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- PDB-4b3v: Crystal structure of the Rubella virus glycoprotein E1 in its pos... -

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Basic information

Entry
Database: PDB / ID: 4b3v
TitleCrystal structure of the Rubella virus glycoprotein E1 in its post-fusion form crystallized in presence of 20mM of Calcium Acetate
ComponentsE1 ENVELOPE GLYCOPROTEIN
KeywordsVIRAL PROTEIN / ENVELOPE GLYCOPROTEIN / MEMBRANE FUSION
Function / homology
Function and homology information


T=4 icosahedral viral capsid / host cell Golgi membrane / host cell mitochondrion / viral nucleocapsid / clathrin-dependent endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane / RNA binding ...T=4 icosahedral viral capsid / host cell Golgi membrane / host cell mitochondrion / viral nucleocapsid / clathrin-dependent endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane / RNA binding / membrane / metal ion binding
Similarity search - Function
Rubella membrane glycoprotein E1, domain 3 / Rubella membrane glycoprotein E1, domain 1 / Rubella membrane glycoprotein E1, domain 2 / Rubella capsid / Rubella membrane glycoprotein E1 / Rubella membrane glycoprotein E2 / Rubella membrane glycoprotein E1, domain 2 / Rubella membrane glycoprotein E1, domain 3 / Rubella membrane glycoprotein E1, domain 1 / Rubella capsid domain superfamily ...Rubella membrane glycoprotein E1, domain 3 / Rubella membrane glycoprotein E1, domain 1 / Rubella membrane glycoprotein E1, domain 2 / Rubella capsid / Rubella membrane glycoprotein E1 / Rubella membrane glycoprotein E2 / Rubella membrane glycoprotein E1, domain 2 / Rubella membrane glycoprotein E1, domain 3 / Rubella membrane glycoprotein E1, domain 1 / Rubella capsid domain superfamily / Rubella membrane glycoprotein E1 / Rubella membrane glycoprotein E2 / Rubella capsid protein / Viral Envelope Glycoprotein; domain 2 / Tick-borne Encephalitis virus Glycoprotein; domain 1 / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / 2-acetamido-2-deoxy-beta-D-galactopyranose / DI(HYDROXYETHYL)ETHER / Structural polyprotein
Similarity search - Component
Biological speciesRUBELLA VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.98 Å
AuthorsVaney, M.C. / DuBois, R.M. / Tortorici, M.A. / Rey, F.A.
Citation
Journal: Nature / Year: 2013
Title: Functional and Evolutionary Insight from the Crystal Structure of Rubella Virus Protein E1.
Authors: Dubois, R.M. / Vaney, M.C. / Tortorici, M.A. / Kurdi, R.A. / Barba-Spaeth, G. / Krey, T. / Rey, F.A.
#1: Journal: Cell(Cambridge,Mass.) / Year: 2001
Title: The Fusion Glycoprotein Shell of Semliki Forest Virus: An Icosahedral Assembly Primed for Fusogenic Activation at Endosomal Ph.
Authors: Lescar, J. / Roussel, A. / Wien, M.W. / Navaza, J. / Fuller, S.D. / Wengler, G. / Wengler, G. / Rey, F.A.
#2: Journal: Nature / Year: 2004
Title: Conformational Change and Protein-Protein Interactions of the Fusion Protein of Semliki Forest Virus.
Authors: Gibbons, D.L. / Vaney, M. / Roussel, A. / Vigouroux, A. / Reilly, B. / Lepault, J. / Kielian, M. / Rey, F.A.
#3: Journal: Structure / Year: 2006
Title: Structure and Interactions at the Viral Surface of the Envelope Protein E1 of Semliki Forest Virus.
Authors: Roussel, A. / Lescar, J. / Vaney, M. / Wengler, G. / Wengler, G. / Rey, F.A.
#4: Journal: Embo J. / Year: 2004
Title: Structure of a Flavivirus Envelope Glycoprotein in its Low-Ph-Induced Membrane Fusion Conformation.
Authors: Bressanelli, S. / Stiasny, K. / Allison, S.L. / Stura, E.A. / Duquerroy, S. / Lescar, J. / Heinz, F.X. / Rey, F.A.
History
DepositionJul 26, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 9, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 23, 2013Group: Database references
Revision 1.2Mar 18, 2015Group: Database references
Revision 1.3Jun 14, 2017Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_vector_type
Revision 1.4Oct 16, 2019Group: Data collection / Derived calculations / Other / Category: pdbx_database_status / reflns_shell / struct_conn
Item: _pdbx_database_status.status_code_sf / _reflns_shell.Rmerge_I_obs / _struct_conn.pdbx_leaving_atom_flag
Revision 1.5Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.6Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _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: E1 ENVELOPE GLYCOPROTEIN
B: E1 ENVELOPE GLYCOPROTEIN
C: E1 ENVELOPE GLYCOPROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)155,60440
Polymers151,7203
Non-polymers3,88437
Water20,3751131
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A: E1 ENVELOPE GLYCOPROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,92514
Polymers50,5731
Non-polymers1,35113
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: E1 ENVELOPE GLYCOPROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,61112
Polymers50,5731
Non-polymers1,03811
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: E1 ENVELOPE GLYCOPROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,06814
Polymers50,5731
Non-polymers1,49413
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)121.272, 126.163, 129.375
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 3 molecules ABC

#1: Protein E1 ENVELOPE GLYCOPROTEIN / ENVELOPE GLYCOPROTEIN E1


Mass: 50573.352 Da / Num. of mol.: 3 / Fragment: ECTODOMAIN, RESIDUES 583-1018
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RUBELLA VIRUS / Strain: M33 / Plasmid: PMT MODIFIED INVITROGEN / Cell line (production host): SCHNEIDER 2 / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: P08563

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Sugars , 2 types, 6 molecules

#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Sugar ChemComp-NGA / 2-acetamido-2-deoxy-beta-D-galactopyranose / N-acetyl-beta-D-galactosamine / 2-acetamido-2-deoxy-beta-D-galactose / 2-acetamido-2-deoxy-D-galactose / 2-acetamido-2-deoxy-galactose / N-ACETYL-D-GALACTOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGalpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-galactopyranosamineCOMMON NAMEGMML 1.0
b-D-GalpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GalNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 7 types, 1162 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#7: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#8: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#9: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1131 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsCALCIUM ION (CA): THE CALCIUM IONS ARE BONDED TO RESIDUES AT THE FUSION LOOPS OF THREE PROTOMERS. ...CALCIUM ION (CA): THE CALCIUM IONS ARE BONDED TO RESIDUES AT THE FUSION LOOPS OF THREE PROTOMERS. SODIUM ION (NA): THE SODIUM ION IS BONDED TO RESIDUES AT THE FUSION LOOPS OF ONE PROTOMER. GLYCEROL (GOL): E1 PROTEIN WAS CRYSTALLIZED IN PRESENCE OF HIGH CONCENTRATION OF GLYCEROL. N-ACETYL-D-GALACTOSAMINE (NGA): THE THR RESIDUE 430 IS O-GLYCOSILATED. N-ACETYL-D-GLUCOSAMINE (NAG): THE ASN RESIDUES 76 AND 177 ARE N-GLYCOSILATED.

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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 Å3/Da / Density % sol: 59 % / Description: NONE
Crystal growDetails: 1-6% PEG 4K, 100 MM NAHEPES PH 8, 25% GLYCEROL, 20 MM CA(OAC)2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Jul 2, 2010 / Details: DYNAMICALLY BENDABLE
RadiationMonochromator: DOUBLE-CRYSTAL FIXED-EXIT / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.98→43.72 Å / Num. obs: 135009 / % possible obs: 97.1 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Biso Wilson estimate: 29.81 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.1
Reflection shellResolution: 1.98→2.08 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 2 / % possible all: 81.5

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Processing

Software
NameVersionClassification
BUSTER2.11.2refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4ADI

4adi


Resolution: 1.98→28.99 Å / Cor.coef. Fo:Fc: 0.9503 / Cor.coef. Fo:Fc free: 0.946 / SU R Cruickshank DPI: 0.13 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.137 / SU Rfree Blow DPI: 0.117 / SU Rfree Cruickshank DPI: 0.114
Details: REFINEMENT NOTE 1, IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA CA. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=11228. NUMBER WITH APPROX DEFAULT ...Details: REFINEMENT NOTE 1, IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA CA. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=11228. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=4.
RfactorNum. reflection% reflectionSelection details
Rfree0.1979 6752 5.02 %RANDOM
Rwork0.1847 ---
obs0.1854 134445 97.31 %-
Displacement parametersBiso mean: 33.11 Å2
Baniso -1Baniso -2Baniso -3
1-0.2306 Å20 Å20 Å2
2---0.6752 Å20 Å2
3---0.4447 Å2
Refine analyzeLuzzati coordinate error obs: 0.242 Å
Refinement stepCycle: LAST / Resolution: 1.98→28.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9707 0 242 1131 11080
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00710442HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.9414347HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d3258SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes187HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1572HARMONIC5
X-RAY DIFFRACTIONt_it10442HARMONIC20
X-RAY DIFFRACTIONt_nbd2SEMIHARMONIC5
X-RAY DIFFRACTIONt_omega_torsion2.62
X-RAY DIFFRACTIONt_other_torsion14.29
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1355SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies25HARMONIC1
X-RAY DIFFRACTIONt_utility_distance2HARMONIC1
X-RAY DIFFRACTIONt_utility_angle4HARMONIC1
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact12290SEMIHARMONIC4
LS refinement shellResolution: 1.98→2.03 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2346 347 4.62 %
Rwork0.2206 7166 -
all0.2212 7513 -
obs--97.31 %
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)
11.9620.8649-0.40873.0287-0.49031.46430.0129-0.001-0.0343-0.01620.00520.11130.1029-0.1833-0.0181-0.0438-0.0377-0.0196-0.01590.0085-0.0535-40.5402-38.247328.5063
22.4684-0.132-0.16831.2345-0.13471.70540.0132-0.16550.05470.19540.00120.1613-0.0138-0.1043-0.0145-0.02560.01240.0657-0.0289-0.0113-0.0346-40.184-21.957943.5689
31.91640.8734-0.28181.9336-0.90592.34970.0212-0.172-0.18530.0135-0.0018-0.04750.0785-0.0084-0.0194-0.02620.02720.0037-0.03690.0358-0.0385-24.9805-38.206144.3322
40.60450.2269-0.5250.3074-0.48431.03060.01780.11630.0471-0.02750.00510.00170.0261-0.0671-0.0229-0.0320.01680.0073-0.0147-0.0048-0.0415-8.3255-10.9281-6.0225
50.41270.4602-0.31440.8041-0.4120.61770.0184-0.00940.05250.05630.00490.0367-0.13160.0143-0.0234-0.01050.0173-0.0123-0.04810.0028-0.0325-9.25138.855812.0076
60.76520.2544-0.49150.2195-0.16220.4832-0.0054-0.0164-0.0417-0.01510.0135-0.06420.02310.0427-0.0081-0.02780.0040.0023-0.0342-0.0144-0.01099.5219-9.957813.9236
72.773-0.4188-0.90430.9886-0.29021.3872-0.0117-0.06080.11790.08320.13480.2955-0.0061-0.2261-0.1231-0.09920.04420.030.02540.03760.0016-47.6969-10.776423.2608
80.802-0.1004-0.51932.2446-1.70833.23770.0294-0.1562-0.01260.23620.00250.0046-0.03650.11-0.03180.02840.004-0.0188-0.0259-0.011-0.088-12.682-18.376551.655
92.31322.21290.18333.5456-0.06680.90830.0095-0.0086-0.1706-0.0535-0.0407-0.03690.1523-0.11160.03120.0013-0.00790-0.0759-0.0359-0.0243-20.7266-47.388117.3055
101.84330.2053-0.97990.1002-1.91490.21820.00620.0202-0.00420.0580.0128-0.01220.0679-0.0132-0.019-0.0248-0.01020.0190.06560.0450.0418-55.8458-24.830134.9221
110.22591.1537-0.22540.2575-0.20590.72970.00310.0122-0.04050.0111-0.00890.0620.0008-0.02870.00580.06680.04-0.00360.04060.0018-0.0234-27.918-29.287259.7159
120.23780.2828-0.79770.8528-0.94470.1644-0.0031-0.0233-0.020.01350.0011-0.0108-0.002-0.0240.0020.0462-0.0032-0.0205-0.0084-0.00730.0534-32.4842-54.045932.3576
130.91820.46230.03990-0.14260.02840.0054-0.02290.0718-0.0156-0.0041-0.0184-0.0521-0.0789-0.0013-0.01890.01780.0353-0.02690.02910.024-23.00066.52138.5595
1400.37520.001900.53510.22320.01120.0294-0.0130.028-0.0099-0.08220.03940.1167-0.0013-0.03370.0121-0.00280.01690.04890.01636.6649-5.888827.5903
150.02350.1895-0.66710.6154-0.25960-0.00480.09920.00580.0002-0.00210.01760.0398-0.00360.0069-0.0131-0.0370.02340.0223-0.0182-0.0238-5.9614-24.6212-2.843
160.01510.0217-0.00380-0.0130.01420.00010.00360.0006-0.0061-0.00140.0024-0.0014-0.00130.00130.0099-0.0132-0.03870.02090.0109-0.0095-47.9083-31.602520.058
170.01780.0049-0.00590.0317-0.00770.0424-0.0001-0.00080.00070.00010.00060.00110.0013-0.0036-0.00060.01790.0133-0.00660.0386-0.0160.0432-16.709419.126710.1594
180.0021-0.0025-0.01260.0168-0.00260.02-0.00010.00160.00520.00020.0004-0.0017-0.00420.0004-0.00040.0218-0.00820.01680.0016-0.01830.0028-33.1564-13.845351.0674
190.01650.0009-0.03190.01330.014300.00050.0009-0.00020.0002-0.001-0.004400.00550.0005-0.00170.02260.01-0.0055-0.02010.0367-17.0924-46.386237.9064
200-0.00610.01880.00950.00370.003100.0026-0.0014-0.00090.00010.00070.0014-0.0002-0.00020.0110.0195-0.0103-0.0025-0.00530.013915.8912-24.32479.7509
210.0261-0.0005-0.02450.020.00190.0223-0.0006-0.0006-0.0044-0.0003-0.00030.0010.002-0.00070.00090.0380.0082-0.00870.0187-0.01440.0359-7.8759-19.2657-15.0956
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:30, 163:200, 318:327)
2X-RAY DIFFRACTION2(CHAIN B AND RESID 1:30, 163:200, 318:327)
3X-RAY DIFFRACTION3(CHAIN C AND RESID 1:30, 163:200, 318:327)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 31:162)
5X-RAY DIFFRACTION5(CHAIN B AND RESID 31:162)
6X-RAY DIFFRACTION6(CHAIN C AND RESID 31:162)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 342:413)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 342:413)
9X-RAY DIFFRACTION9(CHAIN C AND RESID 342:413)
10X-RAY DIFFRACTION10(CHAIN A AND RESID 328:341)
11X-RAY DIFFRACTION11(CHAIN B AND RESID 328:341)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 328:341)
13X-RAY DIFFRACTION13(CHAIN A AND RESID 414:435)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 414:435)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 414:435)
16X-RAY DIFFRACTION16(CHAIN A AND RESID 1436)
17X-RAY DIFFRACTION17(CHAIN A AND RESID 1437)
18X-RAY DIFFRACTION18(CHAIN B AND RESID 1436)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 1436)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 1437)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 1438)

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