BMRB Entry 15105

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15105
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of the first Clip domain in PAP2 (CASP Target)
Deposition date:
2007-01-22
Original release date:
2008-06-25
Authors:
Huang, R.; Lv, Z.; Dai, H.; Velde, D.; Prakash, O.; Jiang, H.
Citation:

Citation: Huang, R.; Lu, Z.; Dai, H.; Velde, D.; Prakash, O.; Jiang, H.. "The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2"  Biochemistry 46, 11431-11439 (2007).
PubMed: 17880110

Assembly members:

Assembly members:
Prophenoloxidase_activating_proteinase-2, polymer, 66 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Tobacco hawkmoth   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prophenoloxidase_activating_proteinase-2: MHHHHHHAMGQACTLPNNDK GTCKSLLQCDVASKIISKKP RTAQDEKFLRESACGFDGQT PKVCCP

Data sets:
Data typeCount
13C chemical shifts213
15N chemical shifts50
1H chemical shifts333

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1clip domain1

Entities:

Entity 1, clip domain 66 residues - Formula weight is not available

1   METHISHISHISHISHISHISALAMETGLY
2   GLNALACYSTHRLEUPROASNASNASPLYS
3   GLYTHRCYSLYSSERLEULEUGLNCYSASP
4   VALALASERLYSILEILESERLYSLYSPRO
5   ARGTHRALAGLNASPGLULYSPHELEUARG
6   GLUSERALACYSGLYPHEASPGLYGLNTHR
7   PROLYSVALCYSCYSPRO

Samples:

sample: Prophenoloxidase activating proteinase-2, [U-100% 13C; U-100% 15N], 1.0 mM; phosphate buffer 100 mM

sample_conditions_1: pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_15N-separated_NOESYsampleisotropicsample_conditions_1

Software:

xwinnmr, Bruker - collection

SPARKY, Goddard - data analysis

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

CNS v2.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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