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

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Basic information

Entry
Database: PDB / ID: 5txl
TitleSTRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WITH A DOUBLE STRANDED DNA AND AN INCOMING DATP
Components
  • (HIV-1 REVERSE TRANSCRIPTASE ...) x 2
  • DNA (5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG) P*CP*GP*CP*CP*GP)-3')
  • DNA (5'-D(*AP*TP*GP*GP*AP*AP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP* CP*TP*GP*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 / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency ...HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / host cell / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / symbiont-mediated suppression of host gene expression / viral translational frameshifting / lipid binding / symbiont entry into host cell / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / proteolysis / DNA 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. / Retropepsin-like catalytic domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / RNase H type-1 domain profile. / Ribonuclease H domain / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Reverse transcriptase domain / Retrovirus capsid, C-terminal / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase (RT) catalytic domain profile. / 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 / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H 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'-DEOXYADENOSINE 5'-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: 2.501 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 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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
Revision 2.2Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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(*AP*TP*GP*GP*AP*AP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP* CP*TP*GP*TP*G)-3')
P: DNA (5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG) P*CP*GP*CP*CP*GP)-3')
C: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
E: DNA (5'-D(*AP*TP*GP*GP*AP*AP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP* CP*TP*GP*TP*G)-3')
F: DNA (5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG) P*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)263,82022
Polymers261,6498
Non-polymers2,17114
Water3,945219
1
A: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
B: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
T: DNA (5'-D(*AP*TP*GP*GP*AP*AP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP* CP*TP*GP*TP*G)-3')
P: DNA (5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG) P*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,98912
Polymers130,8254
Non-polymers1,1648
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15720 Å2
ΔGint-83 kcal/mol
Surface area48360 Å2
MethodPISA
2
C: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
E: DNA (5'-D(*AP*TP*GP*GP*AP*AP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP* CP*TP*GP*TP*G)-3')
F: DNA (5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*(MRG) P*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,83110
Polymers130,8254
Non-polymers1,0066
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15300 Å2
ΔGint-64 kcal/mol
Surface area48960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.380, 133.846, 139.340
Angle α, β, γ (deg.)90.00, 97.30, 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: 64022.414 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: 51928.629 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, RNA-directed DNA polymerase, DNA-directed DNA polymerase

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DNA chain , 2 types, 4 molecules TEPF

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


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


Mass: 6490.267 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: SYNTHESIZED / 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, 231 molecules

#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-DTP / 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE


Mass: 491.182 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O12P3
#8: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#9: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 219 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 3.4 Å3/Da / Density % sol: 63.79 %
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 PILATUS 6M-F / 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: 2.5→50 Å / Num. obs: 111859 / % possible obs: 98.7 % / Observed criterion σ(I): -1 / Redundancy: 4.1 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 15.6
Reflection shellResolution: 2.5→2.54 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.53 / CC1/2: 0.619 / % possible all: 88.1

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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: 2.501→48.075 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 23.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2245 3349 3 %Random
Rwork0.1927 ---
obs0.1937 111811 98.54 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.501→48.075 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15824 1802 135 219 17980
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00618432
X-RAY DIFFRACTIONf_angle_d0.89925389
X-RAY DIFFRACTIONf_dihedral_angle_d15.84810742
X-RAY DIFFRACTIONf_chiral_restr0.0532767
X-RAY DIFFRACTIONf_plane_restr0.0062876
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5011-2.53690.29851220.3013897X-RAY DIFFRACTION85
2.5369-2.57470.32961430.29434282X-RAY DIFFRACTION93
2.5747-2.6150.33521230.28824359X-RAY DIFFRACTION97
2.615-2.65780.29141410.27084535X-RAY DIFFRACTION99
2.6578-2.70370.29291400.27984483X-RAY DIFFRACTION99
2.7037-2.75280.28061320.26964584X-RAY DIFFRACTION100
2.7528-2.80580.26911520.25554545X-RAY DIFFRACTION100
2.8058-2.8630.27831290.24194584X-RAY DIFFRACTION100
2.863-2.92530.27991560.23234563X-RAY DIFFRACTION100
2.9253-2.99330.26271380.22084552X-RAY DIFFRACTION100
2.9933-3.06820.23571450.22234580X-RAY DIFFRACTION100
3.0682-3.15110.27131370.23084561X-RAY DIFFRACTION100
3.1511-3.24380.24081470.2184587X-RAY DIFFRACTION100
3.2438-3.34850.26071480.21414561X-RAY DIFFRACTION100
3.3485-3.46810.23481340.20944583X-RAY DIFFRACTION100
3.4681-3.60690.2371440.19784574X-RAY DIFFRACTION100
3.6069-3.7710.23951460.1924583X-RAY DIFFRACTION100
3.771-3.96980.19311370.17894565X-RAY DIFFRACTION100
3.9698-4.21830.23211360.16654590X-RAY DIFFRACTION100
4.2183-4.54380.17241400.16034583X-RAY DIFFRACTION100
4.5438-5.00060.19311390.15484629X-RAY DIFFRACTION100
5.0006-5.72320.19571220.1714606X-RAY DIFFRACTION100
5.7232-7.20680.23441580.19484582X-RAY DIFFRACTION99
7.2068-48.08370.17211400.15334494X-RAY DIFFRACTION95
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)
10.0010.02990.01340.00650.01010.0140.1965-0.0110.0719-0.22260.03740.00320.0138-0.1408-01.1397-0.2811-0.02730.75910.15220.4735-13.42416.124818.7589
2-0.0031-0.01440.04630.05730.01210.00450.28640.25940.1724-0.22910.02830.0866-0.0187-0.0550.05121.8609-0.3377-0.21811.08230.45120.9688-14.432227.842121.5344
30.0744-0.03170.03220.0344-0.0573-0.00220.17870.09120.4743-0.236-0.0477-0.15970.12550.04930.01731.0303-0.3938-0.02240.55470.0980.3295-8.473320.773929.2812
40.0524-0.0302-0.0660.1658-0.05530.13440.21490.13920.5098-0.63960.2008-0.2935-0.24980.07510.32821.1306-0.47780.18660.64540.0440.62133.836321.723937.2898
50.12510.1113-0.00940.1936-0.13630.1951-0.0435-0.2350.0753-0.25880.2170.0196-0.5362-0.12990.04010.6468-0.21260.04690.127-0.04530.7626-20.598626.944756.8983
60.00630.0242-0.03360.02040.01280.05040.0977-0.07890.2472-0.0610.00610.2246-0.28220.0178-00.3891-0.06150.00130.254-0.08790.5113-18.029114.46365.9584
70.0744-0.0808-0.05550.2420.09870.0650.0406-0.0224-0.0666-0.0018-0.04790.111-0.0890.1222-0.01760.2845-0.0743-0.05230.3185-0.13420.3541-16.29344.077569.0204
80.19260.0359-0.19530.1543-0.05210.1287-0.0958-0.05690.1583-0.09240.0870.0859-0.0495-0.069500.19240.0215-0.06020.3918-0.02780.4203-45.5828-4.677673.6538
90.0901-0.0518-0.05170.03320.02080.09440.07510.08320.0987-0.1131-0.04690.15770.0097-0.2778-00.26460.0116-0.05580.3864-0.07660.4816-46.0952-8.008774.3105
100.03610.0288-0.03380.00230.02140.00420.1630.21490.0864-0.2054-0.0993-0.04490.12460.17750.00820.4984-0.3278-0.150.3368-0.30550.2764-10.1971-7.912934.5033
110.720.053-0.13710.29730.11440.3278-0.19370.1735-0.2764-0.31710.3174-0.1994-0.05660.39240.01290.5288-0.1410.10110.4753-0.15920.4521-2.8104-14.860941.6956
120.00360.051-0.05290.23260.1161-0.0075-0.0292-0.1098-0.18210.15290.1213-0.02270.13410.22780.01040.31030.09930.00860.5704-0.08060.6086-14.1898-27.850662.5256
130.0885-0.1749-0.17470.31810.09220.1313-0.268-0.0172-0.08840.08740.0320.10590.34890.0455-0.15320.352-0.06780.04090.2257-0.13280.4357-31.0031-26.768366.1455
140.13680.0050.07240.18750.06040.1195-0.1598-0.0261-0.0448-0.06760.04860.1573-0.0173-0.0334-0.14720.2719-0.0806-0.02830.3309-0.11350.3992-17.7363-13.868457.4678
150.00260.00640.00520.00550.00620.00230.114-0.005-0.01830.01490.056-0.0434-0.0164-0.039601.3066-0.0633-0.34270.93180.27060.9063-24.356827.197230.2617
160.0059-0.00840.0033-0.01590.01290.01550.041-0.01290.0278-0.34380.03550.314-0.17730.0619-00.815-0.2354-0.15630.7860.16580.814-26.028313.113546.4217
170.0046-0.00040.00070.0040.00580.00580.03990.0198-0.0443-0.05940.02930.05940.07880.064601.2593-0.29280.09240.992-0.00211.1262-37.7454-7.178249.922
180.00820.00780.00010.00170.00060.0069-0.0344-0.04-0.0516-0.0426-0.0758-0.0048-0.0106-0.0506-01.0561-0.5149-0.21041.16190.02231.3022-52.143-14.62854.9896
190.0134-0.03010.00630.025-0.00390.00790.15020.00670.1614-0.2855-0.1207-0.2477-0.0825-0.108300.6553-0.2053-0.14170.7877-0.01880.7741-43.6573-7.460251.2715
200.00690.0026-0.02430.00580.00770.0121-0.19220.02150.0862-0.17070.00690.0882-0.21860.0338-01.0704-0.22980.00270.78330.27131.0326-23.337517.142843.7301
210.35290.09580.02990.3545-0.31630.59320.53710.59220.9757-0.2967-0.1220.5445-0.2517-0.250.3651.25030.26890.05610.6929-0.0141-0.6113-26.8168-46.4852-2.5295
220.7069-0.06960.05780.59650.13740.5515-0.014-0.1843-0.0626-0.17420.08270.0267-0.1105-0.13210.04280.2304-0.0355-0.05690.2609-0.05590.2663-31.5336-56.883242.5509
230.1197-0.08230.07580.1604-0.04620.02840.25140.1050.033-0.4641-0.2326-0.09180.2640.36340.03410.8490.1360.21970.5368-0.01320.4384-3.7324-59.55938.3538
240.0327-0.0103-0.02030.00140.01960.01950.0351-0.0643-0.0324-0.20020.0383-0.14120.1530.380200.71230.22920.12670.78060.01130.58410.1656-66.165319.4728
250.07040.0765-0.04810.1783-0.0780.047-0.26950.13640.0506-0.8773-0.06620.01780.14190.8343-0.27840.42120.64190.64811.11080.10380.18277.2623-66.101217.3863
260.0448-0.00450.14070.0885-0.11070.07830.23160.05520.0477-0.0016-0.0997-0.12020.19890.17050.02570.16010.15480.08140.52910.02090.35072.2109-67.945242.3228
270.1618-0.1710.2810.2431-0.24340.23240.1213-0.0659-0.1683-0.188-0.2034-0.03860.10510.0108-0.00010.31560.07170.00150.3653-0.01290.3766-12.1999-74.915650.3078
280.0496-0.00270.00510.13380.03120.0557-0.0063-0.03820.1159-0.2365-0.24780.11980.13980.404-0.00370.3990.07460.03640.5049-0.05430.3631-9.1599-63.588233.3541
290.0029-0.0017-00.0020.00350.00190.0627-0.00730.0020.12-0.02460.01240.04410.0221-00.9872-0.08-0.10350.9275-0.18160.5988-39.4004-55.4948-6.1853
300.00180.0064-0.0126-0.00820.02240.00710.4722-0.0286-0.0717-0.14860.01080.14520.2037-0.077401.0985-0.1352-0.06750.83130.07210.6436-32.2575-57.54813.9888
310.0012-0.0125-0.00670.02160.0310.01270.2002-0.0205-0.24680.0199-0.0969-0.16140.1612-0.047301.009-0.1077-0.09320.88650.14841.4403-30.3632-79.799333.875
320.00110.00080.00490.00210.00150.0013-0.05940.00110.0433-0.0309-0.07620.01330.0032-0.019-01.4233-0.10140.18041.0857-0.25851.3438-31.3531-87.492132.8668
33-0.00950.02210.0207-0.0196-0.02390.01240.19520.2115-0.1553-0.4297-0.20230.236-0.0860.051300.8739-0.0675-0.08010.485-0.02080.3718-33.0513-64.418520.3005
340.00570.0018-0.0006-0.0029-0.00210.0004-0.01030.03580.0427-0.0787-0.02890.1039-0.02240.0041-01.20630.2244-0.06981.12010.12480.5304-31.2681-45.74463.96
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 83 )
3X-RAY DIFFRACTION3chain 'A' and (resid 84 through 143 )
4X-RAY DIFFRACTION4chain 'A' and (resid 144 through 226 )
5X-RAY DIFFRACTION5chain 'A' and (resid 227 through 325 )
6X-RAY DIFFRACTION6chain 'A' and (resid 326 through 363 )
7X-RAY DIFFRACTION7chain 'A' and (resid 364 through 421 )
8X-RAY DIFFRACTION8chain 'A' and (resid 422 through 515 )
9X-RAY DIFFRACTION9chain 'A' and (resid 516 through 554 )
10X-RAY DIFFRACTION10chain 'B' and (resid 4 through 27 )
11X-RAY DIFFRACTION11chain 'B' and (resid 28 through 194 )
12X-RAY DIFFRACTION12chain 'B' and (resid 195 through 269 )
13X-RAY DIFFRACTION13chain 'B' and (resid 270 through 363 )
14X-RAY DIFFRACTION14chain 'B' and (resid 364 through 428 )
15X-RAY DIFFRACTION15chain 'T' and (resid 702 through 706 )
16X-RAY DIFFRACTION16chain 'T' and (resid 707 through 716 )
17X-RAY DIFFRACTION17chain 'T' and (resid 717 through 721 )
18X-RAY DIFFRACTION18chain 'T' and (resid 722 through 725 )
19X-RAY DIFFRACTION19chain 'P' and (resid 803 through 812 )
20X-RAY DIFFRACTION20chain 'P' and (resid 813 through 822 )
21X-RAY DIFFRACTION21chain 'C' and (resid -1 through 325 )
22X-RAY DIFFRACTION22chain 'C' and (resid 326 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 807 )
33X-RAY DIFFRACTION33chain 'F' and (resid 808 through 818 )
34X-RAY DIFFRACTION34chain 'F' and (resid 819 through 822 )

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