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Found 1 Document (1.885 seconds)

BMRB: 34225

6FE6

Solution structure of a last generation P2-P4 macrocyclic inhibitor

Authors

Gallo, M., Eliseo, T., Cicero, D.O.

Assembly

Non-structural 3 protease

Entity

1. Non-structural 3 protease, entity 1 (polymer), 165 monomers, 17421.76 Da Detail

TGRDKNQVEG EVQVVSTATQ SFLATCVNGV CWTVYHGAGS KTLAGPKGPI TQMYTNVDQD LVGWQAPPGA RSLTPCTCGS SDLYLVTRHA DVIPVRRRGD SRGSLLSPRP VSYLKGSSGG PLLCPSGHAV GIFRAAVCTR GVAKAVDFVP VESMETTMRA SKKKK

2. Non-structural 3 protease, entity 4P2 (polymer, Thiol state: not present), 5 monomers, 793.9689 Da
3. Non-structural 3 protease, entity ZN (non-polymer), 65.409 Da

Total weight

18281.137 Da

Max. entity weight

17421.76 Da

Entity Connection

na 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS76:SG	3:ZN1:ZN
2	na	sing	1:CYS78:SG	3:ZN1:ZN

Source organism

Hepatitis C virus subtype 1b

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.7 %, Completeness: 79.5 %, Completeness (bb): 86.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	79.5 % (1430 of 1798)	81.6 % (757 of 928)	75.9 % (535 of 705)	83.6 % (138 of 165)
Backbone	86.5 % (837 of 968)	91.1 % (307 of 337)	82.8 % (395 of 477)	87.7 % (135 of 154)
Sidechain	72.3 % (706 of 977)	76.1 % (450 of 591)	67.5 % (253 of 375)	27.3 % (3 of 11)
Aromatic	61.2 % (60 of 98)	79.6 % (39 of 49)	40.4 % (19 of 47)	100.0 % (2 of 2)
Methyl	90.9 % (169 of 186)	92.5 % (86 of 93)	89.2 % (83 of 93)

1. entity 1

TGRDKNQVEG EVQVVSTATQ SFLATCVNGV CWTVYHGAGS KTLAGPKGPI TQMYTNVDQD LVGWQAPPGA RSLTPCTCGS SDLYLVTRHA DVIPVRRRGD SRGSLLSPRP VSYLKGSSGG PLLCPSGHAV GIFRAAVCTR GVAKAVDFVP VESMETTMRA SKKKK

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	HCV NS3 protease	[U-99% 15N]	500 uM
2	P2P4M	NA	500 uM
3	sodium chloride	NA	100 mM
4	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
5	DTT	NA	1 mM
6	sodium azide	NA	0.01 %

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] [U-99% 13C] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

Sample #3

Solvent system 100% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] [U-99% 13C] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 100% D2O

#	Name	Isotope labeling	Concentration
13	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
14	P2P4M	NA	500 uM
15	sodium chloride	NA	100 mM
16	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
17	DTT	NA	1 mM
18	sodium azide	NA	0.01 %

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	na	direct	1.0
¹⁵N	liquid anhydrous ammonia	nitrogen	na	indirect	0.1013291

Referencing offset: -0.45 ppm, Outliers: 2 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	na	direct	1.0
¹⁵N	liquid anhydrous ammonia	nitrogen	na	indirect	0.1013291

Referencing offset: -0.45 ppm, Outliers: 2 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	na	direct	1.0
¹⁵N	liquid anhydrous ammonia	nitrogen	na	indirect	0.1013291

Referencing offset: -0.2 ppm, Outliers: 1 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	na	direct	1.0
¹⁵N	liquid anhydrous ammonia	nitrogen	na	indirect	0.1013291

Referencing offset: 0.06 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 18 models in PDB: 6FE6, Strand ID: A Detail

Release date

2019-01-21

Citation

Solution structure of a last generation macrocyclic inhibitor. Hepatitis C virus NS3 protease complex: when S prime region occupancy is not enough to stabilize the protein conformation in the absence of NS4A
Gallo, M., Eliseo, T., Monteagudo, E.S., Sabetta, S., Paci, M., Summa, V., Cicero, D.O.

Related entities 1. Non-structural 3 protease, entity 1, : 1 : 4 : 2 : 1 : 128 entities Detail

Interaction partners 1. Non-structural 3 protease, entity 1, : 357 interactors Detail

More details for 357 interactors identified by 17 citations

Experiments performed 15 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	HCV NS3 protease	[U-99% 15N]	500 uM
2	P2P4M	NA	500 uM
3	sodium chloride	NA	100 mM
4	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
5	DTT	NA	1 mM
6	sodium azide	NA	0.01 %

2 2D 1H-15N HSQC

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] [U-99% 13C] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

3 2D 1H-13C HSQC aliphatic

Instrument

Bruker Avance - 700 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 (±0.01) atm, Temperature 308 (±0.2) K, pH 6.8 (±0.1), Details 500 uM [U-99% 15N] [U-99% 13C] HCV NS3 protease, 500 uM NA P2P4M, 100 mM NA sodium chloride, 0.3 % deuterated n-octyl beta-D-glucopyranoside, 1 mM NA DTT, 0.01 % NA sodium azide, 100% D2O

#	Name	Isotope labeling	Concentration
13	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
14	P2P4M	NA	500 uM
15	sodium chloride	NA	100 mM
16	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
17	DTT	NA	1 mM
18	sodium azide	NA	0.01 %

4 3D HNCO

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

5 3D HNCA

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

6 3D HN(CO)CA

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

7 2D 1H-13C HSQC aromatic

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
13	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
14	P2P4M	NA	500 uM
15	sodium chloride	NA	100 mM
16	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
17	DTT	NA	1 mM
18	sodium azide	NA	0.01 %

8 3D CBCANH

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

9 3D CBCA(CO)NH

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

10 3D 1H-15N NOESY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HCV NS3 protease	[U-99% 15N]	500 uM
2	P2P4M	NA	500 uM
3	sodium chloride	NA	100 mM
4	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
5	DTT	NA	1 mM
6	sodium azide	NA	0.01 %

11 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

12 3D 1H-15N TOCSY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
1	HCV NS3 protease	[U-99% 15N]	500 uM
2	P2P4M	NA	500 uM
3	sodium chloride	NA	100 mM
4	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
5	DTT	NA	1 mM
6	sodium azide	NA	0.01 %

13 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
8	P2P4M	NA	500 uM
9	sodium chloride	NA	100 mM
10	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
11	DTT	NA	1 mM
12	sodium azide	NA	0.01 %

14 F1-edited, F3-filtered 3D HMQC-NOESY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
13	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
14	P2P4M	NA	500 uM
15	sodium chloride	NA	100 mM
16	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
17	DTT	NA	1 mM
18	sodium azide	NA	0.01 %

15 double-filtered [F1-C/N,F2-C/N]-NOESY

Instrument

Bruker Avance - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
13	HCV NS3 protease	[U-99% 15N] [U-99% 13C]	500 uM
14	P2P4M	NA	500 uM
15	sodium chloride	NA	100 mM
16	n-octyl beta-D-glucopyranoside	deuterated	0.3 %
17	DTT	NA	1 mM
18	sodium azide	NA	0.01 %

NMR combined restraints 7 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34225_6fe6.nef
Input source #2: Coordindates	6fe6.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)
1:76:CYS:SG	3:1:ZN:ZN	unknown	unknown	n/a
1:78:CYS:SG	3:1:ZN:ZN	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	1	ZN	ZINC ION	Distance restraints
C	1	4P2	(3aR,7S,10S,12R,24aR)-7-cyclopentyl-N-{(1R,2S)-1-[(cyclopropylsulfonyl)carbamoyl]-2-ethenylcyclopropyl}-5,8-dioxo-1,2,3,3a,5,6,7,8,11,12,20,21,22,23,24,24a-hexadecahydro-10H-9,12-methanocyclopenta[18,19][1,10,3,6]dioxadiazacyclononadecino[12,11-b]quinoline-10-carboxamide	None

Sequence alignments

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

-------30--------40--------50--------60--------70--------80--------90-------100-------110-------120-
TGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
TGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGD
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

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

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	165	0	0	100.0

Content subtype: combined_34225_6fe6.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1404		97.0 (chain: A, length: 165)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1552 (1)	noe	93.9 (chain: A, length: 165)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	3447 (1)	noe	93.3 (chain: A, length: 165), 100.0 (chain: B, length: 1)
3	Distance restraints	CNS/XPLOR_distance_constraints_6	Warning	16 (1)	undefined	3.0 (chain: A, length: 165), 100.0 (chain: B, length: 1)
4	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	101 (1)	hbond	39.4 (chain: A, length: 165)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_7	OK	254 (254)	.	90.9 (chain: A, length: 165)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 97.0%
- Total number of assignments
  - ¹H chemical shifts: 748
  - ¹³C chemical shifts: 519
  - ¹⁵N chemical shifts: 137
- Completeness of assignments
  - Entity_assemble_ID: A
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
57	HIS	HD1	12.7
57	HIS	HE2	16.92
57	HIS	ND1	239.2
57	HIS	NE2	172.6
110	HIS	ND1	226.0
110	HIS	NE2	171.0
149	HIS	ND1	222.0
149	HIS	NE2	169.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	928	746	80.4
¹³C chemical shifts	705	519	73.6
¹⁵N chemical shifts	176	131	74.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	337	305	90.5
¹³C chemical shifts	330	275	83.3
¹⁵N chemical shifts	154	129	83.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	591	441	74.6
¹³C chemical shifts	375	244	65.1
¹⁵N chemical shifts	22	2	9.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	96	85	88.5
¹³C chemical shifts	96	82	85.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	39	79.6
¹³C chemical shifts	47	19	40.4
¹⁵N chemical shifts	2	2	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 93.9%
- Total number of restraints: 1552
- Weight of restraints: 1.0 (1552)
- Potential type of restraints: square-well-parabolic (1552)
- Range of distance target values: 2.22, 4.1 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
    None
  - Chain_ID: C
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 93.3%
    - Entity_assembly_ID: B, Chain length: 1, Sequence coverage: 100.0%
  - Total number of restraints: 3446
  - Weight of restraints: 1.0 (3446)
  - Potential type of restraints: square-well-parabolic (3446)
  - Range of distance target values: 1.9, 4.26 (Å)
  - Histogram of distance target values
  - Histogram of discrepancy in distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
    - Chain_ID: C
      None
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_6
    - Status: Warning
    - Experiment type: undefined
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 3.0%
      - Entity_assembly_ID: B, Chain length: 1, Sequence coverage: 100.0%
    - Total number of restraints: 16
    - Weight of restraints: 1.0 (16)
    - Potential type of restraints: square-well-parabolic (16)
    - Range of distance target values: 2.32, 4.26 (Å)
    - Histogram of distance target values
    - Distance restraints per residue
      - Chain_ID: A
      - Chain_ID: B
      - Chain_ID: C
        None
    - Distance restraints on contact map
    - Saveframe: CNS/XPLOR_distance_constraints_3
      - Status: Warning
      - Experiment type: hbond
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 39.4%
      - Total number of restraints: 101
        Total hydrogen bond restraints: 101
        O...H-x: 9
        O...h-N: 9
        Long range: 83
        O...H-x: 41
        O...h-N: 41
        O...h-N (too far!): 1
      - Weight of restraints: 1.0 (101)
        Total hydrogen bond restraints: 1.0 (101)
        O...H-x: 1.0 (9)
        O...h-N: 1.0 (9)
        Long range: 1.0 (83)
        O...H-x: 1.0 (41)
        O...h-N: 1.0 (41)
        O...h-N (too far!): 1.0 (1)
      - Potential type of restraints: square-well-parabolic (101)
        Total hydrogen bond restraints: square-well-parabolic (101)
        O...H-x: square-well-parabolic (9)
        O...h-N: square-well-parabolic (9)
        Long range: square-well-parabolic (83)
        O...H-x: square-well-parabolic (41)
        O...h-N: square-well-parabolic (41)
        O...h-N (too far!): square-well-parabolic (1)
      - Range of distance target values: 1.9, 3.55 (Å)
      - Histogram of distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
        None
        Chain_ID: C
        None
      - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_7
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 165, Sequence coverage: 90.9%
- Total number of restraints: 254
- Total number of restraints per polymer type: 254
- Weight of restraints: 1.0 (254)
- Potential type of restraints: square-well-parabolic (254)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Complex, HCV, Inhibitor, NS3 Protease, VIRAL PROTEIN

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Found 1 Document (1.885 seconds)

BMRB: 34225

Sample #1

Sample #2

Sample #3

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Non-structural 3 protease, entity 1, : 1 : 4 : 2 : 1 : 128 entities Detail

Interaction partners 1. Non-structural 3 protease, entity 1, : 357 interactors Detail

Experiments performed 15 experiments Detail

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NMR combined restraints 7 contents Detail