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- PDB-7a0s: 50S Deinococcus radiodurans ribosome bounded with mycinamicin I -

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Basic information

Entry
Database: PDB / ID: 7a0s
Title50S Deinococcus radiodurans ribosome bounded with mycinamicin I
Components
  • (50S ribosomal protein ...) x 26
  • RNA (122-MER)
  • RNA (2732-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
ETHANOL / : / mycinamicin I / SPERMIDINE / : / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) ...ETHANOL / : / mycinamicin I / 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: 3.22 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 10, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 18, 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 (2732-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)1,337,466416
Polymers1,325,89128
Non-polymers11,575388
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)169.995, 410.736, 697.778
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 (2732-MER)


Mass: 933429.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Deinococcus radiodurans R1 (radioresistant)
References: GenBank: 1026245073
#2: RNA chain RNA (122-MER)


Mass: 39605.695 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: 29976.580 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: 22308.156 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: 19992.455 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: 15966.381 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: 15543.239 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: 12926.067 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: 18347.818 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: 10980.562 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: 15190.869 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: 9609.091 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: 7073.173 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: 6579.690 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: 5626.587 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 , 8 types, 388 molecules

#29: Chemical ChemComp-QU2 / mycinamicin I / (1~{R},2~{R},3~{R},6~{E},8~{S},9~{S},10~{S},12~{R},14~{E},16~{R})-2-[[(2~{R},3~{R},4~{R},5~{R},6~{R})-3,4-dimethoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxymethyl]-9-[(2~{S},3~{R},4~{S},6~{R})-4-(dimethylamino)-6-methyl-3-oxidanyl-oxan-2-yl]oxy-3-ethyl-8,10,12-trimethyl-4,17-dioxabicyclo[14.1.0]heptadeca-6,14-diene-5,13-dione


Mass: 711.880 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C37H61NO12 / Feature type: SUBJECT OF INVESTIGATION
#30: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 367 / 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.: 8 / Source method: obtained synthetically / Formula: C7H19N3
#32: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#33: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#34: Chemical ChemComp-EOH / ETHANOL


Mass: 46.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O
#35: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Ca
#36: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K

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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: 4.81 Å3/Da / Density % sol: 74.41 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop
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.
PH range: 7.8

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Feb 19, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.873 Å / Relative weight: 1
ReflectionResolution: 3.21→50 Å / Num. obs: 389019 / % possible obs: 99.6 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.182 / Rpim(I) all: 0.096 / Rrim(I) all: 0.207 / Χ2: 1.884 / Net I/σ(I): 4.7 / Num. measured all: 1739141
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.21-3.274.51.574193430.4480.8231.7841.03299.6
3.27-3.324.51.391193490.5040.7251.5751.04999.7
3.32-3.394.51.206193190.5860.6271.3651.06299.8
3.39-3.464.51.049193860.6690.5451.1871.09899.8
3.46-3.534.50.965193310.6950.5031.0931.13899.8
3.53-3.624.50.806193840.7620.4210.9131.1699.8
3.62-3.714.30.72191440.8010.3870.8211.22998.7
3.71-3.814.50.582193880.8720.3010.6581.27699.8
3.81-3.924.70.475194230.9120.2420.5351.30499.9
3.92-4.044.40.408194510.9270.2160.4641.39499.9
4.04-4.194.60.344194040.9490.1760.3881.51499.9
4.19-4.364.80.276194730.9680.1370.3091.66299.9
4.36-4.554.80.236194840.9740.1170.2651.80899.9
4.55-4.794.70.203194880.9780.1020.2282.07999.9
4.79-5.094.60.175194890.9820.0890.1972.33499.8
5.09-5.494.20.149194420.9830.080.172.66899.2
5.49-6.044.40.13195470.9870.0670.1472.93499.6
6.04-6.914.40.114195550.9880.0590.133.21199.6
6.91-8.74.30.093197200.990.0480.1053.82699.6
8.7-503.80.064198990.9950.0380.0754.56898.1

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Processing

Software
NameVersionClassification
PHENIX1.18_3845refinement
HKL-2000data scaling
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
PHENIX1.12_2829phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3PIO

3pio


Resolution: 3.22→49.67 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 30.39 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2534 19317 4.97 %
Rwork0.2237 369323 -
obs0.2252 388640 99.1 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 320.64 Å2 / Biso mean: 134.8461 Å2 / Biso min: 49.84 Å2
Refinement stepCycle: final / Resolution: 3.22→49.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23414 60533 539 0 84486
Biso mean--100.28 --
Num. residues----5920
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.22-3.250.40525550.3819106381119386
3.25-3.290.38686490.36671229912948100
3.29-3.330.35156040.35721237212976100
3.33-3.370.36286810.35661224312924100
3.37-3.420.3786260.34641236812994100
3.42-3.460.36656340.33481228912923100
3.46-3.510.3396290.33251229412923100
3.51-3.570.32016670.3081231912986100
3.57-3.620.34096160.29491236712983100
3.62-3.680.3066330.2811121511278499
3.68-3.750.30226170.2672122451286299
3.75-3.810.296720.25361231512987100
3.81-3.890.28546290.24731239713026100
3.89-3.970.27545940.23971239612990100
3.97-4.050.26246500.231237313023100
4.05-4.150.24566370.21561237213009100
4.15-4.250.23946170.2051237112988100
4.25-4.370.2516570.20321239013047100
4.37-4.490.22746200.20021237812998100
4.49-4.640.23726170.20011240113018100
4.64-4.80.22456780.19341238713065100
4.8-50.21686650.18261239413059100
5-5.220.21216620.17991235513017100
5.22-5.50.20136710.1778123121298399
5.5-5.840.2376240.18341243013054100
5.84-6.290.21886830.1876123931307699
6.29-6.920.23687110.19071242713138100
6.92-7.920.2277060.18521247613182100
7.92-9.970.23296520.202125571320999
9.97-49.670.22256610.2068126141327597
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)
10.45540.02940.01120.3097-0.0660.6562-0.06880.27540.1463-0.17720.06210.082-0.16430.14320.02550.547-0.2349-0.14382.17520.1970.480140.9725544.8278114.7711
20.0071-0.0570.03050.4621-0.17920.21130.02910.03390.0313-0.4613-0.1696-0.31140.01740.62520.14111.6747-0.17760.18693.65410.05940.954387.1495520.766733.7954
30.18990.27110.11721.16120.04120.169-0.0089-0.11820.2794-0.08410.0612-0.2865-0.1177-0.1463-0.05211.0672-0.5595-0.08631.91440.12461.029262.3117595.9091136.7098
40.46330.1696-0.10081.1286-0.19950.6562-0.0532-0.0723-0.27350.04770.0636-0.08670.12820.0668-0.00080.5403-0.01720.00232.10780.03320.661747.3582489.6091151.0791
50.1036-0.12350.12130.56910.09590.27510.26070.2202-0.1478-0.4207-0.05910.54270.0882-0.2659-0.17511.0874-0.1758-0.38392.67590.39741.1988-10.0706551.13877.2672
62.37340.13980.61771.8399-0.6880.4473-0.05280.2654-0.04120.045-0.6707-0.6187-0.21620.46260.71561.5852-0.33120.04284.29290.45361.4195118.7139546.098439.2601
70.9184-0.2389-0.29161.1014-0.3630.66450.0840.5764-0.5503-0.73550.02220.0970.44410.6339-0.10531.68820.44890.00552.399-0.43341.077782.1893459.5251116.3378
80.78470.25250.47110.6628-0.22850.5310.15710.2009-0.14580.0630.0320.08970.40520.2184-0.19580.907-0.15390.05732.0659-0.14190.678837.9955477.1317108.9169
90.7835-0.10970.35890.4686-0.06610.20620.0323-0.0491-0.14030.0799-0.0205-0.20940.0007-0.011-0.01490.54260.0906-0.0372.12860.15660.696983.7017511.9999158.6134
100.0398-0.096-0.0930.22660.21940.21290.29180.29330.068-0.5539-0.12890.3615-0.135-0.0885-0.16651.5715-0.0852-0.39372.79060.41951.037419.6696558.78256.9172
110.09770.0117-0.14890.5509-0.37720.4616-0.1266-0.0741-0.0074-0.40030.144-0.18150.63370.4282-0.01491.42650.07590.06953.5531-0.03780.889488.6438507.998580.4336
120.7720.09130.12020.2411-0.01660.0229-0.065-0.2534-0.00780.06130.1047-0.04810.01170.0096-0.04280.48340.02950.0141.94150.11260.555423.9383517.8779173.4621
130.0026-0.00010.00710.29830.02120.02060.06470.04490.0031-0.5964-0.1774-0.0714-0.0946-0.08660.10882.3495-0.20590.08283.16790.29950.849480.8737541.949217.1753
141.64390.4815-0.27740.96370.1710.1754-0.0592-0.3055-0.24170.04180.0754-0.31280.01950.1235-0.02640.58360.03680.03032.29460.18890.675765.246505.2842178.3013
150.13320.05850.16210.3928-0.35320.6857-0.01360.5311-0.1094-0.4930.18420.08320.34150.2759-0.20261.0298-0.246-0.22682.3165-0.1770.765420.6119495.063890.506
161.72180.95461.27012.59341.21871.0640.16830.2692-0.3966-0.5671-0.12480.46750.0766-0.1827-0.05811.1785-0.4163-0.25642.6504-0.190.95418.8116491.007278.404
170.685-0.62540.30260.79-0.21190.15250.13740.0437-0.0562-0.32030.03770.48430.2178-0.0381-0.15760.6544-0.2011-0.17522.04080.14820.7764-1.8431517.6091133.5706
180.7085-0.13650.0491.76410.83581.7223-0.1644-0.0189-0.1309-0.0507-0.11341.0693-0.6347-0.71150.271.10770.5190.00171.96990.23061.4435-4.9116573.9686153.6052
190.56560.3768-0.74632.2466-0.61951.06870.1923-0.1129-0.1801-0.0446-0.12410.5468-0.14040.1509-0.06780.92660.1965-0.33852.66240.1761.3165-34.948550.4429117.7267
201.1690.35640.28680.58310.2090.7605-0.01730.5677-0.2713-0.53940.0478-0.1989-0.06480.3586-0.02531.93530.39650.2333.6024-0.30381.222494.4963490.850557.2931
210.195-0.2716-0.2270.74310.01281.91360.1446-0.0120.0258-0.48110.031-0.04370.31630.1987-0.1681.5663-0.27670.03422.8540.08160.729863.7457534.466847.8364
220.861-0.2495-0.0290.7590.2310.43930.22910.60040.5532-0.0537-0.2681-0.1221-0.73730.07050.04241.8254-0.3718-0.33941.94980.81711.411138.6988598.177196.7469
231.01540.6043-0.47820.3696-0.20011.21410.0619-0.24070.12370.01290.17390.2151-0.1812-0.2957-0.23591.26220.3019-0.06432.55-0.10111.8693-20.7919581.6707139.6217
240.3088-0.3050.1180.3396-0.17490.13410.2345-0.0023-0.1712-0.42980.10930.10250.1726-0.0974-0.34241.4816-0.2573-0.1962.9018-0.17480.815740.0437502.262859.7295
250.77050.0790.87781.1938-0.10451.0320.21330.01770.11950.12820.01570.48990.1616-0.9349-0.22720.5542-0.0652-0.03891.73060.09540.794912.5086510.4991145.8751
260.3485-0.1543-0.16580.1961-0.05780.4123-0.29080.27690.08680.01310.0172-0.04380.37410.31850.26981.8467-0.24650.14973.21280.47851.046171.2029571.873750.8121
271.20870.28690.98680.2353-0.09832.0308-0.04070.20060.2636-0.20720.1030.26680.09090.0801-0.05990.94660.1317-0.22671.81780.24450.868120.3891570.6519126.6845
280.27940.3209-0.37080.5925-0.26520.6069-0.25290.09310.0843-0.2559-0.1759-0.1734-0.00740.11190.41591.4791-0.3554-0.15992.98010.52080.930142.0876558.681961.2014
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain 'X' and resid 1 through 2877)X1 - 2877
2X-RAY DIFFRACTION2(chain 'Y' and resid 2 through 123)Y2 - 123
3X-RAY DIFFRACTION3(chain 'A' and resid 2 through 273)A2 - 273
4X-RAY DIFFRACTION4(chain 'B' and resid 1 through 206)B1 - 206
5X-RAY DIFFRACTION5(chain 'C' and resid 1 through 196)C1 - 196
6X-RAY DIFFRACTION6(chain 'D' and resid 3 through 179)D3 - 179
7X-RAY DIFFRACTION7(chain 'E' and resid 5 through 175)E5 - 175
8X-RAY DIFFRACTION8(chain 'G' and resid 30 through 171)G30 - 171
9X-RAY DIFFRACTION9(chain 'H' and resid 1 through 134)H1 - 134
10X-RAY DIFFRACTION10(chain 'I' and resid 1 through 137)I1 - 137
11X-RAY DIFFRACTION11(chain 'J' and resid 6 through 140)J6 - 140
12X-RAY DIFFRACTION12(chain 'K' and resid 1 through 115)K1 - 115
13X-RAY DIFFRACTION13(chain 'L' and resid 8 through 111)L8 - 111
14X-RAY DIFFRACTION14(chain 'M' and resid 2 through 119)M2 - 119
15X-RAY DIFFRACTION15(chain 'N' and resid 2 through 118)N2 - 118
16X-RAY DIFFRACTION16(chain 'O' and resid 1 through 98)O1 - 98
17X-RAY DIFFRACTION17(chain 'P' and resid 6 through 134)P6 - 134
18X-RAY DIFFRACTION18(chain 'Q' and resid 2 through 93)Q2 - 93
19X-RAY DIFFRACTION19(chain 'R' and resid 4 through 113)R4 - 113
20X-RAY DIFFRACTION20(chain 'S' and resid 1 through 175)S1 - 175
21X-RAY DIFFRACTION21(chain 'T' and resid 10 through 83)T10 - 83
22X-RAY DIFFRACTION22(chain 'U' and resid 6 through 79)U6 - 79
23X-RAY DIFFRACTION23(chain 'V' and resid 13 through 66)V13 - 66
24X-RAY DIFFRACTION24(chain 'W' and resid 1 through 55)W1 - 55
25X-RAY DIFFRACTION25(chain 'Z' and resid 3 through 59)Z3 - 59
26X-RAY DIFFRACTION26(chain '1' and resid 6 through 54)16 - 54
27X-RAY DIFFRACTION27(chain '2' and resid 1 through 46)21 - 46
28X-RAY DIFFRACTION28(chain '3' and resid 2 through 64)32 - 64

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