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- PDB-4x4p: Crystal structure of the A.fulgidus CCA-adding enzyme in complex ... -

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Basic information

Entry
Database: PDB / ID: 4x4p
TitleCrystal structure of the A.fulgidus CCA-adding enzyme in complex with a G70A arginyl-tRNA minihelix ending in CCAC
Components
  • CCA-adding enzyme
  • G70A tRNA minihelix ending in CCAC
KeywordsRNA BINDING PROTEIN / protein-RNA complex / tRNA / non-coding RNA / CCA-adding enzyme / nucleotidyltransferase / ncRNA
Function / homology
Function and homology information


CCA tRNA nucleotidyltransferase / tRNA surveillance / CCACCA tRNA nucleotidyltransferase activity / CCA tRNA nucleotidyltransferase activity / tRNA 3'-terminal CCA addition / RNA repair / tRNA binding / magnesium ion binding / ATP binding
Similarity search - Function
CCA tRNA nucleotidyltransferase, domain 2 / Archaeal tRNA CCA-adding enzyme catalytic domain / tRNA nucleotidyltransferase, archaea / tRNA nucleotidyltransferase, substrate binding / tRNA nucleotidyltransferase, domain 2 / : / tRNA nucleotidyltransferase, second domain / CCA-adding enzyme, C-terminal domain / Poly(A) polymerase predicted RNA binding domain / Nucleotidyltransferase, class I-like, C-terminal ...CCA tRNA nucleotidyltransferase, domain 2 / Archaeal tRNA CCA-adding enzyme catalytic domain / tRNA nucleotidyltransferase, archaea / tRNA nucleotidyltransferase, substrate binding / tRNA nucleotidyltransferase, domain 2 / : / tRNA nucleotidyltransferase, second domain / CCA-adding enzyme, C-terminal domain / Poly(A) polymerase predicted RNA binding domain / Nucleotidyltransferase, class I-like, C-terminal / 2-5OAS/ClassI-CCAase, nucleotidyltransferase domain / Polymerase, nucleotidyl transferase domain / Poly(a)-polymerase, middle domain / Nucleotidyltransferase domain / Beta Polymerase, domain 2 / Beta Polymerase; domain 2 / Nucleotidyltransferase superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
RNA / RNA (> 10) / CCA-adding enzyme
Similarity search - Component
Biological speciesArchaeoglobus fulgidus (archaea)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / molecular replacement / Resolution: 3 Å
AuthorsKuhn, C.-D. / Joshua-Tor, L.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Cell / Year: 2015
Title: On-Enzyme Refolding Permits Small RNA and tRNA Surveillance by the CCA-Adding Enzyme.
Authors: Kuhn, C.D. / Wilusz, J.E. / Zheng, Y. / Beal, P.A. / Joshua-Tor, L.
History
DepositionDec 3, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 11, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Feb 25, 2015Group: Database references
Revision 1.3Nov 22, 2017Group: Derived calculations / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_entity_src_syn ...entity_src_gen / pdbx_entity_src_syn / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_entity_src_syn.pdbx_alt_source_flag ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Nov 20, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Dec 27, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CCA-adding enzyme
B: G70A tRNA minihelix ending in CCAC
C: CCA-adding enzyme
D: G70A tRNA minihelix ending in CCAC
E: CCA-adding enzyme
F: G70A tRNA minihelix ending in CCAC
G: CCA-adding enzyme
H: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)261,90218
Polymers260,9428
Non-polymers96110
Water00
1
A: CCA-adding enzyme
B: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,7167
Polymers65,2352
Non-polymers4805
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3950 Å2
ΔGint-93 kcal/mol
Surface area28070 Å2
MethodPISA
2
C: CCA-adding enzyme
D: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,3313
Polymers65,2352
Non-polymers961
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2490 Å2
ΔGint-36 kcal/mol
Surface area27440 Å2
MethodPISA
3
E: CCA-adding enzyme
F: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,4284
Polymers65,2352
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2660 Å2
ΔGint-47 kcal/mol
Surface area26970 Å2
MethodPISA
4
G: CCA-adding enzyme
H: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,4284
Polymers65,2352
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2700 Å2
ΔGint-42 kcal/mol
Surface area27120 Å2
MethodPISA
5
A: CCA-adding enzyme
B: G70A tRNA minihelix ending in CCAC
C: CCA-adding enzyme
D: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,04710
Polymers130,4714
Non-polymers5766
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11290 Å2
ΔGint-142 kcal/mol
Surface area50670 Å2
MethodPISA
6
E: CCA-adding enzyme
F: G70A tRNA minihelix ending in CCAC
G: CCA-adding enzyme
H: G70A tRNA minihelix ending in CCAC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)130,8558
Polymers130,4714
Non-polymers3844
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10160 Å2
ΔGint-103 kcal/mol
Surface area49280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.108, 58.112, 217.806
Angle α, β, γ (deg.)85.200, 87.980, 89.810
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A and (resseq 3:89 or resseq 97:121 or resseq 123:437 )
21chain C and (resseq 3:89 or resseq 97:121 or resseq 123:437 )
31chain E and (resseq 3:89 or resseq 97:121 or resseq 123:437 )
41chain G and (resseq 3:89 or resseq 97:121 or resseq 123:437 )

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain A and (resseq 3:89 or resseq 97:121 or resseq 123:437 )A3 - 89
121chain A and (resseq 3:89 or resseq 97:121 or resseq 123:437 )A97 - 121
131chain A and (resseq 3:89 or resseq 97:121 or resseq 123:437 )A123 - 437
211chain C and (resseq 3:89 or resseq 97:121 or resseq 123:437 )C3 - 89
221chain C and (resseq 3:89 or resseq 97:121 or resseq 123:437 )C97 - 121
231chain C and (resseq 3:89 or resseq 97:121 or resseq 123:437 )C123 - 437
311chain E and (resseq 3:89 or resseq 97:121 or resseq 123:437 )E3 - 89
321chain E and (resseq 3:89 or resseq 97:121 or resseq 123:437 )E97 - 121
331chain E and (resseq 3:89 or resseq 97:121 or resseq 123:437 )E123 - 437
411chain G and (resseq 3:89 or resseq 97:121 or resseq 123:437 )G3 - 89
421chain G and (resseq 3:89 or resseq 97:121 or resseq 123:437 )G97 - 121
431chain G and (resseq 3:89 or resseq 97:121 or resseq 123:437 )G123 - 437

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Components

#1: Protein
CCA-adding enzyme / CCA tRNA nucleotidyltransferase / tRNA CCA-pyrophosphorylase / tRNA adenylyl-/cytidylyl- ...CCA tRNA nucleotidyltransferase / tRNA CCA-pyrophosphorylase / tRNA adenylyl-/cytidylyl- transferase / tRNA nucleotidyltransferase / tRNA-NT


Mass: 53672.484 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) (archaea)
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126
Gene: cca, AF_2156 / Plasmid: pET22 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIPL
References: UniProt: O28126, CCA tRNA nucleotidyltransferase
#2: RNA chain
G70A tRNA minihelix ending in CCAC


Mass: 11562.915 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: SO4

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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: 2.91 Å3/Da / Density % sol: 57.66 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.3
Details: 30% 2-Propanol, 0.1M Sodium Acetate pH 5.3, 0.2M Lithium Sulfate, 4.8% PEG 1.5K
PH range: 5.3

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 4, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
Reflection twinOperator: -k,-h,-l / Fraction: 0.13
ReflectionResolution: 3→29.576 Å / Num. obs: 53506 / % possible obs: 94.1 % / Redundancy: 2 % / Rpim(I) all: 0.073 / Rrim(I) all: 0.109 / Rsym value: 0.081 / Net I/av σ(I): 8.767 / Net I/σ(I): 9.1 / Num. measured all: 107845
Reflection shell

Diffraction-ID: 1 / Redundancy: 2 % / Rejects: _

Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRpim(I) allRsym valueNet I/σ(I) obs% possible all
3-3.160.3482.21646280900.3170.3482.596.4
3.16-3.350.2263.31504674520.2070.2263.996
3.35-3.590.1534.91434370190.1380.1535.994.3
3.59-3.870.1047.11297464530.0950.1048.393.6
3.87-4.240.0789.51151057490.0710.07810.492.3
4.24-4.740.05712.91050052320.0510.05713.691.3
4.74-5.480.05313.5946147270.0480.0531493.2
5.48-6.710.05613.2814140010.050.05612.894.6
6.71-9.490.03618.2615331370.0330.03617.494.6
9.49-29.5760.02622.9325516460.0230.0262391.8

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
SCALA3.3.20data scaling
PDB_EXTRACT3.14data extraction
XDSdata reduction
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
RefinementResolution: 3→29.576 Å / Cross valid method: FREE R-VALUE / σ(F): 0.96 / Phase error: 33.84 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflection
Rfree0.2738 4210 4.33 %
Rwork0.2235 93504 -
obs0.2257 -85.56 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 252.67 Å2 / Biso mean: 69.3324 Å2 / Biso min: 22.02 Å2
Refinement stepCycle: final / Resolution: 3→29.576 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14332 2609 50 0 16991
Biso mean--62.05 --
Num. residues----1849
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717601
X-RAY DIFFRACTIONf_angle_d1.09324273
X-RAY DIFFRACTIONf_chiral_restr0.0442658
X-RAY DIFFRACTIONf_plane_restr0.0062681
X-RAY DIFFRACTIONf_dihedral_angle_d13.5487085
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A8601X-RAY DIFFRACTION7.68TORSIONAL
12C8601X-RAY DIFFRACTION7.68TORSIONAL
13E8601X-RAY DIFFRACTION7.68TORSIONAL
14G8601X-RAY DIFFRACTION7.68TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3-3.05170.36532000.30364741494181
3.0517-3.10710.41540.29894803495787
3.1071-3.16680.35852060.29384811501784
3.1668-3.23130.31461900.27834903509385
3.2313-3.30140.31861740.27494371454580
3.3014-3.37810.32611890.26164942513186
3.3781-3.46240.29091770.25424726490383
3.4624-3.55580.27561980.23834603480182
3.5558-3.66010.28091880.23744581476980
3.6601-3.7780.23921840.22654561474581
3.778-3.91260.2851730.22234855502883
3.9126-4.06870.25021760.22434436461280
4.0687-4.25320.30891650.21184538470381
4.2532-4.47640.28651930.20954732492581
4.4764-4.75530.24811620.19934356451879
4.7553-5.12010.2511900.19184731492183
5.1201-5.63080.24751750.20274577475281
5.6308-6.43540.24932110.21724895510685
6.4354-8.06970.25181750.20294657483283
8.0697-26.47850.23451840.18734685486983
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)
13.31191.2709-0.39574.1722-1.50685.7024-0.13090.6787-0.2316-0.86780.41890.3146-0.0219-0.3813-0.28970.4762-0.0902-0.0560.51620.0070.524244.1193-39.58769.9573
23.52640.7022-1.68192.50770.06132.41530.04670.19660.01480.0468-0.149-0.0943-0.06630.11640.09990.16450.0315-0.00350.23220.04110.357747.5878-32.326790.1422
31.3854-0.8316-0.35110.64560.25570.1062-0.1060.3087-0.21640.1099-0.210.1360.3585-0.03480.34490.4129-0.02810.10510.3256-0.00560.43621.6452-45.755497.9378
41.4099-0.9528-0.33390.96110.43181.70140.17040.3336-0.0871-0.0143-0.1252-0.0074-0.1467-0.0383-0.00550.2572-0.07970.07250.24160.08180.326511.0302-26.0055101.0935
51.4338-1.4653-1.03621.49451.05870.74810.70070.47880.6298-0.4327-0.3931-0.1125-1.0673-0.2335-0.27510.9030.09770.42210.7651-0.08141.119917.9485-10.313590.8971
64.13472.5751-0.86151.6484-0.99254.8432-0.13860.93110.8457-1.16120.0318-0.625-0.8947-0.0194-0.610.5850.10890.10490.99950.13610.748437.6138-20.136480.7994
72.26060.6825-0.14142.9165-0.11510.72450.2564-0.7801-0.17070.9334-0.1019-0.10720.1313-0.1073-0.11571.0969-0.01290.08680.42910.17380.5472.31536.572156.2856
80.5988-0.2990.13652.1591-0.22531.0212-0.17190.01240.1970.1330.12840.1039-0.0237-0.07230.00020.50480.01140.10560.10220.12620.44773.38775.278132.2601
90.9867-0.1263-0.46280.53380.20990.8869-0.05440.07760.05980.26750.01630.12840.0734-0.06770.03390.4875-0.04340.07880.12560.09670.38111.0588-27.9812126.1697
102.0143-3.0706-0.43427.21272.04752.61340.27870.05930.63630.24020.9513-1.9560.87331.22-1.03220.96420.01660.1160.7845-0.32611.253927.2289-17.5546139.8491
117.61060.7983-2.56051.3593-1.71022.50640.1919-1.51960.8591.8318-0.50470.5402-0.7337-0.28130.33530.8446-0.12730.05160.876-0.23140.586333.2307-29.9777123.4796
125.0016-3.00720.23573.01161.60092.8034-0.681-0.3916-0.61050.32571.3008-0.32930.40391.5906-0.62740.94290.05850.31060.883-0.30471.078823.983-14.574142.037
132.8453-1.52030.81153.1157-0.86114.2127-0.3184-0.4866-0.07121.37940.19330.2418-1.0388-0.47280.18170.7960.1710.08320.46050.030.515145.24821.676341.875
144.94140.205-3.55520.54180.89464.8068-0.6069-0.3711-0.54230.31840.23470.22590.3253-0.07050.33730.77810.2166-0.00180.45510.09340.548749.9992-9.80136.9865
154.7096-1.78951.49773.27771.06822.5962-0.1067-0.0384-0.1866-0.13580.15660.209-0.02550.218-0.06360.32990.03660.07090.24630.06390.305246.3149-4.888517.4455
161.011-0.2927-0.04510.35620.19250.1329-0.0865-0.22270.7168-0.0735-0.0141-0.2007-0.0863-0.00730.14590.53370.1299-0.07240.3688-0.12250.641421.81717.424313.4814
170.64590.51730.12822.01750.95511.3683-0.0067-0.16760.061-0.0521-0.0320.1050.27290.10740.0370.41930.1186-0.01010.24550.10090.460311.0282-12.619410.3909
181.63652.8206-0.83868.8533-1.57790.43420.8952-0.1058-2.09440.7749-0.0016-0.79551.5-0.317-0.80711.046-0.0607-0.34170.6733-0.05721.305125.9351-24.073925.6319
193.42260.91580.31560.26180.4578.31730.5381-1.16950.00120.5368-0.018-0.7363-0.35330.7863-0.46581.45140.0797-0.36040.9121-0.40371.1910.6754-32.969212.2396
208.03063.80811.53425.96230.20653.7580.50130.2873-0.2479-0.7212-1.0961.279-0.1238-0.42350.67190.80830.1169-0.06360.5863-0.25560.852124.9562-19.482624.1554
212.9381-0.5614-0.74281.09620.04863.07740.00070.70990.5107-0.79120.06130.14550.36530.2695-0.10651.50880.0885-0.16790.57280.20690.6414-0.6094-43.6787-45.9874
222.1629-0.67750.30053.78570.66420.2730.01710.1097-0.2016-0.53750.07790.02320.1639-0.0258-0.07290.63630.03560.01150.15810.1130.42865.935-46.5373-24.1399
230.9965-0.19080.77410.3336-0.37320.7707-0.2559-0.3247-0.0456-0.2482-0.04810.3962-0.166-0.21530.17710.57540.1778-0.0720.32-0.0370.5724-6.4373-20.8113-17.2446
241.5543-0.06370.51960.61430.00720.8394-0.2179-0.08470.0948-0.28330.09320.0655-0.0434-0.0210.10090.67780.1240.03530.19850.1110.412313.4626-10.0916-14.1958
258.01152.12961.50745.94181.72278.08040.15380.7526-0.6398-0.95641.1077-1.23850.68050.5623-1.19731.0512-0.2186-0.16580.5380.0410.963819.5821-26.5335-30.9217
263.4789-0.9374-1.26661.7997-1.81843.4760.35120.1026-0.1720.0647-0.5354-0.5531-0.1941-0.10780.31221.18760.1846-0.52311.2638-0.57741.411434.4297-15.2826-25.9232
274.46180.8945.28970.3410.86388.84560.24920.345-0.1184-0.22480.12510.57061.1187-0.0339-0.27250.87680.0876-0.10891.0057-0.37011.139133.1714-8.5428-11.9825
287.13875.44511.59034.25931.50631.2385-0.1851-0.3860.9880.04130.16040.0964-0.41680.39250.08390.9180.0735-0.21520.7804-0.29181.220822.0167-22.499-29.3217
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 115 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 116 through 247 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 248 through 289 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 290 through 437 )A0
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 27 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 28 through 36 )B0
7X-RAY DIFFRACTION7chain 'C' and (resid 3 through 144 )C0
8X-RAY DIFFRACTION8chain 'C' and (resid 145 through 263 )C0
9X-RAY DIFFRACTION9chain 'C' and (resid 264 through 437 )C0
10X-RAY DIFFRACTION10chain 'D' and (resid 1 through 12 )D0
11X-RAY DIFFRACTION11chain 'D' and (resid 13 through 19 )D0
12X-RAY DIFFRACTION12chain 'D' and (resid 20 through 35 )D0
13X-RAY DIFFRACTION13chain 'E' and (resid 3 through 106 )E0
14X-RAY DIFFRACTION14chain 'E' and (resid 107 through 144 )E0
15X-RAY DIFFRACTION15chain 'E' and (resid 145 through 247 )E0
16X-RAY DIFFRACTION16chain 'E' and (resid 248 through 289 )E0
17X-RAY DIFFRACTION17chain 'E' and (resid 290 through 437 )E0
18X-RAY DIFFRACTION18chain 'F' and (resid 1 through 9 )F0
19X-RAY DIFFRACTION19chain 'F' and (resid 10 through 19 )F0
20X-RAY DIFFRACTION20chain 'F' and (resid 20 through 35 )F0
21X-RAY DIFFRACTION21chain 'G' and (resid 2 through 115 )G0
22X-RAY DIFFRACTION22chain 'G' and (resid 116 through 247 )G0
23X-RAY DIFFRACTION23chain 'G' and (resid 248 through 289 )G0
24X-RAY DIFFRACTION24chain 'G' and (resid 290 through 437 )G0
25X-RAY DIFFRACTION25chain 'H' and (resid 1 through 6 )H0
26X-RAY DIFFRACTION26chain 'H' and (resid 7 through 12 )H0
27X-RAY DIFFRACTION27chain 'H' and (resid 13 through 19 )H0
28X-RAY DIFFRACTION28chain 'H' and (resid 20 through 35 )H0

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