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 50366

Title: hCEACAM1 N-terminal IgV domain N97A mutant   PubMed: 33742094

Deposition date: 2020-06-26 Original release date: 2021-03-22

Authors: Sun, Zhen-Yu; Wagner, Gerhard; Kim, Walter; Huang, Yu-Hwa; Blumberg, Richard; Gandhi, Amit

Citation: Gandhi, Amit; Sun, Zhen-Yu; Kim, Walter; Huang, Yu-Hwa; Kondo, Yasuyuki; Bonsor, Daniel; Sundberg, Eric; Kuchroo, Vijay; Petsko, Gregory; Blumberg, Richard. "Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium"  Commun. Biol. 4, 360-360 (2021).

Assembly members:
entity_1, polymer, 108 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: Escherichia coli   Vector: pET21d

Entity Sequences (FASTA):
entity_1: AQLTTESMPFNVAEGKEVLL LVHNLPQQLFGYSWYKGERV DGNRQIVGYAIGTQQATPGP ANSGRETIYPNASLLIQNVT QNDTGFYTLQVIKSDLVAEE ATGQFHVY

Data sets:
Data typeCount
13C chemical shifts304
15N chemical shifts92
1H chemical shifts92

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hCEACAM1 N-terminal IgV domain N97A mutant1

Entities:

Entity 1, hCEACAM1 N-terminal IgV domain N97A mutant 108 residues - Formula weight is not available

1   ALAGLNLEUTHRTHRGLUSERMETPROPHE
2   ASNVALALAGLUGLYLYSGLUVALLEULEU
3   LEUVALHISASNLEUPROGLNGLNLEUPHE
4   GLYTYRSERTRPTYRLYSGLYGLUARGVAL
5   ASPGLYASNARGGLNILEVALGLYTYRALA
6   ILEGLYTHRGLNGLNALATHRPROGLYPRO
7   ALAASNSERGLYARGGLUTHRILETYRPRO
8   ASNALASERLEULEUILEGLNASNVALTHR
9   GLNASNASPTHRGLYPHETYRTHRLEUGLN
10   VALILELYSSERASPLEUVALALAGLUGLU
11   ALATHRGLYGLNPHEHISVALTYR

Samples:

sample_1: hCEACAM1-N97A, [U-100% 13C; U-100% 15N], 0.3 mM; HEPES 10 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

VNMRj - collection

NMRPipe - processing

hmsIST - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Agilent DD2 700 MHz

Related Database Links:

UNP P13688
AlphaFold Q9UQV9

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