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Found 1 Document (0.891 seconds)

BMRB: 19614

2MH3

The basic-helix-loop-helix region of the transcriptional repressor HES-1 is preorganized to bind DNA

Authors

Wienk, H., Popovic, M., Coglievina, M., Boelens, R., Pongor, S., Pintar, A.

Assembly

basic-helix-loop-helix region of the transcriptional repressor HES-1

Entity

1. basic-helix-loop-helix region of the transcriptional repressor HES-1 (polymer, Thiol state: not present), 70 monomers, 8205.550 × 2 Da Detail

MKPKTASEHR KSSKPIMEKR RRARINESLS QLKTLILDAL KKDSSRHSKL EKADILEMTV KHLRNLQRAQ

Total weight

16411.1 Da

Max. entity weight

8205.55 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

restrained molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.4 %, Completeness (bb): 97.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.4 % (793 of 868)	89.1 % (417 of 468)	93.0 % (304 of 327)	98.6 % (72 of 73)
Backbone	97.8 % (407 of 416)	96.4 % (133 of 138)	98.6 % (207 of 210)	98.5 % (67 of 68)
Sidechain	87.2 % (455 of 522)	86.1 % (284 of 330)	88.8 % (166 of 187)	100.0 % (5 of 5)
Aromatic	33.3 % (4 of 12)	33.3 % (2 of 6)	33.3 % (2 of 6)
Methyl	97.2 % (70 of 72)	100.0 % (36 of 36)	94.4 % (34 of 36)

1. entity

MKPKTASEHR KSSKPIMEKR RRARINESLS QLKTLILDAL KKDSSRHSKL EKADILEMTV KHLRNLQRAQ

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 288 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	entity	[U-99% 13C; U-99% 15N]	2 mM
2	potassium phosphate	natural abundance	50 mM
3	H2O	natural abundance	90 %
4	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.07 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.07 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: 0.05 ppm, Outliers: 2 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	na	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	na	indirect	0.1013291

Referencing offset: -0.43 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2MH3, Strand ID: A, B Detail

Release date

2014-02-02

Citation

The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA
Popovic, M., Wienk, H., Coglievina, M., Boelens, R., Pongor, S., Pintar, A.
Proteins (2014), 82, 537-545, PubMed 24403087 , DOI 10.1002/prot.24507 , Abstract

Related entities 1. basic-helix-loop-helix region of the transcriptional repressor HES-1, : 1 : 11 : 121 entities Detail

Interaction partners 1. basic-helix-loop-helix region of the transcriptional repressor HES-1, : 13 interactors Detail

More details for 13 interactors identified by 3 citations

Experiments performed 4 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19614_2mh3.nef
Input source #2: Coordindates	2mh3.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

---30--------40--------50--------60--------70--------80--------90-----
MKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQ
--------10--------20--------30--------40--------50--------60--------70

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

---30--------40--------50--------60--------70--------80--------90-----
MKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQ
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MKPKTASEHRKSSKPIMEKRRRARINESLSQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRAQ
--------10--------20--------30--------40--------50--------60--------70

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	70	0	0	100.0
B	B	70	0	0	100.0

Content subtype: combined_19614_2mh3.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	787		100.0 (chain: A, length: 70)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	3138 (1)	noe	85.7 (chain: A, length: 70), 85.7 (chain: B, length: 70)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	140 (1)	hbond	61.4 (chain: A, length: 70), 61.4 (chain: B, length: 70)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	192 (192)	.	78.6 (chain: A, length: 70), 78.6 (chain: B, length: 70)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 414
  - ¹³C chemical shifts: 302
  - ¹⁵N chemical shifts: 71
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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 (%)
¹H chemical shifts	468	414	88.5
¹³C chemical shifts	327	302	92.4
¹⁵N chemical shifts	81	71	87.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	138	132	95.7
¹³C chemical shifts	140	138	98.6
¹⁵N chemical shifts	68	66	97.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	330	282	85.5
¹³C chemical shifts	187	164	87.7
¹⁵N chemical shifts	13	5	38.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	39	37	94.9
¹³C chemical shifts	39	34	87.2

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

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 85.7%
  - Entity_assembly_ID: B, Chain length: 70, Sequence coverage: 85.7%
- Total number of restraints: 3128
- Weight of restraints: 1.0 (3128)
- Potential type of restraints: square-well-parabolic (3128)
- Range of distance target values: 1.2, 2.75 (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: 70, Sequence coverage: 61.4%
    - Entity_assembly_ID: B, Chain length: 70, Sequence coverage: 61.4%
  - Total number of restraints: 140
  - Weight of restraints: 1.0 (140)
  - Potential type of restraints: square-well-parabolic (140)
  - 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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 70, Sequence coverage: 78.6%
  - Entity_assembly_ID: B, Chain length: 70, Sequence coverage: 78.6%
- Total number of restraints: 192
- Total number of restraints per polymer type: 192
- Weight of restraints: 1.0 (192)
- Potential type of restraints: square-well-parabolic (192)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords bHLH

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Found 1 Document (0.891 seconds)

BMRB: 19614

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. basic-helix-loop-helix region of the transcriptional repressor HES-1, : 1 : 11 : 121 entities Detail

Interaction partners 1. basic-helix-loop-helix region of the transcriptional repressor HES-1, : 13 interactors Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail