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Found 1 Document (0.728 seconds)

BMRB: 30029

5IIV

GCN4p pH 1.5

Authors

Brady, M.R., Kaplan, A.R., Alexandrescu, A.T.

Assembly

General control protein GCN4

Entity

1. General control protein GCN4 (polymer, Thiol state: not present), 33 monomers, 3828.347 × 2 Da Detail

GSMKQLEDKV EELLSKNYHL ENEVARLKKL VGE

Total weight

7656.694 Da

Max. entity weight

3828.347 Da

Source organism

Saccharomyces cerevisiae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 80.4 %, Completeness (bb): 94.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	80.4 % (324 of 403)	78.0 % (167 of 214)	80.4 % (123 of 153)	94.4 % (34 of 36)
Backbone	94.9 % (188 of 198)	92.6 % (63 of 68)	96.9 % (94 of 97)	93.9 % (31 of 33)
Sidechain	70.8 % (167 of 236)	71.2 % (104 of 146)	69.0 % (60 of 87)	100.0 % (3 of 3)
Aromatic	0.0 % (0 of 12)	0.0 % (0 of 6)	0.0 % (0 of 6)
Methyl	68.4 % (26 of 38)	84.2 % (16 of 19)	52.6 % (10 of 19)

1. entity 1

GSMKQLEDKV EELLSKNYHL ENEVARLKKL VGE

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 1.5, Details 1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	GCN4p	[U-99% 13C; U-99% 15N]		1.5 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 1.5, Details 1.5 mM [U-99% 13C; U-99% 15N] GCN4p, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	GCN4p	[U-99% 13C; U-99% 15N]		1.5 mM

Protein Blocks Logo

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

Release date

2016-03-02

Citation

Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix
Kaplan, A.R., Brady, M.R., Maciejewski, M.W., Kammerer, R.A., Alexandrescu, A.T.
Biochemistry (2017), 56, 1604-1619, PubMed 28230348 , DOI 10.1021/acs.biochem.6b00634 , Abstract

Related entities 1. General control protein GCN4, : 1 : 5 : 58 : 76 entities Detail

Interaction partners 1. General control protein GCN4, : 13 interactors Detail

More details for 13 interactors identified by 9 citations

Experiments performed 7 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30029_5iiv.nef
Input source #2: Coordindates	5iiv.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---
GSMKQLEDKVEELLSKNYHLENEVARLKKLVGE
|||||||||||||||||||||||||||||||||
GSMKQLEDKVEELLSKNYHLENEVARLKKLVGE

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

--------10--------20--------30---
GSMKQLEDKVEELLSKNYHLENEVARLKKLVGE
|||||||||||||||||||||||||||||||||
GSMKQLEDKVEELLSKNYHLENEVARLKKLVGE

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	33	0	0	100.0
B	B	33	0	0	100.0

Content subtype: combined_30029_5iiv.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	322		100.0 (chain: A, length: 33)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	682 (1)	noe	93.9 (chain: A, length: 33), 93.9 (chain: B, length: 33)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	66 (1)	hbond	72.7 (chain: A, length: 33), 72.7 (chain: B, length: 33)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	130 (130)	.	87.9 (chain: A, length: 33), 87.9 (chain: B, length: 33)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 33, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 122
  - ¹H chemical shifts: 166
  - ¹⁵N chemical shifts: 34
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	153	122	79.7
¹H chemical shifts	214	166	77.6
¹⁵N chemical shifts	37	34	91.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	66	63	95.5
¹H chemical shifts	68	63	92.6
¹⁵N chemical shifts	33	31	93.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	87	59	67.8
¹H chemical shifts	146	103	70.5
¹⁵N chemical shifts	4	3	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	20	9	45.0
¹H chemical shifts	20	16	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	6	0	0.0
¹H chemical shifts	6	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 33, Sequence coverage: 93.9%
  - Entity_assembly_ID: B, Chain length: 33, Sequence coverage: 93.9%
- Total number of restraints: 682
- Weight of restraints: 1.0 (682)
- Potential type of restraints: square-well-parabolic (682)
- Range of distance target values: 2.19, 6.01 (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_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 33, Sequence coverage: 72.7%
    - Entity_assembly_ID: B, Chain length: 33, Sequence coverage: 72.7%
  - Total number of restraints: 66
  - Weight of restraints: 1.0 (66)
  - Potential type of restraints: square-well-parabolic (66)
  - Range of distance target values: 2.0, 3.0 (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: 33, Sequence coverage: 87.9%
  - Entity_assembly_ID: B, Chain length: 33, Sequence coverage: 87.9%
- Total number of restraints: 130
- Total number of restraints per polymer type: 130
- Weight of restraints: 1.0 (130)
- Potential type of restraints: square-well-parabolic (130)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Supercoil parameters, canonical alpha helix, closely related NMR structures, conformational transition, electrostatics, knobs-into-holes, leucine zipper, salt bridge

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Found 1 Document (0.728 seconds)

BMRB: 30029

Sample #1

Sample #2

Related entities 1. General control protein GCN4, : 1 : 5 : 58 : 76 entities Detail

Interaction partners 1. General control protein GCN4, : 13 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 5 contents Detail