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- PDB-4o4i: Tubulin-Laulimalide-Epothilone A complex -

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Basic information

Entry
Database: PDB / ID: 4o4i
TitleTubulin-Laulimalide-Epothilone A complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligase
KeywordsCELL CYCLE/INHIBITOR / ALPHA-TUBULIN / BETA-TUBULIN / LIGASE / GTPASE / MICROTUBULE / STATHMIN / LAULIMALIDE / EPOTHILONE A / CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / CELL CYCLE-INHIBITOR complex
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 / tubulin binding / cellular response to interleukin-4 / 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 / tubulin binding / cellular response to interleukin-4 / 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 / EPOTHILONE A / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Laulimalide / 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 / DIFFERENCE FOURIER / Resolution: 2.4 Å
AuthorsProta, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Structural basis of microtubule stabilization by laulimalide and peloruside a.
Authors: Prota, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
History
DepositionDec 18, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 12, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _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.value / _struct_conn.pdbx_dist_value / _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_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: 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)266,03324
Polymers261,6316
Non-polymers4,40118
Water9,134507
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)105.200, 158.030, 180.400
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 / Details: BRAIN / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


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


Mass: 16844.162 Da / Num. of mol.: 1 / Fragment: UNP residues 49-189
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / 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) / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 9 types, 525 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.: 6 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / 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-EP / EPOTHILONE A


Mass: 493.656 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H39NO6S
#10: Chemical ChemComp-LLM / Laulimalide / (1R,3S,7S,8S,10S,12S,15Z,18R)-7-hydroxy-12-{(1S,2E)-1-hydroxy-3-[(2S)-4-methyl-3,6-dihydro-2H-pyran-2-yl]prop-2-en-1-yl }-3-methyl-5-methylidene-9,13,22-trioxatricyclo[16.3.1.0~8,10~]docosa-15,19-dien-14-one


Mass: 514.650 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C30H42O7
#11: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: 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
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 507 / 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: 2.87 Å3/Da / Density % sol: 57.08 %
Crystal growTemperature: 293 K / pH: 6.7
Details: 6% PEG, 16% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1
DetectorType: PSI PILATUS 2M / Detector: PIXEL / Date: Feb 10, 2013
RadiationMonochromator: VERTICALLY COLLIMATING MIRROR (M1, FOCUS AT INFINITY), FOLLOWED BY A BARTELS MONOCHROMATOR WITH DUAL CHANNEL CUT CRYSTALS (DCCM) IN (+--+) GEOMETRY, AND A TOROIDAL MIRROR (M2) TO ...Monochromator: VERTICALLY COLLIMATING MIRROR (M1, FOCUS AT INFINITY), FOLLOWED BY A BARTELS MONOCHROMATOR WITH DUAL CHANNEL CUT CRYSTALS (DCCM) IN (+--+) GEOMETRY, AND A TOROIDAL MIRROR (M2) TO VERTICALLY AND HORIZONTALLY FOCUS THE BEAM AT THE SAMPLE POSITION (WITH 2:1 HORIZONTAL DEMAGNIFICATION)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→52.2 Å / Num. obs: 117491 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 13.4 % / Rmerge(I) obs: 0.136 / Net I/σ(I): 18.5
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 12.7 % / Rmerge(I) obs: 2.253 / Mean I/σ(I) obs: 1.3 / % possible all: 98.9

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Processing

Software
NameVersionClassification
DA+data collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 4O4H

4o4h


Resolution: 2.4→52.206 Å / SU ML: 0.3 / σ(F): 1.99 / Phase error: 23.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2144 5885 5.01 %
Rwork0.1882 --
obs0.1896 117475 99.67 %
all-117880 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.4→52.206 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17460 0 277 507 18244
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00718202
X-RAY DIFFRACTIONf_angle_d1.26724704
X-RAY DIFFRACTIONf_dihedral_angle_d18.956798
X-RAY DIFFRACTIONf_chiral_restr0.0822703
X-RAY DIFFRACTIONf_plane_restr0.0053197
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4001-2.42730.33052210.33313575X-RAY DIFFRACTION99
2.4273-2.45590.33931850.30663654X-RAY DIFFRACTION99
2.4559-2.48580.28641940.28633685X-RAY DIFFRACTION100
2.4858-2.51730.36561600.29333703X-RAY DIFFRACTION99
2.5173-2.55040.30552050.28573681X-RAY DIFFRACTION100
2.5504-2.58540.29241880.26773632X-RAY DIFFRACTION99
2.5854-2.62230.28691950.26333669X-RAY DIFFRACTION100
2.6223-2.66140.3271990.26463693X-RAY DIFFRACTION99
2.6614-2.7030.31192240.25433659X-RAY DIFFRACTION99
2.703-2.74730.29041840.24683696X-RAY DIFFRACTION100
2.7473-2.79470.27191970.24623684X-RAY DIFFRACTION99
2.7947-2.84550.28931980.24013701X-RAY DIFFRACTION100
2.8455-2.90020.27491770.23883709X-RAY DIFFRACTION100
2.9002-2.95940.27481680.23173732X-RAY DIFFRACTION100
2.9594-3.02380.2381890.21353697X-RAY DIFFRACTION100
3.0238-3.09410.26851920.21723704X-RAY DIFFRACTION100
3.0941-3.17150.27241980.21443714X-RAY DIFFRACTION100
3.1715-3.25720.25522040.21473700X-RAY DIFFRACTION100
3.2572-3.35310.26771960.20343709X-RAY DIFFRACTION100
3.3531-3.46130.23041800.18953748X-RAY DIFFRACTION100
3.4613-3.58490.20382070.17923719X-RAY DIFFRACTION100
3.5849-3.72840.19921980.17173714X-RAY DIFFRACTION100
3.7284-3.89810.19561960.15863757X-RAY DIFFRACTION100
3.8981-4.10350.18222000.15073728X-RAY DIFFRACTION100
4.1035-4.36050.15751860.14423783X-RAY DIFFRACTION100
4.3605-4.6970.15091990.13053754X-RAY DIFFRACTION100
4.697-5.16930.17081960.14093784X-RAY DIFFRACTION100
5.1693-5.91640.20271960.16943818X-RAY DIFFRACTION100
5.9164-7.45060.21032110.18193838X-RAY DIFFRACTION100
7.4506-52.21860.14762420.16353950X-RAY DIFFRACTION99
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)
11.6006-0.4238-0.85662.5037-0.51221.74320.21220.15610.3517-0.2005-0.0238-0.0929-0.58950.0627-0.19910.5079-0.01090.05970.3171-0.09190.349428.863899.28554.6882
21.15610.41450.25732.55990.1351.8848-0.01950.16810.0393-0.40160.0924-0.202-0.37880.088-0.08430.2799-0.02680.04410.3139-0.11920.275434.818183.532148.6169
31.2688-0.5002-0.42932.93140.55262.50880.0642-0.02240.08250.1241-0.01750.0103-0.07580.0625-0.04660.22640.00940.0060.2094-0.06760.237424.199881.135962.7731
40.8360.596-0.29151.30560.36994.15050.1454-0.15210.13620.1762-0.08440.7288-0.1814-0.7502-0.04490.38280.01520.12610.4139-0.12880.46569.185284.783971.5505
52.2212-0.91090.13620.97870.22140.8636-0.244-0.16750.03320.8675-0.01630.6692-0.0768-0.56020.18730.6030.00610.15950.3708-0.13110.333916.339590.693880.551
62.1192-0.00730.9292.3351-0.10042.88530.0384-0.109-0.05890.3054-0.01050.37770.0012-0.1046-0.00230.4529-0.02510.0820.3396-0.14390.395318.012889.826873.5757
70.8308-0.3136-0.24932.5431.47291.64080.0745-0.0432-0.04960.5622-0.03010.05870.3918-0.1182-0.09210.35850.01830.04630.2874-0.08610.282222.424869.848266.584
81.37030.1255-0.12132.1221.40953.4133-0.0223-0.1402-0.1150.49020.1698-0.15860.66960.6604-0.11020.34590.0704-0.0190.2591-0.08120.352132.773162.206761.1011
91.7293-0.235-0.17021.38730.77162.33910.00540.09810.2069-0.1344-0.12910.1967-0.4208-0.31410.0320.26050.0423-0.02260.3135-0.11910.312216.736760.022725.8266
100.7105-0.16030.31331.6310.80933.0026-0.078-0.18520.08570.4166-0.06860.17070.1143-0.34690.10880.2246-0.06440.02380.3131-0.07690.304515.185950.809538.2385
112.2973-0.8566-0.52083.5017-0.68741.92050.01180.14230.347-0.00110.03670.2279-0.37790.0973-0.04740.2579-0.0488-0.00390.2612-0.03550.254314.703842.6043-13.0134
121.379-0.49690.17332.10190.48881.6541-0.02050.13940.1164-0.40960.122-0.2196-0.15470.1736-0.07630.1949-0.07630.06350.2575-0.05370.24924.990130.6505-14.4431
131.8247-1.2267-0.68392.2825-0.98831.7614-0.0326-0.03-0.10650.19820.01460.00680.2070.13960.04980.179-0.00060.01030.1874-0.06490.195120.411220.7629-3.7113
141.5973-1.08220.49031.24620.62061.87520.0898-0.0380.03210.0398-0.15850.15810.0854-0.41130.04920.1816-0.04670.05350.2918-0.02840.23553.853128.91320.419
152.5228-0.74351.10092.1156-0.78691.9897-0.0838-0.1990.04820.04770.11440.25750.0915-0.3766-0.02890.2616-0.05120.04740.3047-0.07020.30451.206935.05238.8938
160.7474-0.7061-0.11661.7420.68861.4242-0.047-0.0084-0.0230.24170.0563-0.07910.33310.1762-0.01920.17730.0034-0.01530.199-0.05650.224620.338813.47482.694
173.1913-0.61180.33163.15390.23362.4838-0.28030.34430.324-0.28510.29530.1801-0.2718-0.01630.0080.3428-0.06640.01760.4369-0.02140.241715.059411.5299-40.9165
181.6203-0.8637-0.31412.9378-0.1331.7044-0.10770.5412-0.021-0.50840.1564-0.14980.0470.2281-0.03420.4196-0.04060.10610.6821-0.1910.395728.53142.4438-43.1007
191.9641-0.4777-0.34580.3794-0.15091.032-0.09250.1333-0.3039-0.06550.0887-0.14980.35930.0582-0.00790.475-0.0170.05280.4866-0.17190.415821.7517-8.6509-32.0646
203.90710.8027-0.00432.66280.56782.1389-0.09520.4818-0.1875-0.384-0.240.4890.344-0.90560.29180.499-0.07640.05040.4669-0.11140.29776.6775-7.6929-38.2189
210.48720.30980.3860.5713-0.18242.41550.00190.0755-0.118-0.0490.09730.173-0.1927-0.0975-0.05260.23030.0190.03140.3382-0.0880.29618.33376.3951-23.0083
220.33860.329-0.812.38740.56342.8238-0.33490.0569-0.2269-0.11090.04460.57990.1986-0.80130.26160.4193-0.12280.02580.5733-0.14060.43391.3018-5.9147-25.8615
234.4844-1.3582-0.97283.8203-0.26483.2691-0.14050.12370.13630.33880.17160.5935-0.2069-0.7680.00350.3-0.0211-0.00570.3061-0.0590.24921.84335.3379-18.4939
241.3485-0.1348-0.24680.90260.3892.1008-0.12160.2152-0.34070.04220.1066-0.10830.39250.01980.04850.3704-0.06620.04970.3083-0.14470.354917.9425-9.5966-25.463
255.949-1.2495-4.95452.57191.2027.1161-0.5217-0.4863-0.11750.53510.45490.09610.82930.6536-0.08440.4520.0432-0.02320.4235-0.12030.409426.8692-13.4649-16.9105
261.9995-0.98490.82161.4477-0.21230.3966-0.13050.00350.31950.79120.0621-0.706-0.07560.04110.03090.7567-0.0884-0.0330.4595-0.14910.461327.509693.759481.3203
270.1236-0.2677-0.40831.66421.48531.619-0.0460.051-0.0850.23240.5292-0.48860.33840.6867-0.58440.35060.03930.00430.5846-0.21280.513243.198527.87793.9649
281.59190.3569-1.47791.3624-0.69392.8385-0.2322-0.3416-0.44510.0898-0.1095-0.28820.54740.5740.19840.51990.08330.04580.45960.07650.536611.278156.62591.6656
290.45670.345-0.67671.3197-0.35621.0073-0.4051-0.0372-0.63330.19360.0294-0.37010.89580.22030.30031.07550.08990.26750.47350.12850.8578-1.328245.8782100.1281
302.04840.1676-2.01091.1656-0.12893.1358-0.21130.1489-0.34870.15640.12660.03250.4389-0.16170.07670.54420.00320.08470.3325-0.01560.4222-2.269959.673688.5238
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 160 )
3X-RAY DIFFRACTION3chain 'A' and (resid 161 through 273 )
4X-RAY DIFFRACTION4chain 'A' and (resid 274 through 311 )
5X-RAY DIFFRACTION5chain 'A' and (resid 312 through 338 )
6X-RAY DIFFRACTION6chain 'A' and (resid 339 through 372 )
7X-RAY DIFFRACTION7chain 'A' and (resid 373 through 401 )
8X-RAY DIFFRACTION8chain 'A' and (resid 402 through 437 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 311 )
10X-RAY DIFFRACTION10chain 'B' and (resid 312 through 438 )
11X-RAY DIFFRACTION11chain 'C' and (resid 1 through 72 )
12X-RAY DIFFRACTION12chain 'C' and (resid 73 through 161 )
13X-RAY DIFFRACTION13chain 'C' and (resid 162 through 199 )
14X-RAY DIFFRACTION14chain 'C' and (resid 200 through 311 )
15X-RAY DIFFRACTION15chain 'C' and (resid 312 through 372 )
16X-RAY DIFFRACTION16chain 'C' and (resid 373 through 440 )
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 56 )
18X-RAY DIFFRACTION18chain 'D' and (resid 57 through 160 )
19X-RAY DIFFRACTION19chain 'D' and (resid 161 through 214 )
20X-RAY DIFFRACTION20chain 'D' and (resid 215 through 238 )
21X-RAY DIFFRACTION21chain 'D' and (resid 239 through 268 )
22X-RAY DIFFRACTION22chain 'D' and (resid 269 through 311 )
23X-RAY DIFFRACTION23chain 'D' and (resid 312 through 337 )
24X-RAY DIFFRACTION24chain 'D' and (resid 338 through 415 )
25X-RAY DIFFRACTION25chain 'D' and (resid 416 through 441 )
26X-RAY DIFFRACTION26chain 'E' and (resid 6 through 46 )
27X-RAY DIFFRACTION27chain 'E' and (resid 47 through 143 )
28X-RAY DIFFRACTION28chain 'F' and (resid 1 through 207 )
29X-RAY DIFFRACTION29chain 'F' and (resid 208 through 275 )
30X-RAY DIFFRACTION30chain 'F' and (resid 276 through 378 )

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