BMRBj - BMREntryMaster

Found 1 Document (0.457 seconds)

BMRB: 26057

2NDE

Solution Structure of Mutant of BMAP-28(1-18)

Authors

Agadi, N., Kumar, A.

Assembly

Mutant of BMAP-28(1-18)

Entity

1. Mutant of BMAP-28(1-18) (polymer, Thiol state: not present), 18 monomers, 1993.446 Da Detail

IGLRGLGRKI ALIHKKYG

Formula weight

1993.446 Da

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 79.1 %, Completeness (bb): 74.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	79.1 % (163 of 206)	89.1 % (106 of 119)	65.5 % (57 of 87)
Backbone	74.4 % (67 of 90)	97.5 % (39 of 40)	56.0 % (28 of 50)
Sidechain	83.8 % (109 of 130)	84.8 % (67 of 79)	82.4 % (42 of 51)
Aromatic	83.3 % (10 of 12)	83.3 % (5 of 6)	83.3 % (5 of 6)
Methyl	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)

1. entity

IGLRGLGRKI ALIHKKYG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.6

#	Name	Isotope labeling	Concentration
1	sodium phosphate	natural abundance	20 mM
2	D2O	[U-99% 2H]	10 %
3	H2O	natural abundance	90 %
4	SDS	[U-99% 2H]	50 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 2NDE, Strand ID: A Detail

Release date

2016-05-25

Citation

Structure, Function And Membrane Interaction Studies of Two Synthetic Peptides Using Solution And Solid State NMR
Agadi, N., Kumar, A.
Not known

Related entities 1. Mutant of BMAP-28(1-18), : 3 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_26057_2nde.nef
Input source #2: Coordindates	2nde.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--------
IGLRGLGRKIALIHKKYG
||||||||||||||||||
IGLRGLGRKIALIHKKYG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	18	0	0	100.0

Content subtype: combined_26057_2nde.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	164		100.0 (chain: A, length: 18)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	279 (1)	noe	100.0 (chain: A, length: 18)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	26 (26)	.	88.9 (chain: A, length: 18)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 107
  - ¹³C chemical shifts: 57
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
14	HIS	HE2	8.707

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	106	89.1
¹³C chemical shifts	87	57	65.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	39	97.5
¹³C chemical shifts	36	15	41.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	79	67	84.8
¹³C chemical shifts	51	42	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	13	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	5	83.3
¹³C chemical shifts	6	5	83.3

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 100.0%
- Total number of restraints: 279
- Weight of restraints: 1.0 (279)
- Potential type of restraints: square-well-parabolic (279)
- Range of distance target values: 2.5, 3.25 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 88.9%
- Total number of restraints: 26
- Total number of restraints per polymer type: 26
- Weight of restraints: 1.0 (26)
- Potential type of restraints: square-well-parabolic (26)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords AMP

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Found 1 Document (0.457 seconds)

BMRB: 26057

Sample

Related entities 1. Mutant of BMAP-28(1-18), : 3 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail