| content |
HEADER HYDROLASE 22-AUG-18 6AID
TITLE STRUCTURAL INSIGHTS INTO THE UNIQUE POLYLACTATE DEGRADING MECHANISM OF
TITLE 2 THERMOBIFIDA ALBA CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 35-300;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA ALBA;
SOURCE 3 ORGANISM_TAXID: 53522;
SOURCE 4 GENE: EST2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KITADOKORO,M.KAKARA,S.MATSUI,R.OSOKOSHI,U.THUMARAT,F.KAWAI,
AUTHOR 2 S.KAMITANI
REVDAT 1 27-FEB-19 6AID 0
JRNL AUTH K.KITADOKORO,K.MIZUKI,S.MATSUI,R.OSOKOSHI,T.USCHARA,F.KAWAI,
JRNL AUTH 2 S.KAMITANI
JRNL TITL STRUCTURAL INSIGHTS INTO THE UNIQUE POLYLACTATE-DEGRADING
JRNL TITL 2 MECHANISM OF THERMOBIFIDA ALBA CUTINASE.
JRNL REF FEBS J. 2019
JRNL REFN ISSN 1742-4658
JRNL PMID 30761732
JRNL DOI 10.1111/FEBS.14781
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 53071
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) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2790
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3245
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 178
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2009
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : -0.08000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.045
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.786
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2073 ; 0.030 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1907 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2821 ; 2.443 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4387 ; 1.251 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 260 ; 6.510 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;31.259 ;22.747
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ; 9.808 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.881 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 309 ; 0.167 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2361 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 483 ; 0.002 ; 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): 1043 ; 0.952 ; 0.336
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1042 ; 0.951 ; 0.333
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1302 ; 1.215 ; 0.505
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1303 ; 1.215 ; 0.508
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1030 ; 1.967 ; 0.589
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1031 ; 1.971 ; 0.591
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1520 ; 2.249 ; 0.798
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2427 ; 2.318 ; 6.069
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2428 ; 2.320 ; 6.091
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3980 ; 6.020 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 125 ;16.969 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4032 ; 4.767 ; 5.000
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 : 8
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 40 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9999 -3.6755 11.8091
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.0745
REMARK 3 T33: 0.0646 T12: -0.0030
REMARK 3 T13: 0.0022 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.3525 L22: 0.3048
REMARK 3 L33: 0.4531 L12: -0.0305
REMARK 3 L13: -0.0755 L23: -0.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: 0.0020 S13: 0.0274
REMARK 3 S21: 0.0026 S22: 0.0120 S23: -0.0017
REMARK 3 S31: -0.0136 S32: -0.0026 S33: -0.0239
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0338 -1.1930 24.8988
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: 0.1505
REMARK 3 T33: 0.0610 T12: 0.0560
REMARK 3 T13: 0.0329 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 402 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0840 -19.0567 -0.2820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0348 T22: 0.0682
REMARK 3 T33: 0.0690 T12: -0.0180
REMARK 3 T13: -0.0111 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 403 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3838 -16.6017 14.5874
REMARK 3 T TENSOR
REMARK 3 T11: 0.0553 T22: 0.0600
REMARK 3 T33: 0.0772 T12: 0.0158
REMARK 3 T13: -0.0060 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 722
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1601 -4.0208 8.9585
REMARK 3 T TENSOR
REMARK 3 T11: 0.0194 T22: 0.0445
REMARK 3 T33: 0.0399 T12: -0.0075
REMARK 3 T13: 0.0001 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.3883 L22: 0.3473
REMARK 3 L33: 0.3383 L12: -0.0812
REMARK 3 L13: -0.0497 L23: -0.0686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: 0.0093 S13: 0.0200
REMARK 3 S21: -0.0159 S22: 0.0156 S23: 0.0096
REMARK 3 S31: 0.0077 S32: -0.0168 S33: -0.0347
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 404 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7202 -13.1743 24.9539
REMARK 3 T TENSOR
REMARK 3 T11: 0.0581 T22: 0.0981
REMARK 3 T33: 0.0829 T12: 0.0121
REMARK 3 T13: 0.0038 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 16.5072 L22: 10.6952
REMARK 3 L33: 1.7855 L12: 8.1381
REMARK 3 L13: -1.9002 L23: 2.2990
REMARK 3 S TENSOR
REMARK 3 S11: -0.4479 S12: 0.2103 S13: 0.2119
REMARK 3 S21: -0.0730 S22: 0.1568 S23: 0.7548
REMARK 3 S31: 0.1228 S32: 0.0029 S33: 0.2911
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 405 A 406
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3545 -1.7290 26.9348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0719 T22: 0.0928
REMARK 3 T33: 0.1029 T12: 0.0056
REMARK 3 T13: 0.0124 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.5082 L22: 0.5021
REMARK 3 L33: 1.8376 L12: 0.8345
REMARK 3 L13: -1.6622 L23: -0.9346
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: -0.0300 S13: 0.0076
REMARK 3 S21: 0.0109 S22: -0.0108 S23: 0.0086
REMARK 3 S31: -0.0166 S32: 0.0345 S33: -0.0069
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 407 A 407
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2384 -9.9313 30.3635
REMARK 3 T TENSOR
REMARK 3 T11: 0.0446 T22: 0.1942
REMARK 3 T33: 0.1010 T12: 0.0638
REMARK 3 T13: -0.0487 T23: -0.1101
REMARK 3 L TENSOR
REMARK 3 L11: 39.8810 L22: 265.6608
REMARK 3 L33: 131.3804 L12: 30.3904
REMARK 3 L13: -69.0348 L23: 1.0670
REMARK 3 S TENSOR
REMARK 3 S11: -0.0902 S12: -0.7215 S13: -0.7453
REMARK 3 S21: 2.0993 S22: -1.1051 S23: -1.0059
REMARK 3 S31: 0.6363 S32: 1.1237 S33: 1.1954
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.
REMARK 4
REMARK 4 6AID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300008825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106239
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.89
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.910
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PLATE LIKE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% (W/V) PEG 3350, 0.2 M SODIUM
REMARK 280 ACETATE, 0.2M2 M CALCIUM CHLORIDE, AND 0.1 M SODIUM CHLORIDE, PH
REMARK 280 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 21.13250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.29700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.29700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.13250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.43000
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 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 MET A 23
REMARK 465 ARG A 24
REMARK 465 GLY A 25
REMARK 465 SER A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 ALA A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 GLN A 38
REMARK 465 ALA A 39
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 SER A 169 OG
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 524 O HOH A 671 1.68
REMARK 500 O HOH A 641 O HOH A 668 1.70
REMARK 500 O HOH A 502 O HOH A 522 1.78
REMARK 500 OD1 ASP A 202 O HOH A 501 1.93
REMARK 500 NH2 ARG A 182 O HOH A 502 1.95
REMARK 500 O HOH A 615 O HOH A 684 1.99
REMARK 500 N ALA A 40 O HOH A 503 2.00
REMARK 500 O HOH A 506 O HOH A 540 2.03
REMARK 500 O HOH A 501 O HOH A 692 2.03
REMARK 500 O HOH A 502 O HOH A 683 2.05
REMARK 500 OG SER A 180 OD1 ASP A 202 2.08
REMARK 500 NH1 ARG A 182 O HOH A 502 2.09
REMARK 500 O HOH A 541 O HOH A 599 2.10
REMARK 500 O HOH A 596 O HOH A 642 2.17
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 678 O HOH A 684 2554 1.96
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 ARG A 85 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 4.0 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 THR A 100 -6.73 79.16
REMARK 500 SER A 169 -119.66 65.10
REMARK 500 THR A 192 56.73 34.51
REMARK 500 TRP A 200 55.76 -112.53
REMARK 500 TYR A 214 45.55 -107.23
REMARK 500 HIS A 223 -85.35 -121.98
REMARK 500 GLU A 271 26.74 49.51
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 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 63 O
REMARK 620 2 HOH A 625 O 98.3
REMARK 620 3 HOH A 690 O 83.6 170.9
REMARK 620 4 HOH A 597 O 100.0 98.3 90.1
REMARK 620 5 ASP A 149 O 26.4 117.5 67.4 79.4
REMARK 620 6 ALA A 150 O 18.8 112.9 71.1 85.9 7.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 70 O
REMARK 620 2 ALA A 73 O 96.6
REMARK 620 3 PHE A 76 O 117.1 86.9
REMARK 620 4 HOH A 628 O 158.2 99.7 78.4
REMARK 620 5 HOH A 696 O 93.7 93.5 149.0 71.0
REMARK 620 6 HOH A 556 O 108.8 153.2 74.3 58.5 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 193 O
REMARK 620 2 ALA A 218 O 108.6
REMARK 620 3 SER A 224 OG 112.7 138.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 212 O
REMARK 620 2 GLU A 213 O 67.8
REMARK 620 3 HOH A 686 O 146.3 87.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 213 OE1
REMARK 620 2 GLU A 213 OE2 52.3
REMARK 620 3 ASP A 243 OD1 81.9 133.4
REMARK 620 4 GLU A 292 OE1 97.5 88.2 89.8
REMARK 620 5 HOH A 622 O 85.0 83.2 103.3 167.0
REMARK 620 6 HOH A 654 O 157.7 146.9 76.6 76.7 105.6
REMARK 620 7 HOH A 661 O 125.1 73.1 153.0 85.8 82.3 76.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9YL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LAC A 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VIS RELATED DB: PDB
REMARK 900 NATIVE PROTEIN
REMARK 900 RELATED ID: 3WYN RELATED DB: PDB
REMARK 900 NATIVE PROTEIN WITH CALCIUM ION
DBREF 6AID A 35 300 UNP F7IX06 F7IX06_9ACTN 35 300
SEQADV 6AID MET A 23 UNP F7IX06 INITIATING METHIONINE
SEQADV 6AID ARG A 24 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID GLY A 25 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID SER A 26 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 27 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 28 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 29 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 30 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 31 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID HIS A 32 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID GLY A 33 UNP F7IX06 EXPRESSION TAG
SEQADV 6AID SER A 34 UNP F7IX06 EXPRESSION TAG
SEQRES 1 A 278 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 A 278 PRO ALA GLN ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN
SEQRES 3 A 278 PRO THR GLU SER MET LEU GLU ALA ARG SER GLY PRO PHE
SEQRES 4 A 278 SER VAL SER GLU GLU ARG ALA SER ARG PHE GLY ALA ASP
SEQRES 5 A 278 GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG GLU ASN
SEQRES 6 A 278 ASN THR TYR GLY ALA ILE ALA ILE SER PRO GLY TYR THR
SEQRES 7 A 278 GLY THR GLN SER SER ILE ALA TRP LEU GLY GLU ARG ILE
SEQRES 8 A 278 ALA SER HIS GLY PHE VAL VAL ILE ALA ILE ASP THR ASN
SEQRES 9 A 278 THR THR LEU ASP GLN PRO ASP SER ARG ALA ARG GLN LEU
SEQRES 10 A 278 ASN ALA ALA LEU ASP TYR MET LEU THR ASP ALA SER SER
SEQRES 11 A 278 ALA VAL ARG ASN ARG ILE ASP ALA SER ARG LEU ALA VAL
SEQRES 12 A 278 MET GLY HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU
SEQRES 13 A 278 ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU
SEQRES 14 A 278 THR PRO TRP HIS LEU ASN LYS SER TRP ARG ASP ILE THR
SEQRES 15 A 278 VAL PRO THR LEU ILE ILE GLY ALA GLU TYR ASP THR ILE
SEQRES 16 A 278 ALA SER VAL THR LEU HIS SER LYS PRO PHE TYR ASN SER
SEQRES 17 A 278 ILE PRO SER PRO THR ASP LYS ALA TYR LEU GLU LEU ASP
SEQRES 18 A 278 GLY ALA SER HIS PHE ALA PRO ASN ILE THR ASN LYS THR
SEQRES 19 A 278 ILE GLY MET TYR SER VAL ALA TRP LEU LYS ARG PHE VAL
SEQRES 20 A 278 ASP GLU ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY
SEQRES 21 A 278 PRO ARG THR GLY LEU LEU SER ASP VAL GLU GLU TYR ARG
SEQRES 22 A 278 SER THR CYS PRO PHE
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET 9YL A 404 8
HET NA A 405 1
HET NA A 406 1
HET LAC A 407 6
HETNAM CA CALCIUM ION
HETNAM 9YL ETHYL (2R)-2-OXIDANYLPROPANOATE
HETNAM NA SODIUM ION
HETNAM LAC LACTIC ACID
HETSYN 9YL ETHYL LACTATE
FORMUL 2 CA 3(CA 2+)
FORMUL 5 9YL C5 H10 O3
FORMUL 6 NA 2(NA 1+)
FORMUL 8 LAC C3 H6 O3
FORMUL 9 HOH *222(H2 O)
HELIX 1 AA1 THR A 50 ALA A 56 1 7
HELIX 2 AA2 SER A 69 ALA A 73 5 5
HELIX 3 AA3 THR A 102 SER A 105 5 4
HELIX 4 AA4 ILE A 106 SER A 115 1 10
HELIX 5 AA5 GLN A 131 ASP A 149 1 19
HELIX 6 AA6 SER A 151 ASN A 156 1 6
HELIX 7 AA7 SER A 169 ARG A 182 1 14
HELIX 8 AA8 HIS A 223 ILE A 231 1 9
HELIX 9 AA9 PHE A 248 ILE A 252 5 5
HELIX 10 AB1 ASN A 254 ASP A 270 1 17
HELIX 11 AB2 ASP A 272 ARG A 274 5 3
HELIX 12 AB3 TYR A 275 CYS A 280 1 6
SHEET 1 AA1 6 VAL A 63 ALA A 68 0
SHEET 2 AA1 6 GLY A 79 PRO A 84 -1 O ILE A 81 N GLU A 66
SHEET 3 AA1 6 VAL A 119 ILE A 123 -1 O VAL A 120 N TYR A 82
SHEET 4 AA1 6 TYR A 90 SER A 96 1 N ILE A 93 O VAL A 119
SHEET 5 AA1 6 ILE A 158 HIS A 168 1 O ASP A 159 N TYR A 90
SHEET 6 AA1 6 ALA A 187 LEU A 191 1 O LEU A 191 N GLY A 167
SHEET 1 AA2 3 THR A 207 ALA A 212 0
SHEET 2 AA2 3 LYS A 237 LEU A 242 1 O LEU A 242 N GLY A 211
SHEET 3 AA2 3 VAL A 291 SER A 296 -1 O GLU A 293 N GLU A 241
SSBOND 1 CYS A 280 CYS A 298 1555 1555 2.05
LINK O VAL A 63 CA CA A 402 1555 1555 2.38
LINK O ARG A 70 CA CA A 403 1555 1555 2.38
LINK O ALA A 73 CA CA A 403 1555 1555 2.30
LINK O PHE A 76 CA CA A 403 1555 1555 2.34
LINK O PRO A 193 NA NA A 405 1555 1555 2.81
LINK O ALA A 212 NA NA A 406 1555 1555 2.93
LINK O GLU A 213 NA NA A 406 1555 1555 3.10
LINK OE1 GLU A 213 CA CA A 401 1555 1555 2.44
LINK OE2 GLU A 213 CA CA A 401 1555 1555 2.56
LINK O ALA A 218 NA NA A 405 1555 1555 2.73
LINK OG SER A 224 NA NA A 405 1555 1555 2.72
LINK OD1 ASP A 243 CA CA A 401 1555 1555 2.35
LINK OE1 GLU A 292 CA CA A 401 1555 1555 2.39
LINK CA CA A 401 O HOH A 622 1555 1555 2.30
LINK CA CA A 401 O HOH A 654 1555 1555 2.38
LINK CA CA A 401 O HOH A 661 1555 1555 2.39
LINK CA CA A 402 O HOH A 625 1555 1555 2.38
LINK CA CA A 402 O HOH A 690 1555 1555 2.36
LINK CA CA A 402 O HOH A 597 1555 1555 2.31
LINK CA CA A 403 O HOH A 628 1555 1555 2.68
LINK CA CA A 403 O HOH A 696 1555 1555 2.25
LINK CA CA A 403 O HOH A 556 1555 1555 2.57
LINK NA NA A 406 O HOH A 686 1555 1555 3.02
LINK O ASP A 149 CA CA A 402 1555 4545 2.41
LINK O ALA A 150 CA CA A 402 1555 4545 2.57
CISPEP 1 SER A 233 PRO A 234 0 10.31
CISPEP 2 CYS A 280 PRO A 281 0 5.34
CISPEP 3 CYS A 298 PRO A 299 0 9.75
SITE 1 AC1 6 GLU A 213 ASP A 243 GLU A 292 HOH A 622
SITE 2 AC1 6 HOH A 654 HOH A 661
SITE 1 AC2 6 VAL A 63 ASP A 149 ALA A 150 HOH A 597
SITE 2 AC2 6 HOH A 625 HOH A 690
SITE 1 AC3 6 ARG A 70 ALA A 73 PHE A 76 HOH A 556
SITE 2 AC3 6 HOH A 628 HOH A 696
SITE 1 AC4 9 GLY A 98 TYR A 99 SER A 169 SER A 233
SITE 2 AC4 9 HIS A 247 PHE A 248 LAC A 407 HOH A 550
SITE 3 AC4 9 HOH A 593
SITE 1 AC5 4 PRO A 193 ALA A 218 HIS A 223 SER A 224
SITE 1 AC6 6 ALA A 212 GLU A 213 ASP A 215 SER A 219
SITE 2 AC6 6 VAL A 220 HOH A 686
SITE 1 AC7 6 TYR A 99 MET A 170 TRP A 194 ILE A 217
SITE 2 AC7 6 9YL A 404 HOH A 550
CRYST1 42.265 68.860 78.594 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 0.023660 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014522 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012724 0.00000
TER 2010 PHE A 300
MASTER 591 0 7 12 9 0 14 6 2250 1 46 22
END |