba, Teppei; Mishima, Masaki. "Structural Insights into the Recruitment of SMRT by the Corepressor SHARP under Phosphorylative Regulation" Structure ., .-. (2013).

Assembly members:
SHARP, polymer, 169 residues, 18471.535 Da.
SMRT, polymer, 8 residues, 1102.889 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):
SHARP: VDMVQLLKKYPIVWQGLLAL KNDTAAVQLHFVSGNNVLAH RSLPLSEGGPPLRIAQRMRL EATQLEGVARRMTVETDYCL LLALPCGRDQEDVVSQTESL KAAFITYLQAKQAAGIINVP NPGSNQPAYVLQIFPPCEFS ESHLSRLAPDLLASISNISP HLMIVIASV
SMRT: YETLXDXE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	723
15N chemical shifts	163
1H chemical shifts	1137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

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

Entities:

Entity 1, entity_1 169 residues - 18471.535 Da.

1

VAL

ASP

MET

VAL

GLN

LEU

LYS

TYR

2

PRO

ILE

VAL

TRP

GLN

GLY

LEU

ALA

LEU

3

LYS

ASN

ASP

THR

ALA

VAL

GLN

LEU

HIS

4

PHE

VAL

SER

GLY

ASN

VAL

LEU

ALA

HIS

5

ARG

SER

LEU

PRO

LEU

SER

GLU

GLY

PRO

6

PRO

LEU

ARG

ILE

ALA

GLN

ARG

MET

ARG

LEU

7

GLU

ALA

THR

GLN

LEU

GLU

GLY

VAL

ALA

ARG

8

ARG

MET

THR

VAL

GLU

THR

ASP

TYR

CYS

LEU

9

LEU

ALA

LEU

PRO

CYS

GLY

ARG

ASP

GLN

10

GLU

ASP

VAL

SER

GLN

THR

GLU

SER

LEU

11

LYS

ALA

PHE

ILE

THR

TYR

LEU

GLN

ALA

12

LYS

GLN

ALA

GLY

ILE

ASN

VAL

PRO

13

ASN

PRO

GLY

SER

ASN

GLN

PRO

ALA

TYR

VAL

14

LEU

GLN

ILE

PHE

PRO

CYS

GLU

PHE

SER

15

GLU

SER

HIS

LEU

SER

ARG

LEU

ALA

PRO

ASP

16

LEU

ALA

SER

ILE

SER

ASN

ILE

SER

PRO

17

HIS

LEU

MET

ILE

VAL

ILE

ALA

SER

VAL

Entity 2, entity_2 8 residues - 1102.889 Da.

YETL(SEP)D(SEP)E

1

TYR

GLU

THR

LEU

SEP

ASP

SEP

GLU

Samples:

sample_1: SHARP, [U-100% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; H2O 93%; D2O 7%

sample_2: SHARP, [U-15% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; H2O 93%; D2O 7%

sample_3: SMRT, [U-13C; U-15N]-Leu, Glu, Tyr, Asp, 0.9 mM; SHARP 0.9 mM; H2O 93%; D2O 7%

sample_4: SHARP, [U-100% 13C; U-100% 15N], 0.9 mM; SMRT 0.9 mM; D2O 100%

sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D HC(CO)NH	sample_1	isotropic	sample_conditions_1
3D 13C edited NOESY-HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNHB	sample_2	isotropic	sample_conditions_1
3D HN(CO)NB	sample_2	isotropic	sample_conditions_1
15N edited NOESY-HSQC	sample_1	isotropic	sample_conditions_1
2D 15N filtered 1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz

PDB	1OW1 2RT5
DBJ	BAA76773 BAB32786 BAG10400
EMBL	CAB51072
GB	AAD55931 AAI72907 AAK52750 EAW51756 EDL80993
REF	NP_001258424 NP_055816 NP_062737 XP_002694185 XP_002750362
SP	Q62504 Q96T58
TPG	DAA21211

Biological Magnetic Resonance Data Bank