HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 16-JUL-12 4G45
TITLE STRUCTURE OF CYTOCHROME CYP121 IN COMPLEX WITH 2-METHYLQUINOLIN-6-
TITLE 2 AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 121;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME P450 MT2;
COMPND 5 EC: 1.14.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV2276;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS P450, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.A.HUDSON,K.J.MCLEAN,S.SURADE,Y.-Q.YANG,D.LEYS,A.CIULLI,A.W.MUNRO,
AUTHOR 2 C.ABELL
REVDAT 3 20-MAR-24 4G45 1 REMARK
REVDAT 2 19-SEP-12 4G45 1 JRNL
REVDAT 1 05-SEP-12 4G45 0
JRNL AUTH S.A.HUDSON,K.J.MCLEAN,S.SURADE,Y.-Q.YANG,D.LEYS,A.CIULLI,
JRNL AUTH 2 A.W.MUNRO,C.ABELL
JRNL TITL APPLICATION OF FRAGMENT SCREENING AND MERGING TO THE
JRNL TITL 2 DISCOVERY OF INHIBITORS OF THE MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 3 CYTOCHROME P450 CYP121
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 51 9311 2012
JRNL REFN ISSN 1433-7851
JRNL PMID 22890978
JRNL DOI 10.1002/ANIE.201202544
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 69154
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3677
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) : 1.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4382
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2980
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 784
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.52
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3242 ; 0.030 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4442 ; 3.127 ; 2.020
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 393 ; 5.282 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;29.929 ;23.206
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 536 ;12.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;17.357 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 521 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2423 ; 0.016 ; 0.022
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4G45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69154
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 36.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, PH 6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 176.20000
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 88.10000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 132.15000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.05000
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 220.25000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 176.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 88.10000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.05000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 132.15000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 220.25000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 44.05000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 673 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 927 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 960 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1113 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1116 LIES ON A SPECIAL POSITION.
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 1
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 THR A 2 N CA CB OG1 CG2
REMARK 470 ARG A 17 CZ NH1 NH2
REMARK 470 GLU A 24 CD OE1 OE2
REMARK 470 ARG A 28 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 96 CE NZ
REMARK 470 LYS A 100 NZ
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 GLU A 127 CD OE1 OE2
REMARK 470 LYS A 148 CE NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 184 CD NE CZ NH1 NH2
REMARK 470 GLU A 261 CD OE1 OE2
REMARK 470 LYS A 262 CE NZ
REMARK 470 GLU A 317 CD OE1 OE2
REMARK 470 ARG A 353 CD NE CZ NH1 NH2
REMARK 470 LYS A 364 CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 300 CG
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 643 O HOH A 810 1.55
REMARK 500 O HOH A 1057 O HOH A 1067 1.77
REMARK 500 O HOH A 828 O HOH A 1077 1.83
REMARK 500 OE2 GLU A 221 O HOH A 847 1.88
REMARK 500 O HOH A 874 O HOH A 1145 1.89
REMARK 500 O HOH A 606 O HOH A 1098 1.90
REMARK 500 O HOH A 823 O HOH A 1129 1.95
REMARK 500 O HOH A 988 O HOH A 1091 1.95
REMARK 500 O3 SO4 A 404 O HOH A 1133 1.98
REMARK 500 O HOH A 666 O HOH A 1160 2.01
REMARK 500 O HOH A 1022 O HOH A 1230 2.02
REMARK 500 O HOH A 792 O HOH A 833 2.02
REMARK 500 O HOH A 962 O HOH A 1095 2.07
REMARK 500 O HOH A 850 O HOH A 1170 2.11
REMARK 500 O HOH A 1051 O HOH A 1203 2.11
REMARK 500 O HOH A 829 O HOH A 1225 2.11
REMARK 500 O HOH A 797 O HOH A 1155 2.13
REMARK 500 OE2 GLU A 326 O HOH A 849 2.15
REMARK 500 O HOH A 1017 O HOH A 1023 2.17
REMARK 500 O HOH A 1206 O HOH A 1242 2.17
REMARK 500 O HOH A 715 O HOH A 1170 2.18
REMARK 500 OD1 ASN A 197 O HOH A 1150 2.18
REMARK 500 O HOH A 989 O HOH A 1059 2.18
REMARK 500 O HOH A 763 O HOH A 1227 2.19
REMARK 500 O HOH A 829 O HOH A 965 2.19
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 CAF MQN A 407 O HOH A 1206 8555 1.82
REMARK 500 O HOH A 791 O HOH A 1041 10555 1.91
REMARK 500 O HOH A 1073 O HOH A 1073 10665 1.99
REMARK 500 O HOH A 1147 O HOH A 1224 8555 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 HIS A 146 CG HIS A 146 CD2 0.060
REMARK 500 TRP A 182 CE2 TRP A 182 CD2 0.089
REMARK 500 TRP A 182 CE3 TRP A 182 CZ3 0.123
REMARK 500 GLU A 221 CG GLU A 221 CD 0.114
REMARK 500 HIS A 335 CG HIS A 335 CD2 0.065
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 26 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 GLU A 29 OE1 - CD - OE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 32 CD - NE - CZ ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLU A 56 OE1 - CD - OE2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP A 57 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ASP A 139 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 183 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 183 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 208 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLU A 221 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 291 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 352 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 376 CB - CG - OD1 ANGL. DEV. = 6.4 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 ALA A 3 146.00 -36.44
REMARK 500 GLU A 29 74.61 -156.62
REMARK 500 PHE A 137 -73.48 -141.86
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 72 0.09 SIDE CHAIN
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 HEM A 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 345 SG
REMARK 620 2 HEM A 401 NA 99.7
REMARK 620 3 HEM A 401 NB 91.1 90.7
REMARK 620 4 HEM A 401 NC 87.3 173.0 89.0
REMARK 620 5 HEM A 401 ND 98.2 90.3 170.4 88.9
REMARK 620 6 MQN A 408 NAB 174.1 86.1 87.6 86.9 83.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQN A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQN A 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G44 RELATED DB: PDB
REMARK 900 CYP121 WITH ANOTHER LEAD TARGET
REMARK 900 RELATED ID: 4G46 RELATED DB: PDB
REMARK 900 RELATED ID: 4G47 RELATED DB: PDB
REMARK 900 RELATED ID: 4G48 RELATED DB: PDB
DBREF 4G45 A 1 396 UNP P0A514 CP121_MYCTU 1 396
SEQRES 1 A 396 MET THR ALA THR VAL LEU LEU GLU VAL PRO PHE SER ALA
SEQRES 2 A 396 ARG GLY ASP ARG ILE PRO ASP ALA VAL ALA GLU LEU ARG
SEQRES 3 A 396 THR ARG GLU PRO ILE ARG LYS VAL ARG THR ILE THR GLY
SEQRES 4 A 396 ALA GLU ALA TRP LEU VAL SER SER TYR ALA LEU CYS THR
SEQRES 5 A 396 GLN VAL LEU GLU ASP ARG ARG PHE SER MET LYS GLU THR
SEQRES 6 A 396 ALA ALA ALA GLY ALA PRO ARG LEU ASN ALA LEU THR VAL
SEQRES 7 A 396 PRO PRO GLU VAL VAL ASN ASN MET GLY ASN ILE ALA ASP
SEQRES 8 A 396 ALA GLY LEU ARG LYS ALA VAL MET LYS ALA ILE THR PRO
SEQRES 9 A 396 LYS ALA PRO GLY LEU GLU GLN PHE LEU ARG ASP THR ALA
SEQRES 10 A 396 ASN SER LEU LEU ASP ASN LEU ILE THR GLU GLY ALA PRO
SEQRES 11 A 396 ALA ASP LEU ARG ASN ASP PHE ALA ASP PRO LEU ALA THR
SEQRES 12 A 396 ALA LEU HIS CYS LYS VAL LEU GLY ILE PRO GLN GLU ASP
SEQRES 13 A 396 GLY PRO LYS LEU PHE ARG SER LEU SER ILE ALA PHE MET
SEQRES 14 A 396 SER SER ALA ASP PRO ILE PRO ALA ALA LYS ILE ASN TRP
SEQRES 15 A 396 ASP ARG ASP ILE GLU TYR MET ALA GLY ILE LEU GLU ASN
SEQRES 16 A 396 PRO ASN ILE THR THR GLY LEU MET GLY GLU LEU SER ARG
SEQRES 17 A 396 LEU ARG LYS ASP PRO ALA TYR SER HIS VAL SER ASP GLU
SEQRES 18 A 396 LEU PHE ALA THR ILE GLY VAL THR PHE PHE GLY ALA GLY
SEQRES 19 A 396 VAL ILE SER THR GLY SER PHE LEU THR THR ALA LEU ILE
SEQRES 20 A 396 SER LEU ILE GLN ARG PRO GLN LEU ARG ASN LEU LEU HIS
SEQRES 21 A 396 GLU LYS PRO GLU LEU ILE PRO ALA GLY VAL GLU GLU LEU
SEQRES 22 A 396 LEU ARG ILE ASN LEU SER PHE ALA ASP GLY LEU PRO ARG
SEQRES 23 A 396 LEU ALA THR ALA ASP ILE GLN VAL GLY ASP VAL LEU VAL
SEQRES 24 A 396 ARG LYS GLY GLU LEU VAL LEU VAL LEU LEU GLU GLY ALA
SEQRES 25 A 396 ASN PHE ASP PRO GLU HIS PHE PRO ASN PRO GLY SER ILE
SEQRES 26 A 396 GLU LEU ASP ARG PRO ASN PRO THR SER HIS LEU ALA PHE
SEQRES 27 A 396 GLY ARG GLY GLN HIS PHE CYS PRO GLY SER ALA LEU GLY
SEQRES 28 A 396 ARG ARG HIS ALA GLN ILE GLY ILE GLU ALA LEU LEU LYS
SEQRES 29 A 396 LYS MET PRO GLY VAL ASP LEU ALA VAL PRO ILE ASP GLN
SEQRES 30 A 396 LEU VAL TRP ARG THR ARG PHE GLN ARG ARG ILE PRO GLU
SEQRES 31 A 396 ARG LEU PRO VAL LEU TRP
HET HEM A 401 43
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET MQN A 407 12
HET MQN A 408 12
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETNAM MQN 2-METHYLQUINOLIN-6-AMINE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 MQN 2(C10 H10 N2)
FORMUL 10 HOH *784(H2 O)
HELIX 1 1 ASP A 20 GLU A 29 1 10
HELIX 2 2 SER A 47 GLU A 56 1 10
HELIX 3 3 MET A 62 ALA A 67 5 6
HELIX 4 4 PRO A 79 VAL A 83 5 5
HELIX 5 5 ASN A 84 ALA A 92 1 9
HELIX 6 6 LEU A 94 ILE A 102 1 9
HELIX 7 7 GLY A 108 GLY A 128 1 21
HELIX 8 8 PHE A 137 GLY A 151 1 15
HELIX 9 9 PRO A 153 GLU A 155 5 3
HELIX 10 10 ASP A 156 SER A 163 1 8
HELIX 11 11 SER A 163 PHE A 168 1 6
HELIX 12 12 ILE A 175 GLU A 194 1 20
HELIX 13 13 THR A 200 LYS A 211 1 12
HELIX 14 14 ASP A 212 SER A 216 5 5
HELIX 15 15 SER A 219 GLN A 251 1 33
HELIX 16 16 ARG A 252 LYS A 262 1 11
HELIX 17 17 LEU A 265 ILE A 276 1 12
HELIX 18 18 LEU A 308 PHE A 314 1 7
HELIX 19 19 ARG A 340 PHE A 344 5 5
HELIX 20 20 GLY A 347 MET A 366 1 20
HELIX 21 21 PRO A 374 LEU A 378 5 5
SHEET 1 A 5 ILE A 31 ARG A 35 0
SHEET 2 A 5 GLU A 41 VAL A 45 -1 O LEU A 44 N ARG A 32
SHEET 3 A 5 LEU A 304 VAL A 307 1 O LEU A 306 N TRP A 43
SHEET 4 A 5 LEU A 284 ALA A 288 -1 N ARG A 286 O VAL A 305
SHEET 5 A 5 PHE A 60 SER A 61 -1 N SER A 61 O LEU A 287
SHEET 1 B 3 ALA A 131 ASP A 132 0
SHEET 2 B 3 PRO A 393 LEU A 395 -1 O VAL A 394 N ALA A 131
SHEET 3 B 3 ASP A 370 LEU A 371 -1 N ASP A 370 O LEU A 395
SHEET 1 C 2 ILE A 292 VAL A 294 0
SHEET 2 C 2 VAL A 297 VAL A 299 -1 O VAL A 297 N VAL A 294
LINK SG CYS A 345 FE HEM A 401 1555 1555 2.23
LINK FE HEM A 401 NAB MQN A 408 1555 1555 2.32
CISPEP 1 VAL A 9 PRO A 10 0 -1.00
CISPEP 2 ALA A 129 PRO A 130 0 -1.94
SITE 1 AC1 22 MET A 62 MET A 86 HIS A 146 PHE A 230
SITE 2 AC1 22 GLY A 234 SER A 237 PHE A 280 LEU A 284
SITE 3 AC1 22 ARG A 286 ALA A 337 PHE A 338 GLY A 339
SITE 4 AC1 22 HIS A 343 CYS A 345 PRO A 346 GLY A 347
SITE 5 AC1 22 MQN A 408 HOH A 549 HOH A 558 HOH A 602
SITE 6 AC1 22 HOH A 637 HOH A 787
SITE 1 AC2 8 LYS A 211 PRO A 330 ASN A 331 PRO A 332
SITE 2 AC2 8 THR A 333 SER A 334 HOH A 668 HOH A 750
SITE 1 AC3 6 SER A 12 HOH A 692 HOH A 789 HOH A 843
SITE 2 AC3 6 HOH A 978 HOH A1172
SITE 1 AC4 9 ARG A 58 SER A 61 MET A 62 LYS A 63
SITE 2 AC4 9 HIS A 343 HOH A 586 HOH A 609 HOH A 713
SITE 3 AC4 9 HOH A1133
SITE 1 AC5 8 ARG A 32 MQN A 407 HOH A 646 HOH A1016
SITE 2 AC5 8 HOH A1117 HOH A1169 HOH A1192 HOH A1206
SITE 1 AC6 7 LYS A 33 ARG A 300 MQN A 407 HOH A 781
SITE 2 AC6 7 HOH A 968 HOH A1168 HOH A1196
SITE 1 AC7 10 THR A 4 VAL A 5 LEU A 6 ARG A 300
SITE 2 AC7 10 LYS A 301 GLU A 303 SO4 A 405 SO4 A 406
SITE 3 AC7 10 HOH A1204 HOH A1206
SITE 1 AC8 6 ALA A 233 SER A 237 ARG A 386 HEM A 401
SITE 2 AC8 6 HOH A 549 HOH A 707
CRYST1 77.800 77.800 264.300 90.00 90.00 120.00 P 65 2 2 12
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 0.012853 0.007421 0.000000 0.00000
SCALE2 0.000000 0.014842 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003784 0.00000
(ATOM LINES ARE NOT SHOWN.)
END