BMRB Entry 17607

Name: Solution structure of RBBP1 tudor domain
Published: 2012-05-09

Click here to enlarge.

PDB ID: 2mam
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17607
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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:

Solution structure of RBBP1 tudor domain

Deposition date:

2011-04-28

Original release date:

2012-05-09

Authors:

Gong, Weibin; Feng, Yingang

Citation:

Citation: Gong, Weibin; Zhou, Tao; Mo, Jinjin; Perrett, Sarah; Wang, Jinfeng; Feng, Yingang. "Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1." J. Biol. Chem. 287, 8531-8540 (2012).
PubMed: 22247551

Assembly members:

Assembly members:
entity, polymer, 118 residues, 13172.984 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: pGBO expression vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: ADEPAYLTVGTDVSAKYRGA FCEAKIKTVKRLVKVKVLLK QDNTTQLVQDDQVKGPLRVG AIVETRTSDGSFQEAIISKL TDASWYTVVFDDGDERTLRR TSLCLKGERHFAESETLD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	488
15N chemical shifts	116
1H chemical shifts	719

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBBP1	1

Entities:

Entity 1, RBBP1 118 residues - 13172.984 Da.

1

ALA

ASP

GLU

PRO

ALA

TYR

LEU

THR

VAL

GLY

2

THR

ASP

VAL

SER

ALA

LYS

TYR

ARG

GLY

ALA

3

PHE

CYS

GLU

ALA

LYS

ILE

LYS

THR

VAL

LYS

4

ARG

LEU

VAL

LYS

VAL

LYS

VAL

LEU

LYS

5

GLN

ASP

ASN

THR

GLN

LEU

VAL

GLN

ASP

6

ASP

GLN

VAL

LYS

GLY

PRO

LEU

ARG

VAL

GLY

7

ALA

ILE

VAL

GLU

THR

ARG

THR

SER

ASP

GLY

8

SER

PHE

GLN

GLU

ALA

ILE

SER

LYS

LEU

9

THR

ASP

ALA

SER

TRP

TYR

THR

VAL

PHE

10

ASP

GLY

ASP

GLU

ARG

THR

LEU

ARG

11

THR

SER

LEU

CYS

LEU

LYS

GLY

GLU

ARG

HIS

12

PHE

ALA

GLU

SER

GLU

THR

LEU

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1

PDB	2MAM
DBJ	BAC31192
GB	AAB28543 AAH25436 AAH26230 AAH58209 AAI57976
REF	NP_001074664 NP_001231108 NP_001243510 NP_002883 NP_075376
SP	P29374
TPG	DAA25277
AlphaFold	P29374

BMRB Entry 17607

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: