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- PDB-7a18: 50S Deinococcus radiodurans ribosome bounded with mycinamicin IV -

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Basic information

Entry
Database: PDB / ID: 7a18
Title50S Deinococcus radiodurans ribosome bounded with mycinamicin IV
Components
  • (50S ribosomal protein ...) x 26
  • RNA (122-MER)
  • RNA (2699-MER)
KeywordsANTIBIOTIC / Complex / NPET / Macrolide / A2058
Function / homology
Function and homology information


large ribosomal subunit / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / tRNA binding / cytoplasmic translation / rRNA binding / negative regulation of translation / ribosome ...large ribosomal subunit / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / tRNA binding / cytoplasmic translation / rRNA binding / negative regulation of translation / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / mRNA binding / RNA binding / metal ion binding / cytoplasm
Similarity search - Function
Ribosomal protein L25, long-form / Ribosomal protein L25, beta domain / Ribosomal protein L25, C-terminal / Ribosomal protein TL5, C-terminal domain / Ribosomal protein L16 signature 1. / : / Ribosomal protein L16, conserved site / Ribosomal protein L16 signature 2. / Ribosomal protein L17 signature. / Ribosomal L25p family ...Ribosomal protein L25, long-form / Ribosomal protein L25, beta domain / Ribosomal protein L25, C-terminal / Ribosomal protein TL5, C-terminal domain / Ribosomal protein L16 signature 1. / : / Ribosomal protein L16, conserved site / Ribosomal protein L16 signature 2. / Ribosomal protein L17 signature. / Ribosomal L25p family / Ribosomal protein L25 / Ribosomal protein L28/L24 superfamily / Ribosomal protein L25/Gln-tRNA synthetase, N-terminal / Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily / Ribosomal protein L32p, bacterial type / Ribosomal protein L28 / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L5, bacterial-type / Ribosomal protein L18, bacterial-type / Ribosomal protein L6, bacterial-type / Ribosomal protein L19, conserved site / Ribosomal protein L19 signature. / Ribosomal protein L20 signature. / Ribosomal protein L27, conserved site / Ribosomal protein L27 signature. / Ribosomal protein L14P, bacterial-type / Ribosomal protein L34, conserved site / Ribosomal protein L34 signature. / Ribosomal protein L22, bacterial/chloroplast-type / Ribosomal protein L2, bacterial/organellar-type / Ribosomal protein L35 / Ribosomal protein L35 superfamily / Ribosomal protein L35 / Ribosomal L28 family / Ribosomal protein L33 / Ribosomal protein L33 / Ribosomal protein L28/L24 / Ribosomal protein L18 / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / Ribosomal protein L33 superfamily / Ribosomal protein L30, bacterial-type / : / Ribosomal protein L16 / L28p-like / Ribosomal protein L20 / Ribosomal protein L20 / Ribosomal protein L20, C-terminal / Ribosomal protein L21 / Ribosomal protein L27 / Ribosomal L27 protein / Ribosomal protein L19 / Ribosomal protein L19 superfamily / Ribosomal protein L19 / Ribosomal proteins 50S L24/mitochondrial 39S L24 / Ribosomal protein L17 / Ribosomal protein L17 superfamily / Ribosomal protein L17 / Ribosomal protein L21-like / L21-like superfamily / Ribosomal prokaryotic L21 protein / Ribosomal L32p protein family / Ribosomal protein L24 / Ribosomal protein L32p / Ribosomal protein L34 / Ribosomal protein L34 / Ribosomal protein L13, bacterial-type / Ribosomal protein L3, bacterial/organelle-type / Ribosomal protein L15, bacterial-type / 50S ribosomal protein uL4 / Ribosomal protein L23/L25, conserved site / Ribosomal protein L23 signature. / Ribosomal protein L2 signature. / Ribosomal protein L29, conserved site / Ribosomal protein L29 signature. / : / Ribosomal protein L2, conserved site / Ribosomal protein L15, conserved site / Ribosomal protein L15 signature. / Ribosomal protein L5, N-terminal / Ribosomal protein L5 / Ribosomal protein L5, C-terminal / ribosomal L5P family C-terminus / Ribosomal protein L5 / Ribosomal protein L5 domain superfamily / Ribosomal protein L10e/L16 / Ribosomal protein L10e/L16 superfamily / Ribosomal protein L16p/L10e / Ribosomal protein L6, alpha-beta domain / Ribosomal protein L6 / Ribosomal protein L6 / Ribosomal protein L6, alpha-beta domain superfamily / Ribosomal protein L2, domain 3 / Ribosomal protein L13, conserved site / Ribosomal protein L13 signature. / Ribosomal protein L14P, conserved site / Ribosomal protein L14 signature.
Similarity search - Domain/homology
MYCINAMICIN IV / SPERMIDINE / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein bL28 / Large ribosomal subunit protein bL34 ...MYCINAMICIN IV / SPERMIDINE / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein bL28 / Large ribosomal subunit protein bL34 / Large ribosomal subunit protein bL17 / Large ribosomal subunit protein uL15 / Large ribosomal subunit protein uL30 / Large ribosomal subunit protein uL18 / Large ribosomal subunit protein uL6 / Large ribosomal subunit protein bL33 / Large ribosomal subunit protein bL35 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein bL19 / Large ribosomal subunit protein bL25 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein uL24 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL29 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein uL23 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein bL21 / Large ribosomal subunit protein bL27
Similarity search - Component
Biological speciesDeinococcus radiodurans R1 (radioresistant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsBreiner, E. / Eyal, Z. / Matzov, D. / Halfon, Y. / Cimicata, G. / Rozenberg, H. / Zimmerman, E. / Bashan, A. / Yonath, A.
Funding support United States, 2items
OrganizationGrant numberCountry
European Research Council (ERC)322581
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM118101 United States
CitationJournal: Nucleic Acids Res. / Year: 2021
Title: Ribosome-binding and anti-microbial studies of the mycinamicins, 16-membered macrolide antibiotics from Micromonospora griseorubida.
Authors: Breiner-Goldstein, E. / Eyal, Z. / Matzov, D. / Halfon, Y. / Cimicata, G. / Baum, M. / Rokney, A. / Ezernitchi, A.V. / Lowell, A.N. / Schmidt, J.J. / Rozenberg, H. / Zimmerman, E. / Bashan, ...Authors: Breiner-Goldstein, E. / Eyal, Z. / Matzov, D. / Halfon, Y. / Cimicata, G. / Baum, M. / Rokney, A. / Ezernitchi, A.V. / Lowell, A.N. / Schmidt, J.J. / Rozenberg, H. / Zimmerman, E. / Bashan, A. / Valinsky, L. / Anzai, Y. / Sherman, D.H. / Yonath, A.
History
DepositionAug 12, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 6, 2021Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 31, 2024Group: 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
X: RNA (2699-MER)
Y: RNA (122-MER)
A: 50S ribosomal protein L2
B: 50S ribosomal protein L3
C: 50S ribosomal protein L4
D: 50S ribosomal protein L5
E: 50S ribosomal protein L6
G: 50S ribosomal protein L13
H: 50S ribosomal protein L14
I: 50S ribosomal protein L15
J: 50S ribosomal protein L16
K: 50S ribosomal protein L17
L: 50S ribosomal protein L18
M: 50S ribosomal protein L19
N: 50S ribosomal protein L20
O: 50S ribosomal protein L21
P: 50S ribosomal protein L22
Q: 50S ribosomal protein L23
R: 50S ribosomal protein L24
S: 50S ribosomal protein L25
T: 50S ribosomal protein L27
U: 50S ribosomal protein L28
V: 50S ribosomal protein L29
W: 50S ribosomal protein L30
Z: 50S ribosomal protein L32
1: 50S ribosomal protein L33
2: 50S ribosomal protein L34
3: 50S ribosomal protein L35
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,265,049313
Polymers1,256,60428
Non-polymers8,445285
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: mass spectrometry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)169.590, 410.128, 690.477
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number23
Space group name H-MI222

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Components

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RNA chain , 2 types, 2 molecules XY

#1: RNA chain RNA (2699-MER)


Mass: 875102.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Deinococcus radiodurans
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
#2: RNA chain RNA (122-MER)


Mass: 39276.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: GenBank: 11612676

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50S ribosomal protein ... , 26 types, 26 molecules ABCDEGHIJKLMNOPQRSTUVWZ123

#3: Protein 50S ribosomal protein L2


Mass: 29533.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ9
#4: Protein 50S ribosomal protein L3


Mass: 22033.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXK2
#5: Protein 50S ribosomal protein L4


Mass: 21147.004 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXK1
#6: Protein 50S ribosomal protein L5


Mass: 19834.211 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ0
#7: Protein 50S ribosomal protein L6


Mass: 18266.004 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSL3
#8: Protein 50S ribosomal protein L13


Mass: 15837.267 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXY1
#9: Protein 50S ribosomal protein L14


Mass: 14256.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ2
#10: Protein 50S ribosomal protein L15


Mass: 14798.907 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSK9
#11: Protein 50S ribosomal protein L16


Mass: 15343.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ5
#12: Protein 50S ribosomal protein L17


Mass: 12826.937 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSJ5
#13: Protein 50S ribosomal protein L18


Mass: 11098.696 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSL2
#14: Protein 50S ribosomal protein L19


Mass: 13446.456 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RWB4
#15: Protein 50S ribosomal protein L20


Mass: 13860.079 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSW7
#16: Protein 50S ribosomal protein L21


Mass: 10888.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RY64
#17: Protein 50S ribosomal protein L22


Mass: 14661.262 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ7
#18: Protein 50S ribosomal protein L23


Mass: 10336.936 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXK0
#19: Protein 50S ribosomal protein L24


Mass: 11770.651 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ1
#20: Protein 50S ribosomal protein L25 / General stress protein CTC


Mass: 19184.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RX88
#21: Protein 50S ribosomal protein L27


Mass: 7707.940 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RY65
#22: Protein 50S ribosomal protein L28


Mass: 8148.552 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RRG8
#23: Protein 50S ribosomal protein L29


Mass: 6257.213 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RXJ4
#24: Protein 50S ribosomal protein L30


Mass: 6079.235 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSL0
#25: Protein 50S ribosomal protein L32


Mass: 6508.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: P49228
#26: Protein/peptide 50S ribosomal protein L33


Mass: 5771.778 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSS4
#27: Protein/peptide 50S ribosomal protein L34


Mass: 5497.474 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSH2
#28: Protein 50S ribosomal protein L35


Mass: 7130.701 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: UniProt: Q9RSW6

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Non-polymers , 3 types, 285 molecules

#29: Chemical ChemComp-MIV / MYCINAMICIN IV


Mass: 695.880 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C37H61NO11 / Feature type: SUBJECT OF INVESTIGATION
#30: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 277 / Source method: obtained synthetically / Formula: Mg
#31: Chemical
ChemComp-SPD / SPERMIDINE / N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE / PA(34)


Mass: 145.246 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C7H19N3

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Details

Has ligand of interestY

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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: 4.78 Å3/Da / Density % sol: 74.25 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: Ribosome solution containing 0.0065 mM (180 A/ml) of D50S in 10 mM Hepes pH=7.8, 15 mM MgCl2 and 75 mM NH4Cl crystallization buffer was mixed with 10 mM spermidine, 1 % ethanol and 0.5 % 2- ...Details: Ribosome solution containing 0.0065 mM (180 A/ml) of D50S in 10 mM Hepes pH=7.8, 15 mM MgCl2 and 75 mM NH4Cl crystallization buffer was mixed with 10 mM spermidine, 1 % ethanol and 0.5 % 2-ethyl-1,3-hexanediol precipitants. A 0.005 ml crystallization drop was hanged over 10 % ethanol and 5% 2-ethyl-1,3-hexanediol in ddw reservoir.

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-3 / Wavelength: 0.968 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 11, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.968 Å / Relative weight: 1
ReflectionResolution: 3.3→50.074 Å / Num. obs: 344576 / % possible obs: 97.3 % / Redundancy: 5 % / Rmerge(I) obs: 0.295 / Rpim(I) all: 0.128 / Rrim(I) all: 0.323 / Χ2: 0.969 / Net I/σ(I): 7.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.3-3.363.80.92167170.4430.4831.0490.895.3
3.36-3.423.90.844167840.5640.4390.960.85395.7
3.42-3.4840.817169210.5620.420.9270.89496.2
3.48-3.554.10.748170400.5910.3820.8470.90896.7
3.55-3.634.20.666170750.6420.3350.7510.95697.2
3.63-3.724.30.604171760.6750.3010.680.98897.4
3.72-3.814.50.606171590.6990.2860.6761.01397.6
3.81-3.914.70.552173150.7110.2520.6111.04397.9
3.91-4.034.80.488173300.7540.2210.5391.03898.2
4.03-4.1650.455172940.7720.2020.5011.00298.2
4.16-4.315.20.417173830.7840.1790.4561.02998.5
4.31-4.485.30.372173440.7920.1560.4061.03698.3
4.48-4.685.40.342174170.8180.1420.3721.04398.2
4.68-4.935.50.316173980.8210.1310.3441.05798.5
4.93-5.245.50.292173450.8450.1220.3181.06598
5.24-5.645.40.277171950.8380.1170.3021.04796.6
5.64-6.214.70.245168380.8380.1060.2690.90694.7
6.21-7.16.20.253173990.8550.0980.2730.98897.5
7.1-8.946.40.231176550.880.0890.2490.9198.3
8.94-506.30.202177910.8330.0840.220.73896.6

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX1.15.2_3472refinement
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
PHENIX1.12_2829phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3PIO

3pio


Resolution: 3.4→50 Å / SU ML: 0.52 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 36.1 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3182 15317 4.97 %
Rwork0.2837 292596 -
obs0.2854 307913 93.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 318.72 Å2 / Biso mean: 109.0173 Å2 / Biso min: 36.74 Å2
Refinement stepCycle: final / Resolution: 3.4→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23436 60533 396 0 84365
Biso mean--73.88 --
Num. residues----5916
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.4-3.43860.38485090.3484924990
3.4386-3.47910.37384520.3378933390
3.4791-3.52150.3654800.3365936891
3.5215-3.56610.37464960.3334934291
3.5661-3.6130.37255070.3213943292
3.613-3.66240.3384920.3207952892
3.6624-3.71470.36955260.3221956893
3.7147-3.77020.34144860.3147962893
3.7702-3.82910.34014940.3125954393
3.8291-3.89180.31415240.3093960993
3.8918-3.95890.35815310.3097961793
3.9589-4.03090.37795190.3159972894
4.0309-4.10840.34555140.3084967994
4.1084-4.19220.35395370.3081971294
4.1922-4.28330.35414770.3027980595
4.2833-4.38290.32615400.2913975595
4.3829-4.49240.33655030.2954980394
4.4924-4.61380.32244860.2951987895
4.6138-4.74950.34935050.2916982195
4.7495-4.90260.31194950.2802991895
4.9026-5.07770.30795230.2781989295
5.0777-5.28080.33515660.2766988896
5.2808-5.52080.32834950.2758986495
5.5208-5.81150.30945440.2783980495
5.8115-6.1750.30814720.279979893
6.175-6.65080.28594730.2492994895
6.6508-7.31820.28035210.25151032698
7.3182-8.37290.27995710.24521022098
8.3729-10.53280.27325370.23891029097
10.5328-500.27595420.26351025094
Refinement TLS params.Method: refined / Origin x: 43.6159 Å / Origin y: 128.6647 Å / Origin z: 108.6528 Å
111213212223313233
T0.6405 Å2-0.1146 Å2-0.08 Å2-0.7889 Å20.3154 Å2--0.5533 Å2
L0.7222 °20.0198 °20.0018 °2-0.2832 °2-0.0533 °2--0.6711 °2
S-0.0262 Å °0.4951 Å °0.2654 Å °-0.2151 Å °0.0156 Å °0.086 Å °-0.1067 Å °0.1329 Å °-0.0581 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allX1 - 2877
2X-RAY DIFFRACTION1allX2901
3X-RAY DIFFRACTION1allY2 - 123
4X-RAY DIFFRACTION1allA2 - 272
5X-RAY DIFFRACTION1allB1 - 206
6X-RAY DIFFRACTION1allC2 - 196
7X-RAY DIFFRACTION1allD2 - 177
8X-RAY DIFFRACTION1allE5 - 175
9X-RAY DIFFRACTION1allG30 - 171
10X-RAY DIFFRACTION1allH1 - 134
11X-RAY DIFFRACTION1allI1 - 137
12X-RAY DIFFRACTION1allJ6 - 139
13X-RAY DIFFRACTION1allK1 - 115
14X-RAY DIFFRACTION1allL8 - 111
15X-RAY DIFFRACTION1allM2 - 119
16X-RAY DIFFRACTION1allN2 - 118
17X-RAY DIFFRACTION1allO1 - 98
18X-RAY DIFFRACTION1allP6 - 134
19X-RAY DIFFRACTION1allQ2 - 94
20X-RAY DIFFRACTION1allR4 - 113
21X-RAY DIFFRACTION1allS1 - 175
22X-RAY DIFFRACTION1allT12 - 83
23X-RAY DIFFRACTION1allU6 - 79
24X-RAY DIFFRACTION1allV13 - 66
25X-RAY DIFFRACTION1allW1 - 55
26X-RAY DIFFRACTION1allZ3 - 59
27X-RAY DIFFRACTION1all16 - 54
28X-RAY DIFFRACTION1all21 - 46
29X-RAY DIFFRACTION1all32 - 64
30X-RAY DIFFRACTION1all61 - 367
31X-RAY DIFFRACTION1all71 - 7

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