BMRB Entry 15369

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15369

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Title:
Maize Ribosome-Inactivating protein (MOD)
Deposition date:
2007-07-07
Original release date:
2007-10-16
Authors:
Yang, Yinhua; Mak, Amanda Nga-Sze; Shaw, Pang-Chui; SZE, Kong Hung
Citation:

Citation: Yang, Yinhua; Mak, Amanda Nga-Sze; Shaw, Pang-Chui; Sze, Kong Hung. "(1)H, (13)C and (15)N backbone and side chain resonance assignments of a 28 kDa active mutant of maize ribosome-inactivating protein (MOD)"  Biomol. NMR Assignments 1, 187-189 (2007).
PubMed: 19636861

Assembly members:

Assembly members:
MOD, polymer, 248 residues, 27859 Da.

Natural source:

Natural source:   Common Name: Zea mays   Taxonomy ID: 4577   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Zea mays

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MOD: MKRIVPKFTEIFPVEDANYP YSAFIASVRKDVIKHCTDHK GIFQPVLPPEKKVPELWLYT ELKTRTSSITLAIRMDNLYL VGFRTPGGVWWEFGKDGDTH LLGDNPRWLGFGGRYQDLIG NKGLETVTMGRAEMTRAVND LAKKKKMLEPQADTKSKLVK LVVMVCEGLRFNTVSRTVDA GFNSQHGVTLTVTQGKQVQK WDRISKAAFEWADHPTAVIP DMQKLGIKDKNEAARIVALV KNQTTAAA

Data sets:
Data typeCount
13C chemical shifts1009
15N chemical shifts241
1H chemical shifts1728

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1maize ribosome-inactivating proteins (RIP)1

Entities:

Entity 1, maize ribosome-inactivating proteins (RIP) 248 residues - 27859 Da.

1   METLYSARGILEVALPROLYSPHETHRGLU
2   ILEPHEPROVALGLUASPALAASNTYRPRO
3   TYRSERALAPHEILEALASERVALARGLYS
4   ASPVALILELYSHISCYSTHRASPHISLYS
5   GLYILEPHEGLNPROVALLEUPROPROGLU
6   LYSLYSVALPROGLULEUTRPLEUTYRTHR
7   GLULEULYSTHRARGTHRSERSERILETHR
8   LEUALAILEARGMETASPASNLEUTYRLEU
9   VALGLYPHEARGTHRPROGLYGLYVALTRP
10   TRPGLUPHEGLYLYSASPGLYASPTHRHIS
11   LEULEUGLYASPASNPROARGTRPLEUGLY
12   PHEGLYGLYARGTYRGLNASPLEUILEGLY
13   ASNLYSGLYLEUGLUTHRVALTHRMETGLY
14   ARGALAGLUMETTHRARGALAVALASNASP
15   LEUALALYSLYSLYSLYSMETLEUGLUPRO
16   GLNALAASPTHRLYSSERLYSLEUVALLYS
17   LEUVALVALMETVALCYSGLUGLYLEUARG
18   PHEASNTHRVALSERARGTHRVALASPALA
19   GLYPHEASNSERGLNHISGLYVALTHRLEU
20   THRVALTHRGLNGLYLYSGLNVALGLNLYS
21   TRPASPARGILESERLYSALAALAPHEGLU
22   TRPALAASPHISPROTHRALAVALILEPRO
23   ASPMETGLNLYSLEUGLYILELYSASPLYS
24   ASNGLUALAALAARGILEVALALALEUVAL
25   LYSASNGLNTHRTHRALAALAALA

Samples:

sample_1: MOD, [U-99% 13C; U-99% 15N], 1.5 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
(HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-aromaticsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks