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- PDB-4kvb: Thermus thermophilus HB27 30S ribosomal subunit lacking ribosomal... -

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Basic information

Entry
Database: PDB / ID: 4kvb
TitleThermus thermophilus HB27 30S ribosomal subunit lacking ribosomal protein S17
Components
  • (30S ribosomal protein ...) x 19
  • 16S rRNA
KeywordsRIBOSOME / 30S ribosomal subunit / translation / 50S ribosomal subunit
Function / homology
Function and homology information


ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / tRNA binding / rRNA binding / structural constituent of ribosome / ribosome / translation ...ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / tRNA binding / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / zinc ion binding / cytoplasm / cytosol
Similarity search - Function
30S ribosomal protein Thx / 30S ribosomal protein Thx / 30S ribosomal protein / Ribosomal protein S14, type Z / Ribosomal protein S3, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S14/S29 / Ribosomal protein S6 signature. ...30S ribosomal protein Thx / 30S ribosomal protein Thx / 30S ribosomal protein / Ribosomal protein S14, type Z / Ribosomal protein S3, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S14/S29 / Ribosomal protein S6 signature. / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein S4, bacterial-type / Ribosomal protein S5, bacterial-type / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal protein S9, bacterial/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 / 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 / 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 / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S5 signature. / Ribosomal protein S19/S15 / Ribosomal protein S19/S15, superfamily / Ribosomal protein S19 / Ribosomal protein S2, conserved site / Ribosomal protein S2 / Ribosomal protein S2, flavodoxin-like domain superfamily / Ribosomal protein S2 / Ribosomal protein S7, conserved site / Ribosomal protein S7 signature. / : / K homology domain superfamily, prokaryotic type / Ribosomal protein S5 / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5, N-terminal / Ribosomal protein S5, C-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S5, C-terminal domain / Ribosomal protein S13, conserved site / Ribosomal protein S13 signature. / Ribosomal protein S13 / 30s ribosomal protein S13, C-terminal / Ribosomal protein S13/S18 / Ribosomal protein S13 family profile. / Ribosomal protein S8 signature. / Ribosomal protein S14 / Ribosomal protein S14p/S29e / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S4, conserved site / Ribosomal protein S15 signature. / Ribosomal protein S4 signature. / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S4/S9, N-terminal / K homology domain-like, alpha/beta / Ribosomal protein S4/S9 / Ribosomal protein S8 / Ribosomal protein S8 superfamily / Ribosomal protein S8 / S4 RNA-binding domain profile. / Ribosomal protein S10p/S20e / Ribosomal protein S13-like, H2TH / Ribosomal protein S10 domain / Ribosomal protein S10 domain superfamily / Ribosomal protein S10p/S20e / Ribosomal S11, conserved site / Ribosomal protein S11 signature. / S4 RNA-binding domain
Similarity search - Domain/homology
: / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bTHX / Small ribosomal subunit protein uS10 ...: / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bTHX / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS9
Similarity search - Component
Biological speciesThermus thermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.198 Å
AuthorsMurphy, E.L. / Jogl, G.
CitationJournal: To be Published
Title: Structural robustness of the ribosome inferred from the X-ray crystal structure of a 30S ribosomal subunit lacking ribosomal protein S17
Authors: Connetti, J.L. / Murphy, E.L. / Dahlberg, A.E. / Gregory, S.T. / Jogl, G.
History
DepositionMay 22, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 4, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.2Sep 20, 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 / struct_ref_seq_dif / struct_site
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_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.4Feb 19, 2025Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 ..._chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2 / _chem_comp_bond.pdbx_aromatic_flag / _chem_comp_bond.value_order

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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
R: 30S ribosomal protein S18
S: 30S ribosomal protein S19
T: 30S ribosomal protein S20
U: 30S ribosomal protein Thx
hetero molecules


Theoretical massNumber of molelcules
Total (without water)776,896215
Polymers771,55720
Non-polymers5,339195
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)397.316, 397.316, 215.505
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number92
Space group name H-MP41212

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Components

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RNA chain , 1 types, 1 molecules A

#1: RNA chain 16S rRNA


Mass: 494210.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: GenBank: AE017221.1

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30S ribosomal protein ... , 19 types, 19 molecules BCDEFGHIJKLMNOPRSTU

#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 (bacteria) / Strain: HB27 / References: UniProt: P62662
#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 (bacteria) / Strain: HB27 / References: UniProt: P62663
#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 (bacteria) / Strain: HB27 / References: UniProt: P62664
#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 (bacteria) / Strain: HB27 / References: UniProt: P62665
#6: Protein 30S ribosomal protein S6


Mass: 11988.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62666
#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 (bacteria) / Strain: HB27 / References: UniProt: P62667
#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 (bacteria) / Strain: HB27 / References: UniProt: P62668
#9: Protein 30S ribosomal protein S9


Mass: 14429.661 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62669
#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 (bacteria) / Strain: HB27 / References: UniProt: P62653
#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 (bacteria) / Strain: HB27 / References: UniProt: P62654
#12: Protein 30S ribosomal protein S12


Mass: 14867.713 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P61941
#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 (bacteria) / Strain: HB27 / References: UniProt: P62655
#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 (bacteria) / Strain: HB27 / References: UniProt: P62656
#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 (bacteria) / Strain: HB27 / References: UniProt: P62657
#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 (bacteria) / Strain: HB27 / References: UniProt: P62238
#17: Protein 30S ribosomal protein S18


Mass: 10258.299 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62659
#18: Protein 30S ribosomal protein S19


Mass: 10605.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62660
#19: Protein 30S ribosomal protein S20


Mass: 11722.116 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62661
#20: Protein/peptide 30S ribosomal protein Thx


Mass: 3350.030 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus (bacteria) / Strain: HB27 / References: UniProt: P62613

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Non-polymers , 3 types, 195 molecules

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


Mass: 24.305 Da / Num. of mol.: 158 / Source method: obtained synthetically / Formula: Mg
#22: Chemical...
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 35 / Source method: obtained synthetically / Formula: K
#23: Chemical ChemComp-ZN / ZINC ION


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

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Details

Has protein modificationY

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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: 5.51 Å3/Da / Density % sol: 77.68 %
Crystal growTemperature: 277 K / Method: hanging drop / pH: 6.5 / Details: MPD, pH 6.5, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 1, 2013
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 3.993→30 Å / Num. all: 134627 / Num. obs: 145334 / % possible obs: 92.6 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3
Reflection shellResolution: 3.993→4.23 Å / % possible all: 93.1

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIXdev_1370refinement
PDB_EXTRACT3.11data extraction
CBASSdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4JI5

4ji5


Resolution: 4.198→29.915 Å / SU ML: 0.7 / σ(F): 1.33 / Phase error: 28.51 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2576 5804 5 %
Rwork0.2171 110383 -
obs0.2192 116187 92.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 682.45 Å2 / Biso mean: 200.5256 Å2 / Biso min: 48.47 Å2
Refinement stepCycle: LAST / Resolution: 4.198→29.915 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18381 32552 195 0 51128
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00255116
X-RAY DIFFRACTIONf_angle_d0.581925
X-RAY DIFFRACTIONf_chiral_restr0.02210285
X-RAY DIFFRACTIONf_plane_restr0.0034765
X-RAY DIFFRACTIONf_dihedral_angle_d15.26325749
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
4.1982-4.24570.3921750.36693473364889
4.2457-4.29550.40961990.3553661386094
4.2955-4.34780.40181730.3413730390395
4.3478-4.40260.38232260.33593631385794
4.4026-4.46040.38571700.33273731390195
4.4604-4.52130.35541720.32463714388694
4.5213-4.58560.36341820.31653663384593
4.5856-4.65380.34482060.31253718392495
4.6538-4.72630.3611940.29943682387694
4.7263-4.80350.32051900.28813697388794
4.8035-4.8860.29751890.27663699388894
4.886-4.97440.30461880.27193683387194
4.9744-5.06960.32581750.27453707388294
5.0696-5.17260.31551960.25743674387094
5.1726-5.28450.28822070.24973671387893
5.2845-5.40670.26991990.22973649384893
5.4067-5.54110.27011950.2153675387093
5.5411-5.68990.27911750.21483684385993
5.6899-5.85610.25681660.21383707387393
5.8561-6.04370.26182020.21363672387493
6.0437-6.25780.27272090.20793667387693
6.2578-6.50590.27871960.20223686388293
6.5059-6.79870.22422100.19213668387893
6.7987-7.15250.23891950.17833688388392
7.1525-7.59370.19941830.16533678386192
7.5937-8.1690.20472070.16123638384592
8.169-8.97090.21722120.16733671388392
8.9709-10.22330.19281870.17083722390992
10.2233-12.71370.21062180.17093685390391
12.7137-29.91570.22692080.19933759396789
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)
10.5017-0.8069-0.29741.53470.03690.1707-0.1421-0.13580.06570.24380.1489-0.33710.15240.1887-0.00472.1592-0.0979-0.03662.0988-0.15452.339993.071-171.181-18.43
20.48640.092-0.18830.60640.1780.57280.056-0.06580.0056-0.0630.0661-0.1285-0.00090.1222-0.12931.9215-0.202-0.03641.967-0.04612.079275.867-128.485-7.121
31.1247-0.39950.22431.2185-0.58430.71320.21930.2822-0.0535-0.14010.02660.1815-0.06380.1518-0.21492.0024-0.20890.2281.9697-0.11741.899946.278-98.377-9.896
42.5423-0.4424-0.07281.1755-0.37110.23350.49560.79090.5177-0.4034-0.00190.1867-0.1847-0.2247-0.35462.22860.03540.41682.11820.23362.075539.334-71.868-35.381
51.543-0.0391-0.281.22710.00250.52140.12050.17750.4212-0.14290.16250.4088-0.3662-0.2112-0.26562.34580.07320.34532.19220.30312.261216.145-60.807-19.813
60.8394-0.756-0.01350.2028-0.1942-0.05720.13960.1283-0.4791-0.10280.03310.76460.09660.0447-0.1542.449-0.1087-0.0292.3711-0.06932.110949.009-125.5670.819
72.71830.264-0.19723.8679-2.63088.0035-0.3012-0.322-0.21320.2552-0.3167-0.55980.3197-0.06810.5242.0105-0.4507-0.02211.7475-0.48832.130999.733-71.7499.395
83.11073.5517-0.64964.3046-0.44297.3709-0.37611.12171.06352.0891.3593-1.4666-0.5757-1.7185-1.02191.56670.21360.06751.7132-0.39172.30687.165-63.279-3.957
96.5465-2.21994.60452.1669-0.33194.28441.4283-0.34591.1707-0.5616-0.2091-0.02420.268-0.2294-1.34253.0974-0.0960.92312.01110.11242.054271.852-55.26-13.46
105.0345-2.642.87182.82470.964.9728-0.42140.29460.7897-0.00770.59680.0674-0.82190.4541-0.19371.8349-0.63220.29521.3599-0.07892.035894.832-67.3510.907
114.47420.0274-0.35416.2814-2.29387.34590.11090.14140.40610.8016-0.24820.8264-1.23730.54850.19271.94820.23040.32492.1181-0.15241.491440.475-60.857-36.274
128.7747-4.1209-3.47078.64481.31942.2958-0.4569-1.23680.34531.3420.60050.68221.12110.5209-0.13231.943-0.30670.24621.83660.11421.727240.191-64.212-50.616
136.6743-0.053-1.50655.5937-2.1795.4882-0.64692.31750.4164-1.15390.5274-0.8578-1.1712-0.1535-0.17223.0469-0.13820.28081.89160.01911.358249.736-63.909-56.991
145.71970.1911.36492.17050.04596.61920.6766-0.0331-0.3224-0.88660.0422-0.03990.9545-0.231-0.91041.77420.06350.30021.83820.1151.588958.147-81.545-36.655
156.5067-0.16213.27494.2349-1.89044.62480.638-0.0023-0.2506-0.41050.1886-0.1153-1.195-1.5378-0.86441.61050.11370.47341.8981-0.04491.317652.652-72.649-33.074
160.81260.58920.12131.03050.79940.82580.1837-0.5306-1.6354-0.2391-0.21930.00692.11870.4225-0.00173.23631.595-0.73911.0377-0.12492.004578.129-114.874-54.426
172.05830.6195-1.07950.9920.07712.2146-0.875-0.03010.043-0.0684-0.79310.91310.6543-1.45490.27951.3145-1.80410.53212.3907-0.33091.895683.15-106.586-60.87
187.8399-2.33191.96678.4173-6.17544.52720.19110.73470.322-1.03320.35511.2621-0.4336-0.1337-0.88281.92860.01220.12692.02550.05371.857870.312-102.349-46.514
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1052.32711.16464.11082.67340.27886.970.1802-0.0135-0.34010.56460.1280.1403-0.12580.6527-0.45682.10420.04820.31861.5684-0.08532.003194.263-193.394-9.672
1068.1114-2.9283-3.46814.4879-3.29557.48960.84840.0566-0.6609-1.93610.1166-2.66270.9090.0623-1.08592.1241-0.5781-0.41151.2599-0.36471.7041107.777-195.302-0.542
1073.82992.2221.32012.7882-3.02559.7433-0.3545-0.98311.20530.2542-0.4593-1.2004-0.69340.1990.66242.10650.2158-0.19651.8533-0.55722.3472110.345-191.4449.816
1086.5976-1.465-2.86121.654-1.25284.0586-0.55160.4361-0.86871.1361-1.0282-1.88941.6433-0.23751.53852.454-0.00420.34791.58350.6214.0887-3.127-64.145-15.412
1098.9299-2.98281.16423.058-0.85477.87951.00360.3716-0.76781.3645-0.1097-0.4105-1.1833-1.3562-0.79662.1499-0.04040.51872.4040.56162.7946-0.873-57.041-20.134
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 4:342 )A4 - 342
2X-RAY DIFFRACTION2( CHAIN A AND RESID 343:834 )A343 - 834
3X-RAY DIFFRACTION3( CHAIN A AND RESID 835:1009 )A835 - 1009
4X-RAY DIFFRACTION4( CHAIN A AND RESID 1010:1132 )A1010 - 1132
5X-RAY DIFFRACTION5( CHAIN A AND RESID 1133:1346 )A1133 - 1346
6X-RAY DIFFRACTION6( CHAIN A AND RESID 1347:1544 )A1347 - 1544
7X-RAY DIFFRACTION7( CHAIN B AND RESID 6:80 )B6 - 80
8X-RAY DIFFRACTION8( CHAIN B AND RESID 81:104 )B81 - 104
9X-RAY DIFFRACTION9( CHAIN B AND RESID 105:148 )B105 - 148
10X-RAY DIFFRACTION10( CHAIN B AND ( RESID 149:240 OR RESID 301:301 ) )B149 - 240
11X-RAY DIFFRACTION10( CHAIN B AND ( RESID 149:240 OR RESID 301:301 ) )B301
12X-RAY DIFFRACTION11( CHAIN C AND RESID 2:28 )C2 - 28
13X-RAY DIFFRACTION12( CHAIN C AND RESID 29:66 )C29 - 66
14X-RAY DIFFRACTION13( CHAIN C AND RESID 67:112 )C67 - 112
15X-RAY DIFFRACTION14( CHAIN C AND RESID 113:169 )C113 - 169
16X-RAY DIFFRACTION15( CHAIN A AND RESID 1786:1786 ) OR ( CHAIN C AND RESID 170:207 )A1786
17X-RAY DIFFRACTION15( CHAIN A AND RESID 1786:1786 ) OR ( CHAIN C AND RESID 170:207 )C170 - 207
18X-RAY DIFFRACTION16( CHAIN D AND RESID 2:15 )D2 - 15
19X-RAY DIFFRACTION17( CHAIN D AND RESID 16:36 )D16 - 36
20X-RAY DIFFRACTION18( CHAIN D AND RESID 37:52 )D37 - 52
21X-RAY DIFFRACTION19( CHAIN D AND RESID 53:98 )D53 - 98
22X-RAY DIFFRACTION20( CHAIN D AND RESID 99:138 )D99 - 138
23X-RAY DIFFRACTION21( CHAIN D AND RESID 139:148 )D139 - 148
24X-RAY DIFFRACTION22( CHAIN D AND RESID 149:164 )D149 - 164
25X-RAY DIFFRACTION23( CHAIN D AND RESID 165:185 )D165 - 185
26X-RAY DIFFRACTION24( CHAIN D AND RESID 186:209 )D186 - 209
27X-RAY DIFFRACTION25( CHAIN E AND RESID 5:12 )E5 - 12
28X-RAY DIFFRACTION26( CHAIN E AND RESID 13:22 )E13 - 22
29X-RAY DIFFRACTION27( CHAIN E AND RESID 23:35 )E23 - 35
30X-RAY DIFFRACTION28( CHAIN E AND RESID 36:50 )E36 - 50
31X-RAY DIFFRACTION29( CHAIN E AND RESID 51:64 )E51 - 64
32X-RAY DIFFRACTION30( CHAIN E AND RESID 65:79 )E65 - 79
33X-RAY DIFFRACTION31( CHAIN E AND RESID 80:86 )E80 - 86
34X-RAY DIFFRACTION32( CHAIN E AND RESID 87:103 )E87 - 103
35X-RAY DIFFRACTION33( CHAIN E AND RESID 104:140 )E104 - 140
36X-RAY DIFFRACTION34( CHAIN E AND ( RESID 141:154 OR RESID 201:201 ) )E141 - 154
37X-RAY DIFFRACTION34( CHAIN E AND ( RESID 141:154 OR RESID 201:201 ) )E201
38X-RAY DIFFRACTION35( CHAIN F AND RESID 1:15 )F1 - 15
39X-RAY DIFFRACTION36( CHAIN F AND RESID 16:32 )F16 - 32
40X-RAY DIFFRACTION37( CHAIN F AND RESID 33:42 )F33 - 42
41X-RAY DIFFRACTION38( CHAIN F AND RESID 43:47 )F43 - 47
42X-RAY DIFFRACTION39( CHAIN F AND RESID 48:68 )F48 - 68
43X-RAY DIFFRACTION40( CHAIN F AND RESID 69:81 )F69 - 81
44X-RAY DIFFRACTION41( CHAIN F AND RESID 82:92 )F82 - 92
45X-RAY DIFFRACTION42( CHAIN F AND RESID 93:101 )F93 - 101
46X-RAY DIFFRACTION43( CHAIN G AND RESID 2:11 )G2 - 11
47X-RAY DIFFRACTION44( CHAIN G AND RESID 12:128 )G12 - 128
48X-RAY DIFFRACTION45( CHAIN G AND RESID 129:156 )G129 - 156
49X-RAY DIFFRACTION46( CHAIN H AND RESID 1:18 )H1 - 18
50X-RAY DIFFRACTION47( CHAIN H AND RESID 19:29 )H19 - 29
51X-RAY DIFFRACTION48( CHAIN H AND RESID 30:41 )H30 - 41
52X-RAY DIFFRACTION49( CHAIN H AND RESID 42:85 )H42 - 85
53X-RAY DIFFRACTION50( CHAIN H AND RESID 86:95 )H86 - 95
54X-RAY DIFFRACTION51( CHAIN H AND RESID 96:108 )H96 - 108
55X-RAY DIFFRACTION52( CHAIN H AND RESID 109:138 )H109 - 138
56X-RAY DIFFRACTION53( CHAIN I AND RESID 2:12 )I2 - 12
57X-RAY DIFFRACTION54( CHAIN I AND RESID 13:21 )I13 - 21
58X-RAY DIFFRACTION55( CHAIN I AND RESID 22:32 )I22 - 32
59X-RAY DIFFRACTION56( CHAIN I AND RESID 33:40 )I33 - 40
60X-RAY DIFFRACTION57( CHAIN I AND RESID 41:52 )I41 - 52
61X-RAY DIFFRACTION58( CHAIN I AND RESID 53:58 )I53 - 58
62X-RAY DIFFRACTION59( CHAIN I AND RESID 59:69 )I59 - 69
63X-RAY DIFFRACTION60( CHAIN I AND RESID 70:88 )I70 - 88
64X-RAY DIFFRACTION61( CHAIN I AND RESID 89:119 )I89 - 119
65X-RAY DIFFRACTION62( CHAIN I AND RESID 120:128 )I120 - 128
66X-RAY DIFFRACTION63( CHAIN J AND RESID 3:28 )J3 - 28
67X-RAY DIFFRACTION64( CHAIN J AND RESID 29:80 )J29 - 80
68X-RAY DIFFRACTION65( CHAIN J AND RESID 81:94 )J81 - 94
69X-RAY DIFFRACTION66( CHAIN J AND RESID 95:100 )J95 - 100
70X-RAY DIFFRACTION67( CHAIN K AND RESID 11:23 )K11 - 23
71X-RAY DIFFRACTION68( CHAIN K AND RESID 24:73 )K24 - 73
72X-RAY DIFFRACTION69( CHAIN K AND RESID 74:78 )K74 - 78
73X-RAY DIFFRACTION70( CHAIN K AND RESID 79:110 )K79 - 110
74X-RAY DIFFRACTION71( CHAIN K AND RESID 111:122 )K111 - 122
75X-RAY DIFFRACTION72( CHAIN K AND RESID 123:129 )K123 - 129
76X-RAY DIFFRACTION73( CHAIN L AND RESID 5:12 )L5 - 12
77X-RAY DIFFRACTION74( CHAIN L AND RESID 13:22 )L13 - 22
78X-RAY DIFFRACTION75( CHAIN L AND RESID 23:31 )L23 - 31
79X-RAY DIFFRACTION76( CHAIN L AND RESID 32:120 )L32 - 120
80X-RAY DIFFRACTION77( CHAIN L AND RESID 121:128 )L121 - 128
81X-RAY DIFFRACTION78( CHAIN M AND RESID 2:14 )M2 - 14
82X-RAY DIFFRACTION79( CHAIN M AND RESID 15:26 )M15 - 26
83X-RAY DIFFRACTION80( CHAIN M AND RESID 27:66 )M27 - 66
84X-RAY DIFFRACTION81( CHAIN M AND RESID 67:83 )M67 - 83
85X-RAY DIFFRACTION82( CHAIN M AND RESID 84:93 )M84 - 93
86X-RAY DIFFRACTION83( CHAIN M AND RESID 94:111 )M94 - 111
87X-RAY DIFFRACTION84( CHAIN M AND RESID 112:126 )M112 - 126
88X-RAY DIFFRACTION85( CHAIN N AND RESID 2:14 )N2 - 14
89X-RAY DIFFRACTION86( CHAIN N AND RESID 15:24 )N15 - 24
90X-RAY DIFFRACTION87( CHAIN N AND RESID 25:29 )N25 - 29
91X-RAY DIFFRACTION88( CHAIN N AND RESID 30:61 )N30 - 61
92X-RAY DIFFRACTION89( CHAIN O AND RESID 2:44 )O2 - 44
93X-RAY DIFFRACTION90( CHAIN O AND RESID 45:73 )O45 - 73
94X-RAY DIFFRACTION91( CHAIN O AND RESID 74:89 )O74 - 89
95X-RAY DIFFRACTION92( CHAIN P AND RESID 1:16 )P1 - 16
96X-RAY DIFFRACTION93( CHAIN P AND RESID 17:36 )P17 - 36
97X-RAY DIFFRACTION94( CHAIN P AND RESID 37:48 )P37 - 48
98X-RAY DIFFRACTION95( CHAIN P AND RESID 49:61 )P49 - 61
99X-RAY DIFFRACTION96( CHAIN P AND RESID 62:83 )P62 - 83
100X-RAY DIFFRACTION97( CHAIN R AND RESID 16:20 )R16 - 20
101X-RAY DIFFRACTION98( CHAIN R AND RESID 21:43 )R21 - 43
102X-RAY DIFFRACTION99( CHAIN R AND RESID 44:59 )R44 - 59
103X-RAY DIFFRACTION100( CHAIN R AND RESID 60:88 )R60 - 88
104X-RAY DIFFRACTION101( CHAIN S AND RESID 2:12 )S2 - 12
105X-RAY DIFFRACTION102( CHAIN S AND RESID 13:25 )S13 - 25
106X-RAY DIFFRACTION103( CHAIN S AND RESID 26:30 )S26 - 30
107X-RAY DIFFRACTION104( CHAIN S AND RESID 31:81 )S31 - 81
108X-RAY DIFFRACTION105( CHAIN T AND RESID 8:46 )T8 - 46
109X-RAY DIFFRACTION106( CHAIN T AND RESID 47:75 )T47 - 75
110X-RAY DIFFRACTION107( CHAIN T AND RESID 76:106 )T76 - 106
111X-RAY DIFFRACTION108( CHAIN U AND RESID 2:8 )U2 - 8
112X-RAY DIFFRACTION109( CHAIN U AND ( RESID 9:25 OR RESID 101:101 ) )U9 - 25
113X-RAY DIFFRACTION109( CHAIN U AND ( RESID 9:25 OR RESID 101:101 ) )U101

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