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 17855

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for high mobility group protein-like protein NHP1 from Babesia bovis T2Bo. Seattle Structure Genomics Center for Infectious Disease (SSGCID)

Deposition date: 2011-08-11 Original release date: 2011-08-31

Authors: Barnwal, Ravi; Varani, Gabriele

Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "1H and 15N Assigned Chemical Shifts for high mobility group protein-like protein NHP1 from Babesia bovis"  Not known ., .-..

Assembly members:
high_mobility_group_protein-like_protein_NHP1, polymer, 97 residues, 11140.849 Da.

Natural source:   Common Name: Babesia bovis   Taxonomy ID: 5865   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Babesia bovis

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

Entity Sequences (FASTA):
high_mobility_group_protein-like_protein_NHP1: MAGASDRTGVRRPRKAKKDP NAPKRALSSYMFFAKEKRVE IIAENPEIAKDVAAIGKMIG AAWNALSDEEKKPYERMSDE DRVRYEREKAEYAQRKV

Data sets:
Data typeCount
13C chemical shifts386
15N chemical shifts89
1H chemical shifts544

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NHP11

Entities:

Entity 1, NHP1 97 residues - 11140.849 Da.

1   METALAGLYALASERASPARGTHRGLYVAL
2   ARGARGPROARGLYSALALYSLYSASPPRO
3   ASNALAPROLYSARGALALEUSERSERTYR
4   METPHEPHEALALYSGLULYSARGVALGLU
5   ILEILEALAGLUASNPROGLUILEALALYS
6   ASPVALALAALAILEGLYLYSMETILEGLY
7   ALAALATRPASNALALEUSERASPGLUGLU
8   LYSLYSPROTYRGLUARGMETSERASPGLU
9   ASPARGVALARGTYRGLUARGGLULYSALA
10   GLUTYRALAGLNARGLYSVAL

Samples:

sample_1: high mobility group protein-like protein NHP1, [U-98% 13C; U-98% 15N], 1.2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAN64348 BAN64485
GB AAA27799 EDO05788
REF XP_001609356
SP P40632

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