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- PDB-7nev: Structure of the hemiacetal complex between the SARS-CoV-2 Main P... -

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Basic information

Entry
Database: PDB / ID: 7nev
TitleStructure of the hemiacetal complex between the SARS-CoV-2 Main Protease and Leupeptin
Components
  • 3C-like proteinase
  • LEUPEPTIN
KeywordsPEPTIDE BINDING PROTEIN / SARS-CoV-2 / mPro / COVID-!9
Function / homology
Function and homology information


protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs ...protein guanylyltransferase activity / RNA endonuclease activity, producing 3'-phosphomonoesters / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / TRAF3-dependent IRF activation pathway / snRNP Assembly / Replication of the SARS-CoV-2 genome / double membrane vesicle viral factory outer membrane / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / SARS coronavirus main proteinase / host cell endosome / 3'-5'-RNA exonuclease activity / : / host cell endoplasmic reticulum-Golgi intermediate compartment / symbiont-mediated suppression of host toll-like receptor signaling pathway / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / SARS-CoV-2 modulates host translation machinery / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / copper ion binding / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. ...RNA-dependent RNA polymerase, SARS-CoV-like / Nonstructural protein 14, betacoronavirus / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / NSP12 RNA-dependent RNA polymerase, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidovirus 2-O-methyltransferase / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nonstructural protein 13, 1B domain, coronavirus / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerization / Nonstructural protein 15, middle domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Lipocalin signature. / Non-structural protein NSP3, SUD-N (Mac2) domain, betacoronavirus / Sarbecovirus Nsp3c-N domain profile. / Non-structural protein NSP3, N-terminal, betacoronavirus / Polyprotein cleavage domain PL2pro superfamily, betacoronavirus / Non-structural protein NSP3, SUD-N (Mac2) domain superfamily, betacoronavirus / Betacoronavirus SUD-C domain / Betacoronavirus replicase NSP3, N-terminal / NSP1 globular domain superfamily, betacoronavirus / Non-structural protein 2, SARS-CoV-like / Carbamoyl-phosphate synthase subdomain signature 2. / Coronavirus 3Ecto domain profile. / : / Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile. / NSP1, C-terminal domain, betacoronavirus / Betacoronavirus Nsp3c-M domain profile. / NSP1, globular domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain, betacoronavirus / Non-structural protein NSP3, SUD-M domain superfamily, betacoronavirus / Betacoronavirus replicase NSP1 / Betacoronavirus single-stranded poly(A) binding domain / Betacoronavirus (BetaCoV) Nsp1 C-terminal domain profile. / Betacoronavirus Nsp3c-C domain profile. / Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain profile. / DPUP/SUD, C-terminal, betacoronavirus / Non-structural protein NSP3, nucleic acid-binding domain superfamily, betacoronavirus / Non-structural protein 6, betacoronavirus / Betacoronavirus nucleic acid-binding (NAB) / Non-structural protein NSP3, nucleic acid-binding domain, betacoronavirus / Non-structural protein NSP3A domain-like superfamily / Papain-like protease, N-terminal domain superfamily, coronavirus / Papain-like viral protease, palm and finger domains, coronavirus / : / Coronavirus (CoV) Nsp2 middle domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / NSP1, globular domain, alpha/betacoronavirus / : / Coronavirus (CoV) Nsp3 Y domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus
Similarity search - Domain/homology
LEUPEPTIN / IMIDAZOLE / Replicase polyprotein 1ab
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
Streptomyces roseus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsGuenther, S. / Reinke, P.Y.A. / Oberthuer, D. / Yefanov, O. / Gelisio, L. / Ginn, H.M. / Lieske, J. / Domaracky, M. / Brehm, W. / Rahmani Mashhour, A. ...Guenther, S. / Reinke, P.Y.A. / Oberthuer, D. / Yefanov, O. / Gelisio, L. / Ginn, H.M. / Lieske, J. / Domaracky, M. / Brehm, W. / Rahmani Mashhour, A. / White, T.A. / Knoska, J. / Pena Esperanza, G. / Koua, F. / Tolstikova, A. / Groessler, M. / Fischer, P. / Hennicke, V. / Fleckenstein, H. / Trost, F. / Galchenkova, M. / Gevorkov, Y. / Li, C. / Awel, S. / Xavier, P.L. / Ullah, N. / Andaleeb, H. / Falke, S. / Alves Franca, B. / Schwinzer, M. / Brognaro, H. / Werner, N. / Perbandt, M. / Tidow, H. / Seychell, B. / Beck, T. / Meier, S. / Zaitsev-Doyle, J.J. / Rogers, C. / Gieseler, H. / Melo, D. / Monteiro, D.C.F. / Dunkel, I. / Lane, T.J. / Peck, A. / Saouane, S. / Hakanpaeae, J. / Meyer, J. / Noei, H. / Gribbon, P. / Ellinger, B. / Kuzikov, M. / Wolf, M. / Zhang, L. / Ehrt, C. / Pletzer-Zelgert, J. / Wollenhaupt, J. / Feiler, C. / Weiss, M. / Schluenzen, F. / Schulz, E.C. / Mehrabi, P. / Norton-Baker, B. / Schmidt, C. / Lorenzen, K. / Schubert, R. / Sun, X. / Han, H. / Chari, A. / Fernandez Garcia, Y. / Turk, D. / Hilgenfeld, R. / Rarey, M. / Zaliani, A. / Chapman, H.N. / Pearson, A. / Betzel, C. / Meents, A.
Funding support Germany, European Union, 2items
OrganizationGrant numberCountry
German Research Foundation (DFG)EXC 2056 - project ID 390715994 Germany
European CommissionEU project 101003551 - EXSCALATE4CoV (E4C)European Union
Citation
Journal: Science / Year: 2021
Title: X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease.
Authors: Gunther, S. / Reinke, P.Y.A. / Fernandez-Garcia, Y. / Lieske, J. / Lane, T.J. / Ginn, H.M. / Koua, F.H.M. / Ehrt, C. / Ewert, W. / Oberthuer, D. / Yefanov, O. / Meier, S. / Lorenzen, K. / ...Authors: Gunther, S. / Reinke, P.Y.A. / Fernandez-Garcia, Y. / Lieske, J. / Lane, T.J. / Ginn, H.M. / Koua, F.H.M. / Ehrt, C. / Ewert, W. / Oberthuer, D. / Yefanov, O. / Meier, S. / Lorenzen, K. / Krichel, B. / Kopicki, J.D. / Gelisio, L. / Brehm, W. / Dunkel, I. / Seychell, B. / Gieseler, H. / Norton-Baker, B. / Escudero-Perez, B. / Domaracky, M. / Saouane, S. / Tolstikova, A. / White, T.A. / Hanle, A. / Groessler, M. / Fleckenstein, H. / Trost, F. / Galchenkova, M. / Gevorkov, Y. / Li, C. / Awel, S. / Peck, A. / Barthelmess, M. / Schlunzen, F. / Lourdu Xavier, P. / Werner, N. / Andaleeb, H. / Ullah, N. / Falke, S. / Srinivasan, V. / Franca, B.A. / Schwinzer, M. / Brognaro, H. / Rogers, C. / Melo, D. / Zaitseva-Doyle, J.J. / Knoska, J. / Pena-Murillo, G.E. / Mashhour, A.R. / Hennicke, V. / Fischer, P. / Hakanpaa, J. / Meyer, J. / Gribbon, P. / Ellinger, B. / Kuzikov, M. / Wolf, M. / Beccari, A.R. / Bourenkov, G. / von Stetten, D. / Pompidor, G. / Bento, I. / Panneerselvam, S. / Karpics, I. / Schneider, T.R. / Garcia-Alai, M.M. / Niebling, S. / Gunther, C. / Schmidt, C. / Schubert, R. / Han, H. / Boger, J. / Monteiro, D.C.F. / Zhang, L. / Sun, X. / Pletzer-Zelgert, J. / Wollenhaupt, J. / Feiler, C.G. / Weiss, M.S. / Schulz, E.C. / Mehrabi, P. / Karnicar, K. / Usenik, A. / Loboda, J. / Tidow, H. / Chari, A. / Hilgenfeld, R. / Uetrecht, C. / Cox, R. / Zaliani, A. / Beck, T. / Rarey, M. / Gunther, S. / Turk, D. / Hinrichs, W. / Chapman, H.N. / Pearson, A.R. / Betzel, C. / Meents, A.
History
DepositionFeb 5, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 3, 2021Provider: repository / Type: Initial release
Revision 1.1Apr 14, 2021Group: Database references / Source and taxonomy / Structure summary
Category: citation / citation_author ...citation / citation_author / entity / entity_name_com / entity_src_gen
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity_name_com.name / _entity_src_gen.gene_src_common_name
Revision 1.2May 19, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.name
Revision 1.3Jan 31, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model
Item: _citation.journal_id_ISSN / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 3C-like proteinase
B: LEUPEPTIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,6728
Polymers34,2552
Non-polymers4176
Water10,395577
1
A: 3C-like proteinase
B: LEUPEPTIN
hetero molecules

A: 3C-like proteinase
B: LEUPEPTIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,34416
Polymers68,5104
Non-polymers83412
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area6690 Å2
ΔGint-27 kcal/mol
Surface area25110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.811, 52.682, 46.230
Angle α, β, γ (deg.)90.000, 102.783, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Components on special symmetry positions
IDModelComponents
11A-406-

CL

21A-810-

HOH

31A-862-

HOH

41A-1014-

HOH

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Components

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Protein / Protein/peptide , 2 types, 2 molecules AB

#1: Protein 3C-like proteinase / 3CL-PRO / 3CLp / Main protease / Mpro / Non-structural protein 5 / nsp5 / SARS coronavirus main proteinase


Mass: 33825.547 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: rep, 1a-1b / Production host: Escherichia coli (E. coli)
References: UniProt: P0DTD1, SARS coronavirus main proteinase
#2: Protein/peptide LEUPEPTIN / /


Type: Oligopeptide / Class: Enzyme inhibitor / Mass: 429.578 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Streptomyces roseus (bacteria) / References: LEUPEPTIN

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Non-polymers , 4 types, 583 molecules

#3: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#4: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#5: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 577 / Source method: isolated from a natural source / Formula: H2O

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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: 1.97 Å3/Da / Density % sol: 37.68 %
Crystal growTemperature: 291 K / Method: vapor diffusion
Details: Co-crystallization with the compounds was achieved by equilibrating a 6.25 mg/ml protein solution in 20 mM HEPES buffer (pH 7.8) containing 1 mM DTT, 1 mMEDTA, and 150 mM NaCl against a ...Details: Co-crystallization with the compounds was achieved by equilibrating a 6.25 mg/ml protein solution in 20 mM HEPES buffer (pH 7.8) containing 1 mM DTT, 1 mMEDTA, and 150 mM NaCl against a reservoir solution of 100 mM MIB, pH 7.5, containing 25% w/w PEG 1500 and 5% v/v DMSO. Prior to crystallization compound solutions in DMSO were dried onto the wells of SwissCI 96-well plates. To obtain well-diffracting crystals in a reproducible way seeding was applied for crystal growth. Crystals appeared within a few hours and reached their final size after 2 - 3 days. Crystals were manually harvested and flash-frozen in liquid nitrogen for subsequent X-ray diffraction data collection.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Apr 9, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 1.69→31.28 Å / Num. obs: 29274 / % possible obs: 97.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 17.23 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.067 / Net I/σ(I): 10.2
Reflection shellResolution: 1.69→1.73 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.528 / Mean I/σ(I) obs: 1.7 / Num. unique obs: 2106 / CC1/2: 0.53 / % possible all: 96.5

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Processing

Software
NameVersionClassification
PHENIX1.19_4092refinement
XDSdata reduction
DIALSdata reduction
DIALSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6YNQ

6ynq


Resolution: 1.7→23.8 Å / SU ML: 0.2025 / Cross valid method: FREE R-VALUE / σ(F): 1.4 / Phase error: 24.5517
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2336 1439 5.01 %
Rwork0.1832 27304 -
obs0.1856 28743 97.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 21.9 Å2
Refinement stepCycle: LAST / Resolution: 1.7→23.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2334 0 36 577 2947
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00242478
X-RAY DIFFRACTIONf_angle_d0.56133364
X-RAY DIFFRACTIONf_chiral_restr0.0421379
X-RAY DIFFRACTIONf_plane_restr0.0058436
X-RAY DIFFRACTIONf_dihedral_angle_d5.952336
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.760.34391490.2962660X-RAY DIFFRACTION95.8
1.76-1.830.2921580.26052659X-RAY DIFFRACTION96.05
1.83-1.910.29121390.24062667X-RAY DIFFRACTION96.29
1.91-2.020.27871540.21762711X-RAY DIFFRACTION96.82
2.02-2.140.24881380.19342690X-RAY DIFFRACTION97.58
2.14-2.310.25181460.19382748X-RAY DIFFRACTION97.41
2.31-2.540.2491190.19182762X-RAY DIFFRACTION98.16
2.54-2.910.26481250.1872779X-RAY DIFFRACTION98.17
2.91-3.660.1961570.15952780X-RAY DIFFRACTION98.89
3.66-23.80.18931540.14192848X-RAY DIFFRACTION99.17
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)
11.0440890108-0.1858130565620.2202850123630.363173619363-0.2352470907050.2180741970690.0230425054627-0.0482504847826-0.05054577857460.0087200215171-0.01128642483450.08161786687170.0301663849971-0.00693847440559-0.01785391464470.09682920548960.000688267455954-0.01547670864220.07858819700810.001352063869950.05050460988967.4727478633-10.486201384210.1830532406
20.544262127498-0.126401287005-0.1626580297640.927928756978-0.1711989129490.117742479791-0.0133105405566-0.1846232445130.1945612077020.4114057438060.103454675060.0406063235516-0.271589492762-0.02433416869210.06448902666710.215883540116-0.0007701489524430.01215305958090.1800381537810.02903438679590.13781792823715.0479852866-11.585018920728.4662722548
31.21249472694-0.262456014430.2195573339011.47571514997-0.7917451222761.098401790290.006134424710790.03129028378420.022872609438-0.101086930736-0.05598523732060.01489345225670.09051028916050.0374269270084-0.0109498922770.05453346391790.003736127954430.0003063756160710.08016727175920.006633425324580.030122986105311.6305924014-7.54335221529.59079717852
40.542826888221-0.2066201113440.2584970843340.681992330397-0.6825479703682.25940742901-0.035904541293-0.07825930188710.1196866205720.1368846327610.0105356492415-0.0942421519333-0.3116864445190.034400327814-0.04467644578180.0791831976435-0.0261208951162-0.008681691901460.1039991365040.02806404527320.14238792084614.72744770029.065458654645.1761676399
50.4128196099340.0193725376358-0.4398077150490.729025173939-0.5137914836870.873461410662-0.01174325677150.1052242824740.254559889122-0.00346593984332-0.132574459355-0.140864669222-0.1056204370770.190562509238-0.0003082751725180.171314412693-0.00783272507374-0.009488127854960.157273192560.07130249189780.27494349733115.997624042817.8356406448-11.4680196158
60.4605513295340.04381035463880.2885319725480.0576279753935-0.01366809457190.281183516990.0656853741078-0.09206954802540.3705753809830.0777416401027-0.01873696232880.231350339694-0.217004248944-0.0964955186186-0.03804406481490.1635826193220.0131919354390.04559624387640.1028997606920.05879954842210.257966894458.3576347761720.015783677-7.3974821961
71.02181546050.186425209579-0.06287404832780.3658395044850.2253990903040.172432266017-0.1338115745640.226501283572-0.223953929638-0.2580224180840.07145128796170.2322359554990.326926062751-0.0124455784122-0.1315456904490.335287467671-0.02987418171830.01865931644270.1596548335460.0192058096440.2006525874669.378710213950.432911790897-10.4722742067
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Auth asym-ID: A

IDRefine TLS-IDSelection detailsLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 1 through 43 )A1 - 431 - 43
22chain 'A' and (resid 44 through 69 )A44 - 6944 - 69
33chain 'A' and (resid 70 through 180 )A70 - 18070 - 180
44chain 'A' and (resid 181 through 213 )A181 - 213181 - 213
55chain 'A' and (resid 214 through 260 )A214 - 260214 - 260
66chain 'A' and (resid 261 through 292 )A261 - 292261 - 292
77chain 'A' and (resid 293 through 303 )A - D293 - 801293

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