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- PDB-5txp: STRUCTURE OF Q151M complex (A62V, V75I, F77L, F116Y, Q151M) mutan... -

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Basic information

Entry
Database: PDB / ID: 5txp
TitleSTRUCTURE OF Q151M complex (A62V, V75I, F77L, F116Y, Q151M) mutant HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WITH A DOUBLE STRANDED DNA AND AN INCOMING DDATP
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. DNA polymerase / 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 / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus ...HIV-1 retropepsin / 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 / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / symbiont-mediated suppression of host gene expression / 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 / 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. / 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 / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Ribonuclease H superfamily / 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: 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_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _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 P51 SUBUNIT
B: HIV-1 REVERSE TRANSCRIPTASE P61 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 P51 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P61 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)260,00221
Polymers257,9258
Non-polymers2,07713
Water1,820101
1
A: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
B: HIV-1 REVERSE TRANSCRIPTASE P61 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)130,04911
Polymers128,9634
Non-polymers1,0867
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15710 Å2
ΔGint-90 kcal/mol
Surface area47890 Å2
MethodPISA
2
C: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P61 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)129,95310
Polymers128,9634
Non-polymers9906
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15420 Å2
ΔGint-66 kcal/mol
Surface area48510 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.945, 133.273, 139.062
Angle α, β, γ (deg.)90.00, 97.59, 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 P51 SUBUNIT / Pr160Gag-Pol


Mass: 64049.539 Da / Num. of mol.: 2
Mutation: A62V, V75I, F77L, F116Y, 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 P61 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, 112 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-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.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 101 / 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: 3.2 Å3/Da / Density % sol: 61.6 %
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: 0.9179 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 9, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9179 Å / Relative weight: 1
ReflectionResolution: 2.7→40 Å / Num. obs: 89232 / % possible obs: 99.4 % / Observed criterion σ(I): -1 / Redundancy: 3.9 % / Net I/σ(I): 8.8
Reflection shellResolution: 2.7→2.75 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.687 / Mean I/σ(I) obs: 1.4 / % possible all: 97.8

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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→37.618 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 26.84
RfactorNum. reflection% reflectionSelection details
Rfree0.2388 1788 2 %Random
Rwork0.1961 ---
obs0.197 89184 99.24 %-
Solvent computationShrinkage radii: 1 Å / VDW probe radii: 1.2 Å
Refinement stepCycle: LAST / Resolution: 2.7→37.618 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15828 1802 129 101 17860
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00618422
X-RAY DIFFRACTIONf_angle_d0.74825380
X-RAY DIFFRACTIONf_dihedral_angle_d15.54410744
X-RAY DIFFRACTIONf_chiral_restr0.0532772
X-RAY DIFFRACTIONf_plane_restr0.0062870
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6937-2.76650.4031220.34786499X-RAY DIFFRACTION96
2.7665-2.84790.40481160.31916661X-RAY DIFFRACTION99
2.8479-2.93970.32381440.29556687X-RAY DIFFRACTION99
2.9397-3.04480.30021490.27016690X-RAY DIFFRACTION99
3.0448-3.16660.29411490.25916705X-RAY DIFFRACTION99
3.1666-3.31060.29281660.23626712X-RAY DIFFRACTION100
3.3106-3.48510.27261430.21836735X-RAY DIFFRACTION100
3.4851-3.70320.27841340.20036736X-RAY DIFFRACTION100
3.7032-3.98890.22271210.18736775X-RAY DIFFRACTION100
3.9889-4.38980.21871270.16236769X-RAY DIFFRACTION100
4.3898-5.02370.1961400.15176819X-RAY DIFFRACTION100
5.0237-6.32440.21441330.1826795X-RAY DIFFRACTION100
6.3244-37.62180.1871440.16396813X-RAY DIFFRACTION99
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)
10.0022-0.01170.00780.04040.01810.00810.10330.18870.2033-0.23150.17340.1471-0.1372-0.09140.09671.5761-0.4791-0.17380.97020.35130.5454-14.525624.190120.7105
20.11620.0647-0.04050.1003-0.06050.01980.15820.02110.2936-0.1453-0.09380.04580.0346-0.0483-0.01730.9349-0.5840.03090.4520.17480.3432-8.76220.772529.2391
30.1555-0.1513-0.12210.18860.11460.11630.24390.02740.4841-0.33760.2501-0.3712-0.08010.25760.19061.1301-0.48740.19590.71110.07310.75183.590721.622937.2364
40.0944-0.00130.03430.0315-0.08310.34880.0093-0.06070.159-0.17790.1770.0306-0.4755-0.03590.00370.7925-0.03090.02990.3040.04930.9413-20.818726.782656.8365
50.1029-0.0118-0.08580.16120.08730.09250.1398-0.09920.04920.04990.02690.1547-0.21520.21970.15820.1491-0.2853-0.14950.0872-0.3730.3581-17.2578.017967.6889
60.0953-0.0465-0.15680.20260.15150.2161-0.1626-0.18280.18040.00180.18760.1698-0.1542-0.12-0.00910.13540.0647-0.03620.3642-0.0020.3962-45.7467-4.698973.5082
70.0567-0.035-0.01360.0139-0.00030.05780.04030.12330.0312-0.2535-0.05210.06210.028-0.3-00.36720.0053-0.08010.3776-0.07370.5509-46.2346-8.018374.1481
80.1326-0.1340.06660.3487-0.05310.11630.13820.11030.0321-0.4680.2022-0.16-0.05290.39540.19910.4372-0.30420.04880.4764-0.23970.3572-5.3727-7.161240.3882
90.40160.05060.07370.1073-0.01770.0076-0.24810.1353-0.4301-0.36110.5445-0.3458-0.16080.65520.11830.6116-0.05420.12880.5933-0.28710.6297-1.1908-21.431842.4148
100.02210.016-0.03050.04120.0085-0.0191-0.0343-0.003-0.1014-0.00220.1037-0.0191-0.0240.2184-00.36160.0210.07890.5089-0.06230.6135-22.0659-26.659265.4317
110.1174-0.1746-0.12210.23550.05930.1431-0.3311-0.0796-0.21660.0830.0945-0.06270.40440.1129-0.13090.299-0.07180.02550.1917-0.16720.4033-31.2937-26.742965.8971
120.09180.03760.00180.10050.05830.031-0.2284-0.1690.0872-0.1054-0.06530.31310.1112-0.161-0.31010.0112-0.3766-0.26330.0015-0.44230.3425-17.9904-13.905657.2997
130.00150.00290.0010.00340.00170.00180.0349-0.0146-0.01120.0158-0.0087-0.0133-0.0167-0.067401.2926-0.0131-0.13380.89810.20180.9942-24.433627.179230.261
140.00140.00130.00180.0030.00020.0015-0.01580.00010.0542-0.06670.03190.0523-0.05340.002-00.9638-0.2894-0.07130.8320.19590.8236-17.818515.158344.4559
150.0128-0.0089-0.00370.00470.00620.0141-0.17660.0931-0.0154-0.0935-0.10130.03280.31240.0432-01.1546-0.2399-0.03570.9660.08511.1803-36.29311.644549.1806
160.00340.0043-0.00180.0017-0.0020.0027-0.018-0.0192-0.0375-0.013-0.0685-0.0084-0.02980.0091-01.0395-0.4758-0.23961.42540.00961.3727-52.221-14.668954.971
170.0115-0.01340.00450.0114-0.00890.01970.128-0.00210.1906-0.1982-0.0234-0.1775-0.0405-0.004300.6647-0.2191-0.14660.87010.01640.7622-43.769-7.478251.2333
180.006-0.0045-0.0040.0042-0.00580.0036-0.30870.03050.1717-0.0926-0.19550.0574-0.0990.056501.5319-0.2721-0.13161.23340.37141.3336-28.453112.634443.5555
190.0052-0.0013-0.00110.0042-0.00270.0013-0.06390.02560.0049-0.0227-0.04230.0286-0.0480.0198-01.1558-0.31980.03080.98410.24891.1493-15.684424.131143.9702
200.40980.28950.00050.3879-0.05710.29850.43110.42590.3592-0.4909-0.23030.2749-0.1264-0.19320.15171.2650.2084-0.02630.79980.01740.3705-26.605-46.3083-2.6022
210.0753-0.0555-0.11030.15070.0170.10730.05270.01710.0649-0.3114-0.00280.0171-0.0196-0.01730.07210.498-0.0655-0.00320.2465-0.10810.4006-24.1176-44.079831.8548
220.10950.12060.01070.34930.10260.224-0.0801-0.2555-0.104-0.16220.11590.0416-0.0787-0.21570.00990.2268-0.0404-0.06410.43760.01740.3833-37.6794-66.624350.5936
230.04080.0230.01420.09990.05530.03360.13310.02150.0886-0.2167-0.0816-0.04790.14690.20410.03210.83940.17010.25040.4636-0.00280.4098-3.6151-59.29428.3976
240.0245-0.0039-0.02340.00720.00340.02270.0541-0.05280.0076-0.1422-0.0059-0.06350.0430.204400.73180.17390.15410.78260.03450.63310.1678-66.021219.4913
250.09680.00840.00850.32740.12840.232-0.117-0.0765-0.1772-0.481-0.032-0.30810.13220.5456-0.20260.60270.42480.33831.09580.1590.5047.1917-65.833617.4619
260.04070.02620.09110.12850.01670.08940.16690.09940.0775-0.1354-0.0767-0.16280.08260.15550.01410.31630.1040.14720.65420.07250.46551.9894-67.705142.2468
270.0625-0.07610.10870.1028-0.13460.11130.0544-0.055-0.2453-0.134-0.2005-0.0392-0.0167-0.041-0.00010.30980.0388-0.01540.41550.00720.498-12.497-74.828950.1773
280.0182-0.0029-0.01690.0524-0.00730.045-0.0609-0.0741-0.1308-0.1385-0.17670.01670.10520.334100.40840.04570.02180.4925-0.01980.4211-9.3816-63.383533.2111
290.0033-0.003-0.00190.00340.00320.00240.0304-0.01590.01650.07310.0233-0.00050.01560.0231-01.20290.0347-0.10541.0926-0.22220.8736-39.3454-55.4858-6.2463
300.00170-0.00780.00510.01430.00910.30760.0363-0.0809-0.2090.03630.14380.03650.029301.3023-0.2043-0.06440.92970.01370.718-32.2118-57.467813.9075
310.0006-0.0046-0.00510.00810.01090.00820.1001-0.0031-0.1496-0.0469-0.0584-0.02490.0219-0.0074-01.2683-0.14140.00031.05820.17521.4395-30.4145-79.733433.8365
320.0018-0.0049-0.01510.00890.02690.032-0.04420.225-0.1013-0.1234-0.0346-0.04820.01750.0525-00.7822-0.10580.10520.4082-0.09960.627-31.961-78.137431.7052
330.0027-0.0081-0.00980.01070.01650.01550.12910.13-0.0232-0.2176-0.08330.1117-0.0597-0.062501.5631-0.0003-0.16941.24610.12040.8031-32.6211-54.80978.9571
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 83 )
2X-RAY DIFFRACTION2chain 'A' and (resid 84 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 90 )
9X-RAY DIFFRACTION9chain 'B' and (resid 91 through 210 )
10X-RAY DIFFRACTION10chain 'B' and (resid 211 through 269 )
11X-RAY DIFFRACTION11chain 'B' and (resid 270 through 363 )
12X-RAY DIFFRACTION12chain 'B' and (resid 364 through 428 )
13X-RAY DIFFRACTION13chain 'T' and (resid 702 through 706 )
14X-RAY DIFFRACTION14chain 'T' and (resid 707 through 711 )
15X-RAY DIFFRACTION15chain 'T' and (resid 712 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 818 )
19X-RAY DIFFRACTION19chain 'P' and (resid 819 through 822 )
20X-RAY DIFFRACTION20chain 'C' and (resid -1 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 822 )

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