BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27725

Title: 1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli   PubMed: 30684235

Deposition date: 2018-12-12 Original release date: 2019-02-07

Authors: Jia, Moye; Hu, Yunfei; Jin, Changwen

Citation: Jia, Moye; Hu, Yunfei; Jin, Changwen. "1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli"  Biomol. NMR Assignments 13, 183-186 (2019).

Assembly members:
SurA_P2, polymer, 115 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
SurA_P2: MKNISVTEVHARHILLKPSP IMTDEQARVKLEQIAADIKS GKTTFAAAAKEFSQDPGSAN QGGDLGWATPDIFDPAFRDA LTRLNKGQMSAPVHSSFGWH LIELLDTRNVDKTDA

Data sets:
Data typeCount
13C chemical shifts495
15N chemical shifts116
1H chemical shifts776

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SurA_P21

Entities:

Entity 1, SurA_P2 115 residues - Formula weight is not available

The first Met residue is artificially added at the N-terminus of the recombinant protein. K278-A391 is the remainder based on Uniprot P0ABZ6.

1   METLYSASNILESERVALTHRGLUVALHIS
2   ALAARGHISILELEULEULYSPROSERPRO
3   ILEMETTHRASPGLUGLNALAARGVALLYS
4   LEUGLUGLNILEALAALAASPILELYSSER
5   GLYLYSTHRTHRPHEALAALAALAALALYS
6   GLUPHESERGLNASPPROGLYSERALAASN
7   GLNGLYGLYASPLEUGLYTRPALATHRPRO
8   ASPILEPHEASPPROALAPHEARGASPALA
9   LEUTHRARGLEUASNLYSGLYGLNMETSER
10   ALAPROVALHISSERSERPHEGLYTRPHIS
11   LEUILEGLULEULEUASPTHRARGASNVAL
12   ASPLYSTHRASPALA

Samples:

sample_1: SurA_P2, [U-95% 13C; U-95% 15N], 0.6 mM; D2O, [U-99% 2H], 10 % v/v; TRIS 30 mM; sodium chloride 100 mM; DSS 0.01 % w/v

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-COSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

UNP P0ABZ6

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts