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- PDB-7w76: Crystal structure of the K. lactis Bre1 RBD in complex with Rad6,... -

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Basic information

Entry
Database: PDB / ID: 7w76
TitleCrystal structure of the K. lactis Bre1 RBD in complex with Rad6, crystal form II
Components
  • E3 ubiquitin-protein ligase BRE1
  • Ubiquitin-conjugating enzyme E2 2
KeywordsGENE REGULATION / Complex / ubiquitin / ubiquitin ligase
Function / homology
Function and homology information


HULC complex / E2 ubiquitin-conjugating enzyme / sporulation resulting in formation of a cellular spore / ubiquitin conjugating enzyme activity / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / chromatin organization / protein ubiquitination / DNA repair / zinc ion binding ...HULC complex / E2 ubiquitin-conjugating enzyme / sporulation resulting in formation of a cellular spore / ubiquitin conjugating enzyme activity / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / chromatin organization / protein ubiquitination / DNA repair / zinc ion binding / ATP binding / nucleus / cytoplasm
Similarity search - Function
E3 ubiquitin ligase Bre1 / BRE1 E3 ubiquitin ligase / : / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. ...E3 ubiquitin ligase Bre1 / BRE1 E3 ubiquitin ligase / : / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 2 / E3 ubiquitin-protein ligase BRE1
Similarity search - Component
Biological speciesKluyveromyces lactis NRRL Y-1140 (yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.05 Å
AuthorsShi, M. / Zhao, J. / Xiang, S.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32071205 China
National Natural Science Foundation of China (NSFC)31870769 China
CitationJournal: Elife / Year: 2023
Title: Structural basis for the Rad6 activation by the Bre1 N-terminal domain.
Authors: Shi, M. / Zhao, J. / Zhang, S. / Huang, W. / Li, M. / Bai, X. / Zhang, W. / Zhang, K. / Chen, X. / Xiang, S.
History
DepositionDec 3, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 29, 2023Provider: repository / Type: Initial release
Revision 1.1Apr 5, 2023Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.3Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 2
B: Ubiquitin-conjugating enzyme E2 2
C: E3 ubiquitin-protein ligase BRE1
D: E3 ubiquitin-protein ligase BRE1
E: E3 ubiquitin-protein ligase BRE1
F: E3 ubiquitin-protein ligase BRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,0269
Polymers131,7466
Non-polymers2803
Water00
1
A: Ubiquitin-conjugating enzyme E2 2
C: E3 ubiquitin-protein ligase BRE1
D: E3 ubiquitin-protein ligase BRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,0615
Polymers65,8733
Non-polymers1882
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11130 Å2
ΔGint-104 kcal/mol
Surface area24500 Å2
MethodPISA
2
B: Ubiquitin-conjugating enzyme E2 2
E: E3 ubiquitin-protein ligase BRE1
F: E3 ubiquitin-protein ligase BRE1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,9654
Polymers65,8733
Non-polymers921
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10200 Å2
ΔGint-90 kcal/mol
Surface area24190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.221, 113.221, 386.165
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11D-301-

SO4

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 0 through 89 or resid 98 through 157 or resid 1000))
21(chain B and resid 0 through 1000)
12(chain C and (resid 17 through 121 or resid 133 through 170))
22(chain D and (resid 17 through 121 or resid 133 through 170))
32(chain E and resid 17 through 170)
42(chain F and (resid 17 through 121 or resid 133 through 170))

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111HISHISLEULEU(chain A and (resid 0 through 89 or resid 98 through 157 or resid 1000))AA0 - 893 - 92
121PROPROALAALA(chain A and (resid 0 through 89 or resid 98 through 157 or resid 1000))AA98 - 157101 - 160
131GOLGOLGOLGOL(chain A and (resid 0 through 89 or resid 98 through 157 or resid 1000))AG1000
211HISHISGOLGOL(chain B and resid 0 through 1000)BB - H0 - 10003
112SERSERLYSLYS(chain C and (resid 17 through 121 or resid 133 through 170))CC17 - 12117 - 121
122ARGARGASPASP(chain C and (resid 17 through 121 or resid 133 through 170))CC133 - 170133 - 170
212SERSERLYSLYS(chain D and (resid 17 through 121 or resid 133 through 170))DD17 - 12117 - 121
222ARGARGASPASP(chain D and (resid 17 through 121 or resid 133 through 170))DD133 - 170133 - 170
312SERSERASPASP(chain E and resid 17 through 170)EE17 - 17017 - 170
412SERSERLYSLYS(chain F and (resid 17 through 121 or resid 133 through 170))FF17 - 12117 - 121
422ARGARGASPASP(chain F and (resid 17 through 121 or resid 133 through 170))FF133 - 170133 - 170

NCS ensembles :
ID
1
2

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Components

#1: Protein Ubiquitin-conjugating enzyme E2 2 / E2 ubiquitin-conjugating enzyme 2 / Ubiquitin carrier protein UBC2 / Ubiquitin-protein ligase UBC2


Mass: 19547.471 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Kluyveromyces lactis NRRL Y-1140 (yeast)
Strain: NRRL Y-1140 / Gene: UBC2 / Production host: Escherichia coli (E. coli)
References: UniProt: Q6CUD9, E2 ubiquitin-conjugating enzyme
#2: Protein
E3 ubiquitin-protein ligase BRE1 / RING-type E3 ubiquitin transferase BRE1


Mass: 23162.822 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Kluyveromyces lactis NRRL Y-1140 (yeast)
Strain: NRRL Y-1140 / Gene: BRE1 / Production host: Escherichia coli (E. coli)
References: UniProt: Q6CWM4, RING-type E3 ubiquitin transferase
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
Has ligand of interestN
Has protein modificationY

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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: 2.74 Å3/Da / Density % sol: 55.11 %
Description: THE ENTRY CONTAINS FRIEDEL PAIRS IN I/F_PLUS/MINUS COLUMNS.
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: sodium acetrate trithydrate, ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97846 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 1, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97846 Å / Relative weight: 1
ReflectionResolution: 3.05→50 Å / Num. obs: 58132 / % possible obs: 99.7 % / Redundancy: 10.3 % / Rmerge(I) obs: 0.135 / Rpim(I) all: 0.027 / Rrim(I) all: 0.138 / Χ2: 1.039 / Net I/σ(I): 4.6
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.05-3.18.351.1627160.8760.2461.1910.53196.9
3.1-3.168.90.91528340.9350.190.9370.54598.3
3.16-3.229.90.80928100.9820.1640.8280.46499.5
3.22-3.2910.20.74227940.9780.150.7590.455100
3.29-3.3610.30.57628200.980.1170.5890.473100
3.36-3.4310.30.49528840.9790.1020.5070.502100
3.43-3.5210.350.4728560.9790.0980.4810.544100
3.52-3.6210.050.3628180.9940.0760.3690.555100
3.62-3.729.50.31128540.9920.0680.3190.61399.9
3.72-3.849.80.27128620.9920.0580.2780.636100
3.84-3.9810.10.20728640.9960.0430.2120.768100
3.98-4.1410.30.17728920.9960.0350.1810.779100
4.14-4.3310.20.15529200.9970.0310.1580.853100
4.33-4.5610.10.1428120.9970.0280.1430.952100
4.56-4.849.550.11628920.9980.0240.1191.133100
4.84-5.219.70.1229420.9970.0250.1231.11899.9
5.21-5.7410.650.12229720.9980.0250.1251.082100
5.74-6.5710.950.1130100.9970.0220.1131.199100
6.57-8.2711.750.08430800.9990.0170.0861.756100
8.27-5013.850.07333960.9990.0140.0743.686100

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
SCALEPACKdata scaling
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1ayz

1ayz


Resolution: 3.05→32.18 Å / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 34.43 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.286 2657 5.13 %
Rwork0.2372 49122 -
obs0.2396 51779 98.24 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 297.64 Å2 / Biso mean: 122.3942 Å2 / Biso min: 40.19 Å2
Refinement stepCycle: final / Resolution: 3.05→32.18 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7486 0 17 0 7503
Biso mean--112.69 --
Num. residues----941
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1172X-RAY DIFFRACTION14.194TORSIONAL
12B1172X-RAY DIFFRACTION14.194TORSIONAL
21C2637X-RAY DIFFRACTION14.194TORSIONAL
22D2637X-RAY DIFFRACTION14.194TORSIONAL
23E2637X-RAY DIFFRACTION14.194TORSIONAL
24F2637X-RAY DIFFRACTION14.194TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 19

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.05-3.110.4691170.40292378249591
3.11-3.170.44091280.36222528265696
3.17-3.230.41461430.35132550269397
3.23-3.30.47361500.33062566271698
3.3-3.380.39091230.31012577270098
3.38-3.460.32081740.29062567274198
3.46-3.550.30821490.28562620276999
3.55-3.660.28661240.27122598272299
3.66-3.780.31921320.25182612274499
3.78-3.910.2841640.24392564272898
3.91-4.070.32971430.23762613275699
4.07-4.250.26741560.22012576273299
4.25-4.480.28861500.22742620277099
4.48-4.760.20471340.20426342768100
4.76-5.120.25111590.228125862745100
5.12-5.630.31491170.25622647276499
5.63-6.440.29421250.27662624274999
6.45-8.090.30591290.229326642793100
8.1-32.180.20341400.15912598273899
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)
11.11870.88290.06125.0241-2.94632.3072-0.79631.2563-0.0981-0.5366-0.0691-1.5271-0.3308-1.4285-0.77270.4814-0.1617-0.10791.52270.03490.5101-10.0372-26.6111-62.3632
20.5373-0.2451-0.20690.40830.48010.50630.15990.48610.2732-0.3211-0.4324-0.06080.0077-1.3390.00020.69780.1379-0.151.0283-0.11920.6919-4.2262-22.372-53.6128
32.296-0.3795-1.91051.62710.99811.89050.3202-0.01620.1132-0.1595-0.3161-0.1343-0.6474-0.55390.140.4886-0.0749-0.08390.4622-0.02190.54215.6185-22.78-53.1518
41.55080.63651.76430.54941.34983.6835-0.73960.5180.13-0.95840.67180.1362-1.25390.6812-0.03070.39040.0261-0.09750.5195-0.09430.626910.5564-27.0387-59.085
50.89910.81570.53130.7621-0.03831.00240.6586-0.3671-0.18830.7787-0.2895-0.1850.13520.10360.030.5895-0.0201-0.12890.4042-0.01590.637315.4296-25.2312-45.275
60.0402-0.06130.05270.0554-0.05990.0506-0.3728-0.1917-0.60360.32940.94880.2115-0.66010.0309-0.00121.2250.07370.06471.0655-0.04950.9581-5.3704-15.5463-44.998
70.67520.90.57773.298-0.04330.7086-1.32420.7319-0.97070.41410.88430.5938-0.9026-0.7614-0.44071.7340.36690.67971.59990.17621.1765-38.4306-38.265621.1505
83.43110.84511.13353.5707-0.25980.41891.0058-0.5046-0.18421.37440.03760.3964-1.2745-1.0341.49351.85670.5010.6111.28890.260.9579-29.8333-45.038111.6127
90.63471.48390.39753.86171.62050.75260.4994-0.1406-0.43172.11880.7881-1.09070.56680.74272.85211.81370.47950.3320.23770.25090.6327-21.2976-46.957611.3298
101.63821.2155-0.5242.5169-0.77185.59520.74660.30050.24690.8633-0.03970.1303-0.3679-1.18121.61781.2804-0.01620.21030.55370.09140.9182-17.75-51.35841.3141
110.198-0.32050.26630.459-0.40030.3188-0.460.63450.3309-0.6575-1.27150.17191.75180.1393-0.02681.1935-0.28480.00571.1848-0.16280.8592-11.269-27.9306-40.2388
128.26120.00756.5919-0.01880.83674.66570.783-2.2508-0.22680.0274-0.1996-0.17490.7023-1.99830.29850.7279-0.1444-0.01310.692-0.16270.684424.278-19.5067-17.1551
130.3233-0.24730.41280.52850.36110.6641-0.14550.74250.3631-0.8413-0.0842-0.5557-0.3074-0.0328-0.00070.96810.01450.17090.6988-0.19241.190859.8377-14.2089-10.2195
141.0564-0.04840.43050.66-1.43821.58290.1092-0.44280.0668-0.23370.3421-0.16240.1714-0.44671.01951.1917-0.294-0.02151.0383-0.21530.701930.4738-31.4938-14.7926
150.55371.0530.79153.86681.43391.18770.5056-0.18650.39362.7125-0.6935-0.00760.6744-0.3862-0.02591.0326-0.07740.2661.3066-0.27870.8379-2.4255-17.713-23.096
161.94720.09571.19140.00960.30432.0884-0.3653-0.7006-0.40610.14870.3877-0.16260.1433-0.5026-0.00770.7947-0.0478-0.0410.3311-0.05420.85537.6885-23.3452-12.1877
170.10830.0985-0.03580.0783-0.0038-0.00360.71820.3065-0.04190.7011-0.77730.46540.8767-2.39510.00020.9243-0.1593-0.08110.8347-0.26160.888743.8189-27.9578-1.6202
181.7557-1.5726-1.74371.81661.01952.21790.6076-0.3161-0.68911.0370.1701-1.51661.43091.31080.26551.12120.2091-0.46820.233-0.25981.641761.0671-28.8195-0.0404
193.2908-0.12530.10260.1259-0.1941-0.3049-0.62021.0762-0.96060.03440.353-0.08561.2872-0.5643-0.43941.544-0.24080.03541.0305-0.15790.893229.4483-35.2268-22.3687
200.2632-0.0126-0.04530.248-0.10450.0259-0.495-0.30520.1930.59820.83560.22240.676-0.65140.00061.4159-0.61510.02771.448-0.04730.7645-3.3361-32.1317-35.0997
211.00630.47171.5271.5494-0.09772.88050.02040.5909-0.28750.1991-1.15950.2207-0.8034-0.5116-1.82271.97950.71661.33842.20030.26691.2377-38.8458-36.76931.1178
221.4283-0.8281-2.9044-0.2040.10941.76720.272-0.1525-0.01690.2290.16650.0692-0.33-0.5970.41341.0297-0.02520.16621.49210.13870.9132-10.8442-51.7035-30.5784
230.0637-0.0370.15730.0571-0.03560.5553-0.16321.19290.22840.22360.4686-0.97470.1402-0.3648-0.00521.5483-0.0154-0.28661.36810.46862.553328.0851-68.6602-53.8876
241.5089-0.6920.94570.4525-0.23180.82721.0065-1.2786-2.13881.3833-0.4926-0.71151.014-0.27580.07651.28350.34970.01541.02230.2331.541414.6041-68.0899-45.848
252.14673.1214-1.54884.5838-2.06681.5324-0.5231-0.1823-0.76990.6077-0.3773-3.0330.1834-0.395-0.44430.97660.2582-0.68391.3387-0.12251.709523.6883-59.7364-45.321
260.5241-0.67130.16980.23230.20150.98990.5207-0.48610.15210.46630.3307-0.24840.25780.00350.12171.2093-0.06140.03971.34810.05290.9066-2.9735-43.0541-31.7035
270.05770.0606-0.01310.069-0.0170.0067-0.3170.2019-0.2370.0573-0.2755-0.0224-0.2287-0.2186-0.00942.5701-0.30780.04982.64180.27532.0114-31.9501-47.1424-22.8537
280.0189-0.03050.01120.03020.01410.073-0.4638-0.5083-0.7894-0.4831-0.3951-0.9807-0.30670.2454-0.00251.87940.1068-0.18532.860.52141.5423-36.5779-45.661-16.6827
291.10811.0662-0.1752-1.0185-0.38650.91060.6368-0.82450.66390.65210.0219-0.0032-0.35670.41570.03850.9316-0.04620.27430.9368-0.05610.88631.3659-51.3414-37.123
300.59310.22470.4720.6826-0.04830.3699-0.229-1.06230.0041-0.42410.3525-0.0419-0.60680.07180.00030.6069-0.00880.04740.7597-0.02260.788811.1456-48.343-52.5314
310.3107-0.1251-0.08420.2918-0.06340.0561-0.5234-0.34310.5169-0.6425-1.2637-1.33770.28780.0435-0.06831.2404-0.0811-0.1611.2935-0.13611.21728.0593-47.4911-49.1428
321.0709-0.34530.30770.48570.23421.3683-0.09910.36490.11930.6410.3547-0.0313-0.65640.14081.20531.1203-0.14840.04291.11910.13230.8272-1.1317-40.7831-22.7657
330.047-0.020.02130.06210.0210.0059-0.04841.70060.67570.4606-1.0720.0104-0.3587-0.0411-0.00281.75080.18930.0282.21960.28111.3594-30.8429-34.4376-6.7296
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 0 through 18 )A0 - 18
2X-RAY DIFFRACTION2chain 'A' and (resid 19 through 41 )A19 - 41
3X-RAY DIFFRACTION3chain 'A' and (resid 42 through 77 )A42 - 77
4X-RAY DIFFRACTION4chain 'A' and (resid 78 through 101 )A78 - 101
5X-RAY DIFFRACTION5chain 'A' and (resid 102 through 150 )A102 - 150
6X-RAY DIFFRACTION6chain 'A' and (resid 151 through 158 )A151 - 158
7X-RAY DIFFRACTION7chain 'B' and (resid -1 through 18 )B-1 - 18
8X-RAY DIFFRACTION8chain 'B' and (resid 19 through 68 )B19 - 68
9X-RAY DIFFRACTION9chain 'B' and (resid 69 through 114 )B69 - 114
10X-RAY DIFFRACTION10chain 'B' and (resid 115 through 157 )B115 - 157
11X-RAY DIFFRACTION11chain 'C' and (resid 12 through 21 )C12 - 21
12X-RAY DIFFRACTION12chain 'C' and (resid 22 through 80 )C22 - 80
13X-RAY DIFFRACTION13chain 'C' and (resid 81 through 128 )C81 - 128
14X-RAY DIFFRACTION14chain 'C' and (resid 129 through 173 )C129 - 173
15X-RAY DIFFRACTION15chain 'D' and (resid 16 through 29 )D16 - 29
16X-RAY DIFFRACTION16chain 'D' and (resid 30 through 97 )D30 - 97
17X-RAY DIFFRACTION17chain 'D' and (resid 98 through 110 )D98 - 110
18X-RAY DIFFRACTION18chain 'D' and (resid 111 through 131 )D111 - 131
19X-RAY DIFFRACTION19chain 'D' and (resid 132 through 172 )D132 - 172
20X-RAY DIFFRACTION20chain 'D' and (resid 173 through 183 )D173 - 183
21X-RAY DIFFRACTION21chain 'E' and (resid 14 through 22 )E14 - 22
22X-RAY DIFFRACTION22chain 'E' and (resid 23 through 80 )E23 - 80
23X-RAY DIFFRACTION23chain 'E' and (resid 81 through 85 )E81 - 85
24X-RAY DIFFRACTION24chain 'E' and (resid 86 through 110 )E86 - 110
25X-RAY DIFFRACTION25chain 'E' and (resid 111 through 133 )E111 - 133
26X-RAY DIFFRACTION26chain 'E' and (resid 134 through 170 )E134 - 170
27X-RAY DIFFRACTION27chain 'F' and (resid 17 through 21 )F17 - 21
28X-RAY DIFFRACTION28chain 'F' and (resid 22 through 29 )F22 - 29
29X-RAY DIFFRACTION29chain 'F' and (resid 30 through 97 )F30 - 97
30X-RAY DIFFRACTION30chain 'F' and (resid 98 through 121 )F98 - 121
31X-RAY DIFFRACTION31chain 'F' and (resid 122 through 133 )F122 - 133
32X-RAY DIFFRACTION32chain 'F' and (resid 134 through 172 )F134 - 172
33X-RAY DIFFRACTION33chain 'F' and (resid 173 through 182 )F173 - 182

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