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- PDB-7bgu: Mason-Pfizer Monkey Virus Protease mutant C7A/D26N/C106A in compl... -

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Basic information

Entry
Database: PDB / ID: 7bgu
TitleMason-Pfizer Monkey Virus Protease mutant C7A/D26N/C106A in complex with peptidomimetic inhibitor
Components
  • Gag-Pro-Pol polyprotein
  • peptidomimetic inhibitor
KeywordsHYDROLASE / Mason-Pfizer Monkey Virus / M-PMV / retropepsin / active site inhibitor / active site mutant
Function / homology
Function and homology information


dUTP diphosphatase / dUTP diphosphatase activity / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases ...dUTP diphosphatase / dUTP diphosphatase activity / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / viral nucleocapsid / DNA recombination / structural constituent of virion / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / proteolysis / DNA binding / RNA binding / zinc ion binding
Similarity search - Function
GAG-polyprotein viral zinc-finger / Beta-retroviral matrix protein / Beta-retroviral matrix superfamily / Retroviral GAG p10 protein / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / dUTPase-like / dUTPase ...GAG-polyprotein viral zinc-finger / Beta-retroviral matrix protein / Beta-retroviral matrix superfamily / Retroviral GAG p10 protein / G-patch domain / G-patch domain profile. / G-patch domain / glycine rich nucleic binding domain / dUTPase-like / dUTPase / dUTPase, trimeric / dUTPase-like superfamily / gag protein p24 N-terminal domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Retropepsin-like catalytic domain / Ribonuclease H domain / RNase H type-1 domain profile. / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Retrovirus capsid, C-terminal / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Ribonuclease H superfamily / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
Gag-Pro-Pol polyprotein
Similarity search - Component
Biological speciesMason-Pfizer monkey virus
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.433 Å
AuthorsWosicki, S. / Gilski, M. / Kazmierczyk, M. / Jaskolski, M. / Zabranska, H. / Pichova, I.
Funding support Czech Republic, 1items
OrganizationGrant numberCountry
Czech Academy of SciencesRVO 61388963 Czech Republic
Citation
Journal: Protein Sci. / Year: 2021
Title: Crystal structures of inhibitor complexes of M-PMV protease with visible flap loops.
Authors: Wosicki, S. / Kazmierczyk, M. / Gilski, M. / Zabranska, H. / Pichova, I. / Jaskolski, M.
#1: Journal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Comparison of a retroviral protease in monomeric and dimeric states.
Authors: Wosicki, S. / Gilski, M. / Zabranska, H. / Pichova, I. / Jaskolski, M.
#2: Journal: Acta Crystallogr. D Biol. Crystallogr. / Year: 2011
Title: High-resolution structure of a retroviral protease folded as a monomer.
Authors: Gilski, M. / Kazmierczyk, M. / Krzywda, S. / Zabranska, H. / Cooper, S. / Popovic, Z. / Khatib, F. / DiMaio, F. / Thompson, J. / Baker, D. / Pichova, I. / Jaskolski, M.
#3: Journal: Nature / Year: 1989
Title: Crystal structure of a retroviral protease proves relationship to aspartic protease family.
Authors: Miller, M. / Jaskolski, M. / Rao, J.K. / Leis, J. / Wlodawer, A.
#4: Journal: Science / Year: 1989
Title: Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease.
Authors: Wlodawer, A. / Miller, M. / Jaskolski, M. / Sathyanarayana, B.K. / Baldwin, E. / Weber, I.T. / Selk, L.M. / Clawson, L. / Schneider, J. / Kent, S.B.
#5: Journal: Nat. Struct. Mol. Biol. / Year: 2011
Title: Crystal structure of a monomeric retroviral protease solved by protein folding game players.
Authors: Khatib, F. / DiMaio, F. / Cooper, S. / Kazmierczyk, M. / Gilski, M. / Krzywda, S. / Zabranska, H. / Pichova, I. / Thompson, J. / Popovic, Z. / Jaskolski, M. / Baker, D.
History
DepositionJan 8, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 15, 2021Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _struct_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id ..._struct_conn.pdbx_leaving_atom_flag / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Gag-Pro-Pol polyprotein
B: Gag-Pro-Pol polyprotein
C: Gag-Pro-Pol polyprotein
D: Gag-Pro-Pol polyprotein
G: peptidomimetic inhibitor
F: peptidomimetic inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,8488
Polymers53,3716
Non-polymers4772
Water3,045169
1
A: Gag-Pro-Pol polyprotein
B: Gag-Pro-Pol polyprotein
F: peptidomimetic inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,9244
Polymers26,6863
Non-polymers2381
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5540 Å2
ΔGint-36 kcal/mol
Surface area10730 Å2
MethodPISA
2
C: Gag-Pro-Pol polyprotein
D: Gag-Pro-Pol polyprotein
G: peptidomimetic inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,9244
Polymers26,6863
Non-polymers2381
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4640 Å2
ΔGint-31 kcal/mol
Surface area10740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)29.068, 67.893, 69.739
Angle α, β, γ (deg.)77.070, 83.340, 83.180
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain F
21chain G
12(chain A and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))
22(chain B and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))
32(chain C and (resid 1 through 16 or resid 20...
42(chain D and (resid 1 through 16 or resid 20...

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
111PROPROTHRTHRchain FFF1 - 71 - 7
211PROPROTHRTHRchain GGE1 - 71 - 7
112TRPTRPLEULEU(chain A and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))AA1 - 161 - 16
122METMETGLYGLY(chain A and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))AA20 - 5420 - 54
132ASNASNPROPRO(chain A and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))AA60 - 10860 - 108
212TRPTRPLEULEU(chain B and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))BB1 - 161 - 16
222METMETGLYGLY(chain B and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))BB20 - 5420 - 54
232ASNASNPROPRO(chain B and (resid 1 through 16 or resid 20 through 54 or resid 60 through 108))BB60 - 10860 - 108
312TRPTRPLEULEU(chain C and (resid 1 through 16 or resid 20...CC1 - 161 - 16
322METMETLEULEU(chain C and (resid 1 through 16 or resid 20...CC20 - 5220 - 52
332ARGARGARGARG(chain C and (resid 1 through 16 or resid 20...CC5353
342TRPTRPPROPRO(chain C and (resid 1 through 16 or resid 20...CC1 - 1081 - 108
352TRPTRPPROPRO(chain C and (resid 1 through 16 or resid 20...CC1 - 1081 - 108
362TRPTRPPROPRO(chain C and (resid 1 through 16 or resid 20...CC1 - 1081 - 108
372TRPTRPPROPRO(chain C and (resid 1 through 16 or resid 20...CC1 - 1081 - 108
412TRPTRPLEULEU(chain D and (resid 1 through 16 or resid 20...DD1 - 161 - 16
422METMETLEULEU(chain D and (resid 1 through 16 or resid 20...DD20 - 5220 - 52
432TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108
442TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108
452TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108
462TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108
472TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108
482TRPTRPPROPRO(chain D and (resid 1 through 16 or resid 20...DD1 - 1081 - 108

NCS ensembles :
ID
1
2

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Components

#1: Protein
Gag-Pro-Pol polyprotein / Pr180


Mass: 12899.834 Da / Num. of mol.: 4 / Mutation: C7A, D26N, C106A; ENGINEERED MUTATIONS
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mason-Pfizer monkey virus / Gene: gag-pro-pol / Plasmid: pBPS13ATG
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P07572, dUTP diphosphatase, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases, RNA-directed DNA polymerase, DNA-directed DNA polymerase, ribonuclease H, ...References: UniProt: P07572, dUTP diphosphatase, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases, RNA-directed DNA polymerase, DNA-directed DNA polymerase, ribonuclease H, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases, Hydrolases; Acting on ester bonds
#2: Protein/peptide peptidomimetic inhibitor


Mass: 886.065 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: In the standard definition used by CCP4, the Cgamma atom of the PSA residue is labeled as CA. In the PDB Validation Report this label is interpreted as Calpha causing geometrical alerts. ...Details: In the standard definition used by CCP4, the Cgamma atom of the PSA residue is labeled as CA. In the PDB Validation Report this label is interpreted as Calpha causing geometrical alerts. These alerts are false and should be ignored.
Source: (synth.) synthetic construct (others)
#3: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 169 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.48 Å3/Da / Density % sol: 50.5 % / Description: plate
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: Protein solution: 8.5 mg/mL protein with 1.2-fold molar excess (relative to dimeric protein) of the inhibitor, 10 mM Tris buffer pH 7.4; Reservoir solution: 0.1 M sodium citrate buffer, 6% ...Details: Protein solution: 8.5 mg/mL protein with 1.2-fold molar excess (relative to dimeric protein) of the inhibitor, 10 mM Tris buffer pH 7.4; Reservoir solution: 0.1 M sodium citrate buffer, 6% PEG8000, 5% propan-2-ol;

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X13 / Wavelength: 0.815 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Nov 30, 2007
RadiationMonochromator: Double Crystal Monochromator, Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.815 Å / Relative weight: 1
ReflectionResolution: 2.43→42.87 Å / Num. obs: 19062 / % possible obs: 99 % / Redundancy: 3.94 % / Biso Wilson estimate: 39.94 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.062 / Rrim(I) all: 0.071 / Net I/σ(I): 15.5
Reflection shellResolution: 2.43→2.58 Å / Rmerge(I) obs: 0.363 / Mean I/σ(I) obs: 3.83 / Num. unique obs: 3023 / CC1/2: 0.931 / Rrim(I) all: 0.421 / % possible all: 98

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6s1v, chain B

6s1v


Resolution: 2.433→42.863 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / Phase error: 26.86 / Stereochemistry target values: ML / Details: HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2362 954 5.01 %RANDOM
Rwork0.1796 18089 --
obs0.1825 19043 98.78 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 135.01 Å2 / Biso mean: 50.146 Å2 / Biso min: 21.9 Å2
Refinement stepCycle: final / Resolution: 2.433→42.863 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3525 0 32 170 3727
Biso mean--73.38 47.96 -
Num. residues----440
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0083679
X-RAY DIFFRACTIONf_angle_d1.0925015
X-RAY DIFFRACTIONf_chiral_restr0.066566
X-RAY DIFFRACTIONf_plane_restr0.007619
X-RAY DIFFRACTIONf_dihedral_angle_d17.1681403
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11F0X-RAY DIFFRACTION9.378TORSIONAL
12G0X-RAY DIFFRACTION9.378TORSIONAL
21A1938X-RAY DIFFRACTION9.378TORSIONAL
22B1938X-RAY DIFFRACTION9.378TORSIONAL
23C1938X-RAY DIFFRACTION9.378TORSIONAL
24D1938X-RAY DIFFRACTION9.378TORSIONAL
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.433-2.560.31861330.23122515X-RAY DIFFRACTION97
2.56-2.720.29861370.22352590X-RAY DIFFRACTION98
2.72-2.930.28441370.21652610X-RAY DIFFRACTION99
2.93-3.230.23971370.20192607X-RAY DIFFRACTION99
3.23-3.690.25051360.17742576X-RAY DIFFRACTION99
3.69-4.650.19691360.14442586X-RAY DIFFRACTION99
4.65-42.860.21541380.17032605X-RAY DIFFRACTION99
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)
10.5704-0.87511.41786.8451-6.1766.5039-0.2145-0.120.25620.3166-0.4544-0.5192-0.27470.40840.64890.2812-0.0988-0.01670.43680.0710.41965.43284.779431.7876
23.32972.2279-0.42637.0445-1.05613.24820.14440.0071-0.6852-0.1097-0.2833-0.37230.50330.19080.15940.33010.07510.06190.39270.01120.37020.6634-11.056432.6458
31.6947-0.9351-0.12821.8545-1.38882.18660.12270.9833-0.8222-0.8403-0.01250.29250.6112-0.0414-0.08420.8399-0.1094-0.08330.5247-0.17950.8373-8.7924-12.786219.7319
44.01731.32640.82757.74736.19238.49250.1145-0.1801-0.1928-0.4837-0.44870.0857-0.1662-0.59240.30370.25280.0477-0.02950.28620.06830.2943-3.1849-8.865236.129
55.07180.05311.13845.3668-0.18244.40630.1738-0.210.1594-0.1639-0.19110.4615-0.2784-0.2835-0.02730.38560.02280.04860.36810.10620.373-3.45133.035631.7093
64.91824.4923-1.74564.2174-2.54949.2292-0.93890.170.6601-1.28091.2124-0.6031-1.8204-0.8751-0.3240.72430.20260.02840.62640.00370.5273-9.390711.031429.1857
73.2712-4.70973.23977.764-4.53133.7563-0.224-0.00440.21190.02430.0715-0.07720.4092-1.22040.1220.3172-0.06210.06370.34390.02520.3183-11.29229.294620.8491
83.3258-2.0056-0.75914.25551.39927.54140.03970.4121-0.4352-0.3942-0.05130.26230.5103-0.11190.00140.3168-0.0953-0.02510.3499-0.00720.3464-3.0775.40598.4528
92.2339-0.3184-0.98829.75783.48794.78590.00630.2417-0.10010.20190.03070.25810.2857-0.2930.0120.1968-0.0058-0.06470.38460.02540.3257-1.679512.88289.6088
103.6904-0.4199-0.781.9911-1.12786.0991-0.0315-0.29690.03290.21420.0306-0.0926-0.3440.1247-0.02780.3515-0.0466-0.02260.37330.10150.3721-1.393410.688422.0135
115.09581.1269-1.84632.90732.5128.0622-0.39511.330.32140.75640.39040.25710.6057-0.54720.03540.4658-0.1283-0.12120.62990.13890.434-3.8722-33.5327-5.8955
123.84650.1971.52464.56-0.18233.4394-0.0552-0.23450.10460.39490.11860.0445-0.1458-0.4313-0.06460.31540.03950.04990.3130.03380.26820.0351-33.121313.3161
134.06093.2716-5.61382.6323-4.51827.75761.2191-0.35930.39061.5486-1.5056-1.2009-1.46190.33530.37041.0224-0.169-0.16440.8891-0.03780.637712.1857-20.115915.0628
144.1819-0.38750.58152.61613.43264.82120.189-0.16570.00110.13650.3199-0.4591-0.14910.0845-0.45910.2728-0.00940.03230.24980.03270.34174.8119-35.907513.3225
153.52470.95682.59242.6186-1.67985.26470.10620.3972-0.0762-0.1895-0.03770.01510.43210.6672-0.05860.32430.05020.01770.40760.08410.35195.0842-34.11830.884
164.51721.4424-1.35953.98822.26292.46870.00540.45670.5482-0.5277-0.32830.46960.06650.67150.35240.59280.12650.06730.426-0.01770.435210.0214-33.9889-9.7288
171.1610.3458-2.56357.64-3.48567.39290.081-0.40110.14290.2227-0.2032-0.38860.04730.14880.19160.33640.04630.05020.44480.09070.369413.1808-26.6528-6.4561
180.7006-1.44960.25235.9924-0.47412.4248-0.1898-0.20220.26520.30850.0922-0.0738-0.1576-0.23940.07680.2881-0.013-0.06890.3649-0.00870.35355.205-12.5929-7.4823
192.8997-0.5385-0.99747.39824.94049.32540.00210.02230.3480.2617-0.2427-0.1511-0.22150.1370.25730.2583-0.0415-0.07120.32810.10930.39192.9823-14.3927-12.7798
204.012-1.4135-0.01867.8719-2.05832.876-0.0365-0.2305-0.6654-0.16010.44320.82160.5142-0.0859-0.42380.3063-0.0137-0.0310.43580.15410.41222.9562-26.6464-8.9136
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:15)A1 - 15
2X-RAY DIFFRACTION2(chain A and resid 16:47)A16 - 47
3X-RAY DIFFRACTION3(chain A and resid 48:60)A48 - 60
4X-RAY DIFFRACTION4(chain A and resid 61:88)A61 - 88
5X-RAY DIFFRACTION5(chain A and resid 89:108)A89 - 108
6X-RAY DIFFRACTION6(chain B and resid 1:7)B1 - 7
7X-RAY DIFFRACTION7(chain B and resid 8:14)B8 - 14
8X-RAY DIFFRACTION8(chain B and resid 15:61)B15 - 61
9X-RAY DIFFRACTION9(chain B and resid 62:88)B62 - 88
10X-RAY DIFFRACTION10(chain B and resid 89:108)B89 - 108
11X-RAY DIFFRACTION11(chain C and resid 1:8)C1 - 8
12X-RAY DIFFRACTION12(chain C and resid 9:47)C9 - 47
13X-RAY DIFFRACTION13(chain C and resid 48:61)C48 - 61
14X-RAY DIFFRACTION14(chain C and resid 62:88)C62 - 88
15X-RAY DIFFRACTION15(chain C and resid 89:108)C89 - 108
16X-RAY DIFFRACTION16(chain D and resid 1:5)D1 - 5
17X-RAY DIFFRACTION17(chain D and resid 6:14)D6 - 14
18X-RAY DIFFRACTION18(chain D and resid 15:58)D15 - 58
19X-RAY DIFFRACTION19(chain D and resid 59:88)D59 - 88
20X-RAY DIFFRACTION20(chain D and resid 89:108)D89 - 108

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