BMRB Entry 16962

Title:
1J and 2J coupling constants in human oxidized ERp18
Deposition date:
2010-05-27
Original release date:
2011-01-19
Authors:
Schmidt, Jurgen; Lohr, Frank
Citation:

Citation: Schmidt, Jurgen; Zhou, Shen; Rowe, Michelle; Howard, Mark; Williamson, Richard; Lohr, Frank. "One-bond and two-bond j couplings help annotate protein secondary-structure motifs: J-coupling indexing applied to human endoplasmic reticulum protein ERp18."  Proteins 79, 428-443 (2011).
PubMed: 21117079

Assembly members:

Assembly members:
ERp18, polymer, 157 residues, 17774 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHIA128

Data typeCount
coupling constants1268

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERp11

Entities:

Entity 1, ERp1 157 residues - 17774 Da.

The actual protein sequence is preceded by an N-terminal His-tag (MHHHHHHM).

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:

doubly_labeled: ERp18, [U-95% 13C; U-95% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O, [U-99% 2H], 10%; H2O 90%

singly_labeled: ERp18, [U-95% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D Ca-coupled [15N,1H]-TROSY-HNCOdoubly_labeledisotropicsample_conditions_1
3D [1Ha,13Ca]-multiple-quantum HCAN quantitative J-correlationdoubly_labeledisotropicsample_conditions_1
3D Cb-coupled [15N,1H]-TROSY-HN(CO)CAdoubly_labeledisotropicsample_conditions_1
3D Ca-coupled H(CACO)NHdoubly_labeledisotropicsample_conditions_1
3D Ha-coupled [15N,1H]-TROSY-H(N)COCAdoubly_labeledisotropicsample_conditions_1
3D Ha-coupled [15N,1H]-TROSY-HN(CO)CAdoubly_labeledisotropicsample_conditions_1
2D ct-[13C,1H]-IPAP-HSQCdoubly_labeledisotropicsample_conditions_1
2D IPAP-type HN(CO-a/b-NCa-J)-TROSYdoubly_labeledisotropicsample_conditions_1
2D IPAP-type HN(a/b-NCO-J)-TROSYdoubly_labeledisotropicsample_conditions_1
2D [15N,1H]-IPAP-HSQCsingly_labeledisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

jeval, JM Schmidt - coupling constant extraction, data analysis, multiplet simulation

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 500 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 15964
PDB
DBJ BAG52132
GB AAD20035 AAH01493 AAH08913 AAH08953 AAN34781
REF NP_001253090 NP_056997 XP_001110583 XP_002915769 XP_003364421
SP O95881
AlphaFold O95881