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 15964

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15964
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution structure of Oxidised ERp18   PubMed: 19361226

Deposition date: 2008-09-25 Original release date: 2009-04-22

Authors: Rowe, Michelle; Alanen, Heli; Ruddock, Lloyd; Kelly, Geoff; Schmidt, Jurgen; Williamson, Richard; Howard, Mark

Citation: Rowe, Michelle; Ruddock, Lloyd; Kelly, Geoff; Schmidt, Jurgen; Williamson, Richard; Howard, Mark. "Solution Structure and Dynamics of ERp18: a Small ER Resident Oxidoreductase"  Biochemistry 48, 4596-4606 (2009).

Assembly members:
ERp18, polymer, 157 residues, 17771 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
ERp18: MHHHHHHMSDGHNGLGKGFG DHIHWRTLEDGKKEAAASGL PLMVIIHKSWCGACKALKPK FAESTEISELSHNFVMVNLE DEEEPKDEDFSPDGGYIPRI LFLDPSGKVHPEIINENGNP SYKYFYVSAEQVVQGMKEAQ ERLTGDAFRKKHLEDEL

Data sets:
Data typeCount
13C chemical shifts589
15N chemical shifts149
1H chemical shifts1022

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERp181

Entities:

Entity 1, ERp18 157 residues - 17771 Da.

Residues 1-8 represent a non-native affinity tag

1   METHISHISHISHISHISHISMETSERASP
2   GLYHISASNGLYLEUGLYLYSGLYPHEGLY
3   ASPHISILEHISTRPARGTHRLEUGLUASP
4   GLYLYSLYSGLUALAALAALASERGLYLEU
5   PROLEUMETVALILEILEHISLYSSERTRP
6   CYSGLYALACYSLYSALALEULYSPROLYS
7   PHEALAGLUSERTHRGLUILESERGLULEU
8   SERHISASNPHEVALMETVALASNLEUGLU
9   ASPGLUGLUGLUPROLYSASPGLUASPPHE
10   SERPROASPGLYGLYTYRILEPROARGILE
11   LEUPHELEUASPPROSERGLYLYSVALHIS
12   PROGLUILEILEASNGLUASNGLYASNPRO
13   SERTYRLYSTYRPHETYRVALSERALAGLU
14   GLNVALVALGLNGLYMETLYSGLUALAGLN
15   GLUARGLEUTHRGLYASPALAPHEARGLYS
16   LYSHISLEUGLUASPGLULEU

Samples:

Oxidised_15N_ERp18: ERp18, [U-99% 15N], 0.7-1.5 mM; sodium phosphate 20 mM; sodium chloride 100%; D2O 10%

Oxidised_13C_15N_ERp18: ERp18, [U-99% 13C; U-99% 15N], 1-1.5 mM; sodium phosphate 20 mM; sodium chloride 100%; D2O 10%

Oxidised_ERp18_in_D2O: ERp18, [U-99% 13C; U-99% 15N], 0.7-1.5 mM; sodium phosphate 20 mM; sodium chloride 100%; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCOxidised_15N_ERp18isotropicsample_conditions_1
2D 1H-13C HSQCOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D CBCA(CO)NHOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HNCACBOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HBHA(CO)NHOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HBHANHOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HNCOOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D C(CO)NHOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HCCH-TOCSYOxidised_13C_15N_ERp18isotropicsample_conditions_1
3D HCCH-TOCSYOxidised_ERp18_in_D2Oisotropicsample_conditions_1
3D 1H-15N TOCSYOxidised_15N_ERp18isotropicsample_conditions_1
3D 1H-15N NOESYOxidised_15N_ERp18isotropicsample_conditions_1
3D 1H-13C NOESYOxidised_13C_15N_ERp18isotropicsample_conditions_1

Software:

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

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

CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization, refinement

ProcheckNMR, Laskowski and MacArthur - data analysis, validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16962
PDB
DBJ BAG52132
GB AAD20035 AAH01493 AAH08913 AAH08953 AAN34781
REF NP_001253090 NP_056997 XP_001110583 XP_002915769 XP_003364421
SP O95881

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