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HEADER HYDROLASE 07-MAR-25 9M6F
TITLE A THERMOSTABLE ZEARALENONE DEGRADING ENZYME MUTANT - S102A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ZEALARENONE DEGRADING ENZYME;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MONOSPORASCUS SP. GIB2;
SOURCE 3 ORGANISM_TAXID: 2211647;
SOURCE 4 GENE: DL765_008938;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZEARALENONE LACTONASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.OUYANG,W.XU
REVDAT 1 18-MAR-26 9M6F 0
JRNL AUTH B.OUYANG,W.XU
JRNL TITL A THERMOSTABLE ZEARALENONE DEGRADING ENZYME MUTANT - S102A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21_5207: ???)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.640
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15918
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.301
REMARK 3 R VALUE (WORKING SET) : 0.296
REMARK 3 FREE R VALUE : 0.382
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.260
REMARK 3 FREE R VALUE TEST SET COUNT : 837
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 22.5800 - 4.8900 1.00 2488 153 0.3011 0.4108
REMARK 3 2 4.8900 - 3.8900 1.00 2524 128 0.2795 0.3502
REMARK 3 3 3.8900 - 3.4000 1.00 2540 136 0.3034 0.3361
REMARK 3 4 3.4000 - 3.0900 1.00 2514 124 0.2791 0.3492
REMARK 3 5 3.0900 - 2.8700 1.00 2509 167 0.3162 0.4551
REMARK 3 6 2.8700 - 2.7000 1.00 2506 129 0.3234 0.4186
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.620
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.010
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) : 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 : 0.008 2155
REMARK 3 ANGLE : 1.110 2939
REMARK 3 CHIRALITY : 0.054 321
REMARK 3 PLANARITY : 0.010 378
REMARK 3 DIHEDRAL : 17.848 786
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 9M6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 11-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1300057262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.987
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16132
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 24.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
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: PHASER
REMARK 200 STARTING MODEL: 6L7M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM CHLORIDE, 0.05 M TRIS
REMARK 280 -HCL PH 8.5, 30% PEG 550 MME, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,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 31.94833
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 63.89667
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 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 O HOH A 308 O HOH A 309 2.17
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 ALA A 48 CB - CA - C ANGL. DEV. = 9.9 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 ARG A 4 48.07 -154.36
REMARK 500 ASN A 11 35.60 -94.68
REMARK 500 PRO A 30 -174.48 -69.46
REMARK 500 LYS A 41 -67.75 158.67
REMARK 500 SER A 62 -109.40 70.07
REMARK 500 SER A 64 31.47 -92.80
REMARK 500 ALA A 67 144.76 -178.98
REMARK 500 ALA A 102 -138.60 60.79
REMARK 500 ARG A 120 -71.08 -75.30
REMARK 500 GLU A 143 0.78 -68.83
REMARK 500 LEU A 166 42.50 -97.62
REMARK 500 THR A 194 -37.92 -130.83
REMARK 500 MET A 244 -88.25 -129.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 2 0.14 SIDE CHAIN
REMARK 500 ARG A 4 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 309 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 310 DISTANCE = 8.50 ANGSTROMS
DBREF1 9M6F A 1 267 UNP A0A4Q4TP46_9PEZI
DBREF2 9M6F A A0A4Q4TP46 1 267
SEQADV 9M6F ALA A 102 UNP A0A4Q4TP4 SER 102 ENGINEERED MUTATION
SEQRES 1 A 267 MET ARG THR ARG SER THR LEU THR ASP ARG ASN GLY ILE
SEQRES 2 A 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 A 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 A 267 ASP LYS PRO MET SER LEU ILE ALA ALA LYS GLY PHE THR
SEQRES 5 A 267 CYS THR THR PHE ASP MET ALA GLY MET SER ARG SER TRP
SEQRES 6 A 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 A 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 A 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 A 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 A 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 A 267 ALA SER PRO LEU PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 A 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU SER GLU GLU
SEQRES 13 A 267 MET PRO GLN THR ASN PHE GLY HIS ASP LEU THR ALA TRP
SEQRES 14 A 267 HIS GLU LEU GLY GLU GLU VAL HIS ALA ARG LEU ARG LYS
SEQRES 15 A 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 A 267 PRO LEU SER SER PRO THR SER LYS GLU ASP LEU THR LYS
SEQRES 17 A 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 A 267 ARG VAL PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 A 267 GLY ILE PRO ILE GLY THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 A 267 TYR LEU SEP HIS PRO GLU VAL LEU ALA GLU HIS ILE VAL
SEQRES 21 A 267 ASP THR THR ARG LYS TYR LEU
MODRES 9M6F SEP A 250 SER MODIFIED RESIDUE
HET SEP A 250 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 HOH *10(H2 O)
HELIX 1 AA1 LYS A 41 LYS A 49 1 9
HELIX 2 AA2 MET A 61 TRP A 65 5 5
HELIX 3 AA3 PRO A 68 TYR A 72 5 5
HELIX 4 AA4 THR A 76 LEU A 88 1 13
HELIX 5 AA5 ALA A 102 TYR A 115 1 14
HELIX 6 AA6 PRO A 116 MET A 119 5 4
HELIX 7 AA7 PRO A 133 LEU A 139 1 7
HELIX 8 AA8 GLU A 145 GLU A 155 1 11
HELIX 9 AA9 MET A 157 GLY A 163 1 7
HELIX 10 AB1 LEU A 166 LEU A 172 1 7
HELIX 11 AB2 GLY A 173 ARG A 189 1 17
HELIX 12 AB3 THR A 194 SER A 199 1 6
HELIX 13 AB4 SER A 202 THR A 207 1 6
HELIX 14 AB5 PRO A 220 VAL A 223 5 4
HELIX 15 AB6 PHE A 224 ALA A 234 1 11
HELIX 16 AB7 PHE A 246 HIS A 251 1 6
HELIX 17 AB8 HIS A 251 ARG A 264 1 14
HELIX 18 AB9 LYS A 265 LEU A 267 5 3
SHEET 1 AA1 3 ARG A 2 THR A 3 0
SHEET 2 AA1 3 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 3 THR A 6 THR A 8 -1 N LEU A 7 O TRP A 15
SHEET 1 AA2 6 ARG A 2 THR A 3 0
SHEET 2 AA2 6 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA2 6 THR A 52 PHE A 56 -1 O THR A 55 N GLU A 18
SHEET 4 AA2 6 HIS A 25 ILE A 29 1 N VAL A 26 O THR A 54
SHEET 5 AA2 6 THR A 97 GLY A 100 1 O THR A 97 N VAL A 27
SHEET 6 AA2 6 GLY A 122 PRO A 124 1 O LEU A 123 N PHE A 98
SHEET 1 AA3 2 TRP A 213 GLY A 216 0
SHEET 2 AA3 2 ILE A 238 LEU A 241 1 O LEU A 241 N VAL A 215
LINK C LEU A 249 N SEP A 250 1555 1555 1.33
LINK C SEP A 250 N HIS A 251 1555 1555 1.33
CRYST1 73.688 73.688 95.845 90.00 90.00 120.00 P 31 3
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 0.013571 0.007835 0.000000 0.00000
SCALE2 0.000000 0.015670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010434 0.00000
TER 2096 LEU A 267
MASTER 279 0 1 18 11 0 0 6 2105 1 12 21
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