BMRB Entry 6645

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6645
MolProbity Validation Chart

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Title:
1H, 13C and 15N backbone and side chain resonance assignments of Haloferax volcanii DHFR1
Deposition date:
2005-05-23
Original release date:
2005-12-14
Authors:
Binbuga, Bulent; Young, John
Citation:

Citation: Binbuga, Bulent; Young, John. "1H, 13C and 15N backbone and side chain resonance assignments of Haloferax volcanii DHFR1"  J. Biomol. NMR 33, 281-281 (2005).
PubMed: 16341756

Assembly members:

Assembly members:
Haloferax volcanii Dihydrofolate reductase (hv-DHFR1), polymer, 162 residues, 17195 Da.

Natural source:

Natural source:   Common Name: Haloferax volcanii   Taxonomy ID: 2246   Superkingdom: Archaea   Kingdom: not available   Genus/species: Haloferax volcanii

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pET-11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Haloferax volcanii Dihydrofolate reductase (hv-DHFR1): MELVSVAALAENRVIGRDGE LPWPSIPADKKQYRSRVADD PVVLGRTTFESMRDDLPGSA QIVMSRSERSFSVDTAHRAA SVEEAVDIAASLDAETAYVI GGAAIYALFQPHLDRMVLSR VPGEYEGDTYYPEWDAAEWE LDAETDHEGFTLQEWVRSAS SR

Data sets:
Data typeCount
13C chemical shifts599
15N chemical shifts147
1H chemical shifts948

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Haloferax_volcanii_Dihydrofolate_reductase1

Entities:

Entity 1, Haloferax_volcanii_Dihydrofolate_reductase 162 residues - 17195 Da.

1   METGLULEUVALSERVALALAALALEUALA
2   GLUASNARGVALILEGLYARGASPGLYGLU
3   LEUPROTRPPROSERILEPROALAASPLYS
4   LYSGLNTYRARGSERARGVALALAASPASP
5   PROVALVALLEUGLYARGTHRTHRPHEGLU
6   SERMETARGASPASPLEUPROGLYSERALA
7   GLNILEVALMETSERARGSERGLUARGSER
8   PHESERVALASPTHRALAHISARGALAALA
9   SERVALGLUGLUALAVALASPILEALAALA
10   SERLEUASPALAGLUTHRALATYRVALILE
11   GLYGLYALAALAILETYRALALEUPHEGLN
12   PROHISLEUASPARGMETVALLEUSERARG
13   VALPROGLYGLUTYRGLUGLYASPTHRTYR
14   TYRPROGLUTRPASPALAALAGLUTRPGLU
15   LEUASPALAGLUTHRASPHISGLUGLYPHE
16   THRLEUGLNGLUTRPVALARGSERALASER
17   SERARG

Samples:

2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7: Haloferax Volcanii Dihydrofolate reductase (hv-DHFR), [U-1H; U-13C; U-15N], 2 mM; NaCl 3.5 mM; Tris buffer 10 mM

3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7: ionic strength: 0.010 M; pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQC (example)2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HNCA2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HN(CO)CA2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HNCACB2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
CBCANH2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HNCO2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HN(CA)CO2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
CCC-TOCSY2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7
HCC-TOCSY2mM_of_hv-DHFR_in_3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7not available3.5_M_NaCl_and_10mM_Tris_buffer_at_pH_7

Software:

NMRDraw -

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15253
PDB
GB AAA72219 ADE04659 ELK54743 ELY28035 ELZ74269
REF WP_004043660 WP_004063628 YP_003535331
SP P15093
AlphaFold P15093

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