BMRB Entry 18734

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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/BMR18734
MolProbity Validation Chart

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Title:
NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799
Deposition date:
2012-09-21
Original release date:
2012-10-25
Authors:
Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Dutta, Samit
Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799"  .

Assembly members:

Assembly members:
ZP_02034617.1, polymer, 100 residues, 11087.459 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 411467   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudoflavonifractor Pseudoflavonifractor capillosus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ZP_02034617.1: GSHEGEPVVGMDKSLFAGNT VIREITVQPNIGLLYDGMFS GCTALEKLILTGEDPSAYSA GDGLRDGADFLICVPEEALD RYRRDYFWQTYAAWIQPMEQ

Data sets:
Data typeCount
13C chemical shifts315
15N chemical shifts100
1H chemical shifts673

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ZP_02034617.11

Entities:

Entity 1, ZP_02034617.1 100 residues - 11087.459 Da.

1   GLYSERHISGLUGLYGLUPROVALVALGLY
2   METASPLYSSERLEUPHEALAGLYASNTHR
3   VALILEARGGLUILETHRVALGLNPROASN
4   ILEGLYLEULEUTYRASPGLYMETPHESER
5   GLYCYSTHRALALEUGLULYSLEUILELEU
6   THRGLYGLUASPPROSERALATYRSERALA
7   GLYASPGLYLEUARGASPGLYALAASPPHE
8   LEUILECYSVALPROGLUGLUALALEUASP
9   ARGTYRARGARGASPTYRPHETRPGLNTHR
10   TYRALAALATRPILEGLNPROMETGLUGLN

Samples:

sample_1: ZP_02034617.1, [U-99% 13C; U-99% 15N], 1.2 mM; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

XEASY, Bartels et al. - processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

UNIO, Herrmann and Wuthrich - chemical shift assignment, peak picking, structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB EDN01860
REF WP_006570766

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