BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16251

Title: Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus, Northeast Structural Genomics Consortium Target SyR103B

Authors: Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
syr103b_protein, polymer, 110 residues, 13529.361 Da.

Natural source:   Common Name: Staphyloccus saprophyticus   Taxonomy ID: 29385   Superkingdom: Bacteria   Kingdom: not available   Genus/species: staphylococcus saprophyticus

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

Entity Sequences (FASTA):
syr103b_protein: MITFADYFYQWYEVNKLPHV SESTKRHYESAYKHIKDHFR HKLLKDIKRTEYQKFLNEYG LTHSYETIRKLNSYIRNAFD DAIHEGYVIKNPTYKAELHA SVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts480
15N chemical shifts118
1H chemical shifts781

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1syr103b1

Entities:

Entity 1, syr103b 110 residues - 13529.361 Da.

Residues 2-102 correspond to the 59-159 fragment of the native protein. Residues 103-110 represent a non-native affinity tag, and residue 1 is a result of a new transcription initiation site

1   METILETHRPHEALAASPTYRPHETYRGLN
2   TRPTYRGLUVALASNLYSLEUPROHISVAL
3   SERGLUSERTHRLYSARGHISTYRGLUSER
4   ALATYRLYSHISILELYSASPHISPHEARG
5   HISLYSLEULEULYSASPILELYSARGTHR
6   GLUTYRGLNLYSPHELEUASNGLUTYRGLY
7   LEUTHRHISSERTYRGLUTHRILEARGLYS
8   LEUASNSERTYRILEARGASNALAPHEASP
9   ASPALAILEHISGLUGLYTYRVALILELYS
10   ASNPROTHRTYRLYSALAGLULEUHISALA
11   SERVALLEUGLUHISHISHISHISHISHIS

Samples:

NC: syr103b_protein, [U-100% 13C; U-100% 15N], 0.69 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90.00%; D2O 10.00%

NC5: syr103b_protein, [U-5% 13C; U-100% 15N], 0.6 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90.00%; D2O 10.00%

sample_conditions_1: ionic strength: 0.215 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D 1H-15N,13C NOESYNCisotropicsample_conditions_1
3D 1H-13C NOESYNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
3D HCCH-COSY aromaticNCisotropicsample_conditions_1
2D 1H-15N LR-HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D MEXICONCisotropicsample_conditions_1
2D CLEANEXNCisotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CSI v2.0, Wishart and Sykes - data analysis

TALOS v2007.068.09.07, Shen, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure validation

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAE19092
REF WP_011303617 WP_019469479