BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30575

Title: The putative coiled coil domain of NPHP1 folds as a three helix bundle

Deposition date: 2019-02-21 Original release date: 2019-08-09

Authors: Musco, G.; Mannella, V.

Citation: Mannella, V.; Quilici, G.; Nigro, E.; Lampis, M.; Minici, C.; Degano, M.; Boletta, A.; Musco, G.. "The N-terminal domain of NPHP1 folds into a monomeric left-handed antiparallel three-stranded coiled-coil with antiapoptotic function"  . ., .-..

Assembly members:
entity_1, polymer, 119 residues, 13676.493 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

Entity Sequences (FASTA):
entity_1: GPMAMLARRQRDPLQALRRR NQELKQQVDSLLSESQLKEA LEPNKRQHIYQRCIQLKQAI DENKNALQKLSKADESAPVA NYNQRKEEEHTLLDKLTQQL QGLAVTISRENITEVGAPT

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts122
1H chemical shifts847

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 119 residues - 13676.493 Da.

1   GLYPROMETALAMETLEUALAARGARGGLN
2   ARGASPPROLEUGLNALALEUARGARGARG
3   ASNGLNGLULEULYSGLNGLNVALASPSER
4   LEULEUSERGLUSERGLNLEULYSGLUALA
5   LEUGLUPROASNLYSARGGLNHISILETYR
6   GLNARGCYSILEGLNLEULYSGLNALAILE
7   ASPGLUASNLYSASNALALEUGLNLYSLEU
8   SERLYSALAASPGLUSERALAPROVALALA
9   ASNTYRASNGLNARGLYSGLUGLUGLUHIS
10   THRLEULEUASPLYSLEUTHRGLNGLNLEU
11   GLNGLYLEUALAVALTHRILESERARGGLU
12   ASNILETHRGLUVALGLYALAPROTHR

Samples:

sample_1: NPHP1 CC, [U-99% 13C; U-99% 15N], 0.8 mM

sample_2: NPHP1CC, [U-99% 13C; U-99% 15N], 0.8 mM

sample_3: NPHP1CC, [U-99% 15N], 0.9 mM

sample_4: NPHP1CC 0.7 mM

sample_5: NPHP1CC 0.7 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.3; pressure: 1 .; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

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