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 16456

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16456

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Title: The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site   PubMed: 16815922

Deposition date: 2009-08-19 Original release date: 2010-03-08

Authors: Tossavainen, Helena; Pihalajamaa, Tero; Huttenen, Toni; Raulo, Erkki; Rauvala, Heikki; Permi, Perttu; Kilperlainen, Ilkka

Citation: Tossavainen, Helena; Pihalajamaa, Tero; Huttenen, Toni; Raulo, Erkki; Rauvala, Heikki; Permi, Perttu; Kilperlainen, Ilkka. "The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site"  Protein Sci. 15, 1760-1768 (2006).

Assembly members:
TRAP-TSR, polymer, 49 residues, Formula weight is not available
heparin, polymer, 225 residues, 24745.02 Da.

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

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

Entity Sequences (FASTA):
TRAP-TSR: GSASCGVWDEWSPCSVTCGK GTRSRKREILHEGCTSEIQE QCEEERCPP
heparin: IVGGRKARPRQFPFLASIQN QGRHFCGGALIHARFVMTAA SCFQSQNPGVSTVVLGAYDL RRRERQSRQTFSISSMSENG YDPQQNLNDLMLLQLDREAN LTSSVTILPLPLQNATVEAG TRCQVAGWGSQRSGGRLSRF PRFVNVTVTPEDQCRPNNVC TGVLTRRGGICNGDGGTPLV CEGLAHGVASFSLGPCGRGP DFFTRVALFRDWIDGVLNNP GPGPA

Data sets:
  • assigned_chemical_shifts
  • binding_constants
Data typeCount
binding constants8

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRAP-TSR1
2heparin2

Entities:

Entity 1, TRAP-TSR 49 residues - Formula weight is not available

1   GLYSERALASERCYSGLYVALTRPASPGLU
2   TRPSERPROCYSSERVALTHRCYSGLYLYS
3   GLYTHRARGSERARGLYSARGGLUILELEU
4   HISGLUGLYCYSTHRSERGLUILEGLNGLU
5   GLNCYSGLUGLUGLUARGCYSPROPRO

Entity 2, heparin 225 residues - 24745.02 Da.

1   ILEVALGLYGLYARGLYSALAARGPROARG
2   GLNPHEPROPHELEUALASERILEGLNASN
3   GLNGLYARGHISPHECYSGLYGLYALALEU
4   ILEHISALAARGPHEVALMETTHRALAALA
5   SERCYSPHEGLNSERGLNASNPROGLYVAL
6   SERTHRVALVALLEUGLYALATYRASPLEU
7   ARGARGARGGLUARGGLNSERARGGLNTHR
8   PHESERILESERSERMETSERGLUASNGLY
9   TYRASPPROGLNGLNASNLEUASNASPLEU
10   METLEULEUGLNLEUASPARGGLUALAASN
11   LEUTHRSERSERVALTHRILELEUPROLEU
12   PROLEUGLNASNALATHRVALGLUALAGLY
13   THRARGCYSGLNVALALAGLYTRPGLYSER
14   GLNARGSERGLYGLYARGLEUSERARGPHE
15   PROARGPHEVALASNVALTHRVALTHRPRO
16   GLUASPGLNCYSARGPROASNASNVALCYS
17   THRGLYVALLEUTHRARGARGGLYGLYILE
18   CYSASNGLYASPGLYGLYTHRPROLEUVAL
19   CYSGLUGLYLEUALAHISGLYVALALASER
20   PHESERLEUGLYPROCYSGLYARGGLYPRO
21   ASPPHEPHETHRARGVALALALEUPHEARG
22   ASPTRPILEASPGLYVALLEUASNASNPRO
23   GLYPROGLYPROALA

Samples:

sample_1: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; D2O 6%; H2O 94%

sample_2: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 0.1 mM; D2O 6%; H2O 94%

sample_3: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 0.2 mM; D2O 6%; H2O 94%

sample_4: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 0.3 mM; D2O 6%; H2O 94%

sample_5: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 0.4 mM; D2O 6%; H2O 94%

sample_6: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 0.6 mM; D2O 6%; H2O 94%

sample_7: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 1.25 mM; D2O 6%; H2O 94%

sample_8: TRAP-TSR, [U-13C; U-15N], 0.5 mM; bis-Tris buffer 20 mM; heparin 1.9 mM; D2O 6%; H2O 94%

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1
2D 1H-15N HSQCsample_8isotropicsample_conditions_1

Software:

SPARKY, Goddard - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - energy minimization

ProcheckNMR, Laskowski and MacArthur - data analysis

Molmol, Koradi, Billeter and Wuthrich - visualization

NMR spectrometers:

  • Varian Unity Inova 500 MHz
  • Varian Unity Inova 600 MHz

Related Database Links:

PDB
DBJ BAA31173 BAA31174 BAA31178 BAA31191 BAA31192
EMBL CAA31440 CAE46497 CAA41601
GB AAA29774 AAC18657 AAW78130 AAW78131 AAW78136 AAB59353 AAH44940 AAH69495 AAH93931 AAH93933
PRF 1411304A 1708291A 1617124A
SP P16893 P20160
REF NP_001691 XP_003813807 XP_004059659 XP_009432518 XP_524023