BMRB Entry 15403

Title:
Simian Foamy Virus (mac) protease structure
Deposition date:
2007-07-23
Original release date:
2007-09-24
Authors:
Hartl, Maximilian; Schweimer, Kristian; Woehrl, Birgitta
Citation:

Citation: Hartl, Maximilian; Wohrl, Birgitta; Schweimer, Kristian. "Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus"  Biomol. NMR Assignments 1, 175-177 (2007).
PubMed: 19636858

Assembly members:

Assembly members:
SFVmac_Pol_1-101_6His, polymer, 107 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: simian foamy virus   Taxonomy ID: 11642   Superkingdom: Viruses   Kingdom: not available   Genus/species: Spumavirus simian foamy virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28c

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts442
15N chemical shifts94
1H chemical shifts698

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SFVmac Pol 1-101 6His1

Entities:

Entity 1, SFVmac Pol 1-101 6His 107 residues - Formula weight is not available

1   METASPPROLEUGLNLEULEUGLNPROLEU
2   GLUALAGLUILELYSGLYTHRLYSLEULYS
3   ALAHISTRPASPSERGLYALATHRILETHR
4   CYSVALPROGLUALAPHELEUGLUASPGLU
5   ARGPROILEGLNTHRMETLEUILELYSTHR
6   ILEHISGLYGLULYSGLNGLNASPVALTYR
7   TYRLEUTHRPHELYSVALGLNGLYARGLYS
8   VALGLUALAGLUVALLEUALASERPROTYR
9   ASPTYRILELEULEUASNPROSERASPVAL
10   PROTRPLEUMETLYSLYSPROLEUGLNLEU
11   THRHISHISHISHISHISHIS

Samples:

sample_1: SFVmac Pol 1-101 6His, [U-100% 13C; U-100% 15N], 1 mM; phosphate buffer 7.4 50 mM; NaCl 100 mM; DTT mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
EMBL CAA41394
GB AGM61336
PIR S18738
REF YP_001961122
SP P23074
AlphaFold P23074

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