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HEADER HYDROLASE 01-FEB-08 3C5V
TITLE PP2A-SPECIFIC METHYLESTERASE APO FORM (PME)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN PHOSPHATASE METHYLESTERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PME-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: PPME1, PME1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS DEMETHYLASE, PP2A, ALTERNATIVE SPLICING, HYDROLASE,
KEYWDS 2 PHOSPHOPROTEIN, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XING,Z.LI,Y.CHEN,J.STOCK,P.D.JEFFREY,Y.SHI
REVDAT 1 15-APR-08 3C5V 0
JRNL AUTH Y.XING,Z.LI,Y.CHEN,J.STOCK,P.D.JEFFREY,Y.SHI
JRNL TITL STRUCTURAL MECHANISM OF DEMETHYLATION AND
JRNL TITL 2 INACTIVATION OF PROTEIN PHOSPHATASE 2A
JRNL REF CELL(CAMBRIDGE,MASS.) V. 133 154 2008
JRNL REFN ASTM CELLB5 US ISSN 0092-8674
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1749029.610
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24574
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 SET) : 0.183
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1191
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3821
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 196
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2278
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 283
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.43000
REMARK 3 B22 (A**2) : -1.43000
REMARK 3 B33 (A**2) : 2.87000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.160 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.010 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.500 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.880 ; 3.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 60.34
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3C5V COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-2005; 18-MAR-2005
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X25; X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10; 0.97945, 0.97910,
REMARK 200 0.96410
REMARK 200 MONOCHROMATOR : SI(111); SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC
REMARK 200 QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25077
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
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: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% V/V JEFFAMINE-2001, 200MM
REMARK 280 SODIUM CHLORIDE, 5MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -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 30.28100
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 60.56200
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 60.56200
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 30.28100
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 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLY A 240
REMARK 465 ILE A 241
REMARK 465 THR A 242
REMARK 465 SER A 243
REMARK 465 PRO A 244
REMARK 465 GLU A 245
REMARK 465 GLY A 246
REMARK 465 SER A 247
REMARK 465 LYS A 248
REMARK 465 LYS A 281
REMARK 465 ASP A 282
REMARK 465 HIS A 283
REMARK 465 GLY A 377
REMARK 465 GLY A 378
REMARK 465 PHE A 379
REMARK 465 GLN A 380
REMARK 465 CYS A 381
REMARK 465 VAL A 382
REMARK 465 PHE A 383
REMARK 465 PRO A 384
REMARK 465 GLY A 385
REMARK 465 CYS A 386
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 HIS A 87 -157.60 -100.92
REMARK 500 SER A 156 -117.52 47.69
REMARK 500 ALA A 321 -76.33 -140.75
REMARK 500 HIS A 349 -108.23 -107.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C5W RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PME-1 WITH INTERNAL PROTEOLYTIC DELETION (DELTA 249-280)
DBREF 3C5V A 39 248 UNP Q9Y570 PPME1_HUMAN 39 248
DBREF 3C5V A 281 386 UNP Q9Y570 PPME1_HUMAN 281 386
SEQRES 1 A 316 ARG ASP PHE SER PRO VAL PRO TRP SER GLN TYR PHE GLU
SEQRES 2 A 316 SER MET GLU ASP VAL GLU VAL GLU ASN GLU THR GLY LYS
SEQRES 3 A 316 ASP THR PHE ARG VAL TYR LYS SER GLY SER GLU GLY PRO
SEQRES 4 A 316 VAL LEU LEU LEU LEU HIS GLY GLY GLY HIS SER ALA LEU
SEQRES 5 A 316 SER TRP ALA VAL PHE THR ALA ALA ILE ILE SER ARG VAL
SEQRES 6 A 316 GLN CYS ARG ILE VAL ALA LEU ASP LEU ARG SER HIS GLY
SEQRES 7 A 316 GLU THR LYS VAL LYS ASN PRO GLU ASP LEU SER ALA GLU
SEQRES 8 A 316 THR MET ALA LYS ASP VAL GLY ASN VAL VAL GLU ALA MET
SEQRES 9 A 316 TYR GLY ASP LEU PRO PRO PRO ILE MET LEU ILE GLY HIS
SEQRES 10 A 316 SER MET GLY GLY ALA ILE ALA VAL HIS THR ALA SER SER
SEQRES 11 A 316 ASN LEU VAL PRO SER LEU LEU GLY LEU CYS MET ILE ASP
SEQRES 12 A 316 VAL VAL GLU GLY THR ALA MET ASP ALA LEU ASN SER MET
SEQRES 13 A 316 GLN ASN PHE LEU ARG GLY ARG PRO LYS THR PHE LYS SER
SEQRES 14 A 316 LEU GLU ASN ALA ILE GLU TRP SER VAL LYS SER GLY GLN
SEQRES 15 A 316 ILE ARG ASN LEU GLU SER ALA ARG VAL SER MET VAL GLY
SEQRES 16 A 316 GLN VAL LYS GLN CYS GLU GLY ILE THR SER PRO GLU GLY
SEQRES 17 A 316 SER LYS LYS ASP HIS PRO TYR THR TRP ARG ILE GLU LEU
SEQRES 18 A 316 ALA LYS THR GLU LYS TYR TRP ASP GLY TRP PHE ARG GLY
SEQRES 19 A 316 LEU SER ASN LEU PHE LEU SER CYS PRO ILE PRO LYS LEU
SEQRES 20 A 316 LEU LEU LEU ALA GLY VAL ASP ARG LEU ASP LYS ASP LEU
SEQRES 21 A 316 THR ILE GLY GLN MET GLN GLY LYS PHE GLN MET GLN VAL
SEQRES 22 A 316 LEU PRO GLN CYS GLY HIS ALA VAL HIS GLU ASP ALA PRO
SEQRES 23 A 316 ASP LYS VAL ALA GLU ALA VAL ALA THR PHE LEU ILE ARG
SEQRES 24 A 316 HIS ARG PHE ALA GLU PRO ILE GLY GLY PHE GLN CYS VAL
SEQRES 25 A 316 PHE PRO GLY CYS
FORMUL 2 HOH *283(H2 O)
HELIX 1 1 PRO A 45 TYR A 49 5 5
HELIX 2 2 SER A 88 SER A 91 5 4
HELIX 3 3 TRP A 92 SER A 101 1 10
HELIX 4 4 SER A 127 GLY A 144 1 18
HELIX 5 5 SER A 156 SER A 168 1 13
HELIX 6 6 VAL A 183 ARG A 201 1 19
HELIX 7 7 SER A 207 SER A 218 1 12
HELIX 8 8 ASN A 223 GLN A 234 1 12
HELIX 9 9 GLU A 290 LYS A 293 5 4
HELIX 10 10 THR A 294 ARG A 303 1 10
HELIX 11 11 GLY A 304 CYS A 312 1 9
HELIX 12 12 ASP A 327 GLN A 336 1 10
HELIX 13 13 ALA A 350 ALA A 355 1 6
HELIX 14 14 ALA A 355 HIS A 370 1 16
SHEET 1 A 8 SER A 52 ASN A 60 0
SHEET 2 A 8 GLY A 63 SER A 72 -1 O ASP A 65 N VAL A 58
SHEET 3 A 8 ARG A 106 LEU A 110 -1 O ALA A 109 N TYR A 70
SHEET 4 A 8 VAL A 78 LEU A 82 1 N LEU A 79 O ARG A 106
SHEET 5 A 8 ILE A 150 HIS A 155 1 O ILE A 153 N LEU A 82
SHEET 6 A 8 LEU A 174 ILE A 180 1 O LEU A 175 N ILE A 150
SHEET 7 A 8 LYS A 316 LEU A 320 1 O LEU A 317 N LEU A 177
SHEET 8 A 8 GLN A 340 VAL A 343 1 O GLN A 340 N LYS A 316
SHEET 1 B 2 VAL A 235 GLN A 237 0
SHEET 2 B 2 TYR A 285 TRP A 287 -1 O THR A 286 N LYS A 236
CRYST1 82.512 82.512 90.843 90.00 90.00 120.00 P 31 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 0.012119 0.006997 0.000000 0.00000
SCALE2 0.000000 0.013994 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011008 0.00000
TER 2279 ILE A 376
MASTER 286 0 0 14 10 0 0 6 2561 1 0 25
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