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M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMfMeMgMhMiMjMkMlMnMmMoMpMqMrMsMtMuMvMwMxMyMzM{M|MM}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMM!MM M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMHMFMGMIMJMKMLMMMNMOMPMQMSMRMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMuMtMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M=M<M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMe(MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M'M&M(M)M*M+M,M-M.M/M0M1M2M3M5M4M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M~M}MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM\M[M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M-M,M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMe]q(KKKKKKKKKK K K K K KKKKKKKKKKKKKKKKKKK K!K"K#K$K%K&K'K(K)K*K+K,K-K.K/K0K1K2K3K4K5K6K8K7K9K:K;KK?K@KBKCKAKDKEKFKGKHKIKJKKKLKMKNKOKPKQKRKSKTKUKVKWKXKYKZK[K]K\K^K_K`KaKbKcKdKeKfKgKhKiKjKkKlKmKnKoKpKqKrKsKtKuKvKwKxKyKzK{K|K}K~KKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMfMeMgMhMiMjMkMlMnMmMoMpMqMrMsMtMuMvMwMxMyMzM{M|M~MM}MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMM M!MM"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMGMHMFMIMJMKMLMMMNMOMPMQMSMRMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMuMtMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M=M<M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMe(MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M'M&M(M)M*M+M,M-M.M/M0M1M2M3M5M4M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M~M}MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM\M[M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M-M,M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMeXq]qNaNN]q]q(X pdb_headerqKX$HEADER HYDROLASE 24-OCT-19 6L5T TITLE THE CRYSTAL STRUCTURE OF SADS-COV PAPAIN LIKE PROTEASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEPTIDASE C16; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PAPAIN LIKE PROTEASE; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SWINE ACUTE DIARRHEA SYNDROME CORONAVIRUS; SOURCE 3 ORGANISM_TAXID: 2032731; SOURCE 4 GENE: ORF1AB, ORF1AB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A-SUMO KEYWDS PROTEASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR C.P.FAN REVDAT 2 13-MAY-20 6L5T 1 JRNL REVDAT 1 2 08-APR-20 6L5T 0 JRNL AUTH L.WANG,W.HU,C.FAN JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF SADS-COV JRNL TITL 2 PAPAIN-LIKE PROTEASE 2. JRNL REF PROTEIN SCI. V. 29 1228 2020 JRNL REFN ESSN 1469-896X JRNL PMID 32216114 JRNL DOI 10.1002/PRO.3857 REMARK 2 REMARK 2 RESOLUTION. 1.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.15.2_3472 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 26899 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.181 REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.212 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1345 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 34.2600 - 3.7000 1.00 2747 144 0.1631 0.1849 REMARK 3 2 3.7000 - 2.9400 1.00 2588 137 0.1624 0.1820 REMARK 3 3 2.9400 - 2.5700 1.00 2574 135 0.1814 0.2286 REMARK 3 4 2.5700 - 2.3300 1.00 2553 134 0.1882 0.2282 REMARK 3 5 2.3300 - 2.1700 1.00 2536 134 0.1766 0.2207 REMARK 3 6 2.1700 - 2.0400 1.00 2528 134 0.1869 0.2204 REMARK 3 7 2.0400 - 1.9400 1.00 2528 132 0.1956 0.2436 REMARK 3 8 1.9400 - 1.8500 1.00 2518 132 0.2177 0.2711 REMARK 3 9 1.8500 - 1.7800 1.00 2489 132 0.2288 0.2416 REMARK 3 10 1.7800 - 1.7200 1.00 2493 131 0.2539 0.3175 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.182 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.285 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.82 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.11 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.013 1840 REMARK 3 ANGLE : 1.130 2500 REMARK 3 CHIRALITY : 0.078 285 REMARK 3 PLANARITY : 0.008 315 REMARK 3 DIHEDRAL : 3.602 1054 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 28.9797 38.6283 35.8902 REMARK 3 T TENSOR REMARK 3 T11: 0.1469 T22: 0.1826 REMARK 3 T33: 0.1510 T12: 0.0023 REMARK 3 T13: 0.0069 T23: -0.0318 REMARK 3 L TENSOR REMARK 3 L11: 0.6051 L22: 0.7679 REMARK 3 L33: 0.3551 L12: 0.3345 REMARK 3 L13: 0.1927 L23: -0.0799 REMARK 3 S TENSOR REMARK 3 S11: 0.0530 S12: -0.1106 S13: 0.0280 REMARK 3 S21: 0.0836 S22: -0.1118 S23: 0.0331 REMARK 3 S31: -0.0450 S32: -0.0392 S33: 0.0670 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6L5T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-19. REMARK 100 THE DEPOSITION ID IS D_1300014247. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JAN-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26961 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720 REMARK 200 RESOLUTION RANGE LOW (A) : 41.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.80 REMARK 200 R MERGE (I) : 0.11600 REMARK 200 R SYM (I) : 0.11600 REMARK 200 FOR THE DATA SET : 16.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 12.50 REMARK 200 R MERGE FOR SHELL (I) : 1.63600 REMARK 200 R SYM FOR SHELL (I) : 1.63600 REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: AUTOSOL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 36.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES (PH6.5), 0.1M CACL2, 16% PEG REMARK 280 20000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.11550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.17500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.25550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.17500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.11550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.25550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 1 REMARK 465 ASP A 2 REMARK 465 VAL A 3 REMARK 465 LYS A 4 REMARK 465 VAL A 5 REMARK 465 LYS A 6 REMARK 465 VAL A 7 REMARK 465 THR A 8 REMARK 465 ALA A 9 REMARK 465 ASP A 10 REMARK 465 GLY A 11 REMARK 465 ARG A 12 REMARK 465 ASN A 13 REMARK 465 ILE A 14 REMARK 465 ASN A 15 REMARK 465 ASP A 16 REMARK 465 VAL A 17 REMARK 465 ILE A 18 REMARK 465 VAL A 19 REMARK 465 THR A 20 REMARK 465 THR A 21 REMARK 465 ALA A 22 REMARK 465 GLU A 23 REMARK 465 THR A 24 REMARK 465 PHE A 25 REMARK 465 ASP A 26 REMARK 465 ALA A 27 REMARK 465 GLN A 28 REMARK 465 LEU A 29 REMARK 465 GLY A 30 REMARK 465 PRO A 31 REMARK 465 SER A 32 REMARK 465 ALA A 33 REMARK 465 ASN A 34 REMARK 465 GLY A 35 REMARK 465 ALA A 36 REMARK 465 GLU A 37 REMARK 465 SER A 38 REMARK 465 LEU A 39 REMARK 465 VAL A 40 REMARK 465 GLY A 41 REMARK 465 VAL A 42 REMARK 465 VAL A 43 REMARK 465 PRO A 44 REMARK 465 THR A 45 REMARK 465 PRO A 46 REMARK 465 THR A 47 REMARK 465 ASP A 48 REMARK 465 GLY A 49 REMARK 465 GLY A 50 REMARK 465 LYS A 51 REMARK 465 VAL A 52 REMARK 465 GLY A 250 REMARK 465 ASN A 251 REMARK 465 THR A 252 REMARK 465 ASP A 253 REMARK 465 ASN A 254 REMARK 465 SER A 292 REMARK 465 TYR A 293 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 VAL A 53 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD1 ASP A 279 O HOH A 501 1.84 REMARK 500 O HOH A 594 O HOH A 607 2.10 REMARK 500 O HOH A 679 O HOH A 683 2.14 REMARK 500 O HOH A 508 O HOH A 578 2.15 REMARK 500 O HOH A 532 O HOH A 661 2.17 REMARK 500 O HOH A 529 O HOH A 697 2.17 REMARK 500 O HOH A 650 O HOH A 657 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 663 O HOH A 700 1655 2.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 69 35.70 -99.36 REMARK 500 SER A 97 141.14 -174.35 REMARK 500 LYS A 114 64.86 66.51 REMARK 500 ASN A 212 31.25 74.44 REMARK 500 ASN A 290 62.14 34.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 180 SG REMARK 620 2 CYS A 183 SG 115.7 REMARK 620 3 CYS A 209 SG 112.7 114.6 REMARK 620 4 HIS A 211 ND1 103.1 101.0 108.0 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401 LINK SG CYS A 180 ZN ZN A 401 1555 1555 2.330 LINK SG CYS A 183 ZN ZN A 401 1555 1555 2.300 LINK SG CYS A 209 ZN ZN A 401 1555 1555 2.330 LINK ND1 HIS A 211 ZN ZN A 401 1555 1555 2.020 CISPEP 1 GLY A 237 PRO A 238 0 10.96 DBREF1 6L5T A 1 293 UNP A0A2P1G738_9NIDO DBREF2 6L5T A A0A2P1G738 1588 1880 SEQRES 1 A 293 LYS ASP VAL LYS VAL LYS VAL THR ALA ASP GLY ARG ASN SEQRES 2 A 293 ILE ASN ASP VAL ILE VAL THR THR ALA GLU THR PHE ASP SEQRES 3 A 293 ALA GLN LEU GLY PRO SER ALA ASN GLY ALA GLU SER LEU SEQRES 4 A 293 VAL GLY VAL VAL PRO THR PRO THR ASP GLY GLY LYS VAL SEQRES 5 A 293 VAL ASN THR VAL PRO ASP VAL ASN TRP SER LYS HIS PHE SEQRES 6 A 293 GLY PHE SER ASP ALA ALA ALA PHE ALA VAL LEU ASP HIS SEQRES 7 A 293 SER LYS PHE ALA PHE ASP SER GLU VAL VAL ASP GLY LYS SEQRES 8 A 293 ARG ALA LEU ALA ASP SER ASP ASN ASN CYS TRP VAL ASN SEQRES 9 A 293 ALA THR CYS LEU ALA LEU GLN PHE LEU LYS PRO THR PHE SEQRES 10 A 293 LYS TYR VAL GLY TRP GLU ASP LEU TRP ASN LYS PHE VAL SEQRES 11 A 293 THR GLY ASP VAL ALA GLY PHE VAL HIS LEU LEU TYR TYR SEQRES 12 A 293 ILE GLU GLY VAL ASP LYS GLY ALA LYS GLY ASP VAL GLU SEQRES 13 A 293 SER THR LEU SER LYS LEU ASP LYS TYR ILE VAL SER SER SEQRES 14 A 293 GLY SER VAL THR VAL GLU ARG SER THR LEU CYS ASP ARG SEQRES 15 A 293 CYS ASN SER THR VAL LYS THR VAL THR GLY ALA ILE ALA SEQRES 16 A 293 GLU ALA SER VAL ILE LEU ASN GLY HIS THR ASP GLY HIS SEQRES 17 A 293 CYS PRO HIS ASN PHE GLU TRP ARG VAL GLN VAL ILE GLY SEQRES 18 A 293 VAL LYS GLY ASP ILE ILE LEU LEU HIS SER GLY SER LEU SEQRES 19 A 293 LEU ASN GLY PRO TYR VAL TYR GLY ASP ALA TYR VAL ALA SEQRES 20 A 293 PHE SER GLY ASN THR ASP ASN GLY HIS TYR THR VAL PHE SEQRES 21 A 293 ASP ASN LYS LEU SER LYS MET TYR ASP GLY ILE LYS CYS SEQRES 22 A 293 VAL LYS THR THR LEU ASP THR LEU VAL ALA SER SER VAL SEQRES 23 A 293 VAL ILE ARG ASN GLY SER TYR HET ZN A 401 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ FORMUL 3 HOH *200(H2 O) HELIX 1 AA1 PRO A 57 GLY A 66 1 10 HELIX 2 AA2 ASP A 69 VAL A 75 1 7 HELIX 3 AA3 HIS A 78 ALA A 82 5 5 HELIX 4 AA4 ASN A 100 LYS A 114 1 15 HELIX 5 AA5 TYR A 119 THR A 131 1 13 HELIX 6 AA6 VAL A 134 GLY A 146 1 13 HELIX 7 AA7 ASP A 154 ASP A 163 1 10 HELIX 8 AA8 LYS A 164 ILE A 166 5 3 HELIX 9 AA9 THR A 277 LEU A 281 5 5 SHEET 1 AA1 2 SER A 85 VAL A 88 0 SHEET 2 AA1 2 LYS A 91 LEU A 94 -1 O ALA A 93 N GLU A 86 SHEET 1 AA2 4 THR A 186 GLY A 192 0 SHEET 2 AA2 4 GLY A 170 SER A 177 -1 N ARG A 176 O THR A 186 SHEET 3 AA2 4 GLU A 214 GLY A 224 -1 O ARG A 216 N SER A 177 SHEET 4 AA2 4 HIS A 204 HIS A 208 -1 N HIS A 204 O VAL A 217 SHEET 1 AA3 7 ILE A 194 GLU A 196 0 SHEET 2 AA3 7 ILE A 226 LEU A 229 1 O LEU A 229 N ALA A 195 SHEET 3 AA3 7 VAL A 282 ILE A 288 -1 O ILE A 288 N ILE A 226 SHEET 4 AA3 7 ALA A 244 PHE A 248 -1 N ALA A 244 O VAL A 287 SHEET 5 AA3 7 TYR A 257 ASP A 261 -1 O PHE A 260 N TYR A 245 SHEET 6 AA3 7 LYS A 266 ASP A 269 -1 O LYS A 266 N ASP A 261 SHEET 7 AA3 7 LYS A 272 LYS A 275 -1 O VAL A 274 N MET A 267 SITE 1 AC1 4 CYS A 180 CYS A 183 CYS A 209 HIS A 211 CRYST1 81.986 81.986 134.345 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012197 0.007042 0.000000 0.00000 SCALE2 0.000000 0.014084 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007444 0.00000 qeaNN]q(]q(]q(G@TG@TG@` @e]q(G@VG@VG@^eeXP 32 2 1qeeaN]q (]q!(KKKJKKKe]q"(KKKJKKKe]q#(KKKJKKKe]q$(KKKJKKKe]q%(KKKJKKKe]q&(KKKJKKKe]q'(KKKJKKKe]q((KK KJKKKe]q)(KKKJKKKe]q*(KK KJKKKe]q+(K K KJKKKe]q,(K K KJKKKe]q-(K K KJKKKe]q.(K KKJKKKe]q/(KKKJKKKe]q0(KKKJKKKe]q1(KKKJKKKe]q2(KKKJKKKe]q3(KKKJKKKe]q4(KKKJKKKe]q5(KKKJKKKe]q6(KKKJKKKe]q7(KKKJKKKe]q8(KKKJKKKe]q9(KKKJKKKe]q:(KKKJKKKe]q;(KKKJKKKe]q<(KKKJKKKe]q=(KK!KJKKKe]q>(KKKJKKKe]q?(KKKJKKKe]q@(KKKJKKKe]qA(KK"KJKKKe]qB(KK KJKKKe]qC(K 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M" M# M$ M% M& M' M( M) M* M+ M, M- M. M/ M0 M1 M2 M3 M4 M5 M6 M7 M8 M9 M: M< M; M= M> M? M@ MA MB MC MD ME MF MG MH MI MJ MK ML MM MN MO MP MQ MR MS MT MU MV MW MX MY MZ M[ M\ M] M^ M_ M` Ma Mb Mc Md Me Mf Mg Mh Mi Mj Mk Ml Mm Mn Mo Mp Mq Mr Ms Mt Mu Mv Mw Mx My Mz M{ M| M} M~ M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M! M" M# M$ M% M& M' M( M) M* M+ M, M- M. M/ M0 M1 M2 M3 M4 M5 M6 M7 M8 M9 M: M; M< M= M> M? 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M" M# M$ M% M& M' M( M) M* M+ M, M- M. M/ M0 M1 M2 M3 M4 M5 M6 M7 M8 M9 M: M< M; M= M> M? M@ MA MB MC MD ME MF MG MH MI MJ MK ML MM MN MO MP MQ MR MS MT MU MV MW MX MY MZ M[ M\ M] M^ M_ M` Ma Mb Mc Md Me Mf Mg Mh Mi Mj Mk Ml Mm Mn Mo Mp Mq Mr Ms Mt Mu Mv Mw Mx My Mz M{ M| M} M~ M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M! M" M# M$ M% M& M' M( M) M* M+ M, M- M. M/ M0 M1 M2 M3 M4 M5 M6 M7 M8 M9 M: M; M< M= M> M? M@ MA MB MC MD ME MF MG MH MI MJ MK ML MM MN MO MP MQ MR MS MT MU MV MW MX MY MZ M[ M\ M] M^ M_ M` Ma Mb Mc Md Me Mf Mg Mh Mi Mj Mk Ml Mm Mn Mo Mp Mq Mr Ms Mt Mu Mv Mw Mx My Mz M{ M| M} M~ M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M M eh]r%#NaNN]r&#]r'#(X pdb_headerr(#KXHEADER HYDROLASE 14-MAY-20 6WZU TITLE THE CRYSTAL STRUCTURE OF PAPAIN-LIKE PROTEASE OF SARS COV-2 , P3221 TITLE 2 SPACE GROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: NON-STRUCTURAL PROTEIN 3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PAPAIN-LIKE PROTEINASE,PP1AB,ORF1AB POLYPROTEIN,NSP3,PL2- COMPND 5 PRO,PAPAIN-LIKE PROTEASE,PL-PRO; COMPND 6 EC: 3.4.19.121, 3.4.22.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: REP, 1A-1B; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG53 KEYWDS COVID-19, CORONAVIRUS, SARS, COV-2, PAPAIN-LIKE PROTEASE, IDP51000, KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, KEYWDS 3 HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR J.OSIPIUK,C.TESAR,M.ENDRES,R.JEDRZEJCZAK,A.JOACHIMIAK,CENTER FOR AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID) REVDAT 3 10-FEB-21 6WZU 1 JRNL REVDAT 2 27-JAN-21 6WZU 1 COMPND REVDAT 1 27-MAY-20 6WZU 0 JRNL AUTH J.OSIPIUK,S.A.AZIZI,S.DVORKIN,M.ENDRES,R.JEDRZEJCZAK, JRNL AUTH 2 K.A.JONES,S.KANG,R.S.KATHAYAT,Y.KIM,V.G.LISNYAK,S.L.MAKI, JRNL AUTH 3 V.NICOLAESCU,C.A.TAYLOR,C.TESAR,Y.A.ZHANG,Z.ZHOU,G.RANDALL, JRNL AUTH 4 K.MICHALSKA,S.A.SNYDER,B.C.DICKINSON,A.JOACHIMIAK JRNL TITL STRUCTURE OF PAPAIN-LIKE PROTEASE FROM SARS-COV-2 AND ITS JRNL TITL 2 COMPLEXES WITH NON-COVALENT INHIBITORS. JRNL REF NAT COMMUN V. 12 743 2021 JRNL REFN ESSN 2041-1723 JRNL PMID 33531496 JRNL DOI 10.1038/S41467-021-21060-3 REMARK 2 REMARK 2 RESOLUTION. 1.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.84 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 47056 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.161 REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.174 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2498 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.79 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3320 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.2500 REMARK 3 BIN FREE R VALUE SET COUNT : 209 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2502 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 25 REMARK 3 SOLVENT ATOMS : 223 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.18000 REMARK 3 B22 (A**2) : 0.18000 REMARK 3 B33 (A**2) : -0.58000 REMARK 3 B12 (A**2) : 0.09000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.082 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.820 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2666 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 2380 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3637 ; 1.492 ; 1.658 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5579 ; 1.421 ; 1.572 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 342 ; 5.885 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;41.303 ;24.091 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 460 ;13.659 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.243 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 356 ; 0.070 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2986 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 538 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 508 REMARK 3 ORIGIN FOR THE GROUP (A): 3.9837 80.5346 28.5665 REMARK 3 T TENSOR REMARK 3 T11: 0.0144 T22: 0.0101 REMARK 3 T33: 0.0025 T12: -0.0064 REMARK 3 T13: 0.0037 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 0.1930 L22: 0.3886 REMARK 3 L33: 0.3945 L12: 0.0299 REMARK 3 L13: -0.0047 L23: -0.2134 REMARK 3 S TENSOR REMARK 3 S11: 0.0103 S12: -0.0326 S13: 0.0117 REMARK 3 S21: 0.0322 S22: -0.0101 S23: 0.0123 REMARK 3 S31: 0.0367 S32: -0.0246 S33: -0.0002 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 6WZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1000249301. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49598 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790 REMARK 200 RESOLUTION RANGE LOW (A) : 48.840 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 14.20 REMARK 200 R MERGE (I) : 0.13700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 12.40 REMARK 200 R MERGE FOR SHELL (I) : 1.78100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.720 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: HKL-3000 REMARK 200 STARTING MODEL: 6WRH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M ACETATE BUFFER, 0.8 NAH2PO4/1.2 REMARK 280 M K2HPO4, SEEDS FROM PLPROTEASE C111S MUTANT CRYSTALS, PH 4.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.56333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.78167 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.78167 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 89.56333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A -2 REMARK 465 ASN A -1 REMARK 465 ALA A 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ILE A 14 -60.26 -122.73 REMARK 500 GLU A 143 77.31 -107.14 REMARK 500 LYS A 279 -127.36 -122.14 REMARK 500 ASN A 308 -69.53 -137.39 REMARK 500 ASN A 308 -68.60 -137.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 501 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 189 SG REMARK 620 2 CYS A 192 SG 114.2 REMARK 620 3 CYS A 224 SG 115.1 103.4 REMARK 620 4 CYS A 226 SG 105.4 108.8 109.9 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6W9C RELATED DB: PDB REMARK 900 PAPAIN-LIKE PROTEASE OF SARS COV-2, C2 SPACE GROUP REMARK 900 RELATED ID: 6WRH RELATED DB: PDB REMARK 900 PAPAIN-LIKE PROTEASE OF SARS COV-2 , C111S MUTANT REMARK 900 RELATED ID: IDP51000 RELATED DB: TARGETTRACK DBREF 6WZU A 1 315 UNP P0DTD1 R1AB_SARS2 1564 1878 SEQADV 6WZU SER A -2 UNP P0DTD1 CLONING ARTIFACT SEQADV 6WZU ASN A -1 UNP P0DTD1 CLONING ARTIFACT SEQADV 6WZU ALA A 0 UNP P0DTD1 CLONING ARTIFACT SEQRES 1 A 318 SER ASN ALA GLU VAL ARG THR ILE LYS VAL PHE THR THR SEQRES 2 A 318 VAL ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET SEQRES 3 A 318 SER MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU SEQRES 4 A 318 ASP GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER SEQRES 5 A 318 HIS GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP SEQRES 6 A 318 THR LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR SEQRES 7 A 318 ASP PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN SEQRES 8 A 318 HIS THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU SEQRES 9 A 318 THR SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA SEQRES 10 A 318 THR ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE SEQRES 11 A 318 ASN PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG SEQRES 12 A 318 ALA GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA SEQRES 13 A 318 TYR CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG SEQRES 14 A 318 GLU THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SEQRES 15 A 318 SER CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS SEQRES 16 A 318 GLY GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL SEQRES 17 A 318 MET TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS SEQRES 18 A 318 GLY VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR SEQRES 19 A 318 LYS TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET SEQRES 20 A 318 SER ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR SEQRES 21 A 318 PHE THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS SEQRES 22 A 318 GLY HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR SEQRES 23 A 318 CYS ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR SEQRES 24 A 318 LYS GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER SEQRES 25 A 318 TYR THR THR THR ILE LYS HET ZN A 501 1 HET GOL A 502 6 HET PO4 A 503 5 HET PO4 A 504 5 HET CL A 505 1 HET CL A 506 1 HET GOL A 507 6 HETNAM ZN ZINC ION HETNAM GOL GLYCEROL HETNAM PO4 PHOSPHATE ION HETNAM CL CHLORIDE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 ZN ZN 2+ FORMUL 3 GOL 2(C3 H8 O3) FORMUL 4 PO4 2(O4 P 3-) FORMUL 6 CL 2(CL 1-) FORMUL 9 HOH *223(H2 O) HELIX 1 AA1 THR A 26 GLY A 32 1 7 HELIX 2 AA2 HIS A 47 GLU A 51 5 5 HELIX 3 AA3 ASP A 61 HIS A 73 1 13 HELIX 4 AA4 SER A 78 LYS A 91 1 14 HELIX 5 AA5 ASN A 110 GLN A 121 1 12 HELIX 6 AA6 PRO A 129 ALA A 141 1 13 HELIX 7 AA7 ALA A 144 CYS A 155 1 12 HELIX 8 AA8 ASP A 164 HIS A 175 1 12 HELIX 9 AA9 GLY A 201 VAL A 205 1 5 HELIX 10 AB1 SER A 212 GLY A 219 1 8 SHEET 1 AA1 5 HIS A 17 ASP A 22 0 SHEET 2 AA1 5 THR A 4 THR A 10 -1 N ILE A 5 O VAL A 21 SHEET 3 AA1 5 THR A 54 VAL A 57 1 O PHE A 55 N PHE A 8 SHEET 4 AA1 5 THR A 34 LEU A 36 -1 N TYR A 35 O TYR A 56 SHEET 5 AA1 5 ALA A 39 ASP A 40 -1 O ALA A 39 N LEU A 36 SHEET 1 AA2 2 GLN A 97 VAL A 98 0 SHEET 2 AA2 2 LEU A 101 THR A 102 -1 O LEU A 101 N VAL A 98 SHEET 1 AA3 4 GLY A 193 LYS A 200 0 SHEET 2 AA3 4 LYS A 182 CYS A 189 -1 N ARG A 183 O LEU A 199 SHEET 3 AA3 4 GLN A 229 GLU A 238 -1 O THR A 231 N VAL A 188 SHEET 4 AA3 4 VAL A 220 PRO A 223 -1 N ILE A 222 O ALA A 230 SHEET 1 AA4 4 GLY A 193 LYS A 200 0 SHEET 2 AA4 4 LYS A 182 CYS A 189 -1 N ARG A 183 O LEU A 199 SHEET 3 AA4 4 GLN A 229 GLU A 238 -1 O THR A 231 N VAL A 188 SHEET 4 AA4 4 SER A 309 THR A 311 -1 O TYR A 310 N GLN A 237 SHEET 1 AA5 7 MET A 206 MET A 208 0 SHEET 2 AA5 7 PHE A 241 LYS A 254 1 O SER A 245 N TYR A 207 SHEET 3 AA5 7 GLU A 295 LYS A 306 -1 O VAL A 303 N MET A 244 SHEET 4 AA5 7 CYS A 260 GLY A 266 -1 N CYS A 260 O PHE A 304 SHEET 5 AA5 7 GLY A 271 SER A 278 -1 O LYS A 274 N GLU A 263 SHEET 6 AA5 7 LEU A 282 ASP A 286 -1 O TYR A 283 N THR A 277 SHEET 7 AA5 7 LEU A 289 SER A 293 -1 O LEU A 289 N ASP A 286 LINK SG CYS A 189 ZN ZN A 501 1555 1555 2.28 LINK SG CYS A 192 ZN ZN A 501 1555 1555 2.38 LINK SG CYS A 224 ZN ZN A 501 1555 1555 2.32 LINK SG CYS A 226 ZN ZN A 501 1555 1555 2.30 SITE 1 AC1 4 CYS A 189 CYS A 192 CYS A 224 CYS A 226 SITE 1 AC2 3 SER A 85 ASN A 88 HIS A 89 SITE 1 AC3 2 HIS A 47 SER A 49 SITE 1 AC4 7 HIS A 73 ASN A 128 PRO A 129 GLN A 174 SITE 2 AC4 7 HIS A 175 GLU A 203 HOH A 626 SITE 1 AC5 2 PHE A 127 HOH A 649 SITE 1 AC6 5 THR A 10 VAL A 11 ASP A 12 ASN A 15 SITE 2 AC6 5 GLU A 67 SITE 1 AC7 6 ARG A 65 ASP A 164 TYR A 264 TYR A 273 SITE 2 AC7 6 THR A 301 HOH A 614 CRYST1 81.986 81.986 134.345 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012197 0.007042 0.000000 0.00000 SCALE2 0.000000 0.014084 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007444 0.00000 r)#eaNN]r*#(]r+#(]r,#(G@TG@TG@` @e]r-#(G@VG@VG@^eeXP 32 2 1r.#eeaN]r/#(]r0#(KKKJKKKe]r1#(KKKJKKKe]r2#(KKKJKKKe]r3#(KKKJKKKe]r4#(KK KJKKKe]r5#(KKKJKKKe]r6#(KKKJKKKe]r7#(KKKJKKKe]r8#(KKKJKKKe]r9#(K K KJKKKe]r:#(K K KJKKKe]r;#(K K KJKKKe]r<#(K K KJKKKe]r=#(K KKJKKKe]r>#(K KKJKKKe]r?#(K 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KKKKGGGGGGhNe]r,S(MjShX675r-ShXHOHr.SjbjbhhhKKKG@CPG?G?QGKKKKMt KJKKKKKKKMCKKGMr KKKKGGGGGGhNe]r/S(MjShX676r0ShXHOHr1SjbjbhhhKKKG@Jj=G?G?QGKKKKMu KJKKKKKKKMDKKGMs KKKKGGGGGGhNe]r2S(MjShX677r3ShXHOHr4SjbjbhhhKKKG@JO\ G?G?QGKKKKMv KJKKKKKKKMEKKGMt KKKKGGGGGGhNe]r5S(MjShX678r6ShXHOHr7SjbjbhhhKKKG@ENG?G?QGKKKKMw KJKKKKKKKMFKKGMu KKKKGGGGGGhNe]r8S(MjShX679r9ShXHOHr:SjbjbhhhKKKG@AGG?G?QGKKKKMx KJKKKKKKKMGKKGMv KKKKGGGGGGhNe]r;S(MjShX680rS(MjShX681r?ShXHOHr@SjbjbhhhKKKG@F G?G?QGKKKKMz KJKKKKKKKMIKKGMx KKKKGGGGGGhNe]rAS(MjShX682rBShXHOHrCSjbjbhhhKKKG@: G?G?QGKKKKM{ KJKKKKKKKMJKKGMy KKKKGGGGGGhNe]rDS(MjShX683rEShXHOHrFSjbjbhhhKKKG@HG?G?QGKKKKM| KJKKKKKKKMKKKGMz KKKKGGGGGGhNe]rGS(MjShX684rHShXHOHrISjbjbhhhKKKG@H1G?G?QGKKKKM} KJKKKKKKKMLKKGM{ KKKKGGGGGGhNe]rJS(MjShX685rKShXHOHrLSjbjbhhhKKKG@C"`G?G?QGKKKKM~ KJKKKKKKKMMKKGM| KKKKGGGGGGhNe]rMS(MjShX686rNShXHOHrOSjbjbhhhKKKG@HzG?G?QGKKKKM KJKKKKKKKMNKKGM} KKKKGGGGGGhNe]rPS(MjShX687rQShXHOHrRSjbjbhhhKKKG@K/\ G?G?QGKKKKM KJKKKKKKKMOKKGM~ KKKKGGGGGGhNe]rSS(MjShX688rTShXHOHrUSjbjbhhhKKKG@K\ G?G?QGKKKKM KJKKKKKKKMPKKGM KKKKGGGGGGhNe]rVS(MjShX689rWShXHOHrXSjbjbhhhKKKG@I=G?G?QGKKKKM KJKKKKKKKMQKKGM KKKKGGGGGGhNe]rYS(MjShX690rZShXHOHr[SjbjbhhhKKKG@B`G?G?QGKKKKM KJKKKKKKKMRKKGM KKKKGGGGGGhNe]r\S(MjShX691r]ShXHOHr^SjbjbhhhKKKG@M^`G?G?QGKKKKM KJKKKKKKKMSKKGM KKKKGGGGGGhNe]r_S(MjShX692r`ShXHOHraSjbjbhhhKKKG@@G?G?QGKKKKM KJKKKKKKKMTKKGM KKKKGGGGGGhNe]rbS(MjShX693rcShXHOHrdSjbjbhhhKKKG@HG?G?QGKKKKM KJKKKKKKKMUKKGM KKKKGGGGGGhNe]reS(MjShX694rfShXHOHrgSjbjbhhhKKKG@H޸`G?G?QGKKKKM KJKKKKKKKMVKKGM KKKKGGGGGGhNe]rhS(MjShX695riShXHOHrjSjbjbhhhKKKG@BzG?G?QGKKKKM KJKKKKKKKMWKKGM KKKKGGGGGGhNe]rkS(MjShX696rlShXHOHrmSjbjbhhhKKKG@F)G?G?QGKKKKM KJKKKKKKKMXKKGM KKKKGGGGGGhNe]rnS(MjShX697roShXHOHrpSjbjbhhhKKKG@HG?G?QGKKKKM KJKKKKKKKMYKKGM KKKKGGGGGGhNe]rqS(MjShX698rrShXHOHrsSjbjbhhhKKKG@If`G?G?QGKKKKM KJKKKKKKKMZKKGM KKKKGGGGGGhNe]rtS(MjShX699ruShXHOHrvSjbjbhhhKKKG@BpG?G?QGKKKKM KJKKKKKKKM[KKGM KKKKGGGGGGhNe]rwS(MjShX700rxShXHOHrySjbjbhhhKKKG@CG?G?QGKKKKM KJKKKKKKKM\KKGM KKKKGGGGGGhNe]rzS(MjShX701r{ShXHOHr|SjbjbhhhKKKG@@ G?G?QGKKKKM KJKKKKKKKM]KKGM KKKKGGGGGGhNe]r}S(MjShX702r~ShXHOHrSjbjbhhhKKKG@@ff`G?G?QGKKKKM KJKKKKKKKM^KKGM KKKKGGGGGGhNe]rS(MjShX703rShXHOHrSjbjbhhhKKKG@Ew @G?G?QGKKKKM KJKKKKKKKM_KKGM KKKKGGGGGGhNe]rS(MjShX704rShXHOHrSjbjbhhhKKKG@F*=G?G?QGKKKKM KJKKKKKKKM`KKGM KKKKGGGGGGhNe]rS(MjShX705rShXHOHrSjbjbhhhKKKG@E G?G?QGKKKKM KJKKKKKKKMaKKGM KKKKGGGGGGhNe]rS(MjShX706rShXHOHrSjbjbhhhKKKG@F G?G?QGKKKKM KJKKKKKKKMbKKGM KKKKGGGGGGhNe]rS(MjShX707rShXHOHrSjbjbhhhKKKG@B=G?G?QGKKKKM KJKKKKKKKMcKKGM KKKKGGGGGGhNe]rS(MjShX708rShXHOHrSjbjbhhhKKKG@? @G?G?QGKKKKM KJKKKKKKKMdKKGM KKKKGGGGGGhNe]rS(MjShX709rShXHOHrSjbjbhhhKKKG@JTzG?G?QGKKKKM KJKKKKKKKMeKKGM KKKKGGGGGGhNe]rS(MjShX710rShXHOHrSjbjbhhhKKKG@EU€G?G?QGKKKKM KJKKKKKKKMfKKGM KKKKGGGGGGhNe]rS(MjShX711rShXHOHrSjbjbhhhKKKG@LTzG?G?QGKKKKM KJKKKKKKKMgKKGM KKKKGGGGGGhNe]rS(MjShX712rShXHOHrSjbjbhhhKKKG@GG?G?QGKKKKM KJKKKKKKKMhKKGM KKKKGGGGGGhNe]rS(MjShX713rShXHOHrSjbjbhhhKKKG@E1G?G?QGKKKKM KJKKKKKKKMiKKGM KKKKGGGGGGhNe]rS(MjShX714rShXHOHrSjbjbhhhKKKG@@€G?G?QGKKKKM KJKKKKKKKMjKKGM KKKKGGGGGGhNe]rS(MjShX715rShXHOHrSjbjbhhhKKKG@CB`G?G?QGKKKKM KJKKKKKKKMkKKGM KKKKGGGGGGhNe]rS(MjShX716rShXHOHrSjbjbhhhKKKG@IJ=G?G?QGKKKKM KJKKKKKKKMlKKGM KKKKGGGGGGhNe]rS(MjShX717rShXHOHrSjbjbhhhKKKG@@33@G?G?QGKKKKM KJKKKKKKKMmKKGM KKKKGGGGGGhNe]rS(MjShX718rShXHOHrSjbjbhhhKKKG@ACG?G?QGKKKKM KJKKKKKKKMnKKGM KKKKGGGGGGhNe]rS(MjShX719rShXHOHrSjbjbhhhKKKG@C#G?G?QGKKKKM KJKKKKKKKMoKKGM KKKKGGGGGGhNe]rS(MjShX720rShXHOHrSjbjbhhhKKKG@DaGG?G?QGKKKKM KJKKKKKKKMpKKGM KKKKGGGGGGhNe]rS(MjShX721rShXHOHrSjbjbhhhKKKG@FJ=G?G?QGKKKKM KJKKKKKKKMqKKGM KKKKGGGGGGhNe]rS(MjShX722rShXHOHrSjbjbhhhKKKG@B:@G?G?QGKKKKM KJKKKKKKKMrKKGM KKKKGGGGGGhNe]rS(MjShX723rShXHOHrSjbjbhhhKKKG@EpG?G?QGKKKKM KJKKKKKKKMsKKGM KKKKGGGGGGhNe]rS(MjShX724rShXHOHrSjbjbhhhKKKG@B0G?G?QGKKKKM KJKKKKKKKMtKKGM KKKKGGGGGGhNe]rS(MjShX725rShXHOHrSjbjbhhhKKKG@FGG?G?QGKKKKM KJKKKKKKKMuKKGM KKKKGGGGGGhNe]rS(MjShX726rShXHOHrSjbjbhhhKKKG@HQG?G?QGKKKKM KJKKKKKKKMvKKGM KKKKGGGGGGhNe]rS(MjShX727rShXHOHrSjbjbhhhKKKG@C @G?G?QGKKKKM KJKKKKKKKMwKKGM KKKKGGGGGGhNe]rS(MjShX728rShXHOHrSjbjbhhhKKKG@@3@G?G?QGKKKKM KJKKKKKKKMxKKGM KKKKGGGGGGhNe]rS(MjShX729rShXHOHrSjbjbhhhKKKG@FJ=G?G?QGKKKKM KJKKKKKKKMyKKGM KKKKGGGGGGhNe]rS(MjShX730rShXHOHrSjbjbhhhKKKG@F=G?G?QGKKKKM KJKKKKKKKMzKKGM KKKKGGGGGGhNe]rS(MjShX731rShXHOHrSjbjbhhhKKKG@EG?G?QGKKKKM KJKKKKKKKM{KKGM KKKKGGGGGGhNe]rS(MjShX732rShXHOHrSjbjbhhhKKKG@HzG?G?QGKKKKM KJKKKKKKKM|KKGM KKKKGGGGGGhNe]rS(MjShX733rShXHOHrSjbjbhhhKKKG@A' G?G?QGKKKKM KJKKKKKKKM}KKGM KKKKGGGGGGhNe]rS(MjShX734rShXHOHrSjbjbhhhKKKG@D€G?G?QGKKKKM KJKKKKKKKM~KKGM KKKKGGGGGGhNe]rS(MjShX735rShXHOHrSjbjbhhhKKKG@I3@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX736rShXHOHrSjbjbhhhKKKG@DG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX737rShXHOHrSjbjbhhhKKKG@>G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX738rShXHOHrSjbjbhhhKKKG@=f`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX739rShXHOHrSjbjbhhhKKKG@@`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX740rShXHOHrSjbjbhhhKKKG@JQG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX741rShXHOHrSjbjbhhhKKKG@I`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX742rShXHOHrSjbjbhhhKKKG@G)G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX743rShXHOHrSjbjbhhhKKKG@DxQG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX744rShXHOHrSjbjbhhhKKKG@H`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rS(MjShX745rShXHOHrTjbjbhhhKKKG@EG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX746rThXHOHrTjbjbhhhKKKG@I^`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX747rThXHOHrTjbjbhhhKKKG@HG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX748rThXHOHr TjbjbhhhKKKG@JK G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r T(MjShX749r ThXHOHr TjbjbhhhKKKG@KpG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r T(MjShX750rThXHOHrTjbjbhhhKKKG@C>`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX751rThXHOHrTjbjbhhhKKKG@@=G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX752rThXHOHrTjbjbhhhKKKG@H G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX753rThXHOHrTjbjbhhhKKKG@C@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX754rThXHOHrTjbjbhhhKKKG@F3@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX755rThXHOHrTjbjbhhhKKKG@H=G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX756r ThXHOHr!TjbjbhhhKKKG@BG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r"T(MjShX757r#ThXHOHr$TjbjbhhhKKKG@Gf`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r%T(MjShX758r&ThXHOHr'TjbjbhhhKKKG@@*=G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r(T(MjShX759r)ThXHOHr*TjbjbhhhKKKG@A`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r+T(MjShX760r,ThXHOHr-TjbjbhhhKKKG@JPG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r.T(MjShX761r/ThXHOHr0TjbjbhhhKKKG@HG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r1T(MjShX762r2ThXHOHr3TjbjbhhhKKKG@D3@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r4T(MjShX763r5ThXHOHr6TjbjbhhhKKKG@FPG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r7T(MjShX764r8ThXHOHr9TjbjbhhhKKKG@JzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r:T(MjShX765r;ThXHOHrThXHOHr?TjbjbhhhKKKG@HGG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r@T(MjShX767rAThXHOHrBTjbjbhhhKKKG@BzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rCT(MjShX768rDThXHOHrETjbjbhhhKKKG@L)G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rFT(MjShX769rGThXHOHrHTjbjbhhhKKKG@GG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rIT(MjShX770rJThXHOHrKTjbjbhhhKKKG@D~`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rLT(MjShX771rMThXHOHrNTjbjbhhhKKKG@@QG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rOT(MjShX772rPThXHOHrQTjbjbhhhKKKG@J9G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rRT(MjShX773rSThXHOHrTTjbjbhhhKKKG@I' G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rUT(MjShX774rVThXHOHrWTjbjbhhhKKKG@Bu€G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rXT(MjShX775rYThXHOHrZTjbjbhhhKKKG@A' G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r[T(MjShX776r\ThXHOHr]TjbjbhhhKKKG@GG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r^T(M jShX777r_ThXHOHr`TjbjbhhhKKKG@BAGG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]raT(M jShX778rbThXHOHrcTjbjbhhhKKKG@JQG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rdT(M jShX779reThXHOHrfTjbjbhhhKKKG@K=G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rgT(M jShX780rhThXHOHriTjbjbhhhKKKG@BG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rjT(M jShX781rkThXHOHrlTjbjbhhhKKKG@BG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rmT(MjShX782rnThXHOHroTjbjbhhhKKKG@HG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rpT(MjShX783rqThXHOHrrTjbjbhhhKKKG@L5€G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rsT(MjShX784rtThXHOHruTjbjbhhhKKKG@K`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rvT(MjShX785rwThXHOHrxTjbjbhhhKKKG@Cb`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]ryT(MjShX786rzThXHOHr{TjbjbhhhKKKG@JG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]r|T(MjShX787r}ThXHOHr~TjbjbhhhKKKG@Ff`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX788rThXHOHrTjbjbhhhKKKG@J G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX789rThXHOHrTjbjbhhhKKKG@L`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX790rThXHOHrTjbjbhhhKKKG@GyG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX791rThXHOHrTjbjbhhhKKKG@L\ G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX792rThXHOHrTjbjbhhhKKKG@GHG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX793rThXHOHrTjbjbhhhKKKG@JG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX794rThXHOHrTjbjbhhhKKKG@GzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX795rThXHOHrTjbjbhhhKKKG@L)G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX796rThXHOHrTjbjbhhhKKKG@IzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX797rThXHOHrTjbjbhhhKKKG@@\ G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX798rThXHOHrTjbjbhhhKKKG@@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(MjShX799rThXHOHrTjbjbhhhKKKG@H|)G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M jShX800rThXHOHrTjbjbhhhKKKG@DG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M!jShX801rThXHOHrTjbjbhhhKKKG@I @G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M"jShX802rThXHOHrTjbjbhhhKKKG@J*=G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M#jShX803rThXHOHrTjbjbhhhKKKG@C"`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M$jShX804rThXHOHrTjbjbhhhKKKG@E' G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M%jShX805rThXHOHrTjbjbhhhKKKG@FG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M&jShX806rThXHOHrTjbjbhhhKKKG@I@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M'jShX807rThXHOHrTjbjbhhhKKKG@LG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M(jShX808rThXHOHrTjbjbhhhKKKG@K1G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M)jShX809rThXHOHrTjbjbhhhKKKG@JxQG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M*jShX810rThXHOHrTjbjbhhhKKKG@DNG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M+jShX811rThXHOHrTjbjbhhhKKKG@FG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M,jShX812rThXHOHrTjbjbhhhKKKG@K)G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M-jShX813rThXHOHrTjbjbhhhKKKG@JYG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M.jShX814rThXHOHrTjbjbhhhKKKG@EzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M/jShX815rThXHOHrTjbjbhhhKKKG@E`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M0jShX816rThXHOHrTjbjbhhhKKKG@Iff`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M1jShX817rThXHOHrTjbjbhhhKKKG@JУG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M2jShX818rThXHOHrTjbjbhhhKKKG@FGG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M3jShX819rThXHOHrTjbjbhhhKKKG@D~`G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M4jShX820rThXHOHrTjbjbhhhKKKG@B@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M5jShX821rThXHOHrTjbjbhhhKKKG@FzG?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M6jShX822rThXHOHrTjbjbhhhKKKG@D3@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNe]rT(M7jShX823rThXHOHrTjbjbhhhKKKG@HZ@G?G?QGKKKKM KJKKKKKKKMKKGM KKKKGGGGGGhNeeKK]rT(]rT(]rT(G@TG@TG@` @e]rT(G@VG@VG@^eeXP 32 2 1rTeKJM NNeheeXcolorsrT]rTX color_extrT]rTXunique_settingsrT]rTXselector_secretsrT]rTXsettingsrT]rT(]rT(K3KKe]rT(K