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 15105

Title: Solution Structure of the first Clip domain in PAP2 (CASP Target)   PubMed: 17880110

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: 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).

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

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

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

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts