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Found 1 Document (0.812 seconds)

BMRB: 15987

2K9I

NMR structure of plasmid copy control protein ORF56 from sulfolobus islandicus

Authors

Weininger, U., Balbach, J.

Assembly

ORF56

Entity

1. ORF56 (polymer, Thiol state: not present), 55 monomers, 6523.541 × 2 Da Detail

GRPYKLLNGI KLGVYIPQEW HDRLMEIAKE KNLTLSDVCR LAIKEYLDNH DKQKK

Total weight

13047.082 Da

Max. entity weight

6523.541 Da

Source organism

Sulfolobus islandicus

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 98.6 %, Completeness (bb): 99.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	98.6 % (364 of 369)	98.6 % (364 of 369)
Backbone	99.1 % (110 of 111)	99.1 % (110 of 111)
Sidechain	98.4 % (254 of 258)	98.4 % (254 of 258)
Aromatic	100.0 % (22 of 22)	100.0 % (22 of 22)
Methyl	100.0 % (31 of 31)	100.0 % (31 of 31)

1. ORF56

GRPYKLLNGI KLGVYIPQEW HDRLMEIAKE KNLTLSDVCR LAIKEYLDNH DKQKK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 5.0

#	Name	Isotope labeling	Type	Concentration
1	entity_2	[U-13C; U-15N]		1 mM
2	entity_2	natural abundance		2 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2K9I, Strand ID: A, B Detail

Release date

2008-10-14

Citation

Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus
Weininger, U., Zeeb, M., Neumann, P., Low, C., Stubbs, M.T., Lipps, G., Balbach, J.
Biochemistry (2009), 48, 10030-10037, PubMed 19788170 , DOI 10.1021/bi900760n , Abstract

Related entities 1. ORF56, : 1 : 1 : 10 entities Detail

Experiments performed 8 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15987_2k9i.nef
Input source #2: Coordindates	2k9i.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------
GRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
GRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK
--------10--------20--------30--------40--------50-----

Entity_assembly_ID (NMR): B vs Auth_asym_ID (model): B

-------10--------20--------30--------40--------50------
GRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK
|||||||||||||||||||||||||||||||||||||||||||||||||||||||
GRPYKLLNGIKLGVYIPQEWHDRLMEIAKEKNLTLSDVCRLAIKEYLDNHDKQKK
--------10--------20--------30--------40--------50-----

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	55	0	0	100.0
B	B	55	0	0	100.0

Content subtype: combined_15987_2k9i.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	363		100.0 (chain: A, length: 55)
1	Distance restraints	CNS/XPLOR_distance_constraints_6	Warning	94 (1)	noe	38.2 (chain: A, length: 55), 41.8 (chain: B, length: 55)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	107 (1)	hbond	63.6 (chain: A, length: 55), 63.6 (chain: B, length: 55)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	160 (160)	.	80.0 (chain: A, length: 55), 80.0 (chain: B, length: 55)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 55, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 363
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
30	LYS	HZ1	8.006
30	LYS	HZ2	8.006
30	LYS	HZ3	8.006

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	369	360	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	111	110	99.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	258	250	96.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	32	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	22	22	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_6
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 55, Sequence coverage: 38.2%
  - Entity_assembly_ID: B, Chain length: 55, Sequence coverage: 41.8%
- Total number of restraints: 94
- Weight of restraints: 1.0 (94)
- Potential type of restraints: lower-bound-parabolic (4), square-well-parabolic (90)
- Range of distance target values: 1.8, 3.65 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 55, Sequence coverage: 63.6%
    - Entity_assembly_ID: B, Chain length: 55, Sequence coverage: 63.6%
  - Total number of restraints: 107
  - Weight of restraints: 1.0 (107)
  - Potential type of restraints: square-well-parabolic (107)
  - Range of distance target values: 2.05, 3.05 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 55, Sequence coverage: 80.0%
  - Entity_assembly_ID: B, Chain length: 55, Sequence coverage: 80.0%
- Total number of restraints: 160
- Total number of restraints per polymer type: 160
- Weight of restraints: 1.0 (160)
- Potential type of restraints: square-well-parabolic (160)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords plasmid copy control protein, ribbon helix helix protein

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Found 1 Document (0.812 seconds)

BMRB: 15987

Sample

Related entities 1. ORF56, : 1 : 1 : 10 entities Detail

Experiments performed 8 experiments Detail

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NMR combined restraints 5 contents Detail