BMRB Entry 16583

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16583

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Title:
2J coupling constants in Xylanase from Bacillus agaradhaerens
Deposition date:
2009-10-25
Original release date:
2010-02-08
Authors:
Schmidt, Jurgen; Lohr, Frank
Citation:

Citation: Schmidt, Jurgen; Hua, Yixun; Lohr, Frank. "Correlation of (2)J couplings with protein secondary structure."  Proteins 78, 1544-1562 (2010).
PubMed: 20131375

Assembly members:

Assembly members:
Xylanase, polymer, 207 residues, 23155.6 Da.

Natural source:

Natural source:   Common Name: Bacillus agaradhaerens   Taxonomy ID: 76935   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Bacillus agaradhaerens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Xylanase: MIVTDNSIGNHDGYDYEFWK DSGGSGTMILNHGGTFSAQW NNVNNILFRKGKKFNETQTH QQVGNMSINYGANFQPNGNA YLCVYGWTVDPLVEYYIVDS WGNWRPPGATPKGTITVDGG TYDIYETLRVNQPSIKGIAT FKQYWSVRRSKRTSGTISVS NHFRAWENLGMNMGKMYEVA LTVEGYQSSGSANVYSNTLR INGNPLS

Data sets:
Data typeCount
coupling constants977

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 207 residues - 23155.6 Da.

1   METILEVALTHRASPASNSERILEGLYASN
2   HISASPGLYTYRASPTYRGLUPHETRPLYS
3   ASPSERGLYGLYSERGLYTHRMETILELEU
4   ASNHISGLYGLYTHRPHESERALAGLNTRP
5   ASNASNVALASNASNILELEUPHEARGLYS
6   GLYLYSLYSPHEASNGLUTHRGLNTHRHIS
7   GLNGLNVALGLYASNMETSERILEASNTYR
8   GLYALAASNPHEGLNPROASNGLYASNALA
9   TYRLEUCYSVALTYRGLYTRPTHRVALASP
10   PROLEUVALGLUTYRTYRILEVALASPSER
11   TRPGLYASNTRPARGPROPROGLYALATHR
12   PROLYSGLYTHRILETHRVALASPGLYGLY
13   THRTYRASPILETYRGLUTHRLEUARGVAL
14   ASNGLNPROSERILELYSGLYILEALATHR
15   PHELYSGLNTYRTRPSERVALARGARGSER
16   LYSARGTHRSERGLYTHRILESERVALSER
17   ASNHISPHEARGALATRPGLUASNLEUGLY
18   METASNMETGLYLYSMETTYRGLUVALALA
19   LEUTHRVALGLUGLYTYRGLNSERSERGLY
20   SERALAASNVALTYRSERASNTHRLEUARG
21   ILEASNGLYASNPROLEUSER

Samples:

sample_1: Xylanase, [U-95% 13C; U-95% 15N], 1.5 mM; sodium acetate 10 mM; sodium azide 0.03%; Pefabloc protease inhibitor 50 ug/ml; D2O, [U-2H], 5%; H2O 95%

sample_conditions_1: pH: 5.4; pressure: 1 atm; temperature: 302 K

Experiments:

NameSampleSample stateSample conditions
3D Ca-coupled [15N,1H]-TROSY-HNCOsample_1isotropicsample_conditions_1
2D IPAP-type HN(CO-a/b-NCa-J)-TROSYsample_1isotropicsample_conditions_1
2D IPAP-type HN(a/b-NCO-J)-TROSYsample_1isotropicsample_conditions_1
3D Ha-coupled [15N,1H]-TROSY-iHNCAsample_1isotropicsample_conditions_1
3D quantitative J-correlated [15N,1H]-TROSY-HNCsample_1isotropicsample_conditions_1
2D Cb-coupled [13C,1H]-HSQCsample_1isotropicsample_conditions_1
2D CO-coupled ct-[13C,1H]-HSQCsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection, processing

jeval, JM Schmidt - coupling constant extraction, data analysis, multiplet simulation

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DMX 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 950 MHz

Related Database Links:

BMRB 15908
PDB
GB AEP40122 AEP40123 AEP40124