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- PDB-6uu6: E. coli sigma-S transcription initiation complex with a 4-nt RNA ... -

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Basic information

Entry
Database: PDB / ID: 6uu6
TitleE. coli sigma-S transcription initiation complex with a 4-nt RNA and a UTP ("Old" crystal soaked with UTP, ddCTP, and dinucleotide ApG for 30 minutes)
Components
  • (DNA-directed RNA polymerase subunit ...Polymerase) x 4
  • (Synthetic DNA 50-mer (promoter ...) x 2
  • RNA 4-mer (dinucleotide ApG primed synthesis)
  • RNA polymerase sigma factor RpoS
KeywordsTRANSCRIPTION / TRANSFERASE/DNA/RNA / Transcription initiation / RNA polymerase / DNA promoter / transcription bubble / de novo RNA synthesis / DNA scrunching / sigma-S factor / TRANSFERASE-DNA-RNA complex
Function / homology
Function and homology information


bacterial-type RNA polymerase core enzyme binding / sigma factor antagonist complex / RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / sigma factor activity / bacterial-type flagellum-dependent cell motility ...bacterial-type RNA polymerase core enzyme binding / sigma factor antagonist complex / RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / sigma factor activity / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcription elongation factor complex / DNA-directed RNA polymerase complex / regulation of DNA-templated transcription elongation / transcription antitermination / cell motility / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / response to heat / protein-containing complex assembly / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / negative regulation of DNA-templated transcription / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / membrane / cytosol / cytoplasm
Similarity search - Function
RNA polymerase sigma factor RpoS / Sigma-70 factors family signature 1. / RNA polymerase sigma-70 region 1.2 / Sigma-70 factor, region 1.2 / RNA polymerase sigma-70 region 3 / Sigma-70 region 3 / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 ...RNA polymerase sigma factor RpoS / Sigma-70 factors family signature 1. / RNA polymerase sigma-70 region 1.2 / Sigma-70 factor, region 1.2 / RNA polymerase sigma-70 region 3 / Sigma-70 region 3 / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 / RNA polymerase sigma-70 region 2 / RNA polymerase sigma-70 like domain / Sigma-70 region 2 / RNA polymerase sigma factor, region 2 / RNA polymerase sigma factor, region 3/4-like / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 4 / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 5 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
URIDINE 5'-TRIPHOSPHATE / DNA / DNA (> 10) / RNA / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / RNA polymerase sigma factor RpoS
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Escherichia coli K-12 (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.201 Å
AuthorsZuo, Y. / De, S. / Steitz, T.A.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM22778 United States
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Iscience / Year: 2020
Title: Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation.
Authors: Zuo, Y. / De, S. / Feng, Y. / Steitz, T.A.
History
DepositionOct 30, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 26, 2020Provider: repository / Type: Initial release
Revision 1.1Sep 2, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 2.0Apr 13, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / database_2 / entity / entity_src_gen / ndb_struct_na_base_pair / ndb_struct_na_base_pair_step / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_polymer_linkage / struct_asym / struct_conn / struct_ref_seq
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.label_seq_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.pdbx_label_seq_id / _atom_site_anisotrop.type_symbol / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_gen.pdbx_gene_src_scientific_name / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_struct_assembly_gen.asym_id_list / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_end
Revision 2.1Oct 11, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AAA: DNA-directed RNA polymerase subunit alpha
BBB: DNA-directed RNA polymerase subunit alpha
CCC: DNA-directed RNA polymerase subunit beta
DDD: DNA-directed RNA polymerase subunit beta'
EEE: DNA-directed RNA polymerase subunit omega
FFF: RNA polymerase sigma factor RpoS
111: Synthetic DNA 50-mer (promoter non-template strand)
222: Synthetic DNA 50-mer (promoter template strand)
333: RNA 4-mer (dinucleotide ApG primed synthesis)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)441,63214
Polymers440,9689
Non-polymers6645
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)132.395, 154.105, 232.152
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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DNA-directed RNA polymerase subunit ... , 4 types, 5 molecules AAABBBCCCDDDEEE

#1: Protein DNA-directed RNA polymerase subunit alpha / Polymerase / RNAP subunit alpha / RNA polymerase subunit alpha / Transcriptase subunit alpha


Mass: 26899.572 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoA, pez, phs, sez, b3295, JW3257 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A7Z4, DNA-directed RNA polymerase
#2: Protein DNA-directed RNA polymerase subunit beta / Polymerase / RNAP subunit beta / RNA polymerase subunit beta / Transcriptase subunit beta


Mass: 150820.875 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoB, Z5560, ECs4910 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A8V4, DNA-directed RNA polymerase
#3: Protein DNA-directed RNA polymerase subunit beta' / Polymerase / RNAP subunit beta' / RNA polymerase subunit beta' / Transcriptase subunit beta'


Mass: 155366.781 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoC, tabB, b3988, JW3951 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A8T7, DNA-directed RNA polymerase
#4: Protein DNA-directed RNA polymerase subunit omega / Polymerase / RNAP omega subunit / RNA polymerase omega subunit / Transcriptase subunit omega


Mass: 10118.352 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoZ, b3649, JW3624 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A800, DNA-directed RNA polymerase

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Synthetic DNA 50-mer (promoter ... , 2 types, 2 molecules 111222

#6: DNA chain Synthetic DNA 50-mer (promoter non-template strand)


Mass: 15313.812 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#7: DNA chain Synthetic DNA 50-mer (promoter template strand)


Mass: 15562.970 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Protein / RNA chain , 2 types, 2 molecules FFF333

#5: Protein RNA polymerase sigma factor RpoS / Sigma S / Sigma-38


Mass: 38777.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K12 / Gene: rpoS, appR, katF, nur, otsX, sigS, b2741, JW5437 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P13445
#8: RNA chain RNA 4-mer (dinucleotide ApG primed synthesis)


Mass: 1208.803 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 3 types, 5 molecules

#9: Chemical ChemComp-UTP / URIDINE 5'-TRIPHOSPHATE / Uridine triphosphate


Mass: 484.141 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H15N2O15P3 / Comment: UTP*YM
#10: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#11: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

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Details

Has ligand of interestN

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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: 2.69 Å3/Da / Density % sol: 54.2 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: PEG3350, sodium chloride, HEPES / Temp details: Room temperature

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 6, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 4.2→49.1 Å / Num. obs: 35121 / % possible obs: 99.1 % / Redundancy: 6.8 % / CC1/2: 0.999 / Net I/σ(I): 7.53
Reflection shellResolution: 4.2→4.45 Å / Redundancy: 6.8 % / Mean I/σ(I) obs: 0.46 / Num. unique obs: 5349 / CC1/2: 0.114 / % possible all: 95.2

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Processing

Software
NameVersionClassification
REFMAC5.8.0257refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5IPL

5ipl


Resolution: 4.201→49.077 Å / Cor.coef. Fo:Fc: 0.867 / Cor.coef. Fo:Fc free: 0.851 / SU B: 713.838 / SU ML: 3.475 / Cross valid method: FREE R-VALUE / ESU R Free: 1.557
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflectionSelection details
Rfree0.389 1678 4.799 %0
Rwork0.3425 ---
all0.345 ---
obs-34963 98.872 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 251.227 Å2
Baniso -1Baniso -2Baniso -3
1-0.154 Å20 Å20 Å2
2---0.06 Å20 Å2
3----0.094 Å2
Refinement stepCycle: LAST / Resolution: 4.201→49.077 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27579 1396 51 0 29026
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01329595
X-RAY DIFFRACTIONr_bond_other_d0.0010.01727663
X-RAY DIFFRACTIONr_angle_refined_deg1.451.61940264
X-RAY DIFFRACTIONr_angle_other_deg1.0171.61964120
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.71453511
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.68121.7261582
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.54155173
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.19315263
X-RAY DIFFRACTIONr_chiral_restr0.0670.23883
X-RAY DIFFRACTIONr_gen_planes_refined0.0380.0232224
X-RAY DIFFRACTIONr_gen_planes_other0.0350.026071
X-RAY DIFFRACTIONr_nbd_refined0.2280.36875
X-RAY DIFFRACTIONr_symmetry_nbd_other0.2390.329460
X-RAY DIFFRACTIONr_nbtor_refined0.1570.52963
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2680.5967
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.160.561
X-RAY DIFFRACTIONr_metal_ion_refined0.2060.52
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.350.354
X-RAY DIFFRACTIONr_nbd_other0.4010.397
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.3860.58
X-RAY DIFFRACTIONr_mcbond_it5.84120.48414062
X-RAY DIFFRACTIONr_mcbond_other5.84120.48414061
X-RAY DIFFRACTIONr_mcangle_it10.39934.55517567
X-RAY DIFFRACTIONr_mcangle_other10.39834.55517568
X-RAY DIFFRACTIONr_scbond_it4.3521.0515533
X-RAY DIFFRACTIONr_scbond_other4.3521.05115534
X-RAY DIFFRACTIONr_scangle_it8.08935.35422697
X-RAY DIFFRACTIONr_scangle_other8.08935.35522698
X-RAY DIFFRACTIONr_lrange_it23.899287.733107628
X-RAY DIFFRACTIONr_lrange_other23.899287.732107629
X-RAY DIFFRACTIONr_ncsr_local_group_10.1330.056383
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
4.201-4.310.521140.53522630.53525760.5180.51192.27480.529
4.31-4.4270.4951270.49823640.49824920.2840.2399.95990.492
4.427-4.5540.4521160.42822930.4324130.4230.43899.83420.426
4.554-4.6930.4161280.39122370.39223660.5320.54799.95770.391
4.693-4.8450.452990.39121860.39422870.5450.54299.91260.39
4.845-5.0140.3951230.38820810.38822050.4560.49199.95460.39
5.014-5.2010.421960.39220560.39321520.5220.5481000.396
5.201-5.4110.417970.39419580.39620560.5020.53999.95140.396
5.411-5.6480.396880.40719050.40720010.4960.51699.60020.41
5.648-5.920.499800.43718150.4419120.5190.50399.11090.439
5.92-6.2350.497910.42117120.42518090.5810.56499.66830.42
6.235-6.6070.462600.37916570.38117280.6240.69399.36340.373
6.607-7.0540.415840.31315390.31816340.7130.7799.32680.291
7.054-7.6060.311840.26114240.26415150.7880.81599.5380.24
7.606-8.3120.369680.23113460.23814220.820.87899.43740.211
8.312-9.260.27680.20212150.20612910.8940.92599.38030.191
9.26-10.6290.329480.21310750.21811440.8730.92498.16430.205
10.629-12.8680.267370.2259330.22710060.9360.92996.42150.226
12.868-17.6030.36480.3297350.3317940.8550.85998.61460.332
17.603-49.0770.474220.5014910.4995260.6090.67897.52850.603
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)
16.27331.0051-0.71842.0129-0.19641.90550.1149-0.93220.50690.37050.1713-0.32960.34140.3846-0.28610.14460.1033-0.11870.2415-0.1860.165541.529-5.1164.509
24.1328-0.391-1.447.45152.60363.92060.19591.04240.0288-0.95740.20070.5919-0.062-1.064-0.39660.187-0.0719-0.08550.77270.45020.518818.145-1.554-40.158
36.2082-1.2683-0.8865.19072.01035.45660.04060.52030.6763-0.56860.1508-0.04870.05420.1996-0.19130.3319-0.07190.12960.3640.35020.615754.571.773-57.522
413.3474.9418-2.06486.39172.04336.877-0.28980.45350.764-0.54690.1346-0.2293-0.5107-0.02380.15530.9620.39380.13020.81850.11660.694471.796-30.504-29.68
59.5253-4.2729-4.59677.755-5.456512.10971.02211.36581.6254-0.9153-0.1595-0.5736-0.4734-1.167-0.86261.7134-0.1082-0.02430.7816-0.35681.94150.92732.007-18.335
615.9369-3.674-2.44413.7545-2.63493.95290.19950.34910.01980.01580.17650.3753-0.4068-0.264-0.3761.8167-0.14980.05581.0431-0.61381.689534.26430.80810.934
712.00363.81233.35737.0654.48263.56030.093-0.8985-0.30391.25750.38610.70320.6801-0.0259-0.47921.24040.08210.31051.86250.21961.8249-28.517-3.3232.445
85.67460.73251.40150.2627-0.05836.65550.7588-0.1178-0.57280.4069-0.1823-0.23710.16731.9091-0.57661.27110.06460.04461.0549-0.28251.481686.7121.695-51.778
91.14971.03354.7361.07694.449320.09860.0076-0.2224-0.05230.2097-0.39240.49250.6595-0.5460.38480.9475-0.14280.23752.4411-0.1252.544576.81821.011-29.558
100.44521.31410.36915.60891.47410.4411-0.51040.39140.3260.1060.52351.3212-0.15040.0477-0.01312.66880.04540.25752.5630.51953.203835.04548.906-42.864
117.9756-1.3638-3.06515.56783.08923.1256-0.2263-0.66660.8703-1.28190.2547-0.9749-0.58541.1614-0.02840.52980.2078-0.14281.47680.32211.333479.1612.776-16.258
123.62272.54160.07247.2126-2.71715.45590.0143-0.3458-1.6420.3645-0.121-0.06830.27170.33620.10671.42690.07630.18141.14580.21471.424673.94-62.771-30.924
130.17980.4980.07142.72260.17840.07980.5785-0.3899-0.25071.0717-0.6298-1.92950.41130.15470.05132.6874-0.2063-0.02523.56380.27122.550972.99326.43414.004
147.04040.41961.10282.76650.1495.1760.3417-0.17880.77990.06880.3494-0.17940.1221-0.7397-0.69111.25480.26770.11331.0417-0.07661.76710.40117.7686.852
156.27894.83739.96353.73117.68315.88210.25520.4359-0.5570.12060.2952-0.44030.37240.5227-0.55042.0705-0.26670.32041.8570.03372.366428.831-48.208-53.636
168.5775-6.3022-5.3257.67656.30496.5851-0.01890.8398-4.1676-0.2446-0.73241.39220.36110.59060.75130.89790.30040.01991.167-0.81533.144423.923-29.142-3.592
174.8841-0.7099-0.16024.103-0.83710.22510.10410.83130.2155-0.2184-0.02170.19350.1097-0.2653-0.08240.5431-0.33780.10241.6199-0.06230.9689-3.464-6.602-12.238
1810.353-0.33760.20122.8870.31591.1689-0.0595-0.21870.51240.6123-0.0267-0.21080.4548-0.18260.08611.888-0.08220.04171.93410.0381.823628.467-52.926-30.099
191.9772-2.2156-7.376312.11927.546828.46020.1269-0.44310.2393.1361-0.3191-1.8176-0.20531.5820.19211.4132-0.2847-0.07712.5897-0.44562.539643.1393.483-24.007
207.19882.01143.19141.09672.13655.11160.0248-0.19561.3285-0.82940.51450.2286-1.49160.5703-0.53932.5103-0.47880.23082.4061-0.27873.390781.36730.748-51.55
210.0727-0.0157-0.01870.08190.00190.0618-0.15560.1281-0.3157-0.3469-0.04470.25130.09970.30270.20032.65860.0936-0.04222.5919-0.04812.147548.812-20.964-43.101
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1ALLCCC1 - 28
2X-RAY DIFFRACTION1ALLCCC146 - 152
3X-RAY DIFFRACTION1ALLCCC445 - 455
4X-RAY DIFFRACTION1ALLCCC517 - 832
5X-RAY DIFFRACTION1ALLCCC1056 - 1241
6X-RAY DIFFRACTION1ALLDDD767 - 790
7X-RAY DIFFRACTION1ALLDDD1504
8X-RAY DIFFRACTION1ALL333501
9X-RAY DIFFRACTION2ALLCCC1242 - 1321
10X-RAY DIFFRACTION2ALLDDD343 - 500
11X-RAY DIFFRACTION2ALLDDD791 - 943
12X-RAY DIFFRACTION2ALLDDD1129 - 1153
13X-RAY DIFFRACTION2ALLDDD1213 - 1317
14X-RAY DIFFRACTION2ALLDDD1345 - 1407
15X-RAY DIFFRACTION2ALLDDD1502 - 1503
16X-RAY DIFFRACTION2ALLEEE2 - 91
17X-RAY DIFFRACTION3ALLCCC1322 - 1342
18X-RAY DIFFRACTION3ALLDDD1 - 342
19X-RAY DIFFRACTION3ALLDDD1318 - 1344
20X-RAY DIFFRACTION3ALLDDD1501
21X-RAY DIFFRACTION3ALLFFF218 - 226
22X-RAY DIFFRACTION3ALLFFF232 - 241
23X-RAY DIFFRACTION4ALLCCC153 - 226
24X-RAY DIFFRACTION4ALLCCC337 - 444
25X-RAY DIFFRACTION4ALL11145 - 52
26X-RAY DIFFRACTION5ALLCCC833 - 891
27X-RAY DIFFRACTION5ALLCCC912 - 936
28X-RAY DIFFRACTION5ALLCCC1040 - 1055
29X-RAY DIFFRACTION6ALLAAA52 - 178
30X-RAY DIFFRACTION7ALLBBB52 - 178
31X-RAY DIFFRACTION8ALLFFF53 - 166
32X-RAY DIFFRACTION8ALL11137 - 44
33X-RAY DIFFRACTION9ALLFFF167 - 217
34X-RAY DIFFRACTION9ALL22222 - 26
35X-RAY DIFFRACTION10ALLFFF242 - 329
36X-RAY DIFFRACTION10ALLCCC892 - 911
37X-RAY DIFFRACTION11ALLCCC29 - 145
38X-RAY DIFFRACTION11ALLCCC456 - 516
39X-RAY DIFFRACTION12ALLCCC227 - 336
40X-RAY DIFFRACTION13ALLCCC937 - 1039
41X-RAY DIFFRACTION14ALLAAA1 - 51
42X-RAY DIFFRACTION14ALLAAA179 - 235
43X-RAY DIFFRACTION14ALLBBB1 - 51
44X-RAY DIFFRACTION14ALLBBB179 - 235
45X-RAY DIFFRACTION15ALLDDD1154 - 1212
46X-RAY DIFFRACTION16ALLDDD637 - 766
47X-RAY DIFFRACTION17ALLDDD501 - 636
48X-RAY DIFFRACTION18ALLDDD944 - 1128
49X-RAY DIFFRACTION19ALLFFF227 - 231
50X-RAY DIFFRACTION19ALL22211 - 21
51X-RAY DIFFRACTION19ALL33315 - 18
52X-RAY DIFFRACTION20ALL11120 - 36
53X-RAY DIFFRACTION20ALL22227 - 43
54X-RAY DIFFRACTION21ALL11153 - 59
55X-RAY DIFFRACTION21ALL2223 - 10

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