BMRB Entry 15961

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15961
MolProbity Validation Chart

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Title:
Backbone and Side chain 1H, 13C, and 15N Chemical Shift Assignments for Microneme protein 2 Associated protein
Deposition date:
2008-09-24
Original release date:
2009-03-03
Authors:
Liu, Bing; Sawmynaden, Kovilen; Simpson, Pete; Matthews, Steve
Citation:

Citation: Liu, Bing; Sawmynaden, Kovilen; Marchant, Jan; Simpson, Peter; Matthews, Stephen. "Complete resonance assignments for the MIC2 associated protein from Toxoplasma gondii"  Biomol. NMR Assignments 3, 81-83 (2009).
PubMed: 19636952

Assembly members:

Assembly members:
M2AP, polymer, 182 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M2AP: TFLELVEVPCNSVHVQGVMT PNQMVKVTGAGWDNGVLEFY VTRPTKTGGDTSRSHLASIM CYSKDIDGVPSDKAGKCFLK NFSGEDSSEIDEKEVSLPIK SHNDAFMFVCSSNDGSALQC DVFALDNTNSSDGWKVNTVD LGVSVSPDLAFGLTADGVKV KKLYASSGLTAINDDPSLGC KA

Data sets:
Data typeCount
13C chemical shifts735
15N chemical shifts180
1H chemical shifts1134

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1M2AP1

Entities:

Entity 1, M2AP 182 residues - Formula weight is not available

1   THRPHELEUGLULEUVALGLUVALPROCYS
2   ASNSERVALHISVALGLNGLYVALMETTHR
3   PROASNGLNMETVALLYSVALTHRGLYALA
4   GLYTRPASPASNGLYVALLEUGLUPHETYR
5   VALTHRARGPROTHRLYSTHRGLYGLYASP
6   THRSERARGSERHISLEUALASERILEMET
7   CYSTYRSERLYSASPILEASPGLYVALPRO
8   SERASPLYSALAGLYLYSCYSPHELEULYS
9   ASNPHESERGLYGLUASPSERSERGLUILE
10   ASPGLULYSGLUVALSERLEUPROILELYS
11   SERHISASNASPALAPHEMETPHEVALCYS
12   SERSERASNASPGLYSERALALEUGLNCYS
13   ASPVALPHEALALEUASPASNTHRASNSER
14   SERASPGLYTRPLYSVALASNTHRVALASP
15   LEUGLYVALSERVALSERPROASPLEUALA
16   PHEGLYLEUTHRALAASPGLYVALLYSVAL
17   LYSLYSLEUTYRALASERSERGLYLEUTHR
18   ALAILEASNASPASPPROSERLEUGLYCYS
19   LYSALA

Samples:

sample_1: M2AP, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.9; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB AAK51546 EPR60220 EPT26499 ESS31155 KFG36006
REF XP_002370815
TPE CEL77075

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