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BMRB: 19045

2M5B

The NMR structure of the BID-BAK complex

Authors

Grace, C.R., Kriwacki, R.W., Green, D.R.

Assembly

BID-BAK complex

Entity

1. human cBAK (polymer, Thiol state: all free), 169 monomers, 18933.09 Da Detail

ALPSASEEQV AQDTEEVFRS YVFYRHQQEQ EAEGVAAPAD PEMVTLPLQP SSTMGQVGRQ LAIIGDDINR RYDSEFQTML QHLQPTAENA YEYFTKIATS LFESGINWGR VVALLGFGYR LALHVYQHGL TGFLGQVTRF VVDFMLHHCI ARWIAQRGGW VAALNLGNG

2. human BID BH3 SAHB (polymer, Thiol state: not present), 23 monomers, 2528.928 Da Detail

EDIIRNIARH LAXVGDXXDR SIX

Total weight

21462.018 Da

Max. entity weight

18933.09 Da

Source organism

Exptl. method

Refine. method

torsion angle dynamics, simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 97.9 %, Completeness: 86.6 %, Completeness (bb): 80.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.6 % (1877 of 2167)	98.8 % (1102 of 1115)	70.6 % (598 of 847)	86.3 % (177 of 205)
Backbone	80.4 % (897 of 1116)	99.2 % (383 of 386)	65.1 % (357 of 548)	86.3 % (157 of 182)
Sidechain	92.9 % (1136 of 1223)	98.8 % (720 of 729)	84.1 % (396 of 471)	87.0 % (20 of 23)
Aromatic	83.8 % (176 of 210)	98.1 % (103 of 105)	68.6 % (70 of 102)	100.0 % (3 of 3)
Methyl	92.4 % (207 of 224)	100.0 % (112 of 112)	84.8 % (95 of 112)

1. human cBAK

ALPSASEEQV AQDTEEVFRS YVFYRHQQEQ EAEGVAAPAD PEMVTLPLQP SSTMGQVGRQ LAIIGDDINR RYDSEFQTML QHLQPTAENA YEYFTKIATS LFESGINWGR VVALLGFGYR LALHVYQHGL TGFLGQVTRF VVDFMLHHCI ARWIAQRGGW VAALNLGNG

2. human BID BH3 SAHB

EDIIRNIARH LAXVGDXXDR SIX

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2M5B, Strand ID: A, B Detail

Release date

2013-04-14

Citation

BID-induced structural changes in BAK promote apoptosis
Moldoveanu, T., Grace, C.R., Llambi, F., Nourse, A., Fitzgerald, P., Gehring, K., Kriwacki, R.W., Green, D.R.
Nat. Struct. Mol. Biol. (2013), 20, 589-597, PubMed 23604079 , DOI 10.1038/nsmb.2563 , Abstract

Related entities 1. human cBAK, : 1 : 13 entities Detail

Related entities 2. human BID BH3 SAHB, : 1 : 13 : 13 entities Detail

Interaction partners 2. human BID BH3 SAHB, : 38 interactors Detail

More details for 38 interactors identified by 14 citations

Experiments performed 21 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

2 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

3 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

4 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

5 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

6 2D 1H-1H COSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

7 3D CBCA(CO)NH

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

8 3D HNCA

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

9 3D HNCACB

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

10 3D HBHA(CBCACO)NH

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

11 3D 1H HCCH-TOCSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

12 3D 13C-detected HCC-TOCSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

13 2D 1H-15N TROSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

14 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

15 3D 1H-15N TOCSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

16 3D 1H-13C NOESY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

17 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

18 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

19 2D 13C-1H TROSY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

20 3D 13C/15N half-filtered 15N-edited NOESY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

21 3D 13C/15N half-filtered 13C-edited NOESY

Instrument

Bruker Avance - 600 MHz cryogenically cooled triple resonance z-gradient probe

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 300 K, pH 6.8, Details ~0.5 mM SAHB-BAK 20 mM Phosphate buffer pH 6.8

#	Name	Isotope labeling	Type	Concentration
1	human cBAK	[U-98% 13C; U-98% 15N]		0.5 mM
2	human BID BH3 SAHB	natural abundance		0.5 mM
3	Phosphate buffer	natural abundance		20 mM

NMR combined restraints 8 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19045_2m5b.nef
Input source #2: Coordindates	2m5b.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
2:12:ALA:C	2:13:MK8:N	unknown	unknown	n/a
2:13:MK8:C	2:14:VAL:N	unknown	unknown	n/a
2:16:ASP:C	2:17:MK8:N	unknown	unknown	n/a
2:17:MK8:C	2:18:NLE:N	unknown	unknown	n/a
2:18:NLE:C	2:19:ASP:N	unknown	unknown	n/a
2:22:ILE:C	2:23:NH2:N	unknown	unknown	n/a
2:13:MK8:CE	2:17:MK8:CE	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	92	MK8	2-methyl-L-norleucine	Assigned chemical shifts, Coordinates
B	96	MK8	2-methyl-L-norleucine	Assigned chemical shifts, Coordinates
B	97	NLE	NORLEUCINE	Assigned chemical shifts, Distance restraints, Coordinates
B	102	NH2	AMINO GROUP	Torsion angle restraints, Coordinates

Sequence alignments

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

--20-------30--------40--------50--------60--------70--------80--------90-------100-------110-------
ALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATS
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATS
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

120-------130-------140-------150-------160-------170-------180------
LFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG
-------110-------120-------130-------140-------150-------160---------

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

80-------90-------100--
EDIIRNIARHLAXVGDXXDRSIX
|||||||||||||||||||||||
EDIIRNIARHLAXVGDXXDRSIX
--------10--------20---

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	169	0	0	100.0
B	B	23	0	0	100.0

Content subtype: combined_19045_2m5b.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	7		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1863		100.0 (chain: A, length: 169), 95.7 (chain: B, length: 23)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	3171 (1)	noe	98.8 (chain: A, length: 169)
2	Distance restraints	DYANA/DIANA_distance_constraints_5	OK	350 (1)	noe	87.0 (chain: B, length: 23)
3	Distance restraints	DYANA/DIANA_distance_constraints_7	Warning	195 (1)	noe	10.7 (chain: A, length: 169), 56.5 (chain: B, length: 23)
4	Distance restraints	DYANA/DIANA_distance_constraints_4	Warning	205 (1)	hbond	55.6 (chain: A, length: 169)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_3	OK	218 (218)	.	88.8 (chain: A, length: 169)
2	Dihedral angle restraints	DYANA/DIANA_dihedral_6	OK	19 (19)	.	73.9 (chain: B, length: 23)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 23, Sequence coverage: 95.7%
- Total number of assignments
  - ¹H chemical shifts: 1131
  - ¹³C chemical shifts: 556
  - ¹⁵N chemical shifts: 176
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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
  - Chain_ID: B

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 98.8%
- Total number of restraints: 3158
- Weight of restraints: 1.0 (3158)
- Potential type of restraints: upper-bound-parabolic (3158)
- Range of distance target values: 2.4, 5.5 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
- Distance restraints on contact map
- Saveframe: DYANA/DIANA_distance_constraints_5
  - Status: OK
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: B, Chain length: 23, Sequence coverage: 87.0%
  - Total number of restraints: 349
  - Weight of restraints: 1.0 (349)
  - Potential type of restraints: upper-bound-parabolic (349)
  - Range of distance target values: 2.6, 5.5 (Å)
  - Histogram of distance target values
  - Histogram of discrepancy in distance target values
  - Distance restraints per residue
    - Chain_ID: A
      None
    - Chain_ID: B
  - Distance restraints on contact map
  - Saveframe: DYANA/DIANA_distance_constraints_7
    - Status: Warning
    - Experiment type: noe
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 10.7%
      - Entity_assembly_ID: B, Chain length: 23, Sequence coverage: 56.5%
    - Total number of restraints: 195
    - Weight of restraints: 1.0 (195)
    - Potential type of restraints: upper-bound-parabolic (195)
    - Range of distance target values: 3.24, 5.5 (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: DYANA/DIANA_distance_constraints_4
      - Status: Warning
      - Experiment type: hbond
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 55.6%
        --20-------30--------40--------50--------60--------70--------80--------90-------100-------110------- ALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATS || ||||||||||||||||||| || |||||||||||||| || || ||| |||||||| .....SE.QVAQDTEEVFRSYVFYRHQ.............................VG.QLAIIGDDINRRYD..FQ..LQ.......NAY.YFTKIATS --20-------30--------40--------50--------60--------70--------80--------90-------100-------110------- 120-------130-------140-------150-------160-------170-------180------ LFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG || | |||||||||||||||| | |||||||||||||| |||||||| LF....N.GRVVALLGFGYRLALH.Y......FLGQVTRFVVDFML...IARWIAQR 120-------130-------140-------150-------160-------170----
      - Total number of restraints: 205
        Total hydrogen bond restraints: 205
        O...H-x: 62
        O...h-N: 64
        O...H-x (too close!): 42
        O...h-N (too close!): 37
      - Weight of restraints: 1.0 (205)
        Total hydrogen bond restraints: 1.0 (205)
        O...H-x: 1.0 (62)
        O...h-N: 1.0 (64)
        O...H-x (too close!): 1.0 (42)
        O...h-N (too close!): 1.0 (37)
      - Potential type of restraints: upper-bound-parabolic (205)
        Total hydrogen bond restraints: upper-bound-parabolic (205)
        O...H-x: upper-bound-parabolic (62)
        O...h-N: upper-bound-parabolic (64)
        O...H-x (too close!): upper-bound-parabolic (42)
        O...h-N (too close!): upper-bound-parabolic (37)
      - Range of distance target values: 1.8, 3.0 (Å)
      - Histogram of distance target values
      - Histogram of discrepancy in distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        None
      - Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 169, Sequence coverage: 88.8%
- Total number of restraints: 218
- Total number of restraints per polymer type: 218
- Weight of restraints: 1.0 (218)
- Potential type of restraints: square-well-parabolic (218)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
- Saveframe: DYANA/DIANA_dihedral_6
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: B, Chain length: 23, Sequence coverage: 73.9%
  - Total number of restraints: 19
  - Total number of restraints per polymer type: 19
  - Weight of restraints: 1.0 (19)
  - Potential type of restraints: square-well-parabolic (19)
  - Plot of Phi-Psi angle restraints
  - Dihedral angle restraints per residue
    - Chain_ID: B

Keywords BCL-2 family effector BAK, BH3-only protein BID, effector direct activation, mitochondrial outer membrane premeabilization and apoptosis, NMR solution structure of BID-BAK