BMRBj - BMREntryMaster

Found 1 Document (0.643 seconds)

BMRB: 30477

6DO6

NMR solution structure of wild type apo hFABP1 at 308 K

Authors

Scanlon, M.J., Mohanty, B., Doak, B.C., Patil, R.

Assembly

Fatty acid-binding protein, liver

Entity

1. Fatty acid-binding protein, liver (polymer, Thiol state: all free), 135 monomers, 15201.25 Da Detail

HHHHHHVAMS FSGKYQLQSQ ENFEAFMKAI GLPEELIQKG KDIKGVSEIV QNGKHFKFTI TAGSKVIQNE FTVGEECELE TMTGEKVKTV VQLEGDNKLV TTFKNIKSVT ELNGDIITNT MTLGDIVFKR ISKRI

Formula weight

15201.25 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamicsConstrained energy minimization

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.3 %, Completeness: 86.0 %, Completeness (bb): 82.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.0 % (1384 of 1610)	91.9 % (769 of 837)	75.5 % (472 of 625)	96.6 % (143 of 148)
Backbone	82.3 % (665 of 808)	95.0 % (266 of 280)	68.5 % (270 of 394)	96.3 % (129 of 134)
Sidechain	90.5 % (838 of 926)	90.3 % (503 of 557)	90.4 % (321 of 355)	100.0 % (14 of 14)
Aromatic	74.1 % (86 of 116)	75.9 % (44 of 58)	72.4 % (42 of 58)
Methyl	96.8 % (151 of 156)	94.9 % (74 of 78)	98.7 % (77 of 78)

1. entity 1

HHHHHHVAMS FSGKYQLQSQ ENFEAFMKAI GLPEELIQKG KDIKGVSEIV QNGKHFKFTI TAGSKVIQNE FTVGEECELE TMTGEKVKTV VQLEGDNKLV TTFKNIKSVT ELNGDIITNT MTLGDIVFKR ISKRI

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5, Details 1 mM [U-13C; U-15N] Human liver fatty acid binding protein (hFABP1), 20 mM sodium phosphate, 50 mM sodium chloride, pH 5.5 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 6 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.03 ppm, Outliers: 6 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: -0.1 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 10 models in PDB: 6DO6, Strand ID: A Detail

Release date

2018-12-20

Citation

A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor α agonists
Patil, R., Mohanty, B., Liu, B., Chandrashekaran, I.R., Headey, S.J., Williams, M.L., Clements, C.S., Ilyichova, O., Doak, B.C., Genissel, P., Weaver, R.J., Vuillard, L., Halls, M.L., Porter, C., Scanlon, M.J.
J. Biol. Chem. (2018), 294, 3720-3734, PubMed 30598509 , DOI 10.1074/jbc.RA118.006848 , Abstract

Related entities 1. Fatty acid-binding protein, liver, : 1 : 2 : 26 : 197 entities Detail

Interaction partners 1. Fatty acid-binding protein, liver, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 9 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker AvanceIII - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 5.5, Details 1 mM [U-13C; U-15N] Human liver fatty acid binding protein (hFABP1), 20 mM sodium phosphate, 50 mM sodium chloride, pH 5.5 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

2 2D 1H-13C HSQC aliphatic

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

3 2D 1H-13C HSQC aromatic

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

4 3D HNCA

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

5 3D HNCACB

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

6 3D CBCA(CO)NH

Instrument

Bruker AvanceIII - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

7 3D 13Cali-edited [1H,1H]-NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

8 3D 15N-edited [1H,1H]-NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

9 3D 13Caro-edited [1H,1H]-NOESY

Instrument

Bruker AvanceIII - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	sodium chloride	natural abundance	50 mM
3	Human liver fatty acid binding protein (hFABP1)	[U-13C; U-15N]	1 mM

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_30477_6do6.nef
Input source #2: Coordindates	6do6.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

----------------10--------20--------30--------40--------50--------60--------70--------80--------90--
HHHHHHVAMSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLV
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
HHHHHHVAMSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLV
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

-----100-------110-------120-------
TTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI
|||||||||||||||||||||||||||||||||||
TTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI
-------110-------120-------130-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	135	0	0	100.0

Content subtype: combined_30477_6do6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1362		95.6 (chain: A, length: 135)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	3479 (1)	noe	95.6 (chain: A, length: 135)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 95.6%
- Total number of assignments
  - ¹H chemical shifts: 772
  - ¹³C chemical shifts: 446
  - ¹⁵N chemical shifts: 144
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	837	772	92.2
¹³C chemical shifts	625	446	71.4
¹⁵N chemical shifts	150	144	96.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	280	268	95.7
¹³C chemical shifts	270	129	47.8
¹⁵N chemical shifts	134	128	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	557	504	90.5
¹³C chemical shifts	355	317	89.3
¹⁵N chemical shifts	16	16	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	82	81	98.8
¹³C chemical shifts	82	81	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	58	42	72.4
¹³C chemical shifts	58	40	69.0

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 135, Sequence coverage: 95.6%
- Total number of restraints: 3479
- Weight of restraints: 1.0 (3479)
- Potential type of restraints: upper-bound-parabolic (3479)
- Range of distance target values: 2.4, 5.5 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Keywords LIPID BINDING PROTEIN

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.643 seconds)

BMRB: 30477

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Fatty acid-binding protein, liver, : 1 : 2 : 26 : 197 entities Detail

Interaction partners 1. Fatty acid-binding protein, liver, : 2 interactors Detail

Experiments performed 9 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail