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 15603

Title: SOLUTION NMR STRUCTURE OF LIPOPROTEIN SPR FROM ESCHERICHIA COLI K12. NORTHEAST STRUCTURAL GENOMICS TARGET ER541-37-162   PubMed: 18715016

Authors: Aramini, James; Zhao, Li; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, GVT; Huang, Yuanpeng; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Aramini, James; Rossi, Paolo; Huang, Yuanpeng; Zhao, Li; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Locke, Jessica; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Inouye, Masayori; Montelione, Gaetano. "Solution NMR Structure of the NlpC/P60 Domain of Lipoprotein Spr from Escherichia coli: Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad"  Biochemistry 47, 9715-9717 (2008).

Assembly members:
ER541-37-162, polymer, 136 residues, 15724.854 Da.

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

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

Entity Sequences (FASTA):
ER541-37-162: MNVDVKSRIMDQYADWKGVR YRLGGSTKKGIDCSGFVQRT FREQFGLELPRSTYEQQEMG KSVSRSNLRTGDLVLFRAGS TGRHVGIYIGNNQFVHASTS SGVIISSMNEPYWKKRYNEA RRVLSRSLEHHHHHHH

Data typeCount
13C chemical shifts580
15N chemical shifts135
1H chemical shifts897

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 136 residues - 15724.854 Da.

C-terminal LEHHHHHH purifcation tag starting at residue 163.

1   METASNVALASPVALLYSSERARGILEMET
2   ASPGLNTYRALAASPTRPLYSGLYVALARG
3   TYRARGLEUGLYGLYSERTHRLYSLYSGLY
4   ILEASPCYSSERGLYPHEVALGLNARGTHR
5   PHEARGGLUGLNPHEGLYLEUGLULEUPRO
6   ARGSERTHRTYRGLUGLNGLNGLUMETGLY
7   LYSSERVALSERARGSERASNLEUARGTHR
8   GLYASPLEUVALLEUPHEARGALAGLYSER
9   THRGLYARGHISVALGLYILETYRILEGLY
10   ASNASNGLNPHEVALHISALASERTHRSER
11   SERGLYVALILEILESERSERMETASNGLU
12   PROTYRTRPLYSLYSARGTYRASNGLUALA
13   ARGARGVALLEUSERARGSERLEUGLUHIS
14   HISHISHISHISHISHIS

Samples:

sample_1: ER541-37-162, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_2: ER541-37-162, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_3: ER541-37-162, [U-5% 13C; U-100% 15N], 1.03 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D simultaneous CN NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D simultaneous CN NOESYsample_2isotropicsample_conditions_1
3D CCcoNH TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
HNHAsample_1isotropicsample_conditions_1
2D 1H-13C high res. (L/V stereospecific assignment) (aliph)sample_3isotropicsample_conditions_1
2D 1H-15N hetNOEsample_3isotropicsample_conditions_1
2D 1H-13C high res. (L/V stereospecific assignment) (arom)sample_3isotropicsample_conditions_1
2D 1H-13C HSQC (arom)sample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

VNMR v6.1C, Varian - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - data analysis, peak picking

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA13140 BAA15983 BAB36490 BAG77968 BAI26300
EMBL CAP76677 CAQ32581 CAQ89766 CAQ99102 CAR03606
GB AAC75236 AAG57313 AAN43781 AAN81166 AAP17598
REF NP_311094 NP_416680 NP_708074 WP_000241007 WP_000241008
SP P0AFV4 P0AFV5 P0AFV6 P0AFV7