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- PDB-5txm: STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WIT... -

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Basic information

Entry
Database: PDB / ID: 5txm
TitleSTRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WITH A DOUBLE STRANDED DNA AND AN INCOMING DDATP
Components
  • (HIV-1 Reverse Transcriptase ...Reverse transcriptase) x 2
  • DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')
  • DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')
KeywordsTRANSFERASE/DNA / RT / DNA / crosslink / N site complex / pyrophosphorolysis / P51 / P66 / TRANSFERASE / DRUG RESISTANCE / MUTATION / TRANSFERASE-DNA complex
Function / homology
Function and homology information


HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA ...HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / viral penetration into host nucleus / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / viral nucleocapsid / DNA recombination / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / symbiont-mediated suppression of host gene expression / lipid binding / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane
Similarity search - Function
HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. ...HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / Immunodeficiency lentiviral matrix, N-terminal / gag gene protein p17 (matrix protein) / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Retropepsin-like catalytic domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Ribonuclease H domain / RNase H type-1 domain profile. / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Retrovirus capsid, C-terminal / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Nucleotidyltransferase; domain 5 / Ribonuclease H superfamily / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / Alpha-Beta Plaits / Roll / DNA/RNA polymerase superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
sucrose / 2',3'-dideoxyadenosine triphosphate / DNA / DNA (> 10) / Gag-Pol polyprotein
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsDas, K. / Martinez, S.M. / Arnold, E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI027690 United States
Citation
Journal: Antimicrob. Agents Chemother. / Year: 2017
Title: Structural Insights into HIV Reverse Transcriptase Mutations Q151M and Q151M Complex That Confer Multinucleoside Drug Resistance.
Authors: Das, K. / Martinez, S.E. / Arnold, E.
#1: Journal: J.Biol.Chem. / Year: 2009
Title: Structural Basis For The Role Of The K65R Mutation In Hiv-1 Reverse Transcriptase Polymerization, Excision Antagonism, And Tenofovir Resistance.
Authors: Das, K. / Bandwar, R.P. / White, K.L. / Feng, J.Y. / Sarafianos, S.G. / Tuske, S. / Tu, X. / Clark, A.D. / Boyer, P.L. / Hou, X. / Gaffney, B.L. / Jones, R.A. / Miller, M.D. / Hughes, S.H. / Arnold, E.
#2: Journal: Nat.Struct.Mol.Biol. / Year: 2010
Title: Structural Basis Of Hiv-1 Resistance To Azt By Excision.
Authors: Tu, X. / Das, K. / Han, Q. / Bauman, J.D. / Clark, A.D. / Hou, X. / Frenkel, Y.V. / Gaffney, B.L. / Jones, R.A. / Boyer, P.L. / Hughes, S.H. / Sarafianos, S.G. / Arnold, E.
#3: Journal: Proc.Natl.Acad.Sci.Usa / Year: 2008
Title: High-Resolution Structures Of Hiv-1 Reverse Transcriptase/Tmc278 Complexes: Strategic Flexibility Explains Potency Against Resistance Mutations.
Authors: Das, K. / Bauman, J.D. / Clark, A.D. / Frenkel, Y.V. / Lewi, P.J. / Shatkin, A.J. / Hughes, S.H. / Arnold, E.
#4: Journal: J.Med.Chem. / Year: 2004
Title: Roles Of Conformational And Positional Adaptability In Structure-Based Design Of Tmc125-R165335 (Etravirine) And Related Non-Nucleoside Reverse Transcriptase Inhibitors That Are Highly Potent ...Title: Roles Of Conformational And Positional Adaptability In Structure-Based Design Of Tmc125-R165335 (Etravirine) And Related Non-Nucleoside Reverse Transcriptase Inhibitors That Are Highly Potent And Effective Against Wild-Type And Drug-Resistant Hiv-1 Variants.
Authors: Das, K. / Clark, A.D. / Lewi, P.J. / Heeres, J. / De Jonge, M.R. / Koymans, L.M. / Vinkers, H.M. / Daeyaert, F. / Ludovici, D.W. / Kukla, M.J. / De Corte, B. / Kavash, R.W. / Ho, C.Y. / Ye, ...Authors: Das, K. / Clark, A.D. / Lewi, P.J. / Heeres, J. / De Jonge, M.R. / Koymans, L.M. / Vinkers, H.M. / Daeyaert, F. / Ludovici, D.W. / Kukla, M.J. / De Corte, B. / Kavash, R.W. / Ho, C.Y. / Ye, H. / Lichtenstein, M.A. / Andries, K. / Pauwels, R. / De Bethune, M.P. / Boyer, P.L. / Clark, P. / Hughes, S.H. / Janssen, P.A. / Arnold, E.
History
DepositionNov 17, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 5, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2017Group: Database references
Revision 1.2Jun 7, 2017Group: Database references
Revision 1.3Sep 20, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_asym / struct_conn / struct_conn_type / 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.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _struct_asym.entity_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 4, 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: HIV-1 Reverse Transcriptase P66 subunit
B: HIV-1 Reverse Transcriptase P51 subunit
T: DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')
P: DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')
C: HIV-1 Reverse Transcriptase P66 subunit
D: HIV-1 Reverse Transcriptase P51 subunit
E: DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')
F: DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)260,18623
Polymers257,9858
Non-polymers2,20115
Water3,369187
1
A: HIV-1 Reverse Transcriptase P66 subunit
B: HIV-1 Reverse Transcriptase P51 subunit
T: DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')
P: DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)130,20313
Polymers128,9934
Non-polymers1,2109
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15930 Å2
ΔGint-80 kcal/mol
Surface area48280 Å2
MethodPISA
2
C: HIV-1 Reverse Transcriptase P66 subunit
D: HIV-1 Reverse Transcriptase P51 subunit
E: DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')
F: DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,98310
Polymers128,9934
Non-polymers9906
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15290 Å2
ΔGint-61 kcal/mol
Surface area48970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.337, 133.946, 139.399
Angle α, β, γ (deg.)90.00, 97.71, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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HIV-1 Reverse Transcriptase ... , 2 types, 4 molecules ACBD

#1: Protein HIV-1 Reverse Transcriptase P66 subunit / Pr160Gag-Pol


Mass: 64079.473 Da / Num. of mol.: 2 / Mutation: Q258C, C280S, D498N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Strain: isolate BH10 / Gene: gag-pol / Production host: Escherichia coli (E. coli) / References: UniProt: P03366, RNA-directed DNA polymerase
#2: Protein HIV-1 Reverse Transcriptase P51 subunit / Pr160Gag-Pol


Mass: 50039.488 Da / Num. of mol.: 2 / Mutation: C280S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Strain: isolate BH10 / Gene: gag-pol / Production host: Escherichia coli (E. coli) / References: UniProt: P03366, DNA-directed DNA polymerase

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DNA chain , 2 types, 4 molecules TEPF

#3: DNA chain DNA (5'-D(*TP*GP*GP*TP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*G)-3')


Mass: 8383.385 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Human immunodeficiency virus 1
#4: DNA chain DNA (5'-D(*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG)P*CP*GP*CP*CP*G)-3')


Mass: 6490.267 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Human immunodeficiency virus 1

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Sugars , 1 types, 2 molecules

#5: Polysaccharide beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose /


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: sucrose
DescriptorTypeProgram
DFrufb2-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][b-D-Fruf]{[(2+1)][a-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 5 types, 200 molecules

#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-DDS / 2',3'-dideoxyadenosine triphosphate


Mass: 475.182 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O11P3
#8: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H6O2
#9: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 187 / Source method: isolated from a natural source / Formula: H2O

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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: 3.24 Å3/Da / Density % sol: 62.03 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: PEG 8000, AMMONIUM SULFATE, MGCL2, GLYCEROL, SUCROSE,
PH range: 6.8 - 7.2

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Data collection

DiffractionMean temperature: 104 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Sep 17, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 87934 / % possible obs: 97.4 % / Observed criterion σ(I): -1 / Redundancy: 4.2 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 12.9
Reflection shellResolution: 2.7→2.75 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.57 / CC1/2: 0.484 / % possible all: 91.1

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Processing

Software
NameVersionClassification
PHENIX(1.10_2155: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3V4I

3v4i


Resolution: 2.7→46.046 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 22.98
RfactorNum. reflection% reflectionSelection details
Rfree0.2226 2621 2.98 %Random
Rwork0.1836 ---
obs0.1848 87934 97.42 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.7→46.046 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15824 1802 137 187 17950
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00918437
X-RAY DIFFRACTIONf_angle_d1.0225393
X-RAY DIFFRACTIONf_dihedral_angle_d15.80410743
X-RAY DIFFRACTIONf_chiral_restr0.0622765
X-RAY DIFFRACTIONf_plane_restr0.0082876
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7001-2.74920.34551320.30694182X-RAY DIFFRACTION91
2.7492-2.80210.31441450.29314383X-RAY DIFFRACTION95
2.8021-2.85920.32371230.27664452X-RAY DIFFRACTION97
2.8592-2.92140.31871540.27964499X-RAY DIFFRACTION98
2.9214-2.98930.29441320.25934513X-RAY DIFFRACTION98
2.9893-3.06410.27761460.23794461X-RAY DIFFRACTION98
3.0641-3.14690.26441220.21964515X-RAY DIFFRACTION98
3.1469-3.23950.25041580.21164511X-RAY DIFFRACTION98
3.2395-3.3440.2381420.20774512X-RAY DIFFRACTION98
3.344-3.46350.2331330.1934525X-RAY DIFFRACTION98
3.4635-3.60210.23911370.17954553X-RAY DIFFRACTION99
3.6021-3.7660.2261450.17874522X-RAY DIFFRACTION99
3.766-3.96440.1991340.16774509X-RAY DIFFRACTION98
3.9644-4.21270.21321310.15754541X-RAY DIFFRACTION99
4.2127-4.53770.18911400.15174554X-RAY DIFFRACTION99
4.5377-4.99380.18211330.14644527X-RAY DIFFRACTION98
4.9938-5.71530.18361220.15824514X-RAY DIFFRACTION97
5.7153-7.19620.22411460.19094401X-RAY DIFFRACTION95
7.1962-46.05270.19361460.16214639X-RAY DIFFRACTION98
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)
1-0.00050.00280.0013-0.00550.0001-0.00250.1010.00340.0319-0.13180.0240.0725-0.0248-0.080901.1656-0.2736-0.1280.82340.12510.5183-13.626316.107218.6096
20.0992-0.001-0.0670.0265-0.04710.08620.1190.1490.2532-0.20060.06770.093-0.0558-0.05770.09071.077-0.4027-0.08020.50380.290.3514-11.652124.259925.318
30.1446-0.1024-0.07610.09950.04880.04750.21370.03290.405-0.23440.1075-0.1522-0.1390.09560.15021.0701-0.460.12790.59240.06690.6263.56521.706737.1813
40.01790.0115-0.030.0236-0.07810.20790.0568-0.09650.1093-0.230.11760.0593-0.3423-0.06080.00360.6746-0.097-0.00120.34210.0150.7743-20.935326.987356.7226
50.0551-0.0156-0.02930.2539-0.01590.01960.10320.02460.1267-0.01510.07250.1651-0.29280.13360.2710.1801-0.3007-0.225-0.1931-0.38350.2518-17.37938.174967.6719
60.03970.0008-0.04490.11370.04430.0785-0.1289-0.07380.1882-0.14330.06120.0951-0.1005-0.1459-0.07640.14180.036-0.04080.3423-0.01010.3784-46.0092-4.562673.5194
70.0289-0.0248-0.01250.01980.00430.01850.01920.08110.0062-0.0574-0.04490.09020.0674-0.236400.2728-0.0318-0.03120.3804-0.11480.4823-46.5251-7.889674.1843
80.0596-0.05390.04980.0453-0.04690.05410.04640.12520.0524-0.23530.11-0.0899-0.04360.16180.06350.4765-0.2730.06680.4086-0.14260.2493-3.9856-3.967537.8363
90.0337-0.0011-0.02880.00540.00270.0230.0548-0.0454-0.2575-0.20260.1378-0.01470.13680.1522-00.4979-0.1241-0.01210.4511-0.14620.5717-8.4468-15.497843.583
100.1130.07430.09670.05010.0640.0753-0.14830.1708-0.2755-0.2050.273-0.2217-0.16580.48610.02520.566-0.08650.1470.4159-0.17470.5181-2.1421-19.081341.1885
110.01970.00910.00720.12110.06270.1171-0.2248-0.0262-0.22680.09660.1933-0.03010.41610.16920.05940.36950.02380.05380.3535-0.07520.5488-25.8557-29.535665.3165
120.1002-0.0333-0.00350.05980.07310.0766-0.1265-0.04750.03580.0294-0.0190.13660.0784-0.0569-0.15330.2293-0.0565-0.04850.2778-0.10970.4043-19.2555-15.986359.1636
130.00390.00210.00360.00420.0020.0020.0472-0.0149-0.0130.0255-0.0068-0.01910.0169-0.0268-01.0085-0.0577-0.26240.77980.25540.9278-24.628427.23430.0836
140.0041-0.0066-0.00250.00290.00490.01050.0399-0.0046-0.0003-0.1296-0.03010.0986-0.0496-0.0029-00.7946-0.2365-0.13970.75620.15380.777-26.382213.157946.2392
150.00110.00080.00130.00260.00230.00220.0209-0.0032-0.0239-0.04220.00930.03540.03920.014201.1766-0.26560.00160.99880.04761.1686-38.1015-7.142649.7593
160.00280.0027-0.00150.002-0.00070.0039-0.0086-0.0283-0.01860.0021-0.03510.0018-0.01990.0066-01.1516-0.4391-0.19651.382-0.02741.404-52.5542-14.557454.8151
170.0068-0.010.00410.01-0.00150.01130.0287-0.00970.0989-0.1101-0.0606-0.1265-0.06560.0023-00.5501-0.2572-0.15690.6634-0.05170.6089-44.0572-7.405651.1104
180.0059-0.0054-0.00710.00820.00390.0081-0.085-0.00360.0702-0.11640.00530.0291-0.08380.03-01.2066-0.27460.02990.74790.33291.1352-23.685117.175243.5627
190.39750.0423-0.12480.0551-0.04370.32690.26520.65740.0637-0.47570.0224-0.01850.0334-0.14630.45061.39060.2073-0.03320.80930.00890.357-22.1572-49.1864-10.1906
200.0151-0.03130.03090.0597-0.06360.0948-0.00620.06270.1069-0.0542-0.28260.096-0.3088-0.0242-0.020.93750.1150.22830.526-0.06110.596-38.4136-40.372514.8427
210.0332-0.0318-0.04380.0680.00340.11610.0463-0.00610.0083-0.26630.06220.0344-0.13840.03690.11330.4163-0.0362-0.00870.2199-0.09040.3351-24.34-44.210831.9698
220.06920.05990.01020.2928-0.07070.1181-0.0167-0.2623-0.1427-0.27290.17660.20930.0518-0.34820.10590.1687-0.0589-0.06270.32350.00760.3057-37.9871-66.78750.7975
230.0577-0.030.01430.18720.01130.01030.17890.05230.0165-0.1699-0.0890.03190.11330.22160.04010.77860.13360.20670.4208-0.03960.3822-4.0451-59.62058.3871
240.0167-0.0022-0.01640.00480.00170.01390.0807-0.0143-0.0214-0.0804-0.0118-0.08990.05660.1428-00.77940.21440.15550.7789-0.02050.6141-0.2088-66.213919.5151
250.01210.04760.0250.21510.10720.0567-0.0613-0.0566-0.1249-0.291-0.0882-0.20240.09860.4096-0.23120.70550.36310.19671.00670.14030.47846.8916-66.170817.4711
260.0077-0.01280.02180.0557-0.01990.02860.07240.12640.0526-0.1626-0.0755-0.12450.10540.1126-0.02320.30020.06810.13410.67180.06240.49531.7574-67.951242.3666
270.1097-0.06480.1320.0739-0.11430.12690.2028-0.0307-0.2711-0.2869-0.1660.10480.1862-0.02120.00890.39350.0652-0.01040.4181-0.0010.4066-12.6976-74.880450.3213
280.0114-0.01860.00220.0421-0.00160.0327-0.1365-0.0048-0.0115-0.0357-0.13220.1180.15810.2397-00.4150.06280.02890.48370.00420.3263-9.5636-63.604433.3864
290.0099-0.00230.00230.00130.00260.00410.0237-0.0080.01080.06880.01520.03120.02490.0207-00.94360.049-0.16110.9395-0.15590.6513-39.7069-55.469-6.2719
30-0.0002-0.0017-0.00340.00510.00790.00750.22040.01110.0131-0.1025-0.00870.09710.0609-0.008-01.1581-0.149-0.06480.76470.0690.5513-32.6695-57.538713.9366
310.004-0.0084-0.00490.00980.00830.00480.106-0.0489-0.1366-0.011-0.0122-0.03560.0463-0.02880.00011.1178-0.0689-0.14811.01430.21811.3497-30.7655-79.733433.8107
32-0.0019-0.0007-0.00160.00670.01480.01820.03920.1212-0.0507-0.0618-0.00660.0137-0.00240.111-00.8285-0.17940.06440.3454-0.08280.5576-32.3545-78.223131.7257
330.0005-0.00050.001-0.0001-0.0020.0016-0.06610.0017-0.0076-0.022-0.10530.08580.0302-0.0002-01.4506-0.019-0.1961.19420.0530.9412-33.9202-60.587812.0863
340.00470.001-0.00240.0009-00.004-0.00160.0088-0.0022-0.0605-0.00350.0232-0.0166-0.000601.22610.1256-0.04741.10990.12360.7177-31.5829-45.75983.9123
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 27 )
2X-RAY DIFFRACTION2chain 'A' and (resid 28 through 143 )
3X-RAY DIFFRACTION3chain 'A' and (resid 144 through 226 )
4X-RAY DIFFRACTION4chain 'A' and (resid 227 through 325 )
5X-RAY DIFFRACTION5chain 'A' and (resid 326 through 421 )
6X-RAY DIFFRACTION6chain 'A' and (resid 422 through 515 )
7X-RAY DIFFRACTION7chain 'A' and (resid 516 through 554 )
8X-RAY DIFFRACTION8chain 'B' and (resid 4 through 59 )
9X-RAY DIFFRACTION9chain 'B' and (resid 60 through 99 )
10X-RAY DIFFRACTION10chain 'B' and (resid 100 through 194 )
11X-RAY DIFFRACTION11chain 'B' and (resid 195 through 325 )
12X-RAY DIFFRACTION12chain 'B' and (resid 326 through 428 )
13X-RAY DIFFRACTION13chain 'T' and (resid 702 through 706 )
14X-RAY DIFFRACTION14chain 'T' and (resid 707 through 716 )
15X-RAY DIFFRACTION15chain 'T' and (resid 717 through 721 )
16X-RAY DIFFRACTION16chain 'T' and (resid 722 through 725 )
17X-RAY DIFFRACTION17chain 'P' and (resid 803 through 812 )
18X-RAY DIFFRACTION18chain 'P' and (resid 813 through 822 )
19X-RAY DIFFRACTION19chain 'C' and (resid -1 through 226 )
20X-RAY DIFFRACTION20chain 'C' and (resid 227 through 325 )
21X-RAY DIFFRACTION21chain 'C' and (resid 326 through 421 )
22X-RAY DIFFRACTION22chain 'C' and (resid 422 through 554 )
23X-RAY DIFFRACTION23chain 'D' and (resid 4 through 59 )
24X-RAY DIFFRACTION24chain 'D' and (resid 60 through 99 )
25X-RAY DIFFRACTION25chain 'D' and (resid 100 through 194 )
26X-RAY DIFFRACTION26chain 'D' and (resid 195 through 269 )
27X-RAY DIFFRACTION27chain 'D' and (resid 270 through 363 )
28X-RAY DIFFRACTION28chain 'D' and (resid 364 through 428 )
29X-RAY DIFFRACTION29chain 'E' and (resid 702 through 706 )
30X-RAY DIFFRACTION30chain 'E' and (resid 707 through 716 )
31X-RAY DIFFRACTION31chain 'E' and (resid 717 through 725 )
32X-RAY DIFFRACTION32chain 'F' and (resid 803 through 812 )
33X-RAY DIFFRACTION33chain 'F' and (resid 813 through 818 )
34X-RAY DIFFRACTION34chain 'F' and (resid 819 through 822 )

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