BMRB Entry 17942

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17942
MolProbity Validation Chart

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Title:
1H, 13C and 15N resonance assignment of a complex constisting of hDlg/SAP-97 residues 318-406 and HPV type 51 E6 protein residues 141-151
Deposition date:
2011-09-15
Original release date:
2012-03-09
Authors:
Mischo, Andre; Ohlenschlaeger, Oliver; Goerlach, Matthias
Citation:

Citation: Mischo, Andre; Ohlenschlager, Oliver; Ramachandran, Ramadurai; Gorlach, Matthias. "NMR assignment of a PDZ domain in complex with a HPV51 E6 derived N-terminally pyroglutamic acid modified peptide."  Biomol. NMR Assignments 7, 47-49 (2013).
PubMed: 22392342

Assembly members:

Assembly members:
hDlg, polymer, 97 residues, Formula weight is not available
E6_protein_fragment_of_HPV_type_51, polymer, 11 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: pET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hDlg: MEIKLIKGPKGLGFSIAGGV GNQHIPGDNSIYVTKIIEGG AAHKDGKLQIGDKLLAVNNV CLEEVTHEEAVTALKNTSDF VYLKVAKPTGSHHHHHH
E6_protein_fragment_of_HPV_type_51: XRTRQRNETQV

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts111
1H chemical shifts737

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ domain1
2peptide2

Entities:

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

Sequence starts with M318. Residues 407-411 represent chemical shifts from a linker and hexahistideine tag (starting with GSHH...)

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

Entity 2, peptide 11 residues - Formula weight is not available

residue 141 (first residue in sequence) exists as pyroglutamic acid (PGL)

1   PCAARGTHRARGGLNARGASNGLUTHRGLN
2   VAL

Samples:

sample_1: hDlg, [U-100% 13C; U-100% 15N], 0.8 mM; E6 protein fragment of HPV type 51 2 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%

sample_2: hDlg, [U-100% 13C; U-100% 15N], 0.8 mM; E6 protein fragment of HPV type 51 2 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%

sample_3: hDlg 3 mM; E6 protein fragment of HPV type 51, [U-100% 13C; U-100% 15N], 1.25 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%

sample_4: hDlg 3 mM; E6 protein fragment of HPV type 51, [U-100% 13C; U-100% 15N], 1.25 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Rochus Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15209 17373
PDB
REF XP_012432549
UNP P26554

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