BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	72.3 % (756 of 1046)	74.7 % (411 of 550)	64.0 % (258 of 403)	93.5 % (87 of 93)
Backbone	84.3 % (430 of 510)	99.4 % (171 of 172)	69.4 % (177 of 255)	98.8 % (82 of 83)
Sidechain	66.1 % (409 of 619)	63.5 % (240 of 378)	71.0 % (164 of 231)	50.0 % (5 of 10)
Aromatic	63.1 % (53 of 84)	66.7 % (28 of 42)	62.5 % (25 of 40)	0.0 % (0 of 2)
Methyl	73.3 % (63 of 86)	83.7 % (36 of 43)	62.8 % (27 of 43)

1. Acyl-CoA-binding protein

VSQLFEEKAK AVNELPTKPS TDELLELYAL YKQATVGDND KEKPGIFNMK DRYKWEAWEN LKGKSQEDAE KEYIALVDQL IAKYSS

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 6.75

#	Name	Isotope labeling	Concentration
1	Acyl-CoA-binding protein	[U-13C; U-15N]	2.5 mM
2	H2O		90 %
3	D2O		10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	na	na	null	null	0.0
¹⁵N	na	na	null	null	0.0

Referencing offset: -0.52 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	na	na	null	null	0.0
¹⁵N	na	na	null	null	0.0

Referencing offset: -0.52 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹³C	na	na	null	null	0.0
¹⁵N	na	na	null	null	0.0

Referencing offset: 0.04 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1ST7, Strand ID: A Detail

Release date

2005-02-20

Citation

Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles
Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.
Proteins (2005), 59, 80-90, PubMed 15690348 , DOI 10.1002/prot.20340 , Abstract

Related entities 1. Acyl-CoA-binding protein, : 1 : 2 : 154 entities Detail

Interaction partners 1. Acyl-CoA-binding protein, : 24 interactors Detail

More details for 24 interactors identified by 4 citations

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_6188_1st7.nef
Input source #2: Coordindates	1st7.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------
VSQLFEEKAKAVNELPTKPSTDELLELYALYKQATVGDNDKEKPGIFNMKDRYKWEAWENLKGKSQEDAEKEYIALVDQLIAKYSS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
VSQLFEEKAKAVNELPTKPSTDELLELYALYKQATVGDNDKEKPGIFNMKDRYKWEAWENLKGKSQEDAEKEYIALVDQLIAKYSS

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	86	0	0	100.0

Content subtype: combined_6188_1st7.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	chemical_shift_set_1	Warning	761		100.0 (chain: A, length: 86)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1723 (1)	noe	97.7 (chain: A, length: 86)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	13 (1)	hbond	25.6 (chain: A, length: 86)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	131 (131)	.	100.0 (chain: A, length: 86)

Assigned chemical shifts

Saveframe: chemical_shift_set_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 100.0%

--------10--------20--------30--------40--------50--------60--------70--------80------
VSQLFEEKAKAVNELPTKPSTDELLELYALYKQATVGDNDKEKPGIFNMKDRYKWEAWENLKGKSQEDAEKEYIALVDQLIAKYSS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
VSQLFEEKAKAVNELPTKPSTDELLELYALYKQATVGDNDKEKPGIFNMKDRYKWEAWENLKGKSQEDAEKEYIALVDQLIAKYSS

Total number of assignments
- ¹H chemical shifts: 424
- ¹³C chemical shifts: 249
- ¹⁵N chemical shifts: 88

Completeness of assignments

Entity_assemble_ID: A

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
17	THR	HG1	7.04
18	LYS	HZ1	7.52
18	LYS	HZ2	7.52
18	LYS	HZ3	7.52
41	LYS	HZ1	7.99
41	LYS	HZ2	7.99
41	LYS	HZ3	7.99
50	LYS	HZ1	7.85
50	LYS	HZ2	7.85
50	LYS	HZ3	7.85
62	LYS	HZ1	7.81
62	LYS	HZ2	7.81
62	LYS	HZ3	7.81
65	SER	HG	6.09
73	TYR	HH	9.39

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	550	408	74.2
¹³C chemical shifts	403	249	61.8
¹⁵N chemical shifts	94	88	93.6

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	172	171	99.4
¹³C chemical shifts	172	86	50.0
¹⁵N chemical shifts	83	83	100.0

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	378	237	62.7
¹³C chemical shifts	231	163	70.6
¹⁵N chemical shifts	11	5	45.5

Methyl group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	36	81.8
¹³C chemical shifts	44	27	61.4

Aromatic group atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	42	28	66.7
¹³C chemical shifts	40	25	62.5
¹⁵N chemical shifts	2	0	0.0

Peptide bond of PRO
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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 97.7%
- Total number of restraints: 1723
- Weight of restraints: 1.0 (1723)
- Potential type of restraints: square-well-parabolic (1723)
- Range of distance target values: 2.25, 3.65 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 25.6%
  - Total number of restraints: 13
  - Weight of restraints: 1.0 (13)
  - Potential type of restraints: square-well-parabolic (13)
  - Range of distance target values: 1.9, 1.9 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 86, Sequence coverage: 100.0%
- Total number of restraints: 131
- Total number of restraints per polymer type: 131
- Weight of restraints: 1.0 (131)
- Potential type of restraints: square-well-parabolic (131)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Four helix bundle

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Found 1 Document (1.463 seconds)

BMRB: 6188

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Acyl-CoA-binding protein, : 1 : 2 : 154 entities Detail

Interaction partners 1. Acyl-CoA-binding protein, : 24 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail