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- PDB-4adi: Crystal structure of the Rubella virus envelope glycoprotein E1 i... -

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Basic information

Entry
Database: PDB / ID: 4adi
TitleCrystal structure of the Rubella virus envelope glycoprotein E1 in post-fusion form (crystal form I)
ComponentsE1 ENVELOPE GLYCOPROTEIN
KeywordsVIRAL PROTEIN / 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 / metal ion binding / membrane
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 / SIRAS / Resolution: 1.8 Å
AuthorsDuBois, R.M. / Vaney, M.C. / Tortorici, M.A. / Al Kurdi, R. / Barba-Spaeth, G. / 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: 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.
#2: 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.
#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
DepositionDec 26, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 9, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 23, 2013Group: Database references
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / 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_database_status.status_code_sf / _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_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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 1.3Nov 13, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_sheet
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification / _struct_sheet.number_strands
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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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)156,66344
Polymers151,7203
Non-polymers4,94341
Water27,8691547
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27710 Å2
ΔGint-56.8 kcal/mol
Surface area49020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)129.980, 121.380, 126.430
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 / SPIKE GLYCOPROTEIN E1


Mass: 50573.352 Da / Num. of mol.: 3 / Fragment: ECTODOMAIN, UNP RESIDUES 583-1018
Source method: isolated from a genetically manipulated source
Details: POLYPROTEIN FRAGMENT RESIDUES 1-435 / 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, 12 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.: 6
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
#7: 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.: 6
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 , 5 types, 1576 molecules

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


Mass: 92.094 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#5: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1547 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Nonpolymer detailsNA (NA): THE SODIUM IONS ARE BONDED TO RESIDUES AT THE FUSION LOOPS. GLYCEROL (GOL): E1 PROTEIN WAS ...NA (NA): THE SODIUM IONS ARE BONDED TO RESIDUES AT THE FUSION LOOPS. GLYCEROL (GOL): E1 PROTEIN WAS CRYSTALLIZED IN PRESENCE OF HIGH CONCENTRATION OF GLYCEROL. N-ACETYL-D-GALACTOSAMINE (NGA): THE THR RESIDUES 429 AND 430 ARE O-GLYCOSILATED. N-ACETYL-D-GLUCOSAMINE (NAG): THE ASN RESIDUES 76 AND 177 ARE N-GLYCOSILATED.
Sequence detailsECTODOMAIN OF E1 FROM AMINO ACIDS FROM 1 (583 IN POLYPROTEIN) TO 436 (1018 IN POLYPROTEIN) WITH THE ...ECTODOMAIN OF E1 FROM AMINO ACIDS FROM 1 (583 IN POLYPROTEIN) TO 436 (1018 IN POLYPROTEIN) WITH THE FOLLOWING SEQUENCE AT THE C-TERMINAL FEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK

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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: 3.03 Å3/Da / Density % sol: 59 % / Description: NONE
Crystal growDetails: 1-3% PEG 4K, 0.1M NAHEPES PH7.5-8, 30% GLYCEROL

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 2, 2007 / 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: 1.78→45.3 Å / Num. obs: 188417 / % possible obs: 98.3 % / Observed criterion σ(I): 2 / Redundancy: 8.6 % / Biso Wilson estimate: 27.23 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 16.7
Reflection shellResolution: 1.78→1.87 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 2 / % possible all: 88.1

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Processing

Software
NameVersionClassification
BUSTER2.11.2refinement
XDSdata reduction
SCALAdata scaling
SHARPphasing
RefinementMethod to determine structure: SIRAS
Starting model: NONE

Resolution: 1.8→20 Å / Cor.coef. Fo:Fc: 0.9613 / Cor.coef. Fo:Fc free: 0.9551 / SU R Cruickshank DPI: 0.087 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.093 / SU Rfree Blow DPI: 0.086 / SU Rfree Cruickshank DPI: 0.083
Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA. NUMBER OF ATOM WITH PROPER CCP4 ATOM TYPE=11659. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. ...Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA. NUMBER OF ATOM WITH PROPER CCP4 ATOM TYPE=11659. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=3.
RfactorNum. reflection% reflectionSelection details
Rfree0.1831 18506 10.06 %RANDOM
Rwork0.1666 ---
obs0.1682 183967 99.64 %-
Displacement parametersBiso mean: 30.15 Å2
Baniso -1Baniso -2Baniso -3
1--0.6267 Å20 Å20 Å2
2--0.7929 Å20 Å2
3----0.1662 Å2
Refine analyzeLuzzati coordinate error obs: 0.189 Å
Refinement stepCycle: LAST / Resolution: 1.8→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9572 0 317 1547 11436
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00710488HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.9614459HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d3322SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes189HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1602HARMONIC5
X-RAY DIFFRACTIONt_it10488HARMONIC20
X-RAY DIFFRACTIONt_nbd6SEMIHARMONIC5
X-RAY DIFFRACTIONt_omega_torsion2.99
X-RAY DIFFRACTIONt_other_torsion15.15
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1392SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies40HARMONIC1
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact13030SEMIHARMONIC4
LS refinement shellResolution: 1.8→1.85 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2395 1313 10.18 %
Rwork0.2177 11581 -
all0.2199 12894 -
obs--99.64 %
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)
10.780.3379-0.06231.4746-0.45491.87440.0157-0.0858-0.13450.001-0.01760.0350.1427-0.00980.002-0.03490.0013-0.0004-0.03450.031-0.013736.289480.763338.3142
21.63260.0768-0.21691.74980.13181.8139-0.001-0.0641-0.0755-0.0578-0.01360.13760.2203-0.2680.0146-0.0273-0.0706-0.0167-0.0189-0.0114-0.043621.219381.222921.9566
31.50110.0084-0.46971.4013-0.57691.6012-0.0153-0.0788-0.04340.11290.0380.18060.0123-0.061-0.0227-0.0284-0.00520.0296-0.0155-0.0213-0.025520.415896.496438.3459
40.77510.45-0.43590.4803-0.23850.3095-0.0224-0.0215-0.0601-0.03020.01-0.08340.01550.02710.0123-0.0332-0.0017-0.0033-0.024-0.0137-0.006170.339112.47611.2455
50.46640.3091-0.3250.3977-0.4430.6681-0.02480.1082-0.0146-0.04270.0145-0.02240.0438-0.04870.0103-0.02240.01010.0107-0.0025-0.0189-0.04552.8614111.966-8.9435
60.36050.3968-0.10530.5552-0.19030.1531-0.0055-0.00150.04230.0298-0.00180.028-0.04060.00190.00730.00030.0029-0.0098-0.0244-0.0013-0.024850.7924130.87510.1866
71.76921.11930.10052.47250.10230.9759-0.0573-0.0511-0.3323-0.1734-0.0543-0.02480.263-0.07520.11160.0217-0.01590.0435-0.1037-0.05030.019941.645773.762810.674
82.8370.4162-1.62840.46120.07911.6993-0.00530.07480.16420.04520.04540.1310.0428-0.2865-0.0401-0.07150.0174-0.00550.0490.0007-0.034713.1121108.91618.5781
90.5353-0.35390.12142.0341-1.57132.5770.0265-0.1284-0.05110.1612-0.04340.0123-0.06580.08770.017-0.0094-0.0068-0.0321-0.01150.0075-0.057847.6674100.43747.4428
100.17320.9225-1.2011.456-0.54370.2528-0.0008-0.0741-0.01660.00920.0005-0.0204-0.0009-0.0460.00030.02870.01380.0263-0.0145-0.03010.040531.211165.972325.4226
110.60740.312-0.58650.195-0.9050.0793-0.0040.0305-0.02970.0225-0.00540.00330.065-0.02530.0094-0.0379-0.0239-0.00170.056-0.02320.0164.924296.22526.1383
120.28840.2026-0.3190.0851-0.4820.1872-0.0019-0.0119-0.01550.01920.00130.04640.007-0.0010.00060.0370.02080.00950.021-0.0143-0.004732.484990.775454.1889
1300.1999-0.42650.3251-0.11150.0811-0.01050.1085-0.0735-0.0940.00970.0368-0.03220.02820.00070.0215-0.03470.035-0.0049-0.016-0.033856.251398.5675-6.7298
140.3682-0.02190.10710.0554-0.14220-0.0072-0.05720.15460.00880.0219-0.0491-0.0708-0.0689-0.0147-0.00270.00720.0261-0.0252-0.00410.014137.7611128.7695.9038
150.00010.5558-0.55670-0.17780.41770.0004-0.01610.00250.0665-0.0042-0.08150.01210.05830.0038-0.0379-0.0196-0.02190.02510.03550.013667.3604115.36624.6742
160-0.00840.01230.0050.00720.00140.00010.0008-0.0008-0.0002-0.000200.00030.00010.00010.00670.018-0.00630.0036-0.00180.008877.225598.95065.6771
170.0234-0.0002-0.01950.01790.004600.00010.00280.00080.0001-0.0002-0.0048-0.00030.00530.0001-0.0030.04640.013-0.0069-0.01170.039344.646473.463331.5549
180.0066-0.00440.00010.00430.00640.00160.00010.00010-0.0012-0.0008-0.00010.00110.00240.00060.0052-0.01370.00310.0009-0.01230.008861.717899.5599-14.4259
190.00010.0028-0.01310.00540.000900.0004-0.0002-0.0028-0.0010.00010.00020.0029-0.0002-0.00060.0073-0.0131-0.0106-0.0083-0.0110.006554.77104.637-19.1062
200.0078-0.00230.01170.00440.01420.00180.000100.00070.00010.00010.0016-0.002-0.0016-0.00020.00030.0089-0.01810.0113-0.00520.008639.4358117.259-16.4587
210.0260.0193-0.00210.0002-0.01370.01930.00010.00390.0014-0.0039-0.00050.0008-0.002-0.00010.0004-0.0073-0.0087-0.04350.04460.0044-0.011513.757188.179113.9263
220.0010.0014-0.003900.00390.0045-0.0001-0.001-0.0003-0.0001-0.000800.0007-0.00020.00090.00310.00570.00520.01040.00410.007338.6786136.770.7739
230.0037-0.00040.00260-0.047100-0.00050.00010.0003-0.00150.00220.0006-0.00340.0015-0.00870.01990.0165-0.0032-0.00620.007443.1204140.8738.4594
240.0028-0.01180.0027000.00910.0001-0.0014-0.00080.00230-0.00310.00020.0009-0.00010.01420.0061-0.0090.012-0.0147-0.00555.0387137.34124.19
250.00690.00920.00610.02010.00630.0171-0.0001-0.00180.0061-0.00160.001-0.0026-0.005-0.0002-0.00090.0333-0.0089-0.0106-0.0014-0.0535-0.005827.1395104.18846.3615
260.01650.0016-0.00580.00340.00540.0090-0.00060-0.00010.00060.00090.00050.0001-0.00050.01-0.0027-0.00960.00370.01270.002975.7226120.44524.4474
2700.03890.00400.00020.0092-0.0004-0.0032-0.00030.00270.00030.00110.00130.00080.00010.0036-0.0039-0.00990.0102-0.0014-0.007779.9912113.44819.3201
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 1:30, 163:200, 318:327)
2X-RAY DIFFRACTION2CHAIN B AND (RESID 1:30, 163:200, 318:327)
3X-RAY DIFFRACTION3CHAIN C AND (RESID 1:30, 163:200, 318:327)
4X-RAY DIFFRACTION4CHAIN A AND (RESID 31:162)
5X-RAY DIFFRACTION5CHAIN B AND (RESID 31:162)
6X-RAY DIFFRACTION6CHAIN C AND (RESID 31:162)
7X-RAY DIFFRACTION7CHAIN A AND (RESID 342:413)
8X-RAY DIFFRACTION8CHAIN B AND (RESID 342:413)
9X-RAY DIFFRACTION9CHAIN C AND RESID 342:413
10X-RAY DIFFRACTION10CHAIN A AND (RESID 328:341)
11X-RAY DIFFRACTION11CHAIN B AND (RESID 328:341)
12X-RAY DIFFRACTION12CHAIN C AND (RESID 328:341)
13X-RAY DIFFRACTION13CHAIN A AND (RESID 414:435)
14X-RAY DIFFRACTION14CHAIN B AND (RESID 414:435)
15X-RAY DIFFRACTION15CHAIN C AND (RESID 414:435)
16X-RAY DIFFRACTION16CHAIN A AND RESID 1001
17X-RAY DIFFRACTION17CHAIN A AND RESID 2001
18X-RAY DIFFRACTION18CHAIN A AND RESID 3001:3001
19X-RAY DIFFRACTION19CHAIN A AND RESID 4001
20X-RAY DIFFRACTION20CHAIN B AND RESID 1001
21X-RAY DIFFRACTION21CHAIN B AND RESID 2001
22X-RAY DIFFRACTION22CHAIN B AND RESID 3001
23X-RAY DIFFRACTION23CHAIN B AND RESID 4001
24X-RAY DIFFRACTION24CHAIN C AND RESID 1001
25X-RAY DIFFRACTION25CHAIN C AND RESID 2001
26X-RAY DIFFRACTION26CHAIN C AND RESID 3001
27X-RAY DIFFRACTION27CHAIN C AND RESID 4001

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