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`G@9X G?ꗍ@G>G G@"RG4+CG@6G#7@G.CG@7@G'&f`G1S@G@6G%`G(Gt`G@ 7KG.ȴ@G?;d`G#G-Ǯ G@*G@)~vG@9 G@8{G@A@G&zG@<G@ xG0%G@,B @GKƠGA㕀G@u€G@G@ 9`GjG@`G'7@G tG?`G&ۥG@25@G,bMG6G@7\ G =Ge]q(KKKKKKKKKKKKKKKKKKK K!K"K#K$K%K&K'K(K)K*K+K,K-K/K.K0K1K2K3K4K5K6K7K8K9K:K;KK?K@KAKBKCKDKEKFKGKHKIKJKKKLKMKNKOKPKQKRKTKSKUKVKWKXKYKZK[K]K\K^K_K`KaKbKcKdKeKfKgKhKiKjKkKlKmKnKoKpKqKrKsKtKuKvKwKxKyKzK{K|K}K~KKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M&M%M'M(M)M*M+M,M-M.M/M0M1M2M3M4M6M5M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMdMcMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M7M6M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMPMOMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMeMdMfMgMhMiMjMkMlMmMnMoMpMqMrMsMuMtMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMTMSMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMe(MMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M*M)M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMcMbMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMKKKKKK KKKKK K K K MMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"e]q(MMMMMMMMMMMMMMKKKKKKKKK K KK K K KKKKKKKKKKKKKKKKKKK!K K"K#K$K%K&K'K(K)K*K+K,K-K.K/K0K1K2K3K4K5K6K7K8K9K:K;KK?K@KAKBKCKDKFKEKGKHKIKJKKKLKMKOKNKPKQKRKSKTKUKVKWKXKYKZK[K\K]K^K_K`KaKbKcKdKeKfKgKhKiKjKkKlKmKnKoKpKqKrKsKtKuKvKwKxKyKzK{K|K}K~KKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKKMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M(M'M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMVMUMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M)M(M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MBMAMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMWMVMXMYMZM[M\M]M^M_M`MaMbMcMdMeMgMfMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMFMEMGMHMIMJMKMLMMMNMOMPMQMRMSMTMUMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMe(MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"M#M$M%M&M'M(M)M*M+M,M-M.M/M0M1M2M3M4M5M6M7M8M9M:M;M<M=M>M?M@MAMBMCMDMEMFMGMHMIMJMKMLMMMNMOMPMQMRMSMUMTMVMWMXMYMZM[M\M]M^M_M`MaMbMcMdMeMfMgMhMiMjMkMlMmMnMoMpMqMrMsMtMuMvMwMxMyMzM{M|M}M~MMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMM M M M M MMMMMMMMMMMMMMMMMMM M!M"eXq]qNaNN]q]q(X pdb_headerqKX]iHEADER HYDROLASE 08-APR-11 3RGO TITLE CRYSTAL STRUCTURE OF PTPMT1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE MITOCHONDRIAL 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PTEN-LIKE PHOSPHATASE, PHOSPHOINOSITIDE LIPID PHOSPHATASE; COMPND 5 EC: 3.1.3.16, 3.1.3.48; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: PLIP, PTPMT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28 KEYWDS PHOSPHATIDYLGLYCEROL PHOSPHATE (PGP) PHOSPHATASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR J.XIAO,J.L.ENGEL REVDAT 4 08-NOV-17 3RGO 1 REMARK REVDAT 3 03-AUG-11 3RGO 1 JRNL REVDAT 2 20-JUL-11 3RGO 1 JRNL REVDAT 1 06-JUL-11 3RGO 0 JRNL AUTH J.XIAO,J.L.ENGEL,J.ZHANG,M.J.CHEN,G.MANNING,J.E.DIXON JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF PTPMT1, A PHOSPHATASE JRNL TITL 2 REQUIRED FOR CARDIOLIPIN SYNTHESIS. JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 11860 2011 JRNL REFN ISSN 0027-8424 JRNL PMID 21730175 JRNL DOI 10.1073/PNAS.1109290108 REMARK 2 REMARK 2 RESOLUTION. 1.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.5_2 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 12667 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 618 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 34.7550 - 3.0594 1.00 3206 160 0.2231 0.2196 REMARK 3 2 3.0594 - 2.4286 1.00 3007 146 0.2245 0.2703 REMARK 3 3 2.4286 - 2.1216 1.00 2957 155 0.2304 0.2830 REMARK 3 4 2.1216 - 1.9280 0.99 2879 157 0.2499 0.3108 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.34 REMARK 3 B_SOL : 46.55 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.73050 REMARK 3 B22 (A**2) : 2.73050 REMARK 3 B33 (A**2) : -5.46100 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 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 : 0.004 1289 REMARK 3 ANGLE : 0.776 1743 REMARK 3 CHIRALITY : 0.055 198 REMARK 3 PLANARITY : 0.003 217 REMARK 3 DIHEDRAL : 16.639 473 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): 13.1083 -1.3176 -15.3095 REMARK 3 T TENSOR REMARK 3 T11: 0.3722 T22: 0.1683 REMARK 3 T33: 0.3159 T12: 0.0068 REMARK 3 T13: 0.1559 T23: -0.0307 REMARK 3 L TENSOR REMARK 3 L11: 2.1035 L22: 2.0857 REMARK 3 L33: 4.5529 L12: -0.0219 REMARK 3 L13: 0.1938 L23: 0.5842 REMARK 3 S TENSOR REMARK 3 S11: 0.0463 S12: -0.0883 S13: 0.0804 REMARK 3 S21: 0.0657 S22: -0.0658 S23: -0.1551 REMARK 3 S31: 0.0337 S32: 0.1107 S33: -0.0069 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 3RGO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-11. REMARK 100 THE DEPOSITION ID IS D_1000064908. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-DEC-09; 29-JAN-10 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ALS; ALS REMARK 200 BEAMLINE : 8.2.1; 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 0.9798, 0.9800, 0.9573 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; ADSC QUANTUM REMARK 200 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12762 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.928 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.70 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 13.20 REMARK 200 R MERGE FOR SHELL (I) : 0.70500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MME, BIS-TRIS, (NH4)2SO4, PH REMARK 280 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.01200 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 18.22650 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 18.22650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 172.51800 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 18.22650 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 18.22650 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.50600 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 18.22650 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 18.22650 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 172.51800 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 18.22650 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 18.22650 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.50600 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 115.01200 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 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 71 132.33 -34.94 REMARK 500 MET A 72 -5.41 72.17 REMARK 500 CYS A 102 -103.55 -124.87 REMARK 500 LYS A 103 -68.31 -103.81 REMARK 500 SER A 107 -75.83 -135.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3RGQ RELATED DB: PDB DBREF 3RGO A 7 163 UNP Q66GT5 PTPM1_MOUSE 37 193 SEQRES 1 A 157 TRP TYR HIS ARG ILE ASP HIS THR VAL LEU LEU GLY ALA SEQRES 2 A 157 LEU PRO LEU LYS ASN MET THR ARG ARG LEU VAL LEU ASP SEQRES 3 A 157 GLU ASN VAL ARG GLY VAL ILE THR MET ASN GLU GLU TYR SEQRES 4 A 157 GLU THR ARG PHE LEU CYS ASN THR SER LYS GLU TRP LYS SEQRES 5 A 157 LYS ALA GLY VAL GLU GLN LEU ARG LEU SER THR VAL ASP SEQRES 6 A 157 MET THR GLY VAL PRO THR LEU ALA ASN LEU HIS LYS GLY SEQRES 7 A 157 VAL GLN PHE ALA LEU LYS TYR GLN ALA LEU GLY GLN CYS SEQRES 8 A 157 VAL TYR VAL HIS CYS LYS ALA GLY ARG SER ARG SER ALA SEQRES 9 A 157 THR MET VAL ALA ALA TYR LEU ILE GLN VAL HIS ASN TRP SEQRES 10 A 157 SER PRO GLU GLU ALA ILE GLU ALA ILE ALA LYS ILE ARG SEQRES 11 A 157 SER HIS ILE SER ILE ARG PRO SER GLN LEU GLU VAL LEU SEQRES 12 A 157 LYS GLU PHE HIS LYS GLU ILE THR ALA ARG ALA ALA LYS SEQRES 13 A 157 ASN HET SO4 A 1 5 HET SO4 A 2 5 HETNAM SO4 SULFATE ION FORMUL 2 SO4 2(O4 S 2-) FORMUL 4 HOH *48(H2 O) HELIX 1 1 LEU A 22 ASN A 24 5 3 HELIX 2 2 MET A 25 GLU A 33 1 9 HELIX 3 3 THR A 53 ALA A 60 1 8 HELIX 4 4 THR A 77 GLY A 95 1 19 HELIX 5 5 SER A 107 ASN A 122 1 16 HELIX 6 6 SER A 124 ARG A 136 1 13 HELIX 7 7 ARG A 142 ALA A 161 1 20 SHEET 1 A 5 TYR A 8 ARG A 10 0 SHEET 2 A 5 VAL A 15 GLY A 18 -1 O LEU A 17 N HIS A 9 SHEET 3 A 5 CYS A 97 HIS A 101 1 O VAL A 100 N LEU A 16 SHEET 4 A 5 VAL A 35 MET A 41 1 N ARG A 36 O CYS A 97 SHEET 5 A 5 GLU A 63 LEU A 67 1 O LEU A 65 N VAL A 38 SITE 1 AC1 9 HOH A 5 CYS A 102 LYS A 103 ALA A 104 SITE 2 AC1 9 GLY A 105 ARG A 106 SER A 107 ARG A 108 SITE 3 AC1 9 SER A 109 SITE 1 AC2 8 ASN A 42 THR A 69 VAL A 70 ASP A 71 SITE 2 AC2 8 MET A 72 THR A 73 GLY A 74 ARG A 108 CRYST1 36.453 36.453 230.024 90.00 90.00 90.00 P 43 21 2 8 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 0.027433 0.000000 0.000000 0.00000 SCALE2 0.000000 0.027433 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004347 0.00000 qeaNN]q(]q(]q(G@B9G@B9G@lĠe]q(G@VG@VG@VeeX P 43 21 2qeeaN]q (]q!(KKKJKKKe]q"(KKKJKKKe]q#(KKKJKKKe]q$(KKKJKKKe]q%(K KKJKKKe]q&(K KKJKKKe]q'(K KKJKKKe]q((K KKJKKKe]q)(KKKJKKKe]q*(KKKJKKKe]q+(KKKJKKKe]q,(KKKJKKKe]q-(KKKJKKKe]q.(KKKJKKKe]q/(KKKJKKKe]q0(KKKJKKKe]q1(KKKJKKKe]q2(KKKJKKKe]q3(KKKJKKKe]q4(KKKJKKKe]q5(KKKJKKKe]q6(KKKJKKKe]q7(KKKJKKKe]q8(KKKJKKKe]q9(KKKJKKKe]q:(KKKJKKKe]q;(KK KJKKKe]q<(KKKJKKKe]q=(KK(KJKKKe]q>(K K!KJKKKe]q?(K!K"KJKKKe]q@(K!K#KJKKKe]qA(K"K$KJKKKe]qB(K#K%KJKKKe]qC(K$K&KJKKKe]qD(K%K&KJKKKe]qE(K&K'KJKKKe]qF(K(K)KJKKKe]qG(K)K*KJKKKe]qH(K)K,KJKKKe]qI(K*K+KJKKKe]qJ(K*K2KJKKKe]qK(K,K-KJKKKe]qL(K-K.KJKKKe]qM(K-K/KJKKKe]qN(K.K1KJKKKe]qO(K/K0KJKKKe]qP(K0K1KJKKKe]qQ(K2K3KJKKKe]qR(K3K4KJKKKe]qS(K3K6KJKKKe]qT(K4K5KJKKKe]qU(K4K=KJKKKe]qV(K6K7KJKKKe]qW(K7K8KJKKKe]qX(K8K9KJKKKe]qY(K9K:KJKKKe]qZ(K:K;KJKKKe]q[(K:KKJKKKe]q](K>K?KJKKKe]q^(K>KAKJKKKe]q_(K?K@KJKKKe]q`(K?KEKJKKKe]qa(KAKBKJKKKe]qb(KAKCKJKKKe]qc(KBKDKJKKKe]qd(KEKFKJKKKe]qe(KFKGKJKKKe]qf(KFKIKJKKKe]qg(KGKHKJKKKe]qh(KGKMKJKKKe]qi(KIKJKJKKKe]qj(KJKKKJKKKe]qk(KJKLKJKKKe]ql(KMKNKJKKKe]qm(KNKOKJKKKe]qn(KNKQKJKKKe]qo(KOKPKJKKKe]qp(KOKWKJKKKe]qq(KQKRKJKKKe]qr(KRKSKJKKKe]qs(KRKTKJKKKe]qt(KSKVKJKKKe]qu(KTKUKJKKKe]qv(KUKVKJKKKe]qw(KWKXKJKKKe]qx(KXKYKJKKKe]qy(KXK[KJKKKe]qz(KYKZKJKKKe]q{(KYK^KJKKKe]q|(K[K\KJKKKe]q}(K[K]KJKKKe]q~(K^K_KJKKKe]q(K_K`KJKKKe]q(K_KbKJKKKe]q(K`KaKJKKKe]q(K`KeKJKKKe]q(KbKcKJKKKe]q(KbKdKJKKKe]q(KeKfKJKKKe]q(KfKgKJKKKe]q(KfKiKJKKKe]q(KgKhKJKKKe]q(KgKmKJKKKe]q(KiKjKJKKKe]q(KjKkKJKKKe]q(KjKlKJKKKe]q(KmKnKJKKKe]q(KnKoKJKKKe]q(KnKqKJKKKe]q(KoKpKJKKKe]q(KoKuKJKKKe]q(KqKrKJKKKe]q(KrKsKJKKKe]q(KrKtKJKKKe]q(KuKvKJKKKe]q(KvKwKJKKKe]q(KwKxKJKKKe]q(KwKyKJKKKe]q(KyKzKJKKKe]q(KzK{KJKKKe]q(KzK}KJKKKe]q(K{K|KJKKKe]q(K{K~KJKKKe]q(K~KKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]q(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r(KKKJKKKe]r 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