BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27078

Title: Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C

Authors: Courtade, Gaston; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincent; Aachmann, Finn

Citation: Courtade, Gaston; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincent; Aachmann, Finn. "Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C"  Biomol. NMR Assign ., .-. (2017).

Assembly members:
N-ScLPMO10C, polymer, 200 residues, Formula weight is not available
ScCBM2, polymer, 112 residues, Formula weight is not available
ScLPMO10C, polymer, 330 residues, Formula weight is not available

Natural source:   Common Name: Streptomyces coelicolor   Taxonomy ID: 1902   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces coelicolor

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

Entity Sequences (FASTA):
N-ScLPMO10C: HGVAMMPGSRTYLCQLDAKT GTGALDPTNPACQAALDQSG ATALYNWFAVLDSNAGGRGA GYVPDGTLCSAGDRSPYDFS AYNAARSDWPRTHLTSGATI PVEYSNWAAHPGDFRVYLTK PGWSPTSELGWDDLELIQTV TNPPQQGSPGTDGGHYYWDL ALPSGRSGDALIFMQWVRSD SQENFFSCSDVVFDGGNGEV
ScCBM2: MHTGSCMAVYSVENSWSGGF QGSVEVMNHGTEPLNGWAVQ WQPGGGTTLGGVWNGSLTSG SDGTVTVRNVDHNRVVPPDG SVTFGFTATSTGNDFPVDSI GCVAPAHHHHHH
ScLPMO10C: HGVAMMPGSRTYLCQLDAKT GTGALDPTNPACQAALDQSG ATALYNWFAVLDSNAGGRGA GYVPDGTLCSAGDRSPYDFS AYNAARSDWPRTHLTSGATI PVEYSNWAAHPGDFRVYLTK PGWSPTSELGWDDLELIQTV TNPPQQGSPGTDGGHYYWDL ALPSGRSGDALIFMQWVRSD SQENFFSCSDVVFDGGNGEV TGIRGSGSTPDPDPTPTPTD PTTPPTHTGSCMAVYSVENS WSGGFQGSVEVMNHGTEPLN GWAVQWQPGGGTTLGGVWNG SLTSGSDGTVTVRNVDHNRV VPPDGSVTFGFTATSTGNDF PVDSIGCVAP

Data typeCount
13C chemical shifts1573
15N chemical shifts463
1H chemical shifts1561

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1N-ScLPMO10C1
2ScCBM22
3ScLPMO10C3

Entities:

Entity 1, N-ScLPMO10C 200 residues - Formula weight is not available

1   HISGLYVALALAMETMETPROGLYSERARG
2   THRTYRLEUCYSGLNLEUASPALALYSTHR
3   GLYTHRGLYALALEUASPPROTHRASNPRO
4   ALACYSGLNALAALALEUASPGLNSERGLY
5   ALATHRALALEUTYRASNTRPPHEALAVAL
6   LEUASPSERASNALAGLYGLYARGGLYALA
7   GLYTYRVALPROASPGLYTHRLEUCYSSER
8   ALAGLYASPARGSERPROTYRASPPHESER
9   ALATYRASNALAALAARGSERASPTRPPRO
10   ARGTHRHISLEUTHRSERGLYALATHRILE
11   PROVALGLUTYRSERASNTRPALAALAHIS
12   PROGLYASPPHEARGVALTYRLEUTHRLYS
13   PROGLYTRPSERPROTHRSERGLULEUGLY
14   TRPASPASPLEUGLULEUILEGLNTHRVAL
15   THRASNPROPROGLNGLNGLYSERPROGLY
16   THRASPGLYGLYHISTYRTYRTRPASPLEU
17   ALALEUPROSERGLYARGSERGLYASPALA
18   LEUILEPHEMETGLNTRPVALARGSERASP
19   SERGLNGLUASNPHEPHESERCYSSERASP
20   VALVALPHEASPGLYGLYASNGLYGLUVAL

Entity 2, ScCBM2 112 residues - Formula weight is not available

1   METHISTHRGLYSERCYSMETALAVALTYR
2   SERVALGLUASNSERTRPSERGLYGLYPHE
3   GLNGLYSERVALGLUVALMETASNHISGLY
4   THRGLUPROLEUASNGLYTRPALAVALGLN
5   TRPGLNPROGLYGLYGLYTHRTHRLEUGLY
6   GLYVALTRPASNGLYSERLEUTHRSERGLY
7   SERASPGLYTHRVALTHRVALARGASNVAL
8   ASPHISASNARGVALVALPROPROASPGLY
9   SERVALTHRPHEGLYPHETHRALATHRSER
10   THRGLYASNASPPHEPROVALASPSERILE
11   GLYCYSVALALAPROALAHISHISHISHIS
12   HISHIS

Entity 3, ScLPMO10C 330 residues - Formula weight is not available

1   HISGLYVALALAMETMETPROGLYSERARG
2   THRTYRLEUCYSGLNLEUASPALALYSTHR
3   GLYTHRGLYALALEUASPPROTHRASNPRO
4   ALACYSGLNALAALALEUASPGLNSERGLY
5   ALATHRALALEUTYRASNTRPPHEALAVAL
6   LEUASPSERASNALAGLYGLYARGGLYALA
7   GLYTYRVALPROASPGLYTHRLEUCYSSER
8   ALAGLYASPARGSERPROTYRASPPHESER
9   ALATYRASNALAALAARGSERASPTRPPRO
10   ARGTHRHISLEUTHRSERGLYALATHRILE
11   PROVALGLUTYRSERASNTRPALAALAHIS
12   PROGLYASPPHEARGVALTYRLEUTHRLYS
13   PROGLYTRPSERPROTHRSERGLULEUGLY
14   TRPASPASPLEUGLULEUILEGLNTHRVAL
15   THRASNPROPROGLNGLNGLYSERPROGLY
16   THRASPGLYGLYHISTYRTYRTRPASPLEU
17   ALALEUPROSERGLYARGSERGLYASPALA
18   LEUILEPHEMETGLNTRPVALARGSERASP
19   SERGLNGLUASNPHEPHESERCYSSERASP
20   VALVALPHEASPGLYGLYASNGLYGLUVAL
21   THRGLYILEARGGLYSERGLYSERTHRPRO
22   ASPPROASPPROTHRPROTHRPROTHRASP
23   PROTHRTHRPROPROTHRHISTHRGLYSER
24   CYSMETALAVALTYRSERVALGLUASNSER
25   TRPSERGLYGLYPHEGLNGLYSERVALGLU
26   VALMETASNHISGLYTHRGLUPROLEUASN
27   GLYTRPALAVALGLNTRPGLNPROGLYGLY
28   GLYTHRTHRLEUGLYGLYVALTRPASNGLY
29   SERLEUTHRSERGLYSERASPGLYTHRVAL
30   THRVALARGASNVALASPHISASNARGVAL
31   VALPROPROASPGLYSERVALTHRPHEGLY
32   PHETHRALATHRSERTHRGLYASNASPPHE
33   PROVALASPSERILEGLYCYSVALALAPRO

Samples:

15N-CBM2: potassium phosphate 25 mM; sodium chloride 25 mM; ScCBM2, [U-98% 15N], 0.5 mM

15N-CelS2: potassium phosphate 25 mM; sodium chloride 10 mM; N-ScLPMO10C, [U-98% 15N], 0.5 mM

15N-ScLPMO10C: potassium phosphate 25 mM; sodium chloride 10 mM; ScLPMO10C, [U-98% 15N], 0.2 mM

13C15N-CBM2: potassium phosphate 25 mM; sodium chloride 25 mM; ScCBM2, [U-98% 13C; U-98% 15N], 0.5 mM

13C15N-CelS2: potassium phosphate 25 mM; sodium chloride 10 mM; N-ScLPMO10C, [U-98% 13C; U-98% 15N], 0.5 mM

13C15N-ScLPMO10C: potassium phosphate 25 mM; sodium chloride 10 mM; ScLPMO10C, [U-98% 13C; U-98% 15N], 0.3 mM

13C15N-CBM2_D2O: potassium phosphate 25 mM; sodium chloride 25 mM; ScCBM2, [U-98% 13C; U-98% 15N], 0.5 mM

sample_conditions_CelS2: ionic strength: 35 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_CBM2: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N-CBM2isotropicsample_conditions_CBM2
2D 1H-13C HSQC aliphatic13C15N-CBM2isotropicsample_conditions_CBM2
2D 1H-13C HSQC aromatic13C15N-CBM2_D2Oisotropicsample_conditions_CBM2
3D HNHA15N-CBM2isotropicsample_conditions_CBM2
3D HNCO13C15N-CBM2isotropicsample_conditions_CBM2
3D HN(CA)CO13C15N-CBM2isotropicsample_conditions_CBM2
3D HNCA13C15N-CBM2isotropicsample_conditions_CBM2
3D HN(CO)CACB13C15N-CBM2isotropicsample_conditions_CBM2
3D HCCH-TOCSY13C15N-CBM2isotropicsample_conditions_CBM2
2D CACO13C15N-CBM2_D2Oisotropicsample_conditions_CBM2
2D CON13C15N-CBM2_D2Oisotropicsample_conditions_CBM2
3D 1H-15N NOESY15N-CBM2isotropicsample_conditions_CBM2
3D 1H-13C NOESY aliphatic13C15N-CBM2_D2Oisotropicsample_conditions_CBM2
3D 1H-13C NOESY aromatic13C15N-CBM2_D2Oisotropicsample_conditions_CBM2
2D 1H-15N HSQC15N-CelS2isotropicsample_conditions_CelS2
2D 1H-13C HSQC aliphatic13C15N-CelS2isotropicsample_conditions_CelS2
3D HNCA13C15N-CelS2isotropicsample_conditions_CelS2
3D HN(CO)CA13C15N-CelS2isotropicsample_conditions_CelS2
3D HNCO13C15N-CelS2isotropicsample_conditions_CelS2
3D HN(CA)CO13C15N-CelS2isotropicsample_conditions_CelS2
3D CBCANH13C15N-CelS2isotropicsample_conditions_CelS2
3D HBHA(CO)NH13C15N-CelS2isotropicsample_conditions_CelS2
3D HCCH-TOCSY13C15N-CelS2isotropicsample_conditions_CelS2
3D 1H-13C NOESY aliphatic13C15N-CelS2isotropicsample_conditions_CelS2
3D CBCA(CO)NH13C15N-CelS2isotropicsample_conditions_CelS2
2D 1H-15N HSQC15N-ScLPMO10Cisotropicsample_conditions_CelS2
3D HNCO13C15N-ScLPMO10Cisotropicsample_conditions_CelS2
3D HN(CA)CO13C15N-ScLPMO10Cisotropicsample_conditions_CelS2
3D HNCA13C15N-ScLPMO10Cisotropicsample_conditions_CelS2
3D CBCA(CO)NH13C15N-ScLPMO10Cisotropicsample_conditions_CelS2
3D CBCANH13C15N-ScLPMO10Cisotropicsample_conditions_CelS2

Software:

TopSpin v3.5, Bruker Biospin - collection, processing

CARA v1.5/1.8, Keller and Wuthrich - chemical shift assignment

MddNMR v2.0, Orekhov, Jaravine, Mayzel and Kazimierczuk - processing

NMR spectrometers:

  • Bruker Ascend 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
UNP Q9RJY2 Q9RJY2