BMRB Entry 18895

Title:
Backbone and partial sidechain assignment of the microtubule binding domain of the MAP1B light chain
Deposition date:
2012-12-13
Original release date:
2013-01-29
Authors:
Orban-Nemeth, Zsuzsanna; Propst, Friedrich; Henen, Morkos; Konrat, Robert; Kozminski, Wiktor; Zerko, Szymon; Saxena, Saurabh; Stanek, Jan; Geist, Leonhard
Citation:

Citation: Orban-Nemeth, Zsuzsanna; Henen, Morkos; Geist, Leonhard; Zerko, Szymon; Saxena, Saurabh; Stanek, Jan; Komiski, Wiktor; Propst, Friedrich; Konrat, Robert. "Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23339032

Assembly members:

Assembly members:
MAP1B, polymer, 150 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMA25NHis

Data sets:
Data typeCount
13C chemical shifts489
15N chemical shifts124
1H chemical shifts757

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal MAP1B LC1

Entities:

Entity 1, N-terminal MAP1B LC 150 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUPHEMETVALASPPROGLUALALEU
4   ALAILEGLUGLNASNLEUGLYLYSALALEU
5   LYSLYSASPLEULYSGLULYSALALYSTHR
6   LYSLYSPROGLYTHRLYSTHRLYSSERSER
7   SERPROVALLYSLYSGLYASPGLYLYSSER
8   LYSPROSERALAALASERPROLYSPROGLY
9   ALALEULYSGLUSERSERASPLYSVALSER
10   ARGVALALASERPROLYSLYSLYSGLUSER
11   VALGLULYSALAMETLYSTHRTHRTHRTHR
12   PROGLUVALLYSALATHRARGGLYGLUGLU
13   LYSASPLYSGLUTHRLYSASNALAALAASN
14   ALASERALASERLYSSERVALLYSTHRALA
15   THRALAGLYPROGLYTHRTHRLYSTHRALA

Samples:

sample_1: MAP1B, [U-95% 13C; U-90% 15N], 0.6 – 1 mM; D2O, [U-100% 2H], 10%; sodium chloride 300 mM; sodium phosphate 50 mM

sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
5D HN(CA)CONHsample_1isotropicsample_conditions_1
5D (HACA)CON(CA)CONHsample_1isotropicsample_conditions_1
5D (H)NCO(NCA)CONHsample_1isotropicsample_conditions_1
4D HNCACOsample_1isotropicsample_conditions_1
5D HabCabCONHsample_1isotropicsample_conditions_1
5D H(CC-tocsy)CONHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis

MFT, Wiktor Kozminski - processing

TSAR, Kozminski, Zawadzka, Kazimiurcuk - chemical shift assignment

NMR spectrometers:

  • Agilent Direct Drive 700 MHz

Related Database Links:

RefSeq NP_062090.1
EMBL CAA34620 CAC16162
GB EDM10176
PIR S06017
REF NP_062090 XP_008758883
SP P15205
AlphaFold P15205

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