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- PDB-7cnn: vinorelbine in complex with tubulin -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7cnn
Titlevinorelbine in complex with tubulin
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta chain
  • Tubulin tyrosine ligase
KeywordsCELL CYCLE / Vincristinve / tubulin / protein-drug complex
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins ...tubulin-tyrosine ligase activity / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Separation of Sister Chromatids / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / microtubule depolymerization / COPI-mediated anterograde transport / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / mitotic cell cycle / growth cone / microtubule / neuron projection / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytoplasm
Similarity search - Function
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. ...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. / 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. / 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
Similarity search - Domain/homology
Vinorelbine / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Tubulin beta chain / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain
Similarity search - Component
Biological speciesMus musculus (house mouse)
Gallus gallus (chicken)
Sus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.5 Å
AuthorsWang, Y.X. / Wu, C.Y.
CitationJournal: Febs Lett. / Year: 2021
Title: The high-resolution X-ray structure of vinca-domain inhibitors of microtubules provides a rational approach for drug design.
Authors: Chengyong, W. / Jinghong, X. / Yanyan, W. / Qing-Jie, X. / Lingling, M. / Yuyan, L. / Hai, C. / Qian, L. / Quan, Z. / Bo, S. / Yuxi, W.
History
DepositionAug 2, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 4, 2021Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2022Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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 chain
C: Tubulin alpha-1B chain
D: Tubulin beta chain
E: Stathmin-4
F: Tubulin tyrosine ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,13123
Polymers261,6316
Non-polymers3,49917
Water7,530418
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22520 Å2
ΔGint-162 kcal/mol
Surface area80560 Å2
Unit cell
Length a, b, c (Å)104.878, 156.129, 183.000
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: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: Q2XVP4
#2: Protein Tubulin beta chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: A0A287AGU7
#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.) Mus musculus (house mouse) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63042
#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 , 8 types, 435 molecules

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


Mass: 523.180 Da / Num. of mol.: 3 / 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.: 4 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#10: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-GDF / Vinorelbine


Mass: 778.932 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C45H54N4O8 / Comment: medication, chemotherapy*YM
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 418 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 2.86 Å3/Da / Density % sol: 57.04 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 6% PEG, 5% glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9785 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 15, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9785 Å / Relative weight: 1
ReflectionResolution: 2.498→50 Å / Num. obs: 104536 / % possible obs: 99.9 % / Redundancy: 13 % / Rmerge(I) obs: 0.179 / Rpim(I) all: 0.051 / Rrim(I) all: 0.186 / Χ2: 0.964 / Net I/σ(I): 3.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.5-2.5410.51.05651580.6770.3331.1090.9499.7
2.54-2.5912.10.98951380.7610.291.0310.94699.9
2.59-2.6412.90.88151830.8060.250.9170.951100
2.64-2.6913.10.82751800.8420.2340.860.978100
2.69-2.7512.90.71851480.8690.2060.7480.9699.8
2.75-2.8212.50.62551790.8940.1820.6520.974100
2.82-2.89130.52751710.9270.150.5480.986100
2.89-2.9613.70.48751890.940.1340.5050.99599.9
2.96-3.0513.80.39951980.9610.110.4141.004100
3.05-3.1513.70.33551750.9710.0930.3481.009100
3.15-3.2613.40.28152190.9780.0790.2921.01199.9
3.26-3.3912.80.23652030.9840.0680.2451.027100
3.39-3.55130.1952270.9890.0540.1981.03499.8
3.55-3.7313.90.15951970.9930.0440.1651.039100
3.73-3.9713.80.12752240.9950.0350.1321.023100
3.97-4.2713.60.10452470.9960.0290.1080.958100
4.27-4.712.70.08452920.9970.0250.0880.926100
4.7-5.3813.90.08552950.9980.0230.0890.899100
5.38-6.7812.90.09553480.9970.0270.0990.882100
6.78-5012.40.05155650.9990.0150.0540.73699.7

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.14_3260refinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4I55

4i55


Resolution: 2.5→49.957 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2293 2000 1.94 %
Rwork0.1987 100940 -
obs0.1993 102940 98.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 187.9 Å2 / Biso mean: 49.0326 Å2 / Biso min: 18.74 Å2
Refinement stepCycle: final / Resolution: 2.5→49.957 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17423 0 215 418 18056
Biso mean--44.24 39.4 -
Num. residues----2200
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5-2.56070.33821260.2969640489
2.5607-2.62990.29341400.2618701897
2.6299-2.70730.34941430.263719899
2.7073-2.79470.30311420.25677227100
2.7947-2.89450.30211450.25137249100
2.8945-3.01040.25861430.23767253100
3.0104-3.14740.27981440.2287256100
3.1474-3.31330.22641450.2267311100
3.3133-3.52080.23691440.20737276100
3.5208-3.79260.21721450.18637319100
3.7926-4.17410.1931450.16717344100
4.1741-4.77770.1991460.15277356100
4.7777-6.01780.19721460.1733736299
6.0178-49.9570.17111460.1673736796
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)
10.8970.0577-0.01862.07650.19850.992-0.08990.14590.2772-0.41810.2636-0.2452-0.73630.3349-0.25940.5921-0.12430.08180.4109-0.09850.38429.812896.447954.5777
21.18140.01040.2923.1030.51442.0294-0.0840.42620.3011-0.73050.1406-0.0844-0.79990.1523-0.2450.5556-0.08560.06130.4156-0.06420.384229.065586.641943.1392
30.85450.48340.20582.46540.87731.51430.02090.12310.0211-0.08530.2974-0.5419-0.28420.5469-0.28460.2964-0.04740.05940.4637-0.18070.413735.478977.286355.6857
41.43760.14620.46691.810.60382.7190.0547-0.04060.00390.12390.0529-0.0667-0.20440.1777-0.14430.26780.00460.05270.2526-0.06250.26421.517583.619565.338
50.85270.7598-0.41011.36870.88522.42060.2428-0.03810.09840.1089-0.15670.2605-0.3414-0.3228-0.05190.32290.02140.07970.2588-0.08260.34639.541183.817572.3363
60.4738-0.00640.18122.63421.33881.8551-0.0258-0.12240.06380.40570.09030.0535-0.06970.046-0.12990.30030.00560.04430.2693-0.0510.261419.251582.40573.9326
71.0410.2417-0.05092.06191.70563.7188-0.1553-0.1282-0.15160.43210.2577-0.37580.42160.6719-0.23760.29580.1166-0.0760.3894-0.11880.426332.194461.022662.0754
81.7462-0.7226-0.50422.93960.43652.40170.01020.04120.2277-0.18870.1558-0.01-0.4756-0.0643-0.03340.2595-0.04590.03540.18-0.01980.250816.483865.612322.7171
91.326-0.18420.5481.16730.38742.66390.05750.23430.7886-0.49850.008-0.135-1.17810.0375-0.09640.7218-0.00460.03980.35-0.01870.539915.703879.519123.5911
100.823-0.4682-0.5532.75670.58451.97310.10410.19070.168-0.4630.0167-0.0479-0.56440.233-0.1390.3648-0.05440.01890.3965-0.02350.312324.557460.446714.0907
110.8315-0.2439-0.15611.74090.97911.59110.0092-0.09130.0774-0.03590.1006-0.1755-0.14330.2214-0.12470.2024-0.00780.01630.2902-0.06450.283624.11952.86926.2161
120.56480.0968-0.01731.44441.41142.31160.0286-0.06620.0038-0.0691-0.16210.1574-0.0723-0.31640.04020.20050.0124-0.00230.2771-0.06290.31816.82855.782327.9832
130.8449-0.31570.22761.59640.00921.9666-0.0759-0.05110.06590.06320.0644-0.0985-0.13230.0023-0.0780.21190.00410.00770.2837-0.07890.282719.291661.118939.9474
141.54080.06210.28622.0261.12161.5935-0.072-0.05420.0885-0.0921-0.09780.2792-0.1389-0.45410.05630.17390.03430.00490.3359-0.09050.30484.208461.544842.7442
150.3487-0.4748-0.04771.2661.57311.634-0.0197-0.04120.03930.1834-0.03150.16790.1875-0.05550.0420.18110.00240.04140.2031-0.01250.235414.042243.411334.159
160.55370.6001-0.15431.16781.1452.8015-0.1143-0.1613-0.240.22940.0010.00720.25590.4694-0.13170.27910.0586-0.04460.3023-0.02180.364424.553938.290731.9894
171.87-0.97130.14862.7977-0.00291.0512-0.01260.20160.185-0.4015-0.02150.0813-0.2852-0.00650.00310.3181-0.080.01710.32640.01730.25615.192538.7791-16.0173
180.68350.11770.17592.0180.78531.9901-0.08430.10990.0424-0.22290.2078-0.2789-0.16120.2763-0.10840.2215-0.05560.03970.3235-0.04970.290527.547829.6601-10.1791
190.5941-0.9016-0.50561.69690.12221.3815-0.10920.1327-0.0030.060.06530.26660.1169-0.08760.080.2625-0.02080.02620.2627-0.00490.261212.197920.6194-4.8205
200.7353-0.30180.26020.22110.4141.57110.004-0.00790.1057-0.0449-0.07630.25680.0391-0.39290.1360.2123-0.02810.01130.303-0.02760.31313.488930.70052.2949
212.1752-0.7894-0.06921.11460.32181.4364-0.0477-0.24440.1007-0.09720.08070.27330.1046-0.42370.14420.2592-0.09760.0050.2836-0.07420.36290.342134.61178.8567
220.7949-0.5941-0.26221.22260.60471.4068-0.1001-0.0092-0.03930.15260.1080.00160.30230.089-0.00480.2896-0.0240.00520.2393-0.03410.308919.619513.11732.8008
231.9265-0.1330.42331.3985-0.42262.4154-0.06140.82990.1547-0.57610.0390.0799-0.0796-0.36860.0630.482-0.12750.02250.731-0.070.373816.73518.7147-44.0561
240.931-0.3116-0.11411.9379-0.29761.553-0.13220.5543-0.1505-0.4932-0.0415-0.26320.21750.1658-0.08660.5994-0.14040.16950.73-0.20970.500933.2347-1.6636-43.7427
251.5646-0.0989-0.58261.19230.24162.3649-0.23340.3407-0.3059-0.27260.0732-0.01130.4888-0.22530.04620.5223-0.13890.10220.5075-0.19620.37420.144-6.1694-33.8694
260.80030.1003-0.01770.75220.66912.0693-0.27590.387-0.2101-0.19080.11730.09990.0762-0.24410.05950.3567-0.09230.07420.4216-0.09240.391217.47545.7692-22.9
271.210.2578-0.34281.42821.23981.5907-0.20770.4199-0.2771-0.1061-0.09440.38160.3398-0.6140.19220.4301-0.14980.05530.5642-0.14480.45373.2451-0.1738-20.2228
281.03910.6758-0.80531.31910.11042.3767-0.34380.114-0.7247-0.05090.14810.0540.76760.03410.11560.6641-0.12540.17080.4766-0.21890.579518.0774-15.3056-25.2836
291.8723-0.3533-0.8251.79930.40722.3894-0.50820.1188-0.80930.1420.0191-0.08520.8110.4276-0.0090.64850.00290.17250.3875-0.19220.577529.5686-16.9713-23.6936
301.12260.03470.17710.87961.41691.621-0.0131-0.21630.20040.26790.0594-0.30630.22210.4429-0.25560.6308-0.08810.04950.5111-0.12150.47727.940591.819682.7197
310.34670.0145-0.18611.1691.0541.4376-0.0825-0.0215-0.03820.20440.4692-0.41690.40010.5431-0.31730.28790.02180.03420.4993-0.14350.511842.427827.21884.4097
321.7030.1803-1.97010.9324-1.61823.3188-0.2254-0.4388-0.45020.2319-0.0455-0.2950.4660.68260.00320.48180.06940.01390.31580.0470.434111.43657.709787.0717
331.07851.5334-1.36172.3755-0.10282.2992-0.156-0.6983-0.91140.6527-0.006-0.51840.70230.88590.0010.81330.2460.17080.65910.19260.72867.696549.8772101.8324
340.36790.9799-1.12050.9201-0.06791.9679-0.4814-0.0924-0.630.36930.237-0.15230.95310.18760.11570.92920.14650.21140.50980.1040.7093-3.037848.1581100.9608
351.96420.1844-1.31350.70660.11462.8711-0.1528-0.1066-0.2470.31690.1121-0.02740.3958-0.08590.13010.53490.00410.08910.34220.01590.4323-1.104459.407386.9465
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 199 )A103 - 199
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 273 )A200 - 273
5X-RAY DIFFRACTION5chain 'A' and (resid 274 through 311 )A274 - 311
6X-RAY DIFFRACTION6chain 'A' and (resid 312 through 401 )A312 - 401
7X-RAY DIFFRACTION7chain 'A' and (resid 402 through 438 )A402 - 438
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 28 )B1 - 28
9X-RAY DIFFRACTION9chain 'B' and (resid 29 through 59 )B29 - 59
10X-RAY DIFFRACTION10chain 'B' and (resid 60 through 128 )B60 - 128
11X-RAY DIFFRACTION11chain 'B' and (resid 129 through 197 )B129 - 197
12X-RAY DIFFRACTION12chain 'B' and (resid 198 through 243 )B198 - 243
13X-RAY DIFFRACTION13chain 'B' and (resid 244 through 273 )B244 - 273
14X-RAY DIFFRACTION14chain 'B' and (resid 274 through 372 )B274 - 372
15X-RAY DIFFRACTION15chain 'B' and (resid 373 through 401 )B373 - 401
16X-RAY DIFFRACTION16chain 'B' and (resid 402 through 440 )B402 - 440
17X-RAY DIFFRACTION17chain 'C' and (resid 1 through 102 )C1 - 102
18X-RAY DIFFRACTION18chain 'C' and (resid 103 through 161 )C103 - 161
19X-RAY DIFFRACTION19chain 'C' and (resid 162 through 223 )C162 - 223
20X-RAY DIFFRACTION20chain 'C' and (resid 224 through 311 )C224 - 311
21X-RAY DIFFRACTION21chain 'C' and (resid 312 through 372 )C312 - 372
22X-RAY DIFFRACTION22chain 'C' and (resid 373 through 440 )C373 - 440
23X-RAY DIFFRACTION23chain 'D' and (resid 2 through 88 )D2 - 88
24X-RAY DIFFRACTION24chain 'D' and (resid 89 through 127 )D89 - 127
25X-RAY DIFFRACTION25chain 'D' and (resid 128 through 238 )D128 - 238
26X-RAY DIFFRACTION26chain 'D' and (resid 239 through 268 )D239 - 268
27X-RAY DIFFRACTION27chain 'D' and (resid 269 through 372 )D269 - 372
28X-RAY DIFFRACTION28chain 'D' and (resid 373 through 401 )D373 - 401
29X-RAY DIFFRACTION29chain 'D' and (resid 402 through 441 )D402 - 441
30X-RAY DIFFRACTION30chain 'E' and (resid 6 through 46 )E6 - 46
31X-RAY DIFFRACTION31chain 'E' and (resid 47 through 142 )E47 - 142
32X-RAY DIFFRACTION32chain 'F' and (resid 1 through 151 )F1 - 151
33X-RAY DIFFRACTION33chain 'F' and (resid 152 through 235 )F152 - 235
34X-RAY DIFFRACTION34chain 'F' and (resid 236 through 297 )F236 - 297
35X-RAY DIFFRACTION35chain 'F' and (resid 298 through 384 )F298 - 384

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