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- PDB-4yy3: 30S ribosomal subunit- HigB complex -

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Basic information

Entry
Database: PDB / ID: 4yy3
Title30S ribosomal subunit- HigB complex
Components
  • (30S ribosomal protein ...) x 20
  • 16S rRNA
  • Killer protein
KeywordsRIBOSOME / Bacterial toxins / Stringent response / translational control / RNase
Function / homology
Function and homology information


plasmid maintenance / RNA catabolic process / translation repressor activity / RNA endonuclease activity / negative regulation of cell growth / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding ...plasmid maintenance / RNA catabolic process / translation repressor activity / RNA endonuclease activity / negative regulation of cell growth / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / Hydrolases; Acting on ester bonds / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / negative regulation of cell population proliferation / mRNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Toxin HigB-1 / RelE-like toxin of type II toxin-antitoxin system HigB / RelE-like / YaeB-like fold / Toxin-antitoxin system, RelE/ParE toxin domain superfamily / S16 Ribosomal Protein; Chain: A; / Ribosomal protein S16 / Ribosomal protein S18 / 30s Ribosomal Protein S18 / 30s ribosomal protein s13; domain 2 ...Toxin HigB-1 / RelE-like toxin of type II toxin-antitoxin system HigB / RelE-like / YaeB-like fold / Toxin-antitoxin system, RelE/ParE toxin domain superfamily / S16 Ribosomal Protein; Chain: A; / Ribosomal protein S16 / Ribosomal protein S18 / 30s Ribosomal Protein S18 / 30s ribosomal protein s13; domain 2 / Ribosomal protein S13/S18, C-terminal domain / Ribosomal protein S20 / 30s Ribosomal Protein S19; Chain A / Ribosomal protein S19/S15 / Ribosomal protein S3, C-terminal domain / Ribosomal Protein S14/S29 / 30s Ribosomal Protein S14; Chain N / Ribosomal protein S4/S9, N-terminal domain / Ribosomal Protein S4 Delta 41; Chain A, domain 1 / Ribosomal Protein S8; Chain: A, domain 1 - #30 / Ribosomal protein S3 C-terminal domain / Ribosomal protein S6/Translation elongation factor EF1B / Dna Ligase; domain 1 - #10 / Ribosomal protein S11/S14 / Ribosomal protein S10 / S15/NS1, RNA-binding / Helix hairpin bin / Ribosomal Protein S7 / Ribosomal protein S7/S5 / RNA-binding S4 domain / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / K homology (KH) domain / Helicase, Ruva Protein; domain 3 - #50 / Double Stranded RNA Binding Domain - #20 / Glucose-6-phosphate isomerase like protein; domain 1 / Ribosomal Protein S8; Chain: A, domain 1 / Ribosomal Protein S5; domain 2 - #10 / 30S ribosomal protein Thx / 30S ribosomal protein Thx / 30S ribosomal protein / GMP Synthetase; Chain A, domain 3 / Ribosomal Protein S5; domain 2 / Ribosomal protein S14, type Z / Double Stranded RNA Binding Domain / Helicase, Ruva Protein; domain 3 / Nucleic acid-binding proteins / Dna Ligase; domain 1 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Ribosomal protein S3, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S9, bacterial/plastid / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein S4, bacterial-type / Ribosomal protein S14/S29 / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal protein S18, conserved site / Ribosomal protein S18 signature. / Ribosomal protein S16 / Ribosomal protein S16 domain superfamily / Ribosomal protein S16 / Ribosomal protein S15, bacterial-type / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein S6 superfamily / Ribosomal protein S12, bacterial-type / Translation elongation factor EF1B/ribosomal protein S6 / Ribosomal protein S18 / Ribosomal protein S18 / Ribosomal protein S18 superfamily / K Homology domain / K homology RNA-binding domain / Few Secondary Structures / Irregular / Ribosomal protein S3, conserved site / Ribosomal protein S3 signature. / Ribosomal protein S10, conserved site / Ribosomal protein S10 signature. / Ribosomal protein S14, conserved site / Ribosomal protein S14 signature. / Ribosomal protein S2 signature 1. / KH domain / Type-2 KH domain profile. / K Homology domain, type 2 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Ribosomal protein S3, C-terminal / Ribosomal protein S3, C-terminal domain / Ribosomal protein S3, C-terminal domain superfamily / Ribosomal protein S15/S19, conserved site / Ribosomal protein S19 signature. / Ribosomal protein S10
Similarity search - Domain/homology
: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS2 ...: / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS19 / 30S ribosomal protein S17 / 30S ribosomal protein S14 type Z / 30S ribosomal protein S8 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein bTHX / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein bS18 / Endoribonuclease HigB
Similarity search - Component
Biological speciesProteus vulgaris (bacteria)
Thermus thermophilus HB8 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.6 Å
AuthorsSchureck, M.A. / Maehigashi, T. / Dunham, C.M.
CitationJournal: Rna / Year: 2016
Title: mRNA bound to the 30S subunit is a HigB toxin substrate.
Authors: Schureck, M.A. / Maehigashi, T. / Miles, S.J. / Marquez, J. / Dunham, C.M.
History
DepositionMar 23, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 6, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 3, 2016Group: Database references
Revision 1.2Nov 22, 2017Group: Database references / Derived calculations / Refinement description
Category: citation / pdbx_struct_oper_list / software
Item: _citation.journal_id_CSD / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.3Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 16S rRNA
B: 30S ribosomal protein S2
C: 30S ribosomal protein S3
D: 30S ribosomal protein S4
E: 30S ribosomal protein S5
F: 30S ribosomal protein S6
G: 30S ribosomal protein S7
H: 30S ribosomal protein S8
I: 30S ribosomal protein S9
J: 30S ribosomal protein S10
K: 30S ribosomal protein S11
L: 30S ribosomal protein S12
M: 30S ribosomal protein S13
N: 30S ribosomal protein S14 type Z
O: 30S ribosomal protein S15
P: 30S ribosomal protein S16
Q: 30S ribosomal protein S17
R: 30S ribosomal protein S18
S: 30S ribosomal protein S19
T: 30S ribosomal protein S20
V: 30S ribosomal protein Thx
Y: Killer protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)801,954218
Polymers797,10822
Non-polymers4,846196
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area90820 Å2
ΔGint-760 kcal/mol
Surface area280230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)402.594, 402.594, 176.035
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

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30S ribosomal protein ... , 20 types, 20 molecules BCDEFGHIJKLMNOPQRSTV

#2: Protein 30S ribosomal protein S2


Mass: 29317.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80371
#3: Protein 30S ribosomal protein S3


Mass: 26751.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80372
#4: Protein 30S ribosomal protein S4


Mass: 24373.447 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80373
#5: Protein 30S ribosomal protein S5


Mass: 17583.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHQ5
#6: Protein 30S ribosomal protein S6 / TS9


Mass: 11988.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SLP8
#7: Protein 30S ribosomal protein S7


Mass: 18050.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P17291
#8: Protein 30S ribosomal protein S8


Mass: 15868.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHQ2, UniProt: P0DOY9*PLUS
#9: Protein 30S ribosomal protein S9


Mass: 14410.614 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80374
#10: Protein 30S ribosomal protein S10


Mass: 11954.968 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHN7
#11: Protein 30S ribosomal protein S11


Mass: 13737.868 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80376
#12: Protein 30S ribosomal protein S12


Mass: 14637.384 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHN3
#13: Protein 30S ribosomal protein S13


Mass: 14338.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80377
#14: Protein 30S ribosomal protein S14 type Z


Mass: 7158.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHQ1, UniProt: P0DOY6*PLUS
#15: Protein 30S ribosomal protein S15


Mass: 10578.407 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SJ76
#16: Protein 30S ribosomal protein S16


Mass: 10409.983 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SJH3
#17: Protein 30S ribosomal protein S17


Mass: 12325.655 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHP7, UniProt: P0DOY7*PLUS
#18: Protein 30S ribosomal protein S18


Mass: 10258.299 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SLQ0
#19: Protein 30S ribosomal protein S19


Mass: 10605.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SHP2
#20: Protein 30S ribosomal protein S20


Mass: 11736.143 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: P80380
#21: Protein/peptide 30S ribosomal protein Thx / S31


Mass: 3350.030 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: UniProt: Q5SIH3

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RNA chain / Protein , 2 types, 2 molecules AY

#1: RNA chain 16S rRNA


Mass: 493958.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB8 (bacteria) / Strain: HB8 / ATCC 27634 / DSM 579 / References: GenBank: 55771382
#22: Protein Killer protein


Mass: 13713.409 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Proteus vulgaris (bacteria) / Gene: higB / Plasmid: pBAD/Myc-HisA / Production host: Escherichia coli (E. coli) / Strain (production host): BW25113 / References: UniProt: Q7A225

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Non-polymers , 2 types, 196 molecules

#23: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 194 / Source method: obtained synthetically / Formula: Mg
#24: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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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: 4.49 Å3/Da / Density % sol: 72.62 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 14% MPD, 0.2 M KCL , 75 mM NH4Cl, 15 mM MgCl2 , 0.1M MES

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 21, 2012 / Details: MIRRORS
RadiationMonochromator: KOHZU DIAMOND MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 3.6→50 Å / Num. obs: 163739 / % possible obs: 98.6 % / Observed criterion σ(I): -3 / Redundancy: 3 % / Biso Wilson estimate: 109.99 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.098 / Net I/σ(I): 9.8
Reflection shellResolution: 3.6→3.73 Å / Redundancy: 3 % / Rmerge(I) obs: 0.614 / Mean I/σ(I) obs: 1.8 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX1.8.1_1168refinement
XDSdata scaling
XSCALEdata scaling
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1J5E

1j5e


Resolution: 3.6→46.158 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2387 7843 4.79 %Inherited from 1J5E
Rwork0.2144 ---
obs0.2156 163571 98.5 %-
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1 Å
Refinement stepCycle: LAST / Resolution: 3.6→46.158 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19930 32514 196 0 52640
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00756646
X-RAY DIFFRACTIONf_angle_d1.22883971
X-RAY DIFFRACTIONf_dihedral_angle_d17.33226170
X-RAY DIFFRACTIONf_chiral_restr0.10310522
X-RAY DIFFRACTIONf_plane_restr0.0145029
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.6-3.64090.34892570.31135150X-RAY DIFFRACTION100
3.6409-3.68370.33512620.30265211X-RAY DIFFRACTION100
3.6837-3.72860.31622860.29515167X-RAY DIFFRACTION100
3.7286-3.77580.31252850.27735156X-RAY DIFFRACTION100
3.7758-3.82550.29992360.26995281X-RAY DIFFRACTION100
3.8255-3.87780.25952420.25645146X-RAY DIFFRACTION100
3.8778-3.93320.29182750.25825199X-RAY DIFFRACTION99
3.9332-3.99190.29012510.25225235X-RAY DIFFRACTION100
3.9919-4.05420.26872760.25485170X-RAY DIFFRACTION100
4.0542-4.12060.27882800.24335170X-RAY DIFFRACTION100
4.1206-4.19170.27852510.2285253X-RAY DIFFRACTION100
4.1917-4.26780.2712570.22975201X-RAY DIFFRACTION100
4.2678-4.34990.27222720.22265199X-RAY DIFFRACTION100
4.3499-4.43860.25452780.22215178X-RAY DIFFRACTION99
4.4386-4.5350.23612850.21815190X-RAY DIFFRACTION99
4.535-4.64040.22222560.20965207X-RAY DIFFRACTION99
4.6404-4.75630.22352280.20625217X-RAY DIFFRACTION99
4.7563-4.88480.23892410.20115273X-RAY DIFFRACTION99
4.8848-5.02840.2262740.19755159X-RAY DIFFRACTION99
5.0284-5.19050.19992480.1995224X-RAY DIFFRACTION99
5.1905-5.37570.21692420.19115226X-RAY DIFFRACTION99
5.3757-5.59060.21962460.19165236X-RAY DIFFRACTION99
5.5906-5.84460.21232630.18515212X-RAY DIFFRACTION99
5.8446-6.1520.20322350.1875221X-RAY DIFFRACTION98
6.152-6.53650.21942560.19195219X-RAY DIFFRACTION98
6.5365-7.03950.21452680.18325216X-RAY DIFFRACTION98
7.0395-7.7450.22382750.18365182X-RAY DIFFRACTION97
7.745-8.85880.2312780.19495160X-RAY DIFFRACTION96
8.8588-11.13520.19832670.1995153X-RAY DIFFRACTION95
11.1352-46.1620.2222730.21654917X-RAY DIFFRACTION88
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)
10.24380.2444-0.07780.6091-0.0260.34830.0336-0.1078-0.07020.27710.05340.21240.1197-0.0305-0.0770.73080.0910.16650.61150.06950.8272132.036675.19077.3605
20.6009-0.0372-0.21340.25550.00120.35720.05370.2460.0629-0.14770.0323-0.0311-0.04460.0358-0.09880.58510.0450.09260.6908-0.01250.5867170.5718111.3016-51.3805
30.7842-0.17260.01160.3952-0.07180.1872-0.0087-0.34470.270.17230.0813-0.2187-0.09450.1626-0.07390.7983-0.05130.06071.0236-0.31430.91220.6473133.37745.2587
43.66732.5613-0.65182.2267-0.42070.2590.0354-0.1955-0.74430.1255-0.0059-0.58440.1270.0743-0.03030.7670.16110.0050.72410.020.7473166.403871.6798-25.4683
55.3624-1.7714-4.2225.2071.54316.12810.5617-1.21411.24920.51770.1986-0.0569-0.33980.5409-0.75440.5687-0.06970.08530.6705-0.21190.5887167.9778128.96293.6954
67.47260.27591.00495.2801-5.96197.38040.4279-0.31720.8410.0768-0.01990.6219-0.2106-0.702-0.42950.43660.00340.09440.4996-0.15280.7617146.0653120.6828-1.4441
75.2748-1.01443.1892.6662-2.16058.423-0.2085-0.10450.21370.2918-0.08710.0711-0.2084-0.11540.28930.4802-0.10290.21930.3852-0.12750.4645149.5203124.6049-2.538
85.3244-4.71185.19465.0028-3.37826.8470.1593-0.6117-0.2304-0.12140.41970.39970.6088-0.2716-0.55260.61440.01480.09260.62850.07980.5713153.326491.0139-15.9421
92.6283.8501-0.20587.63771.87362.5105-0.15920.6381-0.3174-0.11240.1675-0.31790.35030.7407-0.04830.59270.1554-0.00610.89910.03130.5661174.700477.94196.7489
103.06521.0602-2.05018.50211.752.11430.0868-1.5470.46721.30260.4595-1.18771.15371.721-0.55220.81630.1652-0.28881.19080.03130.9311171.461683.285925.4345
112.78480.71272.5381.7202-0.18987.3250.12380.0722-0.1615-0.33180.23480.1860.8705-0.0723-0.36250.8609-0.09750.10530.45580.13210.8044112.105741.9953-17.1389
124.31974.18425.15854.92454.50116.5689-0.1633-0.14340.9792-0.34710.1131.3270.659-0.24880.06010.885-0.11110.12030.78260.26631.162102.614448.6635-23.2427
139.7868-2.91724.96433.76922.9769.3716-0.87770.03390.313-0.3455-0.16231.0950.11540.14591.03030.8049-0.1922-0.09931.15530.57271.365297.283949.9677-37.6436
140.1716-0.12460.13950.9347-0.40780.19430.00430.00730.03240.22980.11740.5178-0.0438-0.2441-0.12470.70860.05210.20280.73330.07191.0877121.722101.4671-12.5371
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1((chain A and (resid 5:560)) or (chain D) or (chain P) or (chain Q))
2X-RAY DIFFRACTION2((chain A and ((resid 561:587) or (resid 654:920))) or (chain O) or (chain R) or (chain K) or (chain F) or (chain H))
3X-RAY DIFFRACTION3((chain A and (resid 921:1400)) or (chain C) or (chain I) or (chain G) or (chain M) or (chain S) or (chain B) or (chain N))
4X-RAY DIFFRACTION4(chain A and (resid 1401:1544))
5X-RAY DIFFRACTION5(chain E and (resid 5:69))
6X-RAY DIFFRACTION6(chain E and (resid 70:101))
7X-RAY DIFFRACTION7(chain E and (resid 102:154))
8X-RAY DIFFRACTION8(chain L and (resid 5:28))
9X-RAY DIFFRACTION9(chain L and (resid 29:105))
10X-RAY DIFFRACTION10(chain L and (resid 106:128))
11X-RAY DIFFRACTION11(chain T and (resid 8:50))
12X-RAY DIFFRACTION12(chain T and (resid 51:83))
13X-RAY DIFFRACTION13(chain T and (resid 84:106))
14X-RAY DIFFRACTION14(chain A and (resid 588:653))

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