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- PDB-2wdt: Crystal structure of Plasmodium falciparum UCHL3 in complex with ... -

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Basic information

Entry
Database: PDB / ID: 2wdt
TitleCrystal structure of Plasmodium falciparum UCHL3 in complex with the suicide inhibitor UbVME
Components
  • UBIQUITIN
  • UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3
KeywordsHYDROLASE/PROTEIN BINDING / HYDROLASE-PROTEIN BINDING COMPLEX / ENZYME-LIGAND COMPLEX / UBIQUITIN ISOPEPTIDASE / UCH-L SUPERFAMILY / CYSTEIN PROTEINASE / PEPTIDASE_C12 / HYDROLASE
Function / homology
Function and homology information


Synthesis of active ubiquitin: roles of E1 and E2 enzymes / UCH proteinases / Neddylation / : / : / protein modification process => GO:0036211 / deNEDDylase activity / protein deneddylation / Peptide chain elongation / Selenocysteine synthesis ...Synthesis of active ubiquitin: roles of E1 and E2 enzymes / UCH proteinases / Neddylation / : / : / protein modification process => GO:0036211 / deNEDDylase activity / protein deneddylation / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / protein deubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / ubiquitin ligase complex / 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 / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / cytosolic ribosome / 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 / Downregulation of ERBB4 signaling / Regulation of FZD by ubiquitination / 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 / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / VLDLR internalisation and degradation / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Josephin domain DUBs / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / ubiquitin binding / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / activated TAK1 mediates p38 MAPK activation / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / Negative regulators of DDX58/IFIH1 signaling / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Deactivation of the beta-catenin transactivating complex / Assembly of the pre-replicative complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A
Similarity search - Function
Ubiquitin carboxyl-terminal hydrolase, domain 1 / Ubiquitin carboxyl-terminal hydrolase, domain 2 / Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily / Ubiquitin carboxyl-terminal hydrolase, family 1 / Ubiquitin carboxyl-terminal hydrolase (UCH) catalytic domain profile. / Peptidase C12, ubiquitin carboxyl-terminal hydrolase / Actin-binding Protein, T-fimbrin; domain 1 / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e ...Ubiquitin carboxyl-terminal hydrolase, domain 1 / Ubiquitin carboxyl-terminal hydrolase, domain 2 / Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily / Ubiquitin carboxyl-terminal hydrolase, family 1 / Ubiquitin carboxyl-terminal hydrolase (UCH) catalytic domain profile. / Peptidase C12, ubiquitin carboxyl-terminal hydrolase / Actin-binding Protein, T-fimbrin; domain 1 / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Dna Ligase; domain 1 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Papain-like cysteine peptidase superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin-60S ribosomal protein L40 / Ubiquitin carboxyl-terminal hydrolase UCHL3
Similarity search - Component
Biological speciesPLASMODIUM FALCIPARUM (malaria parasite P. falciparum)
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsWeihofen, W.A. / Artavanis-Tsakonas, K. / Gaudet, R. / Ploegh, H.L.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Characterization and Structural Studies of the Plasmodium Falciparum Ubiquitin and Nedd8 Hydrolase Uchl3.
Authors: Artavanis-Tsakonas, K. / Weihofen, W.A. / Antos, J.M. / Coleman, B.I. / Comeaux, C.A. / Duraisingh, M.T. / Gaudet, R. / Ploegh, H.L.
History
DepositionMar 26, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 29, 2009Provider: 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
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_conn / struct_site
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 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 2.1Dec 13, 2023Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 2.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3
B: UBIQUITIN
C: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3
D: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,1696
Polymers71,0984
Non-polymers712
Water3,405189
1
A: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3
D: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,5853
Polymers35,5492
Non-polymers351
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2650 Å2
ΔGint-19.9 kcal/mol
Surface area13130 Å2
MethodPISA
2
B: UBIQUITIN
C: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,5853
Polymers35,5492
Non-polymers351
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2700 Å2
ΔGint-20.5 kcal/mol
Surface area13160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.400, 75.300, 85.700
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.801, -0.599, 0.008), (-0.599, -0.801, -0.005), (0.01, -0.001, -1)
Vector: -0.1647, -0.9035, -0.3297)

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Components

#1: Protein UBIQUITIN CARBOXYL-TERMINAL HYDROLASE L3 / UCHL3 / UCH-L3 / UBIQUITIN THIOLESTERASE


Mass: 26930.320 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PLASMODIUM FALCIPARUM (malaria parasite P. falciparum)
Strain: CLONE 3D7 / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8IKM8*PLUS, ubiquitinyl hydrolase 1
#2: Protein UBIQUITIN


Mass: 8618.910 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-75
Source method: isolated from a genetically manipulated source
Details: C-TERMINAL GLY76 OF WILDTYPE UBIQUITIN IS REPLACED BY A VINYL METHYLESTER MOIETY (UBVME)
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PTYB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62988, UniProt: P0CG48*PLUS
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 189 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Nonpolymer detailsMETHYL 4-AMINOBUTANOATE (GVE): ACTIVE SITE CYS95 OF UCHL3 FORMS A COVALENT BOND TO METHYL 4- ...METHYL 4-AMINOBUTANOATE (GVE): ACTIVE SITE CYS95 OF UCHL3 FORMS A COVALENT BOND TO METHYL 4-AMINOBUTANOATE WHICH IS IN TURN FUSED TO GLY75 OF UBIQUITIN
Sequence detailsCDNA OF PLASMODIUM FALCIPARUM UCHL3 WAS GENERATED AS DESCRIBED IN FRICKEL ET AL., CELL. MICROBIOL. ...CDNA OF PLASMODIUM FALCIPARUM UCHL3 WAS GENERATED AS DESCRIBED IN FRICKEL ET AL., CELL. MICROBIOL. 2007, 9, 1601-10. SEQUENCE DIFFERS FROM THE UCHL3 SEQUENCE ANNOTATED IN THE PLASMODIUM DATABASE (PLASMODB ENTRY PF14- 0576).

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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: 3.3 Å3/Da / Density % sol: 63 % / Description: NONE
Crystal growpH: 5.5 / Details: 100 MM BIS-TRIS PH 5.5, 200 MM NACL, 25 % PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.979
DetectorType: ADSC CCD / Detector: CCD / Date: Jun 30, 2007
Details: TRIPLE STRIPED VERTICAL AND HORIZANTAL FOCUSSING MIRRORS IN KIRKPATRICK- BAEZ GEOMETRY
RadiationMonochromator: CRYOGENICALLY-COOLED DOUBLE CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.3→30 Å / Num. obs: 39592 / % possible obs: 98.1 % / Observed criterion σ(I): 3 / Redundancy: 5.7 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 8
Reflection shellResolution: 2.3→2.36 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.1 / % possible all: 90.2

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Processing

Software
NameVersionClassification
REFMAC5.4.0066refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XD3

1xd3


Resolution: 2.3→19.85 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.927 / SU B: 11.763 / SU ML: 0.146 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.216 / ESU R Free: 0.192 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-4 AND 227-232 OF CHAINS A AND C ARE DISORDERED RESTRAINTS FOR REFMAC5 FOR METHYL 4- AMINOBUTANOATE WERE GENERATED WITH THE DUNDEE PRODRG DSERVER
RfactorNum. reflection% reflectionSelection details
Rfree0.235 1062 2.7 %RANDOM
Rwork0.187 ---
obs0.188 38252 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Solvent model: BABINET FOR INITIAL AND SIMPLE SCALING FOR FURTHER REFINEMENT
Displacement parametersBiso mean: 35.33 Å2
Baniso -1Baniso -2Baniso -3
1--0.8 Å20 Å20 Å2
2--3.3 Å20 Å2
3----2.5 Å2
Refinement stepCycle: LAST / Resolution: 2.3→19.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4564 0 2 189 4755
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0224655
X-RAY DIFFRACTIONr_bond_other_d0.0010.023166
X-RAY DIFFRACTIONr_angle_refined_deg1.3191.9646278
X-RAY DIFFRACTIONr_angle_other_deg0.9083.0017750
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9395554
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.59125.667240
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.415850
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.7511518
X-RAY DIFFRACTIONr_chiral_restr0.0850.2698
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0215108
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02886
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.711.52793
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.35424538
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.93231862
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.1214.51740
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: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.255 76 -
Rwork0.216 2746 -
obs--100 %
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)
19.56641.44820.188411.2609-2.414513.54620.01760.41590.43510.3581-0.0432-0.0616-1.91040.89380.02560.2105-0.14490.0208-0.23940.0178-0.0912-6.652-9.084-15.72
23.06150.9211-3.35985.4125-1.203411.80330.22220.13270.6233-0.13250.1391-0.3033-1.27510.4585-0.3613-0.1034-0.0742-0.0218-0.10590.034-0.1226-6.34-12.803-12.216
310.46122.5385-0.69884.8313-1.39759.3429-0.3149-0.14650.0679-0.0273-0.0719-0.6370.23190.9370.3867-0.22880.05210.0301-0.1116-0.0068-0.1465-3.539-20.974-9.097
43.7231.4047-4.57110.43432.055911.37750.11890.3075-0.2648-0.62760.05460.76380.7771-0.1898-0.1735-0.0439-0.0365-0.0623-0.03590.0031-0.2116-12.63-23.353-18.358
53.67860.3271-0.99352.7042-1.219311.046-0.07620.60310.5265-0.47950.17170.1219-0.7621-0.4629-0.0954-0.0408-0.0030.0003-0.07940.0745-0.1221-11.088-14.663-18.741
69.40373.4933-6.87042.4657-5.542515.6772-0.3526-0.0672-0.149-0.2169-0.4834-0.41010.86921.52880.836-0.19860.14660.0504-0.20820.0066-0.1468-9.832-26.8950.194
710.3909-3.35440.75822.6254-1.71583.011-0.1447-0.0174-0.57720.21590.4081-0.08730.66840.0368-0.2634-0.0189-0.10860.043-0.0987-0.0181-0.0703-22.692-56.383-12.439
83.05550.46090.64825.31-1.966510.36750.03010.0655-0.464-0.25480.19720.0021.1365-0.326-0.2273-0.1106-0.07540.0541-0.1821-0.0152-0.1086-20.3-53.813-16.244
92.6931-2.2519-0.28287.7871-2.53610.1571-0.06410.2721-0.1412-0.3732-0.2868-0.5010.60390.72090.351-0.1446-0.02380.0502-0.04480.0184-0.0715-13.17-49.188-19.531
105.25852.87070.03927.9916-2.679911.84530.0990.04310.47210.2895-0.1090.1557-1.09350.22740.01-0.0526-0.04470.0296-0.1373-0.0425-0.1248-18.38-41.562-10.324
115.81022.4656-0.57297.2915-4.524610.107-0.0084-0.3689-0.09410.42650.21050.17460.0485-1.0473-0.2022-0.2149-0.04660.0202-0.1442-0.015-0.2278-22.513-49.126-9.556
126.5981-3.9051.97136.368-7.856711.6211-0.3782-0.19480.19410.0068-0.4309-0.33450.34521.70410.809-0.1758-0.0686-0.0011-0.06090.0257-0.1282-14.509-40.523-28.682
1311.8389-2.73025.43598.06613.22497.61290.18130.4632-0.1261-0.3692-0.263-0.0261-0.38490.87490.0817-0.1588-0.05-0.0158-0.06820.0133-0.1377-6.697-33.6-40.506
149.66171.1735-2.832610.15317.49996.9767-0.0881-0.3858-0.04420.81150.4091-0.51440.4018-0.0599-0.3210.02520.0175-0.0417-0.0537-0.0259-0.1777-15.852-33.34-27.691
152.2850.98760.13975.1673-1.26813.43030.1105-0.10350.11450.2690.1750.4569-0.4286-0.8713-0.2856-0.16010.02160.05310.0754-0.0102-0.2326-26.768-32.835-30.686
161.14120.72370.70751.9733-1.17763.92280.0841-0.1117-0.19050.0478-0.04760.1478-0.4262-0.3394-0.03650.01450.04330.01030.01840.0081-0.0785-22.171-28.283-42.257
174.778-0.15431.64963.28022.14599.3221-0.03420.03760.5575-0.1855-0.01520.1157-1.4584-0.36870.04940.21230.10360.0212-0.1621-0.0052-0.0543-21.083-17.315-43.845
1812.1475-0.016610.14366.6404-2.76979.6139-0.37580.65970.38260.172-0.1274-0.1232-0.7270.69490.50310.04180.0114-0.0011-0.02190.0035-0.0624-16.839-25.601-51.898
199.5869-2.70984.88738.2622-6.4425.90780.05360.27980.7107-0.0289-0.451-0.309-0.35760.8340.39750.0909-0.04640.0066-0.03480.0191-0.0253-8.689-24.561-40.435
208.1085-8.9388-1.591410.13320.88163.0418-0.4579-0.6516-0.06651.06210.6861-0.46480.29220.099-0.2281-0.0203-0.0534-0.04040.06750.040.0117-4.239-39.077-33.553
218.8942-0.5453-0.65052.4730.14635.1472-0.0570.0262-0.3865-0.03910.11460.49710.0586-0.9918-0.0576-0.044-0.03250.02590.12550.0307-0.0944-28.131-35.657-40.752
224.34180.5089-3.04654.8191-2.34199.74010.00720.0273-0.1459-0.07660.14060.46870.0221-1.5047-0.1479-0.2241-0.1224-0.04440.2605-0.0162-0.107-33.81-39.098-39.429
239.1850.50719.696111.4379-5.632113.82270.32690.3162-1.1734-0.74030.19720.11751.0074-0.1251-0.52410.0663-0.10550.0295-0.0169-0.0456-0.0404-25.403-51.811-36.741
240.9174-0.31360.63119.8411.39692.67250.0079-0.12960.25220.6580.2435-0.6711-0.0104-0.3634-0.2514-0.093-0.05530.04010.1217-0.0174-0.1261-24.085-36.965-29.166
2512.0867-0.728-0.06734.61331.71130.6382-0.0297-0.40690.19980.2818-0.1358-0.22150.2069-0.14030.1656-0.05950.0352-0.0189-0.0634-0.0092-0.0362-7.763-36.72512.406
266.9763-1.23732.74210.03292.25445.54850.05210.61860.1107-0.2893-0.01-0.2682-0.04030.2995-0.0421-0.09980.00710.0385-0.0487-0.0332-0.0877-15.178-31.73-0.757
272.84670.1929-0.23464.7446-0.59632.49930.02170.09770.0704-0.22120.03760.1512-0.128-0.485-0.0593-0.17630.0829-0.0258-0.0393-0.0362-0.2259-23.956-25.6531.743
281.2397-0.7721-0.5041.5737-0.71073.98790.0484-0.0961-0.21620.0564-0.0405-0.0845-0.0132-0.3407-0.0079-0.0560.0347-0.01450.0111-0.0031-0.0287-23.311-31.90813.835
292.90410.64062.04364.31332.76259.45110.1043-0.2645-0.31520.2313-0.1780.31860.8892-1.28520.0738-0.0651-0.1203-0.00530.0676-0.0115-0.015-29.036-41.28215.367
3010.32010.8074-6.38643.20783.14168.1907-0.2753-0.5022-0.50140.2818-0.0540.01350.3230.19710.32930.03770.0079-0.0295-0.04630.0044-0.0139-20.77-37.26123.357
318.63410.6212-5.78114.6167-4.85648.1836-0.3015-0.207-0.45340.1591-0.0987-0.12370.3820.27420.4002-0.00220.02180.0011-0.0528-0.03930.0524-14.596-42.94911.981
3211.42522.48981.30240.69830.67641.1384-0.07360.91730.1335-0.22450.2211-0.0953-0.14990.2137-0.1476-0.01420.05140.03140.00690.02110.0399-2.535-34.0535.29
332.2422-3.13740.67014.6018-0.44231.35870.0229-0.07270.17060.12610.0470.0391-0.3537-0.1572-0.06990.01360.0936-0.02620.05440.0009-0.0316-23.665-22.40712.274
344.22880.13270.41732.6307-0.88273.0850.02140.03190.37810.198-0.0041-0.0094-0.4947-0.2674-0.01740.03210.17240.0119-0.0828-0.0603-0.0705-26.061-16.29110.909
3513.92630.2509-11.379810.1455-0.387710.39020.5607-0.66241.23550.397-0.2323-0.8389-1.10140.5423-0.32840.1004-0.0123-0.0652-0.033-0.02330.0584-11.748-11.1418.048
3610.75318.08852.67376.63531.97382.0379-0.1517-0.0116-0.1728-0.2460.068-0.1462-0.1562-0.16570.0837-0.01190.05360.0013-0.018-0.0053-0.042-19.545-23.9240.624
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1B1 - 5
2X-RAY DIFFRACTION2B6 - 22
3X-RAY DIFFRACTION3B23 - 44
4X-RAY DIFFRACTION4B45 - 55
5X-RAY DIFFRACTION5B56 - 70
6X-RAY DIFFRACTION6B71 - 75
7X-RAY DIFFRACTION7D1 - 5
8X-RAY DIFFRACTION8D6 - 22
9X-RAY DIFFRACTION9D23 - 44
10X-RAY DIFFRACTION10D45 - 55
11X-RAY DIFFRACTION11D56 - 70
12X-RAY DIFFRACTION12D71 - 75
13X-RAY DIFFRACTION13A5 - 9
14X-RAY DIFFRACTION14A10 - 16
15X-RAY DIFFRACTION15A17 - 80
16X-RAY DIFFRACTION16A81 - 108
17X-RAY DIFFRACTION17A109 - 128
18X-RAY DIFFRACTION18A129 - 135
19X-RAY DIFFRACTION19A136 - 147
20X-RAY DIFFRACTION20A148 - 161
21X-RAY DIFFRACTION21A162 - 180
22X-RAY DIFFRACTION22A181 - 206
23X-RAY DIFFRACTION23A207 - 216
24X-RAY DIFFRACTION24A217 - 226
25X-RAY DIFFRACTION25C5 - 9
26X-RAY DIFFRACTION26C10 - 16
27X-RAY DIFFRACTION27C17 - 80
28X-RAY DIFFRACTION28C81 - 108
29X-RAY DIFFRACTION29C109 - 128
30X-RAY DIFFRACTION30C129 - 135
31X-RAY DIFFRACTION31C136 - 147
32X-RAY DIFFRACTION32C148 - 161
33X-RAY DIFFRACTION33C162 - 180
34X-RAY DIFFRACTION34C181 - 206
35X-RAY DIFFRACTION35C207 - 216
36X-RAY DIFFRACTION36C217 - 226

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