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 18637

Title: 1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus   PubMed: 23179061

Deposition date: 2012-08-03 Original release date: 2013-02-12

Authors: Rey Burusco, M Florencia; Ibanez Shimabukuro, Marina; Cooper, Alan; Kennedy, Malcolm; Corsico, Betina; Smith, Brian

Citation: Rey-Burusco, M. Florencia; Ibanez-Shimabukuro, Marina; Cooper, Alan; Kennedy, Malcolm; Corsico, Betina; Smith, Brian. "H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus."  Biomol. NMR Assignments 8, 19-21 (2014).

Assembly members:
rNa-FAR-1, polymer, 170 residues, 18779.5025 Da.

Natural source:   Common Name: nematodes   Taxonomy ID: 51031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Necator americanus

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

Entity Sequences (FASTA):
rNa-FAR-1: MGSSHHHHHHSSGHMFKYED IPADYRDLMPPEARDFLQNL SDGDKTVLKEVFKAGPYKNT EESIAALKKKSPELGAKVEK LHAMVKSKIAALGPEAKGFA EKSIEIARGIKARYYTGNEP TKDDLKASVKEVLKLYKAMS DAGKADFGKQFPFLAKVFES GKAAKFAGEN

Data typeCount
13C chemical shifts862
15N chemical shifts282
1H chemical shifts1244

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1rNa-FAR-11

Entities:

Entity 1, rNa-FAR-1 170 residues - 18779.5025 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYHISMETPHELYSTYRGLUASP
3   ILEPROALAASPTYRARGASPLEUMETPRO
4   PROGLUALAARGASPPHELEUGLNASNLEU
5   SERASPGLYASPLYSTHRVALLEULYSGLU
6   VALPHELYSALAGLYPROTYRLYSASNTHR
7   GLUGLUSERILEALAALALEULYSLYSLYS
8   SERPROGLULEUGLYALALYSVALGLULYS
9   LEUHISALAMETVALLYSSERLYSILEALA
10   ALALEUGLYPROGLUALALYSGLYPHEALA
11   GLULYSSERILEGLUILEALAARGGLYILE
12   LYSALAARGTYRTYRTHRGLYASNGLUPRO
13   THRLYSASPASPLEULYSALASERVALLYS
14   GLUVALLEULYSLEUTYRLYSALAMETSER
15   ASPALAGLYLYSALAASPPHEGLYLYSGLN
16   PHEPROPHELEUALALYSVALPHEGLUSER
17   GLYLYSALAALALYSPHEALAGLYGLUASN

Samples:

Na-FAR-1: rNa-FAR-1, [U-99% 13C; U-99% 15N], 50.0 mM; H2O 95%; D2O 5%; sodium chloride 50 mM; NaPi 20 mM

apoNaFAR-1: ionic strength: 0.070 M; pH: 7.200; pressure: 1.000 atm; temperature: 311.000 K

CondSet2: ionic strength: 0.320 M; pH: 7.200; pressure: 1.000 atm; temperature: 311.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCNa-FAR-1isotropicapoNaFAR-1
C HSQC3 (h[C]_H.through-space)Na-FAR-1isotropicapoNaFAR-1
CBCACONH3 (H[N[co[{CA|ca[C]}]]])Na-FAR-1isotropicapoNaFAR-1
HNCACO3 (H[N[ca[CO]]])Na-FAR-1isotropicapoNaFAR-1
HcccoNH3 (HccoNH)Na-FAR-1isotropicapoNaFAR-1
3D C(CO)NHNa-FAR-1isotropicapoNaFAR-1
3D HNCACBNa-FAR-1isotropicapoNaFAR-1
3D HNCONa-FAR-1isotropicapoNaFAR-1
3D HCCH-TOCSYNa-FAR-1isotropicapoNaFAR-1
hCCH TOCSY3 (hC_CH.relayed)Na-FAR-1isotropicapoNaFAR-1
3D HCCH-COSYNa-FAR-1isotropicapoNaFAR-1
3D 1H-15N NOESYNa-FAR-1isotropicapoNaFAR-1
3D 1H-13C NOESYNa-FAR-1isotropicapoNaFAR-1
CBHE (hbCBcgcdceHE)Na-FAR-1isotropicapoNaFAR-1
CBHD (hbCBcgcdHD)Na-FAR-1isotropicapoNaFAR-1

Software:

ANALYSIS v2.0, CCPN - data analysis

CcpNmr_Entry_Completion_Interface v2.1, PDBe & CCPN - data deposition

DANGLE v1.1, Cheung & Broadhurst - secondary structure prediction

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

NEMBASE4 NAC00128
PDB
GB ETN71481
REF XP_013293708

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