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- PDB-6ts2: Truncated version of Chaetomium thermophilum UDP-Glucose Glucosyl... -

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Basic information

Entry
Database: PDB / ID: 6ts2
TitleTruncated version of Chaetomium thermophilum UDP-Glucose Glucosyl Transferase (UGGT) lacking domain TRXL2 (417-650).
ComponentsUDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
KeywordsPROTEIN BINDING / Endoplasmic Reticulum / Glycoprotein Folding / ERQC / UGGT / truncation / deletion / thioredoxin-like domain
Function / homology
Function and homology information


UDP-glucose:glycoprotein glucosyltransferase activity / protein N-linked glycosylation via asparagine / unfolded protein binding / endoplasmic reticulum lumen / nucleotide binding / metal ion binding
Similarity search - Function
UDP-glucose:glycoprotein glucosyltransferase, thioredoxin-like domain 4 / UGGT, thioredoxin-like domain 3 / UGGT, thioredoxin-like domain 1 / UGGT, thioredoxin-like domain 2 / UDP-glucose:Glycoprotein Glucosyltransferase / Thioredoxin-like domain / Thioredoxin-like domain / Thioredoxin-like domain / Thioredoxin-like domain / Glucosyltransferase 24, catalytic domain ...UDP-glucose:glycoprotein glucosyltransferase, thioredoxin-like domain 4 / UGGT, thioredoxin-like domain 3 / UGGT, thioredoxin-like domain 1 / UGGT, thioredoxin-like domain 2 / UDP-glucose:Glycoprotein Glucosyltransferase / Thioredoxin-like domain / Thioredoxin-like domain / Thioredoxin-like domain / Thioredoxin-like domain / Glucosyltransferase 24, catalytic domain / Glucosyltransferase 24 / UDP-glucose:Glycoprotein Glucosyltransferase / Nucleotide-diphospho-sugar transferases / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
UDP-glucose-glycoprotein glucosyltransferase-like protein
Similarity search - Component
Biological speciesChaetomium thermophilum (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 5.74 Å
AuthorsRoversi, P. / Zitzmann, N.
Funding support United Kingdom, 3items
OrganizationGrant numberCountry
Wellcome Trust204801/Z/16/Z United Kingdom
Wellcome Trust106272/Z/14/Z United Kingdom
Wellcome Trust214090/Z/18/Z United Kingdom
Citation
Journal: Structure / Year: 2021
Title: Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.
Authors: Modenutti, C.P. / Blanco Capurro, J.I. / Ibba, R. / Alonzi, D.S. / Song, M.N. / Vasiljevic, S. / Kumar, A. / Chandran, A.V. / Tax, G. / Marti, L. / Hill, J.C. / Lia, A. / Hensen, M. / ...Authors: Modenutti, C.P. / Blanco Capurro, J.I. / Ibba, R. / Alonzi, D.S. / Song, M.N. / Vasiljevic, S. / Kumar, A. / Chandran, A.V. / Tax, G. / Marti, L. / Hill, J.C. / Lia, A. / Hensen, M. / Waksman, T. / Rushton, J. / Rubichi, S. / Santino, A. / Marti, M.A. / Zitzmann, N. / Roversi, P.
#1: Journal: Biorxiv / Year: 2019
Title: Clamping, bending, and twisting inter-domain motions in the misfold-recognising portion of UDP-glucose:glycoprotein glucosyl-transferase
Authors: Roversi, P. / Zitzmann, N.
History
DepositionDec 19, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 8, 2020Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / 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_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.pdbx_formal_charge / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 13, 2021Group: Database references / Derived calculations / Structure summary
Category: chem_comp / citation ...chem_comp / citation / citation_author / struct_conn
Item: _chem_comp.pdbx_synonyms / _struct_conn.pdbx_leaving_atom_flag
Revision 2.2Apr 14, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.title / _citation.year
Revision 2.3Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model
Item: _citation.journal_id_ISSN / _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: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
B: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
C: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
D: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)575,33024
Polymers569,6834
Non-polymers5,64720
Water00
1
A: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,0356
Polymers142,4211
Non-polymers1,6155
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,7116
Polymers142,4211
Non-polymers1,2905
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,8736
Polymers142,4211
Non-polymers1,4525
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,7116
Polymers142,4211
Non-polymers1,2905
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)151.145, 191.014, 158.807
Angle α, β, γ (deg.)90, 117.7, 90
Int Tables number4
Space group name H-MP1211

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Components

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Protein / Non-polymers , 2 types, 8 molecules ABCD

#1: Protein
UDP-glucose-glycoprotein glucosyltransferase-like protein,UDP-glucose-glycoprotein glucosyltransferase-like protein


Mass: 142420.688 Da / Num. of mol.: 4
Mutation: Deletion of CtUGGT TRXL2 domain i.e. residues CtUGGT 417-650
Source method: isolated from a genetically manipulated source
Details: Deletion of CtUGGT TRXL2 domain i.e. residues CtUGGT 417-650.,Deletion of CtUGGT TRXL2 domain i.e. residues CtUGGT 417-650.
Source: (gene. exp.) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus)
Gene: CTHT_0048990 / Plasmid: pHLsec / Cell (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: G0SB58
#6: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca

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Sugars , 4 types, 16 molecules

#2: 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.: 1
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
#3: 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.: 2
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
#4: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...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: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-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_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#5: 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.: 12
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

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Details

Has ligand of interestN

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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: 3.56 Å3/Da / Density % sol: 65.48 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.85 / Details: 0.1M Sodium citrate pH 5.5, 20% w/v PEG 3,000

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 13, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 5.74→140.609 Å / Num. obs: 17344 / % possible obs: 91.5 % / Redundancy: 5.6 % / CC1/2: 0.991 / Rmerge(I) obs: 0.15 / Rpim(I) all: 0.069 / Rrim(I) all: 0.165 / Net I/σ(I): 3.6
Reflection shellResolution: 5.74→6.152 Å / Rmerge(I) obs: 1.432 / Mean I/σ(I) obs: 1.3 / Num. unique obs: 817 / CC1/2: 0.467 / Rpim(I) all: 0.636 / Rrim(I) all: 1.569

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Processing

Software
NameVersionClassification
BUSTER2.10.3refinement
XDSdata reduction
STARANISOdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5nv4

5nv4


Resolution: 5.74→140.6 Å / Cor.coef. Fo:Fc: 0.768 / Cor.coef. Fo:Fc free: 0.706 / Cross valid method: THROUGHOUT / SU Rfree Blow DPI: 2.162
Details: The final model was refined in autoBUSTER with one set of TLS thermal motion tensors per domain and non-crystallographic symmetry and external restraints to the PDB ID 5NV4 structure
RfactorNum. reflection% reflectionSelection details
Rfree0.2489 829 -RANDOM
Rwork0.174 ---
obs0.1778 17344 74.9 %-
Displacement parametersBiso mean: 133.74 Å2
Baniso -1Baniso -2Baniso -3
1--7.3581 Å20 Å21.6844 Å2
2--7.6558 Å20 Å2
3----0.2977 Å2
Refine analyzeLuzzati coordinate error obs: 0.52 Å
Refinement stepCycle: LAST / Resolution: 5.74→140.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms35718 0 361 0 36079
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00936972HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.0750147HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d12933SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes6228HARMONIC5
X-RAY DIFFRACTIONt_it36556HARMONIC10
X-RAY DIFFRACTIONt_chiral_improper_torsion4813SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact28011SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion2.86
X-RAY DIFFRACTIONt_other_torsion21.7
LS refinement shellResolution: 5.725→6.03 Å
RfactorNum. reflection% reflection
Rfree0.3268 13 -
Rwork0.2164 --
obs--12.8 %
Refinement TLS params.

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)
10.16-3.90862.99448.31551.18333.10060.21460.1799-0.37510.17990.2017-0.0203-0.3751-0.0203-0.41630.18170.02760.0945-0.22840.1711-0.317938.654314.187240.4087
24.785-3.72811.93973.1190.95240.7177-0.120.0515-0.08330.05150.2769-0.7349-0.0833-0.7349-0.1569-0.3402-0.0356-0.0830.044-0.19040.1435-0.41411.811536.4616
33.815-1.1744-2.3392.40112.67063.5107-0.1529-0.29370.5798-0.29370.0927-0.33360.5798-0.33360.0601-0.0069-0.15750.0222-0.2450.089-0.362632.9283-23.868723.1118
43.33992.35982.1740.68260.90843.2427-0.1289-0.34690.0415-0.34690.1220.2580.04150.2580.00680.0405-0.2052-0.00360.11510.0639-0.323754.416-10.572819.6144
52.7402-1.28651.71293.3421-3.81035.7269-0.03190.1833-0.70840.1833-0.0173-0.6467-0.7084-0.64670.04910.11250.17160.0688-0.18440.0001-0.012230.938414.17129.3087
62.64990.1437-0.32522.87050.84471.39890.2822-0.234-0.1709-0.234-0.33670.1346-0.17090.13460.0545-0.24320.0710.18390.03990.1917-0.127653.81061.2245-8.3246
70.28223.07232.43576.90770.40932.4802-0.2688-0.180.0125-0.18-0.08740.40670.01250.40670.3563-0.083-0.2052-0.312-0.13240.06390.08325.191550.992213.5891
83.82772.9738-0.30324.4520.341.6233-0.1707-0.15330.1767-0.1533-0.3123-0.22450.1767-0.22450.4829-0.13870.00850.00270.026-0.1672-0.245913.620966.583350.404
96.67822.5757-2.32152.2323-1.93482.8094-0.1518-0.25220.4358-0.2522-0.18140.0550.43580.0550.3332-0.05090.1763-0.2559-0.304-0.0791-0.067142.105187.744725.9824
101.5311.53821.50152.2135-0.61821.98030.2205-0.0908-0.1954-0.0908-0.2972-0.2601-0.1954-0.26010.07670.32530.00470.1113-0.101-0.1692-0.197452.963873.01778.0106
115.61551.6740.19120-2.40829.26070.0953-0.1290.5972-0.1290.298-0.50980.5972-0.5098-0.3933-0.2863-0.2052-0.0636-0.25270.06390.166149.848548.585533.9337
123.34050.98171.16370-2.33151.526-0.0579-0.60010.3818-0.6001-0.1290.12320.38180.12320.1868-0.13160.1370.2148-0.1024-0.0997-0.058676.681558.865420.5072
136.40173.9298-1.68072.882-1.22371.649-0.2344-0.4582-0.7683-0.45820.1598-0.4072-0.7683-0.40720.07460.3722-0.2052-0.11620.17430.06390.1632-14.966320.158-20.5221
145.04911.4319-2.78881.73141.80596.2873-0.16890.30190.07470.30190.54420.44950.07470.4495-0.37530.1004-0.1018-0.0463-0.304-0.1331-0.20510.7096-10.4229-8.152
156.3264-0.5758-0.852902.16713.3845-0.41310.40810.53150.40810.2371-0.59110.5315-0.59110.176-0.1161-0.1718-0.24420.3040.0002-0.0552-29.2186-6.51919.305
161.7158-2.1074-1.28732.7713-2.24692.71210.2755-0.3034-0.6854-0.3034-0.54420.2288-0.68540.22880.26880.27550.06390.0110.26120.20520.3234-39.47916.6725.7122
174.9832.06051.16055.29592.336110.4531-0.03670.3851-0.65880.38510.18140.7349-0.65880.7349-0.14470.4291-0.2052-0.0863-0.24680.06390.1789-5.721426.23688.758
185.8041-1.87661.27778.31552.301910.3497-0.24520.2288-0.76830.22880.1814-0.7349-0.7683-0.73490.06380.3660.2052-0.0428-0.1049-0.06390.2419-30.21934.535527.9944
194.897-3.92982.78463.1331.22371.5742-0.1225-0.23280.6167-0.23280.0298-0.73490.6167-0.73490.09270.02970.20520.19310.0483-0.06390.013653.091742.665591.3893
205.8119-0.8851-2.10330.7560.28074.8976-0.3308-0.17150.1307-0.1715-0.14710.49570.13070.49570.478-0.0414-0.1993-0.0249-0.25160.067-0.2457.982872.09759.8568
214.40110.0105-1.32960-1.0732.6650.0702-0.48410.4381-0.4841-0.1674-0.17850.4381-0.17850.0972-0.07440.02020.0281-0.3040.0006-0.066725.467474.651387.7295
220.479-2.14181.61691.39660.12725.3196-0.2234-0.12660.5046-0.12660.2447-0.01670.5046-0.0167-0.02140.0609-0.0490.3273-0.20710.0934-0.060919.844353.0802100.3259
235.56411.22372.20160.71853.92984.28860.0295-0.10620.655-0.1062-0.18140.71870.6550.71870.15190.1663-0.00160.0273-0.304-0.17250.188230.627638.864770.0446
241.95472.0631.11322.85640.65035.84060.04040.29120.67780.29120.212-0.4910.6778-0.491-0.25240.0365-0.20520.1617-0.3040.06390.18271.152936.996483.0943
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|45 - A|224 A|1603 - A|1605 A|1802 - A|1803 }
2X-RAY DIFFRACTION2{ A|662 - A|880 }
3X-RAY DIFFRACTION3{ A|243 - A|413 A|881 - A|950 A|1607 }
4X-RAY DIFFRACTION4{ A|28 - A|44 A|225 - A|242 A|951 - A|1037 }
5X-RAY DIFFRACTION5{ A|1038 - A|1152 }
6X-RAY DIFFRACTION6{ A|1197 - A|1473 A|1606 A|1801 }
7X-RAY DIFFRACTION7{ B|45 - B|224 B|1603 - B|1605 }
8X-RAY DIFFRACTION8{ B|655 - B|880 }
9X-RAY DIFFRACTION9{ B|243 - B|413 B|881 - B|950 B|1607 }
10X-RAY DIFFRACTION10{ B|28 - B|44 B|225 - B|242 B|951 - B|1037 }
11X-RAY DIFFRACTION11{ B|1038 - B|1154 }
12X-RAY DIFFRACTION12{ B|1197 - B|1473 B|1606 B|1801 }
13X-RAY DIFFRACTION13{ C|45 - C|224 C|1603 - C|1605 C|1803 }
14X-RAY DIFFRACTION14{ C|662 - C|880 }
15X-RAY DIFFRACTION15{ C|243 - C|413 C|881 - C|950 C|1607 }
16X-RAY DIFFRACTION16{ C|28 - C|44 C|225 - C|242 C|951 - C|1037 }
17X-RAY DIFFRACTION17{ C|1038 - C|1149 }
18X-RAY DIFFRACTION18{ C|1197 - C|1473 C|1606 C|1801 }
19X-RAY DIFFRACTION19{ D|45 - D|224 D|1603 - D|1605 }
20X-RAY DIFFRACTION20{ D|653 - D|880 }
21X-RAY DIFFRACTION21{ D|243 - D|413 D|881 - D|950 D|1607 }
22X-RAY DIFFRACTION22{ D|28 - D|44 D|225 - D|242 D|951 - D|1037 }
23X-RAY DIFFRACTION23{ D|1038 - D|1150 }
24X-RAY DIFFRACTION24{ D|1197 - D|1473 D|1606 D|1801 }

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