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- PDB-4qd2: Molecular basis for disruption of E-cadherin adhesion by botulinu... -

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Basic information

Entry
Database: PDB / ID: 4qd2
TitleMolecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
Components
  • (Hemagglutinin component ...) x 3
  • Cadherin-1
KeywordsCELL ADHESION / Oral Toxicity / Botulinum Neurotoxin / E-Cadherin / HA70 / HA17 / HA33
Function / homology
Function and homology information


uterine epithelium development / Apoptotic cleavage of cell adhesion proteins / regulation of branching involved in salivary gland morphogenesis / salivary gland cavitation / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / RHO GTPases activate IQGAPs / Adherens junctions interactions / Degradation of the extracellular matrix / regulation of neuron migration / Integrin cell surface interactions ...uterine epithelium development / Apoptotic cleavage of cell adhesion proteins / regulation of branching involved in salivary gland morphogenesis / salivary gland cavitation / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / RHO GTPases activate IQGAPs / Adherens junctions interactions / Degradation of the extracellular matrix / regulation of neuron migration / Integrin cell surface interactions / positive regulation of cell-cell adhesion / lateral loop / gamma-catenin binding / cell-cell adhesion mediated by cadherin / negative regulation of axon extension / regulation of protein localization to cell surface / trophectodermal cell differentiation / alpha-catenin binding / Schmidt-Lanterman incisure / cellular response to indole-3-methanol / flotillin complex / epithelial cell morphogenesis / bicellular tight junction assembly / intestinal epithelial cell development / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / node of Ranvier / protein metabolic process / catenin complex / cell-cell junction assembly / negative regulation of protein localization to plasma membrane / negative regulation of protein processing / GTPase activating protein binding / adherens junction organization / apical junction complex / ankyrin binding / cochlea development / negative regulation of cell-cell adhesion / cellular response to lithium ion / homophilic cell adhesion via plasma membrane adhesion molecules / microvillus / decidualization / : / canonical Wnt signaling pathway / lateral plasma membrane / establishment of skin barrier / axon terminus / embryo implantation / synapse assembly / protein tyrosine kinase binding / cytoskeletal protein binding / cell adhesion molecule binding / negative regulation of cell migration / cell periphery / protein localization to plasma membrane / sensory perception of sound / cellular response to amino acid stimulus / adherens junction / negative regulation of canonical Wnt signaling pathway / trans-Golgi network / cell morphogenesis / cytoplasmic side of plasma membrane / cell-cell adhesion / beta-catenin binding / positive regulation of protein import into nucleus / regulation of protein localization / negative regulation of epithelial cell proliferation / cell-cell junction / actin cytoskeleton / apical part of cell / lamellipodium / cell junction / actin cytoskeleton organization / postsynapse / regulation of gene expression / basolateral plasma membrane / protein phosphatase binding / in utero embryonic development / molecular adaptor activity / endosome / cadherin binding / axon / protein domain specific binding / glutamatergic synapse / calcium ion binding / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / cell surface / extracellular region / membrane / identical protein binding / plasma membrane / cytoplasm
Similarity search - Function
: / Hemagglutinin component HA-17 / Jelly Rolls - #1090 / Hemagglutinin component HA-70, C-terminal / Haemagglutinin 70 C-terminal domain / Clostridium enterotoxin / Clostridium enterotoxin / Cadherin prodomain like / Ricin-type beta-trefoil lectin domain-like / Cadherin prodomain ...: / Hemagglutinin component HA-17 / Jelly Rolls - #1090 / Hemagglutinin component HA-70, C-terminal / Haemagglutinin 70 C-terminal domain / Clostridium enterotoxin / Clostridium enterotoxin / Cadherin prodomain like / Ricin-type beta-trefoil lectin domain-like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Cadherin / Catenin binding domain superfamily / Cadherins / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherins domain profile. / Cadherin-like / Cadherin-like superfamily / Ricin-type beta-trefoil / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Jelly Rolls / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Hemagglutinin component of the neurotoxin complex / Hemagglutinin component of the neurotoxin complex / Hemagglutinin component of the neurotoxin complex / Cadherin-1
Similarity search - Component
Biological speciesClostridium botulinum (bacteria)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsLee, K. / Zhong, X. / Gu, S. / Kruel, A. / Dorner, M.B. / Perry, K. / Rummel, A. / Dong, M. / Jin, R.
CitationJournal: Science / Year: 2014
Title: Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex.
Authors: Lee, K. / Zhong, X. / Gu, S. / Kruel, A.M. / Dorner, M.B. / Perry, K. / Rummel, A. / Dong, M. / Jin, R.
History
DepositionMay 13, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 25, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 2, 2014Group: Database references
Revision 1.2Sep 20, 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_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_auth_seq_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.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
D: Hemagglutinin component HA33
B: Hemagglutinin component HA17
C: Hemagglutinin component HA33
A: Hemagglutinin component HA70
E: Cadherin-1
I: Hemagglutinin component HA33
G: Hemagglutinin component HA17
H: Hemagglutinin component HA33
F: Hemagglutinin component HA70
J: Cadherin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)274,92116
Polymers274,68110
Non-polymers2406
Water7,242402
1
D: Hemagglutinin component HA33
B: Hemagglutinin component HA17
C: Hemagglutinin component HA33
A: Hemagglutinin component HA70
E: Cadherin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,4618
Polymers137,3405
Non-polymers1203
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
I: Hemagglutinin component HA33
G: Hemagglutinin component HA17
H: Hemagglutinin component HA33
F: Hemagglutinin component HA70
J: Cadherin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,4618
Polymers137,3405
Non-polymers1203
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)86.990, 95.730, 96.140
Angle α, β, γ (deg.)116.89, 96.34, 93.70
Int Tables number1
Space group name H-MP1

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Components

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Hemagglutinin component ... , 3 types, 8 molecules DCIHBGAF

#1: Protein
Hemagglutinin component HA33 / / Hemagglutinin component of the neurotoxin complex


Mass: 34081.656 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Strain: Hall / ATCC 3502 / NCTC 13319 / Type A / Gene: ha70, CBO0801, CLC_0857 / Production host: Escherichia coli (E. coli) / References: UniProt: A5HZZ6
#2: Protein Hemagglutinin component HA17 / / Hemagglutinin component of the neurotoxin complex


Mass: 17069.195 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Strain: Hall / ATCC 3502 / NCTC 13319 / Type A / Gene: ha17, CBO0802, CLC_0858 / Production host: Escherichia coli (E. coli) / References: UniProt: A5HZZ5
#3: Protein Hemagglutinin component HA70 / / Hemagglutinin component of the neurotoxin complex


Mass: 28846.920 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Strain: Hall / ATCC 3502 / NCTC 13319 / Type A / Gene: ha33, CBO0803, CLC_0859 / Production host: Escherichia coli (E. coli) / References: UniProt: A5HZZ4

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Protein , 1 types, 2 molecules EJ

#4: Protein Cadherin-1 / / ARC-1 / Epithelial cadherin / E-cadherin / Uvomorulin / E-Cad/CTF1 / E-Cad/CTF2 / E-Cad/CTF3


Mass: 23260.865 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cdh1 / Production host: Escherichia coli (E. coli) / References: UniProt: P09803

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Non-polymers , 2 types, 408 molecules

#5: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 402 / 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: 2.56 Å3/Da / Density % sol: 51.99 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 100mM Tris (pH8.0), 6% PEG8000, 200mM potassium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97919 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 2, 2012
RadiationMonochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97919 Å / Relative weight: 1
ReflectionResolution: 2.4→49.5 Å / % possible obs: 98 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1
Reflection shellResolution: 2.4→2.53 Å / % possible all: 97.5

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 4LO7 AND 3LNG

4lo7

3lng


Resolution: 2.4→47.73 Å / SU ML: 0.84 / σ(F): 1.04 / Phase error: 27.97 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.247 9313 4.98 %
Rwork0.208 --
obs0.21 186891 87.7 %
all-201058 -
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 35.42 Å2 / ksol: 0.34 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-6.7608 Å2-3.5246 Å2-2.8339 Å2
2---3.7727 Å21.247 Å2
3----2.9882 Å2
Refinement stepCycle: LAST / Resolution: 2.4→47.73 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18604 0 6 402 19012
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00419017
X-RAY DIFFRACTIONf_angle_d0.71425971
X-RAY DIFFRACTIONf_dihedral_angle_d13.7056853
X-RAY DIFFRACTIONf_chiral_restr0.0512927
X-RAY DIFFRACTIONf_plane_restr0.0023360
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.42730.37142850.34975720X-RAY DIFFRACTION85
2.4273-2.45580.38393100.32495763X-RAY DIFFRACTION86
2.4558-2.48580.34032960.3185836X-RAY DIFFRACTION86
2.4858-2.51720.33333040.31225870X-RAY DIFFRACTION86
2.5172-2.55040.34512990.31895788X-RAY DIFFRACTION86
2.5504-2.58530.36372870.3155951X-RAY DIFFRACTION87
2.5853-2.62220.36923050.35876X-RAY DIFFRACTION87
2.6222-2.66140.32523100.28685917X-RAY DIFFRACTION87
2.6614-2.7030.34673220.27515851X-RAY DIFFRACTION88
2.703-2.74730.28893180.27085884X-RAY DIFFRACTION88
2.7473-2.79460.33192900.2715966X-RAY DIFFRACTION88
2.7946-2.84540.29712570.26646059X-RAY DIFFRACTION88
2.8454-2.90020.34622760.24946037X-RAY DIFFRACTION88
2.9002-2.95940.31543330.25055832X-RAY DIFFRACTION88
2.9594-3.02370.29533350.24675950X-RAY DIFFRACTION88
3.0237-3.0940.30093070.23176006X-RAY DIFFRACTION89
3.094-3.17140.29273060.23155912X-RAY DIFFRACTION88
3.1714-3.25710.26423060.22816012X-RAY DIFFRACTION89
3.2571-3.35290.29083160.22716007X-RAY DIFFRACTION89
3.3529-3.46110.28023100.21675975X-RAY DIFFRACTION89
3.4611-3.58480.24533350.19815997X-RAY DIFFRACTION89
3.5848-3.72830.23123130.19615978X-RAY DIFFRACTION89
3.7283-3.89790.2243040.19435999X-RAY DIFFRACTION89
3.8979-4.10330.21993640.18055892X-RAY DIFFRACTION89
4.1033-4.36020.21013310.15646058X-RAY DIFFRACTION89
4.3602-4.69660.1813220.14055924X-RAY DIFFRACTION89
4.6966-5.16870.16023290.13975959X-RAY DIFFRACTION88
5.1687-5.91540.21152910.17845821X-RAY DIFFRACTION86
5.9154-7.44830.2743190.22435695X-RAY DIFFRACTION85
7.4483-47.74410.18413330.1756043X-RAY DIFFRACTION90
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)
15.7122-2.486-2.52383.26222.76727.7313-0.29990.43340.5589-0.7088-0.07630.2388-0.511-0.37230.38710.5558-0.1254-0.20130.41140.01230.4671-45.528312.124730.2393
23.26360.07370.39281.285-0.08052.6956-0.19270.08870.1784-0.21560.10660.1713-0.0247-0.21970.08560.4686-0.1404-0.08780.2845-0.04840.3631-42.299211.848538.0903
30.8844-1.1310.13442.95681.70418.3202-0.05230.2340.0949-0.4643-0.85020.8663-0.8935-2.02830.92020.8059-0.0078-0.13910.9456-0.22740.6408-58.159711.632812.3901
45.4556-0.86010.4525.1348-1.92668.9309-0.50970.48280.3204-1.9515-0.34360.572-1.0317-0.81330.82691.23640.0686-0.27750.6406-0.12610.568-55.746713.29434.2839
56.76890.5385-0.2962.0295-0.24489.5064-0.35540.12920.778-0.5925-0.1811-0.0731-1.7681-0.38930.53341.41780.0667-0.16790.6965-0.02260.9408-53.277419.815911.0409
62.0917-0.3870.47824.5149-0.85094.9721-0.23930.01680.6414-0.5037-0.41231.3814-1.8553-1.87790.63921.85170.6417-0.50491.363-0.42921.2498-64.264621.538.9855
75.0776-0.61741.24192.06632.64594.2309-0.7465-0.4088-0.55440.5664-0.0044-0.30020.96530.03450.73870.75460.0037-0.00850.24610.05530.6091-12.375-8.220958.4634
88.47111.52031.60823.45231.64234.0260.05770.2471-0.95220.0373-0.144-0.14720.05770.28910.09220.34010.0115-0.02150.2578-0.01560.3346-9.886-3.392342.7593
95.28141.8685-2.28180.9672-2.40298.98670.09610.1266-0.19940.328-0.1561-0.4198-0.32220.850.0580.371-0.0151-0.03770.2383-0.01620.4488-6.1471-0.14650.5978
107.62781.1114-7.57064.374-1.25267.50590.5641-0.5120.24470.4568-0.15770.1861-0.73960.4873-0.42630.5382-0.0545-0.10030.34330.00040.325-14.41731.378863.498
112.9416-0.63842.39990.34280.10983.9972-0.18030.0480.26840.4363-0.1701-0.0728-0.08730.07370.34930.5069-0.08040.01130.2439-0.01550.3005-13.65836.635755.2634
126.1347-0.9070.06690.83310.55937.2960.13660.2267-0.5287-0.202-0.3323-0.18750.49180.06140.18930.4682-0.11090.03990.3025-0.06820.5011-19.9634-5.331453.3578
132.53740.3235-0.29340.0814-0.28243.5243-0.08740.2534-0.358-0.2553-0.0535-0.0240.2739-0.17240.12910.5214-0.1252-0.0040.2575-0.05480.3388-21.40811.023346.3227
141.5352-0.7295-1.35955.51011.69934.3967-0.3590.48460.2844-0.61090.19010.51760.1017-0.14750.19560.521-0.1836-0.15430.4210.05990.3309-15.623727.955726.1969
151.3159-0.35050.1922.8978-1.52822.0802-0.1850.26120.2937-0.39330.03760.0021-0.09990.0030.1440.5044-0.1766-0.1160.38730.00180.3682-17.409128.488426.872
166.74910.57780.63698.538-0.4949.1125-0.0241-0.2460.40070.0386-0.0757-0.0295-0.7633-0.59660.11230.61950.0179-0.12850.46480.0780.5603-26.114352.00517.8513
172.5228-2.6271-0.32447.08560.83888.0575-0.22730.3170.2574-0.1894-0.1998-0.0254-0.23250.06440.43070.6854-0.1932-0.28620.5060.11430.636-22.253348.66959.2782
185.4436-4.52822.36975.07510.80896.939-0.7426-0.00790.22381.3250.2356-0.7714-0.23660.45170.50010.9892-0.3299-0.14511.0693-0.06690.7132-27.0672-21.865686.0621
195.1048-2.14920.71094.0112-1.50034.6876-0.2159-0.5281-0.03841.2560.0923-0.71440.07990.47440.12690.9189-0.2361-0.20110.6910.10570.5041-27.4908-21.864379.5369
204.8865-1.3141-0.8986.849-0.41796.0255-0.0073-0.6698-0.7690.5805-0.18630.09671.02060.03670.16840.8583-0.2382-0.16360.49790.1240.4403-31.7059-27.427272.5725
213.23051.9894-0.14295.6845-0.45486.03620.2386-1.1996-0.77211.2711-0.0636-0.60240.8310.441-0.17921.1969-0.1582-0.21280.69970.21440.5269-27.6674-27.177479.1431
223.7969-0.9057-0.53155.57370.07184.54180.4377-0.3304-0.20630.37-0.2191-0.54490.15770.1528-0.22250.5558-0.1574-0.10170.31770.0470.4388-29.7424-21.079863.2335
233.69441.7039-2.13164.8227-0.9792.8092-0.04230.1672-0.4552-0.29130.0091-0.08290.4855-0.2370.02840.5701-0.0932-0.13970.2999-0.03790.348-35.6098-24.626653.6865
242.71551.07060.23594.45490.20341.22170.0868-0.3092-0.14310.339-0.15840.50750.2755-0.37950.06720.5567-0.21340.03080.4842-0.04620.3388-49.7496-8.707665.2025
255.07622.84952.13837.9663.08575.20070.2048-0.47630.69280.3785-0.0275-0.3143-0.08660.1462-0.16630.2817-0.06280.04220.4215-0.1170.3917-27.709223.127572.1822
262.24652.41860.75714.3620.67312.3776-0.0553-0.12350.7259-0.22870.2731-1.1032-0.78180.9603-0.1790.5372-0.22720.04980.6552-0.19520.9206-17.405531.565971.5403
274.4641.11180.7092.5695-0.59964.7995-0.0629-0.35060.31070.3511-0.1795-0.0492-0.6797-0.21930.23960.38220.0238-0.06720.2672-0.05070.3856-65.447450.297368.5933
284.04051.66461.62911.86330.18095.3682-0.01270.1283-0.210.114-0.0995-0.27020.23690.20660.12560.21340.0335-0.02640.1657-0.01740.3344-64.040141.876461.2191
298.3868-2.48841.08523.3352-0.04546.648-0.1606-0.75050.25130.46880.3446-0.22910.01280.4728-0.19410.52430.0144-0.13290.3437-0.0410.3804-39.12937.187685.1416
302.0152-2.27031.97167.7995-2.4539.33480.2580.4488-1.4263-0.18360.1850.18031.1475-0.497-0.45360.7342-0.0641-0.06940.43910.12640.7837-45.32828.391985.9575
316.22690.0350.69827.6603-0.96798.0335-0.3444-1.01950.73230.89840.17770.1084-0.7933-0.08720.13170.65610.0915-0.09230.4662-0.1190.4649-46.430441.871393.3434
325.422-1.47680.39265.40861.21893.7830.00370.25660.2973-1.69750.1832-0.1106-0.2523-0.1491-0.1780.6503-0.3172-0.08620.64620.13750.3424-78.17849.929824.658
333.5327-0.741.19914.4098-0.66693.7512-0.07170.7099-0.5015-0.79520.21490.30030.943-0.0712-0.14360.5676-0.22420.03090.4641-0.03160.2777-77.146937.140528.7822
345.9011.60630.96626.76183.67897.6038-0.51150.16060.7894-0.37370.41471.0903-0.0455-0.66690.0830.3651-0.0683-0.09840.51590.15280.4301-87.192350.824631.0043
351.8573-0.54160.12410.782-1.22764.2425-0.12290.1869-0.0298-0.45250.27520.27430.6614-0.7272-0.14830.4176-0.1766-0.04790.41980.06150.4077-86.596838.227636.3524
364.97180.32852.48190.9422-1.95986.1356-0.17170.33190.0212-0.34590.35050.39420.5382-1.0789-0.17430.3308-0.1319-0.06440.46090.0770.315-88.954242.771237.655
374.0644-0.5172-1.0110.17120.6613.00670.10790.1038-0.0699-0.27980.1195-0.0227-0.2355-0.0535-0.24230.4329-0.1362-0.01040.32520.06330.4299-74.879851.51933.8244
385.4423-0.30541.25923.88511.38725.7192-0.2667-0.5281-0.2858-0.16110.029-0.0387-0.1474-0.19480.24950.237-0.0649-0.03170.27370.08310.4113-80.401949.150945.5121
399.5123-1.27712.86689.98811.08715.5310.17950.4115-0.2948-1.064-0.0261-0.92690.26170.6449-0.14740.4699-0.00470.14150.3482-0.0230.3498-67.352134.73239.6565
403.3043-1.4059-0.55294.3018-0.68624.8499-0.5110.25690.1534-0.01250.4645-0.7349-0.62180.4040.06220.2369-0.0718-0.06280.37980.01780.3347-71.311248.771544.2725
416.3367-1.00982.01253.6356-1.76454.655-0.08341.0190.0246-0.3553-0.0269-0.38950.19440.18130.11340.3703-0.11670.03440.42260.04020.3792-71.147545.362931.4567
424.6257-1.9513-2.0687.08540.93156.4668-0.1363-0.15970.04180.0694-0.1052-0.34010.20230.25920.23530.268-0.0366-0.05520.26880.09180.299-79.23318.652859.8845
431.96560.9518-0.44996.3099-2.81534.4850.055-0.1029-0.2463-0.01550.0844-0.0440.4369-0.0134-0.13430.2134-0.0129-0.05750.2424-0.03870.2864-76.982819.48558.9356
443.84591.0369-2.13083.5774-1.89666.60480.6598-1.0941-0.49932.0945-0.26860.88290.1194-0.8419-0.38911.1284-0.02620.17080.70320.25130.7915-91.88715.047884.3324
458.46480.0085-0.83693.4874-3.70458.55630.1692-1.86670.11831.7275-0.2532-0.0742-0.64820.00680.0761.5404-0.0436-0.09580.69710.07460.6546-82.244111.858488.3338
468.63542.71270.945.3293-4.12784.46910.5709-0.9972-0.32472.0721-0.24130.23370.02390.2353-0.32011.26330.0481-0.06730.49160.09580.6452-78.04297.826584.5209
473.50260.306-0.7973.6412-2.77775.54040.0293-0.6223-1.73210.924-0.1426-0.70640.97710.28160.111.33330.0799-0.16320.59810.21181.1898-78.8963-2.053483.7193
486.2182-3.6248-5.39635.6596-0.02617.51260.97591.1021-0.7088-0.3834-0.11460.3768-1.3531-1.7072-0.8581.0307-0.0705-0.40051.01410.21081.0319-85.095981.566516.5794
490.4821-0.4482.08415.8961.10622.0048-0.18620.61250.0223-1.2429-0.15160.3499-0.3747-1.36930.34720.8692-0.1343-0.26290.9960.18610.7094-80.750178.238315.9969
504.049-1.4345-2.53694.2241-0.15954.2384-0.1060.4137-0.2466-1.26240.13220.49490.352-0.627-0.02220.9093-0.3173-0.31710.6050.15880.5488-74.135171.410919.994
514.8333-0.5112-1.30482.896-0.31345.7244-0.11120.83820.3721-1.35110.25880.5084-0.1927-0.6807-0.13720.9092-0.2606-0.24120.57580.16440.563-73.871277.613120.9833
523.59370.5907-1.16572.7104-0.85783.7548-0.19310.52420.0966-1.28410.0815-0.1572-0.27920.32440.08940.6562-0.2974-0.01140.59740.08430.322-59.478170.653123.7905
531.85070.1989-0.54846.7338-1.07432.5904-0.1415-0.10110.0637-0.40.0413-0.635-0.23470.54540.11050.3418-0.15560.02830.46770.01430.3007-57.838864.801832.4827
543.315-0.2511-0.48162.0024-1.96134.4008-0.5510.3050.0461-1.22060.3399-1.4022-0.21410.38590.16340.6141-0.30880.09690.6362-0.12960.527-51.371471.960623.132
554.24763.1222-1.00373.6193-1.68171.44920.1624-0.36460.340.2022-0.09950.1794-0.35520.1796-0.05880.404-0.0987-0.00720.4069-0.04210.3736-70.571179.415646.4479
567.72872.2041-1.51411.4887-0.23162.9237-0.2316-0.3655-0.1230.0642-0.42221.0870.1513-0.79020.61190.3605-0.08150.07610.6886-0.13461.0176-102.412457.284451.5512
573.49481.5225-2.11213.5703-3.81524.3403-0.26960.5149-0.6374-0.66780.21141.1141.2554-1.48970.07390.5894-0.29270.04181.1583-0.221.2494-110.61642.273448.0686
583.37191.9294-0.83262.0704-0.96151.0665-0.39330.4289-0.6176-0.0792-0.18261.00870.7804-1.55650.52330.5521-0.30210.17371.1611-0.30481.2257-110.690248.288550.9451
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'D' and (resseq 9:31)
2X-RAY DIFFRACTION2chain 'D' and (resseq 32:139)
3X-RAY DIFFRACTION3chain 'D' and (resseq 140:176)
4X-RAY DIFFRACTION4chain 'D' and (resseq 177:227)
5X-RAY DIFFRACTION5chain 'D' and (resseq 228:249)
6X-RAY DIFFRACTION6chain 'D' and (resseq 250:294)
7X-RAY DIFFRACTION7chain 'B' and (resseq 4:17)
8X-RAY DIFFRACTION8chain 'B' and (resseq 18:28)
9X-RAY DIFFRACTION9chain 'B' and (resseq 29:50)
10X-RAY DIFFRACTION10chain 'B' and (resseq 51:60)
11X-RAY DIFFRACTION11chain 'B' and (resseq 61:93)
12X-RAY DIFFRACTION12chain 'B' and (resseq 94:101)
13X-RAY DIFFRACTION13chain 'B' and (resseq 102:146)
14X-RAY DIFFRACTION14chain 'C' and (resseq 9:53)
15X-RAY DIFFRACTION15chain 'C' and (resseq 54:181)
16X-RAY DIFFRACTION16chain 'C' and (resseq 182:222)
17X-RAY DIFFRACTION17chain 'C' and (resseq 223:294)
18X-RAY DIFFRACTION18chain 'A' and (resseq 380:391)
19X-RAY DIFFRACTION19chain 'A' and (resseq 392:421)
20X-RAY DIFFRACTION20chain 'A' and (resseq 422:474)
21X-RAY DIFFRACTION21chain 'A' and (resseq 475:493)
22X-RAY DIFFRACTION22chain 'A' and (resseq 494:524)
23X-RAY DIFFRACTION23chain 'A' and (resseq 525:626)
24X-RAY DIFFRACTION24chain 'E' and (resseq 2:99)
25X-RAY DIFFRACTION25chain 'E' and (resseq 100:146)
26X-RAY DIFFRACTION26chain 'E' and (resseq 147:213)
27X-RAY DIFFRACTION27chain 'I' and (resseq 9:94)
28X-RAY DIFFRACTION28chain 'I' and (resseq 95:150)
29X-RAY DIFFRACTION29chain 'I' and (resseq 151:222)
30X-RAY DIFFRACTION30chain 'I' and (resseq 223:242)
31X-RAY DIFFRACTION31chain 'I' and (resseq 243:294)
32X-RAY DIFFRACTION32chain 'G' and (resseq 4:17)
33X-RAY DIFFRACTION33chain 'G' and (resseq 18:50)
34X-RAY DIFFRACTION34chain 'G' and (resseq 51:60)
35X-RAY DIFFRACTION35chain 'G' and (resseq 61:75)
36X-RAY DIFFRACTION36chain 'G' and (resseq 76:86)
37X-RAY DIFFRACTION37chain 'G' and (resseq 87:101)
38X-RAY DIFFRACTION38chain 'G' and (resseq 102:113)
39X-RAY DIFFRACTION39chain 'G' and (resseq 114:126)
40X-RAY DIFFRACTION40chain 'G' and (resseq 127:136)
41X-RAY DIFFRACTION41chain 'G' and (resseq 137:146)
42X-RAY DIFFRACTION42chain 'H' and (resseq 9:38)
43X-RAY DIFFRACTION43chain 'H' and (resseq 39:169)
44X-RAY DIFFRACTION44chain 'H' and (resseq 170:195)
45X-RAY DIFFRACTION45chain 'H' and (resseq 196:219)
46X-RAY DIFFRACTION46chain 'H' and (resseq 220:254)
47X-RAY DIFFRACTION47chain 'H' and (resseq 255:294)
48X-RAY DIFFRACTION48chain 'F' and (resseq 380:391)
49X-RAY DIFFRACTION49chain 'F' and (resseq 392:415)
50X-RAY DIFFRACTION50chain 'F' and (resseq 416:429)
51X-RAY DIFFRACTION51chain 'F' and (resseq 430:507)
52X-RAY DIFFRACTION52chain 'F' and (resseq 508:542)
53X-RAY DIFFRACTION53chain 'F' and (resseq 543:612)
54X-RAY DIFFRACTION54chain 'F' and (resseq 613:626)
55X-RAY DIFFRACTION55chain 'J' and (resseq 2:99)
56X-RAY DIFFRACTION56chain 'J' and (resseq 100:146)
57X-RAY DIFFRACTION57chain 'J' and (resseq 147:162)
58X-RAY DIFFRACTION58chain 'J' and (resseq 163:213)

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