BMRB Entry 34840

Name: Structure of the WW domain tandem of PRPF40A in complex with SF1
Published: 2024-03-28

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PDB ID: 8pxx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34840
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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 the WW domain tandem of PRPF40A in complex with SF1

Deposition date:

2023-07-24

Original release date:

2024-03-28

Authors:

Martinez-Lumbreras, S.; Sattler, M.

Citation:

Citation: Martinez-Lumbreras, Santiago; Trager, Lena; Mulorz, Miriam M.; Payr, Marco; Dikaya, Varvara; Hipp, Clara; Konig, Julian; Sattler, Michael. "Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs" Nat. Commun. 15, 3888-3888 (2024).
PubMed: 38719828

Assembly members:

Assembly members:
entity_1, polymer, 99 residues, 11450.689 Da.
entity_2, polymer, 27 residues, 2414.689 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGAKSMWTEHKSPDGRTY YYNTETKQSTWEKPDDLKTP AEQLLSKCPWKEYKSDSGKP YYYNSQTKESRWAKPKELED LEGYQNTIVAGSLITKSNL
entity_2: GAMSGSPPLPPGAPPPPPPP PPSGSGN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	425
15N chemical shifts	117
1H chemical shifts	831

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 99 residues - 11450.689 Da.

1

GLY

ALA

MET

GLY

ALA

LYS

SER

MET

TRP

THR

2

GLU

HIS

LYS

SER

PRO

ASP

GLY

ARG

THR

TYR

3

TYR

ASN

THR

GLU

THR

LYS

GLN

SER

THR

4

TRP

GLU

LYS

PRO

ASP

LEU

LYS

THR

PRO

5

ALA

GLU

GLN

LEU

SER

LYS

CYS

PRO

TRP

6

LYS

GLU

TYR

LYS

SER

ASP

SER

GLY

LYS

PRO

7

TYR

ASN

SER

GLN

THR

LYS

GLU

SER

8

ARG

TRP

ALA

LYS

PRO

LYS

GLU

LEU

GLU

ASP

9

LEU

GLU

GLY

TYR

GLN

ASN

THR

ILE

VAL

ALA

10

GLY

SER

LEU

ILE

THR

LYS

SER

ASN

LEU

Entity 2, unit_2 27 residues - 2414.689 Da.

1

GLY

ALA

MET

SER

GLY

SER

PRO

LEU

PRO

2

PRO

GLY

ALA

PRO

3

PRO

SER

GLY

SER

GLY

ASN

Samples:

sample_1: PRPF40A, [U-100% 13C; U-100% 15N], 590 uM; SF1 590 uM

sample_2: PRPF40A, [U-100% 13C; U-100% 15N], 590 uM; SF1 590 uM

sample_3: PRPF40A 900 uM; SF1, [U-100% 13C; U-100% 15N], 900 uM

sample_4: PRPF40A 900 uM; SF1, [U-100% 13C; U-100% 15N], 900 uM

sample_5: PRPF40A, [U-100% 15N], 150 uM; SF1 150 uM

sample_6: PRPF40A, [U-100% 15N], 150 uM; SF1 150 uM; Pf1 phage 10 mg/mL

sample_conditions_1: ionic strength: 133 mM; pH: 6.5; 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-15N HSQC	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
2D DSSE-HSCQ	sample_5	isotropic	sample_conditions_1
3D 1H-13C filtered NOESY	sample_4	isotropic	sample_conditions_1
3D 1H-13C filtered NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D DSSE-HSCQ	sample_6	anisotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

CcpNmr Analysis, CCPN - chemical shift assignment

ARIA, Linge, O'Donoghue and Nilges - structure calculation

PALES, Markus Zweckstetter - data analysis

NMR spectrometers:

Bruker AVANCE III 900 MHz
Bruker AVANCE III 800 MHz
Bruker AVANCE III 600 MHz

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