BMRB Entry 26841

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26841

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Title:
Chemical shift assignment of CBP-ID3
Deposition date:
2016-06-29
Original release date:
2017-07-10
Authors:
Piai, Alessandro; Contreras-Martos, Sara; Kosol, Simone; Varadi, Mihaly; Bekesi, Angela; Lebrun, Pierre; Volkov, Alex; Pierattelli, Roberta; Felli, Isabella; Tompa, Peter
Citation:

Citation: Contreras-Martos, Sara; Piai, Alessandro; Kosol, Simone; Varadi, Mihaly; Bekesi, Angela; Lebrun, Pierre; Volkov, Alexander; Gevaert, Kris; Pierattelli, Roberta; Felli, Isabella; Tompa, Peter. "Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP"  Sci. Rep. 7, 4676-4676 (2017).
PubMed: 28680062

Assembly members:

Assembly members:
ID3, polymer, 406 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ID3: HKQGILGNQPALPAPGAQPP VIPQAQPVRPPNGPLSLPVN RMQVSQGMNSFNPMSLGNVQ LPQAPMGPRAASPMNHSVQM NSMGSVPGMAISPSRMPQPP NMMGAHTNNMMAQAPAQSQF LPQNQFPSSSGAMSVGMGQP PAQTGVSQGQVPGAALPNPL NMLGPQASQLPCPPVTQSPL HPTPPPASTAAGMPSLQHTT PPGMTPPQPAAPTQPSTPVS SSGQTPTPTPGSVPSATQTQ STPTVQAAAQAQVTPQPQTP VQPPSVATPQSSQQQPTPVH AQPPGTPLSQAAASIDNRVP TPSSVASAETNSQQPGPDVP VLEMKTETQAEDTEPDPGES KGEPRSEMMEEDLQGASQVK EETDIAEQKSEPMEVDEKKP EVKVEVKEEEESSSNGTASQ STSPSQ

Data sets:
Data typeCount
13C chemical shifts1092
15N chemical shifts365
1H chemical shifts1378

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ID31

Entities:

Entity 1, ID3 406 residues - Formula weight is not available

1   HISLYSGLNGLYILELEUGLYASNGLNPRO
2   ALALEUPROALAPROGLYALAGLNPROPRO
3   VALILEPROGLNALAGLNPROVALARGPRO
4   PROASNGLYPROLEUSERLEUPROVALASN
5   ARGMETGLNVALSERGLNGLYMETASNSER
6   PHEASNPROMETSERLEUGLYASNVALGLN
7   LEUPROGLNALAPROMETGLYPROARGALA
8   ALASERPROMETASNHISSERVALGLNMET
9   ASNSERMETGLYSERVALPROGLYMETALA
10   ILESERPROSERARGMETPROGLNPROPRO
11   ASNMETMETGLYALAHISTHRASNASNMET
12   METALAGLNALAPROALAGLNSERGLNPHE
13   LEUPROGLNASNGLNPHEPROSERSERSER
14   GLYALAMETSERVALGLYMETGLYGLNPRO
15   PROALAGLNTHRGLYVALSERGLNGLYGLN
16   VALPROGLYALAALALEUPROASNPROLEU
17   ASNMETLEUGLYPROGLNALASERGLNLEU
18   PROCYSPROPROVALTHRGLNSERPROLEU
19   HISPROTHRPROPROPROALASERTHRALA
20   ALAGLYMETPROSERLEUGLNHISTHRTHR
21   PROPROGLYMETTHRPROPROGLNPROALA
22   ALAPROTHRGLNPROSERTHRPROVALSER
23   SERSERGLYGLNTHRPROTHRPROTHRPRO
24   GLYSERVALPROSERALATHRGLNTHRGLN
25   SERTHRPROTHRVALGLNALAALAALAGLN
26   ALAGLNVALTHRPROGLNPROGLNTHRPRO
27   VALGLNPROPROSERVALALATHRPROGLN
28   SERSERGLNGLNGLNPROTHRPROVALHIS
29   ALAGLNPROPROGLYTHRPROLEUSERGLN
30   ALAALAALASERILEASPASNARGVALPRO
31   THRPROSERSERVALALASERALAGLUTHR
32   ASNSERGLNGLNPROGLYPROASPVALPRO
33   VALLEUGLUMETLYSTHRGLUTHRGLNALA
34   GLUASPTHRGLUPROASPPROGLYGLUSER
35   LYSGLYGLUPROARGSERGLUMETMETGLU
36   GLUASPLEUGLNGLYALASERGLNVALLYS
37   GLUGLUTHRASPILEALAGLUGLNLYSSER
38   GLUPROMETGLUVALASPGLULYSLYSPRO
39   GLUVALLYSVALGLUVALLYSGLUGLUGLU
40   GLUSERSERSERASNGLYTHRALASERGLN
41   SERTHRSERPROSERGLN

Samples:

sample_1: ID3, [U-100% 13C; U-100% 15N], 0.4 mM; KH2PO4 50 mM; sodium chloride 150 mM; TCEP 2.5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 297.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D H(CACON)sample_1isotropicsample_conditions_1
4D HCBCACONsample_1isotropicsample_conditions_1
4D HCBCANCOsample_1isotropicsample_conditions_1
4D (HCA)CON(CA)CONsample_1isotropicsample_conditions_1
4D (HN)CON(CA)CONsample_1isotropicsample_conditions_1
5D HNCANCOsample_1isotropicsample_conditions_1
5D HNCACONsample_1isotropicsample_conditions_1
2D BEST-TROSYsample_1isotropicsample_conditions_1
3D BT-HNCOsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1
4D TROSY-(H)NCO(CA)NNHsample_1isotropicsample_conditions_1
4D TROSY-HN(COCA)NNHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance III 950 MHz

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