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HEADER HYDROLASE 11-FEB-11 3QPC
TITLE STRUCTURE OF FUSARIUM SOLANI CUTINASE EXPRESSED IN PICHIA PASTORIS,
TITLE 2 CRYSTALLIZED IN THE PRESENCE OF PARAOXON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 32-228;
COMPND 5 SYNONYM: CUTIN HYDROLASE 1;
COMPND 6 EC: 3.1.1.74;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI;
SOURCE 3 ORGANISM_TAXID: 169388;
SOURCE 4 GENE: CUT1, CUTA;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS ALPHA-BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CUTIN, MONO-ETHYL
KEYWDS 2 PHOSPHORYLATED SERINE RESIDUE, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GOSSER,A.LU,X.KONG,J.K.MONTCLARE,Z.LIU
REVDAT 1 29-FEB-12 3QPC 0
JRNL AUTH Y.GOSSER,A.LU,X.KONG,J.K.MONTCLARE,Z.LIU
JRNL TITL STRUCTURE OF FUSARIUM SOLANI CUTINASE EXPRESSED IN PICHIA
JRNL TITL 2 PASTORIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 0.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 80123
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4396
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 19.9759 - 3.0347 1.00 3353 146 0.1729 0.1898
REMARK 3 2 3.0347 - 2.4101 1.00 3181 168 0.1423 0.1531
REMARK 3 3 2.4101 - 2.1058 1.00 3154 170 0.1288 0.1295
REMARK 3 4 2.1058 - 1.9134 1.00 3104 164 0.1237 0.1457
REMARK 3 5 1.9134 - 1.7764 0.99 3105 158 0.1245 0.1262
REMARK 3 6 1.7764 - 1.6717 0.99 3059 170 0.1181 0.1348
REMARK 3 7 1.6717 - 1.5880 0.99 3073 164 0.1150 0.1560
REMARK 3 8 1.5880 - 1.5189 0.98 3045 154 0.1095 0.1271
REMARK 3 9 1.5189 - 1.4605 0.98 3005 169 0.1102 0.1437
REMARK 3 10 1.4605 - 1.4101 0.98 2990 168 0.1139 0.1358
REMARK 3 11 1.4101 - 1.3660 0.97 2988 163 0.1113 0.1438
REMARK 3 12 1.3660 - 1.3270 0.96 2948 146 0.1137 0.1521
REMARK 3 13 1.3270 - 1.2920 0.96 2959 159 0.1144 0.1448
REMARK 3 14 1.2920 - 1.2605 0.96 2923 154 0.1165 0.1381
REMARK 3 15 1.2605 - 1.2319 0.95 2958 131 0.1227 0.1307
REMARK 3 16 1.2319 - 1.2057 0.95 2911 147 0.1196 0.1413
REMARK 3 17 1.2057 - 1.1815 0.94 2885 146 0.1221 0.1569
REMARK 3 18 1.1815 - 1.1592 0.93 2870 144 0.1270 0.1494
REMARK 3 19 1.1592 - 1.1385 0.92 2773 162 0.1306 0.1443
REMARK 3 20 1.1385 - 1.1192 0.92 2818 163 0.1336 0.1712
REMARK 3 21 1.1192 - 1.1012 0.90 2749 155 0.1435 0.1597
REMARK 3 22 1.1012 - 1.0843 0.89 2671 160 0.1543 0.1942
REMARK 3 23 1.0843 - 1.0683 0.87 2687 149 0.1741 0.1712
REMARK 3 24 1.0683 - 1.0533 0.85 2569 134 0.1900 0.1997
REMARK 3 25 1.0533 - 1.0390 0.83 2543 131 0.2061 0.2373
REMARK 3 26 1.0390 - 1.0255 0.81 2460 134 0.2243 0.2471
REMARK 3 27 1.0255 - 1.0127 0.77 2360 108 0.2551 0.2848
REMARK 3 28 1.0127 - 1.0005 0.73 2235 110 0.3064 0.2871
REMARK 3 29 1.0005 - 0.9889 0.65 1979 89 0.3324 0.3356
REMARK 3 30 0.9889 - 0.9778 0.53 1626 80 0.3741 0.3511
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 : 0.39
REMARK 3 B_SOL : 42.13
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 : 0.014 1587
REMARK 3 ANGLE : 1.521 2170
REMARK 3 CHIRALITY : 0.086 244
REMARK 3 PLANARITY : 0.009 294
REMARK 3 DIHEDRAL : 11.954 586
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3QPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.77009
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80123
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.978
REMARK 200 RESOLUTION RANGE LOW (A) : 19.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG3350, 0.2M MAGNESIUM
REMARK 280 FORMATE, PH 5.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 18.40000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.27300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.19250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.27300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.19250
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 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 109 CB CYS A 109 SG -0.159
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 165 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
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 SER A 30 52.13 -148.80
REMARK 500 THR A 43 -0.30 75.52
REMARK 500 MIR A 120 -122.16 61.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CEX RELATED DB: PDB
REMARK 900 ORIGINAL STRUCTURE OF F. SOLANI CUTINASE ENZYME EXPRESSED
REMARK 900 IN E. COLI
REMARK 900 RELATED ID: 3QPA RELATED DB: PDB
REMARK 900 HIGH RESOLUTION OF FSC STRUCTURE IN THE ABSENCE OF PARAOXON
REMARK 900 RELATED ID: 3QPD RELATED DB: PDB
DBREF 3QPC A 16 212 UNP C7ZGJ1 C7ZGJ1_NECH7 32 228
SEQRES 1 A 197 GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY ASN SER
SEQRES 2 A 197 ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA ARG GLY
SEQRES 3 A 197 SER THR GLU THR GLY ASN LEU GLY THR LEU GLY PRO SER
SEQRES 4 A 197 ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS ASP GLY
SEQRES 5 A 197 VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG ALA THR
SEQRES 6 A 197 LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER SER ALA
SEQRES 7 A 197 ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN ALA ASN
SEQRES 8 A 197 THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY GLY TYR
SEQRES 9 A 197 MIR GLN GLY ALA ALA LEU ALA ALA ALA SER ILE GLU ASP
SEQRES 10 A 197 LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY THR VAL
SEQRES 11 A 197 LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG GLY ARG
SEQRES 12 A 197 ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL PHE CYS
SEQRES 13 A 197 ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU ILE VAL
SEQRES 14 A 197 ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA ARG GLY
SEQRES 15 A 197 PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG ALA VAL
SEQRES 16 A 197 ARG GLY
MODRES 3QPC MIR A 120 SER MONOETHYLPHOSPHORYLSERINE
HET MIR A 120 21
HETNAM MIR MONOETHYLPHOSPHORYLSERINE
HETSYN MIR O-[(S)-ETHOXY(HYDROXY)PHOSPHORYL]-L-SERINE
FORMUL 1 MIR C5 H12 N O6 P
FORMUL 2 HOH *297(H2 O)
HELIX 1 1 LEU A 51 GLY A 64 1 14
HELIX 2 2 THR A 80 LEU A 86 5 7
HELIX 3 3 SER A 91 CYS A 109 1 19
HELIX 4 4 MIR A 120 LEU A 133 1 14
HELIX 5 5 ASP A 134 ASP A 139 1 6
HELIX 6 6 PRO A 163 ASP A 165 5 3
HELIX 7 7 ASP A 175 GLY A 180 5 6
HELIX 8 8 ALA A 185 ALA A 190 5 6
HELIX 9 9 TYR A 191 GLY A 197 1 7
HELIX 10 10 GLY A 197 GLY A 212 1 16
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N PHE A 36 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 O ILE A 115 N ILE A 37
SHEET 4 A 5 ILE A 141 PHE A 147 1 O ALA A 142 N LEU A 114
SHEET 5 A 5 THR A 167 PHE A 170 1 O PHE A 170 N LEU A 146
SSBOND 1 CYS A 31 CYS A 109 1555 1555 2.04
SSBOND 2 CYS A 171 CYS A 178 1555 1555 2.26
CRYST1 36.800 64.385 70.546 90.00 90.00 90.00 P 21 21 21 4
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 0.027174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014175 0.00000
TER 3074 GLY A 212
MASTER 285 0 1 10 5 0 0 6 1741 1 27 16
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