BMRB Entry 18941

Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the LFA-1 wild type I-domain
Deposition date:
2013-01-07
Original release date:
2013-01-24
Authors:
Zimmerman, Tahl; Blanco, Francisco
Citation:

Citation: Zimmerman, Tahl; Oyarzabal, Julen; San-Sebastian, Eider; Majumdar, Sumit; Tejo, Bimo; Siahaan, Teruna; Blanco, Francisco. "ICAM-1 peptide inhibitors of T-cell adhesion bind to the allosteric site of LFA-1. An NMR characterization"  Chem. Biol. Drug Design 70, 347-353 (2007).
PubMed: 17868072

Assembly members:

Assembly members:
LFA-1_I-domain, polymer, 181 residues, 20682.7 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11d

Data sets:
Data typeCount
13C chemical shifts447
15N chemical shifts175
1H chemical shifts305

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LFA-1 I-domain1

Entities:

Entity 1, LFA-1 I-domain 181 residues - 20682.7 Da.

Residues 127-128 come from the cloning and do not belong to the native protein

1   METGLYASNVALASPLEUVALPHELEUPHE
2   ASPGLYSERMETSERLEUGLNPROASPGLU
3   PHEGLNLYSILELEUASPPHEMETLYSASP
4   VALMETLYSLYSLEUSERASNTHRSERTYR
5   GLNPHEALAALAVALGLNPHESERTHRSER
6   TYRLYSTHRGLUPHEASPPHESERASPTYR
7   VALLYSARGLYSASPPROASPALALEULEU
8   LYSHISVALLYSHISMETLEULEULEUTHR
9   ASNTHRPHEGLYALAILEASNTYRVALALA
10   THRGLUVALPHEARGGLUGLULEUGLYALA
11   ARGPROASPALATHRLYSVALLEUILEILE
12   ILETHRASPGLYGLUALATHRASPSERGLY
13   ASNILEASPALAALALYSASPILEILEARG
14   TYRILEILEGLYILEGLYLYSHISPHEGLN
15   THRLYSGLUSERGLNGLUTHRLEUHISLYS
16   PHEALASERLYSPROALASERGLUPHEVAL
17   LYSILELEUASPTHRPHEGLULYSLEULYS
18   ASPLEUPHETHRGLULEUGLNLYSLYSILE
19   TYR

Samples:

sample_1: LFA-1 I-domain polypeptide, [U-13C; U-15N], 700 uM; Sodium chloride 137 mM; sodium phosphate dibasic 2.7 mM; pottasium chloride 2 mM; pottasium sulfate monobasic 2 mM; Magnesium sulfate 10 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
(H)CC(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

xwinnmr, bruker - processing

NMRPipe, Frank Delaglio - processing

NMRView, Bruce A Johnson - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP P20701
PIR S03308
BMRB 4553
PDB
DBJ BAG36913
EMBL CAA68747
GB AAC31672 AAQ14923 AAZ38713 EAW52244 EAW52245
REF NP_001029341 NP_002200 XP_001100800 XP_004057549 XP_005255370
SP P20701
AlphaFold Q9UBC8 P20701

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