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- PDB-5la6: Tubulin-pironetin complex -

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Basic information

Entry
Database: PDB / ID: 5la6
TitleTubulin-pironetin complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine Ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / spindle microtubule / protein modification process ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / microtubule cytoskeleton / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / cilium / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytoplasm / cytosol
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Helix hairpin bin / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Helix hairpin bin / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / ATP-grasp fold, A domain / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Dna Ligase; domain 1 / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Helix non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / PIRONETIN / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain / Tubulin beta-2B chain
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Gallus gallus (chicken)
Bos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.1 Å
AuthorsProta, A.E. / Setter, J. / Waight, A.B. / Bargsten, K. / Murga, J. / Diaz, J.F. / Steinmetz, M.O.
Funding support Switzerland, Spain, 4items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_138659 and 31003A_166608 Switzerland
Spanish Ministry of Economy and CompetitivenessCTQ2014-52949-P Spain
Cultura i Sport de la Generalitat ValencianaPROMETEO 2013/027 Spain
Spanish Ministry of Economy and CompetitivenessBIO2013-42984-R and S2010/BMD-2457 BIPEDD2 Spain
CitationJournal: J.Mol.Biol. / Year: 2016
Title: Pironetin Binds Covalently to alpha Cys316 and Perturbs a Major Loop and Helix of alpha-Tubulin to Inhibit Microtubule Formation.
Authors: Prota, A.E. / Setter, J. / Waight, A.B. / Bargsten, K. / Murga, J. / Diaz, J.F. / Steinmetz, M.O.
History
DepositionJun 13, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 20, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 17, 2016Group: Database references
Revision 1.2Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Jan 10, 2024Group: 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
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_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.ptnr3_symmetry / _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.ptnr2_symmetry / _struct_conn_type.id
Revision 1.4Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tubulin alpha-1B chain
B: Tubulin beta-2B chain
C: Tubulin alpha-1B chain
D: Tubulin beta-2B chain
E: Stathmin-4
F: Tubulin-Tyrosine Ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)264,62919
Polymers261,6316
Non-polymers2,99813
Water6,990388
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21760 Å2
ΔGint-141 kcal/mol
Surface area79430 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.680, 157.200, 180.990
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein Tubulin alpha-1B chain / Alpha-tubulin ubiquitous / Tubulin K-alpha-1 / Tubulin alpha-ubiquitous chain


Mass: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Tissue: brain / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / Tissue: brain / References: UniProt: Q6B856
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63043
#4: Protein Tubulin-Tyrosine Ligase


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 7 types, 401 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#9: Chemical ChemComp-X3H / PIRONETIN


Mass: 326.471 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H34O4
#10: Chemical ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 388 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.87 Å3/Da / Density % sol: 57.19 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 5% PEG, 12% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00002 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Oct 2, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00002 Å / Relative weight: 1
ReflectionResolution: 2.1→48.3 Å / Num. obs: 175571 / % possible obs: 99.9 % / Redundancy: 13.6 % / Rsym value: 0.106 / Net I/σ(I): 18.9
Reflection shellResolution: 2.1→2.15 Å / Redundancy: 13 % / Mean I/σ(I) obs: 0.6 / Rsym value: 4.643 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.1→48.27 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.1
RfactorNum. reflection% reflection
Rfree0.231 8728 4.97 %
Rwork0.184 --
obs0.187 175542 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.1→48.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17302 0 181 388 17871
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717889
X-RAY DIFFRACTIONf_angle_d0.96824256
X-RAY DIFFRACTIONf_dihedral_angle_d15.5686640
X-RAY DIFFRACTIONf_chiral_restr0.0382645
X-RAY DIFFRACTIONf_plane_restr0.0043145
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12380.41082940.39915473X-RAY DIFFRACTION99
2.1238-2.14880.40172940.36855469X-RAY DIFFRACTION100
2.1488-2.1750.36043000.34615485X-RAY DIFFRACTION100
2.175-2.20260.36612920.32835532X-RAY DIFFRACTION100
2.2026-2.23150.36513090.32655487X-RAY DIFFRACTION100
2.2315-2.26210.3332790.31495506X-RAY DIFFRACTION100
2.2621-2.29440.34563040.30295502X-RAY DIFFRACTION100
2.2944-2.32870.35582760.2935509X-RAY DIFFRACTION100
2.3287-2.36510.3423100.28485484X-RAY DIFFRACTION100
2.3651-2.40380.32932950.26765552X-RAY DIFFRACTION100
2.4038-2.44530.30423180.2575482X-RAY DIFFRACTION100
2.4453-2.48970.29172810.23775510X-RAY DIFFRACTION100
2.4897-2.53760.27632870.23025529X-RAY DIFFRACTION100
2.5376-2.58940.27892980.22295537X-RAY DIFFRACTION100
2.5894-2.64570.29082910.22075542X-RAY DIFFRACTION100
2.6457-2.70730.30093140.22345521X-RAY DIFFRACTION100
2.7073-2.7750.26182920.21295513X-RAY DIFFRACTION100
2.775-2.850.25462840.20325560X-RAY DIFFRACTION100
2.85-2.93380.28912680.20755569X-RAY DIFFRACTION100
2.9338-3.02850.25182850.20255578X-RAY DIFFRACTION100
3.0285-3.13670.26462890.19845532X-RAY DIFFRACTION100
3.1367-3.26230.23832640.19585610X-RAY DIFFRACTION100
3.2623-3.41070.24952970.19165567X-RAY DIFFRACTION100
3.4107-3.59050.22072900.1815577X-RAY DIFFRACTION100
3.5905-3.81540.22082610.17045644X-RAY DIFFRACTION100
3.8154-4.10980.18822640.14575647X-RAY DIFFRACTION100
4.1098-4.52310.17122850.1355626X-RAY DIFFRACTION100
4.5231-5.1770.1832970.13255652X-RAY DIFFRACTION100
5.177-6.51990.21483010.16085719X-RAY DIFFRACTION100
6.5199-48.28470.17563090.15435900X-RAY DIFFRACTION100
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)
12.9141-0.1927-0.1066.64940.62812.9033-0.00010.03990.6952-0.65380.3984-0.635-1.43110.4974-0.37781.0081-0.17590.25080.5237-0.16140.644429.168398.833454.9308
24.5543-0.88452.22932.22213.25176.2807-0.14810.39910.6086-1.87070.2488-0.2996-1.79720.5056-0.18371.0249-0.13390.18340.5598-0.07690.567229.107887.681143.0063
32.4841-0.1997-0.15314.51290.48472.5833-0.01150.06210.1418-0.46360.4036-1.0092-0.51230.8887-0.37490.457-0.13720.15140.7536-0.28260.661238.34480.306352.2086
44.44580.2755-0.82844.71530.86532.74150.0926-0.18560.11280.340.141-0.3372-0.0180.4031-0.23570.46490.05940.0060.5056-0.1570.454629.602474.54460.0525
58.5797-5.32412.91887.4684-2.97245.96430.38140.1837-0.4882-0.08290.09891.2604-0.002-1.2273-0.38790.41110.05520.04460.6344-0.08020.68077.994779.190858.5253
65.34314.53022.78257.75545.21496.07850.1495-0.20770.6090.1114-0.18750.5906-0.6375-0.10650.03250.57650.08140.15170.4629-0.05820.533820.266489.562160.3757
75.22840.6911-0.19862.08722.66345.88230.0764-0.39820.26470.94510.742-1.7288-0.50831.2243-0.79230.6607-0.0392-0.01710.7688-0.26930.714232.768785.002972.8993
81.67040.44360.4684.83530.66543.69940.0994-0.28370.27680.93750.00240.59-0.5524-0.3036-0.09050.66320.03480.21480.4891-0.11610.545715.083287.47574.6843
91.7354-0.6184-0.64395.8524.51285.6705-0.0142-0.1787-0.18150.85120.4906-0.47751.03531.047-0.43490.49540.174-0.10780.5307-0.1370.52729.415562.063962.5881
106.7251-1.76691.00777.74551.62655.8344-0.00060.2181.1011-0.5998-0.19050.2449-1.444-0.44090.19720.76550.15820.03130.55710.00590.526716.087972.627222.4533
115.7503-1.9868-0.05146.38551.12837.67520.2331.11130.3887-1.5005-0.48530.4178-0.8842-0.61970.20340.77740.1625-0.01290.7264-0.00960.510820.187462.132710.7983
123.2877-0.6073-1.38715.79223.66555.2992-0.02640.23210.2427-0.57250.2339-0.2851-0.70660.3942-0.20580.3856-0.02530.04040.478-0.05120.393629.490156.964420.8833
134.13611.7561-0.19288.66643.05763.8921-0.094-0.1781-0.1408-0.1417-0.11670.0232-0.1124-0.26150.1890.29480.07070.0190.4485-0.08290.339621.337850.144928.1976
142.0287-3.00480.34093.7713-2.06674.9303-0.4993-0.0251-0.1557-0.2677-0.43981.39940.8132-2.30620.75070.5151-0.0423-0.0421.1299-0.46320.9363-0.364749.11726.0383
154.51311.66911.50617.04735.86678.11660.0665-0.33330.327-0.8445-0.77781.0882-1.0502-1.30910.70930.45890.1488-0.0510.5878-0.13130.52139.665562.605727.9052
162.33282.01011.14995.7848-3.88066.3922-0.0414-0.10890.28370.63880.150.5729-0.5195-0.1179-0.15690.34380.06520.02650.4081-0.12470.443122.818762.335641.3275
175.2749-2.15381.46154.55280.22042.9182-0.2344-0.30570.17570.1808-0.1710.7196-0.2719-1.22530.38770.43830.10460.01410.7618-0.21240.55075.674960.799842.6963
181.4706-1.5396-1.18735.94565.32883.3775-0.2353-0.257-0.23160.90910.08380.14281.01120.34580.16130.50750.01590.00350.4651-0.01040.397222.694837.756831.3424
192.995-1.21630.07977.0819-0.46343.4183-0.11370.14580.4915-0.36320.02770.0518-0.75380.06250.09230.4181-0.0774-0.02970.40540.01990.359213.43744.1405-12.4136
204.7842-3.54480.10277.09850.37655.7632-0.03440.71080.0644-1.23550.1386-0.029-0.362-0.2818-0.15690.5344-0.14790.02640.54490.00450.354118.80132.168-22.3149
211.0485-0.5150.0637.60922.32322.7803-0.11530.26060.0331-0.51280.3147-0.5798-0.20640.4489-0.18970.2994-0.07270.05540.4887-0.0670.433627.523528.9842-10.54
221.7717-0.8133-1.00483.9895-0.30382.6544-0.1273-0.01970.1004-0.02190.04160.01780.17820.13640.06370.2614-0.01110.0220.321-0.0440.314919.439321.7819-3.2669
237.904-2.21861.67522.1639-1.84096.93610.1143-0.2708-0.7591-0.25010.01941.16610.4857-1.4439-0.06520.3778-0.1054-0.01270.5153-0.06010.5877-1.84619.771-8.6009
246.22984.59423.03362.46017.05459.8987-0.1852-0.13230.5851-0.531-0.2220.7648-0.4228-0.54980.39590.30820.0097-0.04450.34220.06050.40586.540334.4134-6.4469
257.9497-1.35893.64311.4117-3.93342.0060.11110.75350.9595-0.38720.74691.2594-0.3069-0.6069-0.69941.1626-0.1422-0.18650.59570.11140.730617.801938.59979.1117
267.41374.62414.16333.5358-0.05952.1593-0.1133-0.1610.64940.25090.12910.161-0.33170.3471-0.04750.33620.00080.04170.3511-0.07660.35819.096227.324310.1492
273.7661-1.96721.9063.948-0.74444.4115-0.1974-0.35960.13760.3637-0.0650.315-0.1927-0.74810.23490.3327-0.05680.05150.4873-0.10920.4149-0.814831.90846.4085
282.5634-1.5926-2.19414.19624.71167.369-0.0674-0.0989-0.05410.42160.2407-0.15370.72850.3751-0.17270.41150.0365-0.00530.326-0.00890.415122.123810.82842.2049
295.3384-2.3262-0.12595.51121.0844.2594-0.13960.8690.1653-0.86070.09620.0836-0.2321-0.2180.08090.6868-0.17810.01810.8689-0.05730.360815.34512.1174-41.6754
303.746-2.1333-1.87414.54791.30152.4763-0.01121.4961-0.5018-1.57630.1038-0.06550.34130.0515-0.03351.2814-0.30830.18351.4259-0.2980.619524.37961.5966-50.4044
312.36360.0482-0.18344.26670.93642.8087-0.21490.6353-0.4469-0.6010.1175-0.4280.34320.32640.05240.7724-0.13910.22970.902-0.28220.629432.18780.3822-37.9874
322.9571-0.9930.09662.8190.15211.3581-0.52720.3931-0.6338-0.42210.5216-0.10130.78770.1819-0.01110.8752-0.14310.18970.6733-0.25940.581924.4621-7.5994-31.2811
332.7965-2.62240.93034.34752.86568.0458-0.60171.0938-1.4271-0.8229-0.00061.140.763-0.51270.46961.305-0.50240.12851.1548-0.42390.83144.7258-14.5301-37.0281
343.1542-1.1895-0.75132.21276.49175.6125-0.17530.2602-0.3954-0.6119-0.11490.73180.1579-0.46450.25560.6722-0.1678-0.00540.6601-0.10510.484110.44191.3171-35.7706
352.4691-1.21383.07685.9617-4.32415.4073-0.12210.3218-0.36290.01480.19710.34650.07550.0313-0.11340.4168-0.07990.09650.4956-0.13060.414319.78825.9224-20.3225
361.9879-0.7873-1.15152.56280.52662.6508-0.16940.5972-0.4392-0.37140.01220.38280.5062-0.67750.15740.5446-0.19080.02810.6256-0.14830.494.39520.1047-21.013
375.1096-1.0864-2.80993.08111.7043.05-0.49370.5858-0.9866-0.04460.1239-0.14171.16370.14630.37891.0230.030.16540.6197-0.23320.753327.492-17.8688-24.6613
383.64050.4424-0.34187.6721-5.34956.67970.4684-0.74280.36570.9319-0.25830.0519-0.27120.7623-0.18331.0876-0.11660.0710.763-0.18650.63925.593894.601884.7316
391.63223.30183.42476.70287.50449.5827-0.0141-0.22850.33930.32920.6252-0.61680.21991.0783-0.63320.4550.04520.00391.005-0.35380.862743.753555.161834.4511
400.1751-1.5599-1.71372.38511.82022.3159-0.13450.1031-0.24390.24810.2899-0.45220.60870.6737-0.24640.67350.04360.13210.9289-0.29620.862342.18337.3703-18.4087
414.31342.4285-1.76646.1073-0.55736.8722-0.63080.5656-1.0127-0.45940.3563-0.25981.785-0.42360.28210.9372-0.07410.17180.5185-0.17680.64716.452654.675169.9193
422.30362.3743-0.91446.6304-8.50152.13530.1655-0.84770.03961.1722-0.1705-0.333-0.24291.0246-0.00250.76270.06710.01740.6929-0.01390.529311.325465.735397.4088
434.3881.37193.80684.4774-1.47515.1479-0.1808-1.10920.42010.6226-0.2-0.7044-0.22641.51130.6441.07740.0951-0.27921.61660.22871.103723.281861.2494108.1911
445.4693-0.29011.28786.18420.35121.3468-0.2519-0.9047-0.63181.27040.428-0.96191.16870.9133-0.26251.21090.3764-0.11211.53120.50171.234219.549552.496106.4431
457.8630.87940.04941.4901-0.44796.3595-0.1504-1.3488-1.79240.5043-0.1005-0.58141.58160.43840.35791.45510.32370.20130.8170.3390.8830.600247.4695110.6855
461.52780.8509-2.0042.5536-1.45133.3582-0.6173-0.4544-1.09260.46930.1192-0.32861.32530.34170.50611.45120.17410.29570.61660.19881.1107-1.263346.83799.4796
473.90740.1642-4.59171.35040.69627.89170.22110.08250.08690.40560.33810.1894-0.3669-0.2408-0.61390.69480.12610.08970.43060.03630.5310.677266.088188.5359
482.94340.2914-2.51371.5879-0.34364.193-0.5978-0.6129-0.79650.34290.1438-0.08441.71730.5510.41521.05170.17110.15390.53020.15650.64362.488455.707997.5197
494.20680.9309-2.24462.1358-5.74049.1975-0.17550.4487-0.8055-0.74960.24880.86211.9724-1.2409-0.07790.9446-0.31580.09010.7341-0.2060.7524-6.061553.33676.9635
502.05391.50665.59188.48820.79612.0441-0.1653-0.18971.4211-0.7496-0.36920.04-0.201-0.48371.05280.81830.08190.18160.6780.04190.8925-8.832163.502286.8408
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 1 THROUGH 64 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 65 THROUGH 99 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 100 THROUGH 160 )
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESID 161 THROUGH 205 )
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESID 206 THROUGH 223 )
6X-RAY DIFFRACTION6CHAIN 'A' AND (RESID 224 THROUGH 244 )
7X-RAY DIFFRACTION7CHAIN 'A' AND (RESID 245 THROUGH 268 )
8X-RAY DIFFRACTION8CHAIN 'A' AND (RESID 269 THROUGH 381 )
9X-RAY DIFFRACTION9CHAIN 'A' AND (RESID 382 THROUGH 438 )
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESID 2 THROUGH 64 )
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESID 65 THROUGH 99 )
12X-RAY DIFFRACTION12CHAIN 'B' AND (RESID 100 THROUGH 160 )
13X-RAY DIFFRACTION13CHAIN 'B' AND (RESID 161 THROUGH 205 )
14X-RAY DIFFRACTION14CHAIN 'B' AND (RESID 206 THROUGH 223 )
15X-RAY DIFFRACTION15CHAIN 'B' AND (RESID 224 THROUGH 244 )
16X-RAY DIFFRACTION16CHAIN 'B' AND (RESID 245 THROUGH 266 )
17X-RAY DIFFRACTION17CHAIN 'B' AND (RESID 267 THROUGH 381 )
18X-RAY DIFFRACTION18CHAIN 'B' AND (RESID 382 THROUGH 438 )
19X-RAY DIFFRACTION19CHAIN 'C' AND (RESID 1 THROUGH 64 )
20X-RAY DIFFRACTION20CHAIN 'C' AND (RESID 65 THROUGH 99 )
21X-RAY DIFFRACTION21CHAIN 'C' AND (RESID 100 THROUGH 160 )
22X-RAY DIFFRACTION22CHAIN 'C' AND (RESID 161 THROUGH 205 )
23X-RAY DIFFRACTION23CHAIN 'C' AND (RESID 206 THROUGH 223 )
24X-RAY DIFFRACTION24CHAIN 'C' AND (RESID 224 THROUGH 245 )
25X-RAY DIFFRACTION25CHAIN 'C' AND (RESID 254 THROUGH 257 )
26X-RAY DIFFRACTION26CHAIN 'C' AND (RESID 258 THROUGH 268 )
27X-RAY DIFFRACTION27CHAIN 'C' AND (RESID 269 THROUGH 381 )
28X-RAY DIFFRACTION28CHAIN 'C' AND (RESID 382 THROUGH 440 )
29X-RAY DIFFRACTION29CHAIN 'D' AND (RESID 2 THROUGH 64 )
30X-RAY DIFFRACTION30CHAIN 'D' AND (RESID 65 THROUGH 99 )
31X-RAY DIFFRACTION31CHAIN 'D' AND (RESID 100 THROUGH 160 )
32X-RAY DIFFRACTION32CHAIN 'D' AND (RESID 161 THROUGH 205 )
33X-RAY DIFFRACTION33CHAIN 'D' AND (RESID 206 THROUGH 223 )
34X-RAY DIFFRACTION34CHAIN 'D' AND (RESID 224 THROUGH 244 )
35X-RAY DIFFRACTION35CHAIN 'D' AND (RESID 245 THROUGH 266 )
36X-RAY DIFFRACTION36CHAIN 'D' AND (RESID 267 THROUGH 381 )
37X-RAY DIFFRACTION37CHAIN 'D' AND (RESID 382 THROUGH 441 )
38X-RAY DIFFRACTION38CHAIN 'E' AND (RESID 6 THROUGH 28 )
39X-RAY DIFFRACTION39CHAIN 'E' AND (RESID 44 THROUGH 90 )
40X-RAY DIFFRACTION40CHAIN 'E' AND (RESID 91 THROUGH 139 )
41X-RAY DIFFRACTION41CHAIN 'F' AND (RESID 1 THROUGH 66 )
42X-RAY DIFFRACTION42CHAIN 'F' AND (RESID 67 THROUGH 96 )
43X-RAY DIFFRACTION43CHAIN 'F' AND (RESID 97 THROUGH 139 )
44X-RAY DIFFRACTION44CHAIN 'F' AND (RESID 140 THROUGH 184 )
45X-RAY DIFFRACTION45CHAIN 'F' AND (RESID 185 THROUGH 198 )
46X-RAY DIFFRACTION46CHAIN 'F' AND (RESID 199 THROUGH 278 )
47X-RAY DIFFRACTION47CHAIN 'F' AND (RESID 279 THROUGH 312 )
48X-RAY DIFFRACTION48CHAIN 'F' AND (RESID 313 THROUGH 339 )
49X-RAY DIFFRACTION49CHAIN 'F' AND (RESID 340 THROUGH 362 )
50X-RAY DIFFRACTION50CHAIN 'F' AND (RESID 373 THROUGH 380 )

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