BMRBj - BMREntryMaster

Found 1 Document (0.4 seconds)

BMRB: 36147

5Z26

solution structure of SMAP-18

Authors

Jung, B., Lee, C.W.

Assembly

SMAP-18

Entity

1. SMAP-18 (polymer, Thiol state: not present), 18 monomers, 2065.475 Da Detail

RGLRRLGRKI AHGVKKYG

Formula weight

2065.475 Da

Source organism

Ovis aries

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 88.9 %, Completeness: 85.1 %, Completeness (bb): 87.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	85.1 % (103 of 121)	85.1 % (103 of 121)
Backbone	87.5 % (35 of 40)	87.5 % (35 of 40)
Sidechain	84.0 % (68 of 81)	84.0 % (68 of 81)
Aromatic	66.7 % (4 of 6)	66.7 % (4 of 6)
Methyl	100.0 % (9 of 9)	100.0 % (9 of 9)

1. SMAP-18

RGLRRLGRKI AHGVKKYG

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 atm, Temperature 298 K, pH 6, Details 10 mM NA-Na,P,O,H sodium phosphate, 2.0 mM NA-C,O,N,H protein solution, 50 mM NA-Na,Cl sodium chloride, 50 % v/v [U-2H] TFE, 10 % v/v [U-2H] H2O, trifluoroethanol/water

#	Name	Isotope labeling	Type	Concentration
1	protein solution	natural abundance	protein	2.0 mM
2	sodium chloride	natural abundance	salt	50 mM
3	sodium phosphate	natural abundance	buffer	10 mM
4	TFE	[U-2H]	solvent	50 % v/v
5	H2O	natural abundance	solvent	40 % v/v
6	D2O	[U-2H]	solvent	10 % v/v

Protein Blocks Logo

Calculated from 20 models in PDB: 5Z26, Strand ID: A Detail

Release date

2018-06-26

Citation

solution structure of SMAP-18
Jung, B., Lee, C.W.

Related entities 1. SMAP-18, : 1 : 3 : 1 : 3 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_36147_5z26.nef
Input source #2: Coordindates	5z26.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--------
RGLRRLGRKIAHGVKKYG
||||||||||||||||||
RGLRRLGRKIAHGVKKYG

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_36147_5z26.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	103		88.9 (chain: A, length: 18)
1	Distance restraints	DYANA/DIANA_distance_constraints_3	OK	317 (1)	noe	88.9 (chain: A, length: 18)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	180 (180)	.	100.0 (chain: A, length: 18)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 88.9%
- Total number of assignments
  - ¹H chemical shifts: 103
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	121	103	85.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	40	35	87.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	68	84.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	4	66.7

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 88.9%
- Total number of restraints: 315
- Weight of restraints: 1.0 (315)
- Potential type of restraints: upper-bound-parabolic (315)
- Range of distance target values: 2.36, 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

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 100.0%
- Total number of restraints: 180
- Total number of restraints per polymer type: 180
- Weight of restraints: 1.0 (180)
- Potential type of restraints: square-well-parabolic (180)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords ANTIMICROBIAL PROTEIN, STRUCTURE FROM CYANA 2.1

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Found 1 Document (0.4 seconds)

BMRB: 36147

Sample

Related entities 1. SMAP-18, : 1 : 3 : 1 : 3 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail