BMRB Entry 17481

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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/BMR17481
MolProbity Validation Chart

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Title:
Solution NMR Structure of Q5HLI9 from Staphylococcus epidermidis, Northeast Structural Genomics Consortium Target SeR147
Deposition date:
2011-02-22
Original release date:
2011-05-02
Authors:
Mills, Jeffrey; Eletsky, Alex; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Sapin, Ari; Mao, Lei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Mills, Jeffrey; Eletsky, Alex; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Sapin, Ari; Mao, Lei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Northeast Structural Genomics Consortium Target SeR147"  To be published ., .-..

Assembly members:

Assembly members:
SeR147, polymer, 164 residues, 18778.254 Da.

Natural source:

Natural source:   Common Name: Staphylococcus epidermidis   Taxonomy ID: 1282   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus epidermidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SeR147: MTIEKKKNKIIFTRTFSAPI NKVFDAYTKRELFEQWFHPQ DASVTVYDFNATKGGSAFYA IQAPQMISYTIAEYLQVDAP YYIEYLDYFATSKGEKDTSM PGMHITLNFEEVKGKTTVTS TSTFPTESAAQQAIDMGVET GMNSTLNQLEKLLNQKLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts634
15N chemical shifts155
1H chemical shifts1046

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SeR1471

Entities:

Entity 1, SeR147 164 residues - 18778.254 Da.

1   METTHRILEGLULYSLYSLYSASNLYSILE
2   ILEPHETHRARGTHRPHESERALAPROILE
3   ASNLYSVALPHEASPALATYRTHRLYSARG
4   GLULEUPHEGLUGLNTRPPHEHISPROGLN
5   ASPALASERVALTHRVALTYRASPPHEASN
6   ALATHRLYSGLYGLYSERALAPHETYRALA
7   ILEGLNALAPROGLNMETILESERTYRTHR
8   ILEALAGLUTYRLEUGLNVALASPALAPRO
9   TYRTYRILEGLUTYRLEUASPTYRPHEALA
10   THRSERLYSGLYGLULYSASPTHRSERMET
11   PROGLYMETHISILETHRLEUASNPHEGLU
12   GLUVALLYSGLYLYSTHRTHRVALTHRSER
13   THRSERTHRPHEPROTHRGLUSERALAALA
14   GLNGLNALAILEASPMETGLYVALGLUTHR
15   GLYMETASNSERTHRLEUASNGLNLEUGLU
16   LYSLEULEUASNGLNLYSLEUGLUHISHIS
17   HISHISHISHIS

Samples:

NC: SeR147, [U-100% 13C; U-100% 15N], 0.6 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; H2O 95%; D2O 5%

NC5: SeR147, [U-5% 13C; U-100% 15N], 0.62 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; H2O 95%; D2O 5%

NC5aniso: SeR147, [U-5% 13C; U-100% 15N], 0.41 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.02%; TRIS 10 mM; phage 13.2 mg/mL; H2O 95%; D2O 5%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HCCH-COSYNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5anisoanisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

PROSA, Guntert - processing

CARA, Keller et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CDM14527
GB AAO05627 AAW52927 AIR83241 AJP25447 EES35074
REF NP_765541 WP_001831546 WP_001832905 WP_002438297 WP_002447189

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