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- PDB-3ihp: Covalent Ubiquitin-Usp5 Complex -

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Basic information

Entry
Database: PDB / ID: 3ihp
TitleCovalent Ubiquitin-Usp5 Complex
Components
  • Ubiquitin
  • Ubiquitin carboxyl-terminal hydrolase 5
KeywordsHYDROLASE / PROTEASE / THIOL PROTEASE / UBL CONJUGATION PATHWAY / METAL-BINDING / ZINC-FINGER / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / SGC / Acetylation / Alternative splicing / Phosphoprotein / Zinc / Cytoplasm / Isopeptide bond / Nucleus / Ubl conjugation
Function / homology
Function and homology information


regulation protein catabolic process at presynapse / : / : / protein modification process => GO:0036211 / deubiquitinase activity / protein K48-linked deubiquitination / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination ...regulation protein catabolic process at presynapse / : / : / protein modification process => GO:0036211 / deubiquitinase activity / protein K48-linked deubiquitination / 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 / negative regulation of ubiquitin-dependent protein catabolic process / 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 / 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 / cytosolic ribosome / 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 / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / 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 / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / Regulation of FZD by ubiquitination / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / Regulation of innate immune responses to cytosolic DNA / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / 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 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / TICAM1, RIP1-mediated IKK complex recruitment / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by REV1 / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / InlB-mediated entry of Listeria monocytogenes into host cell / Regulation of activated PAK-2p34 by proteasome mediated degradation / Josephin domain DUBs / Translesion synthesis by POLI / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / ubiquitin binding / 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 / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / TCF dependent signaling in response to WNT / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Regulation of NF-kappa B signaling / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Regulation of signaling by CBL / Cdc20:Phospho-APC/C mediated degradation of Cyclin A
Similarity search - Function
Ubiquitin carboxyl-terminal hydrolase 5, UBA1 domain / Ubiquitinyl hydrolase / Ubiquitinyl hydrolase, variant UBP zinc finger / Variant UBP zinc finger / UBA-like domain / : / Ubiquitin-associated (UBA) domain / Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger / Zinc finger, UBP-type / Zn-finger in ubiquitin-hydrolases and other protein ...Ubiquitin carboxyl-terminal hydrolase 5, UBA1 domain / Ubiquitinyl hydrolase / Ubiquitinyl hydrolase, variant UBP zinc finger / Variant UBP zinc finger / UBA-like domain / : / Ubiquitin-associated (UBA) domain / Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger / Zinc finger, UBP-type / Zn-finger in ubiquitin-hydrolases and other protein / Zinc finger UBP-type profile. / UBA/TS-N domain / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Ubiquitin associated domain / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / Cysteine proteinases / Zinc/RING finger domain, C3HC4 (zinc finger) / Cathepsin B; Chain A / Herpes Virus-1 / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Helicase, Ruva Protein; domain 3 / 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 / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ETHANAMINE / Polyubiquitin-C / Ubiquitin carboxyl-terminal hydrolase 5 / Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5 / Ubiquitin-60S ribosomal protein L40
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsWalker, J.R. / Avvakumov, G.V. / Xue, S. / Butler-Cole, C. / Weigelt, J. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S. / Structural Genomics Consortium (SGC)
CitationJournal: To be Published
Title: Covalent Ubiquitin-Usp5 Complex
Authors: Walker, J.R. / Avvakumov, G.V. / Xue, S. / Butler-Cole, C. / Weigelt, J. / Bountra, C. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S.
History
DepositionJul 30, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 29, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _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.value / _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.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_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin carboxyl-terminal hydrolase 5
B: Ubiquitin carboxyl-terminal hydrolase 5
C: Ubiquitin
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)208,1969
Polymers207,9394
Non-polymers2565
Water57632
1
A: Ubiquitin carboxyl-terminal hydrolase 5
C: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,0804
Polymers103,9702
Non-polymers1102
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4530 Å2
ΔGint-8 kcal/mol
Surface area35540 Å2
MethodPISA
2
B: Ubiquitin carboxyl-terminal hydrolase 5
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,1165
Polymers103,9702
Non-polymers1463
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4610 Å2
ΔGint-19 kcal/mol
Surface area36140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)68.295, 188.845, 207.860
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 835
2114B1 - 835
1124C1 - 76
2124D1 - 76

NCS ensembles :
ID
2
1

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Ubiquitin carboxyl-terminal hydrolase 5 / Ubiquitin thioesterase 5 / Ubiquitin-specific-processing protease 5 / Deubiquitinating enzyme 5 / ...Ubiquitin thioesterase 5 / Ubiquitin-specific-processing protease 5 / Deubiquitinating enzyme 5 / Isopeptidase T


Mass: 95449.883 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ISOT, USP5 / Plasmid: PET28a-LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3)
References: UniProt: P45974-2, UniProt: P45974*PLUS, EC: 3.1.2.15
#2: Protein Ubiquitin


Mass: 8519.778 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2 / Plasmid: PTBY2 / Production host: Escherichia coli (E. coli) / Strain (production host): B21 (DE3) / References: UniProt: P62988, UniProt: P0CG48*PLUS

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Non-polymers , 4 types, 37 molecules

#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-NEH / ETHANAMINE


Mass: 45.084 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H7N
#5: Chemical ChemComp-CL / CHLORIDE ION


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


Mass: 18.015 Da / Num. of mol.: 32 / 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: 3.22 Å3/Da / Density % sol: 61.82 %
Crystal growTemperature: 298 K / pH: 6.5
Details: Crystals of the covalent ubiquitin complex of Usp5 were grown at 298 K using the hanging drop method by mixing equal volumes of protein solution (25 mg/ml) and Crystallization Buffer (1.45 M ...Details: Crystals of the covalent ubiquitin complex of Usp5 were grown at 298 K using the hanging drop method by mixing equal volumes of protein solution (25 mg/ml) and Crystallization Buffer (1.45 M ammonium sulfate, 0.1 M bis-Tris, pH 6.5, 0.2 M sodium acetate, 5% ethyleneglycol and 1 mM dithiothreitol). The crystals were cryoprotected by immersion in Paratone N in paraffin oil 30% (v/v) and placed in liquid nitrogen., VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.97918
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 11, 2007 / Details: MIRRORS
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.8→35 Å / Num. obs: 66229 / % possible obs: 98 % / Observed criterion σ(I): -3 / Redundancy: 5.4 % / Rsym value: 0.101 / Net I/σ(I): 17.1
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 5.4 % / Mean I/σ(I) obs: 2 / Rsym value: 0.845 / % possible all: 94.6

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2IBI, 2G43, 2DAK, 2DAG

2ibi

2g43

2dak

2dag


Resolution: 2.8→34.9 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.889 / SU B: 30.552 / SU ML: 0.272 / Cross valid method: THROUGHOUT / ESU R: 0.563 / ESU R Free: 0.343 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUMOF TLS AND RESIDUAL U FACTORS.
RfactorNum. reflection% reflectionSelection details
Rfree0.27588 3298 5 %RANDOM
Rwork0.22431 ---
obs0.22688 62592 98.05 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 73.948 Å2
Baniso -1Baniso -2Baniso -3
1--0.35 Å20 Å20 Å2
2--0.39 Å20 Å2
3----0.04 Å2
Refinement stepCycle: LAST / Resolution: 2.8→34.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11759 0 9 32 11800
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02212019
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3081.96716278
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.97551491
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.01424.56557
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.655152014
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.9231568
X-RAY DIFFRACTIONr_chiral_restr0.090.21803
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0219149
X-RAY DIFFRACTIONr_gen_planes_other
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_it0.4691.57512
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.898212082
X-RAY DIFFRACTIONr_scbond_it1.27534507
X-RAY DIFFRACTIONr_scangle_it2.2374.54196
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A4816medium positional0.610.5
22C600medium positional0.330.5
11A4816medium thermal0.392
22C600medium thermal0.452
LS refinement shellResolution: 2.8→2.872 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.358 234 -
Rwork0.303 4388 -
obs--94.21 %
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)
15.5849-0.65662.57990.46020.30025.1070.1846-0.1417-0.0265-0.08530.0434-0.06610.33110.0756-0.2280.4747-0.11320.01580.2297-0.05810.1774-77.4876-62.849-74.8262
24.29541.32050.41690.60720.31570.26540.1766-0.1414-0.0786-0.0657-0.1829-0.07420.0911-0.03690.00630.5287-0.04780.04670.26830.04210.1994-59.4187-53.906-79.8348
34.4352-0.8951-0.29064.73571.2625.4002-0.0974-0.1568-0.17090.21750.15970.59480.0747-0.4805-0.06220.3187-0.03310.12120.21890.0980.3092-37.1802-45.455-76.4435
42.6241-0.14810.5550.83340.36642.54110.07880.12610.0041-0.229-0.17530.02690.1955-0.27480.09650.3838-0.06690.03420.3538-0.08330.2193-61.6675-61.6046-53.8172
50.3761-0.5527-0.78581.14131.62181.8699-0.0119-0.20410.19880.14120.0937-0.14040.03640.3127-0.08190.3537-0.0529-0.01760.49690.10210.3658-40.4289-53.4996-32.822
60.49450.04710.17520.57310.57551.17920.0034-0.0387-0.01450.01250.0218-0.12260.05850.2655-0.02520.3258-0.05730.05390.3613-0.01330.32-41.726-54.8597-34.0322
70.23720.53810.04362.15991.9371.35210.00260.06820.2018-0.2921-0.52510.6153-0.2877-0.59220.52240.28580.0941-0.14290.536-0.18010.4833-61.4187-26.1704-21.0356
89.66931.8553-2.50125.8601-0.24423.22990.1754-0.01190.28740.2337-0.33150.2319-0.4319-0.53520.15610.17870.0385-0.02450.4626-0.16750.2691-73.7781-42.7836-37.4903
92.17110.5145-1.26461.01350.68253.8495-0.03520.2057-0.2945-0.0164-0.0001-0.08260.56830.17520.03540.40230.00620.09520.2688-0.03040.332-48.1201-68.0426-46.2916
103.90712.4008-1.86586.4874-0.08930.89840.0427-0.09490.1780.1649-0.02880.13850.07930.0285-0.01390.370.0069-0.05640.1965-0.05370.2209-74.187320.245813.983
112.73961.22090.02225.26060.3852.39240.2554-0.10250.00760.1474-0.32720.1233-0.1564-0.00870.07180.3872-0.0241-0.04670.1962-0.10990.2305-73.555722.594515.7112
120.1516-0.85430.6754.8296-2.26335.91370.0053-0.06340.0377-0.3756-0.3726-0.43980.70130.95860.36730.40880.21140.06530.44450.16180.3134-117.36919.5143-0.5808
132.31890.948-0.23281.96260.65721.4790.1141-0.0074-0.01840.01310.0908-0.1783-0.21110.1201-0.20490.3464-0.0033-0.0210.1949-0.06980.2979-90.228-2.358212.5205
140.6138-0.4922-0.64611.03681.11941.1945-0.01560.1181-0.2929-0.0505-0.10550.22690.0951-0.17620.1210.338-0.0196-0.08890.27260.01680.4306-114.7891-19.41063.2659
150.84090.37440.05050.61140.62231.2446-0.0084-0.0058-0.13780.0545-0.00390.10790.0851-0.15110.01220.29550.0278-0.0690.24910.01280.3523-108.894-23.0213.7434
160.2444-0.00350.34450.95332.23844.5937-0.00930.1990.1129-0.18890.3899-0.3216-0.22870.6045-0.38060.2337-0.14190.08030.496-0.18510.5427-90.9323-30.4362-26.2722
1712.6904-4.5425-0.26634.418-0.25359.17870.1094-0.14750.195-0.55740.3835-0.4683-0.27870.9051-0.4930.1296-0.06570.03750.3811-0.23780.3502-79.0098-15.7455-8.0439
182.1883-0.27670.52292.76640.41031.59540.1133-0.1560.01650.24080.00460.1281-0.0337-0.0129-0.11790.29480.0481-0.02130.2502-0.01540.2632-103.8947-10.9418.4682
198.98862.61230.2732.7594-5.61277.5587-0.2569-0.02940.47140.1498-0.168-0.1987-0.09770.30490.42490.2448-0.1347-0.02630.3346-0.10170.3338-47.0098-40.9947-30.8543
2015.1866-2.1986-5.44235.1025.17094.95080.2687-0.18750.6116-1.1581-0.0105-0.1977-1.36070.1192-0.25810.7129-0.12420.09930.20770.02060.4363-49.6866-34.2992-38.7771
2110.7048-0.0543-1.19414.61061.29572.51920.28810.9148-0.2322-0.7482-0.22810.317-0.5817-0.0393-0.060.3745-0.0049-0.0290.3633-0.01310.2418-55.5405-42.8028-42.0097
222.3848-1.7581-2.61213.012.42613.75170.0178-0.09070.3397-0.0862-0.0122-0.02240.02780.055-0.00560.3137-0.07420.00880.3783-0.01790.2829-53.1063-45.2677-38.3397
239.56493.95310.06339.4715-2.9852.9559-0.58280.1468-0.5257-0.03740.02920.48720.5536-0.42030.55360.4059-0.08910.05220.3398-0.17340.4919-105.6727-22.5102-10.05
2410.5793-5.51050.78525.16940.33914.41940.35731.1270.3187-0.8135-0.1994-0.1746-0.8415-0.2999-0.15790.38140.0398-0.04650.31990.01850.2591-103.0758-13.8639-15.89
2511.1447-1.1919-0.66382.77893.06723.15110.36020.00280.6687-0.50010.0557-0.3849-0.56410.1829-0.41590.4031-0.03440.01180.2197-0.01060.3357-97.5378-11.4251-6.8727
263.3145-2.3201-1.09763.913.06344.92350.02420.1122-0.2312-0.10950.23410.1053-0.25850.3012-0.25830.285-0.0265-0.05010.21380.02130.3441-99.1186-15.6076-5.3257
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 121
2X-RAY DIFFRACTION2A122 - 203
3X-RAY DIFFRACTION3A204 - 282
4X-RAY DIFFRACTION4A283 - 462
5X-RAY DIFFRACTION5A463 - 513
6X-RAY DIFFRACTION6A514 - 607
7X-RAY DIFFRACTION7A608 - 711
8X-RAY DIFFRACTION8A712 - 749
9X-RAY DIFFRACTION9A769 - 834
10X-RAY DIFFRACTION10B1 - 40
11X-RAY DIFFRACTION11B41 - 156
12X-RAY DIFFRACTION12B173 - 320
13X-RAY DIFFRACTION13B321 - 462
14X-RAY DIFFRACTION14B463 - 520
15X-RAY DIFFRACTION15B521 - 607
16X-RAY DIFFRACTION16B608 - 712
17X-RAY DIFFRACTION17B713 - 750
18X-RAY DIFFRACTION18B768 - 835
19X-RAY DIFFRACTION19C1 - 16
20X-RAY DIFFRACTION20C17 - 39
21X-RAY DIFFRACTION21C40 - 57
22X-RAY DIFFRACTION22C58 - 75
23X-RAY DIFFRACTION23D1 - 16
24X-RAY DIFFRACTION24D17 - 39
25X-RAY DIFFRACTION25D40 - 56
26X-RAY DIFFRACTION26D57 - 75

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