BMRB Entry 17302

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17302
MolProbity Validation Chart

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Title:
1H and 15N RESONANCE ASSIGNMENT OF HUMAN APO L-FABP
Deposition date:
2010-11-17
Original release date:
2012-06-05
Authors:
Cai, Jun; Luecke, Christian; Chen, Zhongjing; Qiao, Ye; Klimtchuk, Elena; Hamilton, James
Citation:

Citation: Cai, Jun; Luecke, Christian; Chen, Zhongjing; Qiao, Ye; Klimtchuk, Elena; Hamilton, James. "Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited"  Biophys. J. 102, 2585-2594 (2012).

Assembly members:

Assembly members:
L-FABP, polymer, 126 residues, 14095.292 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: pMON

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L-FABP: SFSGKYQLQSQENFEAFMKA IGLPEELIQKGKDIKGVSEI VQNGKHFKFTITAGSKVIQN EFTVGEECELETMTGEKVKT VVQLEGDNKLVTTFKNIKSV TELNGDIITNTMTLGDIVFK RISKRI

Data sets:
Data typeCount
15N chemical shifts140
1H chemical shifts938

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1human liver fatty acid binding protein1

Entities:

Entity 1, human liver fatty acid binding protein 126 residues - 14095.292 Da.

the N-terminal residue Met1 is missing; the assignments thus start with Ser2

1   SERPHESERGLYLYSTYRGLNLEUGLNSER
2   GLNGLUASNPHEGLUALAPHEMETLYSALA
3   ILEGLYLEUPROGLUGLULEUILEGLNLYS
4   GLYLYSASPILELYSGLYVALSERGLUILE
5   VALGLNASNGLYLYSHISPHELYSPHETHR
6   ILETHRALAGLYSERLYSVALILEGLNASN
7   GLUPHETHRVALGLYGLUGLUCYSGLULEU
8   GLUTHRMETTHRGLYGLULYSVALLYSTHR
9   VALVALGLNLEUGLUGLYASPASNLYSLEU
10   VALTHRTHRPHELYSASNILELYSSERVAL
11   THRGLULEUASNGLYASPILEILETHRASN
12   THRMETTHRLEUGLYASPILEVALPHELYS
13   ARGILESERLYSARGILE

Samples:

sample_1: potassium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.05%; human liver fatty acid binding protein2 – 3 mM; H2O 95%; D2O 5%

sample_2: potassium phosphate 20 mM; sodium chloride 150 mM; sodium azide 0.05%; human liver fatty acid binding protein, [U-15N], 2 – 3 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

DISCOVER v2000, Accelrys Software Inc. - refinement

NMRView v8.0, Johnson, One Moon Scientific - data analysis, peak picking

xwinnmr v3.5, Bruker Biospin - collection, processing

TOPSPIN v1.3, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17303 19160 19188 19189 25333
PDB
DBJ BAI46102
EMBL CAG46887 CAH90116
GB AAA52418 AAA52419 AAH22287 AAH32801 AAX37108
REF NP_001125017 NP_001434 XP_001140263 XP_003268834 XP_003805902
SP P07148
AlphaFold P07148

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