BMRB Entry 25983

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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/BMR25983
MolProbity Validation Chart

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Title:
Solution NMR structure of ligand free sterol carrier protein 2 like 2 from Aedes aegypti
Deposition date:
2016-03-07
Original release date:
2017-03-02
Authors:
Singarapu, Kiran; Ummanni, Ramesh
Citation:

Citation: Singarapu, Kiran; Ahuja, Ashish; Potula, Purushotam; Ummanni, Ramesh. "Solution Nuclear Magnetic Resonance Studies of Sterol Carrier Protein 2 Like 2 (SCP2L2) Reveal the Insecticide Specific Structural Characteristics of SCP2 Proteins in Aedes aegypti Mosquitoes"  Biochemistry 55, 4919-4927 (2016).
PubMed: 27508310

Assembly members:

Assembly members:
entity, polymer, 111 residues, 11940.874 Da.

Natural source:

Natural source:   Common Name: mosquitos   Taxonomy ID: 7159   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Aedes aegypti

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEt29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MSVETIIERIKARVGAVDPN GPRKVLGVFQLNIKTASGVE QWIVDLKQLKVDQGVFASPD VTVTVGLEDMLAISGKTLTV GDALKQGKIELSGDADLAAK LAEVIHHHHHH

Data sets:
Data typeCount
13C chemical shifts355
15N chemical shifts110
1H chemical shifts752

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 111 residues - 11940.874 Da.

1   METSERVALGLUTHRILEILEGLUARGILE
2   LYSALAARGVALGLYALAVALASPPROASN
3   GLYPROARGLYSVALLEUGLYVALPHEGLN
4   LEUASNILELYSTHRALASERGLYVALGLU
5   GLNTRPILEVALASPLEULYSGLNLEULYS
6   VALASPGLNGLYVALPHEALASERPROASP
7   VALTHRVALTHRVALGLYLEUGLUASPMET
8   LEUALAILESERGLYLYSTHRLEUTHRVAL
9   GLYASPALALEULYSGLNGLYLYSILEGLU
10   LEUSERGLYASPALAASPLEUALAALALYS
11   LEUALAGLUVALILEHISHISHISHISHIS
12   HIS

Samples:

sample_1: entity, [U-100% 15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.7 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - refinement

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

PSVS, Bhattacharya and Montelione - geometry optimization

SPARKY, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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