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- PDB-9g7g: Structure of the clippase PaJOS from Pigmentiphaga aceris -

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Basic information

Entry
Database: PDB / ID: 9g7g
TitleStructure of the clippase PaJOS from Pigmentiphaga aceris
Components
  • PaJOS
  • Polyubiquitin-B
KeywordsHYDROLASE / Ubiquitin / Clippase
Function / homology
Function and homology information


hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / fat pad development / mitochondrion transport along microtubule / female gonad development / seminiferous tubule development / male meiosis I / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / energy homeostasis ...hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / fat pad development / mitochondrion transport along microtubule / female gonad development / seminiferous tubule development / male meiosis I / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / energy homeostasis / regulation of neuron apoptotic process / regulation of proteasomal protein catabolic process / 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 / 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / 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 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / 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 / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / neuron projection morphogenesis / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / regulation of mitochondrial membrane potential / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / positive regulation of protein ubiquitination / 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 / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Negative regulation of FGFR3 signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Fanconi Anemia Pathway / Peroxisomal protein import / Degradation of AXIN / Regulation of TNFR1 signaling / Negative regulation of FGFR2 signaling
Similarity search - Function
: / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
prop-2-en-1-amine / Uncharacterized protein / Polyubiquitin-B
Similarity search - Component
Biological speciesPigmentiphaga aceris (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.89 Å
AuthorsBaumann, U. / Uthoff, M. / Hermanns, T. / Hofmann, K.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)HO 3783/3-1 Germany
CitationJournal: Mol.Cell / Year: 2025
Title: A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode.
Authors: Hermanns, T. / Kolek, S. / Uthoff, M. / de Heiden, R.A. / Mulder, M.P.C. / Baumann, U. / Hofmann, K.
History
DepositionJul 21, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 23, 2025Provider: repository / Type: Initial release
Revision 2.0May 21, 2025Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Experimental preparation / Structure summary
Category: atom_site / exptl_crystal_grow ...atom_site / exptl_crystal_grow / pdbx_modification_feature / pdbx_nonpoly_scheme / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_validate_close_contact / struct_conn
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _exptl_crystal_grow.temp / _pdbx_modification_feature.auth_asym_id / _pdbx_modification_feature.auth_seq_id / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PaJOS
B: Polyubiquitin-B
C: PaJOS
D: Polyubiquitin-B
E: PaJOS
F: Polyubiquitin-B
G: PaJOS
H: Polyubiquitin-B
I: PaJOS
J: Polyubiquitin-B
K: PaJOS
L: Polyubiquitin-B
M: PaJOS
N: Polyubiquitin-B
O: PaJOS
P: Polyubiquitin-B
Q: PaJOS
R: Polyubiquitin-B
S: PaJOS
T: Polyubiquitin-B
U: PaJOS
V: Polyubiquitin-B
W: PaJOS
X: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)436,49636
Polymers435,81024
Non-polymers68512
Water10,773598
1
A: PaJOS
B: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2320 Å2
ΔGint-11 kcal/mol
Surface area13400 Å2
MethodPISA
2
C: PaJOS
D: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2290 Å2
ΔGint-13 kcal/mol
Surface area13260 Å2
MethodPISA
3
E: PaJOS
F: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2240 Å2
ΔGint-13 kcal/mol
Surface area13330 Å2
MethodPISA
4
G: PaJOS
H: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2250 Å2
ΔGint-13 kcal/mol
Surface area13560 Å2
MethodPISA
5
I: PaJOS
J: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2250 Å2
ΔGint-13 kcal/mol
Surface area13350 Å2
MethodPISA
6
K: PaJOS
L: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2300 Å2
ΔGint-11 kcal/mol
Surface area13340 Å2
MethodPISA
7
M: PaJOS
N: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2290 Å2
ΔGint-12 kcal/mol
Surface area13620 Å2
MethodPISA
8
O: PaJOS
P: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2260 Å2
ΔGint-14 kcal/mol
Surface area13580 Å2
MethodPISA
9
Q: PaJOS
R: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2250 Å2
ΔGint-13 kcal/mol
Surface area13530 Å2
MethodPISA
10
S: PaJOS
T: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2310 Å2
ΔGint-12 kcal/mol
Surface area13290 Å2
MethodPISA
11
U: PaJOS
V: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2270 Å2
ΔGint-11 kcal/mol
Surface area13680 Å2
MethodPISA
12
W: PaJOS
X: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,3753
Polymers36,3182
Non-polymers571
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2280 Å2
ΔGint-13 kcal/mol
Surface area13480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)131.946, 81.316, 167.392
Angle α, β, γ (deg.)90.00, 90.23, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
PaJOS


Mass: 27797.758 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pigmentiphaga aceris (bacteria) / Gene: FXN63_18770 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A5C0B1L0
#2: Protein
Polyubiquitin-B


Mass: 8519.778 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli B (bacteria) / References: UniProt: P0CG47
#3: Chemical
ChemComp-AYE / prop-2-en-1-amine / ALLYLAMINE


Mass: 57.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H7N / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 598 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.06 Å3/Da / Density % sol: 40.31 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.2 M magnesium chloride, 0.1 M TRIS pH 8.5, 30 % w/v PEG4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 6, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.89→80 Å / Num. obs: 271333 / % possible obs: 95.9 % / Redundancy: 6.6 % / CC1/2: 0.999 / Rmerge(I) obs: 0.072 / Rrim(I) all: 0.078 / Net I/σ(I): 11.63
Reflection shell
Resolution (Å)Rmerge(I) obsNum. unique obsCC1/2Rrim(I) allDiffraction-ID
1.89-1.941.742157990.3731.9821
1.94-1.991.258174060.571.4141
1.99-2.050.96185650.7371.0591
2.05-2.110.8190320.870.8651
2.11-2.180.617184780.9170.6651
2.18-2.260.477178990.9460.5141
2.26-2.350.353172580.9670.3811
2.35-2.440.284166160.9760.3061
2.44-2.550.22158960.9850.2381
2.55-2.670.173149530.9890.1881
2.67-2.820.136146110.9950.1461
2.82-2.990.107137150.9960.1161
2.99-3.20.081128280.9970.0881
3.2-3.450.063120430.9980.0691
3.45-3.780.05107730.9980.0551
3.78-4.230.043100190.9990.0471
4.23-4.880.03888970.9990.0411
4.88-5.980.03975380.9990.0431
5.98-8.460.03656870.9990.0391
8.46-800.028332010.031

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Processing

Software
NameVersionClassification
PHENIX(dev_5407: ???)refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.89→49.03 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2309 2116 0.78 %
Rwork0.2041 --
obs0.2043 270643 95.61 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.89→49.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28197 0 48 598 28843
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00829000
X-RAY DIFFRACTIONf_angle_d0.92339549
X-RAY DIFFRACTIONf_dihedral_angle_d12.65510549
X-RAY DIFFRACTIONf_chiral_restr0.0614528
X-RAY DIFFRACTIONf_plane_restr0.0095232
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.89-1.930.44991120.420613676X-RAY DIFFRACTION73
1.93-1.980.37081210.365715698X-RAY DIFFRACTION84
1.98-2.040.36151340.314617230X-RAY DIFFRACTION92
2.04-2.10.32461460.283618340X-RAY DIFFRACTION98
2.1-2.160.34021450.266918484X-RAY DIFFRACTION99
2.16-2.240.27791460.255518510X-RAY DIFFRACTION99
2.24-2.330.28321460.244118538X-RAY DIFFRACTION99
2.33-2.440.26131470.23118492X-RAY DIFFRACTION99
2.44-2.570.27311440.228718465X-RAY DIFFRACTION99
2.57-2.730.27371440.235518330X-RAY DIFFRACTION98
2.73-2.940.2791450.247118609X-RAY DIFFRACTION99
2.94-3.230.26411460.230518562X-RAY DIFFRACTION99
3.23-3.70.24241430.196718458X-RAY DIFFRACTION98
3.7-4.660.14971470.146518508X-RAY DIFFRACTION98
4.66-49.030.16681500.151418627X-RAY DIFFRACTION97
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)
12.01930.31840.0012.13150.18721.14810.0642-0.11890.18720.03970.01020.0194-0.0529-0.0027-0.06670.24130.0244-0.02890.3861-0.03320.2978-47.291321.8875-87.6888
25.96181.92492.06454.1991.34723.6712-0.10320.2365-0.1065-0.1662-0.02230.42750.0738-0.5820.13870.2908-0.01-0.06190.5516-0.06250.3614-64.76248.0338-99.9535
32.1734-0.10650.12952.116-0.71921.28780.05690.00520.15020.0062-0.08320.0252-0.07540.13470.03420.28280.0072-0.03660.4569-0.01620.2863-15.969420.7345-81.7948
46.1529-2.3673.34194.0249-1.94523.5937-0.06220.15290.0480.1119-0.1241-0.4539-0.11530.61450.17110.29280.0023-0.01560.64950.05230.30240.40396.6843-68.1534
52.4399-0.2577-0.07132.19150.73791.4930.1306-0.04750.245-0.0025-0.1073-0.1749-0.1676-0.0286-0.01410.2865-0.0325-0.03960.28580.03190.3358-27.241159.9313-141.7759
66.22822.64783.32285.01073.11024.6322-0.0177-0.25070.1955-0.0385-0.27720.353-0.0997-0.4910.28960.26580.0244-0.02890.3486-0.00240.2624-43.547445.3122-155.12
71.3748-0.11630.05472.0363-0.14011.4717-0.0875-0.00970.0389-0.0554-0.06-0.22970.06390.15210.16270.2881-0.0062-0.01960.38290.00190.3126-29.817662.6647-100.0172
82.5737-0.3838-1.76834.7-0.32831.7891-0.1555-0.0676-0.5727-0.03670.07670.5930.171-0.41320.10160.3036-0.03750.00160.4915-0.02880.4108-54.652759.9343-94.9748
92.22670.3908-0.06682.57990.12571.09370.0555-0.11960.26170.013-0.035-0.0495-0.1066-0.027-0.02150.272-0.0333-0.00420.3629-0.02860.2721-90.758820.4306-143.4021
105.62491.59532.12583.94631.08433.753-0.28670.3518-0.0421-0.45660.1390.65940.1014-0.44390.12590.3404-0.0692-0.05260.4501-0.02760.3582-108.65786.5369-155.3106
111.91-0.29880.59142.456-0.48411.3599-0.02780.06670.1881-0.04880.0038-0.0447-0.11240.12030.01490.2593-0.0574-0.01670.3549-0.02870.2973-59.433919.4428-138.1067
126.6467-3.11742.92333.7551-2.04483.3785-0.14540.04510.23180.04120.025-0.4312-0.09940.24920.12930.2581-0.0455-0.03220.3442-0.04430.3265-42.99845.555-124.4277
132.0572-0.2093-0.09332.1352-0.37871.5716-0.03050.0283-0.0033-0.0801-0.2525-0.35260.18450.1980.29210.3343-0.00160.00450.38030.06470.3042-73.373561.3706-155.6756
148.77481.2207-1.93424.2492-0.93192.4099-0.21360.1027-0.6144-0.2102-0.02710.54730.3374-0.58170.23580.3562-0.10080.00190.4521-0.09390.3692-98.022258.1208-150.5587
153.418-0.26660.52712.2581-0.17491.420.0099-0.01110.90670.0223-0.0853-0.0682-0.2030.08170.03580.2268-0.0111-0.02420.2291-0.00840.54594.217362.2299-136.8168
166.8881-1.30342.14243.2483-1.82082.9709-0.057-0.35280.35070.0469-0.1252-0.3244-0.17510.4920.16630.2843-0.0303-0.06170.4866-0.07050.393322.01549.4474-123.9409
172.09040.76520.64822.4680.65152.35910.243-0.57630.07460.3214-0.56740.45670.5404-1.10110.22740.4975-0.29180.0060.949-0.14190.3847-80.084863.8759-121.1337
182.5638-1.3605-2.33143.17890.50263.93460.076-0.5255-0.70020.4112-0.1253-0.37140.57490.1910.04130.5222-0.0654-0.10180.4620.04730.5141-55.818157.8142-125.4745
195.80831.376-1.62352.4977-0.42543.2927-0.5419-0.494-0.62290.0195-0.14720.29070.4773-0.20890.47320.35140.0420.08460.3202-0.02250.4206-12.860922.4212-122.679
205.8455-0.157-0.8193.4855-0.27781.7848-0.7282-0.7235-1.24460.3290.2906-0.31590.40390.56430.37610.44790.15930.1320.49420.09790.513512.038319.0417-127.5215
212.0227-0.05390.33342.0448-0.64892.2556-0.04520.1517-0.0003-0.1732-0.2508-0.34590.4260.71190.26960.44260.08640.04020.76260.12150.3319-94.722124.8424-102.13
226.15921.1754-2.98884.5919-0.47653.9197-0.21230.3343-0.5479-0.196-0.02920.390.5124-0.57250.22840.4851-0.1037-0.00270.56970.00530.3912-118.852818.4926-97.6044
234.2035-2.1708-0.40784.27420.56692.13360.13530.51680.0455-0.4132-0.2573-0.30550.3990.34480.10880.47240.111-0.02160.47010.02450.3346-5.093323.4375-156.9329
246.01812.90150.09644.4040.89822.9359-0.14930.5169-1.3487-0.1146-0.25871.14380.5645-0.6270.36320.6283-0.04880.00250.5625-0.22781.1362-29.250216.2995-152.3169
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resid 28 through 261)
2X-RAY DIFFRACTION2(chain 'B' and resid 1 through 75)
3X-RAY DIFFRACTION3(chain 'C' and resid 28 through 260)
4X-RAY DIFFRACTION4(chain 'D' and resid 1 through 75)
5X-RAY DIFFRACTION5(chain 'E' and resid 28 through 260)
6X-RAY DIFFRACTION6(chain 'F' and resid 1 through 75)
7X-RAY DIFFRACTION7(chain 'G' and resid 26 through 260)
8X-RAY DIFFRACTION8(chain 'H' and resid 1 through 75)
9X-RAY DIFFRACTION9(chain 'I' and resid 28 through 260)
10X-RAY DIFFRACTION10(chain 'J' and resid 1 through 75)
11X-RAY DIFFRACTION11(chain 'K' and resid 28 through 261)
12X-RAY DIFFRACTION12(chain 'L' and resid 1 through 75)
13X-RAY DIFFRACTION13(chain 'M' and resid 26 through 259)
14X-RAY DIFFRACTION14(chain 'N' and resid 1 through 75)
15X-RAY DIFFRACTION15(chain 'O' and resid 28 through 262)
16X-RAY DIFFRACTION16(chain 'P' and resid 1 through 75)
17X-RAY DIFFRACTION17(chain 'Q' and resid 26 through 259)
18X-RAY DIFFRACTION18(chain 'R' and resid 1 through 75)
19X-RAY DIFFRACTION19(chain 'S' and resid 26 through 260)
20X-RAY DIFFRACTION20(chain 'T' and resid 1 through 75)
21X-RAY DIFFRACTION21(chain 'U' and resid 25 through 259)
22X-RAY DIFFRACTION22(chain 'V' and resid 1 through 75)
23X-RAY DIFFRACTION23(chain 'W' and resid 26 through 258)
24X-RAY DIFFRACTION24(chain 'X' and resid 1 through 75)

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