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- PDB-2y26: Transmission defective mutant of Grapevine Fanleaf virus -

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Basic information

Entry
Database: PDB / ID: 2y26
TitleTransmission defective mutant of Grapevine Fanleaf virus
ComponentsCOAT PROTEIN
KeywordsVIRUS / GFLV / FANLEAF DISEASE
Function / homology
Function and homology information


transport of virus in host, cell to cell / host cell plasmodesma / viral capsid / host cell cytoplasm / host cell nucleus / structural molecule activity
Similarity search - Function
Nepovirus subgroup A, RNA2 polyprotein, Protein 2A / Nepovirus subgroup A polyprotein / Nepovirus coat protein / Nepovirus coat protein, C-terminal / Nepovirus coat protein, N-terminal / Nepovirus coat protein, central domain / Nepovirus coat protein, C-terminal domain / Nepovirus coat protein, N-terminal domain / Jelly Rolls - #20 / Viral coat protein subunit ...Nepovirus subgroup A, RNA2 polyprotein, Protein 2A / Nepovirus subgroup A polyprotein / Nepovirus coat protein / Nepovirus coat protein, C-terminal / Nepovirus coat protein, N-terminal / Nepovirus coat protein, central domain / Nepovirus coat protein, C-terminal domain / Nepovirus coat protein, N-terminal domain / Jelly Rolls - #20 / Viral coat protein subunit / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesGRAPEVINE FANLEAF VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsSchellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.
Citation
Journal: Plos Pathog. / Year: 2011
Title: Structural Insights Into Viral Determinants of Nematode Mediated Grapevine Fanleaf Virus Transmission.
Authors: Schellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.
#1: Journal: J.Struct.Biol. / Year: 2011
Title: Strategies for the Crystallization of Viruses: Using Phase Diagrams and Gels to Produce 3D Crystals of Grapevine Fanleaf Virus.
Authors: Schellenberger, P. / Demangeat, G. / Lemaire, O. / Ritzenthaler, C. / Bergdoll, M. / Olieric, V. / Sauter, C. / Lorber, B.
History
DepositionDec 13, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 8, 2011Provider: repository / Type: Initial release
Revision 1.1Dec 28, 2011Group: Database references / Refinement description / Version format compliance
Revision 1.2Oct 22, 2014Group: Atomic model / Database references / Other
Revision 1.3Mar 6, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.4May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.5May 1, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: COAT PROTEIN
B: COAT PROTEIN
C: COAT PROTEIN
D: COAT PROTEIN
E: COAT PROTEIN
F: COAT PROTEIN
G: COAT PROTEIN
H: COAT PROTEIN
I: COAT PROTEIN
J: COAT PROTEIN
K: COAT PROTEIN
L: COAT PROTEIN
M: COAT PROTEIN
N: COAT PROTEIN
O: COAT PROTEIN
P: COAT PROTEIN
Q: COAT PROTEIN
R: COAT PROTEIN
S: COAT PROTEIN
T: COAT PROTEIN


Theoretical massNumber of molelcules
Total (without water)1,122,62420
Polymers1,122,62420
Non-polymers00
Water10,016556
1
A: COAT PROTEIN
B: COAT PROTEIN
C: COAT PROTEIN
D: COAT PROTEIN
E: COAT PROTEIN
F: COAT PROTEIN
G: COAT PROTEIN
H: COAT PROTEIN
I: COAT PROTEIN
J: COAT PROTEIN
K: COAT PROTEIN
L: COAT PROTEIN
M: COAT PROTEIN
N: COAT PROTEIN
O: COAT PROTEIN
P: COAT PROTEIN
Q: COAT PROTEIN
R: COAT PROTEIN
S: COAT PROTEIN
T: COAT PROTEIN

A: COAT PROTEIN
B: COAT PROTEIN
C: COAT PROTEIN
D: COAT PROTEIN
E: COAT PROTEIN
F: COAT PROTEIN
G: COAT PROTEIN
H: COAT PROTEIN
I: COAT PROTEIN
J: COAT PROTEIN
K: COAT PROTEIN
L: COAT PROTEIN
M: COAT PROTEIN
N: COAT PROTEIN
O: COAT PROTEIN
P: COAT PROTEIN
Q: COAT PROTEIN
R: COAT PROTEIN
S: COAT PROTEIN
T: COAT PROTEIN

A: COAT PROTEIN
B: COAT PROTEIN
C: COAT PROTEIN
D: COAT PROTEIN
E: COAT PROTEIN
F: COAT PROTEIN
G: COAT PROTEIN
H: COAT PROTEIN
I: COAT PROTEIN
J: COAT PROTEIN
K: COAT PROTEIN
L: COAT PROTEIN
M: COAT PROTEIN
N: COAT PROTEIN
O: COAT PROTEIN
P: COAT PROTEIN
Q: COAT PROTEIN
R: COAT PROTEIN
S: COAT PROTEIN
T: COAT PROTEIN


Theoretical massNumber of molelcules
Total (without water)3,367,87160
Polymers3,367,87160
Non-polymers00
Water1,08160
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation2
Buried area396300 Å2
ΔGint-1941 kcal/mol
Surface area961590 Å2
2


  • Idetical with deposited unit
  • point asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3


  • Idetical with deposited unit in distinct coordinate
  • point asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
Unit cell
Length a, b, c (Å)408.000, 408.000, 408.000
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number198
Space group name H-MP213
SymmetryPoint symmetry: (Schoenflies symbol: C (n fold cyclic))
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
111
121
131
141
151
161
171
181
191
201
12
22
32
42
52
62
72
82
92
102
112
122
132
142
152
162
172
182
192
202
13
23
33
43
53
63
73
83
93
103
113
123
133
143
153
163
173
183
193
203
14
24
34
44
54
64
74
84
94
104
114
124
134
144
154
164
174
184
194
204

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:8 )
211CHAIN B AND (RESSEQ 1:8 )
311CHAIN C AND (RESSEQ 1:8 )
411CHAIN D AND (RESSEQ 1:8 )
511CHAIN E AND (RESSEQ 1:8 )
611CHAIN F AND (RESSEQ 1:8 )
711CHAIN G AND (RESSEQ 1:8 )
811CHAIN H AND (RESSEQ 1:8 )
911CHAIN I AND (RESSEQ 1:8 )
1011CHAIN J AND (RESSEQ 1:8 )
1111CHAIN K AND (RESSEQ 1:8 )
1211CHAIN L AND (RESSEQ 1:8 )
1311CHAIN M AND (RESSEQ 1:8 )
1411CHAIN N AND (RESSEQ 1:8 )
1511CHAIN O AND (RESSEQ 1:8 )
1611CHAIN P AND (RESSEQ 1:8 )
1711CHAIN Q AND (RESSEQ 1:8 )
1811CHAIN R AND (RESSEQ 1:8 )
1911CHAIN S AND (RESSEQ 1:8 )
2011CHAIN T AND (RESSEQ 1:8 )
112CHAIN A AND (RESSEQ 10:14 )
212CHAIN B AND (RESSEQ 10:14 )
312CHAIN C AND (RESSEQ 10:14 )
412CHAIN D AND (RESSEQ 10:14 )
512CHAIN E AND (RESSEQ 10:14 )
612CHAIN F AND (RESSEQ 10:14 )
712CHAIN G AND (RESSEQ 10:14 )
812CHAIN H AND (RESSEQ 10:14 )
912CHAIN I AND (RESSEQ 10:14 )
1012CHAIN J AND (RESSEQ 10:14 )
1112CHAIN K AND (RESSEQ 10:14 )
1212CHAIN L AND (RESSEQ 10:14 )
1312CHAIN M AND (RESSEQ 10:14 )
1412CHAIN N AND (RESSEQ 10:14 )
1512CHAIN O AND (RESSEQ 10:14 )
1612CHAIN P AND (RESSEQ 10:14 )
1712CHAIN Q AND (RESSEQ 10:14 )
1812CHAIN R AND (RESSEQ 10:14 )
1912CHAIN S AND (RESSEQ 10:14 )
2012CHAIN T AND (RESSEQ 10:14 )
113CHAIN A AND (RESSEQ 20:258 )
213CHAIN B AND (RESSEQ 20:258 )
313CHAIN C AND (RESSEQ 20:258 )
413CHAIN D AND (RESSEQ 20:258 )
513CHAIN E AND (RESSEQ 20:258 )
613CHAIN F AND (RESSEQ 20:258 )
713CHAIN G AND (RESSEQ 20:258 )
813CHAIN H AND (RESSEQ 20:258 )
913CHAIN I AND (RESSEQ 20:258 )
1013CHAIN J AND (RESSEQ 20:258 )
1113CHAIN K AND (RESSEQ 20:258 )
1213CHAIN L AND (RESSEQ 20:258 )
1313CHAIN M AND (RESSEQ 20:258 )
1413CHAIN N AND (RESSEQ 20:258 )
1513CHAIN O AND (RESSEQ 20:258 )
1613CHAIN P AND (RESSEQ 20:258 )
1713CHAIN Q AND (RESSEQ 20:258 )
1813CHAIN R AND (RESSEQ 20:258 )
1913CHAIN S AND (RESSEQ 20:258 )
2013CHAIN T AND (RESSEQ 20:258 )
114CHAIN A AND (RESSEQ 266:504 )
214CHAIN B AND (RESSEQ 266:504 )
314CHAIN C AND (RESSEQ 266:504 )
414CHAIN D AND (RESSEQ 266:504 )
514CHAIN E AND (RESSEQ 266:504 )
614CHAIN F AND (RESSEQ 266:504 )
714CHAIN G AND (RESSEQ 266:504 )
814CHAIN H AND (RESSEQ 266:504 )
914CHAIN I AND (RESSEQ 266:504 )
1014CHAIN J AND (RESSEQ 266:504 )
1114CHAIN K AND (RESSEQ 266:504 )
1214CHAIN L AND (RESSEQ 266:504 )
1314CHAIN M AND (RESSEQ 266:504 )
1414CHAIN N AND (RESSEQ 266:504 )
1514CHAIN O AND (RESSEQ 266:504 )
1614CHAIN P AND (RESSEQ 266:504 )
1714CHAIN Q AND (RESSEQ 266:504 )
1814CHAIN R AND (RESSEQ 266:504 )
1914CHAIN S AND (RESSEQ 266:504 )
2014CHAIN T AND (RESSEQ 266:504 )

NCS ensembles :
ID
1
2
3
4

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Components

#1: Protein
COAT PROTEIN / 2C-CP / RNA2 POLYPROTEIN CHAIN 3


Mass: 56131.176 Da / Num. of mol.: 20 / Mutation: YES / Source method: isolated from a natural source / Source: (natural) GRAPEVINE FANLEAF VIRUS / Strain: GFLV-TD / References: UniProt: P18474
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 556 / Source method: isolated from a natural source / Formula: H2O
Compound detailsNATURAL MUTATION IN CHAIN A, GLY 902 TO ASP NATURAL MUTATION IN CHAIN B, GLY 902 TO ASP NATURAL ...NATURAL MUTATION IN CHAIN A, GLY 902 TO ASP NATURAL MUTATION IN CHAIN B, GLY 902 TO ASP NATURAL MUTATION IN CHAIN C, GLY 902 TO ASP NATURAL MUTATION IN CHAIN D, GLY 902 TO ASP NATURAL MUTATION IN CHAIN E, GLY 902 TO ASP NATURAL MUTATION IN CHAIN F, GLY 902 TO ASP NATURAL MUTATION IN CHAIN G, GLY 902 TO ASP NATURAL MUTATION IN CHAIN H, GLY 902 TO ASP NATURAL MUTATION IN CHAIN I, GLY 902 TO ASP NATURAL MUTATION IN CHAIN J, GLY 902 TO ASP NATURAL MUTATION IN CHAIN K, GLY 902 TO ASP NATURAL MUTATION IN CHAIN L, GLY 902 TO ASP NATURAL MUTATION IN CHAIN M, GLY 902 TO ASP NATURAL MUTATION IN CHAIN N, GLY 902 TO ASP NATURAL MUTATION IN CHAIN O, GLY 902 TO ASP NATURAL MUTATION IN CHAIN P, GLY 902 TO ASP NATURAL MUTATION IN CHAIN Q, GLY 902 TO ASP NATURAL MUTATION IN CHAIN R, GLY 902 TO ASP NATURAL MUTATION IN CHAIN S, GLY 902 TO ASP NATURAL MUTATION IN CHAIN T, GLY 902 TO ASP
Sequence detailsRESIDUES 606 TO 1109 OF RNA2 POLYPROTEIN WITH A MUTATION AT POSITION 902 (G297D VARIANT OF THE COAT PROTEIN)

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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: 5 Å3/Da / Density % sol: 75 %
Description: THE PROTEIN CONTENT OF THIS CRYSTAL WAS 0.25 OF THE UNIT CELL WHICH CORRESPONDS TO A VM OF 5. WHEN THE VIRAL CAVITY THAT CONTAINS THE GENOMIC RNA IS EXCLUDED, THE ACTUAL FRACTION OF UNIT ...Description: THE PROTEIN CONTENT OF THIS CRYSTAL WAS 0.25 OF THE UNIT CELL WHICH CORRESPONDS TO A VM OF 5. WHEN THE VIRAL CAVITY THAT CONTAINS THE GENOMIC RNA IS EXCLUDED, THE ACTUAL FRACTION OF UNIT CELL OCCUPIED BY SOLVENT IS ABOUT 0.25.
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: LARGE CRYSTALS OF GFLV-TD WERE GROWN IN 10 DAYS AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 4 MG/ML AND A RESERVOIR CONTAINING 7% (M/V) PEG 3350, 0.1 M ...Details: LARGE CRYSTALS OF GFLV-TD WERE GROWN IN 10 DAYS AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 4 MG/ML AND A RESERVOIR CONTAINING 7% (M/V) PEG 3350, 0.1 M HEPES NA PH 7.5, 0.2 M PROLINE.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.98
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 8, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.7→38 Å / Num. obs: 604343 / % possible obs: 98.9 % / Observed criterion σ(I): 0 / Redundancy: 10.7 % / Biso Wilson estimate: 44.49 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 17.25
Reflection shellResolution: 2.7→2.77 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.91 / Mean I/σ(I) obs: 1.31 / % possible all: 91.7

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: EM MAP

Resolution: 2.7→35.784 Å / SU ML: 0.38 / σ(F): 1.34 / Phase error: 21.69 / Stereochemistry target values: ML / Details: NONE
RfactorNum. reflection% reflection
Rfree0.2103 30292 5 %
Rwork0.1925 --
obs0.1934 604343 98.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 9.702 Å2 / ksol: 0.318 e/Å3
Displacement parametersBiso mean: 40.86 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 2.7→35.784 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms79100 0 0 556 79656
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00981237
X-RAY DIFFRACTIONf_angle_d1.188110500
X-RAY DIFFRACTIONf_dihedral_angle_d14.64428880
X-RAY DIFFRACTIONf_chiral_restr0.07812320
X-RAY DIFFRACTIONf_plane_restr0.00514040
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A51X-RAY DIFFRACTIONPOSITIONAL
12B51X-RAY DIFFRACTIONPOSITIONAL0.033
13C51X-RAY DIFFRACTIONPOSITIONAL0.033
14D51X-RAY DIFFRACTIONPOSITIONAL0.036
15E51X-RAY DIFFRACTIONPOSITIONAL0.037
16F51X-RAY DIFFRACTIONPOSITIONAL0.038
17G51X-RAY DIFFRACTIONPOSITIONAL0.037
18H51X-RAY DIFFRACTIONPOSITIONAL0.031
19I51X-RAY DIFFRACTIONPOSITIONAL0.039
110J51X-RAY DIFFRACTIONPOSITIONAL0.032
111K51X-RAY DIFFRACTIONPOSITIONAL0.035
112L51X-RAY DIFFRACTIONPOSITIONAL0.036
113M51X-RAY DIFFRACTIONPOSITIONAL0.033
114N51X-RAY DIFFRACTIONPOSITIONAL0.065
115O51X-RAY DIFFRACTIONPOSITIONAL0.041
116P51X-RAY DIFFRACTIONPOSITIONAL0.053
117Q51X-RAY DIFFRACTIONPOSITIONAL0.035
118R51X-RAY DIFFRACTIONPOSITIONAL0.035
119S51X-RAY DIFFRACTIONPOSITIONAL0.037
120T51X-RAY DIFFRACTIONPOSITIONAL0.036
21A38X-RAY DIFFRACTIONPOSITIONAL
22B38X-RAY DIFFRACTIONPOSITIONAL0.031
23C38X-RAY DIFFRACTIONPOSITIONAL0.033
24D38X-RAY DIFFRACTIONPOSITIONAL0.031
25E38X-RAY DIFFRACTIONPOSITIONAL0.038
26F38X-RAY DIFFRACTIONPOSITIONAL0.028
27G38X-RAY DIFFRACTIONPOSITIONAL0.025
28H38X-RAY DIFFRACTIONPOSITIONAL0.028
29I38X-RAY DIFFRACTIONPOSITIONAL0.034
210J38X-RAY DIFFRACTIONPOSITIONAL0.031
211K38X-RAY DIFFRACTIONPOSITIONAL0.027
212L38X-RAY DIFFRACTIONPOSITIONAL0.036
213M38X-RAY DIFFRACTIONPOSITIONAL0.029
214N38X-RAY DIFFRACTIONPOSITIONAL0.038
215O38X-RAY DIFFRACTIONPOSITIONAL0.035
216P38X-RAY DIFFRACTIONPOSITIONAL0.042
217Q38X-RAY DIFFRACTIONPOSITIONAL0.032
218R38X-RAY DIFFRACTIONPOSITIONAL0.043
219S38X-RAY DIFFRACTIONPOSITIONAL0.035
220T38X-RAY DIFFRACTIONPOSITIONAL0.03
31A1869X-RAY DIFFRACTIONPOSITIONAL
32B1869X-RAY DIFFRACTIONPOSITIONAL0.115
33C1869X-RAY DIFFRACTIONPOSITIONAL0.034
34D1869X-RAY DIFFRACTIONPOSITIONAL0.035
35E1869X-RAY DIFFRACTIONPOSITIONAL0.144
36F1869X-RAY DIFFRACTIONPOSITIONAL0.116
37G1869X-RAY DIFFRACTIONPOSITIONAL0.116
38H1869X-RAY DIFFRACTIONPOSITIONAL0.116
39I1869X-RAY DIFFRACTIONPOSITIONAL0.117
310J1869X-RAY DIFFRACTIONPOSITIONAL0.116
311K1869X-RAY DIFFRACTIONPOSITIONAL0.036
312L1869X-RAY DIFFRACTIONPOSITIONAL0.038
313M1869X-RAY DIFFRACTIONPOSITIONAL0.118
314N1869X-RAY DIFFRACTIONPOSITIONAL0.118
315O1869X-RAY DIFFRACTIONPOSITIONAL0.039
316P1869X-RAY DIFFRACTIONPOSITIONAL0.043
317Q1869X-RAY DIFFRACTIONPOSITIONAL0.042
318R1869X-RAY DIFFRACTIONPOSITIONAL0.118
319S1869X-RAY DIFFRACTIONPOSITIONAL0.036
320T1869X-RAY DIFFRACTIONPOSITIONAL0.036
41A1878X-RAY DIFFRACTIONPOSITIONAL
42B1878X-RAY DIFFRACTIONPOSITIONAL0.041
43C1878X-RAY DIFFRACTIONPOSITIONAL0.117
44D1878X-RAY DIFFRACTIONPOSITIONAL0.117
45E1878X-RAY DIFFRACTIONPOSITIONAL0.119
46F1878X-RAY DIFFRACTIONPOSITIONAL0.039
47G1878X-RAY DIFFRACTIONPOSITIONAL0.041
48H1878X-RAY DIFFRACTIONPOSITIONAL0.039
49I1878X-RAY DIFFRACTIONPOSITIONAL0.041
410J1878X-RAY DIFFRACTIONPOSITIONAL0.117
411K1878X-RAY DIFFRACTIONPOSITIONAL0.045
412L1878X-RAY DIFFRACTIONPOSITIONAL0.041
413M1878X-RAY DIFFRACTIONPOSITIONAL0.045
414N1878X-RAY DIFFRACTIONPOSITIONAL0.04
415O1878X-RAY DIFFRACTIONPOSITIONAL0.119
416P1878X-RAY DIFFRACTIONPOSITIONAL0.119
417Q1878X-RAY DIFFRACTIONPOSITIONAL0.043
418R1878X-RAY DIFFRACTIONPOSITIONAL0.04
419S1878X-RAY DIFFRACTIONPOSITIONAL0.12
420T1878X-RAY DIFFRACTIONPOSITIONAL0.041
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7-2.73070.3469150.326817525X-RAY DIFFRACTION91
2.7307-2.76280.3489150.323817819X-RAY DIFFRACTION93
2.7628-2.79650.34579290.312618183X-RAY DIFFRACTION94
2.7965-2.83190.334510340.30618434X-RAY DIFFRACTION96
2.8319-2.86910.3199710.297818870X-RAY DIFFRACTION98
2.8691-2.90840.318310090.280819025X-RAY DIFFRACTION99
2.9084-2.94990.287210070.267319211X-RAY DIFFRACTION100
2.9499-2.9940.283410570.264519173X-RAY DIFFRACTION100
2.994-3.04070.28019870.257119322X-RAY DIFFRACTION100
3.0407-3.09050.281210360.244519223X-RAY DIFFRACTION100
3.0905-3.14380.25769780.23619248X-RAY DIFFRACTION100
3.1438-3.20090.24819490.227319338X-RAY DIFFRACTION100
3.2009-3.26250.244110200.223619300X-RAY DIFFRACTION100
3.2625-3.3290.241110500.219319238X-RAY DIFFRACTION100
3.329-3.40130.223610240.20619277X-RAY DIFFRACTION100
3.4013-3.48040.232510360.205619228X-RAY DIFFRACTION100
3.4804-3.56740.218510040.196219362X-RAY DIFFRACTION100
3.5674-3.66370.22269620.188419328X-RAY DIFFRACTION100
3.6637-3.77140.199310210.17919326X-RAY DIFFRACTION100
3.7714-3.8930.188410710.168619257X-RAY DIFFRACTION100
3.893-4.0320.17979790.158419374X-RAY DIFFRACTION100
4.032-4.19320.167610150.14519304X-RAY DIFFRACTION100
4.1932-4.38370.147510560.135419312X-RAY DIFFRACTION100
4.3837-4.61430.14449880.125719372X-RAY DIFFRACTION100
4.6143-4.90280.135110670.1219389X-RAY DIFFRACTION100
4.9028-5.28020.133310370.117819341X-RAY DIFFRACTION100
5.2802-5.80960.145710730.139719419X-RAY DIFFRACTION100
5.8096-6.64560.165110470.155619470X-RAY DIFFRACTION100
6.6456-8.35510.167310280.158819588X-RAY DIFFRACTION100
8.3551-35.78710.188110270.185919795X-RAY DIFFRACTION99

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