BMRB Entry 7270

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR7270
MolProbity Validation Chart

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Title:
1H, 13C, 15N sequence-specific backbone and sidechain resonance assignments for a putative protein-protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens
Deposition date:
2006-08-18
Original release date:
2007-06-27
Authors:
Chitayat, Seth; Ficko-Blean, Elizabeth; Adams, Jarrett; Gregg, Katie; Boraston, Alisdair; Smith, Steven
Citation:

Citation: Chitayat, Seth; Ficko-Blean, Elizabeth; Adams, Jarrett; Gregg, Katie; Boraston, Alisdair; Smith, Steven. "NMR assignment of backbone and side chain resonances for a putative protein-protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens"  Biomol. NMR Assignments 1, 7-9 (2007).
PubMed: 19636812

Assembly members:

Assembly members:
x82, polymer, 165 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Clostridium Perfringens   Taxonomy ID: 1502   Superkingdom: Eubacteria   Kingdom: Not applicable   Genus/species: Clostridium Perfringens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
x82: MGSSHHHHHHSSGLVPRGSH MASKLKEAAEVTGSVSLEAL EEVQVGENLEVGVGIDELVN AEAFAYDFTLNYDENAFEYV EAISDDGVFVNAKKIEDGKV RVLVSSLTGEPLPAKEVLAK VVLRAEAKAEGSNLSVTNSS VGDGEGLVHEIAGTEKTVNI IEGTS

Data sets:
Data typeCount
13C chemical shifts566
15N chemical shifts156
1H chemical shifts968

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1scaffold protein x821

Entities:

Entity 1, scaffold protein x82 165 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERLYSLEULYSGLUALAALAGLU
4   VALTHRGLYSERVALSERLEUGLUALALEU
5   GLUGLUVALGLNVALGLYGLUASNLEUGLU
6   VALGLYVALGLYILEASPGLULEUVALASN
7   ALAGLUALAPHEALATYRASPPHETHRLEU
8   ASNTYRASPGLUASNALAPHEGLUTYRVAL
9   GLUALAILESERASPASPGLYVALPHEVAL
10   ASNALALYSLYSILEGLUASPGLYLYSVAL
11   ARGVALLEUVALSERSERLEUTHRGLYGLU
12   PROLEUPROALALYSGLUVALLEUALALYS
13   VALVALLEUARGALAGLUALALYSALAGLU
14   GLYSERASNLEUSERVALTHRASNSERSER
15   VALGLYASPGLYGLUGLYLEUVALHISGLU
16   ILEALAGLYTHRGLULYSTHRVALASNILE
17   ILEGLUGLYTHRSER

Samples:

sample_1: x82, [U-13C; U-15N], 1 mM

conditions_1: pH: 7.0; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D CBCACONHnot availablenot availablenot available
3D HCCH-TOCSYnot availablenot availablenot available
3D HC(CO)NHnot availablenot availablenot available
3D C(CO)NHnot availablenot availablenot available
3D aliphatic C13-NOESY-HSQCnot availablenot availablenot available
3D N15-NOESY-HSQCnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HNHAnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Varian Inova 600 MHz
  • Varian Inova 800 MHz

Related Database Links:

PDB
DBJ BAB80940
GB ABG84519 EDT24402 EDT27538 EDT72983 EDT78323
REF NP_562150 WP_003456570 WP_003467250 WP_003471799 WP_003473459
SP Q0TR53 Q8XL08
AlphaFold Q0TR53 Q8XL08

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