BMRB Entry 25851

Name: TRIM24 PHD-Bromo dual-domain backbone assignment
Published: 2016-05-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25851

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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:

TRIM24 PHD-Bromo dual-domain backbone assignment

Deposition date:

2015-10-16

Original release date:

2016-05-31

Authors:

Walser, Reto; Milbradt, Alexander

Citation:

Citation: Walser, Reto; Milbradt, Alexander; Renshaw, Jonathan. "Backbone resonance assignments for the PHD-Bromo dual-domain of the human chromatin reader TRIM24" Biomol. NMR Assignments 10, 207-211 (2016).
PubMed: 26878853

Assembly members:

Assembly members:
TRIM24, polymer, 196 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRIM24: GSTRKEDDPNEDWCAVCQNG GELLCCEKCPKVFHLSCHVP TLTNFPSGEWICTFCRDLSK PEVEYDCDAPSHNSEKKKTE GLVKLTPIDKRKCERLLLFL YCHEMSLAFQDPVPLTVPDY YKIIKNPMDLSTIKKRLQED YSMYSKPEDFVADFRLIFQN CAEFNEPDSEVANAGIKLEN YFEELLKNLYPEKRFP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	327
15N chemical shifts	154
1H chemical shifts	312

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRIM24	1
2	ZN, 1	2
3	ZN, 2	2

Entities:

Entity 1, TRIM24 196 residues - Formula weight is not available

1

GLY

SER

THR

ARG

LYS

GLU

ASP

PRO

ASN

2

GLU

ASP

TRP

CYS

ALA

VAL

CYS

GLN

ASN

GLY

3

GLY

GLU

LEU

CYS

GLU

LYS

CYS

PRO

4

LYS

VAL

PHE

HIS

LEU

SER

CYS

HIS

VAL

PRO

5

THR

LEU

THR

ASN

PHE

PRO

SER

GLY

GLU

TRP

6

ILE

CYS

THR

PHE

CYS

ARG

ASP

LEU

SER

LYS

7

PRO

GLU

VAL

GLU

TYR

ASP

CYS

ASP

ALA

PRO

8

SER

HIS

ASN

SER

GLU

LYS

THR

GLU

9

GLY

LEU

VAL

LYS

LEU

THR

PRO

ILE

ASP

LYS

10

ARG

LYS

CYS

GLU

ARG

LEU

PHE

LEU

11

TYR

CYS

HIS

GLU

MET

SER

LEU

ALA

PHE

GLN

12

ASP

PRO

VAL

PRO

LEU

THR

VAL

PRO

ASP

TYR

13

TYR

LYS

ILE

LYS

ASN

PRO

MET

ASP

LEU

14

SER

THR

ILE

LYS

ARG

LEU

GLN

GLU

ASP

15

TYR

SER

MET

TYR

SER

LYS

PRO

GLU

ASP

PHE

16

VAL

ALA

ASP

PHE

ARG

LEU

ILE

PHE

GLN

ASN

17

CYS

ALA

GLU

PHE

ASN

GLU

PRO

ASP

SER

GLU

18

VAL

ALA

ASN

ALA

GLY

ILE

LYS

LEU

GLU

ASN

19

TYR

PHE

GLU

LEU

LYS

ASN

LEU

TYR

20

PRO

GLU

LYS

ARG

PHE

PRO

Entity 2, ZN, 1 - 65.409 Da.

1

ZN

Samples:

sample_1: TRIM24, [U-100% 13C; U-100% 15N], 0.8 mM; HEPES 50 mM; sodium chloride 100 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.25 M; pH: 7.4; pressure: 1 atm; temperature: 308 K

Experiments:

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

Software:

TOPSPIN v3.2.5, Bruker Biospin - collection

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

Cara, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks