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- PDB-4i3z: Structure of pCDK2/CyclinA bound to ADP and 2 Magnesium ions -

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Basic information

Entry
Database: PDB / ID: 4i3z
TitleStructure of pCDK2/CyclinA bound to ADP and 2 Magnesium ions
Components
  • Cyclin-A2
  • Cyclin-dependent kinase 2
KeywordsTransferase/Cell Cycle / ADP and Magnesium binding / T160 Phosphorylation / Transferase-Cell Cycle complex
Function / homology
Function and homology information


G0 and Early G1 / Telomere Extension By Telomerase / Regulation of APC/C activators between G1/S and early anaphase / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / G2 Phase / p53-Dependent G1 DNA Damage Response / Cyclin A:Cdk2-associated events at S phase entry / Cyclin A/B1/B2 associated events during G2/M transition / DNA Damage/Telomere Stress Induced Senescence / Regulation of TP53 Degradation ...G0 and Early G1 / Telomere Extension By Telomerase / Regulation of APC/C activators between G1/S and early anaphase / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / G2 Phase / p53-Dependent G1 DNA Damage Response / Cyclin A:Cdk2-associated events at S phase entry / Cyclin A/B1/B2 associated events during G2/M transition / DNA Damage/Telomere Stress Induced Senescence / Regulation of TP53 Degradation / Processing of DNA double-strand break ends / Senescence-Associated Secretory Phenotype (SASP) / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / CDK-mediated phosphorylation and removal of Cdc6 / Orc1 removal from chromatin / cyclin A2-CDK1 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / Regulation of TP53 Activity through Phosphorylation / mitotic cell cycle phase transition / Ub-specific processing proteases / cellular response to leptin stimulus / male pronucleus / female pronucleus / cellular response to cocaine / response to glucagon / cyclin-dependent protein serine/threonine kinase regulator activity / cellular response to insulin-like growth factor stimulus / positive regulation of DNA biosynthetic process / cochlea development / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cellular response to platelet-derived growth factor stimulus / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / G2 Phase / cyclin-dependent protein kinase activity / Y chromosome / Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes / positive regulation of heterochromatin formation / p53-Dependent G1 DNA Damage Response / X chromosome / PTK6 Regulates Cell Cycle / regulation of anaphase-promoting complex-dependent catabolic process / regulation of DNA replication / Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / centrosome duplication / Telomere Extension By Telomerase / G0 and Early G1 / Activation of the pre-replicative complex / cyclin-dependent protein kinase holoenzyme complex / cellular response to nitric oxide / Cajal body / cyclin-dependent kinase / animal organ regeneration / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Activation of ATR in response to replication stress / Cyclin E associated events during G1/S transition / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / condensed chromosome / mitotic G1 DNA damage checkpoint signaling / regulation of mitotic cell cycle / regulation of G2/M transition of mitotic cell cycle / cyclin binding / post-translational protein modification / meiotic cell cycle / positive regulation of DNA replication / male germ cell nucleus / response to organic substance / cellular response to estradiol stimulus / G1/S transition of mitotic cell cycle / potassium ion transport / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / SCF(Skp2)-mediated degradation of p27/p21 / Meiotic recombination / Orc1 removal from chromatin / Transcriptional regulation of granulopoiesis / Cyclin D associated events in G1 / G2/M transition of mitotic cell cycle / positive regulation of fibroblast proliferation / cellular senescence / Regulation of TP53 Degradation / nuclear envelope / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / cellular response to hypoxia / Senescence-Associated Secretory Phenotype (SASP) / regulation of gene expression / peptidyl-serine phosphorylation / Ras protein signal transduction / Regulation of TP53 Activity through Phosphorylation / transcription regulator complex / DNA replication
Similarity search - Function
Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin-like ...Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin-like / Cyclin A; domain 1 / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Cyclin-dependent kinase 2 / Cyclin-A2
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsJacobsen, D.M. / Bao, Z.-Q. / O'Brien, P.J. / Brooks, C.L. / Young, M.A.
CitationJournal: J.Am.Chem.Soc. / Year: 2012
Title: Price To Be Paid for Two-Metal Catalysis: Magnesium Ions That Accelerate Chemistry Unavoidably Limit Product Release from a Protein Kinase
Authors: Jacobsen, D.M. / Bao, Z.-Q. / O'Brien, P.J. / Brooks, C.L. / Young, M.A.
History
DepositionNov 27, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 26, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cyclin-dependent kinase 2
B: Cyclin-A2
C: Cyclin-dependent kinase 2
D: Cyclin-A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,23721
Polymers126,3864
Non-polymers1,85117
Water9,386521
1
A: Cyclin-dependent kinase 2
B: Cyclin-A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,16511
Polymers63,1932
Non-polymers9729
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4840 Å2
ΔGint-53 kcal/mol
Surface area23140 Å2
MethodPISA
2
C: Cyclin-dependent kinase 2
D: Cyclin-A2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,07310
Polymers63,1932
Non-polymers8808
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5280 Å2
ΔGint-52 kcal/mol
Surface area23330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.770, 164.130, 73.280
Angle α, β, γ (deg.)90.00, 107.07, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 1:296 )
211chain C and (resseq 1:296 )
112chain B and (resseq 175:431 )
212chain D and (resseq 175:431 )

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Cyclin-dependent kinase 2 / / Cell division protein kinase 2 / p33 protein kinase


Mass: 33786.117 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDK2, CDKN2 / Plasmid: PET28A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P24941, cyclin-dependent kinase
#2: Protein Cyclin-A2 / Cyclin-A


Mass: 29406.934 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 105-421
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ccna, Ccna2, Cyca / Plasmid: PET28A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P51943

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Non-polymers , 5 types, 538 molecules

#3: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 521 / 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: 3.22 Å3/Da / Density % sol: 61.78 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 22% w/v polyacrylic acid sodium salt 5100, 20mM MgCl2, 100mM HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 22, 2010
RadiationMonochromator: DIAMOND LAUE / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.05→43.12 Å / Num. obs: 98449 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1.5 / Rsym value: 0.119 / Net I/σ(I): 7.5
Reflection shellResolution: 2.05→2.16 Å / Mean I/σ(I) obs: 1.6 / Rsym value: 0.857 / % possible all: 97.3

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Processing

Software
NameVersionClassification
MAR345data collection
PHASERphasing
PHENIX(phenix.refine: 1.7_650)refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.05→42.79 Å / SU ML: 0.32 / σ(F): 0 / Phase error: 23.68 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2278 4895 4.98 %
Rwork0.1974 --
obs0.1989 98383 98.55 %
all-98385 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 59.541 Å2 / ksol: 0.401 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-12.1911 Å20 Å27.7294 Å2
2---7.8862 Å2-0 Å2
3----4.3049 Å2
Refinement stepCycle: LAST / Resolution: 2.05→42.79 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8902 0 114 521 9537
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0089229
X-RAY DIFFRACTIONf_angle_d0.88712535
X-RAY DIFFRACTIONf_dihedral_angle_d14.9493434
X-RAY DIFFRACTIONf_chiral_restr0.0611414
X-RAY DIFFRACTIONf_plane_restr0.0041564
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2382X-RAY DIFFRACTIONPOSITIONAL
12C2382X-RAY DIFFRACTIONPOSITIONAL0.046
21B2069X-RAY DIFFRACTIONPOSITIONAL
22D2069X-RAY DIFFRACTIONPOSITIONAL0.077
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.05-2.07330.35781550.33413092X-RAY DIFFRACTION97
2.0733-2.09770.33121540.31513080X-RAY DIFFRACTION97
2.0977-2.12330.29371420.29983039X-RAY DIFFRACTION97
2.1233-2.15020.31131570.28993099X-RAY DIFFRACTION97
2.1502-2.17840.29851470.27133020X-RAY DIFFRACTION97
2.1784-2.20830.29351630.27593082X-RAY DIFFRACTION97
2.2083-2.23980.30151520.26813067X-RAY DIFFRACTION97
2.2398-2.27330.28241590.25333065X-RAY DIFFRACTION97
2.2733-2.30880.28741780.2453042X-RAY DIFFRACTION97
2.3088-2.34660.2581780.22883030X-RAY DIFFRACTION97
2.3466-2.38710.27731450.22513084X-RAY DIFFRACTION97
2.3871-2.43050.25141570.21713054X-RAY DIFFRACTION97
2.4305-2.47720.291780.22363050X-RAY DIFFRACTION98
2.4772-2.52780.27581710.21493128X-RAY DIFFRACTION98
2.5278-2.58280.2311390.20213116X-RAY DIFFRACTION99
2.5828-2.64280.25561630.20143156X-RAY DIFFRACTION99
2.6428-2.70890.22581720.19043133X-RAY DIFFRACTION99
2.7089-2.78210.2281640.17833114X-RAY DIFFRACTION100
2.7821-2.8640.22261700.17653170X-RAY DIFFRACTION100
2.864-2.95640.20711700.17653176X-RAY DIFFRACTION100
2.9564-3.0620.19781640.1743161X-RAY DIFFRACTION100
3.062-3.18460.21881930.17283127X-RAY DIFFRACTION100
3.1846-3.32950.23871850.17483146X-RAY DIFFRACTION100
3.3295-3.50490.20021780.16313158X-RAY DIFFRACTION100
3.5049-3.72440.18521550.16863179X-RAY DIFFRACTION100
3.7244-4.01180.19211390.16813185X-RAY DIFFRACTION100
4.0118-4.41520.18331650.16543174X-RAY DIFFRACTION100
4.4152-5.05320.18241550.16323188X-RAY DIFFRACTION100
5.0532-6.36310.21931600.20053183X-RAY DIFFRACTION100
6.3631-42.79950.22221870.20683190X-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)
10.8906-0.84770.83892.9723-1.3271.57290.4516-0.0595-0.1194-0.47250.06560.1093-0.0258-0.0040.10510.26230.02590.12130.1429-0.0010.549-4.1249-48.7782-4.1773
20.10630.1405-0.030.1928-0.04640.26080.17010.13310.00920.04770.10880.2288-0.059-0.0529-0.15310.20010.05730.01710.20580.03810.27910.0158-46.7445-10.9981
30.6697-0.22270.21190.85680.14220.7179-0.0621-0.0313-0.04920.03230.03480.08770.1450.13430.02460.18070.01510.01950.146-0.00570.155410.1942-38.76530.9224
40.4295-0.2381-0.25640.6714-0.12720.24940.00590.07180.0068-0.3213-0.09580.0590.05270.1037-0.02220.22080.0124-0.0030.1789-0.00030.201711.2184-23.1122-0.0241
50.09920.08660.06810.2934-0.05760.13630.0539-0.07720.12830.0294-0.05710.3126-0.01860.11190.01430.0252-0.0122-0.0090.2093-0.02450.3753.987-15.49446.3919
60.1973-0.2586-0.09910.37380.09970.52960.0296-0.3610.52690.23620.0683-0.1799-0.12570.1548-0.02820.2033-0.02580.03510.2147-0.06550.305614.626-12.69868.7483
70.5189-0.2612-0.09890.45810.28940.2559-0.1207-0.18960.14610.32860.0804-0.09630.22160.1275-0.03650.22850.0315-0.01460.3062-0.01610.168318.8053-29.505812.5171
80.1409-0.0916-0.01140.973-0.1780.3550.0919-0.41580.0128-0.0291-0.34980.20460.17330.60140.03840.2597-0.00230.07650.3904-0.07680.194529.8482-37.3734-6.6848
90.4194-0.2285-0.0790.5171-0.02180.0254-0.0208-0.09940.0493-0.19650.1511-0.1674-0.15620.2112-0.03960.43190.06520.06550.3164-0.04860.311727.1645-51.5408-30.224
100.228-0.00230.27790.29690.0520.5226-0.02320.01930.0146-0.37120.1022-0.0896-0.27950.188-0.03030.2729-0.01330.02360.136-0.0050.111119.1756-39.1516-29.3672
110.4773-0.009-0.10660.64190.0530.13230.0502-0.0983-0.0729-0.37940.02180.0841-0.0247-0.1086-0.01440.30180.0204-0.05950.17080.00560.186610.1472-39.8471-26.9653
120.3133-0.1392-0.00360.2849-0.04250.4467-0.2564-0.0044-0.0031-0.17450.2874-0.0419-0.2340.7144-0.15210.2329-0.07230.0960.4662-0.10330.205238.7849-31.5451-21.2347
130.06660.1523-0.0070.4057-0.1340.1859-0.24020.33810.0293-0.35610.2161-0.0768-0.2530.477-0.15950.5144-0.18610.14570.3921-0.05640.217734.8192-25.5295-34.0492
141.1745-0.7675-0.4790.57320.22760.33290.1159-0.08630.2268-0.2570.0429-0.3330.3287-0.0370.01510.69290.0092-0.17640.14840.02720.326916.346215.8173-36.1487
150.10750.198-0.03660.3193-0.0590.010.07860.04640.0950.2911-0.0974-0.11640.07940.01620.01610.30120.0574-0.09080.18480.03020.249216.661213.8463-44.1277
160.74140.19130.00830.6692-0.16440.4318-0.0271-0.03410.01010.35350.02170.0188-0.1773-0.0847-0.01150.31480.0015-0.01160.13550.01020.11751.42296.1143-39.9729
170.135-0.18430.1450.5328-0.13320.1110.06650.0670.02250.1365-0.0808-0.2914-0.14260.06380.0020.36530.01640.05280.19120.01710.23950.7911-9.5292-41.4764
180.21670.21770.06080.4997-0.04110.0542-0.0441-0.1061-0.08540.36950.001-0.35830.0395-0.02460.00910.43760.018-0.03210.19290.0060.29693.0891-17.2674-32.185
190.7408-0.07970.28220.0323-0.00080.41240.0859-0.1564-0.42650.37690.06050.29910.353-0.11820.05610.4756-0.02690.09570.2170.05860.2702-7.1219-19.8477-36.1477
200.2304-0.10180.08810.35860.16710.42480.0987-0.09430.03060.47250.03320.27320.0058-0.1118-0.00170.39060.01140.13430.26630.01380.2487-12.3638-2.9341-35.2118
210.09070.0686-0.0670.302-0.39490.79370.0056-0.3475-0.03010.302-0.1810.0874-0.1728-0.2143-0.05310.1736-0.04840.06930.24270.04480.1653-10.73125.3445-57.2539
220.402-0.39290.27020.7143-0.14990.2146-0.11920.0979-0.0499-0.41650.1280.08720.1737-0.2284-0.01110.2955-0.0256-0.03120.22880.04480.27574.971919.3057-75.1733
230.41960.0017-0.30550.37250.00170.2205-0.15240.0014-0.049-0.27110.0572-0.1780.2186-0.1287-0.02130.1192-0.00950.0080.1682-0.0030.2113.25865.2271-69.1061
240.0434-0.0601-0.06290.17360.00110.1572-0.0673-0.10120.0571-0.02630.0345-0.1146-0.125-0.04030.01670.117-0.0172-0.03470.1909-0.02920.242613.578812.7006-60.6431
250.183-0.2004-0.1280.30180.26390.2232-0.12020.2963-0.039-0.19180.10720.13830.01030.0504-0.0137-0.0229-0.1614-0.10730.2652-0.00310.17-10.2314-0.2389-74.4087
260.33030.55860.1850.95520.290.3578-0.21420.3704-0.40990.00610.1435-0.3195-0.0461-0.0317-0.04690.3465-0.12170.06540.2911-0.08690.1220.0156-6.474-82.912
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:23)
2X-RAY DIFFRACTION2chain 'A' and (resseq 24:45)
3X-RAY DIFFRACTION3chain 'A' and (resseq 46:158)
4X-RAY DIFFRACTION4chain 'A' and (resseq 159:198)
5X-RAY DIFFRACTION5chain 'A' and (resseq 199:219)
6X-RAY DIFFRACTION6chain 'A' and (resseq 220:266)
7X-RAY DIFFRACTION7chain 'A' and (resseq 267:296)
8X-RAY DIFFRACTION8chain 'B' and (resseq 175:192)
9X-RAY DIFFRACTION9chain 'B' and (resseq 193:207)
10X-RAY DIFFRACTION10chain 'B' and (resseq 208:268)
11X-RAY DIFFRACTION11chain 'B' and (resseq 269:310)
12X-RAY DIFFRACTION12chain 'B' and (resseq 311:399)
13X-RAY DIFFRACTION13chain 'B' and (resseq 400:431)
14X-RAY DIFFRACTION14chain 'C' and (resseq 1:23)
15X-RAY DIFFRACTION15chain 'C' and (resseq 24:45)
16X-RAY DIFFRACTION16chain 'C' and (resseq 46:158)
17X-RAY DIFFRACTION17chain 'C' and (resseq 159:198)
18X-RAY DIFFRACTION18chain 'C' and (resseq 199:219)
19X-RAY DIFFRACTION19chain 'C' and (resseq 220:266)
20X-RAY DIFFRACTION20chain 'C' and (resseq 267:296)
21X-RAY DIFFRACTION21chain 'D' and (resseq 175:192)
22X-RAY DIFFRACTION22chain 'D' and (resseq 193:207)
23X-RAY DIFFRACTION23chain 'D' and (resseq 208:287)
24X-RAY DIFFRACTION24chain 'D' and (resseq 288:310)
25X-RAY DIFFRACTION25chain 'D' and (resseq 311:399)
26X-RAY DIFFRACTION26chain 'D' and (resseq 400:431)

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