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- PDB-5tzw: CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX WITH 1... -

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Basic information

Entry
Database: PDB / ID: 5tzw
TitleCRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX WITH 1-[(3,4-difluorophenyl)carbonyl]-3,3-difluoro-5-{5-methyl-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl}piperidine
ComponentscGMP-dependent 3',5'-cyclic phosphodiesterase
KeywordsHYDROLASE/HYDROLASE INHIBITOR / phosphodiesterase / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


regulation of cGMP-mediated signaling / cellular response to 2,3,7,8-tetrachlorodibenzodioxine / cellular response to macrophage colony-stimulating factor stimulus / cellular response to cGMP / negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / heart valve development / cellular response to granulocyte macrophage colony-stimulating factor stimulus / positive regulation of vascular permeability / negative regulation of vascular permeability / establishment of endothelial barrier ...regulation of cGMP-mediated signaling / cellular response to 2,3,7,8-tetrachlorodibenzodioxine / cellular response to macrophage colony-stimulating factor stimulus / cellular response to cGMP / negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / heart valve development / cellular response to granulocyte macrophage colony-stimulating factor stimulus / positive regulation of vascular permeability / negative regulation of vascular permeability / establishment of endothelial barrier / regulation of mitochondrion organization / aorta development / cGMP-mediated signaling / ventricular septum development / 3',5'-cGMP-stimulated cyclic-nucleotide phosphodiesterase activity / 3',5'-cGMP-inhibited cyclic-nucleotide phosphodiesterase activity / 3',5'-cyclic-nucleotide phosphodiesterase / negative regulation of cGMP-mediated signaling / cGMP catabolic process / phosphate ion binding / negative regulation of cAMP-mediated signaling / cGMP effects / TPR domain binding / monocyte differentiation / cGMP binding / 3',5'-cyclic-GMP phosphodiesterase activity / 3',5'-cyclic-AMP phosphodiesterase activity / cAMP-mediated signaling / cAMP binding / cellular response to transforming growth factor beta stimulus / cellular response to cAMP / synaptic membrane / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / cellular response to mechanical stimulus / positive regulation of inflammatory response / cellular response to xenobiotic stimulus / presynaptic membrane / G alpha (s) signalling events / mitochondrial outer membrane / mitochondrial inner membrane / mitochondrial matrix / positive regulation of gene expression / perinuclear region of cytoplasm / Golgi apparatus / negative regulation of transcription by RNA polymerase II / magnesium ion binding / endoplasmic reticulum / protein homodimerization activity / zinc ion binding / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Catalytic domain of cyclic nucleotide phosphodiesterase 4b2b / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain / 3'5'-cyclic nucleotide phosphodiesterase / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain / 3'5'-cyclic nucleotide phosphodiesterase, conserved site / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain superfamily / 3'5'-cyclic nucleotide phosphodiesterase / 3'5'-cyclic nucleotide phosphodiesterase domain signature. / 3'5'-cyclic nucleotide phosphodiesterase domain profile. / GAF domain ...Catalytic domain of cyclic nucleotide phosphodiesterase 4b2b / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain / 3'5'-cyclic nucleotide phosphodiesterase / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain / 3'5'-cyclic nucleotide phosphodiesterase, conserved site / 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain superfamily / 3'5'-cyclic nucleotide phosphodiesterase / 3'5'-cyclic nucleotide phosphodiesterase domain signature. / 3'5'-cyclic nucleotide phosphodiesterase domain profile. / GAF domain / Domain present in phytochromes and cGMP-specific phosphodiesterases. / GAF domain / Metal dependent phosphohydrolases with conserved 'HD' motif. / GAF-like domain superfamily / HD/PDEase domain / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-7P4 / cGMP-dependent 3',5'-cyclic phosphodiesterase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.59 Å
AuthorsXu, R. / Aertgeerts, K.
CitationJournal: J. Med. Chem. / Year: 2017
Title: Design and Synthesis of Novel and Selective Phosphodiesterase 2 (PDE2a) Inhibitors for the Treatment of Memory Disorders.
Authors: Gomez, L. / Massari, M.E. / Vickers, T. / Freestone, G. / Vernier, W. / Ly, K. / Xu, R. / McCarrick, M. / Marrone, T. / Metz, M. / Yan, Y.G. / Yoder, Z.W. / Lemus, R. / Broadbent, N.J. / ...Authors: Gomez, L. / Massari, M.E. / Vickers, T. / Freestone, G. / Vernier, W. / Ly, K. / Xu, R. / McCarrick, M. / Marrone, T. / Metz, M. / Yan, Y.G. / Yoder, Z.W. / Lemus, R. / Broadbent, N.J. / Barido, R. / Warren, N. / Schmelzer, K. / Neul, D. / Lee, D. / Andersen, C.B. / Sebring, K. / Aertgeerts, K. / Zhou, X. / Tabatabaei, A. / Peters, M. / Breitenbucher, J.G.
History
DepositionNov 22, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 22, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 22, 2017Group: Database references
Revision 1.2Mar 6, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: cGMP-dependent 3',5'-cyclic phosphodiesterase
B: cGMP-dependent 3',5'-cyclic phosphodiesterase
C: cGMP-dependent 3',5'-cyclic phosphodiesterase
D: cGMP-dependent 3',5'-cyclic phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)162,60416
Polymers160,6724
Non-polymers1,93212
Water19,9971110
1
A: cGMP-dependent 3',5'-cyclic phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6514
Polymers40,1681
Non-polymers4833
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: cGMP-dependent 3',5'-cyclic phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6514
Polymers40,1681
Non-polymers4833
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: cGMP-dependent 3',5'-cyclic phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6514
Polymers40,1681
Non-polymers4833
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: cGMP-dependent 3',5'-cyclic phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6514
Polymers40,1681
Non-polymers4833
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)55.806, 72.997, 91.000
Angle α, β, γ (deg.)109.220, 90.960, 91.070
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
cGMP-dependent 3',5'-cyclic phosphodiesterase / Cyclic GMP-stimulated phosphodiesterase / cGSPDE


Mass: 40168.051 Da / Num. of mol.: 4 / Fragment: catalytic domain, UNP residues 323-663
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PDE2A / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): baculovirus insect cell Hi5
References: UniProt: O00408, 3',5'-cyclic-nucleotide phosphodiesterase
#2: Chemical
ChemComp-7P4 / [(5S)-3,3-difluoro-5-(5-methyl[1,2,4]triazolo[1,5-a]pyrimidin-7-yl)piperidin-1-yl](3,4-difluorophenyl)methanone


Mass: 393.338 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C18H15F4N5O
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: Zn
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: Mg
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1110 / 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: 2.19 Å3/Da / Density % sol: 43.9 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.4 / Details: 17-19% PEG3350, 0.2M MgCl2, 0.1M Tris, pH 8.4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.97741 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 7, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97741 Å / Relative weight: 1
ReflectionResolution: 1.59→68.91 Å / Num. obs: 173341 / % possible obs: 95.2 % / Redundancy: 2 % / Biso Wilson estimate: 17.38 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 9.2
Reflection shellResolution: 1.59→1.63 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.669 / % possible all: 77.7

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.21 Å68.91 Å
Translation8.21 Å68.91 Å

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Processing

Software
NameVersionClassification
xia2data scaling
PHASER2.6.1phasing
PHENIX(1.10.1-2155_1692: ???)refinement
PDB_EXTRACT3.2data extraction
xia2data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.59→68.907 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 26.15
RfactorNum. reflection% reflection
Rfree0.2246 8491 4.92 %
Rwork0.1884 --
obs0.1902 172516 94.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 80.92 Å2 / Biso mean: 27.2027 Å2 / Biso min: 8.55 Å2
Refinement stepCycle: final / Resolution: 1.59→68.907 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11045 0 0 1110 12155
Biso mean---33.48 -
Num. residues----1348
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00711344
X-RAY DIFFRACTIONf_angle_d0.85515330
X-RAY DIFFRACTIONf_chiral_restr0.0461627
X-RAY DIFFRACTIONf_plane_restr0.0051983
X-RAY DIFFRACTIONf_dihedral_angle_d17.9834177
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.59-1.60810.37911930.35273995418870
1.6081-1.6270.35842690.33854601487079
1.627-1.64690.35792970.33935331562893
1.6469-1.66770.35922750.32995363563894
1.6677-1.68960.34893190.31665480579994
1.6896-1.71280.38862640.32325415567994
1.7128-1.73730.32792840.30775478576295
1.7373-1.76320.3082900.28785445573595
1.7632-1.79080.31722760.2785512578895
1.7908-1.82010.30873050.26925503580895
1.8201-1.85150.30562800.25495492577295
1.8515-1.88520.28552530.2445514576795
1.8852-1.92140.28252700.23635585585596
1.9214-1.96070.25892700.22535499576996
1.9607-2.00330.24522720.21865573584596
2.0033-2.04990.24842540.21235563581796
2.0499-2.10120.22792660.19375646591296
2.1012-2.1580.22982730.18335591586496
2.158-2.22150.21162810.17335565584697
2.2215-2.29320.20883060.17095552585897
2.2932-2.37510.19733340.16825517585197
2.3751-2.47020.21123110.1685584589597
2.4702-2.58270.21572810.16755658593997
2.5827-2.71880.21572850.16945602588797
2.7188-2.88920.21313120.16445627593997
2.8892-3.11230.20693180.16645621593997
3.1123-3.42550.19982910.15645624591598
3.4255-3.92110.17282970.14865659595698
3.9211-4.940.15422960.13955656595298
4.94-68.97150.22282690.17135774604399
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)
11.24530.37160.61392.33730.73842.17240.0256-0.1903-0.18050.1304-0.01190.05910.1779-0.0231-0.00010.116-0.03850.02220.17360.04030.1399-10.6683-14.8036-0.6761
22.15990.04240.32620.94120.10810.97850.027-0.0344-0.047-0.04680.00780.02030.03340.0076-0.03480.0919-0.01250.00560.0657-00.0667-0.3092-4.8861-8.085
32.5004-0.8528-0.4442.18740.05491.5814-0.0860.02410.4586-0.22280.04710.0572-0.40810.086-0.00750.1863-0.0070.01020.09060.01730.1691-3.87048.4871-10.8448
43.4678-1.57021.63384.3447-2.28714.53750.007-0.15090.2541-0.06430.03950.1671-0.2266-0.1555-0.04220.1030.00540.02220.0734-0.040.1401-8.37998.5221-3.8914
51.5414-0.1314-2.04172.21570.54673.48240.0349-0.66860.01840.1662-0.0068-0.08560.07060.5382-0.04440.1691-0.0164-0.04410.3107-0.01150.129112.892-1.24758.9241
61.9162-0.34340.68941.87240.00452.2091-0.0952-0.18360.50160.2178-0.033-0.1667-0.30290.29860.09620.2283-0.0405-0.01190.2215-0.04020.15998.54989.38417.589
77.5605-1.35715.25390.5844-0.81083.6328-0.08-0.5320.31530.140.0179-0.0887-0.1196-0.18540.05410.33280.02990.03870.4358-0.09950.19888.73415.105821.4392
81.6789-0.5260.16162.621-1.1013.40530.0330.0114-0.2573-0.1605-0.1552-0.11050.42360.28980.10160.20850.06990.00820.1473-0.03850.207626.4336-18.3787-38.6036
95.8779-3.17832.98783.6494-1.9913.40210.1508-0.0968-0.50970.10040.080.15510.3299-0.0034-0.22390.184-0.0035-0.01190.0715-0.00440.150415.5038-14.5979-32.0178
103.0606-0.0324-0.37011.54350.14222.06670.0582-0.10530.03740.0264-0.008-0.0011-0.05310.0095-0.05420.13630.0163-0.00080.04620.00380.073517.6699-3.0471-32.801
112.3532-0.11360.93551.7897-0.22313.30540.0476-0.2425-0.16670.18510.0137-0.1220.09750.2443-0.04440.1470.01390.01360.1420.00910.108625.6502-4.6136-22.6761
123.43030.79680.48232.57140.18661.4781-0.02650.01220.2632-0.12340.099-0.1608-0.35630.0612-0.06110.1881-0.00180.02570.08480.01510.119124.71688.2966-39.2688
139.0203-1.4636-4.75521.56420.20523.25940.08660.6073-0.2201-0.0836-0.20270.10490.0932-0.42240.12260.21030.0218-0.05860.2545-0.03640.13952.0664-3.8067-45.9222
143.21830.66860.27470.86440.25540.99470.02020.54040.4661-0.17820.0170.1392-0.2186-0.2415-0.03610.24780.0473-0.00460.23140.07150.17558.74576.1666-48.2137
158.43441.53335.31690.57811.00383.278-0.17230.2512-0.1577-0.14960.14770.0128-0.21750.01860.05270.31130.02850.03790.38640.04870.14546.7675-0.7593-60.513
161.3114-0.0689-0.24471.6291-0.41292.51050.07560.155-0.3299-0.1657-0.1453-0.34740.32170.56760.06010.19270.07690.02590.2439-0.02780.275953.3946-45.6957-37.6332
176.23781.8379-0.02916.4524-0.62471.60620.06490.0320.0808-0.0621-0.0271-0.7385-0.28650.77120.02570.1752-0.08940.01440.3299-0.03130.219156.4049-33.8399-32.299
186.0408-1.88570.3081.2757-1.06671.86360.0012-0.034-0.09440.07560.08370.0495-0.0868-0.1613-0.08830.1321-0.023-0.00520.0904-0.00930.120233.6636-39.0767-26.8505
194.3985-1.87512.06012.6912-0.99784.3978-0.1-0.4378-0.02490.21010.1321-0.1979-0.09970.2328-0.01190.1251-0.02310.00990.2033-0.03460.152251.727-38.275-21.1396
201.8160.62220.36482.40270.32731.11470.2828-0.0020.38760.02540.0189-0.2982-0.82120.0306-0.1390.3996-0.04760.1070.1497-0.04260.251647.7789-24.4453-36.334
217.02171.2137-2.35352.3408-1.25023.1888-0.01270.6083-0.3584-0.2125-0.0610.20750.2799-0.7850.1090.2221-0.0226-0.06960.3252-0.08270.187330.6798-41.373-46.681
223.13940.66810.19952.09870.12493.26290.28480.30110.2166-0.1441-0.17930.2032-0.2641-0.5731-0.11190.30820.09240.02390.2815-0.02830.146533.2039-30.2243-46.7331
236.12313.32455.42972.21932.57564.9807-0.09920.20860.0735-0.29930.04430.0388-0.2441-0.01810.03330.33060.05390.04410.3744-0.01660.162534.0753-35.6956-60.1193
243.0044-0.3425-1.20192.0824-0.77121.5238-0.1668-0.5719-0.47770.34420.1330.49760.3356-0.35330.03540.2736-0.08810.06360.51460.13940.303915.2825-41.476711.7941
251.15190.11250.37241.35960.6741.29960.14-0.3346-0.42430.071-0.12570.30630.2197-0.3563-0.00330.1802-0.06690.00160.24170.08030.281819.0271-42.93840.1602
262.57220.0070.23980.90670.15751.01710.0581-0.0143-0.2158-0.057-0.01530.09790.0254-0.0856-0.03440.108-0.0088-0.01370.09530.02540.129227.7189-37.032-8.79
275.72033.335.29523.34533.09595.0366-0.18130.3532-0.0067-0.260.14780.286-0.2853-0.00120.03920.16910.01440.010.21640.03140.19921.0798-33.2915-14.4363
289.0226-6.28920.35426.36540.21250.79890.0444-0.00130.5102-0.0543-0.0056-0.3718-0.07-0.024-0.05090.14460.00230.01390.20230.01850.165128.1845-17.5548-3.4622
293.0168-2.01652.11424.4015-3.10454.53020.085-0.1695-0.0084-0.14220.00690.13090.0865-0.0484-0.0540.0608-0.01010.01470.14160.00590.100720.7441-24.1451-1.8428
306.8992-1.298-2.53572.57850.88433.5199-0.0333-0.5653-0.32130.19360.04280.02620.26510.15320.02770.16910.0048-0.04240.23810.06560.141440.6091-36.258910.801
313.8475-1.73681.19391.79760.06881.73570.0026-0.42960.1140.06770.1092-0.1339-0.05690.1283-0.11370.1553-0.01220.010.22460.02820.109837.8102-25.08978.5766
325.498-2.05264.83421.1557-1.52724.3635-0.1617-0.38110.02190.20340.14130.0019-0.1578-0.15370.00740.22770.03790.03450.40670.00250.145837.053-28.18422.5343
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 576 through 635 )A576 - 635
2X-RAY DIFFRACTION2chain 'A' and (resid 636 through 750 )A636 - 750
3X-RAY DIFFRACTION3chain 'A' and (resid 751 through 786 )A751 - 786
4X-RAY DIFFRACTION4chain 'A' and (resid 787 through 815 )A787 - 815
5X-RAY DIFFRACTION5chain 'A' and (resid 816 through 839 )A816 - 839
6X-RAY DIFFRACTION6chain 'A' and (resid 840 through 878 )A840 - 878
7X-RAY DIFFRACTION7chain 'A' and (resid 879 through 917 )A879 - 917
8X-RAY DIFFRACTION8chain 'B' and (resid 578 through 635 )B578 - 635
9X-RAY DIFFRACTION9chain 'B' and (resid 636 through 657 )B636 - 657
10X-RAY DIFFRACTION10chain 'B' and (resid 658 through 738 )B658 - 738
11X-RAY DIFFRACTION11chain 'B' and (resid 739 through 768 )B739 - 768
12X-RAY DIFFRACTION12chain 'B' and (resid 769 through 815 )B769 - 815
13X-RAY DIFFRACTION13chain 'B' and (resid 816 through 840 )B816 - 840
14X-RAY DIFFRACTION14chain 'B' and (resid 841 through 878 )B841 - 878
15X-RAY DIFFRACTION15chain 'B' and (resid 879 through 916 )B879 - 916
16X-RAY DIFFRACTION16chain 'C' and (resid 589 through 675 )C589 - 675
17X-RAY DIFFRACTION17chain 'C' and (resid 676 through 695 )C676 - 695
18X-RAY DIFFRACTION18chain 'C' and (resid 696 through 738 )C696 - 738
19X-RAY DIFFRACTION19chain 'C' and (resid 739 through 768 )C739 - 768
20X-RAY DIFFRACTION20chain 'C' and (resid 769 through 815 )C769 - 815
21X-RAY DIFFRACTION21chain 'C' and (resid 816 through 839 )C816 - 839
22X-RAY DIFFRACTION22chain 'C' and (resid 840 through 878 )C840 - 878
23X-RAY DIFFRACTION23chain 'C' and (resid 879 through 916 )C879 - 916
24X-RAY DIFFRACTION24chain 'D' and (resid 590 through 611 )D590 - 611
25X-RAY DIFFRACTION25chain 'D' and (resid 612 through 674 )D612 - 674
26X-RAY DIFFRACTION26chain 'D' and (resid 675 through 750 )D675 - 750
27X-RAY DIFFRACTION27chain 'D' and (resid 751 through 768 )D751 - 768
28X-RAY DIFFRACTION28chain 'D' and (resid 769 through 786 )D769 - 786
29X-RAY DIFFRACTION29chain 'D' and (resid 787 through 815 )D787 - 815
30X-RAY DIFFRACTION30chain 'D' and (resid 816 through 839 )D816 - 839
31X-RAY DIFFRACTION31chain 'D' and (resid 840 through 878 )D840 - 878
32X-RAY DIFFRACTION32chain 'D' and (resid 879 through 916 )D879 - 916

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