BMRB Entry 17381

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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/BMR17381
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for a putative surface protein
Deposition date:
2010-12-24
Original release date:
2012-02-29
Authors:
Wang, Tao
Citation:

Citation: Wang, Tao. "1H and 15N Assigned Chemical Shifts for a putative surface protein"  .

Assembly members:

Assembly members:
putative_surface_protein, polymer, 97 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus pneumoniae   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-22(b+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
putative_surface_protein: SPKTILGIEVSQEPKKDYLV GDSLDLSEGRFAVAYSNDTM EEHSFTDEGVEISGYDAQKT GRQTLTLHYQGHEVSFDVLV SPKAALNDELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts228
15N chemical shifts84
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1putative surface protein1

Entities:

Entity 1, putative surface protein 97 residues - Formula weight is not available

1   SERPROLYSTHRILELEUGLYILEGLUVAL
2   SERGLNGLUPROLYSLYSASPTYRLEUVAL
3   GLYASPSERLEUASPLEUSERGLUGLYARG
4   PHEALAVALALATYRSERASNASPTHRMET
5   GLUGLUHISSERPHETHRASPGLUGLYVAL
6   GLUILESERGLYTYRASPALAGLNLYSTHR
7   GLYARGGLNTHRLEUTHRLEUHISTYRGLN
8   GLYHISGLUVALSERPHEASPVALLEUVAL
9   SERPROLYSALAALALEUASNASPGLULEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: putative surface protein, [U-99% 13C; U-99% 15N], 0.7 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB
EMBL CEX10252 CIR31810 CIV87805 CKF09277 CKH75363
GB EHD61255 EJG57305
REF WP_055387523

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