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 15465

Title: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF PH1500

Authors: Varnay, I.; Truffault, V.; Coles, M.

Citation: Varnay, I.; Djuranovic, S.; Truffault, V.; Lupas, A.; Kessler, H.; Coles, M.. "The Solution Structure of Ph1500-N"  . ., .-..

Assembly members:
HYPOTHETICAL_PROTEIN_PH1500, polymer, 83 residues, 9456.377 Da.

Natural source:   Common Name: Pyrococcus horikoshii   Taxonomy ID: 53953   Superkingdom: Archaea   Kingdom: not available   Genus/species: PYROCOCCUS HORIKOSHII

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
HYPOTHETICAL_PROTEIN_PH1500: HHHHHHMEGVIMSELKLKPL PKVELPPDFVDVIRIKLQGK TVRTGDVIGISILGKEVKFK VVQAYPSPLRVEDRTKITLV THP

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts70
1H chemical shifts589

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HYPOTHETICAL PROTEIN PH15001

Entities:

Entity 1, HYPOTHETICAL PROTEIN PH1500 83 residues - 9456.377 Da.

1   HISHISHISHISHISHISMETGLUGLYVAL
2   ILEMETSERGLULEULYSLEULYSPROLEU
3   PROLYSVALGLULEUPROPROASPPHEVAL
4   ASPVALILEARGILELYSLEUGLNGLYLYS
5   THRVALARGTHRGLYASPVALILEGLYILE
6   SERILELEUGLYLYSGLUVALLYSPHELYS
7   VALVALGLNALATYRPROSERPROLEUARG
8   VALGLUASPARGTHRLYSILETHRLEUVAL
9   THRHISPRO

Samples:

sample_1: HYPOTHETICAL PROTEIN PH1500 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: HYPOTHETICAL PROTEIN PH1500, [U-100% 15N], 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_3: HYPOTHETICAL PROTEIN PH1500, [U-100% 13C; U-100% 15N], 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
3D_15N-SEPARATED_ NOESYsample_2isotropicsample_conditions_1
HNHAsample_2isotropicsample_conditions_1
HNHBsample_2isotropicsample_conditions_1
CNH-NOESYsample_3isotropicsample_conditions_1
3D_13C-SEPARATED_NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

X-PLOR NIH vNIH-2.9.4A, BRUNGER, A - refinement, structure solution

xwinnmr v3.6, Bruker Biospin - collection, processing

SPARKY v3.110, Goddard - data analysis

NMR spectrometers:

  • BRUKER DMX 600 MHz
  • BRUKER DMX 900 MHz

Related Database Links:

BMRB 18978
PDB
DBJ BAA30608
REF WP_048053406