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 11422

Title: Solution structure of the E. coli ORF135 protein   PubMed: 21553121

Deposition date: 2011-01-01 Original release date: 2013-02-07

Authors: Kawasaki, Kumiko; Mishima, Masaki

Citation: Kawasaki, Kumiko; Yoneyama, Momoko; Murata-Kamiya, Naoko; Harashima, Hideyoshi; Kojima, Chojiro; Ito, Yutaka; Kamiya, Hiroyuki; Mishima, Masaki. "(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein."  Biomol. NMR Assignments ., .-. (2011).

Assembly members:
ORF135 protein, polymer, 140 residues, 15476.681 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
ORF135 protein: GPLGSMKMIEVVAAIIERDG KILLAQRPAQSDQAGLWEFA GGKVEPDESQRQALVRELRE ELGIEATVGEYVASHQREVS GRIIHLHAWHVPDFHGTLQA HEHQALVWCSPEEALQYPLA PADIPLLEAFMALRAARPAD

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts132
1H chemical shifts879

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ORF135 protein1

Entities:

Entity 1, ORF135 protein 140 residues - 15476.681 Da.

1   GLYPROLEUGLYSERMETLYSMETILEGLU
2   VALVALALAALAILEILEGLUARGASPGLY
3   LYSILELEULEUALAGLNARGPROALAGLN
4   SERASPGLNALAGLYLEUTRPGLUPHEALA
5   GLYGLYLYSVALGLUPROASPGLUSERGLN
6   ARGGLNALALEUVALARGGLULEUARGGLU
7   GLULEUGLYILEGLUALATHRVALGLYGLU
8   TYRVALALASERHISGLNARGGLUVALSER
9   GLYARGILEILEHISLEUHISALATRPHIS
10   VALPROASPPHEHISGLYTHRLEUGLNALA
11   HISGLUHISGLNALALEUVALTRPCYSSER
12   PROGLUGLUALALEUGLNTYRPROLEUALA
13   PROALAASPILEPROLEULEUGLUALAPHE
14   METALALEUARGALAALAARGPROALAASP

Samples:

sample_1: ORF135 protein, [U-99% 15N], 1 mM; potassium phosphate 50 mM; potassium chloride 20 mM; DTT 1 mM; EDTA 0.1 mM; H2O 93%; D2O 7%

sample_2: ORF135 protein, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 50 mM; potassium chloride 20 mM; DTT 1 mM; EDTA 0.1 mM; H2O 93%; D2O 7%

sample_3: ORF135 protein, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 50 mM; potassium chloride 20 mM; DTT 1 mM; EDTA 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 70 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
4D HC(CO)NHsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 15N filtered NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

TOPSPIN, Bruker Biospin - collection

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAA15549 BAB35888 BAG77454 BAI25775 BAI30753
EMBL CAP76253 CAQ32233 CAQ98676 CAR03119 CAR13244
GB AAC74829 AAG56745 ABB61654 ABE07431 ABG69708
REF NP_310492 NP_416273 WP_000296338 WP_000781861 WP_000781866
SP P77788

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