HEADER TRANSFERASE/TRANSFERASE INHIBITOR 12-JUL-12 4G2R
TITLE CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE SUBUNIT OF ACC (ACCD6) IN
TITLE 2 COMPLEX WITH INHIBITOR HALOXYFOP FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACCD6, CARBOXYLTRANSFERASE BETA-SUBUNIT OF ACYL-COA
COMPND 3 CARBOXYLASE;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: PCCASE, PROPANOYL-COA:CARBON DIOXIDE LIGASE;
COMPND 6 EC: 6.4.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: ACCD6, MT2307, MTCY427.28, RV2247;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC,
KEYWDS 2 CROTONASE SUPER FAMILY, CARBOXYLTRANSFERASE, TRANSFERASE-HERBICIDE
KEYWDS 3 COMPLEX, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX,
KEYWDS 4 PSI-2, PROTEIN STRUCTURE INITIATIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.M.REDDY,J.B.BRUNING,C.THURMAN,M.SHEREKAR,S.VALLURU,H.EHRENFELD,
AUTHOR 2 J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 4 13-SEP-23 4G2R 1 REMARK
REVDAT 3 01-OCT-14 4G2R 1 JRNL
REVDAT 2 13-AUG-14 4G2R 1 JRNL
REVDAT 1 19-FEB-14 4G2R 0
JRNL AUTH M.C.REDDY,A.BREDA,J.B.BRUNING,M.SHEREKAR,S.VALLURU,
JRNL AUTH 2 C.THURMAN,H.EHRENFELD,J.C.SACCHETTINI
JRNL TITL STRUCTURE, ACTIVITY, AND INHIBITION OF THE
JRNL TITL 2 CARBOXYLTRANSFERASE BETA-SUBUNIT OF ACETYL COENZYME A
JRNL TITL 3 CARBOXYLASE (ACCD6) FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF ANTIMICROB.AGENTS CHEMOTHER. V. 58 6122 2014
JRNL REFN ISSN 0066-4804
JRNL PMID 25092705
JRNL DOI 10.1128/AAC.02574-13
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.630
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
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 58.9638 - 5.5010 1.00 3969 161 0.1680 0.1711
REMARK 3 2 5.5010 - 4.3667 1.00 3821 145 0.1214 0.1384
REMARK 3 3 4.3667 - 3.8149 1.00 3818 135 0.1290 0.1736
REMARK 3 4 3.8149 - 3.4661 1.00 3782 147 0.1458 0.1650
REMARK 3 5 3.4661 - 3.2177 1.00 3793 145 0.1577 0.2000
REMARK 3 6 3.2177 - 3.0280 1.00 3765 136 0.1736 0.2026
REMARK 3 7 3.0280 - 2.8764 1.00 3751 148 0.1833 0.2390
REMARK 3 8 2.8764 - 2.7512 1.00 3763 138 0.1863 0.2544
REMARK 3 9 2.7512 - 2.6452 1.00 3768 143 0.1877 0.2380
REMARK 3 10 2.6452 - 2.5540 1.00 3744 138 0.1978 0.2557
REMARK 3 11 2.5540 - 2.4741 1.00 3747 132 0.1998 0.2806
REMARK 3 12 2.4741 - 2.4034 1.00 3732 136 0.2268 0.2720
REMARK 3 13 2.4034 - 2.3401 1.00 3759 145 0.2544 0.3382
REMARK 3 14 2.3401 - 2.2830 1.00 3709 147 0.2663 0.3217
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 53.81
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.210
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) : 4.71440
REMARK 3 B22 (A**2) : 7.27960
REMARK 3 B33 (A**2) : -11.99400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 6777
REMARK 3 ANGLE : 1.130 9235
REMARK 3 CHIRALITY : 0.083 1042
REMARK 3 PLANARITY : 0.005 1219
REMARK 3 DIHEDRAL : 14.578 2441
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -37.0146 -22.9992 40.3613
REMARK 3 T TENSOR
REMARK 3 T11: 0.1755 T22: 0.1730
REMARK 3 T33: 0.2275 T12: -0.0144
REMARK 3 T13: -0.0090 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 0.6170 L22: 0.5563
REMARK 3 L33: 1.0951 L12: 0.1024
REMARK 3 L13: -0.2526 L23: -0.4306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0502 S13: 0.0583
REMARK 3 S21: 0.0625 S22: 0.0136 S23: 0.0595
REMARK 3 S31: -0.0680 S32: -0.0988 S33: -0.0185
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 4G2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000073664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-11
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : DOUBLE-CRYSTAL, SI(111) LIQUID
REMARK 200 N2 COOLED
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54953
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 58.944
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.50800
REMARK 200 R SYM FOR SHELL (I) : 0.50800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 4FB8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5 M SODIUM FORMATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.89000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.12000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 80.85000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.89000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.12000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.85000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.89000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.12000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.85000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.89000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.12000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.85000
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: 8860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 1
REMARK 465 THR A 2
REMARK 465 ILE A 3
REMARK 465 MET A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 VAL A 9
REMARK 465 GLY A 10
REMARK 465 GLU A 11
REMARK 465 SER A 12
REMARK 465 ASP A 163
REMARK 465 VAL A 164
REMARK 465 VAL A 165
REMARK 465 ARG A 166
REMARK 465 SER A 167
REMARK 465 VAL A 168
REMARK 465 THR A 169
REMARK 465 GLY A 170
REMARK 465 GLU A 171
REMARK 465 ASP A 172
REMARK 465 VAL A 173
REMARK 465 ASP A 174
REMARK 465 MET A 175
REMARK 465 GLU A 301
REMARK 465 ARG A 467
REMARK 465 HIS A 468
REMARK 465 LYS A 469
REMARK 465 ASN A 470
REMARK 465 ILE A 471
REMARK 465 PRO A 472
REMARK 465 LEU A 473
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ILE B 3
REMARK 465 MET B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 VAL B 9
REMARK 465 GLY B 10
REMARK 465 GLU B 11
REMARK 465 SER B 12
REMARK 465 LEU B 13
REMARK 465 ASP B 163
REMARK 465 VAL B 164
REMARK 465 VAL B 165
REMARK 465 ARG B 166
REMARK 465 SER B 167
REMARK 465 VAL B 168
REMARK 465 THR B 169
REMARK 465 GLY B 170
REMARK 465 GLU B 171
REMARK 465 ASP B 172
REMARK 465 VAL B 173
REMARK 465 ASP B 174
REMARK 465 ARG B 467
REMARK 465 HIS B 468
REMARK 465 LYS B 469
REMARK 465 ASN B 470
REMARK 465 ILE B 471
REMARK 465 PRO B 472
REMARK 465 LEU B 473
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 LEU A 13 CG CD1 CD2
REMARK 470 SER A 23 OG
REMARK 470 GLU A 36 CG CD OE1 OE2
REMARK 470 THR A 160 OG1 CG2
REMARK 470 GLU A 182 CG CD OE1 OE2
REMARK 470 THR A 183 OG1 CG2
REMARK 470 HIS A 184 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 186 CG CD CE NZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 VAL A 330 CG1 CG2
REMARK 470 ASP A 331 CG OD1 OD2
REMARK 470 GLU A 411 CG CD OE1 OE2
REMARK 470 GLU A 413 CG CD OE1 OE2
REMARK 470 ARG A 414 CZ NH1 NH2
REMARK 470 GLU A 415 CG CD OE1 OE2
REMARK 470 ASP B 28 CG OD1 OD2
REMARK 470 GLU B 182 CG CD OE1 OE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 ASP B 331 CG OD1 OD2
REMARK 470 GLN B 332 CG CD OE1 NE2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 LYS B 403 CE NZ
REMARK 470 LYS B 404 CE NZ
REMARK 470 GLU B 411 CG CD OE1 OE2
REMARK 470 HIS B 412 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 415 CG CD OE1 OE2
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 OG SER B 188 O HOH B 894 2.03
REMARK 500 O HOH A 670 O HOH A 800 2.05
REMARK 500 OG SER A 188 O HOH A 929 2.06
REMARK 500 NH1 ARG A 305 O HOH A 925 2.07
REMARK 500 O HOH A 903 O HOH B 700 2.08
REMARK 500 O HOH A 629 O HOH A 651 2.10
REMARK 500 O HOH A 909 O HOH A 935 2.10
REMARK 500 O HOH B 604 O HOH B 841 2.11
REMARK 500 O HOH A 757 O HOH A 922 2.14
REMARK 500 O HOH A 910 O HOH B 648 2.14
REMARK 500 O HOH A 621 O HOH A 851 2.15
REMARK 500 NZ LYS A 343 O HOH A 942 2.15
REMARK 500 OE1 GLU A 333 O HOH A 702 2.15
REMARK 500 O HOH B 694 O HOH B 882 2.16
REMARK 500 OD1 ASP B 203 O HOH B 860 2.16
REMARK 500 O HOH B 735 O HOH B 779 2.16
REMARK 500 O PRO B 181 O HOH B 893 2.17
REMARK 500 O SER B 238 O HOH B 814 2.17
REMARK 500 O HOH B 794 O HOH B 840 2.18
REMARK 500 O HOH A 754 O HOH A 917 2.18
REMARK 500 O HOH B 742 O HOH B 785 2.19
REMARK 500 O HOH B 608 O HOH B 895 2.19
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 ASP A 38 -155.39 -139.24
REMARK 500 HIS A 95 93.25 -160.45
REMARK 500 HIS A 184 -58.82 -152.71
REMARK 500 ASP A 255 58.66 -115.76
REMARK 500 ASP A 322 81.33 -150.03
REMARK 500 VAL A 330 -76.16 -44.86
REMARK 500 ASP A 331 46.81 -89.02
REMARK 500 ARG A 361 -71.13 -124.65
REMARK 500 ARG A 465 146.74 81.98
REMARK 500 HIS B 184 -64.59 -127.48
REMARK 500 ASP B 322 77.76 -152.11
REMARK 500 VAL B 330 -77.93 -68.21
REMARK 500 ARG B 361 -74.91 -120.69
REMARK 500 ARG B 465 145.42 157.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 329 VAL B 330 -148.91
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 H1L A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H1L A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H1L B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H1L B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FB8 RELATED DB: PDB
REMARK 900 APO STRUCTURE OF ENZYME
REMARK 900 RELATED ID: TB-RV2247 RELATED DB: TARGETTRACK
DBREF 4G2R A 1 473 UNP P63407 PCC6_MYCTU 1 473
DBREF 4G2R B 1 473 UNP P63407 PCC6_MYCTU 1 473
SEQRES 1 A 473 MET THR ILE MET ALA PRO GLU ALA VAL GLY GLU SER LEU
SEQRES 2 A 473 ASP PRO ARG ASP PRO LEU LEU ARG LEU SER ASN PHE PHE
SEQRES 3 A 473 ASP ASP GLY SER VAL GLU LEU LEU HIS GLU ARG ASP ARG
SEQRES 4 A 473 SER GLY VAL LEU ALA ALA ALA GLY THR VAL ASN GLY VAL
SEQRES 5 A 473 ARG THR ILE ALA PHE CYS THR ASP GLY THR VAL MET GLY
SEQRES 6 A 473 GLY ALA MET GLY VAL GLU GLY CYS THR HIS ILE VAL ASN
SEQRES 7 A 473 ALA TYR ASP THR ALA ILE GLU ASP GLN SER PRO ILE VAL
SEQRES 8 A 473 GLY ILE TRP HIS SER GLY GLY ALA ARG LEU ALA GLU GLY
SEQRES 9 A 473 VAL ARG ALA LEU HIS ALA VAL GLY GLN VAL PHE GLU ALA
SEQRES 10 A 473 MET ILE ARG ALA SER GLY TYR ILE PRO GLN ILE SER VAL
SEQRES 11 A 473 VAL VAL GLY PHE ALA ALA GLY GLY ALA ALA TYR GLY PRO
SEQRES 12 A 473 ALA LEU THR ASP VAL VAL VAL MET ALA PRO GLU SER ARG
SEQRES 13 A 473 VAL PHE VAL THR GLY PRO ASP VAL VAL ARG SER VAL THR
SEQRES 14 A 473 GLY GLU ASP VAL ASP MET ALA SER LEU GLY GLY PRO GLU
SEQRES 15 A 473 THR HIS HIS LYS LYS SER GLY VAL CYS HIS ILE VAL ALA
SEQRES 16 A 473 ASP ASP GLU LEU ASP ALA TYR ASP ARG GLY ARG ARG LEU
SEQRES 17 A 473 VAL GLY LEU PHE CYS GLN GLN GLY HIS PHE ASP ARG SER
SEQRES 18 A 473 LYS ALA GLU ALA GLY ASP THR ASP ILE HIS ALA LEU LEU
SEQRES 19 A 473 PRO GLU SER SER ARG ARG ALA TYR ASP VAL ARG PRO ILE
SEQRES 20 A 473 VAL THR ALA ILE LEU ASP ALA ASP THR PRO PHE ASP GLU
SEQRES 21 A 473 PHE GLN ALA ASN TRP ALA PRO SER MET VAL VAL GLY LEU
SEQRES 22 A 473 GLY ARG LEU SER GLY ARG THR VAL GLY VAL LEU ALA ASN
SEQRES 23 A 473 ASN PRO LEU ARG LEU GLY GLY CYS LEU ASN SER GLU SER
SEQRES 24 A 473 ALA GLU LYS ALA ALA ARG PHE VAL ARG LEU CYS ASP ALA
SEQRES 25 A 473 PHE GLY ILE PRO LEU VAL VAL VAL VAL ASP VAL PRO GLY
SEQRES 26 A 473 TYR LEU PRO GLY VAL ASP GLN GLU TRP GLY GLY VAL VAL
SEQRES 27 A 473 ARG ARG GLY ALA LYS LEU LEU HIS ALA PHE GLY GLU CYS
SEQRES 28 A 473 THR VAL PRO ARG VAL THR LEU VAL THR ARG LYS THR TYR
SEQRES 29 A 473 GLY GLY ALA TYR ILE ALA MET ASN SER ARG SER LEU ASN
SEQRES 30 A 473 ALA THR LYS VAL PHE ALA TRP PRO ASP ALA GLU VAL ALA
SEQRES 31 A 473 VAL MET GLY ALA LYS ALA ALA VAL GLY ILE LEU HIS LYS
SEQRES 32 A 473 LYS LYS LEU ALA ALA ALA PRO GLU HIS GLU ARG GLU ALA
SEQRES 33 A 473 LEU HIS ASP GLN LEU ALA ALA GLU HIS GLU ARG ILE ALA
SEQRES 34 A 473 GLY GLY VAL ASP SER ALA LEU ASP ILE GLY VAL VAL ASP
SEQRES 35 A 473 GLU LYS ILE ASP PRO ALA HIS THR ARG SER LYS LEU THR
SEQRES 36 A 473 GLU ALA LEU ALA GLN ALA PRO ALA ARG ARG GLY ARG HIS
SEQRES 37 A 473 LYS ASN ILE PRO LEU
SEQRES 1 B 473 MET THR ILE MET ALA PRO GLU ALA VAL GLY GLU SER LEU
SEQRES 2 B 473 ASP PRO ARG ASP PRO LEU LEU ARG LEU SER ASN PHE PHE
SEQRES 3 B 473 ASP ASP GLY SER VAL GLU LEU LEU HIS GLU ARG ASP ARG
SEQRES 4 B 473 SER GLY VAL LEU ALA ALA ALA GLY THR VAL ASN GLY VAL
SEQRES 5 B 473 ARG THR ILE ALA PHE CYS THR ASP GLY THR VAL MET GLY
SEQRES 6 B 473 GLY ALA MET GLY VAL GLU GLY CYS THR HIS ILE VAL ASN
SEQRES 7 B 473 ALA TYR ASP THR ALA ILE GLU ASP GLN SER PRO ILE VAL
SEQRES 8 B 473 GLY ILE TRP HIS SER GLY GLY ALA ARG LEU ALA GLU GLY
SEQRES 9 B 473 VAL ARG ALA LEU HIS ALA VAL GLY GLN VAL PHE GLU ALA
SEQRES 10 B 473 MET ILE ARG ALA SER GLY TYR ILE PRO GLN ILE SER VAL
SEQRES 11 B 473 VAL VAL GLY PHE ALA ALA GLY GLY ALA ALA TYR GLY PRO
SEQRES 12 B 473 ALA LEU THR ASP VAL VAL VAL MET ALA PRO GLU SER ARG
SEQRES 13 B 473 VAL PHE VAL THR GLY PRO ASP VAL VAL ARG SER VAL THR
SEQRES 14 B 473 GLY GLU ASP VAL ASP MET ALA SER LEU GLY GLY PRO GLU
SEQRES 15 B 473 THR HIS HIS LYS LYS SER GLY VAL CYS HIS ILE VAL ALA
SEQRES 16 B 473 ASP ASP GLU LEU ASP ALA TYR ASP ARG GLY ARG ARG LEU
SEQRES 17 B 473 VAL GLY LEU PHE CYS GLN GLN GLY HIS PHE ASP ARG SER
SEQRES 18 B 473 LYS ALA GLU ALA GLY ASP THR ASP ILE HIS ALA LEU LEU
SEQRES 19 B 473 PRO GLU SER SER ARG ARG ALA TYR ASP VAL ARG PRO ILE
SEQRES 20 B 473 VAL THR ALA ILE LEU ASP ALA ASP THR PRO PHE ASP GLU
SEQRES 21 B 473 PHE GLN ALA ASN TRP ALA PRO SER MET VAL VAL GLY LEU
SEQRES 22 B 473 GLY ARG LEU SER GLY ARG THR VAL GLY VAL LEU ALA ASN
SEQRES 23 B 473 ASN PRO LEU ARG LEU GLY GLY CYS LEU ASN SER GLU SER
SEQRES 24 B 473 ALA GLU LYS ALA ALA ARG PHE VAL ARG LEU CYS ASP ALA
SEQRES 25 B 473 PHE GLY ILE PRO LEU VAL VAL VAL VAL ASP VAL PRO GLY
SEQRES 26 B 473 TYR LEU PRO GLY VAL ASP GLN GLU TRP GLY GLY VAL VAL
SEQRES 27 B 473 ARG ARG GLY ALA LYS LEU LEU HIS ALA PHE GLY GLU CYS
SEQRES 28 B 473 THR VAL PRO ARG VAL THR LEU VAL THR ARG LYS THR TYR
SEQRES 29 B 473 GLY GLY ALA TYR ILE ALA MET ASN SER ARG SER LEU ASN
SEQRES 30 B 473 ALA THR LYS VAL PHE ALA TRP PRO ASP ALA GLU VAL ALA
SEQRES 31 B 473 VAL MET GLY ALA LYS ALA ALA VAL GLY ILE LEU HIS LYS
SEQRES 32 B 473 LYS LYS LEU ALA ALA ALA PRO GLU HIS GLU ARG GLU ALA
SEQRES 33 B 473 LEU HIS ASP GLN LEU ALA ALA GLU HIS GLU ARG ILE ALA
SEQRES 34 B 473 GLY GLY VAL ASP SER ALA LEU ASP ILE GLY VAL VAL ASP
SEQRES 35 B 473 GLU LYS ILE ASP PRO ALA HIS THR ARG SER LYS LEU THR
SEQRES 36 B 473 GLU ALA LEU ALA GLN ALA PRO ALA ARG ARG GLY ARG HIS
SEQRES 37 B 473 LYS ASN ILE PRO LEU
HET H1L A 501 24
HET H1L A 502 24
HET H1L B 501 24
HET H1L B 502 24
HETNAM H1L (2R)-2-(4-{[3-CHLORO-5-(TRIFLUOROMETHYL)PYRIDIN-2-
HETNAM 2 H1L YL]OXY}PHENOXY)PROPANOIC ACID
HETSYN H1L HALOXYFOP INHIBITOR, R ENANTIOMER
FORMUL 3 H1L 4(C15 H11 CL F3 N O4)
FORMUL 7 HOH *691(H2 O)
HELIX 1 1 LEU A 13 ARG A 16 5 4
HELIX 2 2 ASP A 17 PHE A 26 1 10
HELIX 3 3 VAL A 63 ALA A 67 5 5
HELIX 4 4 GLY A 69 GLN A 87 1 19
HELIX 5 5 ARG A 100 GLU A 103 5 4
HELIX 6 6 GLY A 104 SER A 122 1 19
HELIX 7 7 GLY A 137 LEU A 145 1 9
HELIX 8 8 HIS A 184 SER A 188 5 5
HELIX 9 9 ASP A 197 GLN A 214 1 18
HELIX 10 10 ASP A 219 GLY A 226 1 8
HELIX 11 11 ASP A 229 LEU A 234 5 6
HELIX 12 12 VAL A 244 LEU A 252 1 9
HELIX 13 13 ARG A 290 CYS A 294 5 5
HELIX 14 14 SER A 299 ALA A 300 5 2
HELIX 15 15 LYS A 302 LYS A 302 5 1
HELIX 16 16 ALA A 303 GLY A 314 1 12
HELIX 17 17 TRP A 334 CYS A 351 1 18
HELIX 18 18 GLY A 365 MET A 371 1 7
HELIX 19 19 SER A 373 ASN A 377 5 5
HELIX 20 20 GLY A 393 HIS A 402 1 10
HELIX 21 21 HIS A 402 ALA A 409 1 8
HELIX 22 22 PRO A 410 ALA A 429 1 20
HELIX 23 23 GLY A 431 GLY A 439 1 9
HELIX 24 24 ASP A 446 ALA A 448 5 3
HELIX 25 25 HIS A 449 ALA A 461 1 13
HELIX 26 26 ASP B 17 PHE B 26 1 10
HELIX 27 27 VAL B 63 ALA B 67 5 5
HELIX 28 28 GLY B 69 GLN B 87 1 19
HELIX 29 29 ARG B 100 GLU B 103 5 4
HELIX 30 30 GLY B 104 SER B 122 1 19
HELIX 31 31 GLY B 137 LEU B 145 1 9
HELIX 32 32 HIS B 184 SER B 188 5 5
HELIX 33 33 ASP B 197 GLN B 214 1 18
HELIX 34 34 ASP B 219 GLY B 226 1 8
HELIX 35 35 ASP B 229 LEU B 234 5 6
HELIX 36 36 VAL B 244 LEU B 252 1 9
HELIX 37 37 ARG B 290 CYS B 294 5 5
HELIX 38 38 SER B 297 PHE B 313 1 17
HELIX 39 39 TRP B 334 CYS B 351 1 18
HELIX 40 40 GLY B 365 MET B 371 1 7
HELIX 41 41 SER B 373 ASN B 377 5 5
HELIX 42 42 GLY B 393 HIS B 402 1 10
HELIX 43 43 HIS B 402 ALA B 409 1 8
HELIX 44 44 PRO B 410 ALA B 429 1 20
HELIX 45 45 GLY B 431 GLY B 439 1 9
HELIX 46 46 ASP B 446 ALA B 448 5 3
HELIX 47 47 HIS B 449 ALA B 461 1 13
SHEET 1 A 7 GLU A 32 LEU A 33 0
SHEET 2 A 7 VAL A 42 VAL A 49 -1 O ALA A 46 N GLU A 32
SHEET 3 A 7 VAL A 52 THR A 59 -1 O THR A 54 N GLY A 47
SHEET 4 A 7 ILE A 90 SER A 96 1 O ILE A 93 N PHE A 57
SHEET 5 A 7 GLN A 127 ALA A 136 1 O VAL A 130 N GLY A 92
SHEET 6 A 7 ARG A 156 VAL A 159 1 O ARG A 156 N ALA A 135
SHEET 7 A 7 SER A 177 GLY A 179 -1 O GLY A 179 N VAL A 157
SHEET 1 B 7 GLU A 32 LEU A 33 0
SHEET 2 B 7 VAL A 42 VAL A 49 -1 O ALA A 46 N GLU A 32
SHEET 3 B 7 VAL A 52 THR A 59 -1 O THR A 54 N GLY A 47
SHEET 4 B 7 ILE A 90 SER A 96 1 O ILE A 93 N PHE A 57
SHEET 5 B 7 GLN A 127 ALA A 136 1 O VAL A 130 N GLY A 92
SHEET 6 B 7 VAL A 148 MET A 151 1 O VAL A 150 N VAL A 131
SHEET 7 B 7 ILE A 193 VAL A 194 1 O ILE A 193 N MET A 151
SHEET 1 C 6 ASP A 259 PHE A 261 0
SHEET 2 C 6 MET A 269 LEU A 276 -1 O LEU A 273 N ASP A 259
SHEET 3 C 6 ARG A 279 ASN A 286 -1 O ALA A 285 N VAL A 270
SHEET 4 C 6 LEU A 317 VAL A 323 1 O VAL A 320 N LEU A 284
SHEET 5 C 6 ARG A 355 TYR A 364 1 O LEU A 358 N VAL A 319
SHEET 6 C 6 GLU A 388 ALA A 390 1 O GLU A 388 N ARG A 361
SHEET 1 D 7 ASP A 259 PHE A 261 0
SHEET 2 D 7 MET A 269 LEU A 276 -1 O LEU A 273 N ASP A 259
SHEET 3 D 7 ARG A 279 ASN A 286 -1 O ALA A 285 N VAL A 270
SHEET 4 D 7 LEU A 317 VAL A 323 1 O VAL A 320 N LEU A 284
SHEET 5 D 7 ARG A 355 TYR A 364 1 O LEU A 358 N VAL A 319
SHEET 6 D 7 LYS A 380 ALA A 383 1 O PHE A 382 N THR A 357
SHEET 7 D 7 GLU A 443 LYS A 444 1 O GLU A 443 N ALA A 383
SHEET 1 E 7 GLU B 32 LEU B 33 0
SHEET 2 E 7 VAL B 42 VAL B 49 -1 O ALA B 46 N GLU B 32
SHEET 3 E 7 VAL B 52 THR B 59 -1 O THR B 54 N GLY B 47
SHEET 4 E 7 ILE B 90 SER B 96 1 O ILE B 93 N PHE B 57
SHEET 5 E 7 GLN B 127 ALA B 136 1 O VAL B 130 N GLY B 92
SHEET 6 E 7 ARG B 156 THR B 160 1 O ARG B 156 N ALA B 135
SHEET 7 E 7 ALA B 176 GLY B 179 -1 O GLY B 179 N VAL B 157
SHEET 1 F 7 GLU B 32 LEU B 33 0
SHEET 2 F 7 VAL B 42 VAL B 49 -1 O ALA B 46 N GLU B 32
SHEET 3 F 7 VAL B 52 THR B 59 -1 O THR B 54 N GLY B 47
SHEET 4 F 7 ILE B 90 SER B 96 1 O ILE B 93 N PHE B 57
SHEET 5 F 7 GLN B 127 ALA B 136 1 O VAL B 130 N GLY B 92
SHEET 6 F 7 VAL B 148 MET B 151 1 O VAL B 150 N SER B 129
SHEET 7 F 7 ILE B 193 VAL B 194 1 O ILE B 193 N MET B 151
SHEET 1 G 6 ASP B 259 PHE B 261 0
SHEET 2 G 6 MET B 269 LEU B 276 -1 O LEU B 273 N ASP B 259
SHEET 3 G 6 ARG B 279 ASN B 286 -1 O ALA B 285 N VAL B 270
SHEET 4 G 6 LEU B 317 VAL B 323 1 O VAL B 318 N GLY B 282
SHEET 5 G 6 ARG B 355 TYR B 364 1 O LEU B 358 N VAL B 319
SHEET 6 G 6 GLU B 388 ALA B 390 1 O GLU B 388 N ARG B 361
SHEET 1 H 7 ASP B 259 PHE B 261 0
SHEET 2 H 7 MET B 269 LEU B 276 -1 O LEU B 273 N ASP B 259
SHEET 3 H 7 ARG B 279 ASN B 286 -1 O ALA B 285 N VAL B 270
SHEET 4 H 7 LEU B 317 VAL B 323 1 O VAL B 318 N GLY B 282
SHEET 5 H 7 ARG B 355 TYR B 364 1 O LEU B 358 N VAL B 319
SHEET 6 H 7 LYS B 380 ALA B 383 1 O PHE B 382 N THR B 357
SHEET 7 H 7 GLU B 443 LYS B 444 1 O GLU B 443 N ALA B 383
SHEET 1 I 2 LEU B 295 ASN B 296 0
SHEET 2 I 2 TYR B 326 LEU B 327 1 O LEU B 327 N LEU B 295
CISPEP 1 VAL B 330 ASP B 331 0 4.49
SITE 1 AC1 13 GLY A 98 ALA A 99 LEU A 108 GLY A 137
SITE 2 AC1 13 GLY A 138 TYR A 141 HOH A 940 LEU B 295
SITE 3 AC1 13 TYR B 326 VAL B 337 GLY B 341 GLY B 366
SITE 4 AC1 13 ALA B 370
SITE 1 AC2 15 VAL A 131 ALA A 140 PRO A 143 VAL A 149
SITE 2 AC2 15 MET A 151 VAL A 157 HIS A 184 HIS A 185
SITE 3 AC2 15 SER A 188 HOH A 928 GLN B 332 GLU B 333
SITE 4 AC2 15 TRP B 334 GLY B 335 VAL B 338
SITE 1 AC3 15 LEU A 295 TYR A 326 VAL A 337 GLY A 341
SITE 2 AC3 15 GLY A 366 ALA A 370 GLY B 98 ALA B 99
SITE 3 AC3 15 LEU B 108 PHE B 115 GLY B 137 GLY B 138
SITE 4 AC3 15 TYR B 141 HOH B 777 HOH B 857
SITE 1 AC4 16 GLN A 332 GLU A 333 TRP A 334 VAL A 338
SITE 2 AC4 16 VAL B 131 ALA B 140 PRO B 143 VAL B 149
SITE 3 AC4 16 MET B 151 VAL B 157 VAL B 159 SER B 177
SITE 4 AC4 16 HIS B 184 HIS B 185 SER B 188 HOH B 941
CRYST1 117.780 126.240 161.700 90.00 90.00 90.00 I 2 2 2 16
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 0.008490 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
