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- PDB-3kdf: X-ray Crystal Structure of the Human Replication Protein A Comple... -

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Basic information

Entry
Database: PDB / ID: 3kdf
TitleX-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression
Components
  • Replication protein A 14 kDa subunitDNA replication
  • Replication protein A 32 kDa subunitDNA replication
KeywordsREPLICATION / Wheat germ cell free / protein complex / Center for Eukaryotic Structural Genomics / PSI / replication protein A / Homo sapiens / Protein Structure Initiative / CESG / Acetylation / Alternative splicing / DNA replication / Nucleus / Phosphoprotein / Polymorphism
Function / homology
Function and homology information


protein localization to chromosome / DNA replication factor A complex / Removal of the Flap Intermediate / G-rich strand telomeric DNA binding / regulation of DNA damage checkpoint / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 ...protein localization to chromosome / DNA replication factor A complex / Removal of the Flap Intermediate / G-rich strand telomeric DNA binding / regulation of DNA damage checkpoint / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Removal of the Flap Intermediate from the C-strand / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / regulation of double-strand break repair via homologous recombination / telomeric DNA binding / Presynaptic phase of homologous DNA pairing and strand exchange / PCNA-Dependent Long Patch Base Excision Repair / mismatch repair / Activation of the pre-replicative complex / Regulation of HSF1-mediated heat shock response / HSF1 activation / Activation of ATR in response to replication stress / mitotic G1 DNA damage checkpoint signaling / regulation of mitotic cell cycle / telomere maintenance / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Recognition of DNA damage by PCNA-containing replication complex / nucleotide-excision repair / Fanconi Anemia Pathway / Termination of translesion DNA synthesis / Translesion Synthesis by POLH / double-strand break repair via homologous recombination / base-excision repair / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / Dual Incision in GG-NER / PML body / Meiotic recombination / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / site of double-strand break / regulation of cell population proliferation / Processing of DNA double-strand break ends / protein phosphatase binding / Regulation of TP53 Activity through Phosphorylation / DNA replication / damaged DNA binding / chromosome, telomeric region / nuclear body / DNA repair / ubiquitin protein ligase binding / chromatin / enzyme binding / nucleoplasm / nucleus
Similarity search - Function
Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein 3 / Replication factor A protein 3 / Replication factor A protein-like / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily ...Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein 3 / Replication factor A protein 3 / Replication factor A protein-like / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Replication protein A 32 kDa subunit / Replication protein A 14 kDa subunit
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.975 Å
AuthorsBurgie, E.S. / Bingman, C.A. / Phillips Jr., G.N. / Fox, B.G. / Makino, S.-I. / Center for Eukaryotic Structural Genomics (CESG)
CitationJournal: To be Published
Title: X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression
Authors: Makino, S.-I. / Burgie, E.S. / Bingman, C.A. / Fox, B.G. / Phillips Jr., G.N.
History
DepositionOct 22, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 1, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Revision 1.3Oct 13, 2021Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Replication protein A 14 kDa subunit
D: Replication protein A 32 kDa subunit
C: Replication protein A 14 kDa subunit
B: Replication protein A 32 kDa subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,94711
Polymers57,5134
Non-polymers4347
Water4,648258
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Replication protein A 14 kDa subunit
B: Replication protein A 32 kDa subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,8814
Polymers28,7562
Non-polymers1242
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3000 Å2
ΔGint-13 kcal/mol
Surface area11720 Å2
MethodPISA
3
D: Replication protein A 32 kDa subunit
C: Replication protein A 14 kDa subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,0677
Polymers28,7562
Non-polymers3105
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3230 Å2
ΔGint-14 kcal/mol
Surface area11950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.680, 77.700, 121.300
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Replication protein A 14 kDa subunit / DNA replication / RP-A p14 / Replication factor A protein 3 / RF-A protein 3


Mass: 13774.071 Da / Num. of mol.: 2 / Mutation: M1S
Source method: isolated from a genetically manipulated source
Details: co-expressed with entity 1 / Source: (gene. exp.) Homo sapiens (human) / Description: Wheat Germ / Gene: REPA3, RPA14, RPA3 / Plasmid: pEU-His-Flexi / Production host: cell-free synthesis (others) / References: UniProt: P35244
#2: Protein Replication protein A 32 kDa subunit / DNA replication / RP-A p32 / RP-A p34 / Replication factor A protein 2 / RF-A protein 2


Mass: 14982.417 Da / Num. of mol.: 2 / Fragment: Residues 41-172 / Mutation: A41S
Source method: isolated from a genetically manipulated source
Details: co-expressed with entity 2 / Source: (gene. exp.) Homo sapiens (human) / Description: Wheat Germ / Gene: REPA2, RPA2, RPA32, RPA34 / Plasmid: pEU-His-Flexi / Production host: cell-free synthesis (others) / References: UniProt: P15927
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 258 / 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: 2.73 Å3/Da / Density % sol: 54.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 11% PEG 8000, 50 mM BisTris-propane pH 7.0, 50 mM NaCl, 5 mM HEPES pH 7.0, 0.3 mM TCEP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.9686, 0.97947
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 5, 2009
RadiationMonochromator: Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.96861
20.979471
ReflectionRedundancy: 13.6 % / Av σ(I) over netI: 29.77 / Number: 595468 / Rmerge(I) obs: 0.101 / Χ2: 1.64 / D res high: 1.97 Å / D res low: 50 Å / Num. obs: 43894 / % possible obs: 97.9
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
5.355099.710.0884.8713.8
4.245.3510010.0673.30214.6
3.714.2410010.0711.88614.8
3.373.7110010.0811.84414.8
3.133.3710010.0831.87414.9
2.943.1310010.1011.59114.8
2.82.9410010.1261.30414.7
2.672.810010.1491.30214.6
2.572.6710010.1721.28114.6
2.482.5799.910.1941.20214.5
2.42.4810010.231.17414.4
2.342.410010.2511.12214.3
2.272.3410010.281.10314.1
2.222.2799.910.3061.09713.7
2.172.2299.710.3421.09113.1
2.122.1798.410.3871.10312.5
2.082.1295.910.4431.12311.7
2.042.0892.910.4861.12110.8
22.0488.310.5051.14310
1.97282.710.5661.1348.8
ReflectionResolution: 1.97→50 Å / Num. obs: 43894 / % possible obs: 97.9 % / Redundancy: 13.6 % / Rmerge(I) obs: 0.101 / Χ2: 1.643 / Net I/σ(I): 12.1
Reflection shellResolution: 1.97→2 Å / Redundancy: 8.8 % / Rmerge(I) obs: 0.566 / Num. unique all: 1813 / Χ2: 1.134 / % possible all: 82.7

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Phasing

PhasingMethod: MAD
Phasing MAD set
IDHighest resolution (Å)Lowest resolution (Å)Power acentricPower centricReflection acentricReflection centric
ISO_11.983700394454352
ISO_21.98370.960.821387644289
ANO_11.98372.3980387070
ANO_21.98371.590383700
Phasing MAD set shell
IDResolution (Å)Power acentricPower centricReflection acentricReflection centric
ISO_18.6-3700402211
ISO_16.17-8.600777223
ISO_15.06-6.17001026226
ISO_14.39-5.06001230222
ISO_13.93-4.39001403220
ISO_13.59-3.93001579230
ISO_13.33-3.59001710227
ISO_13.12-3.33001843219
ISO_12.94-3.12001977232
ISO_12.79-2.94002096216
ISO_12.66-2.79002191232
ISO_12.55-2.66002321228
ISO_12.45-2.55002410221
ISO_12.36-2.45002514227
ISO_12.28-2.36002603226
ISO_12.21-2.28002700222
ISO_12.14-2.21002753224
ISO_12.08-2.14002760207
ISO_12.03-2.08002702182
ISO_11.98-2.03002448157
ANO_18.6-374.6204020
ANO_16.17-8.65.82907770
ANO_15.06-6.175.755010260
ANO_14.39-5.065.353012300
ANO_13.93-4.394.334014030
ANO_13.59-3.934.275015790
ANO_13.33-3.593.994017100
ANO_13.12-3.333.686018430
ANO_12.94-3.123.117019770
ANO_12.79-2.942.566020960
ANO_12.66-2.792.253021910
ANO_12.55-2.661.854023210
ANO_12.45-2.551.547024100
ANO_12.36-2.451.278025140
ANO_12.28-2.361.123026000
ANO_12.21-2.280.943026890
ANO_12.14-2.210.772027080
ANO_12.08-2.140.644026340
ANO_12.03-2.080.613024570
ANO_11.98-2.030.6021400
ISO_28.6-372.0061.342402210
ISO_26.17-8.61.8731.312777223
ISO_25.06-6.171.7421.1871026226
ISO_24.39-5.061.3250.9971230222
ISO_23.93-4.391.0990.8851403220
ISO_23.59-3.931.0530.8081579230
ISO_23.33-3.591.0020.6881710227
ISO_23.12-3.330.9720.7041843219
ISO_22.94-3.120.9460.7121976232
ISO_22.79-2.940.9260.6332096216
ISO_22.66-2.790.8760.6012191232
ISO_22.55-2.660.7890.5242320228
ISO_22.45-2.550.7240.4622408221
ISO_22.36-2.450.6360.4272510225
ISO_22.28-2.360.5680.3242599225
ISO_22.21-2.280.4810.2782694217
ISO_22.14-2.210.40.2522714219
ISO_22.08-2.140.3120.1972639195
ISO_22.03-2.080.3110.2082473165
ISO_21.98-2.030.2930.2012174137
ANO_28.6-375.26804020
ANO_26.17-8.67.27507770
ANO_25.06-6.176.947010260
ANO_24.39-5.065.527012300
ANO_23.93-4.394.301014030
ANO_23.59-3.933.941015790
ANO_23.33-3.593.502017100
ANO_23.12-3.333.071018430
ANO_22.94-3.122.492019760
ANO_22.79-2.941.868020960
ANO_22.66-2.791.495021910
ANO_22.55-2.661.177023200
ANO_22.45-2.550.953024080
ANO_22.36-2.450.75025100
ANO_22.28-2.360.642025990
ANO_22.21-2.280.521026870
ANO_22.14-2.210.466026730
ANO_22.08-2.140.396025500
ANO_22.03-2.080.388023500
ANO_21.98-2.030.346020400
Phasing MAD set site
IDCartn x (Å)Cartn y (Å)Cartn z (Å)Atom type symbolB isoOccupancy
1-3.18-28.484-55.005SE29.322.22
2-3.688-61.679-67.97SE31.492.23
3-2.142-9.185-4.444SE33.231.93
4-14.126-66.129-118.469SE36.31.8
5-2.589-40.309-105.169SE37.811.46
6-13.009-69.421-78.692SE44.11.67
7-2.082-18.308-94.903SE41.641.92
8-12.92-1.249-13.456SE47.21.63
9-15.744-50.39-86.194SE55.971.78
10-1.754-44.184-36.165SE49.481.41
11-7.817-61.241-82.184SE64.852.15
12-6.993-72.952-7.28SE55.911.91
13-6.149-42.458-66.284SE38.860.98
14-11.402-1.65-25.381SE58.711.18
15-1.652-4.694-107.558SE56.41.46
16-1.119-19.998-65.187SE40.640.89
17-10.829-72.274-12.473SE52.110.77
18-10.4-76.458-83.926SE55.351.02
19-0.579-9.364-85.886SE52.610.99
20-12.469-69.231-11.16SE31.330.44
Phasing dmMethod: Solvent flattening and Histogram matching / Reflection: 43637
Phasing dm shell
Resolution (Å)Delta phi finalFOM Reflection
9.23-10043.90.878502
7-9.23410.914618
5.86-743.30.913755
5.14-5.86450.924840
4.64-5.1447.10.933971
4.26-4.6443.60.9361039
3.96-4.2643.80.9361117
3.71-3.9650.30.9331197
3.51-3.7150.10.9311252
3.34-3.5150.70.9251340
3.19-3.3448.30.9231395
3.05-3.1951.60.9271448
2.94-3.05510.9111515
2.83-2.94500.9071550
2.74-2.8352.60.9051620
2.65-2.7452.90.9021667
2.58-2.6553.20.8961703
2.51-2.5856.80.891768
2.44-2.5159.50.8881796
2.38-2.4461.60.8851855
2.32-2.38630.8851922
2.27-2.3265.80.8811938
2.22-2.2766.90.871970
2.17-2.2269.20.8762030
2.13-2.1772.90.8742035
2.09-2.1374.80.8751963
2.05-2.0974.10.852017
2.02-2.0578.50.8441934
1.98-2.0280.60.8061880

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
DM5phasing
PHENIX1.5_2refinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 1.975→36.999 Å / Occupancy max: 1 / Occupancy min: 0.27 / FOM work R set: 0.876 / SU ML: 0.27 / σ(F): 1.33 / Phase error: 19.39 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.206 2185 4.99 %
Rwork0.192 --
obs0.192 43791 97.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 59.965 Å2 / ksol: 0.335 e/Å3
Displacement parametersBiso max: 144.09 Å2 / Biso mean: 43.544 Å2 / Biso min: 8.54 Å2
Baniso -1Baniso -2Baniso -3
1--2.544 Å2-0 Å20 Å2
2---2.8 Å2-0 Å2
3---5.344 Å2
Refinement stepCycle: LAST / Resolution: 1.975→36.999 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3684 0 28 258 3970
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0194011
X-RAY DIFFRACTIONf_angle_d1.3525447
X-RAY DIFFRACTIONf_chiral_restr0.102634
X-RAY DIFFRACTIONf_plane_restr0.005702
X-RAY DIFFRACTIONf_dihedral_angle_d17.7971509
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 16

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.975-2.0180.2521030.242073217679
2.018-2.0650.2441250.2382318244388
2.065-2.1170.2521400.2342473261395
2.117-2.1740.2291340.2182592272698
2.174-2.2380.2171300.19926212751100
2.238-2.310.2131450.19926262771100
2.31-2.3920.2111390.20126332772100
2.392-2.4880.2041190.19326742793100
2.488-2.6020.2151470.19226332780100
2.602-2.7390.2291220.226722794100
2.739-2.910.2221580.20426402798100
2.91-3.1350.2411250.20426922817100
3.135-3.450.1941330.18826932826100
3.45-3.9490.1991600.17426912851100
3.949-4.9730.1631460.14127312877100
4.973-37.0050.1781590.1928443003100
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)
12.33760.1881-0.81532.6616-0.24310.1643-0.3559-0.0481-0.02880.13710.36670.14660.05890.00790.00180.2062-0.08170.01650.1787-0.00560.1533-10.107712.003846.4023
20.8642-1.3656-0.62661.84550.83462.5354-0.04180.0676-0.15280.08040.0358-0.27510.36850.3138-0.03190.30650.01460.02140.2908-0.0880.28492.93673.465441.4084
30.9056-0.619-0.64940.72060.90920.9275-0.15630.1011-0.1675-0.1180.1898-0.03390.2174-0.05170.0130.2852-0.06920.02510.2683-0.02680.2262-3.45467.820341.4701
40.1947-0.6224-0.60511.95450.43071.03660.04280.14360.26270.03380.1047-0.2991-0.1305-0.0633-0.1230.2222-0.04640.00940.2569-0.03830.2275-0.759222.650546.7157
51.8953-0.6167-1.25932.79640.6010.86080.01090.33680.2807-0.55470.130.4885-0.3659-0.4071-0.14310.3737-0.0095-0.09240.37550.1370.3823-14.895331.901536.7664
61.89560.2470.11983.3709-1.83181.2652-0.26580.70720.1729-0.72530.54290.23780.313-0.4252-0.19930.4172-0.1893-0.08690.44470.13020.2361-10.854924.166529.542
74.7414-1.5657-4.70442.35471.19535.0936-0.16050.9037-0.04310.6131-0.60350.114-0.4361-3.20780.42490.45360.0078-0.13171.08160.1610.5124-23.81330.26332.6582
81.7113-0.0288-0.80090.5893-0.35321.2728-0.031-0.16150.5664-0.12760.2793-0.2733-0.45340.2445-0.16880.3251-0.07250.01890.21410.01790.2679-2.851330.387239.376
93.1713-4.0937-2.75295.29963.64633.8089-0.3381-1.17270.53042.23180.7959-0.57490.11860.6851-0.48450.4416-0.0244-0.12780.4164-0.11160.249115.333842.340172.6726
102.0411-0.2849-0.85250.5809-0.52872.4724-0.1267-0.0611-0.53980.02720.16520.3210.2484-0.0693-0.01930.21310.03880.05780.21250.08380.32372.32233.535573.3972
113.1142-1.1474-1.30381.5764-0.05370.81830.0098-0.8752-0.22810.48050.34480.20350.2128-0.2743-0.17280.3390.09530.1290.3890.08970.2824-0.265437.661581.6376
120.812-0.0014-0.1381.39820.25531.013-0.053-0.0738-0.17930.03560.15330.3053-0.0235-0.0698-0.06250.17450.02920.02390.20610.01980.24980.708238.861467.7458
136.5225-0.1823-1.61551.3088-0.91821.65280.03920.7198-0.1614-0.6351-0.1413-0.24610.54470.35640.10580.2779-0.01620.04130.38330.00830.25314.000546.960950.0752
140.5572-0.28990.23371.187-0.4461.64050.07950.0883-0.0725-0.20350.04890.0215-0.00820.2635-0.10520.2682-0.03360.02950.2589-0.04110.285511.374649.734853.2642
152.13430.69140.38730.20970.00223.16820.0669-0.10710.37420.0381-0.04130.1235-0.57340.2657-0.06090.1828-0.05520.04260.1022-0.03180.197212.039357.012563.5167
161.84070.4505-0.26163.4082-0.20961.15950.00960.19090.2183-0.17380.10160.1805-0.194-0.1205-0.10850.2022-0.01560.0020.19960.02280.23325.020950.362556.7506
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 2:26)A2 - 26
2X-RAY DIFFRACTION2(chain A and resid 27:65)A27 - 65
3X-RAY DIFFRACTION3(chain A and resid 66:88)A66 - 88
4X-RAY DIFFRACTION4(chain A and resid 89:116)A89 - 116
5X-RAY DIFFRACTION5(chain B and resid 5:48)B5 - 48
6X-RAY DIFFRACTION6(chain B and resid 49:92)B49 - 92
7X-RAY DIFFRACTION7(chain B and resid 93:101)B93 - 101
8X-RAY DIFFRACTION8(chain B and resid 102:131)B102 - 131
9X-RAY DIFFRACTION9(chain C and resid 1:7)C1 - 7
10X-RAY DIFFRACTION10(chain C and resid 8:37)C8 - 37
11X-RAY DIFFRACTION11(chain C and resid 38:62)C38 - 62
12X-RAY DIFFRACTION12(chain C and resid 63:118)C63 - 118
13X-RAY DIFFRACTION13(chain D and resid 5:22)D5 - 22
14X-RAY DIFFRACTION14(chain D and resid 23:43)D23 - 43
15X-RAY DIFFRACTION15(chain D and resid 44:78)D44 - 78
16X-RAY DIFFRACTION16(chain D and resid 79:132)D79 - 132

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