BMRB Entry 34211

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PDB ID:
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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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 typeCount
13C chemical shifts227
15N chemical shifts68
1H chemical shifts463

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 67 residues - 7398.386 Da.

1   METLYSVALPROGLYVALARGVALARGALA
2   LEUTYRASPTYRTHRGLYGLNGLUALAASP
3   GLULEUSERPHELYSALAGLYGLUGLULEU
4   METLYSILESERGLUGLUASPGLUGLNGLY
5   TRPCYSLYSGLYARGLEULEUTHRGLYHIS
6   VALGLYLEUTYRPROALAASNTYRVALGLU
7   LYSVALGLYLEUALAALAALA

Entity 2, entity_2 15 residues - 1616.941 Da.

1   THRLYSGLYPROALAPROASNPROPROPRO
2   ILELEULYSVALTRP

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:

NameSampleSample stateSample conditions
3D 1H-15N NOESY-HSQCsample_6isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_6isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_6isotropicsample_conditions_1
3D H(CCO)NHsample_6isotropicsample_conditions_1
3D H(CCO)NHsample_6isotropicsample_conditions_1
3D HBHA(CO)NHsample_7isotropicsample_conditions_1
3D HN(CO)CAsample_7isotropicsample_conditions_1
3D HNCAsample_7isotropicsample_conditions_1
3D HN(CA)COsample_7isotropicsample_conditions_1
3D HNCOsample_7isotropicsample_conditions_1
3D HNCACBsample_7isotropicsample_conditions_1
2D 13C filtered and 13C edited NOESY-HSQCsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
3D 13C filtered and 13C edited NOESY-HSQC aromaticsample_6isotropicsample_conditions_1
3D 13C filtered and 13C edited NOESY-HSQC aliphaticsample_6isotropicsample_conditions_1
2D 13C filtered TOCSYsample_6isotropicsample_conditions_1
3D 13C filtered NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_9isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_5isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_8isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_8isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_9isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_10isotropicsample_conditions_1
2D 1H-13C NOESY-HSQCsample_10isotropicsample_conditions_1

Software:

CYANA v3.9, Guentert - structure calculation

CARA v3.9, Keller and Wuthrich - chemical shift assignment

Analysis, CCPN - data analysis

TOPSPIN, Bruker Biospin - processing

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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