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- PDB-7sza: Crystal Structure Analysis of human PRPK complex with a compound -

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Basic information

Entry
Database: PDB / ID: 7sza
TitleCrystal Structure Analysis of human PRPK complex with a compound
Components
  • EKC/KEOPS complex subunit TP53RK
  • EKC/KEOPS complex subunit TPRKB
KeywordsTRANSFERASE / protein kinase / p53 / immunomodulatory drugs / IMiDs
Function / homology
Function and homology information


tRNA threonylcarbamoyladenosine metabolic process / EKC/KEOPS complex / tRNA threonylcarbamoyladenosine modification / Hydrolases; Acting on acid anhydrides / tRNA modification in the nucleus and cytosol / tRNA processing / regulation of signal transduction by p53 class mediator / p53 binding / Regulation of TP53 Activity through Phosphorylation / hydrolase activity ...tRNA threonylcarbamoyladenosine metabolic process / EKC/KEOPS complex / tRNA threonylcarbamoyladenosine modification / Hydrolases; Acting on acid anhydrides / tRNA modification in the nucleus and cytosol / tRNA processing / regulation of signal transduction by p53 class mediator / p53 binding / Regulation of TP53 Activity through Phosphorylation / hydrolase activity / non-specific serine/threonine protein kinase / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein kinase binding / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Lipopolysaccharide kinase (Kdo/WaaP) family / Serine/threonine-protein kinase Bud32 / CGI121/TPRKB / CGI121/TPRKB superfamily / Kinase binding protein CGI-121 / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Chem-DUI / CITRATE ANION / EKC/KEOPS complex subunit TP53RK / EKC/KEOPS complex subunit TPRKB
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsSeo, H.-S. / Dhe-Paganon, S.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Biorxiv / Year: 2021
Title: Development of PRPK Directed Phthalimides
Authors: Seo, H.-S. / Mizutani, T. / Hideshima, T. / Vangos, N.E. / Zhang, T. / Anderson, K.C. / Gray, N.S. / Dhe-Paganon, S.
History
DepositionNov 27, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.2Feb 7, 2024Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: EKC/KEOPS complex subunit TP53RK
B: EKC/KEOPS complex subunit TPRKB
C: EKC/KEOPS complex subunit TP53RK
D: EKC/KEOPS complex subunit TPRKB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,5948
Polymers96,6704
Non-polymers9254
Water11,530640
1
A: EKC/KEOPS complex subunit TP53RK
B: EKC/KEOPS complex subunit TPRKB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,7974
Polymers48,3352
Non-polymers4622
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3190 Å2
ΔGint-17 kcal/mol
Surface area18860 Å2
MethodPISA
2
C: EKC/KEOPS complex subunit TP53RK
D: EKC/KEOPS complex subunit TPRKB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,7974
Polymers48,3352
Non-polymers4622
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3100 Å2
ΔGint-16 kcal/mol
Surface area18090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)297.510, 47.490, 62.270
Angle α, β, γ (deg.)90.000, 96.530, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid 18 through 21 and (name N...
21(chain C and (resid 18 through 130 or (resid 131...
12(chain B and ((resid 0 and (name N or name...
22(chain D and (resid 0 through 1 or resid 3...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and ((resid 18 through 21 and (name N...A18 - 21
121(chain A and ((resid 18 through 21 and (name N...A14 - 503
131(chain A and ((resid 18 through 21 and (name N...A14 - 503
211(chain C and (resid 18 through 130 or (resid 131...C18 - 130
221(chain C and (resid 18 through 130 or (resid 131...C131
231(chain C and (resid 18 through 130 or (resid 131...C18 - 504
241(chain C and (resid 18 through 130 or (resid 131...C18 - 504
251(chain C and (resid 18 through 130 or (resid 131...C18 - 504
261(chain C and (resid 18 through 130 or (resid 131...C18 - 504
112(chain B and ((resid 0 and (name N or name...B0
122(chain B and ((resid 0 and (name N or name...B-1 - 175
132(chain B and ((resid 0 and (name N or name...B-1 - 175
142(chain B and ((resid 0 and (name N or name...B-1 - 175
152(chain B and ((resid 0 and (name N or name...B-1 - 175
212(chain D and (resid 0 through 1 or resid 3...D0 - 1
222(chain D and (resid 0 through 1 or resid 3...D3 - 72
232(chain D and (resid 0 through 1 or resid 3...D0 - 175
242(chain D and (resid 0 through 1 or resid 3...D0 - 175
252(chain D and (resid 0 through 1 or resid 3...D0 - 175
262(chain D and (resid 0 through 1 or resid 3...D0 - 175
272(chain D and (resid 0 through 1 or resid 3...D0 - 175
282(chain D and (resid 0 through 1 or resid 3...D0 - 175

NCS ensembles :
ID
1
2

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Components

#1: Protein EKC/KEOPS complex subunit TP53RK / Atypical serine/threonine protein kinase TP53RK / Nori-2 / TP53-regulating kinase / p53-related protein kinase


Mass: 28358.646 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TP53RK, C20orf64, PRPK / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q96S44, Hydrolases; Acting on acid anhydrides, non-specific serine/threonine protein kinase
#2: Protein EKC/KEOPS complex subunit TPRKB / PRPK-binding protein / TP53RK-binding protein


Mass: 19976.223 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TPRKB, CGI-121, My019 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9Y3C4
#3: Chemical ChemComp-DUI / 4-amino-2-[(3R)-2,6-dioxopiperidin-3-yl]-1H-isoindole-1,3(2H)-dione


Mass: 273.244 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H11N3O4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-FLC / CITRATE ANION / Citric acid


Mass: 189.100 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H5O7
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 640 / Source method: isolated from a natural source / Formula: H2O
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: 2.26 Å3/Da / Density % sol: 45.59 %
Crystal growTemperature: 300 K / Method: vapor diffusion, hanging drop / pH: 5.2
Details: 100mM Sodium citrate pH 5.2, 12.8% PEG8000, 10mM MgCl2, 10mM TCEP

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 20, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.9→73.9509 Å / Num. obs: 68512 / % possible obs: 99.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 25.022 Å2 / Rpim(I) all: 0.037 / Rrim(I) all: 0.071 / Net I/σ(I): 13.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
1.9-1.933.71.61231833580.4840.93399.9
5.16-73.953.539.91264535710.0120.02399.4

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.16_3549refinement
PDB_EXTRACT3.25data extraction
xia2data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3ENP, 4WW5

3enp

4ww5


Resolution: 1.9→73.9509 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 22.7 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2163 3389 4.95 %
Rwork0.1728 65113 -
obs0.175 68502 99.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 106.88 Å2 / Biso mean: 36.4617 Å2 / Biso min: 15.47 Å2
Refinement stepCycle: final / Resolution: 1.9→73.9509 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6244 0 66 640 6950
Biso mean--27.41 41.76 -
Num. residues----811
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0086423
X-RAY DIFFRACTIONf_angle_d1.1848694
X-RAY DIFFRACTIONf_dihedral_angle_d7.6854599
X-RAY DIFFRACTIONf_chiral_restr0.0831028
X-RAY DIFFRACTIONf_plane_restr0.0061110
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1402X-RAY DIFFRACTION6.373TORSIONAL
12C1402X-RAY DIFFRACTION6.373TORSIONAL
21B1020X-RAY DIFFRACTION6.373TORSIONAL
22D1020X-RAY DIFFRACTION6.373TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 24

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9-1.92720.38831430.322226472790100
1.9272-1.95590.38121360.319127462882100
1.9559-1.98650.31121340.277426672801100
1.9865-2.01910.28271550.234526832838100
2.0191-2.05390.2431490.212826882837100
2.0539-2.09120.26281280.20326852813100
2.0912-2.13150.2491360.196326742810100
2.1315-2.1750.21951450.188227372882100
2.175-2.22230.2141320.192327032835100
2.2223-2.2740.27461340.21312680281499
2.274-2.33080.27081450.190326812826100
2.3308-2.39390.26941520.185527382890100
2.3939-2.46430.24071220.178727102832100
2.4643-2.54380.2461510.172726702821100
2.5438-2.63480.19351350.171727672902100
2.6348-2.74030.20621210.172726912812100
2.7403-2.8650.22691410.175727182859100
2.865-3.0160.24881630.180527142877100
3.016-3.2050.22291300.171327082838100
3.205-3.45250.20121490.16927332882100
3.4525-3.79990.20331450.14962710285599
3.7999-4.34970.17191460.135127692915100
4.3497-5.47990.1661370.14132741287899
5.4799-73.95090.18381600.1612853301399
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)
12.6191-0.0514-0.45940.4628-0.67911.1492-0.0949-0.1454-0.51460.01310.01090.4013-0.34840.07190.00060.3044-0.01670.02880.38050.00460.3054-75.0843-1.035536.4892
20.73510.10810.28080.6716-1.38391.22980.07890.0016-0.0733-0.08250.07170.1737-0.0244-0.3013-0.00060.22550.0138-0.00150.2619-0.01230.2361-62.9649-12.156132.3036
31.5439-0.7777-0.22530.80480.41850.7961-0.0862-0.15040.21880.14130.110.0033-0.19070.06150.00030.23670.0211-0.00730.225-0.01640.2556-54.4468-1.172334.8553
41.4445-0.9288-0.05480.6799-0.07020.86040.10230.22780.0172-0.0358-0.02190.00410.0936-0.1155-00.2160.00720.01860.2640.00630.2066-57.7608-6.48724.955
53.27060.2322-0.15130.91490.13732.875-0.09850.1969-0.3202-0.44120.0545-0.0240.4510.15950.00020.32990.04740.02640.2947-0.01790.2254-39.5219-20.551122.7832
60.4495-0.56170.36491.04330.20571.09480.04770.06260.116-0.148-0.1053-0.15410.04760.1285-0.00040.21530.00420.02890.2293-0.03310.2239-45.0113-11.074728.4564
71.0888-0.10750.16360.2587-0.79911.60870.07170.23410.1029-0.1082-0.0018-0.08440.31420.0986-0.00010.22290.03350.02680.24-0.00870.1932-45.6909-10.334725.1597
80.65880.1175-0.22170.9113-0.28220.2438-0.0268-0.2225-0.08370.61620.1119-0.26870.25380.03890.00230.26870.0218-0.02960.2812-0.00710.3082-37.3002-14.383936.0211
92.5906-0.5381-0.49550.52250.71941.8128-0.1065-0.0161-0.0749-0.12450.1302-0.22410.10650.40590.00010.2330.06510.03870.37090.00510.2652-31.794-16.188626.8168
100.49440.21420.39930.31150.23120.23690.0792-0.0761-0.25190.62290.01-0.3104-0.36430.388-0.00050.3390.048-0.07960.4027-0.07950.4396-29.1319-10.857238.9793
110.81270.3199-0.26561.43940.57940.68630.1563-0.0286-0.2259-0.32140.12620.13950.3015-0.6773-0.00060.33170.0197-0.03880.37150.03910.3919-77.05160.077113.8
121.8436-0.37970.93972.7529-0.68371.29180.00370.01240.0489-0.1189-0.1365-0.1472-0.2210.11250.00050.26930.01030.0410.23960.02220.1812-74.300816.68458.2039
130.8672-0.89270.59530.9174-0.83321.2746-0.0339-0.03770.03810.12080.051-0.0512-0.130.0777-00.208-0.00040.02250.22910.02410.2238-69.185910.697719.6988
140.1491-0.145-0.12030.15870.22840.3036-0.09350.15090.3798-0.24160.225-0.3169-0.55480.347-0.00170.3041-0.0629-0.04460.31020.03960.3784-59.561217.524119.5083
151.7284-1.67480.45281.96140.36941.25750.4111-0.08740.3090.0939-0.26610.0528-0.70710.1838-0.00110.3218-0.01330.05540.29450.04390.2626-72.169214.066610.5733
160.8789-0.35170.17190.70050.12660.3010.08450.0141-0.07080.50870.41450.59770.123-0.3886-0.00040.30270.02230.0560.36830.06050.2901-84.725512.203311.0036
170.79360.45980.36660.7680.5060.50490.01770.701-0.0561-0.4905-0.1412-0.194-0.22620.4734-0.00120.42120.04050.04980.41560.01270.2677-68.56819.40210.5636
180.62670.16460.40230.7324-0.12920.384-0.27810.2318-0.02770.4882-0.0574-0.4157-0.85981.0485-0.050.3958-0.04010.05750.43920.06110.4448-51.955110.857910.6906
194.5255-0.90532.52683.3384-0.59431.86320.4091.25431.1086-0.5906-0.8582-0.976-0.6541.3054-0.42650.29470.08710.24560.71980.16630.4058-46.7039-0.197413.3453
200.48180.2346-0.21620.7626-0.58330.4106-0.00880.08580.3389-0.0376-0.1431-0.12660.06160.1197-0.00030.22440.00530.03030.28290.04540.2766-56.16014.470621.1046
213.6460.92351.14082.3853-1.62942.27840.82151.8873-1.6666-0.4571-1.1244-0.22980.050.9293-0.39260.45110.2888-0.04040.7283-0.18690.5041-11.817410.1576-16.5142
220.8788-0.23560.02640.44360.65270.84020.45160.3941-0.3834-0.7886-0.41490.68860.66050.4854-0.01170.41930.0691-0.09920.281-0.09640.3406-28.338410.6835-16.8164
231.644-1.06750.7831.39610.32951.47440.20870.3555-0.2696-0.5972-0.6311-0.62120.12860.7506-0.01350.33050.08150.01230.3497-0.0050.2692-22.565616.1428-17.1691
242.032-0.94020.93830.8793-0.59181.36630.18040.13220.33890.2643-0.0496-0.1273-0.24490.25810.00550.28070.0334-0.02890.2519-0.01790.2795-23.391923.839-7.4551
251.9119-1.33190.9561.4918-0.48391.32640.1067-0.1261-0.2999-0.1357-0.00510.25750.25180.0168-0.01470.23290.0178-0.04950.1859-0.0430.3105-27.641612.9493-7.0621
260.032-0.03680.09770.7194-0.66720.70740.12920.716-1.1565-1.2453-0.33211.1330.4177-0.8576-0.07290.5072-0.022-0.19640.4295-0.11350.7753-53.065215.1651-15.1139
272.0505-0.91910.44011.87430.2850.915-0.0341-0.3592-0.29530.29850.07670.1740.0516-0.10200.2490.020.01520.25140.01080.2495-41.665624.6996-3.9468
281.9687-1.38850.10831.2699-0.90091.7127-0.0844-0.1768-0.48780.0180.16360.31850.2847-0.02770.02430.21120.0006-00.18480.01030.3031-38.439119.564-5.673
290.7133-0.7108-0.11570.7308-0.15320.71730.15640.2514-0.0582-0.0811-0.06570.13620.09590.166400.26840.0617-0.02570.262-0.03510.232-42.518532.073-12.0566
301.4502-0.6613-0.84850.73230.37720.4175-0.09440.1608-0.1825-0.05180.11840.46060.1733-0.1464-0.00040.3477-0.0072-0.01550.39080.0550.3505-51.77827.7426-7.7348
310.7037-0.32060.08390.68440.50760.5365-0.10660.00370.22320.2658-0.0960.1232-0.4150.1386-0.00080.32450.0283-0.03340.3049-0.05850.3052-44.273539.6532-6.4825
322.5164-0.43860.0182.052-0.17741.30740.022-0.4411-0.55090.075-0.0221-0.05980.27520.0657-0.00160.42960.0662-0.03820.37840.08250.5055-11.1091-3.20126.9748
331.9723-0.7732-0.80721.6071-0.55031.6997-0.0613-0.4094-0.15830.3165-0.0365-0.2148-0.01560.3339-0.00040.28360.0327-0.05960.30370.01290.3073-11.11487.0814.2592
341.25930.255-0.48790.10750.06240.6172-0.1442-0.87230.11670.79440.1032-0.2121-0.34790.48860.00640.58050.0534-0.10730.46-0.06990.3886-12.873815.864212.5332
352.37240.590.77291.30250.33530.49260.0797-0.3584-0.62770.3354-0.0817-0.5072-0.02350.2214-0.00290.53130.0525-0.01350.47630.12950.6048-7.0846-3.47939.1237
363.0754-0.7170.28011.6759-0.86311.7845-0.1361-0.6127-0.2860.72230.24580.4273-0.1512-0.20650.00060.47190.04240.07310.41270.04980.3204-24.38397.417110.8365
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 14 through 34 )A14 - 34
2X-RAY DIFFRACTION2chain 'A' and (resid 35 through 69 )A35 - 69
3X-RAY DIFFRACTION3chain 'A' and (resid 70 through 93 )A70 - 93
4X-RAY DIFFRACTION4chain 'A' and (resid 94 through 121 )A94 - 121
5X-RAY DIFFRACTION5chain 'A' and (resid 122 through 155 )A122 - 155
6X-RAY DIFFRACTION6chain 'A' and (resid 156 through 171 )A156 - 171
7X-RAY DIFFRACTION7chain 'A' and (resid 172 through 192 )A172 - 192
8X-RAY DIFFRACTION8chain 'A' and (resid 193 through 210 )A193 - 210
9X-RAY DIFFRACTION9chain 'A' and (resid 211 through 231 )A211 - 231
10X-RAY DIFFRACTION10chain 'A' and (resid 232 through 246 )A232 - 246
11X-RAY DIFFRACTION11chain 'B' and (resid -1 through 12 )B-1 - 12
12X-RAY DIFFRACTION12chain 'B' and (resid 13 through 34 )B13 - 34
13X-RAY DIFFRACTION13chain 'B' and (resid 35 through 83 )B35 - 83
14X-RAY DIFFRACTION14chain 'B' and (resid 84 through 96 )B84 - 96
15X-RAY DIFFRACTION15chain 'B' and (resid 97 through 112 )B97 - 112
16X-RAY DIFFRACTION16chain 'B' and (resid 113 through 125 )B113 - 125
17X-RAY DIFFRACTION17chain 'B' and (resid 126 through 141 )B126 - 141
18X-RAY DIFFRACTION18chain 'B' and (resid 142 through 152 )B142 - 152
19X-RAY DIFFRACTION19chain 'B' and (resid 153 through 160 )B153 - 160
20X-RAY DIFFRACTION20chain 'B' and (resid 161 through 175 )B161 - 175
21X-RAY DIFFRACTION21chain 'C' and (resid 18 through 35 )C18 - 35
22X-RAY DIFFRACTION22chain 'C' and (resid 36 through 52 )C36 - 52
23X-RAY DIFFRACTION23chain 'C' and (resid 53 through 69 )C53 - 69
24X-RAY DIFFRACTION24chain 'C' and (resid 70 through 94 )C70 - 94
25X-RAY DIFFRACTION25chain 'C' and (resid 95 through 121 )C95 - 121
26X-RAY DIFFRACTION26chain 'C' and (resid 122 through 139 )C122 - 139
27X-RAY DIFFRACTION27chain 'C' and (resid 140 through 167 )C140 - 167
28X-RAY DIFFRACTION28chain 'C' and (resid 168 through 192 )C168 - 192
29X-RAY DIFFRACTION29chain 'C' and (resid 193 through 210 )C193 - 210
30X-RAY DIFFRACTION30chain 'C' and (resid 211 through 228 )C211 - 228
31X-RAY DIFFRACTION31chain 'C' and (resid 229 through 245 )C229 - 245
32X-RAY DIFFRACTION32chain 'D' and (resid 0 through 35 )D0 - 35
33X-RAY DIFFRACTION33chain 'D' and (resid 36 through 83 )D36 - 83
34X-RAY DIFFRACTION34chain 'D' and (resid 84 through 95 )D84 - 95
35X-RAY DIFFRACTION35chain 'D' and (resid 96 through 125 )D96 - 125
36X-RAY DIFFRACTION36chain 'D' and (resid 126 through 175 )D126 - 175

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