BMRB Entry 15209

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15209

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Title:
Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide
Deposition date:
2007-04-10
Original release date:
2007-10-24
Authors:
Liu, Y.; Baleja, J.; Henry, G.; Hegde, R.
Citation:

Citation: Liu, Y.; Henry, G.; Hegde, R.; Baleja, J.. "Solution Structure of the hDLG/SAP97 PDZ2 domain and its mechanism for interaction with HPV-18 papillomavirus E6 protein"  Biochemistry 46, 10864-10874 (2007).

Assembly members:

Assembly members:
Disks_large_homolog_1, polymer, 97 residues, Formula weight is not available
C-terminal_HPV-18_E6_peptide, polymer, 6 residues, Formula weight is not available

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: pET30a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Disks_large_homolog_1: MEIKLIKGPKGLGFSIAGGV GNQHIPGDNSIYVTKIIEGG AAHKDGKLQIGDKLLAVNNV CLEEVTHEEAVTALKNTSDF VYLKVAKPTGSHHHHHH
C-terminal_HPV-18_E6_peptide: RRETQV

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts93
1H chemical shifts662

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hDlg PDZ2 domain1
2E6CT2

Entities:

Entity 1, hDlg PDZ2 domain 97 residues - Formula weight is not available

1   METGLUILELYSLEUILELYSGLYPROLYS
2   GLYLEUGLYPHESERILEALAGLYGLYVAL
3   GLYASNGLNHISILEPROGLYASPASNSER
4   ILETYRVALTHRLYSILEILEGLUGLYGLY
5   ALAALAHISLYSASPGLYLYSLEUGLNILE
6   GLYASPLYSLEULEUALAVALASNASNVAL
7   CYSLEUGLUGLUVALTHRHISGLUGLUALA
8   VALTHRALALEULYSASNTHRSERASPPHE
9   VALTYRLEULYSVALALALYSPROTHRGLY
10   SERHISHISHISHISHISHIS

Entity 2, E6CT 6 residues - Formula weight is not available

1   ARGARGGLUTHRGLNVAL

Samples:

sample_1: Disks large homolog 1 2 mM; C-terminal HPV-18 E6 peptide 3 mM; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_2: Disks large homolog 1, [U-100% 15N], 2 mM; C-terminal HPV-18 E6 peptide 3 mM; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_3: Disks large homolog 1, [U-100% 13C; U-100% 15N], 2 mM; C-terminal HPV-18 E6 peptide 3 mM; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_4: Disks large homolog 1, [U-100% 13C; U-100% 15N], 2 mM; C-terminal HPV-18 E6 peptide 3 mM; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_5: Disks large homolog 1, [U-100% 15N], 2 mM; C-terminal HPV-18 E6 peptide 3 mM; C8E5 5%; n-octanol 5.75%; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_6: Disks large homolog 1, [U-100% 15N], 2 mM; C-terminal HPV-18 E6 peptide 3 mM; Pf1 phage 10 mg/mL; TCEP 4 mM; DSS 20 uM; phosphate buffer 20 mM

sample_conditions_1: ionic strength: 28.2 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_3isotropicsample_conditions_1
HCCH-TOCSYsample_3isotropicsample_conditions_1
HNCACBsample_3isotropicsample_conditions_1
CBCACONHsample_3isotropicsample_conditions_1
HBHA(CO)NHsample_3isotropicsample_conditions_1
CT-13C/1H-HSQCsample_4isotropicsample_conditions_1
HSQC-DSSE (IPAP) for HN RDCsample_5isotropicsample_conditions_1
HSQC-DSSE (IPAP) for HN RDCsample_6isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

SPARKY v3.112, T. D. Goddard and D. G. Kneller - data analysis

CNS v1.1, Brunger - structure solution

NMR spectrometers:

  • Bruker Avance DRX 600 MHz

Related Database Links:

BMRB 17373 17942
PDB
REF XP_012432549

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