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- PDB-3u73: Crystal structure of stabilized human uPAR mutant in complex with ATF -

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Basic information

Entry
Database: PDB / ID: 3u73
TitleCrystal structure of stabilized human uPAR mutant in complex with ATF
Components
  • Urokinase plasminogen activator surface receptor
  • Urokinase-type plasminogen activator
KeywordsHYDROLASE/HYDROLASE RECEPTOR / glycosylation / HYDROLASE-HYDROLASE RECEPTOR complex
Function / homology
Function and homology information


urokinase plasminogen activator receptor activity / Attachment of GPI anchor to uPAR / positive regulation of homotypic cell-cell adhesion / negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing ...urokinase plasminogen activator receptor activity / Attachment of GPI anchor to uPAR / positive regulation of homotypic cell-cell adhesion / negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / regulation of proteolysis / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / positive regulation of epidermal growth factor receptor signaling pathway / extrinsic component of membrane / plasminogen activation / positive regulation of release of cytochrome c from mitochondria / regulation of cell adhesion mediated by integrin / tertiary granule membrane / positive regulation of DNA binding / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / negative regulation of intrinsic apoptotic signaling pathway / serine protease inhibitor complex / fibrinolysis / cell projection / chemotaxis / blood coagulation / signaling receptor activity / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / positive regulation of protein phosphorylation / protein domain specific binding / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / focal adhesion / signaling receptor binding / Neutrophil degranulation / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane
Similarity search - Function
CD59 antigen, conserved site / Ly-6 / u-PAR domain signature. / Ly-6 antigen / uPA receptor -like domain / u-PAR/Ly-6 domain / Ly-6 antigen/uPA receptor-like / Plasminogen Kringle 4 / Plasminogen Kringle 4 / CD59 / CD59 / Snake toxin-like superfamily ...CD59 antigen, conserved site / Ly-6 / u-PAR domain signature. / Ly-6 antigen / uPA receptor -like domain / u-PAR/Ly-6 domain / Ly-6 antigen/uPA receptor-like / Plasminogen Kringle 4 / Plasminogen Kringle 4 / CD59 / CD59 / Snake toxin-like superfamily / Laminin / Laminin / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / Ribbon / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Urokinase-type plasminogen activator / Urokinase plasminogen activator surface receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.19 Å
AuthorsHuang, M.D. / Xu, X. / Yuan, C.
CitationJournal: J.Mol.Biol. / Year: 2012
Title: Crystal structure of the urokinase receptor in a ligand-free form.
Authors: Xu, X. / Gardsvoll, H. / Yuan, C. / Lin, L. / Ploug, M. / Huang, M.
History
DepositionOct 13, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 18, 2012Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
U: Urokinase plasminogen activator surface receptor
A: Urokinase-type plasminogen activator
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8915
Polymers46,4552
Non-polymers1,4353
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4100 Å2
ΔGint12 kcal/mol
Surface area20230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)130.896, 130.896, 105.315
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

#1: Protein Urokinase plasminogen activator surface receptor / U-PAR / uPAR / Monocyte activation antigen Mo3


Mass: 31455.377 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MO3, PLAUR, UPAR / Plasmid: PMT/BIP / Cell line (production host): S2 CELLS / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: Q03405
#2: Protein Urokinase-type plasminogen activator / U-plasminogen activator / uPA / Urokinase-type plasminogen activator long chain A / Urokinase-type ...U-plasminogen activator / uPA / Urokinase-type plasminogen activator long chain A / Urokinase-type plasminogen activator short chain A / Urokinase-type plasminogen activator chain B


Mass: 14999.958 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PLAU / Plasmid: PMT/BIP / Cell line (production host): S2 CELLS / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: P00749, u-plasminogen activator
#3: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE

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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: 5.61 Å3/Da / Density % sol: 78.06 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 0.2M NaCl, 100mM HEPES, pH7.4, 1.8 M ammonium sulfate, vapor diffusion, sitting drop, temperature 295.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9791 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jan 1, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 3.19→99 Å / Num. all: 17148 / Num. obs: 16246 / % possible obs: 96.4 % / Redundancy: 8 % / Rmerge(I) obs: 0.107 / Net I/σ(I): 9.8
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
3.19-3.314.60.977183.1
3.31-3.456.40.71189
3.45-3.67.40.455194.3
3.6-3.798.20.299197.9
3.79-4.038.90.215199.9
4.03-4.349.10.1431100
4.34-4.7890.0981100
4.78-5.478.90.0921100
5.47-6.898.60.0871100
6.89-9980.049198.9

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
REFMAC5.6.0117refinement
PDB_EXTRACT3.1data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.19→47.76 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.896 / Occupancy max: 1 / Occupancy min: 1 / SU B: 37.026 / SU ML: 0.276 / Cross valid method: THROUGHOUT / ESU R: 0.656 / ESU R Free: 0.372 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.258 877 5.1 %RANDOM
Rwork0.216 ---
obs0.218 16246 96.2 %-
all-17123 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 102.677 Å2
Baniso -1Baniso -2Baniso -3
1--0.81 Å2-0.41 Å20 Å2
2---0.81 Å20 Å2
3---1.22 Å2
Refinement stepCycle: LAST / Resolution: 3.19→47.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3038 0 95 0 3133
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.023225
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.1761.9744365
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.1135389
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.23624.351154
X-RAY DIFFRACTIONr_dihedral_angle_3_deg23.30915531
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.3721522
X-RAY DIFFRACTIONr_chiral_restr0.1370.2472
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0212426
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_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3.19→3.27 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.482 53 -
Rwork0.507 943 -
obs--79.62 %
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)
18.90570.96964.14540.2603-1.051831.0127-0.8601-0.88270.18-0.3087-0.03510.0797-0.6924-0.01040.89520.7831-0.0918-0.2220.24160.20950.924133.2901-36.26441.2635
223.545412.2198-7.08477.7177-2.35613.4372-0.3966-0.68270.2574-0.03950.12340.30360.33660.63890.27310.6645-0.08330.01650.2330.06360.893443.3305-30.168242.1557
314.77829.84992.82239.11337.36212.3523-0.3730.7632-0.4334-0.30130.6197-0.3625-0.26340.2943-0.24670.56380.09560.04140.36220.10670.835451.6846-32.546839.6108
424.6249-3.5224-4.670112.55032.27511.10830.62560.40690.3904-0.1443-0.4244-0.9606-0.1071-0.1854-0.20110.5035-0.13-0.01450.44220.05920.770440.9124-34.624445.2019
52.1371-1.17674.60990.6492-2.5369.9553-0.0819-0.1782-0.07110.04120.1470.0419-0.3134-0.3581-0.06510.5529-0.2386-0.05350.24210.05480.97333.6532-38.240650.6441
69.20883.5312.0769.051-8.653912.07570.43260.2052-0.12020.59830.14920.3862-0.4813-0.0451-0.58180.5713-0.1050.01340.3090.05610.908332.187-42.501251.4625
725.3944.78272.274220.692412.72467.9467-0.2473-0.0892-0.91570.25250.30190.4679-0.01640.0389-0.05460.67620.04140.32220.73260.66361.324823.1142-48.097556.2863
864.155822.201-48.975728.7423-4.832144.37171.12780.55620.9222-0.01560.6187-1.4631-1.1172-0.2584-1.74650.2726-0.0916-0.33970.65750.26510.823920.533-50.60746.8958
916.349-14.49565.559814.9447-7.57645.24140.78380.34670.0313-0.6368-0.39260.27770.23120.2079-0.39120.5672-0.3432-0.12390.3751-0.02350.88328.7631-49.024652.5909
104.004-0.28266.880837.18390.613211.8837-0.53060.4825-0.16880.91070.7189-1.345-0.8530.797-0.18830.4266-0.28560.00220.5117-0.08460.965330.1983-61.66258.813
111.0752-0.66221.13771.28771.00734.53240.0953-0.0401-0.1391-0.20120.04710.0624-0.1673-0.0753-0.14240.4707-0.2314-0.06470.34810.03770.793537.9401-59.584649.8362
1220.85812.2403-16.00750.2484-1.693212.37592.08813.03373.20770.36480.36350.3291-1.0728-2.3195-2.45163.05020.29630.29430.6070.20370.910337.7576-61.958140.7971
133.2132-1.8648-1.764513.0713-2.39561.94450.02650.4550.097-1.7895-0.1279-0.57150.4922-0.29330.10150.6168-0.359-0.16810.41210.15010.798335.0499-54.335338.3195
142.4119-5.5253-5.351624.146815.334412.7058-0.0906-0.1667-0.257-0.5343-0.48310.23560.0680.10490.57370.5801-0.3052-0.14040.36760.07030.864131.44-48.99741.1211
159.27238.2457-9.20837.3338-8.18899.1467-0.1083-0.2926-0.415-0.1154-0.2565-0.37750.1150.28740.36480.6838-0.2189-0.01920.3250.02930.972136.8753-51.689650.5102
1622.73546.000624.53316.793717.164948.61750.2524-0.7478-0.7960.0096-0.05460.0390.2768-0.8738-0.19790.2911-0.3065-0.23110.5270.07630.82925.7965-55.413645.4477
179.2157-7.089813.19386.7507-6.292831.5705-0.2405-0.4301-0.72680.26410.17060.5709-0.1505-1.60850.06990.4025-0.3251-0.10240.5177-0.0571.130521.2241-60.191848.6509
181.45272.748-1.356714.2524-0.60981.6907-0.39740.0204-0.0584-0.49510.33660.17480.37990.05380.06080.5852-0.3479-0.01830.27270.12710.868332.671-62.350349.1976
196.8411-5.8470.31416.5058-0.39441.3136-0.75220.2497-0.6043-0.20220.54540.14040.2812-0.55090.20690.5044-0.34810.0060.37240.01830.831132.8656-67.324550.4137
208.0524-15.5231-8.055430.086415.52778.059-0.5248-0.48160.50460.67761.0867-0.67690.47350.466-0.56190.4648-0.4314-0.28090.67970.22620.776719.8393-53.870958.6864
2118.86357.0095-10.07732.6682-3.728112.45160.26560.84120.0093-0.05610.2573-0.02170.9029-0.7407-0.52290.7313-0.04630.03470.18590.00540.831850.7374-48.988934.7454
2217.04581.9247-5.82570.4821-1.10962.778-0.20720.34150.372-0.51880.0372-0.11590.9103-0.16350.16990.9501-0.02240.17850.1020.02810.843356.7622-45.48727.374
230.1559-0.9460.30827.4055-2.33520.74080.1301-0.1311-0.0255-0.5008-0.01480.23910.166-0.0396-0.11530.5948-0.20730.01480.5160.06640.939353.152-41.109943.0582
2410.9553-1.0902-7.46250.1891.907523.27670.3512-0.4467-0.2059-0.0378-0.0143-0.05830.3114-1.0108-0.33680.5635-0.2026-0.00480.24670.0970.873744.2191-39.984655.3537
255.37843.7446-5.746210.06660.59249.07830.15610.1138-0.0071-0.272-0.2474-0.161-0.1854-0.34220.09130.486-0.02680.0870.16780.16320.942255.6116-40.391134.6318
260.84161.4093-0.6372.3653-1.06940.48390.0385-0.04370.01570.016-0.07-0.0184-0.01560.03850.03160.5704-0.1325-0.01860.27170.05340.890553.6255-34.025347.6924
2722.725-3.2328-20.79552.25638.007833.2289-0.8434-0.0724-0.6092-0.09120.16120.11210.15770.5580.68220.6656-0.00980.00820.03380.1381.065361.0322-50.263936.4272
281.4889-0.97770.14522.4938-1.99672.65320.0569-0.2492-0.06920.5249-0.135-0.0424-0.2562-0.09910.07820.6296-0.1894-0.04990.32380.05990.793451.2489-25.513656.5678
291.9862-0.33513.06362.7625-0.9074.84920.10110.244-0.36990.24580.34540.3696-0.07890.3718-0.44650.5843-0.1193-0.06720.34780.07560.961753.7051-22.852944.8956
300.4846-1.08350.50862.4559-1.15630.5509-0.1294-0.2461-0.17350.23090.34070.3015-0.1872-0.2032-0.21131.1116-0.1912-0.06990.84710.17471.112337.3417-22.194431.7404
311.3789-0.66871.30090.5217-0.70571.3329-0.1233-0.10990.0678-0.0081-0.1578-0.1958-0.0364-0.06520.28110.6319-0.097-0.00390.28780.10980.849554.319-24.306344.9351
320.38831.36010.09024.8804-0.00311.2347-0.0384-0.08740.02180.0866-0.3254-0.015-0.3683-0.24940.36390.5325-0.0271-0.04570.31790.06540.778653.073-16.208337.0157
3311.0117-3.926-2.02761.90691.71062.62630.2145-0.20790.4763-0.1494-0.0355-0.3987-0.6434-0.1823-0.17910.8022-0.1916-0.19560.2194-0.02020.912160.8279-20.134655.9102
344.6915-9.826713.467220.6895-28.297138.7345-0.1984-0.3108-0.08790.65220.56160.3528-0.8109-0.8115-0.36320.6451-0.1225-0.03740.2893-0.05280.896649.5494-11.171646.4009
350.6687-0.02850.18760.6090.0850.0850.07850.08660.074-0.0938-0.20620.0179-0.053-0.00760.12770.6211-0.0059-0.05340.26410.05860.820751.9442-11.18325.6668
361.34880.17451.12743.02730.65361.0337-0.04050.02040.1614-0.0689-0.1463-0.0766-0.0558-0.01510.18680.6339-0.03770.02780.28580.09620.771758.7772-9.974833.2922
3714.79936.27694.51972.77042.933111.54920.18780.002-0.47720.10580.0013-0.20981.01480.0068-0.18920.8455-0.03260.0350.0372-0.00980.904652.0857-29.961223.9637
383.05111.03561.69213.42124.66636.41690.1317-0.25840.09030.0396-0.1314-0.08350.1532-0.1815-0.00030.6245-0.00220.04140.21420.11290.798759.908-18.824630.5976
391.90860.3032.12365.0442-1.64793.17530.3413-0.24360.0572-0.192-0.5174-0.22620.517-0.02230.1760.60020.04540.08050.22070.07710.855659.5102-24.460829.7615
403.06730.316-1.12742.25611.0641.07260.02080.1154-0.4623-0.3213-0.3088-0.11-0.2399-0.18660.2880.56230.0513-0.00180.22330.14490.935762.2112-12.947819.5567
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 16
2X-RAY DIFFRACTION2A17 - 23
3X-RAY DIFFRACTION3A24 - 28
4X-RAY DIFFRACTION4A29 - 33
5X-RAY DIFFRACTION5A34 - 41
6X-RAY DIFFRACTION6A42 - 46
7X-RAY DIFFRACTION7A47 - 51
8X-RAY DIFFRACTION8A52 - 57
9X-RAY DIFFRACTION9A58 - 62
10X-RAY DIFFRACTION10A63 - 68
11X-RAY DIFFRACTION11A69 - 78
12X-RAY DIFFRACTION12A79 - 83
13X-RAY DIFFRACTION13A84 - 90
14X-RAY DIFFRACTION14A91 - 96
15X-RAY DIFFRACTION15A97 - 101
16X-RAY DIFFRACTION16A102 - 107
17X-RAY DIFFRACTION17A108 - 111
18X-RAY DIFFRACTION18A112 - 116
19X-RAY DIFFRACTION19A117 - 126
20X-RAY DIFFRACTION20A127 - 132
21X-RAY DIFFRACTION21U1 - 12
22X-RAY DIFFRACTION22U13 - 23
23X-RAY DIFFRACTION23U24 - 30
24X-RAY DIFFRACTION24U31 - 40
25X-RAY DIFFRACTION25U41 - 49
26X-RAY DIFFRACTION26U50 - 72
27X-RAY DIFFRACTION27U73 - 79
28X-RAY DIFFRACTION28U80 - 118
29X-RAY DIFFRACTION29U119 - 130
30X-RAY DIFFRACTION30U131 - 137
31X-RAY DIFFRACTION31U138 - 157
32X-RAY DIFFRACTION32U158 - 169
33X-RAY DIFFRACTION33U170 - 178
34X-RAY DIFFRACTION34U179 - 185
35X-RAY DIFFRACTION35U186 - 213
36X-RAY DIFFRACTION36U214 - 224
37X-RAY DIFFRACTION37U225 - 235
38X-RAY DIFFRACTION38U236 - 249
39X-RAY DIFFRACTION39U250 - 266
40X-RAY DIFFRACTION40U267 - 280

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