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

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Basic information

Entry
Database: PDB / ID: 5txo
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 DATP
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. 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 / 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 / structural molecule activity / host cell plasma membrane / virion membrane / 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'-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: 2.546 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.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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 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)260,00620
Polymers257,9258
Non-polymers2,08012
Water3,045169
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)130,00310
Polymers128,9634
Non-polymers1,0406
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15380 Å2
ΔGint-89 kcal/mol
Surface area47950 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)130,00310
Polymers128,9634
Non-polymers1,0406
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14940 Å2
ΔGint-92 kcal/mol
Surface area48620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.990, 132.930, 139.120
Angle α, β, γ (deg.)90.00, 97.38, 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: 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 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, 179 molecules

#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: Mg
#7: Chemical ChemComp-DTP / 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE / Deoxyadenosine triphosphate


Mass: 491.182 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C10H16N5O12P3
#8: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


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


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 169 / 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: 3.25 Å3/Da / Density % sol: 62.12 %
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: 0.9181 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Jun 2, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9181 Å / Relative weight: 1
ReflectionResolution: 2.546→50 Å / Num. obs: 104998 / % possible obs: 99.2 % / Observed criterion σ(I): -1 / Redundancy: 3.9 % / Rmerge(I) obs: 0.091 / Net I/σ(I): 9.3
Reflection shellResolution: 2.546→2.59 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.649 / Mean I/σ(I) obs: 1.77 / CC1/2: 0.431 / % possible all: 99

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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: 2.546→45.989 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 24.51
RfactorNum. reflection% reflectionSelection details
Rfree0.2278 3135 2.99 %Random
Rwork0.191 ---
obs0.192 104909 98.81 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.546→45.989 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15829 1802 128 169 17928
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00718425
X-RAY DIFFRACTIONf_angle_d0.95625387
X-RAY DIFFRACTIONf_dihedral_angle_d19.93414603
X-RAY DIFFRACTIONf_chiral_restr0.062774
X-RAY DIFFRACTIONf_plane_restr0.0082870
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5463-2.58610.38031420.33184257X-RAY DIFFRACTION92
2.5861-2.62850.29841350.32084650X-RAY DIFFRACTION99
2.6285-2.67380.32651380.30764600X-RAY DIFFRACTION99
2.6738-2.72240.3241400.3024674X-RAY DIFFRACTION99
2.7224-2.77470.30841400.28894581X-RAY DIFFRACTION99
2.7747-2.83140.32981420.27854665X-RAY DIFFRACTION99
2.8314-2.89290.29071530.26824617X-RAY DIFFRACTION99
2.8929-2.96020.29071530.25924641X-RAY DIFFRACTION100
2.9602-3.03420.28931390.24114645X-RAY DIFFRACTION100
3.0342-3.11630.25551360.2274642X-RAY DIFFRACTION100
3.1163-3.20790.22871590.2164661X-RAY DIFFRACTION100
3.2079-3.31140.28321540.22224655X-RAY DIFFRACTION100
3.3114-3.42980.23261340.20884680X-RAY DIFFRACTION100
3.4298-3.5670.23711330.1944677X-RAY DIFFRACTION100
3.567-3.72930.23271580.18474660X-RAY DIFFRACTION100
3.7293-3.92580.20321380.17464692X-RAY DIFFRACTION100
3.9258-4.17160.21291370.16084675X-RAY DIFFRACTION100
4.1716-4.49350.16651390.15134692X-RAY DIFFRACTION100
4.4935-4.94520.20411440.14984673X-RAY DIFFRACTION100
4.9452-5.65970.19081280.15964714X-RAY DIFFRACTION100
5.6597-7.12630.22761600.17984694X-RAY DIFFRACTION100
7.1263-45.99670.17641330.14884329X-RAY DIFFRACTION90
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)
10.63470.02520.15190.6654-0.08930.22510.18780.170.3124-0.97530.21090.3580.2895-0.8143-0.3421.5877-0.3687-0.17471.38410.20910.7915-13.597316.08518.8955
20.820.18560.230.7197-0.52490.54950.08370.86260.3602-0.81440.07250.4001-0.60660.2044-0.11282.2978-0.4473-0.24791.70250.60331.3353-12.346528.851716.2932
30.25980.1487-0.01551.425-0.08351.543-0.13480.68730.4141-0.83340.45790.1725-0.61330.1884-0.27591.2137-0.4201-0.09260.98730.09510.8148-10.500121.502836.2061
40.82720.45360.05470.25630.0291-0.0028-0.26120.67580.6203-1.06070.2490.68050.3176-0.5117-0.00471.8918-0.4029-0.24711.33080.42960.9438-11.894222.812118.7704
51.44470.3958-0.222.50030.15142.2078-0.09010.40930.7056-0.43350.3373-0.0453-0.53950.1601-0.22071.005-0.28770.00790.58440.04690.8352-8.013124.369746.8156
61.45951.1051-0.65151.321-0.57981.7472-0.0166-0.18910.48630.01620.10960.0839-0.7710.0741-0.05050.694-0.06560.00350.4338-0.16690.7644-17.037719.022365.0537
71.73340.2101-1.39271.7234-0.05911.5136-0.02720.0116-0.02670.16940.1190.0115-0.26690.1345-0.08030.3841-0.0895-0.0650.4095-0.16090.4402-16.43293.762768.9538
82.90260.9697-1.12961.9559-0.24881.7214-0.1310.00760.1093-0.17730.16230.2172-0.0544-0.2436-0.02680.30830.0498-0.04230.4436-0.02930.5005-45.581-4.962473.5811
92.6694-0.54310.06512.54780.34882.370.08840.10850.0328-0.2214-0.12020.23470.1188-0.385-0.02210.2833-0.0127-0.0350.421-0.11290.5181-46.0471-8.276374.1989
102.2367-0.445-0.02782.2513-0.55242.0965-0.08640.34320.0514-0.61850.1937-0.1656-0.01520.414-0.10650.6596-0.20540.0530.6614-0.18170.5224-4.2602-6.03541.086
111.19620.8008-0.13013.08090.05021.2725-0.3330.3797-0.5198-0.78440.5448-0.4650.24720.4228-0.2640.7764-0.10960.16180.7448-0.2780.7366-3.5188-19.984240.4498
120.5231-0.5983-1.14031.79781.24912.3228-0.4989-0.2177-0.4350.15830.1863-0.05790.70150.41140.36710.54990.103-0.00630.53480.00170.6664-25.2334-29.754264.7573
132.25010.56760.87563.18141.94842.3102-0.1662-0.04670.019-0.13350.05940.17090.1282-0.10420.10310.3047-0.0436-0.02860.3893-0.13970.4673-18.9424-16.319259.1632
141.1633-0.61750.91480.3868-0.46940.75210.30230.28941.1564-0.7285-0.0111.2881-1.6012-1.3693-0.15512.05070.1747-0.40751.45050.41211.8082-24.465127.046630.3665
151.2761-0.0725-0.39041.110.51081.7844-0.11070.2764-0.0456-0.86990.12130.633-0.4763-0.47150.13440.9189-0.1966-0.14840.90010.21181.1251-26.134412.861646.4591
165.82992.3635-0.56154.6292-0.5414.0908-0.0199-0.2875-0.912-1.9398-0.31490.84751.1934-0.93790.24921.3366-0.3923-0.13831.0979-0.09031.3804-44.1707-10.644552.0657
172.95560.4236-0.25164.60020.97842.18590.2110.255-0.3175-1.4952-0.3151-0.38850.2401-0.75060.09880.9572-0.219-0.14410.98670.02180.7766-43.7727-7.667351.2011
180.68181.3243-0.33052.8775-0.47570.1911-1.09020.79040.6796-1.79620.90940.6614-0.1212-0.01590.26031.1594-0.3382-0.06310.86510.29891.1401-23.442816.915643.784
191.49730.1656-0.50431.62720.1463.39450.29530.70070.1419-0.7188-0.18650.36280.027-0.5099-0.11771.23570.1543-0.06430.87930.00410.5954-26.575-46.4418-2.5673
201.61740.5826-0.75571.7685-1.12492.2421-0.0216-0.1236-0.0275-0.27450.07430.0573-0.1129-0.0973-0.05770.3655-0.0208-0.05220.3843-0.09820.419-31.4731-56.829542.3796
212.6888-0.27970.31953.1425-0.89832.20620.20890.1112-0.0547-0.6556-0.2754-0.43940.23280.8327-0.01250.85990.17960.22660.79240.01940.5646-2.8272-59.104411.9537
220.6732-0.55920.07641.7352-0.51931.29280.17710.0655-0.3408-0.5415-0.3871-0.48240.59581.05660.04390.95470.36570.27161.26490.13130.79816.7454-67.721317.5636
230.87650.3375-0.15050.4185-0.57330.84730.05540.50940.0132-0.2841-0.088-0.38010.0370.4173-0.08990.55740.06190.15151.06650.09680.81032.185-67.843642.1279
241.7052-0.7347-0.46792.2752-1.29563.52960.07870.0057-0.4009-0.3792-0.3504-0.24670.40710.28150.19790.29810.0171-0.06030.4565-0.04110.474-12.2583-74.960750.1491
252.3019-1.54690.21724.37320.24122.3335-0.1133-0.2041-0.2019-0.0231-0.21060.06490.18450.61010.24150.53740.03980.04620.6816-0.00250.4771-9.1486-63.569933.2658
264.05830.04651.54891.0973-0.14341.36780.43740.53490.05790.3268-0.55561.4876-0.0774-0.81080.14421.55390.1282-0.30821.6797-0.30811.3242-39.1735-55.4504-6.3041
270.9346-0.22970.10421.73680.05840.81590.40440.095-0.2886-0.697-0.20920.6451.1897-0.3657-0.18131.3456-0.1738-0.05670.92490.01370.7652-32.0509-57.507213.8783
283.56051.4758-0.7595.8472-1.19125.13080.1969-0.1953-2.2665-0.3887-0.5109-0.82881.5979-0.22130.08651.3787-0.1388-0.00971.08380.14881.5548-30.2346-79.786533.7268
290.27970.09010.23791.6811-0.33811.4427-0.00160.378-0.98070.0103-0.3218-0.70971.02750.61250.1671.93860.06030.32891.1515-0.2532.0556-31.1867-87.402632.723
300.4345-0.83130.82831.8211-1.9183.1889-0.1770.7185-0.0746-1.7675-0.12280.2980.87810.14080.17331.3731-0.1682-0.07180.86690.02720.695-32.8944-64.398920.1936
310.5682-0.7492-0.34541.15460.95951.79020.06330.2578-0.025-1.06940.1390.4116-0.27860.2109-0.15481.45360.1913-0.01051.14010.10140.7177-31.0631-45.68823.8837
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 59 )
3X-RAY DIFFRACTION3chain 'A' and (resid 60 through 110 )
4X-RAY DIFFRACTION4chain 'A' and (resid 111 through 155 )
5X-RAY DIFFRACTION5chain 'A' and (resid 156 through 296 )
6X-RAY DIFFRACTION6chain 'A' and (resid 297 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 83 )
11X-RAY DIFFRACTION11chain 'B' and (resid 84 through 194 )
12X-RAY DIFFRACTION12chain 'B' and (resid 195 through 325 )
13X-RAY DIFFRACTION13chain 'B' and (resid 326 through 428 )
14X-RAY DIFFRACTION14chain 'T' and (resid 702 through 706 )
15X-RAY DIFFRACTION15chain 'T' and (resid 707 through 716 )
16X-RAY DIFFRACTION16chain 'T' and (resid 717 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 325 )
20X-RAY DIFFRACTION20chain 'C' and (resid 326 through 554 )
21X-RAY DIFFRACTION21chain 'D' and (resid 4 through 83 )
22X-RAY DIFFRACTION22chain 'D' and (resid 84 through 194 )
23X-RAY DIFFRACTION23chain 'D' and (resid 195 through 269 )
24X-RAY DIFFRACTION24chain 'D' and (resid 270 through 363 )
25X-RAY DIFFRACTION25chain 'D' and (resid 364 through 428 )
26X-RAY DIFFRACTION26chain 'E' and (resid 702 through 706 )
27X-RAY DIFFRACTION27chain 'E' and (resid 707 through 716 )
28X-RAY DIFFRACTION28chain 'E' and (resid 717 through 725 )
29X-RAY DIFFRACTION29chain 'F' and (resid 803 through 807 )
30X-RAY DIFFRACTION30chain 'F' and (resid 808 through 818 )
31X-RAY DIFFRACTION31chain 'F' and (resid 819 through 822 )

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