BMRB Entry 34725

Name: RNA binding induces an allosteric switch in Cyp33 to repress MLL1 mediated transcription regulation
Published: 2022-04-11

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PDB ID: 7zew
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34725
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: RNA binding induces an allosteric switch in Cyp33 to repress MLL1 mediated transcription regulation PubMed: 37075125

Deposition date: 2022-03-31 Original release date: 2022-04-11

Authors: Blatter, M.; Allain, F.; Meylan, C.

Citation: Blatter, Markus; Meylan, Charlotte; Clery, Antoine; Giambruno, Roberto; Nikolaev, Yaroslav; Heidecker, Michel; Solanki, Jessica Arvindbhai; Diaz, Manuel; Gabellini, Davide; Allain, Frederic H-T. "RNA binding induces an allosteric switch in Cyp33 to repress MLL1-mediated transcription" Sci. Adv. 9, eadf5330-eadf5330 (2023).

Assembly members:
entity_1, polymer, 117 residues, 13189.849 Da.
entity_2, polymer, 6 residues, 1907.237 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 Vector: PTYB12

Entity Sequences (FASTA):
entity_1: AGHMATTKRVLYVGGLAEEV DDKVLHAAFIPFGDITDIQI PLDYETEKHRGFAFVEFELA EDAAAAIDNMNESELFGRTI RVNLAKPMRIKEGSSRPVWS DDDWLKKFSGKTLEENK
entity_2: AAUAAA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	430
15N chemical shifts	113
1H chemical shifts	855

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 117 residues - 13189.849 Da.

1

ALA

GLY

HIS

MET

ALA

THR

LYS

ARG

VAL

2

LEU

TYR

VAL

GLY

LEU

ALA

GLU

VAL

3

ASP

LYS

VAL

LEU

HIS

ALA

PHE

ILE

4

PRO

PHE

GLY

ASP

ILE

THR

ASP

ILE

GLN

ILE

5

PRO

LEU

ASP

TYR

GLU

THR

GLU

LYS

HIS

ARG

6

GLY

PHE

ALA

PHE

VAL

GLU

PHE

GLU

LEU

ALA

7

GLU

ASP

ALA

ILE

ASP

ASN

MET

8

ASN

GLU

SER

GLU

LEU

PHE

GLY

ARG

THR

ILE

9

ARG

VAL

ASN

LEU

ALA

LYS

PRO

MET

ARG

ILE

10

LYS

GLU

GLY

SER

ARG

PRO

VAL

TRP

SER

11

ASP

TRP

LEU

LYS

PHE

SER

GLY

12

LYS

THR

LEU

GLU

ASN

LYS

Entity 2, unit_2 6 residues - 1907.237 Da.

1

A

U

A

Samples:

sample_1: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 15N], 1 mM; RNA (5'-R(*AP*AP*UP*AP*AP*A)-3') 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM

sample_2: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 13C; U-100% 15N], 1 mM; RNA (5'-R(*AP*AP*UP*AP*AP*A)-3') 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 310.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D F3-FILTERED- F2-EDITED 13C NOESY	sample_2	isotropic	sample_conditions_1
2D F2- FILTERED NOESY	sample_2	isotropic	sample_conditions_1

Software:

Amber v10, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.96, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 900 MHz
Bruker AVANCE III 700 MHz

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