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Found 1 Document (1.222 seconds)

BMRB: 7157

2O7A

NMR spectroscopy of T4 Lysozyme peptide fragments

Authors

Najbar, L.V., Craik, D.J., Wade, J.D., McLeish, M.J.

Assembly

HELIX F

Entity

1. HELIX F (polymer, Thiol state: not present), 13 monomers, 1578.837 Da Detail

GFTNSLRMLQ QKR

Formula weight

1578.837 Da

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 92.3 %, Completeness: 93.4 %, Completeness (bb): 88.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	93.4 % (85 of 91)	93.4 % (85 of 91)
Backbone	88.9 % (24 of 27)	88.9 % (24 of 27)
Sidechain	95.3 % (61 of 64)	95.3 % (61 of 64)
Aromatic	100.0 % (5 of 5)	100.0 % (5 of 5)
Methyl	100.0 % (5 of 5)	100.0 % (5 of 5)

1. helix F (lys 113-125)

GFTNSLRMLQ QKR

Show sample condition

Sample

Temperature 278 (±0) K

#	Name	Concentration
1	helix F (lys 113-125)	1.0 ~ 2.0 mM
2	H2O	90 %
3	D2O	10 %

Chem. Shift Complete2

Sequence coverage: 100.0 %, Completeness: 90.1 %, Completeness (bb): 92.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	90.1 % (164 of 182)	90.1 % (164 of 182)
Backbone	92.6 % (50 of 54)	92.6 % (50 of 54)
Sidechain	89.1 % (114 of 128)	89.1 % (114 of 128)
Aromatic	100.0 % (10 of 10)	100.0 % (10 of 10)
Methyl	100.0 % (10 of 10)	100.0 % (10 of 10)

1. helix F (lys 113-125)

GFTNSLRMLQ QKR

Show sample condition

Sample

Temperature 283 (±0) K

#	Name	Concentration
4	helix F (lys 113-125)	1.0 ~ 2.0 mM
5	TFE	50 %
6	H2O	40 %
7	D2O	10 %

Chem. Shift Complete3

Sequence coverage: 100.0 %, Completeness: 90.1 %, Completeness (bb): 93.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	90.1 % (246 of 273)	90.1 % (246 of 273)
Backbone	93.8 % (76 of 81)	93.8 % (76 of 81)
Sidechain	88.5 % (170 of 192)	88.5 % (170 of 192)
Aromatic	100.0 % (15 of 15)	100.0 % (15 of 15)
Methyl	100.0 % (15 of 15)	100.0 % (15 of 15)

1. helix F (lys 113-125)

GFTNSLRMLQ QKR

Show sample condition

Sample

Temperature 303 (±0) K

#	Name	Concentration
8	helix F (lys 113-125)	1.0 ~ 2.0 mM
9	H2O	90 %
10	D2O	10 %
11	SDS	200 mM

Release date

2008-11-11

Citation

Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments
Najbar, L.V., Craik, D.J., Wade, J.D., McLeish, M.J.
Biochemistry (2000), 39, 5911-5920, PubMed 10801343 , DOI: , Abstract

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 7152 released on 2008-11-11
    Title NMR spectroscopy of T4 Lysozyme peptide fragments
  BMRB: 7153 released on 2008-11-11
    Title NMR spectroscopy of T4 Lysozyme peptide fragments
  BMRB: 7155 released on 2008-11-11
    Title NMR spectroscopy of T4 Lysozyme peptide fragments
  BMRB: 7156 released on 2008-11-11
    Title NMR spectroscopy of T4 Lysozyme peptide fragments
  BMRB: 7154 released on 2006-06-06
    Title NMR spectroscopy of T4 Lysozyme peptide fragments

Related entities 1. HELIX F, : 1 : 100 entities Detail

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr7157_3.str
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

Content subtype: bmr7157_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	chem_shift_list_1	Warning	104	92.3 (chain: 1, length: 13)
2	Assigned chemical shifts	chem_shift_list_2	Warning	94	100.0 (chain: 1, length: 13)
3	Assigned chemical shifts	chem_shift_list_3	Warning	96	100.0 (chain: 1, length: 13)
1	Chemical shift references	chemical_shift_referencing	OK	1	No information

Assigned chemical shifts

Saveframe: chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 13, Sequence coverage: 92.3%
- Total number of assignments
  - ¹H chemical shifts: 104
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: chem_shift_list_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 13, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 94
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: chem_shift_list_3
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 13, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 96
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
7	ARG	HH11	7.26
7	ARG	HH12	7.24
12	LYS	HZ1	7.6
12	LYS	HZ2	7.6
12	LYS	HZ3	7.6
13	ARG	HH11	7.26
13	ARG	HH12	7.24

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
7	ARG	HH11	7.23
12	LYS	HZ1	7.67
12	LYS	HZ2	7.67
12	LYS	HZ3	7.67
13	ARG	HH11	7.25

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
12	LYS	HZ1	7.48
12	LYS	HZ2	7.48
12	LYS	HZ3	7.48
13	ARG	HH11	7.14

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Found 1 Document (1.222 seconds)

BMRB: 7157

Sample

Sample

Sample

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. HELIX F, : 1 : 100 entities Detail

Chemical shift validation 5 contents Detail