BMRB Entry 18600

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18600
MolProbity Validation Chart

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Title:
S67
Deposition date:
2012-07-18
Original release date:
2013-01-09
Authors:
Loening, Nikolaus; Wilson, Zachary; Zobel-Thropp, Pamela; Binford, Greta
Citation:

Citation: Loening, Nikolaus; Wilson, Zachary; Zobel-Thropp, Pamela; Binford, Greta. "Solution Structures of Two Homologous Venom Peptides from Sicarius dolichocephalus."  PLoS ONE 8, e54401-e54401 (2013).
PubMed: 23342149

Assembly members:

Assembly members:
S67, polymer, 36 residues, 4244.7665 Da.

Natural source:

Natural source:   Common Name: Spiders   Taxonomy ID: 571538   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Sicarius dolichocephalus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S67: GTYCIELGERCPNPREGDWC CHKCVPEGKRFYCRDQ

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts49
1H chemical shifts441

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S671

Entities:

Entity 1, S67 36 residues - 4244.7665 Da.

0Gly is an expression artifact

1   GLYTHRTYRCYSILEGLULEUGLYGLUARG
2   CYSPROASNPROARGGLUGLYASPTRPCYS
3   CYSHISLYSCYSVALPROGLUGLYLYSARG
4   PHETYRCYSARGASPGLN

Samples:

13C_15N: S67, [U-98% 15N], 0.2 ± 5e-05 mM; H2O 95%; D2O, [U-2H], 5%

13C_15N-D2O: S67, [U-98% 15N], 0.35 ± 5e-05 mM; D2O, [U-2H], 100%

sample_new_1: S67, [U-13C; U-15N], 0.2 ± 0.05 mM; H2O 95%; D2O, [U-2H], 5%

Standard: ionic strength: 0.020 M; pH: 6.000; pressure: 1.000 atm; temperature: 310.000 K

21min: Time: 21.000 mins

37min: Time: 37.000 mins

54min: Time: 54.000 mins

70min: Time: 70.000 mins

93min: Time: 93.000 mins

117min: Time: 117.000 mins

155min: Time: 155.000 mins

194min: Time: 194.000 mins

330min: Time: 330.000 mins

507min: Time: 507.000 mins

12min: Time: 12.000 mins

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC/HMQC13C_15NisotropicStandard
2D 1H-13C HSQC/HMQC13C_15NisotropicStandard
3D HNCO13C_15NisotropicStandard
HNcaCo (HNcaCO)13C_15NisotropicStandard
HNcoCaCb (H[N[co[{CA|ca[C]}]]])13C_15NisotropicStandard
3D HNCACB13C_15NisotropicStandard
2D 1H-1H NOESY13C_15NisotropicStandard
2D 1H-1H TOCSY13C_15NisotropicStandard
HccoNH (HccoNH)13C_15NisotropicStandard
3D C(CO)NH13C_15NisotropicStandard
2D 1H-15N HSQC/HMQC13C_15NisotropicStandard
3D 1H-15N NOESY13C_15NisotropicStandard
3D 1H-13C NOESY13C_15NisotropicStandard
3D 1H-13C NOESY13C_15NisotropicStandard
3D HCACO13C_15N-D2OisotropicStandard
3D HCCH-TOCSY13C_15N-D2OisotropicStandard
3D 1H-13C NOESY13C_15N-D2OisotropicStandard
2D 1H-13C HSQC/HMQC13C_15N-D2OisotropicStandard
2D 1H-13C HSQC/HMQC13C_15N-D2OisotropicStandard
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic21min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic37min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic54min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic70min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic93min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic117min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic155min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic194min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic330min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic507min
2D 1H-15N HSQC/HMQC13C_15N-D2Oisotropic12min
13C CT-HSQCsample_new_1solutionStandard
13C CT-HSQC AROMATICsample_new_1solutionStandard
HNCACBsample_new_1solutionStandard
HNCOsample_new_1solutionStandard
HNCACOsample_new_1solutionStandard
HNCOCACBsample_new_1solutionStandard
15N HMQCsample_new_1solutionStandard
1H NOESY (120MS)sample_new_1solutionStandard
1H TOCSY (120MS)sample_new_1solutionStandard
CCCONHsample_new_1solutionStandard
HCCONHsample_new_1solutionStandard

Software:

ARIA v2.3.2, Rieping W., Habeck M., Bardiaux B., Bernard A., Malliavin T.E., Nilges M. - NOE assignment, structure calculation

AutoDep v4.3, PDBe - collection

CNS_1.2_PATCH_LEVEL v1, Brunger, Adams, Clore, Gros, Nilges and Read - data analysis

ANALYSIS v2.2, CCPN - chemical shift assignment, project management

TALOS+ v3.60F1, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - protein backbone dihedral angle prediction

TALOSPLUS_3.60F1 vany, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz
  • Bruker DMX, AVANCE 600 MHz

Related Database Links:

PDB

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