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- PDB-6bhj: Structure of HIV-1 Reverse Transcriptase Bound to a 38-mer Hairpi... -

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Basic information

Entry
Database: PDB / ID: 6bhj
TitleStructure of HIV-1 Reverse Transcriptase Bound to a 38-mer Hairpin Template-Primer RNA-DNA Aptamer
Components
  • (HIV-1 REVERSE TRANSCRIPTASE ...Reverse transcriptase) x 2
  • 38-MER RNA-DNA Aptamer
KeywordsTRANSFERASE/DNA / Human immunodeficiency virus 1 / RNA-directed DNA polymerase / Protein/RNA/DNA / Aptamer / TRANSFERASE / 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 / DNA/RNA hybrid / DNA/RNA hybrid (> 10) / Pol protein / Gag-Pol polyprotein
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.81 Å
AuthorsRuiz, F.X. / Miller, M.T. / Tuske, S. / Das, K. / Arnold, E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)NIGMS P50 GM103368 United States
CitationJournal: Curr Res Struct Biol / Year: 2020
Title: Integrative Structural Biology Studies of HIV-1 Reverse Transcriptase Binding to a High-Affinity DNA Aptamer
Authors: Tuske, S. / Zheng, J. / Olson, E.D. / Ruiz, F.X. / Pascal, B.D. / Bauman, J.D. / Das, K. / DeStefano, J.J. / Musier-Forsyth, K. / Griffin, P.R. / Arnold, E.
History
DepositionOct 30, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 31, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 20, 2019Group: Advisory / Author supporting evidence ...Advisory / Author supporting evidence / Data collection / Derived calculations
Category: pdbx_audit_support / pdbx_validate_close_contact ...pdbx_audit_support / pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_conn / struct_conn_type
Item: _pdbx_audit_support.funding_organization
Revision 1.2Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Jul 8, 2020Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
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.pdbx_synonyms / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_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
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
C: HIV-1 REVERSE TRANSCRIPTASE P66 subunit
D: HIV-1 REVERSE TRANSCRIPTASE P51 subunit
E: 38-MER RNA-DNA Aptamer
F: 38-MER RNA-DNA Aptamer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)257,30217
Polymers255,9216
Non-polymers1,38211
Water2,000111
1
A: HIV-1 REVERSE TRANSCRIPTASE P66 subunit
B: HIV-1 REVERSE TRANSCRIPTASE P51 subunit
E: 38-MER RNA-DNA Aptamer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,6959
Polymers127,9603
Non-polymers7356
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11950 Å2
ΔGint-62 kcal/mol
Surface area47590 Å2
MethodPISA
2
C: HIV-1 REVERSE TRANSCRIPTASE P66 subunit
D: HIV-1 REVERSE TRANSCRIPTASE P51 subunit
F: 38-MER RNA-DNA Aptamer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,6078
Polymers127,9603
Non-polymers6475
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11250 Å2
ΔGint-74 kcal/mol
Surface area48080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.055, 127.463, 132.125
Angle α, β, γ (deg.)90.00, 101.81, 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


Mass: 64135.402 Da / Num. of mol.: 2 / Mutation: C280S, D498N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: pol / Production host: Escherichia coli (E. coli) / References: UniProt: A0A076Q3N8, UniProt: P03366*PLUS
#2: Protein HIV-1 REVERSE TRANSCRIPTASE P51 subunit


Mass: 51928.629 Da / Num. of mol.: 2 / Mutation: C280S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: pol / Production host: Escherichia coli (E. coli) / References: UniProt: A0A076Q3N8, UniProt: P03366*PLUS

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DNA/RNA hybrid / Sugars , 2 types, 4 molecules EF

#3: DNA/RNA hybrid 38-MER RNA-DNA Aptamer


Mass: 11896.259 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: 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 , 4 types, 120 molecules

#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


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


Mass: 18.015 Da / Num. of mol.: 111 / 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: 3.02 Å3/Da / Density % sol: 59.21 %
Crystal growTemperature: 278 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 10% PEG 8000, 25 mM BisTris-Propane pH 6.8, 75 mM BisTris-Propane pH 7.4, 50 mM Ammonium Sulfate, 5% glycerol, 5% sucrose

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 27, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 65782 / % possible obs: 93 % / Redundancy: 4.1 % / CC1/2: 0.877 / Rmerge(I) obs: 0.094 / Rpim(I) all: 0.05 / Rrim(I) all: 0.107 / Net I/σ(I): 12.6
Reflection shellResolution: 2.8→2.85 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.624 / Mean I/σ(I) obs: 1.64 / Num. unique obs: 6113 / CC1/2: 0.461 / Rpim(I) all: 0.391 / Rrim(I) all: 0.742 / % possible all: 90

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
HKL-2000data processing
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5D3G

5d3g


Resolution: 2.81→47.692 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 26.65 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2444 2679 4.07 %
Rwork0.2031 --
obs0.2048 65760 92.39 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.81→47.692 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15846 1452 89 111 17498
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.03818065
X-RAY DIFFRACTIONf_angle_d1.08624735
X-RAY DIFFRACTIONf_dihedral_angle_d16.6556939
X-RAY DIFFRACTIONf_chiral_restr0.0782720
X-RAY DIFFRACTIONf_plane_restr0.0042851
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.81-2.86110.35851240.33092921X-RAY DIFFRACTION83
2.8611-2.91620.33451380.32743256X-RAY DIFFRACTION91
2.9162-2.97570.39691300.29863079X-RAY DIFFRACTION86
2.9757-3.04040.30851410.29723288X-RAY DIFFRACTION92
3.0404-3.11110.30871460.28753447X-RAY DIFFRACTION96
3.1111-3.18890.33971450.27673444X-RAY DIFFRACTION96
3.1889-3.27510.31741440.25263389X-RAY DIFFRACTION95
3.2751-3.37140.25371430.22893399X-RAY DIFFRACTION95
3.3714-3.48020.23951450.21073408X-RAY DIFFRACTION94
3.4802-3.60450.24651410.20493286X-RAY DIFFRACTION91
3.6045-3.74880.22961350.20023161X-RAY DIFFRACTION88
3.7488-3.91940.22871470.18433448X-RAY DIFFRACTION96
3.9194-4.12590.21951450.17483427X-RAY DIFFRACTION96
4.1259-4.38420.20531460.1693401X-RAY DIFFRACTION95
4.3842-4.72240.231390.16263318X-RAY DIFFRACTION92
4.7224-5.19720.21741380.17013263X-RAY DIFFRACTION91
5.1972-5.9480.241470.19633474X-RAY DIFFRACTION96
5.948-7.48920.24261390.20753261X-RAY DIFFRACTION90
7.4892-47.69880.21881460.18393411X-RAY DIFFRACTION93
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)
12.8821-1.0829-0.54676.04640.92360.3084-0.32610.23190.99020.99980.1396-1.5467-0.82750.22120.21371.40940.0316-0.3641.42070.13851.0305-22.368585.3723-14.841
29.9802-2.55173.02165.60241.77335.1665-0.6893-1.13491.52940.0728-0.4549-0.8468-0.2412-0.82351.09671.84410.1276-0.2961.202-0.0760.8715-22.908484.8699-8.3913
34.429-2.9359-3.76166.87890.73517.30930.1386-0.27850.50770.79670.0127-0.2634-0.8574-0.1143-0.0870.73570.01640.05130.5744-0.06530.6274-35.173880.6188-35.1637
44.3537-0.9861-0.78184.3995-2.46688.86240.5143-0.07290.86810.2807-0.28650.0856-1.3179-1.0258-0.19140.98870.24370.0710.6409-0.0210.6797-41.304184.7827-35.9562
54.33332.711-0.80035.026-2.74965.78140.4923-0.23581.8125-0.3433-0.4029-0.7687-0.49070.9378-0.0321.1653-0.14150.19221.2256-0.15051.5211-10.449588.2057-52.3895
65.2957-2.461-2.86765.12681.38895.22310.33260.30750.4509-0.4796-0.3159-0.5942-0.6336-0.058-0.00260.39540.04090.03070.39150.1640.5062-22.90169.6008-62.2422
75.997-0.9243-0.22035.55690.79835.5825-0.18240.1691-0.08250.29020.2741-0.09310.00920.3559-0.08920.2568-0.06960.09720.57880.02350.55357.538653.8433-67.7718
83.70360.2175-0.59534.56891.42994.5005-0.0461-0.7304-0.16920.54090.1410.1643-0.0101-0.5925-0.10860.41530.03820.09380.59410.11320.4515-34.50855.475-35.0015
95.05313.5879-3.40933.0678-2.1394.251-0.1797-0.8073-0.0280.27690.48570.1114-0.1343-0.4944-0.1820.65980.20790.13360.5339-0.01920.5243-35.513660.9439-30.758
102.9057-3.0313-2.7729.08466.10864.46-0.5624-0.1643-0.4371.49410.15820.27181.35040.25090.38380.9889-0.00660.36880.62150.20970.9937-33.460835.6523-35.283
114.73671.8260.04694.97741.18487.9948-0.36160.0962-0.60650.29790.07831.38830.4435-1.16850.3730.6397-0.07680.26770.78190.11751.1472-40.666433.163-40.7108
128.26522.0742-5.24516.4713-3.43368.2501-0.57690.0375-0.9789-0.39960.2834-0.05511.3048-0.0640.34840.5091-0.01520.1360.6287-0.02590.84270.376530.0569-66.5183
131.7292-1.05681.63785.1981-3.55024.9809-0.02260.0765-0.1149-0.0884-0.3029-0.18180.43220.48210.26440.29730.0230.06080.46890.06080.5418-19.744543.8044-51.9008
143.7482-1.27991.56034.83682.35852.65370.3519-0.9412-0.25931.32870.1834-1.41640.11030.32-0.53452.0644-0.3089-0.25391.2580.07331.118-13.9349-1.588520.1325
153.9386-4.539-1.42689.5558-2.99455.4983-0.5138-1.82360.1705-1.4980.1989-1.31280.27910.00270.31331.7395-0.1126-0.06291.75480.21671.1045-15.4059-6.362424.8063
161.3323.1205-1.4837.7607-3.64761.75720.2936-0.9553-0.11410.94460.0270.0477-0.87580.5991-0.25761.4727-0.16510.09751.3213-0.10420.6233-23.302915.19465.3003
171.91620.54050.06592.7636-3.32244.27980.2575-0.91350.63071.26950.09580.0977-1.38820.0683-0.33142.1323-0.34620.26161.3915-0.18630.7873-25.086121.71748.8136
189.6104-6.5967-5.46244.40173.69594.96750.0701-2.27880.21380.36881.131-1.64820.00361.4297-1.03951.3982-0.0437-0.32231.8299-0.02511.45922.659915.0356-11.4898
194.56240.9296-2.31176.05731.44277.19750.1457-0.28340.10610.7077-0.1046-0.1555-0.45840.2902-0.04770.5767-0.0059-0.00760.39840.10290.3599-17.487417.8052-25.5819
204.1909-0.43490.37154.95540.23165.0229-0.03630.0264-0.04490.23970.0318-0.2920.06390.22490.02180.21430.02640.03620.55710.05140.4666-4.0025-5.4322-47.302
212.63290.04510.23455.6429-1.87435.16670.1237-0.47090.26780.62940.00870.10650.1165-0.5569-0.13581.037-0.12690.38041.0351-0.05060.6348-38.96381.0207-8.398
224.94492.5874-3.29394.8876-5.21916.48920.4702-0.02950.16412.1991-0.09790.8085-0.372-1.0946-0.34941.4512-0.19280.35041.0809-0.11450.5868-37.08971.8559-1.6329
231.8034-0.62341.70411.80992.88732.02640.5595-0.2686-0.32780.8660.1790.73041.4029-0.9924-0.12171.1216-0.53330.4762.1259-0.1221.071-50.9282-10.999-19.107
244.66410.68781.22563.3428-2.78765.00970.1582-0.25650.670.3345-0.06730.912-0.1139-1.3277-0.09030.8464-0.04270.41141.8228-0.23341.1869-57.1087-5.3198-23.2959
256.04553.0615-1.86057.4082-2.62177.49890.1719-0.0205-0.03710.25720.04930.39960.17030.0093-0.23370.24780.05050.05950.5098-0.01340.4752-24.3515-14.4863-57.6791
267.69562.5069-1.06858.57972.24498.1393-0.04840.1098-0.13330.2812-0.22650.19040.0842-0.91380.17870.3351-0.01240.07850.66770.06810.4229-33.5873-4.0814-32.1877
271.73010.96822.05952.5445-1.3176.27581.1825-0.9168-1.46631.07090.9832-1.8755-0.9022-0.7862-2.24213.18710.43730.07862.28870.21222.2014-9.3569-0.1487-5.719
284.4115.4094-3.07966.7089-4.55629.44521.62632.1047-3.1223-2.66570.2104-1.62842.2734-0.2251-1.84283.91350.474-0.14872.084-0.44162.7405-9.8717-14.5807-30.0889
293.69014.15694.0875.56925.19664.87880.50970.4877-0.56442.6018-0.4078-2.43833.0164-1.9856-0.0284.503-0.1788-0.13512.5613-0.281.6345-10.06742.7906-7.2779
305.05386.23843.92999.28456.26874.234-0.2771-4.11312.272-3.1066-1.5901-1.3384-3.2499-2.64971.92671.82180.4468-0.19331.7648-0.44191.4497-18.664981.2138-27.4724
316.6481-5.471-5.3035.59155.22485.23390.66915.1975-0.23480.2727-0.9578-0.85721.2682-1.70940.31581.11910.240.16871.8629-0.09031.3055-15.102875.9288-44.7
322.8672-2.16624.17543.5146-1.05718.3992-1.17770.76190.5318-0.70711.5294-0.42653.62930.3477-0.2752.5848-0.0786-0.28651.79630.04111.7514-1.611164.88-39.9106
334.4376-4.3463-0.30924.4188-0.22114.3733-0.64971.85021.40322.5490.0764-1.47250.8026-0.55130.53271.80030.53850.16622.20340.09361.7514-0.832958.0385-46.575
344.5335-1.8883-4.29724.53761.45414.1547-0.93550.3931-1.53852.51381.2189-2.50781.3670.6046-0.33781.57190.2365-0.02721.3286-0.68912.231-17.543782.8538-38.5261
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 85 )
2X-RAY DIFFRACTION2chain 'A' and (resid 121 through 149 )
3X-RAY DIFFRACTION3chain 'A' and (resid 86 through 120 )
4X-RAY DIFFRACTION4chain 'A' and (resid 150 through 242 )
5X-RAY DIFFRACTION5chain 'A' and (resid 243 through 315 )
6X-RAY DIFFRACTION6chain 'A' and (resid 316 through 426 )
7X-RAY DIFFRACTION7chain 'A' and (resid 427 through 554 )
8X-RAY DIFFRACTION8chain 'B' and (resid 4 through 85 )
9X-RAY DIFFRACTION9chain 'B' and (resid 121 through 149 )
10X-RAY DIFFRACTION10chain 'B' and (resid 86 through 120 )
11X-RAY DIFFRACTION11chain 'B' and (resid 150 through 242 )
12X-RAY DIFFRACTION12chain 'B' and (resid 243 through 315 )
13X-RAY DIFFRACTION13chain 'B' and (resid 316 through 428 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 85 )
15X-RAY DIFFRACTION15chain 'C' and (resid 121 through 149 )
16X-RAY DIFFRACTION16chain 'C' and (resid 86 through 120 )
17X-RAY DIFFRACTION17chain 'C' and (resid 150 through 242 )
18X-RAY DIFFRACTION18chain 'C' and (resid 243 through 315 )
19X-RAY DIFFRACTION19chain 'C' and (resid 316 through 426 )
20X-RAY DIFFRACTION20chain 'C' and (resid 427 through 553 )
21X-RAY DIFFRACTION21chain 'D' and (resid 6 through 85 )
22X-RAY DIFFRACTION22chain 'D' and (resid 121 through 149 )
23X-RAY DIFFRACTION23chain 'D' and (resid 86 through 120 )
24X-RAY DIFFRACTION24chain 'D' and (resid 150 through 242 )
25X-RAY DIFFRACTION25chain 'D' and (resid 243 through 315 )
26X-RAY DIFFRACTION26chain 'D' and (resid 316 through 427 )
27X-RAY DIFFRACTION27chain 'F' and (resid -1 through 12)
28X-RAY DIFFRACTION28chain 'F' and (resid 13 through 21)
29X-RAY DIFFRACTION29chain 'F' and (resid 22 through 33)
30X-RAY DIFFRACTION30chain 'E' and (resid -1 through 3)
31X-RAY DIFFRACTION31chain 'E' and (resid 4 through 8)
32X-RAY DIFFRACTION32chain 'E' and (resid 9 through 13)
33X-RAY DIFFRACTION33chain 'E' and (resid 14 through 26)
34X-RAY DIFFRACTION34chain 'E' and (resid 27 through 33)

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