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- PDB-6s9e: Tubulin-GDP.AlF complex -

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Basic information

Entry
Database: PDB / ID: 6s9e
TitleTubulin-GDP.AlF complex
Components
  • Stathmin-4
  • Tubulin Tyrosine ligase
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / tubulin / cytoskeleton / GTPase / transitional state
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / double-stranded RNA binding / mitotic cell cycle / nervous system development / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / Stathmin family / Stathmin, conserved site ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / 60s Ribosomal Protein L30; Chain: A; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / 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. / 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 / ALUMINUM FLUORIDE / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsOliva, M.A. / Estevez-Gallego, J. / Diaz, J.F. / Prota, A.E. / Steinmetz, M.O. / Balaguer, F.A. / Lucena-Agell, D.
Funding support Spain, 2items
OrganizationGrant numberCountry
Spanish Ministry of Science, Innovation, and UniversitiesRYC-2011-07900 Spain
Spanish Ministry of Economy and CompetitivenessBFU2016-75319-R Spain
CitationJournal: Elife / Year: 2020
Title: Structural model for differential cap maturation at growing microtubule ends.
Authors: Estevez-Gallego, J. / Josa-Prado, F. / Ku, S. / Buey, R.M. / Balaguer, F.A. / Prota, A.E. / Lucena-Agell, D. / Kamma-Lorger, C. / Yagi, T. / Iwamoto, H. / Duchesne, L. / Barasoain, I. / ...Authors: Estevez-Gallego, J. / Josa-Prado, F. / Ku, S. / Buey, R.M. / Balaguer, F.A. / Prota, A.E. / Lucena-Agell, D. / Kamma-Lorger, C. / Yagi, T. / Iwamoto, H. / Duchesne, L. / Barasoain, I. / Steinmetz, M.O. / Chretien, D. / Kamimura, S. / Diaz, J.F. / Oliva, M.A.
History
DepositionJul 12, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 19, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 18, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 24, 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
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_alt_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.ptnr1_symmetry / _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_alt_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.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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

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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)267,32729
Polymers263,6076
Non-polymers3,71923
Water3,585199
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24430 Å2
ΔGint-145 kcal/mol
Surface area78610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.999, 157.357, 180.261
Angle α, β, γ (deg.)90.000, 90.000, 90.000
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: 48966.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (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 / Source: (natural) Bos taurus (cattle) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / / Stathmin-like protein B3 / RB3


Mass: 22125.301 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: 43549.625 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 , 11 types, 222 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine 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.: 5 / 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-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#10: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#11: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: Chemical ChemComp-AF3 / ALUMINUM FLUORIDE / Aluminium fluoride


Mass: 83.977 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: AlF3 / Feature type: SUBJECT OF INVESTIGATION
#13: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#14: 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
#15: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 199 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.73 Å3/Da / Density % sol: 54.93 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop
Details: 0.1M MES, 0.1M IMIDAZOLE, pH6.5, 0.03M CaCl2, 0.03M MgCl2, 5mM L-Tyrosine, 5% Glycerol, 5.5% PEG4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.979 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 5, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.25→48.003 Å / Num. obs: 140201 / % possible obs: 99 % / Redundancy: 9.6 % / Biso Wilson estimate: 48.9 Å2 / CC1/2: 0.979 / Rmerge(I) obs: 0.075 / Rpim(I) all: 0.025 / Rrim(I) all: 0.08 / Net I/σ(I): 16.5
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.25-2.299.21.2226240967860.6350.4171.2951.897.8
12.32-4890.03388849820.9990.0120.03554.598.5

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Processing

Software
NameVersionClassification
PHENIX1.12_2829refinement
Aimless0.7.4data scaling
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4O2B

4o2b


Resolution: 2.25→48.003 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.07
RfactorNum. reflection% reflection
Rfree0.2278 6923 4.94 %
Rwork0.2029 --
obs0.2041 140102 98.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 221.6 Å2 / Biso mean: 67.6044 Å2 / Biso min: 27.01 Å2
Refinement stepCycle: final / Resolution: 2.25→48.003 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17091 0 341 199 17631
Biso mean--66.07 45.72 -
Num. residues----2160
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00217899
X-RAY DIFFRACTIONf_angle_d0.52624306
X-RAY DIFFRACTIONf_chiral_restr0.0412656
X-RAY DIFFRACTIONf_plane_restr0.0033148
X-RAY DIFFRACTIONf_dihedral_angle_d16.16510783
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.25-2.27560.33182260.304430897
2.2756-2.30230.32472200.294440799
2.3023-2.33040.27912100.2779435098
2.3304-2.35990.30842220.2743442999
2.3599-2.3910.26912480.269434698
2.391-2.42370.32361980.2669443999
2.4237-2.45830.25322180.2542437799
2.4583-2.4950.27142160.2529441098
2.495-2.5340.28392150.25754444100
2.534-2.57560.26042470.247436998
2.5756-2.620.27332200.244440299
2.62-2.66760.28442350.24924438100
2.6676-2.71890.26552240.2443440799
2.7189-2.77440.25952230.2409432897
2.7744-2.83470.28092290.242443599
2.8347-2.90070.26882480.2454420100
2.9007-2.97320.26521940.2488448999
2.9732-3.05360.27572270.2391442899
3.0536-3.14340.26922130.2356446599
3.1434-3.24480.26642280.2316444999
3.2448-3.36080.26982260.2305448499
3.3608-3.49530.23232510.214445399
3.4953-3.65430.23642570.2041433497
3.6543-3.84690.22632390.18694505100
3.8469-4.08780.20292540.1676444899
4.0878-4.40330.20552550.164510100
4.4033-4.8460.16622500.14524528100
4.846-5.54630.18812550.1664444598
5.5463-6.98430.21352320.19324619100
6.9843-48.0030.18442430.179471398
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)
13.6294-0.1511-0.38094.5755-0.58872.2428-0.00720.06730.4554-0.41170.2338-0.3074-0.96050.2655-0.22860.7381-0.12790.14030.4631-0.11170.377828.884497.031453.6487
21.4084-0.65250.81379.6294-0.99683.7541-0.29830.24260.1419-1.19130.4015-0.3586-0.91640.0876-0.12080.8067-0.11060.09330.5549-0.11520.455928.178686.999942.4721
32.0236-0.0517-0.02213.29981.4712.87520.00610.11920.0348-0.01250.2228-0.2934-0.29130.3979-0.22520.402-0.04320.03170.432-0.09480.370929.036480.915458.0693
41.49450.4441-0.7923.83650.8394.61010.093-0.1334-0.07220.5404-0.10130.57290.0008-0.36660.00730.5449-0.02790.10370.4288-0.12860.47514.773283.332970.9443
51.0113-0.03850.85282.12150.99021.0228-0.0603-0.39630.3170.72370.09120.4387-0.254-0.0799-0.05580.6970.02190.14420.5165-0.11140.469517.323487.503479.967
62.9424-0.57311.94415.2165-0.76763.70080.0409-0.04950.06470.6783-0.0220.3468-0.21220.0944-0.0640.5936-0.04670.15410.4495-0.13120.455517.734488.543974.1598
71.83960.4754-0.85585.06123.59876.8768-0.024-0.1504-0.1910.93230.225-0.17110.83060.6169-0.19740.48650.1163-0.06910.3916-0.08680.446329.422761.953362.1011
86.7255-1.8364-0.28118.72912.27535.6546-0.13560.20230.9185-0.48980.07580.1852-0.985-0.18160.030.44520.04370.00010.34030.00330.429715.797972.256722.1763
92.1519-1.5716-0.8369.15890.52823.86840.20390.6116-0.0021-0.6313-0.14570.0249-0.52370.099-0.05670.34-0.0170.02220.5428-0.04380.327224.930758.763913.4418
101.6199-0.2017-0.47873.16851.42593.3959-0.0458-0.0018-0.04740.0015-0.10580.2075-0.0179-0.18250.11760.30070.00360.02170.4159-0.09820.376217.431752.881926.5581
116.4033-3.10245.57753.464-3.05266.7962-0.3042-0.27220.64310.3552-0.02030.049-0.7347-0.15650.27810.4077-0.01930.04590.4519-0.16220.543719.312768.111638.5019
123.1578-1.10631.57692.71030.16473.4418-0.1848-0.24910.0670.2859-0.10040.4354-0.0301-0.95410.26140.4034-0.0060.07770.62-0.18070.50066.351160.085942.7027
130.6511-1.579-1.09397.09455.21223.8915-0.178-0.241-0.04630.7555-0.08430.84020.498-0.12620.21450.4026-0.01140.08820.467-0.08010.421815.375641.934634.0886
141.1808-0.26240.37334.78334.37496.5602-0.1235-0.0549-0.16460.85370.0803-0.19780.96960.51730.01080.39640.0122-0.0740.36310.0020.396125.838837.987631.2369
151.4229-0.53180.30332.96970.04881.933-0.04820.17120.0769-0.21730.1004-0.0702-0.13460.1678-0.0450.2896-0.06170.04230.4128-0.03350.326820.401832.9725-11.9057
161.128-0.5028-0.08961.59881.03071.5470.0024-0.00950.09630.076-0.08260.11390.0431-0.19480.08050.2567-0.06520.0390.328-0.02330.32077.593126.01053.0144
176.059-3.93630.05718.0707-0.36061.50380.05970.7676-0.005-0.8567-0.08580.10610.048-0.14910.01570.6026-0.13720.03610.7733-0.05740.291117.36279.9017-44.0815
181.3303-0.0562-0.32411.43380.33572.1472-0.12080.3703-0.2615-0.24130.1164-0.07610.356-0.00450.01040.5254-0.05750.03790.532-0.16140.399616.8844-2.9184-29.7338
194.49510.4809-1.82582.6957-0.62923.794-0.22470.2829-0.84220.0477-0.0383-0.22290.78070.28380.10870.69710.07130.01530.5271-0.19510.685630.3076-16.3528-24.4579
202.3383-2.53330.76885.0252-0.09780.5092-0.1005-0.21440.13650.7660.4-0.4147-0.65820.4355-0.31160.8242-0.1424-0.01540.7449-0.23260.584127.464193.253181.5392
210.1245-0.3237-0.3952.83912.96653.4196-0.078-0.0283-0.02970.25950.5075-0.45840.37060.7502-0.54880.42930.03980.04030.7798-0.23180.64642.821228.69644.8983
223.33241.5804-1.29544.87850.41746.6264-0.28140.3725-0.747-0.1998-0.0407-0.19951.4689-0.37850.21160.802-0.06130.1250.4721-0.12430.58766.30854.484470.137
233.78540.5011-0.72884.1359-1.64555.3316-0.0695-0.57890.01760.4893-0.3802-1.0666-0.11241.08550.30690.72790.0108-0.08840.83970.08940.700714.372364.968498.8531
242.67170.1932-0.14452.7782-0.78533.4968-0.1947-0.8659-0.58640.7088-0.3843-0.81610.61611.47050.40980.9390.2476-0.05351.07570.35410.918111.578553.4315106.6993
252.15060.4755-0.92752.9881-1.26773.5413-0.3472-0.1605-0.99420.3568-0.0044-0.26561.05020.14480.26591.06120.06920.18160.50510.10290.8668-2.999247.5471100.1267
262.10930.1802-2.31161.2858-0.84637.0036-0.1860.0911-0.45660.18430.19590.05270.6087-0.3489-0.02310.6844-0.01460.0740.43450.01990.5859-0.76159.710687.5714
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 72 )A1 - 72
2X-RAY DIFFRACTION2chain 'A' and (resid 73 through 102 )A73 - 102
3X-RAY DIFFRACTION3chain 'A' and (resid 103 through 259 )A103 - 259
4X-RAY DIFFRACTION4chain 'A' and (resid 260 through 306 )A260 - 306
5X-RAY DIFFRACTION5chain 'A' and (resid 307 through 336 )A307 - 336
6X-RAY DIFFRACTION6chain 'A' and (resid 337 through 381 )A337 - 381
7X-RAY DIFFRACTION7chain 'A' and (resid 382 through 437 )A382 - 437
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 64 )B2 - 64
9X-RAY DIFFRACTION9chain 'B' and (resid 65 through 128 )B65 - 128
10X-RAY DIFFRACTION10chain 'B' and (resid 129 through 238 )B129 - 238
11X-RAY DIFFRACTION11chain 'B' and (resid 239 through 259 )B239 - 259
12X-RAY DIFFRACTION12chain 'B' and (resid 260 through 373 )B260 - 373
13X-RAY DIFFRACTION13chain 'B' and (resid 374 through 401 )B374 - 401
14X-RAY DIFFRACTION14chain 'B' and (resid 402 through 438 )B402 - 438
15X-RAY DIFFRACTION15chain 'C' and (resid 1 through 199 )C1 - 199
16X-RAY DIFFRACTION16chain 'C' and (resid 200 through 440 )C200 - 440
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 88 )D1 - 88
18X-RAY DIFFRACTION18chain 'D' and (resid 89 through 401 )D89 - 401
19X-RAY DIFFRACTION19chain 'D' and (resid 402 through 441 )D402 - 441
20X-RAY DIFFRACTION20chain 'E' and (resid 6 through 46 )E6 - 46
21X-RAY DIFFRACTION21chain 'E' and (resid 47 through 141 )E47 - 141
22X-RAY DIFFRACTION22chain 'F' and (resid 1 through 66 )F1 - 66
23X-RAY DIFFRACTION23chain 'F' and (resid 67 through 128 )F67 - 128
24X-RAY DIFFRACTION24chain 'F' and (resid 129 through 207 )F129 - 207
25X-RAY DIFFRACTION25chain 'F' and (resid 208 through 283 )F208 - 283
26X-RAY DIFFRACTION26chain 'F' and (resid 284 through 378 )F284 - 378

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