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HEADER HYDROLASE 11-JAN-10 3LCR
TITLE THIOESTERASE FROM TAUTOMYCETIN BIOSYNTHHETIC PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAUTOMYCETIN BIOSYNTHETIC PKS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 7326-7620;
COMPND 5 EC: 3.1.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. CK4412;
SOURCE 3 ORGANISM_TAXID: 404220;
SOURCE 4 GENE: TMCB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-BETA HYDROLASE, THIOESTERASE, POLYKETIDE SYNTHASE,
KEYWDS 2 PHOSPHOPANTETHEINE, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.AKEY,J.B.SCAGLIONE,J.L.SMITH,D.H.SHERMAN
REVDAT 1 18-AUG-10 3LCR 0
JRNL AUTH J.B.SCAGLIONE,D.L.AKEY,R.SULLIVAN,J.D.KITTENDORF,C.M.RATH,
JRNL AUTH 2 E.S.KIM,J.L.SMITH,D.H.SHERMAN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF THE
JRNL TITL 2 TAUTOMYCETIN THIOESTERASE: ANALYSIS OF A STEREOSELECTIVE
JRNL TITL 3 POLYKETIDE HYDROLASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2010
JRNL REFN ESSN 1521-3773
JRNL PMID 20623733
JRNL DOI 10.1002/ANIE.201000032
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 35951
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1786
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2297
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4185
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.00000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : -1.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.39000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.198
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4282 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5818 ; 1.172 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 4.988 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 195 ;35.020 ;23.128
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 663 ;15.253 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.663 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 648 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3318 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2727 ; 0.846 ; 3.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4335 ; 1.459 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1555 ; 0.952 ; 3.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1483 ; 1.515 ; 5.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 10
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 3 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2810 38.0210 17.5990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3835 T22: 0.1099
REMARK 3 T33: 0.0682 T12: -0.0395
REMARK 3 T13: 0.1342 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 6.8528 L22: 7.8724
REMARK 3 L33: 5.3729 L12: -2.6476
REMARK 3 L13: 0.8076 L23: -1.2488
REMARK 3 S TENSOR
REMARK 3 S11: -0.1930 S12: -0.1603 S13: -0.0559
REMARK 3 S21: 0.9096 S22: 0.1515 S23: 0.0334
REMARK 3 S31: 0.2946 S32: 0.2185 S33: 0.0415
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 33 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9160 39.4220 22.8630
REMARK 3 T TENSOR
REMARK 3 T11: 0.2507 T22: 0.1501
REMARK 3 T33: 0.1200 T12: -0.1458
REMARK 3 T13: 0.1045 T23: -0.0771
REMARK 3 L TENSOR
REMARK 3 L11: 4.3625 L22: 1.4569
REMARK 3 L33: 3.8393 L12: 0.7731
REMARK 3 L13: -2.6114 L23: -0.6441
REMARK 3 S TENSOR
REMARK 3 S11: -0.4238 S12: 0.4369 S13: -0.3815
REMARK 3 S21: -0.1639 S22: 0.1196 S23: 0.1682
REMARK 3 S31: 0.6399 S32: -0.5273 S33: 0.3042
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 106 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2190 51.2210 24.1870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1124 T22: 0.1215
REMARK 3 T33: 0.1066 T12: -0.0234
REMARK 3 T13: 0.0267 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 3.8276 L22: 1.1068
REMARK 3 L33: 3.1775 L12: 0.3789
REMARK 3 L13: -0.2353 L23: -0.0771
REMARK 3 S TENSOR
REMARK 3 S11: -0.2067 S12: 0.2335 S13: 0.2158
REMARK 3 S21: -0.0419 S22: 0.0704 S23: 0.1825
REMARK 3 S31: 0.0193 S32: -0.3445 S33: 0.1363
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 166 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2500 43.2550 24.7770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1869 T22: 0.1207
REMARK 3 T33: 0.0813 T12: 0.0098
REMARK 3 T13: 0.1171 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 4.0823 L22: 3.5161
REMARK 3 L33: 3.9478 L12: -0.3587
REMARK 3 L13: -0.8724 L23: 0.6494
REMARK 3 S TENSOR
REMARK 3 S11: -0.3391 S12: -0.1255 S13: -0.1289
REMARK 3 S21: 0.0620 S22: -0.0032 S23: -0.0730
REMARK 3 S31: 0.5536 S32: 0.1614 S33: 0.3424
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 214 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3800 48.4650 38.4440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1825 T22: 0.1196
REMARK 3 T33: 0.0612 T12: 0.0173
REMARK 3 T13: 0.0620 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 4.6999 L22: 2.2306
REMARK 3 L33: 4.1272 L12: -0.2176
REMARK 3 L13: -0.9748 L23: -0.2925
REMARK 3 S TENSOR
REMARK 3 S11: -0.3163 S12: -0.5102 S13: 0.1938
REMARK 3 S21: 0.2410 S22: 0.0486 S23: 0.0636
REMARK 3 S31: 0.1607 S32: 0.0972 S33: 0.2677
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 : B 3 B 32
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5900 39.9980 4.7280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1566 T22: 0.1561
REMARK 3 T33: 0.1307 T12: -0.0230
REMARK 3 T13: 0.1005 T23: -0.0805
REMARK 3 L TENSOR
REMARK 3 L11: 6.9061 L22: 3.5998
REMARK 3 L33: 8.8409 L12: -1.8145
REMARK 3 L13: 0.9893 L23: 0.1008
REMARK 3 S TENSOR
REMARK 3 S11: 0.1064 S12: 0.2803 S13: 0.1963
REMARK 3 S21: 0.2695 S22: -0.2325 S23: 0.4460
REMARK 3 S31: 0.0092 S32: -0.3029 S33: 0.1261
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 : B 33 B 105
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7540 23.2560 -2.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1327 T22: 0.1092
REMARK 3 T33: 0.1884 T12: -0.0114
REMARK 3 T13: -0.0254 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 2.2863 L22: 3.6716
REMARK 3 L33: 4.8897 L12: -0.7351
REMARK 3 L13: -1.3493 L23: 1.7546
REMARK 3 S TENSOR
REMARK 3 S11: -0.1551 S12: -0.1214 S13: -0.3943
REMARK 3 S21: 0.4989 S22: 0.0997 S23: -0.2787
REMARK 3 S31: 0.5875 S32: 0.0152 S33: 0.0554
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 : B 106 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7850 30.2180 -2.4910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0417 T22: 0.2151
REMARK 3 T33: 0.3532 T12: -0.0478
REMARK 3 T13: -0.0587 T23: -0.0839
REMARK 3 L TENSOR
REMARK 3 L11: 2.6890 L22: 5.1891
REMARK 3 L33: 5.1310 L12: -1.3771
REMARK 3 L13: -0.2346 L23: 0.6079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0982 S12: -0.1220 S13: 0.1670
REMARK 3 S21: 0.2588 S22: 0.1800 S23: -1.0014
REMARK 3 S31: -0.2039 S32: 0.5691 S33: -0.2783
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 166 B 213
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2040 38.1590 -2.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1649
REMARK 3 T33: 0.0624 T12: 0.0483
REMARK 3 T13: 0.0269 T23: -0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 3.3790 L22: 3.0338
REMARK 3 L33: 4.1473 L12: -0.5569
REMARK 3 L13: -1.1509 L23: 0.3640
REMARK 3 S TENSOR
REMARK 3 S11: 0.1648 S12: 0.1336 S13: 0.1254
REMARK 3 S21: 0.0225 S22: -0.1214 S23: -0.0430
REMARK 3 S31: -0.3452 S32: -0.5118 S33: -0.0433
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 214 B 280
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9180 36.4240 -16.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.1895 T22: 0.1364
REMARK 3 T33: 0.1558 T12: -0.0136
REMARK 3 T13: 0.1468 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 4.0037 L22: 4.8472
REMARK 3 L33: 3.4745 L12: -1.0744
REMARK 3 L13: -0.3422 L23: 0.3052
REMARK 3 S TENSOR
REMARK 3 S11: 0.2033 S12: 0.4254 S13: 0.2355
REMARK 3 S21: -0.6893 S22: -0.0445 S23: -0.7470
REMARK 3 S31: -0.5526 S32: -0.0021 S33: -0.1588
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3LCR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97937,0.97956,0.96112
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 FOR THE DATA SET : 16.5000
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 (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : 0.51100
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100-400 MM AMMONIUM FORMATE, 30% PEG
REMARK 280 3350, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.09150
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 1
REMARK 465 GLN A 2
REMARK 465 ASP A 38
REMARK 465 PRO A 39
REMARK 465 ALA A 40
REMARK 465 GLY A 41
REMARK 465 PRO A 42
REMARK 465 HIS A 281
REMARK 465 TYR A 282
REMARK 465 SER A 283
REMARK 465 THR A 284
REMARK 465 GLU A 285
REMARK 465 GLY A 286
REMARK 465 TRP A 287
REMARK 465 GLY A 288
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 LEU A 291
REMARK 465 ARG A 292
REMARK 465 THR A 293
REMARK 465 GLU A 294
REMARK 465 GLU A 295
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 ALA B 1
REMARK 465 GLN B 2
REMARK 465 HIS B 281
REMARK 465 TYR B 282
REMARK 465 SER B 283
REMARK 465 THR B 284
REMARK 465 GLU B 285
REMARK 465 GLY B 286
REMARK 465 TRP B 287
REMARK 465 GLY B 288
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 465 LEU B 291
REMARK 465 ARG B 292
REMARK 465 THR B 293
REMARK 465 GLU B 294
REMARK 465 GLU B 295
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 ALA A 122 -109.27 49.59
REMARK 500 SER A 132 -122.19 55.87
REMARK 500 GLN A 232 56.27 -100.52
REMARK 500 ALA B 122 -125.00 39.36
REMARK 500 SER B 132 -122.65 57.40
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 DMS B 3092
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 3092
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 3613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3613
DBREF 3LCR A 1 295 UNP A4KCE5 A4KCE5_9ACTO 7326 7620
DBREF 3LCR B 1 295 UNP A4KCE5 A4KCE5_9ACTO 7326 7620
SEQADV 3LCR MET A -23 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -22 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -21 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -20 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -19 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -18 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS A -17 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER A -16 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER A -15 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLY A -14 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR VAL A -13 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASP A -12 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR LEU A -11 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLY A -10 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR THR A -9 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLU A -8 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASN A -7 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR LEU A -6 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR TYR A -5 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR PHE A -4 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLN A -3 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER A -2 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASN A -1 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ALA A 0 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR MET B -23 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -22 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -21 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -20 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -19 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -18 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR HIS B -17 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER B -16 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER B -15 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLY B -14 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR VAL B -13 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASP B -12 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR LEU B -11 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLY B -10 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR THR B -9 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLU B -8 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASN B -7 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR LEU B -6 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR TYR B -5 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR PHE B -4 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR GLN B -3 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR SER B -2 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ASN B -1 UNP A4KCE5 EXPRESSION TAG
SEQADV 3LCR ALA B 0 UNP A4KCE5 EXPRESSION TAG
SEQRES 1 A 319 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 319 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ALA GLN
SEQRES 3 A 319 SER ASP TYR PHE GLY GLU LEU PHE LEU GLN ALA MET ARG
SEQRES 4 A 319 THR GLY GLU LEU ALA GLN ALA GLN GLN LEU MET ALA GLY
SEQRES 5 A 319 ALA ALA GLN LEU ARG LEU LYS TYR GLY ASP PRO ALA GLY
SEQRES 6 A 319 PRO GLU ALA VAL PRO GLU ILE VAL ARG LEU GLY ARG GLY
SEQRES 7 A 319 GLN LEU GLY PRO GLN LEU ILE LEU VAL CYS PRO THR VAL
SEQRES 8 A 319 MET THR THR GLY PRO GLN VAL TYR SER ARG LEU ALA GLU
SEQRES 9 A 319 GLU LEU ASP ALA GLY ARG ARG VAL SER ALA LEU VAL PRO
SEQRES 10 A 319 PRO GLY PHE HIS GLY GLY GLN ALA LEU PRO ALA THR LEU
SEQRES 11 A 319 THR VAL LEU VAL ARG SER LEU ALA ASP VAL VAL GLN ALA
SEQRES 12 A 319 GLU VAL ALA ASP GLY GLU PHE ALA LEU ALA GLY HIS SER
SEQRES 13 A 319 SER GLY GLY VAL VAL ALA TYR GLU VAL ALA ARG GLU LEU
SEQRES 14 A 319 GLU ALA ARG GLY LEU ALA PRO ARG GLY VAL VAL LEU ILE
SEQRES 15 A 319 ASP SER TYR SER PHE ASP GLY ASP GLY GLY ARG PRO GLU
SEQRES 16 A 319 GLU LEU PHE ARG SER ALA LEU ASN GLU ARG PHE VAL GLU
SEQRES 17 A 319 TYR LEU ARG LEU THR GLY GLY GLY ASN LEU SER GLN ARG
SEQRES 18 A 319 ILE THR ALA GLN VAL TRP CYS LEU GLU LEU LEU ARG GLY
SEQRES 19 A 319 TRP ARG PRO GLU GLY LEU THR ALA PRO THR LEU TYR VAL
SEQRES 20 A 319 ARG PRO ALA GLN PRO LEU VAL GLU GLN GLU LYS PRO GLU
SEQRES 21 A 319 TRP ARG GLY ASP VAL LEU ALA ALA MET GLY GLN VAL VAL
SEQRES 22 A 319 GLU ALA PRO GLY ASP HIS PHE THR ILE ILE GLU GLY GLU
SEQRES 23 A 319 HIS VAL ALA SER THR ALA HIS ILE VAL GLY ASP TRP LEU
SEQRES 24 A 319 ARG GLU ALA HIS ALA HIS TYR SER THR GLU GLY TRP GLY
SEQRES 25 A 319 GLY GLY LEU ARG THR GLU GLU
SEQRES 1 B 319 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 319 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ALA GLN
SEQRES 3 B 319 SER ASP TYR PHE GLY GLU LEU PHE LEU GLN ALA MET ARG
SEQRES 4 B 319 THR GLY GLU LEU ALA GLN ALA GLN GLN LEU MET ALA GLY
SEQRES 5 B 319 ALA ALA GLN LEU ARG LEU LYS TYR GLY ASP PRO ALA GLY
SEQRES 6 B 319 PRO GLU ALA VAL PRO GLU ILE VAL ARG LEU GLY ARG GLY
SEQRES 7 B 319 GLN LEU GLY PRO GLN LEU ILE LEU VAL CYS PRO THR VAL
SEQRES 8 B 319 MET THR THR GLY PRO GLN VAL TYR SER ARG LEU ALA GLU
SEQRES 9 B 319 GLU LEU ASP ALA GLY ARG ARG VAL SER ALA LEU VAL PRO
SEQRES 10 B 319 PRO GLY PHE HIS GLY GLY GLN ALA LEU PRO ALA THR LEU
SEQRES 11 B 319 THR VAL LEU VAL ARG SER LEU ALA ASP VAL VAL GLN ALA
SEQRES 12 B 319 GLU VAL ALA ASP GLY GLU PHE ALA LEU ALA GLY HIS SER
SEQRES 13 B 319 SER GLY GLY VAL VAL ALA TYR GLU VAL ALA ARG GLU LEU
SEQRES 14 B 319 GLU ALA ARG GLY LEU ALA PRO ARG GLY VAL VAL LEU ILE
SEQRES 15 B 319 ASP SER TYR SER PHE ASP GLY ASP GLY GLY ARG PRO GLU
SEQRES 16 B 319 GLU LEU PHE ARG SER ALA LEU ASN GLU ARG PHE VAL GLU
SEQRES 17 B 319 TYR LEU ARG LEU THR GLY GLY GLY ASN LEU SER GLN ARG
SEQRES 18 B 319 ILE THR ALA GLN VAL TRP CYS LEU GLU LEU LEU ARG GLY
SEQRES 19 B 319 TRP ARG PRO GLU GLY LEU THR ALA PRO THR LEU TYR VAL
SEQRES 20 B 319 ARG PRO ALA GLN PRO LEU VAL GLU GLN GLU LYS PRO GLU
SEQRES 21 B 319 TRP ARG GLY ASP VAL LEU ALA ALA MET GLY GLN VAL VAL
SEQRES 22 B 319 GLU ALA PRO GLY ASP HIS PHE THR ILE ILE GLU GLY GLU
SEQRES 23 B 319 HIS VAL ALA SER THR ALA HIS ILE VAL GLY ASP TRP LEU
SEQRES 24 B 319 ARG GLU ALA HIS ALA HIS TYR SER THR GLU GLY TRP GLY
SEQRES 25 B 319 GLY GLY LEU ARG THR GLU GLU
HET DMS A3092 4
HET FMT A3613 3
HET DMS B3092 4
HET FMT B3613 3
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM FMT FORMIC ACID
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 4 FMT 2(C H2 O2)
FORMUL 7 HOH *218(H2 O)
HELIX 1 1 ASP A 4 GLY A 17 1 14
HELIX 2 2 GLU A 18 ARG A 33 1 16
HELIX 3 3 GLY A 71 VAL A 74 5 4
HELIX 4 4 TYR A 75 ASP A 83 1 9
HELIX 5 5 THR A 105 ALA A 122 1 18
HELIX 6 6 SER A 132 ARG A 148 1 17
HELIX 7 7 GLY A 168 GLY A 190 1 23
HELIX 8 8 ASN A 193 LEU A 208 1 16
HELIX 9 9 PRO A 235 ALA A 244 1 10
HELIX 10 10 PHE A 256 GLU A 260 5 5
HELIX 11 11 HIS A 263 ALA A 280 1 18
HELIX 12 12 ASP B 4 THR B 16 1 13
HELIX 13 13 GLU B 18 ARG B 33 1 16
HELIX 14 14 GLY B 71 VAL B 74 5 4
HELIX 15 15 TYR B 75 ASP B 83 1 9
HELIX 16 16 THR B 105 ALA B 122 1 18
HELIX 17 17 SER B 132 ARG B 148 1 17
HELIX 18 18 GLY B 168 THR B 189 1 22
HELIX 19 19 ASN B 193 LEU B 208 1 16
HELIX 20 20 PRO B 235 ALA B 244 1 10
HELIX 21 21 PHE B 256 GLU B 260 5 5
HELIX 22 22 HIS B 263 ALA B 280 1 18
SHEET 1 A 2 LYS A 35 TYR A 36 0
SHEET 2 A 2 LEU A 102 PRO A 103 1 O LEU A 102 N TYR A 36
SHEET 1 B 7 GLU A 47 LEU A 51 0
SHEET 2 B 7 ARG A 87 VAL A 92 -1 O VAL A 88 N LEU A 51
SHEET 3 B 7 GLN A 59 VAL A 63 1 N LEU A 62 O SER A 89
SHEET 4 B 7 PHE A 126 HIS A 131 1 O ALA A 127 N ILE A 61
SHEET 5 B 7 VAL A 155 ILE A 158 1 O ILE A 158 N GLY A 130
SHEET 6 B 7 THR A 220 PRO A 225 1 O LEU A 221 N LEU A 157
SHEET 7 B 7 GLN A 247 ALA A 251 1 O VAL A 249 N ARG A 224
SHEET 1 C 2 LYS B 35 TYR B 36 0
SHEET 2 C 2 LEU B 102 PRO B 103 1 O LEU B 102 N TYR B 36
SHEET 1 D 7 GLU B 47 ARG B 50 0
SHEET 2 D 7 ARG B 87 VAL B 92 -1 O ALA B 90 N VAL B 49
SHEET 3 D 7 GLN B 59 VAL B 63 1 N LEU B 62 O SER B 89
SHEET 4 D 7 PHE B 126 HIS B 131 1 O ALA B 129 N VAL B 63
SHEET 5 D 7 VAL B 155 ILE B 158 1 O ILE B 158 N GLY B 130
SHEET 6 D 7 THR B 220 PRO B 225 1 O LEU B 221 N LEU B 157
SHEET 7 D 7 GLN B 247 ALA B 251 1 O VAL B 249 N ARG B 224
SITE 1 AC1 5 THR B 69 VAL B 74 PHE B 182 TYR B 185
SITE 2 AC1 5 HOH B 372
SITE 1 AC2 3 THR A 69 VAL A 74 TYR A 185
SITE 1 AC3 5 VAL B 67 SER B 132 SER B 133 TYR B 161
SITE 2 AC3 5 HOH B 355
SITE 1 AC4 5 VAL A 67 SER A 132 SER A 133 TYR A 161
SITE 2 AC4 5 HOH A 374
CRYST1 54.102 80.183 64.706 90.00 103.76 90.00 P 1 21 1 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 0.018484 0.000000 0.004527 0.00000
SCALE2 0.000000 0.012471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015911 0.00000
TER 2078 ALA A 280
TER 4187 ALA B 280
MASTER 539 0 4 22 18 0 7 6 4417 2 14 50
END |