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- PDB-5txn: STRUCTURE OF Q151M MUTANT HIV-1 REVERSE TRANSCRIPTASE (RT) TERNAR... -

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Basic information

Entry
Database: PDB / ID: 5txn
TitleSTRUCTURE OF Q151M MUTANT 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(*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 / 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 / symbiont-mediated suppression of host gene expression / 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 / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / viral translational frameshifting / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / 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 / Reverse transcriptase domain / Reverse transcriptase (RNA-dependent DNA polymerase) / 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 / 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: 2.55 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: Atomic model / Data collection ...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 / 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
Revision 2.2Nov 13, 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(*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)259,86219
Polymers257,8778
Non-polymers1,98411
Water3,207178
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)129,8839
Polymers128,9394
Non-polymers9445
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14990 Å2
ΔGint-67 kcal/mol
Surface area48100 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)129,97910
Polymers128,9394
Non-polymers1,0406
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14900 Å2
ΔGint-89 kcal/mol
Surface area48410 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.039, 133.634, 139.206
Angle α, β, γ (deg.)90.00, 97.88, 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: 64025.477 Da / Num. of mol.: 2 / Mutation: Q151M, 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, DNA-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, 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(*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, 187 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-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#9: Chemical ChemComp-SO4 / SULFATE ION


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


Mass: 18.015 Da / Num. of mol.: 178 / 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: 3.22 Å3/Da / Density % sol: 61.76 %
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: CHESS / Beamline: F1 / Wavelength: 0.9191 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Mar 30, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9191 Å / Relative weight: 1
ReflectionResolution: 2.55→50 Å / Num. obs: 106245 / % possible obs: 98.1 % / Observed criterion σ(I): -1 / Redundancy: 5 % / Rmerge(I) obs: 0.095 / Net I/σ(I): 9
Reflection shellResolution: 2.55→2.59 Å / Redundancy: 4.1 % / % possible all: 97

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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: 2.55→33.38 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 25.33
RfactorNum. reflection% reflectionSelection details
Rfree0.226 3048 2.92 %Random
Rwork0.196 ---
obs0.197 104269 98.2 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.55→33.38 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15820 1802 123 178 17923
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00618414
X-RAY DIFFRACTIONf_angle_d0.8125380
X-RAY DIFFRACTIONf_dihedral_angle_d15.94210738
X-RAY DIFFRACTIONf_chiral_restr0.0432768
X-RAY DIFFRACTIONf_plane_restr0.0062874
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.55-2.58980.36781220.33314533X-RAY DIFFRACTION97
2.5898-2.63230.31951250.31994565X-RAY DIFFRACTION97
2.6323-2.67770.34351330.30814530X-RAY DIFFRACTION97
2.6777-2.72630.3391520.29824612X-RAY DIFFRACTION98
2.7263-2.77870.30671150.28654524X-RAY DIFFRACTION98
2.7787-2.83540.35271370.26964594X-RAY DIFFRACTION98
2.8354-2.8970.28691230.25854581X-RAY DIFFRACTION98
2.897-2.96440.2821480.24164578X-RAY DIFFRACTION98
2.9644-3.03850.23351360.23434597X-RAY DIFFRACTION98
3.0385-3.12060.26951370.23334586X-RAY DIFFRACTION99
3.1206-3.21230.24531640.22044621X-RAY DIFFRACTION99
3.2123-3.31590.27591330.21794609X-RAY DIFFRACTION99
3.3159-3.43430.29291420.21934635X-RAY DIFFRACTION99
3.4343-3.57170.24091350.2124639X-RAY DIFFRACTION99
3.5717-3.7340.23691560.1954638X-RAY DIFFRACTION99
3.734-3.93060.23471400.18444658X-RAY DIFFRACTION99
3.9306-4.17640.18541590.16644640X-RAY DIFFRACTION99
4.1764-4.49820.18641400.1574652X-RAY DIFFRACTION99
4.4982-4.94960.19441610.15264625X-RAY DIFFRACTION99
4.9496-5.66280.20351380.16784690X-RAY DIFFRACTION99
5.6628-7.12310.20991300.18684719X-RAY DIFFRACTION100
7.1231-33.38310.1451220.1534395X-RAY DIFFRACTION91
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)
10.60680.36970.30130.9022-0.33530.57750.09570.19050.2073-0.88340.26740.3413-0.11-0.6366-0.25471.5716-0.33-0.11841.1560.22870.7659-14.145916.099618.9191
20.9408-0.0547-0.09650.8994-0.61340.44350.06630.62260.6342-0.66520.11660.2574-0.5074-0.2961-0.23262.1924-0.4364-0.16271.43080.40571.1599-14.728127.768521.4817
30.88320.0015-0.40762.0433-0.2121.92210.06230.4190.6864-0.77550.1970.0017-0.51960.1395-0.20681.1012-0.33540.03660.68070.09280.7803-5.30323.126838.3688
42.4553-0.1333-0.30521.2589-0.99161.873-0.023-0.11460.3713-0.10730.40050.484-0.7548-0.3356-0.34490.82880.004-0.00680.4903-0.03421.0477-23.990124.99259.9411
52.55011.3062-1.04072.04410.04182.21830.0723-0.02230.31660.0870.0720.1163-0.36710.1526-0.10690.3872-0.062-0.0430.3424-0.12540.4572-17.59218.062867.6639
63.28990.7284-1.18872.2240.06381.8404-0.14310.08310.1804-0.18470.13270.2388-0.096-0.217-0.01250.2460.0515-0.04870.399-0.02890.4561-46.1429-4.659373.4677
72.5953-0.9113-0.26132.57290.28712.7190.03830.11180.0274-0.3324-0.16890.23490.0989-0.4360.07290.29650.0022-0.04510.4254-0.09580.5174-46.6173-7.985574.0689
83.3895-0.7280.07542.3613-0.85063.0773-0.12540.5262-0.2635-0.74620.2251-0.14480.10170.3124-0.11190.6271-0.20660.08880.572-0.17690.5039-5.6796-7.172540.333
91.20741.05150.01431.14830.10631.6621-0.41190.4343-0.4271-0.84340.5985-0.51410.1420.3827-0.20120.7771-0.17530.18580.7523-0.24370.6568-2.9932-17.016839.1912
102.771-1.1160.41642.94941.06961.6260.024-0.3468-0.2518-0.15330.3397-1.1504-0.05270.8622-0.34380.5620.13920.06790.8075-0.19810.9308-0.6203-29.837851.4572
111.1913-0.0568-1.90931.24680.76954.0882-0.55380.0357-0.56130.17190.02440.24651.2777-0.19990.4550.5829-0.0230.09670.4113-0.04760.7005-38.4753-29.782270.2576
122.04090.6851.05853.0811.87212.6907-0.1404-0.1003-0.0352-0.10840.00920.24940.0916-0.19240.11310.2817-0.0469-0.02320.3741-0.11990.4347-19.468-16.064659.0531
130.7353-0.81270.8881.0195-1.02711.14370.55950.27391.0822-0.79690.10991.2019-1.9858-1.5341-0.53312.08960.1601-0.28421.54660.52681.7306-24.707727.165130.1218
141.00290.1449-0.42050.92680.43751.1688-0.14870.4877-0.2775-0.93610.10460.6984-0.3304-0.32080.1610.922-0.1973-0.22960.90780.20731.0584-26.51313.068546.2683
155.63761.8122-0.46244.2673-0.19274.5411-0.15330.0555-1.0875-1.94730.06751.0191.2867-0.9477-0.02741.315-0.3833-0.08181.0038-0.06061.3353-44.6199-10.47451.909
163.41370.6578-0.04174.72861.03652.9965-0.01870.3901-0.2837-1.3972-0.3936-0.33930.4996-0.85610.26720.9705-0.2586-0.12361.01460.02670.8261-44.242-7.462351.0535
170.85661.3523-0.49712.3956-0.67440.3157-0.97280.80330.7277-1.73780.78250.8724-0.0772-0.15280.23941.251-0.3188-0.05660.90230.35421.2149-23.78217.10843.6034
180.93590.2755-0.30180.681-0.66060.6164-0.04830.7516-0.2193-0.49590.12280.25680.3963-0.4898-0.06351.82940.0297-0.21051.2979-0.1530.7614-28.6465-57.2768-15.732
191.45120.1013-0.42522.08040.15653.10280.33940.56780.2377-0.7839-0.2050.3245-0.2436-0.2966-0.0761.15280.1778-0.03680.75470.01550.5552-26.1171-42.79841.9998
201.55660.3755-1.65342.5502-0.67033.79810.09820.11070.2044-0.380.03560.0117-0.25410.0361-0.1140.4891-0.0485-0.01430.3125-0.11680.4287-24.3841-44.204131.86
211.8820.03790.20861.3629-1.20041.5099-0.005-0.2533-0.2753-0.28640.19140.16690.0267-0.2622-0.18850.2862-0.0821-0.07640.54640.01420.428-39.5546-67.456651.7294
222.55760.59120.11712.4975-0.29882.3987-0.0936-0.0495-0.2718-0.19190.1020.24740.1459-0.2942-0.00010.2782-0.0317-0.04160.4291-0.02330.4444-37.0494-66.292449.9339
232.5721-0.41170.19973.3261-1.17682.25560.14430.1378-0.2212-0.63-0.1814-0.54060.37180.9332-0.0440.86890.18620.22010.7755-0.00040.5578-3.124-59.150912.0706
240.7957-0.5985-0.13471.6336-0.46591.510.20860.1252-0.2402-0.6466-0.4073-0.44520.73350.96360.05960.92960.35050.24741.17710.10040.70846.4604-67.777217.7917
250.89580.1604-0.36830.6804-0.6980.56940.00610.2880.0455-0.3209-0.1034-0.39590.13110.56-0.03880.47520.02460.15371.03550.0550.69051.718-67.848742.3427
261.9721-0.8146-0.92212.3223-0.90023.6380.0456-0.0061-0.3657-0.3635-0.2947-0.20250.28350.20690.19560.28090.0013-0.07080.479-0.06170.4569-12.7593-74.922350.1818
272.8612-1.72090.47845.12980.51962.253-0.1415-0.2256-0.24820.0871-0.13810.24210.20630.45970.24570.48510.06180.0770.5963-0.01690.3475-9.6026-63.59733.3444
283.26841.17062.22571.1050.072.34650.56470.29680.15260.3079-0.68021.7241-0.2107-0.90280.03141.52140.1442-0.34251.4616-0.26751.3009-39.3413-55.5265-6.3525
292.03010.4531-0.3312.4991-0.65981.62420.42150.037-0.1851-0.8677-0.1160.90051.06-0.2144-0.52711.2848-0.1971-0.09240.85450.00120.7543-32.3584-57.517113.8812
303.96781.6151-0.7926.4892-1.58675.52930.5797-0.2535-2.1416-0.1855-0.9576-1.22681.2524-0.27570.23981.2888-0.064-0.02191.03560.18271.5777-30.6473-79.761433.8775
312.4461-0.256-0.76972.8147-0.12643.1092-0.31410.5862-1.5909-1.6242-0.4007-1.12081.42620.59420.43351.1684-0.02640.21510.6754-0.05171.0205-32.2024-78.202231.7377
321.6034-1.50391.2483.8428-1.94613.82620.38210.8566-0.7404-1.0098-0.64650.95870.77260.43470.34251.7851-0.1346-0.1951.20210.04770.9944-33.5857-60.519712.0993
330.1922-0.3484-0.4910.79531.16672.50540.25220.7214-0.0301-1.0861-0.17620.443-0.39990.7366-0.02821.36210.2801-0.021.18670.11850.6058-31.2744-45.71883.8231
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 0 THROUGH 27 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 28 THROUGH 83 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 84 THROUGH 269 )
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESID 270 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 90 )
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESID 91 THROUGH 174 )
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESID 175 THROUGH 244 )
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESID 245 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 725 )
16X-RAY DIFFRACTION16CHAIN 'P' AND (RESID 803 THROUGH 812 )
17X-RAY DIFFRACTION17CHAIN 'P' AND (RESID 813 THROUGH 822 )
18X-RAY DIFFRACTION18CHAIN 'C' AND (RESID 0 THROUGH 83 )
19X-RAY DIFFRACTION19CHAIN 'C' AND (RESID 84 THROUGH 325 )
20X-RAY DIFFRACTION20CHAIN 'C' AND (RESID 326 THROUGH 421 )
21X-RAY DIFFRACTION21CHAIN 'C' AND (RESID 422 THROUGH 473 )
22X-RAY DIFFRACTION22CHAIN 'C' AND (RESID 474 THROUGH 554 )
23X-RAY DIFFRACTION23CHAIN 'D' AND (RESID 4 THROUGH 83 )
24X-RAY DIFFRACTION24CHAIN 'D' AND (RESID 84 THROUGH 194 )
25X-RAY DIFFRACTION25CHAIN 'D' AND (RESID 195 THROUGH 269 )
26X-RAY DIFFRACTION26CHAIN 'D' AND (RESID 270 THROUGH 363 )
27X-RAY DIFFRACTION27CHAIN 'D' AND (RESID 364 THROUGH 428 )
28X-RAY DIFFRACTION28CHAIN 'E' AND (RESID 702 THROUGH 706 )
29X-RAY DIFFRACTION29CHAIN 'E' AND (RESID 707 THROUGH 716 )
30X-RAY DIFFRACTION30CHAIN 'E' AND (RESID 717 THROUGH 725 )
31X-RAY DIFFRACTION31CHAIN 'F' AND (RESID 803 THROUGH 812 )
32X-RAY DIFFRACTION32CHAIN 'F' AND (RESID 813 THROUGH 818 )
33X-RAY DIFFRACTION33CHAIN 'F' AND (RESID 819 THROUGH 822 )

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