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- PDB-4iij: Crystal structure of tubulin-stathmin-TTL-apo complex -

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Basic information

Entry
Database: PDB / ID: 4iij
TitleCrystal structure of tubulin-stathmin-TTL-apo complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin tyrosine ligase, TTL
KeywordsCELL CYCLE / alpha-tubulin / beta-tubulin / ligase / GTPase / microtubule / stathmin
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
Rossmann fold - #11480 / 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 ...Rossmann fold - #11480 / 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. / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 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
GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / 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 / Difference Fourier / Resolution: 2.6 Å
AuthorsProta, A.E. / Magiera, M.M. / Kuijpers, M. / Bargsten, K. / Frey, D. / Wieser, M. / Jaussi, R. / Hoogenraad, C.C. / Kammerer, R.A. / Janke, C. / Steinmetz, M.O.
CitationJournal: J.Cell Biol. / Year: 2013
Title: Structural basis of tubulin tyrosination by tubulin tyrosine ligase.
Authors: Prota, A.E. / Magiera, M.M. / Kuijpers, M. / Bargsten, K. / Frey, D. / Wieser, M. / Jaussi, R. / Hoogenraad, C.C. / Kammerer, R.A. / Janke, C. / Steinmetz, M.O.
History
DepositionDec 20, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 30, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 13, 2013Group: Database references
Revision 1.2Feb 20, 2013Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Sep 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_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, TTL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)264,03720
Polymers261,6316
Non-polymers2,40514
Water1,65792
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)103.530, 155.910, 181.020
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 (cattle) / Organ: 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 (cattle) / Organ: 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) / Strain (production host): NiCo21 (DE3) / References: UniProt: P63043
#4: Protein Tubulin tyrosine ligase, TTL


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Plasmid: PA23_007_ggTTL_KH6_2-378_NSKn1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: E1BQ43

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Non-polymers , 7 types, 106 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-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
#10: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


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


Mass: 18.015 Da / Num. of mol.: 92 / 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: 2.79 Å3/Da / Density % sol: 55.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 4-10% PEG 4000, 4-6% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 100 mM MES/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: 0.99987 Å
DetectorType: PSI PILATUS 2M / Detector: PIXEL / Date: Jan 26, 2012
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: 0.99987 Å / Relative weight: 1
ReflectionResolution: 2.6→62.3 Å / Num. all: 90649 / Num. obs: 90604 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 26.7 % / Biso Wilson estimate: 61.5 Å2 / Net I/σ(I): 23.5
Reflection shellResolution: 2.6→2.67 Å / Redundancy: 25.7 % / Mean I/σ(I) obs: 1.07 / Num. unique all: 6591 / % possible all: 99.9

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHENIX(phenix.refine: 1.7.3_928)model building
PHENIX(phenix.refine: 1.7.3_928)refinement
XDSdata reduction
XDSdata scaling
PHENIX1.7.3_928phasing
RefinementMethod to determine structure: Difference Fourier
Starting model: PDB ENTRY 4I4T

4i4t


Resolution: 2.6→62.275 Å / SU ML: 0.32 / σ(F): 1.99 / Phase error: 25.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2353 4511 4.98 %RANDOM
Rwork0.1974 ---
all0.1993 90649 --
obs0.1993 90582 99.94 %-
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.176 Å2 / ksol: 0.323 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-7.9029 Å20 Å2-0 Å2
2--18.5304 Å2-0 Å2
3----0.1876 Å2
Refinement stepCycle: LAST / Resolution: 2.6→62.275 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16571 0 141 92 16804
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00417278
X-RAY DIFFRACTIONf_angle_d0.80523464
X-RAY DIFFRACTIONf_dihedral_angle_d14.8126448
X-RAY DIFFRACTIONf_chiral_restr0.0572560
X-RAY DIFFRACTIONf_plane_restr0.0033053
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.62960.34371380.30932819X-RAY DIFFRACTION100
2.6296-2.66050.3621450.30632824X-RAY DIFFRACTION100
2.6605-2.69290.31971420.31332807X-RAY DIFFRACTION100
2.6929-2.7270.32161610.29942870X-RAY DIFFRACTION100
2.727-2.76290.33661650.27972792X-RAY DIFFRACTION100
2.7629-2.80080.31651630.27942857X-RAY DIFFRACTION100
2.8008-2.84080.3121310.26822839X-RAY DIFFRACTION100
2.8408-2.88320.30531400.26172862X-RAY DIFFRACTION100
2.8832-2.92820.30891310.26532851X-RAY DIFFRACTION100
2.9282-2.97620.31141480.25192851X-RAY DIFFRACTION100
2.9762-3.02750.27551400.23522855X-RAY DIFFRACTION100
3.0275-3.08260.2781490.23112818X-RAY DIFFRACTION100
3.0826-3.14190.26281530.22872868X-RAY DIFFRACTION100
3.1419-3.2060.3041410.22632855X-RAY DIFFRACTION100
3.206-3.27570.31330.22922871X-RAY DIFFRACTION100
3.2757-3.35190.26991830.21652838X-RAY DIFFRACTION100
3.3519-3.43570.24971490.21572846X-RAY DIFFRACTION100
3.4357-3.52860.25971530.2072845X-RAY DIFFRACTION100
3.5286-3.63240.24491600.19292855X-RAY DIFFRACTION100
3.6324-3.74970.22381440.18332862X-RAY DIFFRACTION100
3.7497-3.88370.21441610.17572862X-RAY DIFFRACTION100
3.8837-4.03910.20991380.17292889X-RAY DIFFRACTION100
4.0391-4.22290.19751450.16332882X-RAY DIFFRACTION100
4.2229-4.44550.20741460.152908X-RAY DIFFRACTION100
4.4455-4.7240.16441580.14112880X-RAY DIFFRACTION100
4.724-5.08850.21740.15362880X-RAY DIFFRACTION100
5.0885-5.60030.24721470.192903X-RAY DIFFRACTION100
5.6003-6.410.24371500.20252939X-RAY DIFFRACTION100
6.41-8.07320.21081570.18782966X-RAY DIFFRACTION100
8.0732-62.29290.20621660.19493077X-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)
10.566-0.6259-0.23652.88051.46172.2345-0.04750.1840.1191-0.52480.2653-0.2919-0.61440.5176-0.14930.5798-0.15220.10240.5505-0.18020.495531.353387.141452.2594
20.9967-0.3027-0.42042.45840.94223.58150.0905-0.04430.06710.2373-0.0430.2407-0.2407-0.0905-0.03950.4215-0.00350.05930.3742-0.10810.453918.967480.961266.2668
30.5971-0.498-0.0872.45581.23381.8482-0.0576-0.20550.08780.42410.09930.2066-0.04050.0579-0.0270.562-0.00080.07690.4141-0.11560.434518.492581.936573.6684
40.44280.39640.68981.6871.2923.5588-0.03540.1286-0.44560.4470.04-0.06580.55410.9504-0.10710.48030.1235-0.0480.4905-0.17380.5232.679760.737860.8868
522.0003-3.48812.00031.99992.0001-0.99691.90274.4576-4.0872-2.7051-1.69117.05281.31483.71651.47760.27470.40340.86560.34771.0425.574165.392384.2253
62.2816-0.7891-0.92163.30220.41152.04590.14560.29330.4216-0.3226-0.225-0.0468-0.5546-0.32090.10160.44590.0416-0.00770.4252-0.04760.434216.132769.175719.8702
71.1658-0.3153-0.42541.7399-0.05451.27510.04840.42180.1375-0.11530.0113-0.0088-0.17280.0996-0.02680.3399-0.01940.01170.5437-0.04430.377629.089755.506414.7538
81.36560.6685-0.15292.13420.53551.96580.029-0.27810.0929-0.0224-0.0520.01-0.16570.11270.02560.21110.03090.00570.3428-0.12910.383824.359852.23426.2742
91.9542-0.6444-0.30361.0832-0.42431.47480.0657-0.1511-0.29970.0723-0.27770.49130.585-0.65970.17430.3375-0.07830.13840.6852-0.29760.59315.378149.876928.3959
100.8078-0.3041-0.26260.80490.33541.18370.1536-0.03360.09130.0367-0.12560.2217-0.1278-0.1454-0.04830.35850.01280.0170.4687-0.18180.500712.152960.541836.5016
111.4292-0.27640.31481.86610.66322.0163-0.2045-0.26830.09710.29550.02590.4678-0.0132-0.73270.16080.44980.01660.07380.691-0.19240.57336.568859.681645.03
120.9156-0.9892-0.1131.51750.9931.3540.0296-0.3313-0.00840.0868-0.0390.37920.1519-0.06970.02390.3890.00190.05020.4138-0.0930.420815.251241.090234.1799
131.3553-0.0565-0.3252.18342.35525.7091-0.0871-0.1718-0.340.57270.05380.05130.65780.73280.00940.3805-0.005-0.05860.32950.01150.386225.726837.155831.1382
141.1325-0.79380.05862.47360.19611.3405-0.08270.20.0806-0.17170.1158-0.0573-0.10070.1697-0.01850.2616-0.06820.03020.4113-0.0280.330820.457932.4287-12.0454
151.074-0.3993-0.17191.46620.94692.16050.0131-0.07960.03520.0606-0.02230.15730.0806-0.2418-00.241-0.08050.02950.314-0.0440.33748.071725.21312.9582
162.6653-0.3920.32152.24120.21841.5837-0.07470.70210.0164-0.45770.185-0.04810.1701-0.1-0.0810.6796-0.08180.03660.8287-0.08510.428317.62749.0856-44.4882
171.3788-0.0203-0.16351.02530.07121.4846-0.05620.472-0.2365-0.34430.0486-0.19130.3363-0.0062-0.01710.5802-0.05630.08660.5852-0.19610.43821.3248-2.7534-33.8823
181.2672-0.1179-0.32011.10930.66761.8349-0.19660.4297-0.4006-0.08580.11330.08440.4007-0.20550.09090.6406-0.12290.05770.5529-0.15720.4839.2463-4.4449-21.5557
191.8516-0.0323-0.61431.2805-0.27361.59970.01230.201-0.5861-0.1039-0.04440.06970.37280.3448-0.01280.87140.05690.08150.5552-0.20790.70730.7468-17.1573-25.1075
202.2389-0.61680.34236.8043-2.47641.90510.0486-0.58160.2480.9639-0.1824-0.27580.02940.81610.03841.1509-0.032-0.00750.7702-0.21090.550624.165394.290884.7085
210.35020.1872-0.00661.45371.14911.4119-0.1473-0.0052-0.05310.18390.5774-0.40160.40210.8474-0.29190.41110.07270.03260.7289-0.23390.669843.207228.05315.2453
222.07760.7403-1.57712.33380.11142.0785-0.11690.3118-0.54450.04250.1412-0.0970.8257-0.0616-0.03360.7755-0.0370.07580.5429-0.13070.60625.996753.365370.271
232.09830.72750.43152.2454-2.18352.76260.1286-0.42660.02560.8318-0.089-0.001-0.00260.718-0.36190.7013-0.0444-0.03051.00060.11580.433810.947264.392897.9893
240.9690.279-0.45051.2408-0.17921.628-0.4603-0.2699-0.6999-0.09280.0843-0.55461.1828-0.2020.20150.9360.10360.11530.51110.18660.8051-1.767350.731198.238
252.0604-0.132-1.40340.68180.63582.0501-0.2075-0.0537-0.56050.28780.229-0.01260.2594-0.1612-0.01880.78270.03860.11640.47280.04370.6283-3.122855.845591.8113
262.1091-0.7836-0.85983.42080.33382.7913-0.1905-0.32110.09860.2151-0.52440.7876-1.8359-0.7390.69841.2099-0.0646-0.09030.87170.05040.6931-10.468666.784689.8743
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:180)
2X-RAY DIFFRACTION2chain 'A' and (resseq 181:311)
3X-RAY DIFFRACTION3chain 'A' and (resseq 312:401)
4X-RAY DIFFRACTION4chain 'A' and (resseq 402:436)
5X-RAY DIFFRACTION5chain 'A' and (resseq 437:437)
6X-RAY DIFFRACTION6chain 'B' and (resseq 1:88)
7X-RAY DIFFRACTION7chain 'B' and (resseq 89:127)
8X-RAY DIFFRACTION8chain 'B' and (resseq 128:197)
9X-RAY DIFFRACTION9chain 'B' and (resseq 198:223)
10X-RAY DIFFRACTION10chain 'B' and (resseq 224:295)
11X-RAY DIFFRACTION11chain 'B' and (resseq 296:373)
12X-RAY DIFFRACTION12chain 'B' and (resseq 374:401)
13X-RAY DIFFRACTION13chain 'B' and (resseq 402:438)
14X-RAY DIFFRACTION14chain 'C' and (resseq 1:197)
15X-RAY DIFFRACTION15chain 'C' and (resseq 198:440)
16X-RAY DIFFRACTION16chain 'D' and (resseq 2:88)
17X-RAY DIFFRACTION17chain 'D' and (resseq 89:295)
18X-RAY DIFFRACTION18chain 'D' and (resseq 296:401)
19X-RAY DIFFRACTION19chain 'D' and (resseq 402:441)
20X-RAY DIFFRACTION20chain 'E' and (resseq 6:27)
21X-RAY DIFFRACTION21chain 'E' and (resseq 43:144)
22X-RAY DIFFRACTION22chain 'F' and (resseq 1:66)
23X-RAY DIFFRACTION23chain 'F' and (resseq 67:97)
24X-RAY DIFFRACTION24chain 'F' and (resseq 185:227)
25X-RAY DIFFRACTION25chain 'F' and (resseq 259:362)
26X-RAY DIFFRACTION26chain 'F' and (resseq 371:384)

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