BMRB Entry 19646

Title:
Solution structure of the major factor VIII binding region on von Willebrand factor
Deposition date:
2013-12-02
Original release date:
2014-04-09
Authors:
Shiltagh, Nuha; Kirkpatrick, John; Cabrita, Lisa; McKinnon, Tom; Thalassinos, Konstantinos; Tuddenham, Edward; Hansen, Flemming
Citation:

Citation: Shiltagh, Nuha; Kirkpatrick, John; Cabrita, Lisa; McKinnon, Tom; Thalassinos, Konstantinos; Tuddenham, Edward; Hansen, D. Flemming. "Solution structure of the major factor VIII binding region on von Willebrand factor."  Blood ., .-. (2014).
PubMed: 24700780

Assembly members:

Assembly members:
VWF_TIL-E, polymer, 103 residues, 11351.283 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32b+

Data sets:
Data typeCount
13C chemical shifts287
15N chemical shifts85
1H chemical shifts587

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1major factor VIII binding region on von Willebrand factor1

Entities:

Entity 1, major factor VIII binding region on von Willebrand factor 103 residues - 11351.283 Da.

Residues 1-4 (GAMG) are cloning artefacts. The VWF sequence proper begins at residue 5, and represents residues 766-864 in full-length VWF.

1   GLYALAMETGLYSERCYSARGPROPROMET
2   VALLYSLEUVALCYSPROALAASPASNLEU
3   ARGALAGLUGLYLEUGLUCYSTHRLYSTHR
4   CYSGLNASNTYRASPLEUGLUCYSMETSER
5   METGLYCYSVALSERGLYCYSLEUCYSPRO
6   PROGLYMETVALARGHISGLUASNARGCYS
7   VALALALEUGLUARGCYSPROCYSPHEHIS
8   GLNGLYLYSGLUTYRALAPROGLYGLUTHR
9   VALLYSILEGLYCYSASNTHRCYSVALCYS
10   ARGASPARGLYSTRPASNCYSTHRASPHIS
11   VALCYSASP

Samples:

sample_1: VWF TIL-E, [U-13C; U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: VWF TIL-E, [U-10% 13C], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: VWF TIL-E, [U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_4: VWF TIL-E, [U-13C; U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_5: VWF TIL-E, [U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_6: VWF TIL-E, [U-13C; U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_7: VWF TIL-E, [U-13C; U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; Pf1 phage 5 ± 1 mg/mL; H2O 90%; D2O 10%

sample_8: VWF TIL-E, [U-13C; U-15N], 300 ± 100 mM; sodium phosphate 20 mM; sodium chloride 100 mM; pentaethylene glycol dodecyl ether 2 ± 0.2 % w/v; n-hexanol 50 ± 5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 15N HSQC-NOESY-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CACO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
2D constant-time 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
{1H}15N steady-state NOEsample_3isotropicsample_conditions_1
15N R1rho relaxationsample_3isotropicsample_conditions_1
15N R1 relaxationsample_3isotropicsample_conditions_1
15N R2-CPMG relaxation dispersionsample_5isotropicsample_conditions_1
15N R2-CPMG relaxation dispersionsample_5isotropicsample_conditions_1
2D IPAP-15N HSQCsample_6isotropicsample_conditions_1
2D IPAP-15N HSQCsample_7anisotropicsample_conditions_1
2D IPAP-15N HSQCsample_8anisotropicsample_conditions_1
2D IPAP-E.COSY-15N HSQCsample_6isotropicsample_conditions_1
2D IPAP-E.COSY-15N HSQCsample_8anisotropicsample_conditions_1
3D IPAP-HNCO(J-CA)sample_6isotropicsample_conditions_1
3D IPAP-HNCO(J-CA)sample_8anisotropicsample_conditions_1
3D HN(CO)CA(J-CB)sample_6isotropicsample_conditions_1
3D HN(CO)CA(J-CB)sample_8anisotropicsample_conditions_1
3D IPAP-(HA)CA(CO)NHsample_6isotropicsample_conditions_1
3D IPAP-(HA)CA(CO)NHsample_8anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D constant-time 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
2D constant-time 1H-13C HSQCsample_4isotropicsample_conditions_1

Software:

VNMRJ v2.2D, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance III 500 MHz
  • Bruker Avance III 700 MHz

Related Database Links:

PDB
GB AAB59512

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