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- PDB-4u01: HCV NS3/4A serine protease in complex with 6570 -

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Basic information

Entry
Database: PDB / ID: 4u01
TitleHCV NS3/4A serine protease in complex with 6570
Components
  • NS4A protein
  • Non-structural 3 protease
KeywordsHYDROLASE / HVC / NS3/4A protease / drug design / PROTEROS BIOSTRUCTURES GMBH
Function / homology
Function and homology information


positive stranded viral RNA replication / virion component => GO:0044423 / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity ...positive stranded viral RNA replication / virion component => GO:0044423 / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / viral process / serine-type peptidase activity / viral genome replication / SH3 domain binding / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / viral nucleocapsid / clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / ribonucleoprotein complex / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / ATP hydrolysis activity / protein-containing complex / proteolysis / RNA binding / zinc ion binding / ATP binding / identical protein binding / membrane
Similarity search - Function
Thrombin, subunit H - #120 / : / Hepatitis C virus core protein, chain A superfamily / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b ...Thrombin, subunit H - #120 / : / Hepatitis C virus core protein, chain A superfamily / Hepatitus C virus, Non-structural 5a protein, C-terminal / Hepatitis C virus NS5A, 1B domain superfamily / Hepatitis C virus non-structural protein NS2, C-terminal domain / Hepatitis C virus non-structural protein NS2, N-terminal domain / Hepatitis C virus non-structural protein NS2 / HCV NS5a protein C-terminal region / Hepatitis C virus, Non-structural protein NS4b / Hepatitis C virus, Core protein, N-terminal / Hepatitis C virus non-structural protein NS4b / Hepatitis C virus capsid protein / Hepatitis C virus, Non-structural protein NS2 / Hepatitis C virus, Non-structural 5a protein / Hepatitis C virus, Non-structural 5a protein, domain 1a / Hepatitis C virus non-structural 5a, 1B domain / NS5A domain 1a superfamily / Hepatitis C virus non-structural 5a protein membrane anchor / Hepatitis C virus non-structural 5a zinc finger domain / Hepatitis C virus non-structural 5a domain 1b / Hepacivirus nonstructural protein 2 (NS2) protease domain profile. / Hepatitis C virus, Non-structural protein NS4a / Hepatitis C virus non-structural protein NS4a / Hepatitis C virus, Core protein, C-terminal / Hepatitis C virus core protein / Hepatitis C virus, Non-structural protein E2/NS1 / Hepatitis C virus non-structural protein E2/NS1 / Hepatitis C virus, Envelope glycoprotein E1 / Hepatitis C virus envelope glycoprotein E1 / RNA dependent RNA polymerase, hepatitis C virus / Viral RNA dependent RNA polymerase / Hepatitis C virus, NS3 protease, Peptidase S29 / Hepatitis C virus NS3 protease / Hepacivirus/Pegivirus NS3 protease domain profile. / DEAD box, Flavivirus / Flavivirus DEAD domain / Trypsin-like serine proteases / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Thrombin, subunit H / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Chem-39W / Non-structural 3 protease / NS4A protein / Genome polyprotein
Similarity search - Component
Biological speciesHepatitis C virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsParsy, C.C. / Alexandre, F.-R. / Brandt, G. / Caillet, C. / Chaves, D. / Derock, M. / Gloux, D. / Griffon, Y. / Lallos, L.B. / Leroy, F. ...Parsy, C.C. / Alexandre, F.-R. / Brandt, G. / Caillet, C. / Chaves, D. / Derock, M. / Gloux, D. / Griffon, Y. / Lallos, L.B. / Leroy, F. / Liuzzi, M. / Loi, A.-G. / Mayes, B. / Moulat, L. / Moussa, A. / Chiara, M. / Roques, V. / Rosinovsky, E. / Seifer, M. / Stewart, A. / Wang, J. / Standring, D. / Surleraux, D.
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2015
Title: Discovery and structural diversity of the hepatitis C virus NS3/4A serine protease inhibitor series leading to clinical candidate IDX320.
Authors: Parsy, C.C. / Alexandre, F.R. / Bidau, V. / Bonnaterre, F. / Brandt, G. / Caillet, C. / Cappelle, S. / Chaves, D. / Convard, T. / Derock, M. / Gloux, D. / Griffon, Y. / Lallos, L.B. / Leroy, ...Authors: Parsy, C.C. / Alexandre, F.R. / Bidau, V. / Bonnaterre, F. / Brandt, G. / Caillet, C. / Cappelle, S. / Chaves, D. / Convard, T. / Derock, M. / Gloux, D. / Griffon, Y. / Lallos, L.B. / Leroy, F. / Liuzzi, M. / Loi, A.G. / Moulat, L. / Chiara, M. / Rahali, H. / Roques, V. / Rosinovsky, E. / Savin, S. / Seifer, M. / Standring, D. / Surleraux, D.
History
DepositionJul 11, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jul 29, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 14, 2015Group: Database references
Revision 1.2Nov 11, 2015Group: Database references
Revision 1.3May 8, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Non-structural 3 protease
B: Non-structural 3 protease
C: Non-structural 3 protease
D: Non-structural 3 protease
E: Non-structural 3 protease
F: Non-structural 3 protease
G: Non-structural 3 protease
H: Non-structural 3 protease
J: Non-structural 3 protease
K: NS4A protein
L: NS4A protein
M: NS4A protein
N: NS4A protein
O: NS4A protein
P: NS4A protein
Q: NS4A protein
T: NS4A protein
U: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)215,98240
Polymers208,33118
Non-polymers7,65122
Water00
1
A: Non-structural 3 protease
K: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9824
Polymers23,1482
Non-polymers8342
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2520 Å2
ΔGint-50 kcal/mol
Surface area9270 Å2
MethodPISA
2
B: Non-structural 3 protease
L: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0185
Polymers23,1482
Non-polymers8703
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2660 Å2
ΔGint-58 kcal/mol
Surface area9160 Å2
MethodPISA
3
C: Non-structural 3 protease
M: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9824
Polymers23,1482
Non-polymers8342
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2490 Å2
ΔGint-50 kcal/mol
Surface area9340 Å2
MethodPISA
4
D: Non-structural 3 protease
N: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0185
Polymers23,1482
Non-polymers8703
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2630 Å2
ΔGint-58 kcal/mol
Surface area9180 Å2
MethodPISA
5
E: Non-structural 3 protease
O: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0185
Polymers23,1482
Non-polymers8703
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2660 Å2
ΔGint-61 kcal/mol
Surface area9190 Å2
MethodPISA
6
F: Non-structural 3 protease
P: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9824
Polymers23,1482
Non-polymers8342
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2490 Å2
ΔGint-51 kcal/mol
Surface area9150 Å2
MethodPISA
7
G: Non-structural 3 protease
Q: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0185
Polymers23,1482
Non-polymers8703
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2620 Å2
ΔGint-57 kcal/mol
Surface area9160 Å2
MethodPISA
8
H: Non-structural 3 protease
T: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9824
Polymers23,1482
Non-polymers8342
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2500 Å2
ΔGint-49 kcal/mol
Surface area9120 Å2
MethodPISA
9
J: Non-structural 3 protease
U: NS4A protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9824
Polymers23,1482
Non-polymers8342
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2490 Å2
ΔGint-52 kcal/mol
Surface area9280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)150.034, 174.363, 133.010
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91J
12K
22L
32M
42N
52O
62P
72Q
82T
92U

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1116A1 - 1000
2116B1 - 1000
3116C1 - 1000
4116D1 - 1000
5116E1 - 1000
6116F1 - 1000
7116G1 - 1000
8116H1 - 1000
9116J1 - 1000
1126K210 - 245
2126L210 - 245
3126M210 - 245
4126N210 - 245
5126O210 - 245
6126P210 - 245
7126Q210 - 245
8126T210 - 245
9126U210 - 245

NCS ensembles :
ID
1
2

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Components

#1: Protein
Non-structural 3 protease


Mass: 21461.828 Da / Num. of mol.: 9 / Fragment: UNP residues 1-180
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hepatitis C virus (isolate Con1) / Production host: Escherichia coli (E. coli) / References: UniProt: A6N4J4, UniProt: Q9WMX2*PLUS
#2: Protein/peptide
NS4A protein


Mass: 1686.097 Da / Num. of mol.: 9 / Fragment: UNP residues 21-34
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hepatitis C virus / Gene: NS4A / Production host: Escherichia coli (E. coli) / References: UniProt: F0UY39
#3: Chemical
ChemComp-39W / (2S,3aS,10Z,11aS,12aR)-2-({8-fluoro-7-methoxy-2-[4-(propan-2-yl)-1,3-thiazol-2-yl]quinolin-4-yl}oxy)-5-methyl-N-[(1-methylcyclopropyl)sulfonyl]-4,14-dioxo-1,2,3,3a,4,5,6,7,8,9,11a,12,13,14-tetradecahydro-12aH-cyclopropa[m]pyrrolo[1,2-c][1,3,6]triazacyclotetradecine-12a-carboxamide / IDX320


Mass: 768.918 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C37H45FN6O7S2
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Zn
#5: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.03 Å3/Da / Density % sol: 39.34 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: PEG

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.007 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 14, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.007 Å / Relative weight: 1
ReflectionResolution: 2.8→43.23 Å / Num. all: 41838 / Num. obs: 41817 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 68.5 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 11.77
Reflection shellResolution: 2.8→3 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.619 / % possible all: 96.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→43.23 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.899 / SU B: 46.337 / SU ML: 0.454 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.479 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.28986 2088 5 %RANDOM
Rwork0.23336 ---
obs0.23618 39729 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 91.754 Å2
Baniso -1Baniso -2Baniso -3
1-0.66 Å20 Å20 Å2
2--1.08 Å20 Å2
3----1.74 Å2
Refinement stepCycle: 1 / Resolution: 2.8→43.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12870 0 490 0 13360
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02213635
X-RAY DIFFRACTIONr_bond_other_d0.0010.0212744
X-RAY DIFFRACTIONr_angle_refined_deg1.1892.01718675
X-RAY DIFFRACTIONr_angle_other_deg0.92329484
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.17451737
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.13421.633441
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.345152079
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.44415126
X-RAY DIFFRACTIONr_chiral_restr0.0620.22187
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0214967
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022646
X-RAY DIFFRACTIONr_nbd_refined0.1940.22579
X-RAY DIFFRACTIONr_nbd_other0.1760.212959
X-RAY DIFFRACTIONr_nbtor_refined0.1710.26585
X-RAY DIFFRACTIONr_nbtor_other0.0820.28266
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1270.2304
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1480.248
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1940.2130
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.150.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.664211064
X-RAY DIFFRACTIONr_mcbond_other0.10323636
X-RAY DIFFRACTIONr_mcangle_it0.896314013
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.29845922
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.92364554
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A2696loose positional0.35
12B2696loose positional0.45
13C2696loose positional0.475
14D2696loose positional0.275
15E2696loose positional0.265
16F2696loose positional0.295
17G2696loose positional0.295
18H2696loose positional0.285
19J2696loose positional0.265
21K203loose positional0.355
22L203loose positional0.295
23M203loose positional0.325
24N203loose positional0.385
25O203loose positional0.275
26P203loose positional0.315
27Q203loose positional0.275
28T203loose positional0.345
29U203loose positional0.325
11A2696loose thermal3.0510
12B2696loose thermal1.3510
13C2696loose thermal1.6810
14D2696loose thermal1.8310
15E2696loose thermal1.2810
16F2696loose thermal1.4810
17G2696loose thermal1.4610
18H2696loose thermal1.4510
19J2696loose thermal2.510
21K203loose thermal2.8110
22L203loose thermal1.3910
23M203loose thermal1.7710
24N203loose thermal1.3210
25O203loose thermal0.9810
26P203loose thermal1.410
27Q203loose thermal1.210
28T203loose thermal3.3910
29U203loose thermal1.5610
LS refinement shellResolution: 2.802→2.875 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.433 149 -
Rwork0.37 2890 -
obs--100 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
16.6694-0.58380.15454.0125-0.64956.5047-0.07050.2722-0.54030.0607-0.04630.1930.54070.2650.1169-0.6355-0.00050.0058-0.3367-0.0392-0.338469.1614.14-19.827
25.8612-0.02470.46552.86510.51368.3556-0.03181.1028-0.1292-0.3915-0.27980.43050.2316-1.24990.3116-0.53230.01590.0026-0.0743-0.0835-0.142555.41616.689-28.908
34.8862-1.28830.39817.42151.63889.9232-0.0780.0823-0.11360.0455-0.3150.90720.3571-0.73360.3931-0.3086-0.04540.0433-0.3771-0.06-0.229451.50212.0677.972
46.97312.0479-0.73394.3605-2.42798.47830.0651-1.52950.25471.5585-0.34050.72670.1807-0.95180.27530.1408-0.08460.2026-0.039-0.23660.02346.9514.16623.879
57.23672.8329-1.04399.02192.05485.06210.5005-0.7449-0.57841.5266-0.0404-0.92240.3816-0.1135-0.4601-0.12130.0923-0.2187-0.4040.0064-0.173785.9812.9099.115
69.2842.37160.80574.95150.82774.49970.4013-0.0628-0.51080.29080.151-1.5998-0.31351.1561-0.5524-0.1380.0589-0.2135-0.3299-0.15310.2457100.89219.0264.936
76.0822.85881.665710.84422.73628.47260.3207-0.29740.85621.056-0.6780.957-0.0582-0.33580.3572-0.61870.07710.1625-0.328-0.0177-0.255248.83343.915-6.724
85.96160.8860.70756.38741.34819.69-0.00421.22830.2069-1.2027-0.06450.71790.1724-0.16260.0687-0.45970.2461-0.1523-0.16690.0383-0.146645.62641.24-22.888
97.65450.17241.61577.68971.10384.94950.50410.55980.3278-0.7055-0.2981-0.34650.1120.1169-0.2061-0.4542-0.0158-0.1586-0.31890.0749-0.139482.18346.271-9.651
107.9049-0.9030.64096.8611-0.90856.33330.4420.38040.51110.13910.0191-1.65780.35411.2722-0.4612-0.47610.0575-0.1884-0.2063-0.03920.310997.80543.989-4.319
113.92171.74830.16266.8993-1.75388.2908-0.43540.02760.62550.17220.1917-0.132-1.00621.33010.2438-0.2443-0.2665-0.02530.022-0.0006-0.011267.28244.04920.43
128.60511.36010.09393.99711.21316.8804-0.5156-0.66080.28220.46430.06830.2376-0.7187-1.16050.4473-0.40520.05130.0387-0.3768-0.0529-0.130954.87939.57330.638
138.1405-1.23411.00887.697-2.96878.36960.6090.3889-0.1514-0.5302-0.7325-0.27240.3410.15310.1236-0.56140.0895-0.045-0.27760.0357-0.121268.11170.311-17.871
148.3135-2.18632.06595.4613-0.97327.58720.83281.2332-0.2698-1.3105-0.57140.69860.3014-0.8961-0.2613-0.16340.3336-0.13990.04530.00490.009355.75372.378-28.897
158.42231.68550.54997.5612.66616.6001-0.61941.0218-1.3873-1.04080.6217-0.42280.3728-0.2766-0.00230.0685-0.57940.24080.0049-0.19970.200949.63472.3649.457
1611.62515.4114-1.50268.04221.71875.2918-0.3571-1.0559-0.46620.65930.0509-0.1654-0.0326-0.31820.3061-0.0788-0.31020.1180.01790.12030.011646.07577.01125.047
179.7653-1.0905-0.07427.5699-2.91088.18040.4995-1.2881-0.2692.8481-0.1809-0.63230.18270.2587-0.31850.4316-0.0652-0.2218-0.0384-0.13310.253182.97172.46712.108
186.20194.44170.61184.22-0.44020.80310.0703-0.6579-0.66750.6091-0.4328-1.62170.53291.4890.36250.43440.1473-0.2180.5693-0.11781.408798.47774.5936.368
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 94
2X-RAY DIFFRACTION2A95 - 182
3X-RAY DIFFRACTION2K220 - 232
4X-RAY DIFFRACTION3B1 - 94
5X-RAY DIFFRACTION4B95 - 182
6X-RAY DIFFRACTION4L220 - 232
7X-RAY DIFFRACTION5C1 - 94
8X-RAY DIFFRACTION6C95 - 182
9X-RAY DIFFRACTION6M220 - 232
10X-RAY DIFFRACTION7D1 - 94
11X-RAY DIFFRACTION8D95 - 182
12X-RAY DIFFRACTION8N220 - 232
13X-RAY DIFFRACTION9E1 - 94
14X-RAY DIFFRACTION10E95 - 182
15X-RAY DIFFRACTION10O220 - 232
16X-RAY DIFFRACTION11F1 - 94
17X-RAY DIFFRACTION12F95 - 182
18X-RAY DIFFRACTION12P220 - 232
19X-RAY DIFFRACTION13G1 - 94
20X-RAY DIFFRACTION14G95 - 182
21X-RAY DIFFRACTION14Q220 - 232
22X-RAY DIFFRACTION15H1 - 94
23X-RAY DIFFRACTION16H95 - 182
24X-RAY DIFFRACTION16T220 - 232
25X-RAY DIFFRACTION17J1 - 94
26X-RAY DIFFRACTION18J95 - 182
27X-RAY DIFFRACTION18U220 - 232

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