BMRB Entry 16315

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16315
MolProbity Validation Chart

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Title:
NMR structure of fragment 87-196 from the putative phage integrase IntS of E. coli: Northeast Structural Genomics Consortium target ER652A
Deposition date:
2009-05-25
Original release date:
2012-08-03
Authors:
Cort, John; Ramelot, Theresa; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.V.T.; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR structure of fragment 87-196 from the putative phage integrase IntS of E. coli"  .

Assembly members:

Assembly members:
fragment 87-196, polymer, 236 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. Coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fragment 87-196: SSNNNSFSAIYKEWYEHKKQ VWSVGYATELAKMFDDDILP IIGGLEIQDIEPMQLLEVIR RFEDRGAMERANKARRRCGE VFRYAIVTGRAKYNPAPDLA DAMKGYRKKNLEHHHHHHSS NNNSFSAIYKEWYEHKKQVW SVGYATELAKMFDDDILPII GGLEIQDIEPMQLLEVIRRF EDRGAMERANKARRRCGEVF RYAIVTGRAKYNPAPDLADA MKGYRKKNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts492
15N chemical shifts124
1H chemical shifts721

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1fragment 87-1961

Entities:

Entity 1, fragment 87-196 236 residues - Formula weight is not available

1   SERSERASNASNASNSERPHESERALAILE
2   TYRLYSGLUTRPTYRGLUHISLYSLYSGLN
3   VALTRPSERVALGLYTYRALATHRGLULEU
4   ALALYSMETPHEASPASPASPILELEUPRO
5   ILEILEGLYGLYLEUGLUILEGLNASPILE
6   GLUPROMETGLNLEULEUGLUVALILEARG
7   ARGPHEGLUASPARGGLYALAMETGLUARG
8   ALAASNLYSALAARGARGARGCYSGLYGLU
9   VALPHEARGTYRALAILEVALTHRGLYARG
10   ALALYSTYRASNPROALAPROASPLEUALA
11   ASPALAMETLYSGLYTYRARGLYSLYSASN
12   LEUGLUHISHISHISHISHISHISSERSER
13   ASNASNASNSERPHESERALAILETYRLYS
14   GLUTRPTYRGLUHISLYSLYSGLNVALTRP
15   SERVALGLYTYRALATHRGLULEUALALYS
16   METPHEASPASPASPILELEUPROILEILE
17   GLYGLYLEUGLUILEGLNASPILEGLUPRO
18   METGLNLEULEUGLUVALILEARGARGPHE
19   GLUASPARGGLYALAMETGLUARGALAASN
20   LYSALAARGARGARGCYSGLYGLUVALPHE
21   ARGTYRALAILEVALTHRGLYARGALALYS
22   TYRASNPROALAPROASPLEUALAASPALA
23   METLYSGLYTYRARGLYSLYSASNLEUGLU
24   HISHISHISHISHISHIS

Samples:

sample_1: H2O 95%; D2O, [U-2H], 5%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [biosynthetically directed 5%C; U-99% 15N], 0.95 mM

sample_2: D2O, [U-2H], 100%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [U-99% 13C; U-99% 15N], 1.2 mM

sample_3: D2O, [U-2H], 100%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [5% 13C; natural abundance, 1.2 mM

sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
4D 1H-13C-13C-1H HMQC-NOESY-HMQCsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

FELIX, Accelrys Software Inc. - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 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