BMRB Entry 34211

Name: Complex structure of PACSIN SH3 domain and TRPV4 proline rich region
Published: 2018-09-24

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PDB ID: 6f55
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34211
MolProbity Validation Chart

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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:

Complex structure of PACSIN SH3 domain and TRPV4 proline rich region

Deposition date:

2017-11-30

Original release date:

2018-09-24

Authors:

Glogowski, N.; Goretzki, B.; Diehl, E.; Duchardt-Ferner, E.; Hacker, C.; Hellmich, U.

Citation:

Citation: Goretzki, B.; Glogowski, N.; Diehl, E.; Duchardt-Ferner, E.; Hacker, C.; Gaudet, R.; Hellmich, U.. "Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP2" Structure 26, 1583-1159 (2018).
PubMed: 30244966

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, 7398.386 Da.
entity_2, polymer, 15 residues, 1616.941 Da.

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKVPGVRVRALYDYTGQEAD ELSFKAGEELMKISEEDEQG WCKGRLLTGHVGLYPANYVE KVGLAAA
entity_2: TKGPAPNPPPILKVW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	227
15N chemical shifts	68
1H chemical shifts	463

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, entity_1 67 residues - 7398.386 Da.

1

MET

LYS

VAL

PRO

GLY

VAL

ARG

VAL

ARG

ALA

2

LEU

TYR

ASP

TYR

THR

GLY

GLN

GLU

ALA

ASP

3

GLU

LEU

SER

PHE

LYS

ALA

GLY

GLU

LEU

4

MET

LYS

ILE

SER

GLU

ASP

GLU

GLN

GLY

5

TRP

CYS

LYS

GLY

ARG

LEU

THR

GLY

HIS

6

VAL

GLY

LEU

TYR

PRO

ALA

ASN

TYR

VAL

GLU

7

LYS

VAL

GLY

LEU

ALA

Entity 2, entity_2 15 residues - 1616.941 Da.

1

THR

LYS

GLY

PRO

ALA

PRO

ASN

PRO

2

ILE

LEU

LYS

VAL

TRP

Samples:

sample_1: Pacsin 3 SH3, [U-13C; U-15N], 250 uM; PRR, unlabeled, 1.25 mM

sample_4: Pacsin 3 SH3, unlabeled, 256.8 uM; PRR, selectively 13C P124 and 15N A125, 1.284 mM

sample_5: Pacsin 3 SH3, [U-13C; U-15N], 256.8 uM; PRR, selectively 13C P128, 1.284 mM

sample_6: Pacsin 3 SH3, [U-13C; U-15N], 576 uM; PRR, unlabeled, 2.88 mM

sample_7: Pacsin 3 SH3, [U-13C; U-15N], 250 uM

sample_8: Pacsin 3 SH3, unlabeled, 235 uM; PRR, selectively 13C P126, 1.175 mM

sample_9: Pacsin 3 SH3, unlabeled, 235 uM; PRR, selectively 13C K122 P130, 1.175 mM

sample_10: Pacsin 3 SH3, unlabeled, 229 uM; PRR, selectively 13C P129 K133, 1.145 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY-HSQC	sample_6	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_6	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_6	isotropic	sample_conditions_1
3D H(CCO)NH	sample_6	isotropic	sample_conditions_1
3D H(CCO)NH	sample_6	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_7	isotropic	sample_conditions_1
3D HN(CO)CA	sample_7	isotropic	sample_conditions_1
3D HNCA	sample_7	isotropic	sample_conditions_1
3D HN(CA)CO	sample_7	isotropic	sample_conditions_1
3D HNCO	sample_7	isotropic	sample_conditions_1
3D HNCACB	sample_7	isotropic	sample_conditions_1
2D 13C filtered and 13C edited NOESY-HSQC	sample_6	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_6	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_6	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_6	isotropic	sample_conditions_1
3D 13C filtered and 13C edited NOESY-HSQC aromatic	sample_6	isotropic	sample_conditions_1
3D 13C filtered and 13C edited NOESY-HSQC aliphatic	sample_6	isotropic	sample_conditions_1
2D 13C filtered TOCSY	sample_6	isotropic	sample_conditions_1
3D 13C filtered NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C NOESY-HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_9	isotropic	sample_conditions_1
2D 1H-13C NOESY-HSQC	sample_5	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_5	isotropic	sample_conditions_1
2D 1H-13C NOESY-HSQC	sample_8	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_8	isotropic	sample_conditions_1
2D 1H-13C NOESY-HSQC	sample_9	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_10	isotropic	sample_conditions_1
2D 1H-13C NOESY-HSQC	sample_10	isotropic	sample_conditions_1

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