BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15590

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15590

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Title: Merozoite surface protein 2 in 10 mM HOAc   PubMed: 18440022

Deposition date: 2007-12-11 Original release date: 2008-05-29

Authors: Perugini, Matthew; Yao, Shenggen; Adda, Christopher; Murphy, Vicent; Low, Andrew; Anders, Robin; Norton, Raymond

Citation: Zhang, Xuecheng; Perugini, Matthew; Yao, Shenggen; Adda, Christopher; Murphy, Vicent; Low, Andrew; Anders, Robin; Norton, Raymond. "Solution Conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2"  J. Mol. Biol. 379, 105-121 (2008).

Assembly members:
MSP2, polymer, 222 residues, Formula weight is not available

Natural source:   Common Name: Plasmodium falciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
MSP2: MIKNESKYSNTFINNAYNMS IRRSMANEGSNTNSVGANAP NADTIASGSQRSTNSASTST TNNGESQTTTPTAADTIASG SQRSTNSASTSTTNNGESQT TTPTAADTPTATESNSPSPP ITTTESSSSGNAPNKTDGKG EESEKQNELNESTEEGPRAP QEPQTAENENPAAPENKGTG QHGHMHGSRNNHPQNTSDSQ KECTDGNKENCGAATSLLSN SS

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts204
1H chemical shifts437

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MSP21

Entities:

Entity 1, MSP2 222 residues - Formula weight is not available

1   METILELYSASNGLUSERLYSTYRSERASN
2   THRPHEILEASNASNALATYRASNMETSER
3   ILEARGARGSERMETALAASNGLUGLYSER
4   ASNTHRASNSERVALGLYALAASNALAPRO
5   ASNALAASPTHRILEALASERGLYSERGLN
6   ARGSERTHRASNSERALASERTHRSERTHR
7   THRASNASNGLYGLUSERGLNTHRTHRTHR
8   PROTHRALAALAASPTHRILEALASERGLY
9   SERGLNARGSERTHRASNSERALASERTHR
10   SERTHRTHRASNASNGLYGLUSERGLNTHR
11   THRTHRPROTHRALAALAASPTHRPROTHR
12   ALATHRGLUSERASNSERPROSERPROPRO
13   ILETHRTHRTHRGLUSERSERSERSERGLY
14   ASNALAPROASNLYSTHRASPGLYLYSGLY
15   GLUGLUSERGLULYSGLNASNGLULEUASN
16   GLUSERTHRGLUGLUGLYPROARGALAPRO
17   GLNGLUPROGLNTHRALAGLUASNGLUASN
18   PROALAALAPROGLUASNLYSGLYTHRGLY
19   GLNHISGLYHISMETHISGLYSERARGASN
20   ASNHISPROGLNASNTHRSERASPSERGLN
21   LYSGLUCYSTHRASPGLYASNLYSGLUASN
22   CYSGLYALAALATHRSERLEULEUSERASN
23   SERSER

Samples:

sample_1: MSP2, [U-98% 13C; U-98% 15N], 0.44 mM; acetic acid 10 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%

sample_2: MSP2, [U-98% 15N], 0.35 mM; acetic acid 10 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 10 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, data analysis, processing

XEASY v1.3.13, Bartels et al. - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

EMBL CAA70441
GB AAC02228 AAC37199 AAC38836 AAF25441 AAG47593

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts