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 11522

Title: 1H, 13C and 15N backbone resonance assignments of the monomeric human M-ficolin fibrinogen-like domain secreted by Brevibacillus choshinensis   PubMed: 23708873

Deposition date: 2013-02-22 Original release date: 2013-06-04

Authors: Tanio, Michikazu; Kusunoki, Hideki; Kohno, Toshiyuki

Citation: Tanio, Michikazu; Kusunoki, Hideki; Kohno, Toshiyuki. "1H, 13C and 15N backbone resonance assignments of the monomeric human M-ficolin fibrinogen-like domain secreted by Brevibacillus choshinensis"  Biomol NMR Assign. ., .-. (2013).

Assembly members:
M-ficolin, polymer, 238 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Brevibacillus choshinensis   Vector: pNCMO2

Entity Sequences (FASTA):
M-ficolin: AGSPRNCKDLLDRGYSSSGW HTIYLPDCRPLTVLCDMDTD GGGWTVFQRRMDGSVDFYRD WAAYKQGFGSQLGEFWLGND NIHALTAQGSSELRVDLVDF EGNHQFAKYKSFKVADEAEK YKLVLGAFVGGSAGNSLTGH NNNFFSTKDQDNDVSSSNCA EKFQGAWWYADCHASNLNGL YLMGPHESYANGINWSAAKG YKYSYKVSEMKVRPAFLEQK LISEEDLNSAVDHHHHHH

Data typeCount
13C chemical shifts650
15N chemical shifts208
1H chemical shifts208

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1the monomeric human M-ficolin fibrinogen-like domain1

Entities:

Entity 1, the monomeric human M-ficolin fibrinogen-like domain 238 residues - Formula weight is not available

Residues 112-114 at the N-terminus and 327-350 at the C-terminus are non-native sequances. This is a monomeric mutant of the M-ficolin fibrinogen-like domain.

1   ALAGLYSERPROARGASNCYSLYSASPLEU
2   LEUASPARGGLYTYRSERSERSERGLYTRP
3   HISTHRILETYRLEUPROASPCYSARGPRO
4   LEUTHRVALLEUCYSASPMETASPTHRASP
5   GLYGLYGLYTRPTHRVALPHEGLNARGARG
6   METASPGLYSERVALASPPHETYRARGASP
7   TRPALAALATYRLYSGLNGLYPHEGLYSER
8   GLNLEUGLYGLUPHETRPLEUGLYASNASP
9   ASNILEHISALALEUTHRALAGLNGLYSER
10   SERGLULEUARGVALASPLEUVALASPPHE
11   GLUGLYASNHISGLNPHEALALYSTYRLYS
12   SERPHELYSVALALAASPGLUALAGLULYS
13   TYRLYSLEUVALLEUGLYALAPHEVALGLY
14   GLYSERALAGLYASNSERLEUTHRGLYHIS
15   ASNASNASNPHEPHESERTHRLYSASPGLN
16   ASPASNASPVALSERSERSERASNCYSALA
17   GLULYSPHEGLNGLYALATRPTRPTYRALA
18   ASPCYSHISALASERASNLEUASNGLYLEU
19   TYRLEUMETGLYPROHISGLUSERTYRALA
20   ASNGLYILEASNTRPSERALAALALYSGLY
21   TYRLYSTYRSERTYRLYSVALSERGLUMET
22   LYSVALARGPROALAPHELEUGLUGLNLYS
23   LEUILESERGLUGLUASPLEUASNSERALA
24   VALASPHISHISHISHISHISHIS

Samples:

sample_1: M-ficolin, [U-13C; U-15N; U-2H], 0.02 – 0.65 mM; H2O 90%; D2O, [U-2H], 10%; MES 10 mM; sodium chloride 50 mM; calcium chloride 5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY HSQCsample_1isotropicsample_conditions_1
3D TROSY HNCACBsample_1isotropicsample_conditions_1
3D TROSY HN(COCA)CBsample_1isotropicsample_conditions_1
3D TROSY HNCAsample_1isotropicsample_conditions_1
3D TROSY HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1
3D TROSY HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAA12120 BAG37382
GB AAB50706 AAH20635 ABM82352 ABM85362 AIC54383
REF NP_001994 XP_004048886
SP O00602

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