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- PDB-3muu: Crystal structure of the Sindbis virus E2-E1 heterodimer at low pH -

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Basic information

Entry
Database: PDB / ID: 3muu
TitleCrystal structure of the Sindbis virus E2-E1 heterodimer at low pH
ComponentsStructural polyprotein
KeywordsVIRAL PROTEIN / Beta barrels / Ig-like folds
Function / homology
Function and homology information


icosahedral viral capsid, spike / togavirin / T=4 icosahedral viral capsid / ubiquitin-like protein ligase binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / clathrin-dependent endocytosis of virus by host cell / host cell cytoplasm / membrane fusion / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane ...icosahedral viral capsid, spike / togavirin / T=4 icosahedral viral capsid / ubiquitin-like protein ligase binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / clathrin-dependent endocytosis of virus by host cell / host cell cytoplasm / membrane fusion / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / structural molecule activity / virion attachment to host cell / host cell plasma membrane / virion membrane / proteolysis / RNA binding / membrane
Similarity search - Function
Alphavirus E2 glycoprotein, domain C / Alphavirus E2 glycoprotein, A domain / Immunoglobulin-like - #350 / Alphavirus E2 glycoprotein, domain B / Peptidase S3, togavirin / Alphavirus E2 glycoprotein / Alphavirus E3 spike glycoprotein / Alphavirus E1 glycoprotein / Alphavirus E2 glycoprotein, domain A / Alphavirus E2 glycoprotein, domain C ...Alphavirus E2 glycoprotein, domain C / Alphavirus E2 glycoprotein, A domain / Immunoglobulin-like - #350 / Alphavirus E2 glycoprotein, domain B / Peptidase S3, togavirin / Alphavirus E2 glycoprotein / Alphavirus E3 spike glycoprotein / Alphavirus E1 glycoprotein / Alphavirus E2 glycoprotein, domain A / Alphavirus E2 glycoprotein, domain C / Alphavirus E2 glycoprotein / Alphavirus core protein / Alphavirus E3 glycoprotein / Alphavirus E1 glycoprotein / Alphavirus core protein (CP) domain profile. / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / Immunoglobulin E-set / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Structural polyprotein
Similarity search - Component
Biological speciesSindbis virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.29 Å
AuthorsLi, L. / Jose, J. / Xiang, Y. / Kuhn, R.J. / Rossmann, M.G.
CitationJournal: Nature / Year: 2010
Title: Structural changes of envelope proteins during alphavirus fusion.
Authors: Long Li / Joyce Jose / Ye Xiang / Richard J Kuhn / Michael G Rossmann /
Abstract: Alphaviruses are enveloped RNA viruses that have a diameter of about 700 Å and can be lethal human pathogens. Entry of virus into host cells by endocytosis is controlled by two envelope ...Alphaviruses are enveloped RNA viruses that have a diameter of about 700 Å and can be lethal human pathogens. Entry of virus into host cells by endocytosis is controlled by two envelope glycoproteins, E1 and E2. The E2-E1 heterodimers form 80 trimeric spikes on the icosahedral virus surface, 60 with quasi-three-fold symmetry and 20 coincident with the icosahedral three-fold axes arranged with T = 4 quasi-symmetry. The E1 glycoprotein has a hydrophobic fusion loop at one end and is responsible for membrane fusion. The E2 protein is responsible for receptor binding and protects the fusion loop at neutral pH. The lower pH in the endosome induces the virions to undergo an irreversible conformational change in which E2 and E1 dissociate and E1 forms homotrimers, triggering fusion of the viral membrane with the endosomal membrane and then releasing the viral genome into the cytoplasm. Here we report the structure of an alphavirus spike, crystallized at low pH, representing an intermediate in the fusion process and clarifying the maturation process. The trimer of E2-E1 in the crystal structure is similar to the spikes in the neutral pH virus except that the E2 middle region is disordered, exposing the fusion loop. The amino- and carboxy-terminal domains of E2 each form immunoglobulin-like folds, consistent with the receptor attachment properties of E2.
History
DepositionMay 3, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 24, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jul 26, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Structural polyprotein
B: Structural polyprotein
C: Structural polyprotein
D: Structural polyprotein
E: Structural polyprotein
F: Structural polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)505,01518
Polymers495,7066
Non-polymers9,30812
Water0
1
A: Structural polyprotein
B: Structural polyprotein
C: Structural polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)252,5079
Polymers247,8533
Non-polymers4,6546
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Structural polyprotein
E: Structural polyprotein
F: Structural polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)252,5079
Polymers247,8533
Non-polymers4,6546
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)67.482, 158.430, 160.676
Angle α, β, γ (deg.)60.42, 89.80, 89.65
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
12A
22B
32C
42D
52E
62F
13A
23B
33C
43D
53E
63F

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain 'A' and (resseq 259:445 or resseq 456: 653) and (not element H) and (not element D)A0
211chain 'B' and (resseq 259:445 or resseq 456: 653) and (not element H) and (not element D)B0
311chain 'C' and (resseq 259:445 or resseq 456: 653 ) and (not element H) and (not element D)C0
411chain 'D' and (resseq 259:445 or resseq 456: 653 ) and (not element H) and (not element D)D0
511chain 'E' and (resseq 259:445 or resseq 456: 653 ) and (not element H) and (not element D)E0
611chain 'F' and (resseq 259:445 or resseq 456: 653 ) and (not element H) and (not element D)F0
112chain 'A' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)A0
212chain 'B' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)B0
312chain 'C' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)C0
412chain 'D' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)D0
512chain 'E' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)E0
612chain 'F' and (resseq 6:157 or resseq 255:340 ) and (not element H) and (not element D)F0
113chain 'A' and (resseq 294:380 ) and (not element H) and (not element D)A0
213chain 'B' and (resseq 294:380 ) and (not element H) and (not element D)B0
313chain 'C' and (resseq 294:380 ) and (not element H) and (not element D)C0
413chain 'D' and (resseq 294:380 ) and (not element H) and (not element D)D0
513chain 'E' and (resseq 294:380 ) and (not element H) and (not element D)E0
613chain 'F' and (resseq 294:380 ) and (not element H) and (not element D)F0

NCS ensembles :
ID
1
2
3

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Components

#1: Protein
Structural polyprotein / p130 / Capsid protein / Coat protein / C / p62 / E3/E2 / E3 protein / Spike glycoprotein E3 / E2 ...p130 / Capsid protein / Coat protein / C / p62 / E3/E2 / E3 protein / Spike glycoprotein E3 / E2 envelope glycoprotein / Spike glycoprotein E2 / 6K protein / E1 envelope glycoprotein / Spike glycoprotein E1


Mass: 82617.719 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sindbis virus / Strain: Toto64 / Plasmid: pMT/BiP/V5-His / Production host: Drosophila (fruit flies) / Strain (production host): S2 cells
References: UniProt: P03316, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
#2: Polysaccharide
alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#4: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE

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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: 3.01 Å3/Da / Density % sol: 59.16 %
Crystal growTemperature: 293 K / pH: 5.6
Details: PEG8000 10%, Sodium/Potassium Tartrate 325 mM, Sodium/Potassium Phosphate 100 mM pH5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.97934,0.97951,0.94934
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 31, 2009
RadiationMonochromator: SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.979341
20.979511
30.949341
ReflectionResolution: 3.3→70 Å / Num. obs: 162989 / % possible obs: 97.3 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Rmerge(I) obs: 0.128 / Rsym value: 0.128 / Net I/σ(I): 12.5
Reflection shellResolution: 3.3→3.36 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.658 / Mean I/σ(I) obs: 1.8 / Rsym value: 0.658 / % possible all: 82.9

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Processing

Software
NameVersionClassification
HKL-2000data collection
SHARPphasing
PHENIX(phenix.refine: 1.6_289)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 3.29→60.72 Å / SU ML: 0.35 / σ(F): 1.96 / Phase error: 28.28 / Stereochemistry target values: ML_SAD
RfactorNum. reflection% reflection
Rfree0.252 8227 5.05 %
Rwork0.239 --
obs0.24 162989 92.4 %
all-176472 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 69.49 Å2 / ksol: 0.27 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-40.8597 Å2-2.2902 Å2-0.2614 Å2
2---15.5516 Å25.1022 Å2
3----25.3081 Å2
Refinement stepCycle: LAST / Resolution: 3.29→60.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28537 0 622 0 29159
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00729988
X-RAY DIFFRACTIONf_angle_d1.23540957
X-RAY DIFFRACTIONf_dihedral_angle_d23.49211016
X-RAY DIFFRACTIONf_chiral_restr0.084770
X-RAY DIFFRACTIONf_plane_restr0.0055142
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2149X-RAY DIFFRACTIONPOSITIONAL0.029
12B2149X-RAY DIFFRACTIONPOSITIONAL0.029
13C2145X-RAY DIFFRACTIONPOSITIONAL0.031
14D2149X-RAY DIFFRACTIONPOSITIONAL0.02
15E2149X-RAY DIFFRACTIONPOSITIONAL0.026
16F2145X-RAY DIFFRACTIONPOSITIONAL0.038
21A1874X-RAY DIFFRACTIONPOSITIONAL0.024
22B1874X-RAY DIFFRACTIONPOSITIONAL0.024
23C1874X-RAY DIFFRACTIONPOSITIONAL0.022
24D1866X-RAY DIFFRACTIONPOSITIONAL0.015
25E1874X-RAY DIFFRACTIONPOSITIONAL0.018
26F1848X-RAY DIFFRACTIONPOSITIONAL0.016
31A640X-RAY DIFFRACTIONPOSITIONAL0.014
32B640X-RAY DIFFRACTIONPOSITIONAL0.014
33C640X-RAY DIFFRACTIONPOSITIONAL0.029
34D640X-RAY DIFFRACTIONPOSITIONAL0.016
35E640X-RAY DIFFRACTIONPOSITIONAL0.011
36F640X-RAY DIFFRACTIONPOSITIONAL0.009
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2852-3.40260.39614520.37188877X-RAY DIFFRACTION53
3.4026-3.53880.34937580.331514684X-RAY DIFFRACTION87
3.5388-3.69990.34148560.325816110X-RAY DIFFRACTION96
3.6999-3.89490.29028460.285816443X-RAY DIFFRACTION98
3.8949-4.13890.25789570.254116415X-RAY DIFFRACTION98
4.1389-4.45840.25219560.21716487X-RAY DIFFRACTION98
4.4584-4.90680.18498700.180216301X-RAY DIFFRACTION98
4.9068-5.61640.1918660.186216572X-RAY DIFFRACTION98
5.6164-7.07440.21258540.199516454X-RAY DIFFRACTION99
7.0744-60.73350.25258120.236916419X-RAY DIFFRACTION97
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)
1-0.5355-1.2157-1.76481.82251.50171.34320.03730.24780.18960.59620.0808-0.09070.39570.6696-0.00030.4703-0.09180.03770.1075-0.01270.369437.212141.972155.1748
2-0.19820.02150.44940.43450.31621.70580.02410.1176-0.0687-0.0877-0.095-0.2583-0.49730.2398-0.00280.43450.09590.03210.3672-0.06590.333437.6389103.374961.5421
3-1.00052.0048-0.07731.3541-1.15650.74050.2475-0.31380.2521-0.5089-0.0351-0.50240.32110.21190.08150.30570.0361-0.03990.25320.09820.221937.276378.05864.5403
4-0.73040.4552-0.99421.2799-0.59360.5764-0.0366-0.08690.1884-0.77290.20630.21760.5383-0.6760.01320.43520.08130.03490.18350.020.37741.8644120.889772.417
50.15940.00791.04190.30840.00332.35070.0127-0.1551-0.03990.0053-0.06540.1939-0.7014-0.202-0.00030.4125-0.10670.01010.32790.04560.289841.9898182.46965.9988
6-0.2063-1.1877-0.37761.98321.32391.30040.05060.0992-0.03710.48970.09020.28630.3816-0.13340.02040.33320.0276-0.08310.2983-0.05740.268742.0484157.3294122.8845
70.37-0.33120.19380.275-0.16760.09070.63510.08440.2719-0.3175-0.585-0.6143-0.04310.1854-0.00012.229-0.09030.60051.56250.00451.323859.836319.212614.0082
80.09220.21230.00530.492-0.06830.14790.61220.80210.10860.2824-0.1337-1.63830.50220.266-0.00111.74320.5474-0.07771.26740.11851.126160.355378.8213101.5324
90.07790.0693-0.13130.0288-0.10020.16870.4631-0.49490.0076-0.18830.0362-0.4417-0.53460.7884-0.00032.1544-0.1732-0.36911.2606-0.15021.439160.6725124.10346.1697
100.19560.17390.17270.19550.08470.21260.641-0.48830.83530.5542-0.5550.50440.1858-0.5480.00022.49860.27460.821.4864-0.13441.548118.735198.5507113.5256
110.2372-0.3316-0.16370.44930.21810.11120.5479-0.8538-0.68010.2148-0.51531.07190.1110.3209-0.00032.1065-0.4795-0.06221.51640.0241.538519.2533158.106425.7818
120.3717-0.1248-0.23710.14080.02620.17830.04471.1804-0.0126-0.4269-0.02010.4045-1.1349-0.5393-0.00032.52850.4903-0.50771.52580.1011.425419.1337204.3335122.0135
131.0269-0.77670.25121.9943-1.18941.91020.09620.0407-0.57210.2070.12590.5115-0.3686-0.6036-0.00040.4248-0.14920.22140.71670.0350.73786.433763.646753.4278
141.14570.315-0.06651.94810.58451.44940.1133-0.17230.1534-0.3048-0.22070.5776-0.1731-0.478700.47830.28080.01470.6476-0.08180.70966.584191.201643.3107
150.448-0.3804-0.171.6350.46152.0147-0.06130.25410.1732-0.1588-0.06250.4290.3451-0.50830.00020.5095-0.0896-0.17010.8021-0.01450.54976.439968.727424.2769
160.6656-0.57330.11632.73281.20151.42710.0817-0.1126-0.1148-0.37840.1388-0.6808-0.00870.5883-0.00010.59910.17360.17860.7927-0.04780.807173.0032142.537874.2229
170.9666-0.9404-0.03692.62-1.18971.51170.00210.35140.30770.2307-0.1901-0.7137-0.37080.7211-0.00010.3765-0.28050.06820.65210.04620.662872.8465170.370384.3349
180.662-0.1823-0.79760.9632-0.40321.37590.0382-0.39520.2712-0.0919-0.1706-0.2490.34160.482700.54740.1392-0.21870.75890.07050.533172.8297147.8197103.2329
190.2834-0.15730.14040.0562-0.07790.0695-0.13970.6521-0.63260.2347-0.60470.6914-0.1014-0.15520.00050.5076-0.14650.2360.8148-0.12980.986317.02248.534944.0058
200.86370.52250.56080.31910.31360.3194-0.4302-0.8666-0.1595-0.21920.0139-0.3419-0.3735-1.1398-0.00060.58210.3740.13811.0429-0.10710.649516.758791.345960.6746
210.65380.4491-0.54420.579-0.33810.4363-0.24310.8510.9484-0.44270.9220.97430.43260.5587-0.00390.0486-0.0366-0.39640.61690.1750.680416.87784.327315.944
220.5540.39710.01750.26470.0086-0.00080.0169-0.2647-0.6711-0.6428-0.718-0.6097-0.2559-0.16360.00250.25660.23840.22420.69490.13790.978261.9418127.74484.4041
230.3488-0.29150.34830.2392-0.28230.3468-0.12330.62790.09390.14140.01580.4178-0.27560.7991-0.00170.5032-0.31870.11760.9824-0.00780.64562.5722169.864366.5112
240.1187-0.047-0.02080.0503-0.01120.00120.2816-0.35210.460.4110.4475-0.60910.2721-0.14140.00110.31440.1319-0.24740.6284-0.13810.87261.6751165.3545110.4699
251.0726-0.66471.19131.2134-0.23421.61860.36430.152-0.2374-0.2774-0.2204-0.0838-0.17510.103-0.00050.3204-0.06190.14140.53270.14850.451444.22551.681827.5484
261.20911.2975-0.14331.4067-0.48721.45530.3538-0.50290.0512-0.2607-0.1638-0.05520.30330.0837-0.00010.48320.1597-0.01330.3769-0.04670.670444.03574.787566.3885
270.4845-0.5998-0.22541.2163-0.18190.51570.1680.29920.10090.3851-0.2211-0.06720.1948-0.03310.00020.3015-0.107-0.12070.5024-0.08730.283544.214296.63826.9387
280.98860.38390.45451.4157-0.80451.85720.2246-0.1758-0.2502-0.1534-0.06790.1023-0.40410.045-0.00020.140.11710.19010.4514-0.16530.310635.2129131.132699.8783
291.1095-1.06030.0341.15350.50391.50970.120.2712-0.04120.5596-0.10630.03930.1658-0.0780.00050.2883-0.1986-0.00720.21970.01660.562135.3494154.048961.2387
300.97520.6263-0.86851.3425-0.11340.92250.1694-0.23620.2358-0.1413-0.0518-0.11160.2664-0.04190.00020.24010.0497-0.15280.550.12810.29835.2718175.8809100.6286
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 358:653 OR RESSEQ 761:765)
2X-RAY DIFFRACTION2CHAIN B AND (RESSEQ 358:653 OR RESSEQ 761:765)
3X-RAY DIFFRACTION3CHAIN C AND (RESSEQ 358:653 OR RESSEQ 761:765)
4X-RAY DIFFRACTION4CHAIN D AND (RESSEQ 358:653 OR RESSEQ 761:765)
5X-RAY DIFFRACTION5CHAIN E AND (RESSEQ 358:653 OR RESSEQ 761:765)
6X-RAY DIFFRACTION6CHAIN F AND (RESSEQ 358:653 OR RESSEQ 761:765)
7X-RAY DIFFRACTION7CHAIN A AND (RESSEQ 654:740)
8X-RAY DIFFRACTION8CHAIN B AND (RESSEQ 654:740)
9X-RAY DIFFRACTION9CHAIN C AND (RESSEQ 654:740)
10X-RAY DIFFRACTION10CHAIN D AND (RESSEQ 654:740)
11X-RAY DIFFRACTION11CHAIN E AND (RESSEQ 654:740)
12X-RAY DIFFRACTION12CHAIN F AND (RESSEQ 654:740)
13X-RAY DIFFRACTION13CHAIN A AND (RESSEQ 4:143)
14X-RAY DIFFRACTION14CHAIN B AND (RESSEQ 4:143)
15X-RAY DIFFRACTION15CHAIN C AND (RESSEQ 4:143)
16X-RAY DIFFRACTION16CHAIN D AND (RESSEQ 4:143)
17X-RAY DIFFRACTION17CHAIN E AND (RESSEQ 4:143)
18X-RAY DIFFRACTION18CHAIN F AND (RESSEQ 4:143)
19X-RAY DIFFRACTION19CHAIN A AND (RESSEQ 144:268)
20X-RAY DIFFRACTION20CHAIN B AND (RESSEQ 144:268)
21X-RAY DIFFRACTION21CHAIN C AND (RESSEQ 144:268)
22X-RAY DIFFRACTION22CHAIN D AND (RESSEQ 144:268)
23X-RAY DIFFRACTION23CHAIN E AND (RESSEQ 144:268)
24X-RAY DIFFRACTION24CHAIN F AND (RESSEQ 144:268)
25X-RAY DIFFRACTION25CHAIN A AND (RESSEQ 269:343 OR RESSEQ 751:754)
26X-RAY DIFFRACTION26CHAIN B AND (RESSEQ 269:343 OR RESSEQ 751:754)
27X-RAY DIFFRACTION27CHAIN C AND (RESSEQ 269:342 OR RESSEQ 751:754)
28X-RAY DIFFRACTION28CHAIN D AND (RESSEQ 269:344 OR RESSEQ 751:754)
29X-RAY DIFFRACTION29CHAIN E AND (RESSEQ 269:342 OR RESSEQ 751:754)
30X-RAY DIFFRACTION30CHAIN F AND (RESSEQ 269:344 OR RESSEQ 751:754)

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