BMRB Entry 17694

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17694
MolProbity Validation Chart

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Title:
1H, 15N and 13C backbone and side-chain assignments of a family 32 carbohydrate-binding module (CBM32) from the Clostridium perfringens NagH
Deposition date:
2011-06-08
Original release date:
2011-09-14
Authors:
Grondin, Julie; Chitayat, Seth; Ficko-Blean, Elizabeth; Boraston, Alisdair; Smith, Steven
Citation:

Citation: Grondin, Julie; Chitayat, Seth; Ficko-Blean, Elizabeth; Boraston, Alisdair; Smith, Steven. "1H, 15N and 13C backbone and side-chain resonance assignments of a family 32 carbohydrate-binding module from the Clostridium perfringens NagH."  Biomol. NMR Assignments 6, 139-142 (2012).
PubMed: 21912839

Assembly members:

Assembly members:
GH84A_CBM32-1, polymer, 164 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Clostridium perfringens   Taxonomy ID: 1502   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium perfringens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GH84A_CBM32-1: MGSSHHHHHHSSGLVPRGSH MASDPNRIIATYISNRQDAP TGNPDNIFDNNASTELVYKN PNRIDVGTYVGVKYSNPITL NNVEFLMGANSNPNDTMQKA KIQYTVDGREWIDLEEGVEY TMPGAIKVENLDLKVRGVRL IATEARENTWLGVRDINVNK KEDS

Data sets:
Data typeCount
13C chemical shifts597
15N chemical shifts158
1H chemical shifts980

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1GH84A_CBM32-11

Entities:

Entity 1, GH84A_CBM32-1 164 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERASPPROASNARGILEILEALA
4   THRTYRILESERASNARGGLNASPALAPRO
5   THRGLYASNPROASPASNILEPHEASPASN
6   ASNALASERTHRGLULEUVALTYRLYSASN
7   PROASNARGILEASPVALGLYTHRTYRVAL
8   GLYVALLYSTYRSERASNPROILETHRLEU
9   ASNASNVALGLUPHELEUMETGLYALAASN
10   SERASNPROASNASPTHRMETGLNLYSALA
11   LYSILEGLNTYRTHRVALASPGLYARGGLU
12   TRPILEASPLEUGLUGLUGLYVALGLUTYR
13   THRMETPROGLYALAILELYSVALGLUASN
14   LEUASPLEULYSVALARGGLYVALARGLEU
15   ILEALATHRGLUALAARGGLUASNTHRTRP
16   LEUGLYVALARGASPILEASNVALASNLYS
17   LYSGLUASPSER

Samples:

sample_1: GH84A_CBM32-1, [U-100% 13C; U-100% 15N], 0.8 mM; H20 90%; D20 10%; TRIS 25 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 75 mM; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 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