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Found 1 Document (0.685 seconds)

BMRB: 19249

2M8E

NMR structure of the PAI subdomain of Sleeping Beauty transposase

Authors

Eubanks, C., Schreifels, J., Aronovich, E., Carlson, D., Hacjkett, P., Nesmelova, I.

Assembly

PAI subdomain of Sleeping Beauty transposase

Entity

1. PAI subdomain of Sleeping Beauty transposase (polymer, Thiol state: not present), 57 monomers, 6376.315 Da Detail

ASMGKSKEIS QDLRKKIVDL HKSGSSLGAI SKRLKVPRSS VQTIVRKYKH HGTTQHH

Formula weight

6376.315 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.5 %, Completeness: 77.5 %, Completeness (bb): 93.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	77.5 % (323 of 417)	75.1 % (269 of 358)	91.5 % (54 of 59)
Backbone	93.6 % (162 of 173)	92.3 % (108 of 117)	96.4 % (54 of 56)
Sidechain	66.0 % (161 of 244)	66.8 % (161 of 241)	0.0 % (0 of 3)
Aromatic	35.7 % (5 of 14)	35.7 % (5 of 14)
Methyl	79.3 % (23 of 29)	79.3 % (23 of 29)

1. entity

ASMGKSKEIS QDLRKKIVDL HKSGSSLGAI SKRLKVPRSS VQTIVRKYKH HGTTQHH

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 7

#	Name	Isotope labeling	Concentration
1	entity	[U-100% 15N]	0.15 mM
2	sodium phosphate	natural abundance	20 mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 7

#	Name	Isotope labeling	Concentration
5	entity	[U-100% 15N]	0.15 mM
6	sodium phosphate	natural abundance	20 mM
7	H2O	natural abundance	90 %
8	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 14 models in PDB: 2M8E, Strand ID: A Detail

Release date

2013-12-15

Citation

NMR structural analysis of Sleeping Beauty transposase binding to DNA
Carpentier, C.E., Schreifels, J.M., Aronovich, E.L., Carlson, D.F., Hackett, P.B., Nesmelova, I.V.
Protein Sci. (2014), 23, 23-33, PubMed 24243759 , DOI 10.1002/pro.2386 , Abstract

Related entities 1. PAI subdomain of Sleeping Beauty transposase, : 1 : 19 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19249_2m8e.nef
Input source #2: Coordindates	2m8e.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-------
ASMGKSKEISQDLRKKIVDLHKSGSSLGAISKRLKVPRSSVQTIVRKYKHHGTTQHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ASMGKSKEISQDLRKKIVDLHKSGSSLGAISKRLKVPRSSVQTIVRKYKHHGTTQHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	57	0	0	100.0

Content subtype: combined_19249_2m8e.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	328		96.5 (chain: A, length: 57)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	488 (1)	noe	96.5 (chain: A, length: 57)
2	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	52 (1)	hbond	66.7 (chain: A, length: 57)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	74 (74)	.	82.5 (chain: A, length: 57)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 96.5%
- Total number of assignments
  - ¹H chemical shifts: 274
  - ¹⁵N chemical shifts: 54
- 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	358	273	76.3
¹⁵N chemical shifts	63	54	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	117	109	93.2
¹⁵N chemical shifts	56	54	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	241	164	68.0
¹⁵N chemical shifts	7	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	30	24	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	5	35.7

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 96.5%
- Total number of restraints: 488
- Weight of restraints: 1.0 (488)
- Potential type of restraints: square-well-parabolic (488)
- Range of distance target values: 3.0, 4.0 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_2
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 57, Sequence coverage: 66.7%
  - Total number of restraints: 52
  - Weight of restraints: 1.0 (52)
  - Potential type of restraints: square-well-parabolic (52)
  - Range of distance target values: 2.25, 3.0 (Å)
  - Histogram of distance target values
  - 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: 57, Sequence coverage: 82.5%
- Total number of restraints: 74
- Total number of restraints per polymer type: 74
- Weight of restraints: 1.0 (74)
- Potential type of restraints: square-well-parabolic (74)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords protein

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Found 1 Document (0.685 seconds)

BMRB: 19249

Sample #1

Sample #2

Related entities 1. PAI subdomain of Sleeping Beauty transposase, : 1 : 19 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail