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- PDB-2j7q: Crystal structure of the ubiquitin-specific protease encoded by m... -

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Basic information

Entry
Database: PDB / ID: 2j7q
TitleCrystal structure of the ubiquitin-specific protease encoded by murine cytomegalovirus tegument protein M48 in complex with a ubquitin-based suicide substrate
Components
  • (MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, ...) x 2
  • UBIQUITIN
KeywordsHYDROLASE / HERPESVIRIDAE / NUCLEAR PROTEIN / COVALENT ENZYME-LIGAND COMPLEX / DEUBIQUITINATING ENZYME / PAPAIN-LIKE FOLD / CYSTEINE PROTEASE
Function / homology
Function and homology information


: / : / protein modification process => GO:0036211 / : / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency ...: / : / protein modification process => GO:0036211 / : / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / cytosolic ribosome / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / NF-kB is activated and signals survival / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Pexophagy / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by REV1 / TICAM1, RIP1-mediated IKK complex recruitment / Regulation of BACH1 activity / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Downregulation of TGF-beta receptor signaling / Translesion synthesis by POLI / Josephin domain DUBs / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of activated PAK-2p34 by proteasome mediated degradation / TNFR1-induced NF-kappa-B signaling pathway / TCF dependent signaling in response to WNT / Regulation of NF-kappa B signaling / activated TAK1 mediates p38 MAPK activation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Ubiquitin-dependent degradation of Cyclin D / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Fanconi Anemia Pathway / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulation of FGFR3 signaling / Peroxisomal protein import / TNFR2 non-canonical NF-kB pathway / Deactivation of the beta-catenin transactivating complex / Stabilization of p53 / Assembly of the pre-replicative complex / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Vpu mediated degradation of CD4 / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Cdc20:Phospho-APC/C mediated degradation of Cyclin A
Similarity search - Function
Cathepsin B; Chain A - #120 / Cathepsin B; Chain A / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / : / Ubiquitin domain signature. ...Cathepsin B; Chain A - #120 / Cathepsin B; Chain A / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
METHYL 4-AMINOBUTANOATE / Polyubiquitin-C / Ubiquitin-60S ribosomal protein L40
Similarity search - Component
Biological speciesMURINE CYTOMEGALOVIRUS (Murine cytomegalovirus)
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.8 Å
AuthorsSchlieker, C. / Weihofen, W.A. / Frijns, E. / Kattenhorn, L.M. / Gaudet, R. / Ploegh, H.L.
CitationJournal: Mol.Cell / Year: 2007
Title: Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
Authors: Schlieker, C. / Weihofen, W.A. / Frijns, E. / Kattenhorn, L.M. / Gaudet, R. / Ploegh, H.L.
History
DepositionOct 16, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 20, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Other / Refinement description
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / software / struct_conn
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.ptnr1_symmetry / _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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _software.name / _struct_conn.conn_type_id / _struct_conn.id / _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.ptnr1_symmetry / _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_conn.ptnr2_symmetry
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP
B: UBIQUITIN
C: MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP
D: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,99711
Polymers68,4034
Non-polymers5947
Water12,737707
1
A: MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP
B: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,5576
Polymers34,1972
Non-polymers3604
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
C: MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP
D: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)34,4405
Polymers34,2062
Non-polymers2343
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)40.907, 57.298, 67.279
Angle α, β, γ (deg.)73.37, 85.37, 88.54
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.9983, -0.05553, -0.0176), (-0.05542, -0.99844, 0.00712), (-0.01797, -0.00614, -0.99982)-0.22632, 0.2038, -0.5368
2given(0.99891, -0.04369, 0.0165), (-0.04364, -0.99904, -0.00344), (0.01663, 0.00272, -0.99986)-0.01119, -0.05838, -0.73378

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Components

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MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, ... , 2 types, 2 molecules AC

#1: Protein MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP


Mass: 25677.289 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: DEUBIQUITINATING MODULE OF MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48. ACTIVE SITE CYSTEINE 23 IS COVALENTLY LINKED TO THE FORMER VINYLMETHYLESTER MOIETY OF THE SUICIDE SUBSTATE UBVME
Source: (gene. exp.) MURINE CYTOMEGALOVIRUS (Murine cytomegalovirus)
Strain: MCMV STRAIN SMITH / Plasmid: PET28 (NOVAGEN) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
#3: Protein MCMV TEGUMENT PROTEIN M48 ENCODED UBIQUITIN- SPECIFIC PROTEASE, M48USP


Mass: 25686.316 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: DEUBIQUITINATING MODULE OF MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48. ACTIVE SITE CYSTEINE 23 IS COVALENTLY LINKED TO THE FORMER VINYLMETHYLESTER MOIETY OF THE SUICIDE SUBSTATE UBVME
Source: (gene. exp.) MURINE CYTOMEGALOVIRUS (Murine cytomegalovirus)
Strain: MCMV STRAIN SMITH / Plasmid: PET28 (NOVAGEN) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)

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Protein , 1 types, 2 molecules BD

#2: Protein UBIQUITIN


Mass: 8519.778 Da / Num. of mol.: 2
Fragment: UBIQUITIN FUSED TO VINYLMETHYLESTER, UBVME, RESIDUES 1-75
Source method: isolated from a genetically manipulated source
Details: THE C-TERMINAL GLY 76 IS REPLACED BY THE VINYLMETHYLESTER MOIETY
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PTYB (NEW ENGLAND BIOLABS) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62988, UniProt: P0CG48*PLUS

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Non-polymers , 5 types, 714 molecules

#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-GVE / METHYL 4-AMINOBUTANOATE


Type: peptide-like / Mass: 117.146 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H11NO2
#6: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 707 / Source method: isolated from a natural source / Formula: H2O

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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: 1.95 Å3/Da / Density % sol: 36.49 %
Crystal growpH: 7.5 / Details: 200 MM MAGNESIUM FORMATE, 14% PEG 3350, pH 7.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9797
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 31, 2006
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9797 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 52323 / % possible obs: 97.4 % / Observed criterion σ(I): 2 / Redundancy: 4.2 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 8.3
Reflection shellResolution: 1.8→1.86 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 3.5 / % possible all: 84.2

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
HKL2Mapphasing
RefinementMethod to determine structure: SAD / Resolution: 1.8→50 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.925 / SU B: 4.84 / SU ML: 0.079 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.128 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.214 1076 2 %RANDOM
Rwork0.156 ---
obs0.157 51609 97.4 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 10.21 Å2
Baniso -1Baniso -2Baniso -3
1-0.62 Å2-0.1 Å20.04 Å2
2---0.5 Å20.26 Å2
3----0.27 Å2
Refinement stepCycle: LAST / Resolution: 1.8→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4755 0 38 707 5500
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0224893
X-RAY DIFFRACTIONr_bond_other_d0.0010.023280
X-RAY DIFFRACTIONr_angle_refined_deg1.4421.9816628
X-RAY DIFFRACTIONr_angle_other_deg0.9393.0018003
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3555612
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.30723.805205
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.78115821
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.4451532
X-RAY DIFFRACTIONr_chiral_restr0.0870.2779
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.025378
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02966
X-RAY DIFFRACTIONr_nbd_refined0.2070.2949
X-RAY DIFFRACTIONr_nbd_other0.1990.23438
X-RAY DIFFRACTIONr_nbtor_refined0.1770.22395
X-RAY DIFFRACTIONr_nbtor_other0.0850.22501
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1680.2514
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.160.227
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2450.297
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1890.253
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.2571.53763
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.37924981
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.48832026
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.4624.51647
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.8→1.85 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.28 81
Rwork0.194 3690
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)
10.60890.11060.38951.1867-0.66591.6740.0052-0.00160.10880.17480.05930.1065-0.2354-0.0803-0.064500.02280.0269-0.02220.0023-0.0222-6.556416.3499-16.3688
22.54154.0853-1.581912.9931-5.87173.1041-0.01060.05880.03540.02660.27170.3502-0.108-0.3509-0.2611-0.03060.01330.03470.01420.0103-0.0292-14.4758.7138-13.591
30.98770.13810.07560.713-0.25830.69360.03780.0152-0.05280.0015-0.0372-0.04070.02770.034-0.0006-0.0405-0.0018-0.001-0.0287-0.01-0.04071.13571.8444-19.9135
40.6930.1339-0.08831.5166-0.19571.71670.00620.01060.13180.0468-0.0047-0.1381-0.14790.0733-0.0015-0.0123-0.02080.0004-0.0262-0.0029-0.01995.303416.0723-18.1917
55.423-15.54882.972451.41-10.33823.4062-0.0002-0.33850.72020.5234-0.2056-2.56240.00240.24330.2058-0.0283-0.0418-0.03870.0767-0.03940.116814.893911.2969-9.2347
60.83680.03850.32660.7148-0.07851.06120.02870.1499-0.0839-0.04950.03350.06720.0455-0.0431-0.0623-0.0331-0.0003-0.0005-0.0091-0.0143-0.0215-7.0331-0.872-27.8101
71.0621-0.114-0.46724.4957-1.26893.6978-0.0124-0.1613-0.0260.0158-0.0971-0.25340.30.19640.1095-0.00610.0085-0.0012-0.04070.0083-0.06287.6994-16.8115-4.1404
81.0369-0.7064-0.27386.5192-1.74432.57880.0278-0.0296-0.0531-0.7825-0.089-0.09610.44660.07450.06120.0763-0.00620.011-0.0550.0007-0.08275.7283-16.1304-12.6627
90.67560.1677-0.11551.0367-0.34751.22310.01990.0032-0.1068-0.08560.04490.05750.1648-0.0688-0.0648-0.0239-0.0111-0.0174-0.0221-0.0045-0.0205-7.9868-16.592416.1592
101.84580.2589-0.37323.2847-1.12251.22090.0210.10880.24640.00230.13610.24950.0126-0.2442-0.157-0.05270.0092-0.01890.02190.013-0.0034-14.3669-0.93868.8831
110.88680.0083-0.11740.8156-0.26410.54630.011-0.05390.06350.0267-0.0169-0.0549-0.01650.01740.0059-0.04470.005-0.0036-0.0309-0.0141-0.03662.1698-2.258920.8187
121.20640.0968-0.0060.75580.25251.4436-0.0093-0.0298-0.1331-0.04210.0206-0.10860.13040.0671-0.0112-0.01210.016-0.0023-0.04270.0019-0.01224.4878-16.428117.8167
130.9605-0.18470.17933.28720.10450.28940.05550.153-0.0156-0.2110.0263-0.36640.02620.1267-0.0818-0.03990.01550.01020.0079-0.02420.005410.5942-7.572910.8259
142.43861.28050.25691.73590.42791.48180.0976-0.29990.29280.1536-0.13710.1877-0.0199-0.11120.0394-0.03740.00470.01310.0008-0.03930.0081-9.29121.978630.4134
151.1129-0.3040.27464.5252-0.07121.47270.01860.10160.0598-0.26390.0081-0.2718-0.20210.0703-0.0268-0.007-0.01680.0227-0.0374-0.0101-0.04787.566615.84863.7185
160.26070.28920.11726.1082-0.86261.30410.0354-0.02290.05530.4771-0.1342-0.2773-0.27140.04920.09880.0155-0.019-0.0167-0.0422-0.0061-0.04046.838916.384512.4469
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 44
2X-RAY DIFFRACTION2A45 - 69
3X-RAY DIFFRACTION3A70 - 142
4X-RAY DIFFRACTION4A143 - 183
5X-RAY DIFFRACTION5A184 - 190
6X-RAY DIFFRACTION6A191 - 231
7X-RAY DIFFRACTION7B1 - 37
8X-RAY DIFFRACTION8B38 - 75
9X-RAY DIFFRACTION9C1 - 53
10X-RAY DIFFRACTION10C54 - 76
11X-RAY DIFFRACTION11C77 - 142
12X-RAY DIFFRACTION12C143 - 182
13X-RAY DIFFRACTION13C183 - 196
14X-RAY DIFFRACTION14C197 - 231
15X-RAY DIFFRACTION15D1 - 40
16X-RAY DIFFRACTION16D41 - 75

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