HEADER OXIDOREDUCTASE 03-JUL-12 4FXS
TITLE INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE FROM VIBRIO CHOLERAE COMPLEXED
TITLE 2 WITH IMP AND MYCOPHENOLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.205;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: VC0767, VC_0767;
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: PMCSG28
KEYWDS STRUCTURAL GENOMICS, IMPDH, IMP, MYCOPHENOLIC ACID, MOA, NIAID,
KEYWDS 2 NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,N.MALTSEVA,M.MAKOWSKA-GRZYSKA,R.JEDRZEJCZAK,W.F.ANDERSON,
AUTHOR 2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 2 15-NOV-17 4FXS 1 REMARK
REVDAT 1 25-JUL-12 4FXS 0
JRNL AUTH J.OSIPIUK,N.MALTSEVA,M.MAKOWSKA-GRZYSKA,R.JEDRZEJCZAK,
JRNL AUTH 2 W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE FROM VIBRIO CHOLERAE
JRNL TITL 2 COMPLEXED WITH IMP AND MYCOPHENOLIC ACID.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29244
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1541
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) : 2.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.28000
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): 0.230
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.555
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3637 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4929 ; 1.740 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 481 ; 6.775 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;38.823 ;24.178
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 635 ;19.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.590 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 576 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2692 ; 0.007 ; 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): 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 486
REMARK 3 RESIDUE RANGE : A 701 A 703
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2062 33.8535 22.1812
REMARK 3 T TENSOR
REMARK 3 T11: 0.2360 T22: 0.1132
REMARK 3 T33: 0.1335 T12: -0.0864
REMARK 3 T13: -0.0662 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 1.1532 L22: 1.2406
REMARK 3 L33: 0.9509 L12: 0.5953
REMARK 3 L13: -0.3860 L23: -0.3108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0184 S12: 0.2231 S13: 0.2836
REMARK 3 S21: -0.1271 S22: 0.0062 S23: 0.1261
REMARK 3 S31: -0.3644 S32: 0.1205 S33: 0.0122
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. U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4FXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29245
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 30.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 21.70
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 22.10
REMARK 200 R MERGE FOR SHELL (I) : 0.91300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SODIUM/POTASSIUM PHOSPHATE, 0.01 M
REMARK 280 IMP, 0.01 M MYCOPHENOLIC ACID, PH 5.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 55.98000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 94.49700
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 55.98000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 94.49700
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 55.98000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 94.49700
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 55.98000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 94.49700
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 55.98000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 94.49700
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 55.98000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 94.49700
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 55.98000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 94.49700
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 55.98000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 55.98000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 94.49700
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 MSE A 1
REMARK 465 HIS A 2
REMARK 465 GLY A 94
REMARK 465 VAL A 95
REMARK 465 ALA A 168
REMARK 465 THR A 169
REMARK 465 GLY A 170
REMARK 465 ALA A 171
REMARK 465 LYS A 179
REMARK 465 ALA A 180
REMARK 465 ARG A 181
REMARK 465 ASP A 202
REMARK 465 PHE A 203
REMARK 465 HIS A 204
REMARK 465 LYS A 205
REMARK 465 ALA A 206
REMARK 465 ASP A 408
REMARK 465 ASN A 409
REMARK 465 ALA A 410
REMARK 465 ARG A 487
REMARK 465 LEU A 488
REMARK 465 GLY A 489
REMARK 465 GLY A 490
REMARK 465 GLU A 491
REMARK 465 ASN A 492
REMARK 465 LEU A 493
REMARK 465 TYR A 494
REMARK 465 PHE A 495
REMARK 465 GLN A 496
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 GLU A 172 CG CD OE1 OE2
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 118 CG HIS A 118 CD2 0.056
REMARK 500 HIS A 253 CG HIS A 253 CD2 0.055
REMARK 500 HIS A 475 CG HIS A 475 CD2 0.061
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 PRO A 45 44.79 -81.61
REMARK 500 VAL A 54 -56.48 -125.95
REMARK 500 TYR A 117 16.62 47.20
REMARK 500 ASN A 129 119.47 -166.96
REMARK 500 ASP A 146 95.05 -59.46
REMARK 500 ASN A 189 -162.04 -118.89
REMARK 500 ALA A 200 59.28 30.52
REMARK 500 ALA A 281 11.47 -143.38
REMARK 500 LYS A 398 35.27 -70.48
REMARK 500 SER A 400 6.20 -157.16
REMARK 500 SER A 401 -152.15 -87.63
REMARK 500 ASP A 402 15.62 -158.38
REMARK 500 ARG A 403 -20.49 70.86
REMARK 500 ASP A 412 21.77 -143.61
REMARK 500 HIS A 473 167.90 -49.12
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 K A 703 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 307 O
REMARK 620 2 GLY A 304 O 87.8
REMARK 620 3 GLY A 302 O 115.4 96.2
REMARK 620 4 HOH A 828 O 70.2 123.5 54.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FEZ RELATED DB: PDB
REMARK 900 INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE FROM VIBRIO CHOLERAE,
REMARK 900 DELETION MUTANT
REMARK 900 RELATED ID: 4FF0 RELATED DB: PDB
REMARK 900 INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE FROM VIBRIO CHOLERAE,
REMARK 900 DELETION MUTANT, COMPLEXED WITH IMP
REMARK 900 RELATED ID: 4FO4 RELATED DB: PDB
REMARK 900 INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE FROM VIBRIO CHOLERAE,
REMARK 900 DELETION MUTANT, COMPLEXED WITH IMP AND MYCOPHENOLIC ACID.
REMARK 900 RELATED ID: CSGID-IDP04364 RELATED DB: TARGETTRACK
DBREF 4FXS A 1 489 UNP Q9KTW3 Q9KTW3_VIBCH 1 489
SEQADV 4FXS GLY A 490 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS GLU A 491 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS ASN A 492 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS LEU A 493 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS TYR A 494 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS PHE A 495 UNP Q9KTW3 EXPRESSION TAG
SEQADV 4FXS GLN A 496 UNP Q9KTW3 EXPRESSION TAG
SEQRES 1 A 496 MSE HIS MSE LEU ARG ILE ALA LYS GLU ALA LEU THR PHE
SEQRES 2 A 496 ASP ASP VAL LEU LEU VAL PRO ALA HIS SER THR VAL LEU
SEQRES 3 A 496 PRO ASN THR ALA ASP LEU ARG THR ARG LEU THR LYS ASN
SEQRES 4 A 496 ILE ALA LEU ASN ILE PRO MSE VAL SER ALA SER MSE ASP
SEQRES 5 A 496 THR VAL THR GLU ALA ARG LEU ALA ILE ALA LEU ALA GLN
SEQRES 6 A 496 GLU GLY GLY ILE GLY PHE ILE HIS LYS ASN MSE SER ILE
SEQRES 7 A 496 GLU GLN GLN ALA ALA GLN VAL HIS GLN VAL LYS ILE PHE
SEQRES 8 A 496 GLU ALA GLY VAL VAL THR HIS PRO VAL THR VAL ARG PRO
SEQRES 9 A 496 GLU GLN THR ILE ALA ASP VAL MSE GLU LEU THR HIS TYR
SEQRES 10 A 496 HIS GLY PHE ALA GLY PHE PRO VAL VAL THR GLU ASN ASN
SEQRES 11 A 496 GLU LEU VAL GLY ILE ILE THR GLY ARG ASP VAL ARG PHE
SEQRES 12 A 496 VAL THR ASP LEU THR LYS SER VAL ALA ALA VAL MSE THR
SEQRES 13 A 496 PRO LYS GLU ARG LEU ALA THR VAL LYS GLU GLY ALA THR
SEQRES 14 A 496 GLY ALA GLU VAL GLN GLU LYS MSE HIS LYS ALA ARG VAL
SEQRES 15 A 496 GLU LYS ILE LEU VAL VAL ASN ASP GLU PHE GLN LEU LYS
SEQRES 16 A 496 GLY MSE ILE THR ALA LYS ASP PHE HIS LYS ALA GLU SER
SEQRES 17 A 496 LYS PRO ASN ALA CYS LYS ASP GLU GLN GLY ARG LEU ARG
SEQRES 18 A 496 VAL GLY ALA ALA VAL GLY ALA ALA PRO GLY ASN GLU GLU
SEQRES 19 A 496 ARG VAL LYS ALA LEU VAL GLU ALA GLY VAL ASP VAL LEU
SEQRES 20 A 496 LEU ILE ASP SER SER HIS GLY HIS SER GLU GLY VAL LEU
SEQRES 21 A 496 GLN ARG ILE ARG GLU THR ARG ALA ALA TYR PRO HIS LEU
SEQRES 22 A 496 GLU ILE ILE GLY GLY ASN VAL ALA THR ALA GLU GLY ALA
SEQRES 23 A 496 ARG ALA LEU ILE GLU ALA GLY VAL SER ALA VAL LYS VAL
SEQRES 24 A 496 GLY ILE GLY PRO GLY SER ILE CYS THR THR ARG ILE VAL
SEQRES 25 A 496 THR GLY VAL GLY VAL PRO GLN ILE THR ALA ILE ALA ASP
SEQRES 26 A 496 ALA ALA GLY VAL ALA ASN GLU TYR GLY ILE PRO VAL ILE
SEQRES 27 A 496 ALA ASP GLY GLY ILE ARG PHE SER GLY ASP ILE SER LYS
SEQRES 28 A 496 ALA ILE ALA ALA GLY ALA SER CYS VAL MSE VAL GLY SER
SEQRES 29 A 496 MSE PHE ALA GLY THR GLU GLU ALA PRO GLY GLU VAL ILE
SEQRES 30 A 496 LEU TYR GLN GLY ARG SER TYR LYS ALA TYR ARG GLY MSE
SEQRES 31 A 496 GLY SER LEU GLY ALA MSE SER LYS GLY SER SER ASP ARG
SEQRES 32 A 496 TYR PHE GLN THR ASP ASN ALA ALA ASP LYS LEU VAL PRO
SEQRES 33 A 496 GLU GLY ILE GLU GLY ARG ILE ALA TYR LYS GLY HIS LEU
SEQRES 34 A 496 LYS GLU ILE ILE HIS GLN GLN MSE GLY GLY LEU ARG SER
SEQRES 35 A 496 CYS MSE GLY LEU THR GLY SER ALA THR VAL GLU ASP LEU
SEQRES 36 A 496 ARG THR LYS ALA GLN PHE VAL ARG ILE SER GLY ALA GLY
SEQRES 37 A 496 MSE LYS GLU SER HIS VAL HIS ASP VAL GLN ILE THR LYS
SEQRES 38 A 496 GLU ALA PRO ASN TYR ARG LEU GLY GLY GLU ASN LEU TYR
SEQRES 39 A 496 PHE GLN
MODRES 4FXS MSE A 3 MET SELENOMETHIONINE
MODRES 4FXS MSE A 46 MET SELENOMETHIONINE
MODRES 4FXS MSE A 51 MET SELENOMETHIONINE
MODRES 4FXS MSE A 76 MET SELENOMETHIONINE
MODRES 4FXS MSE A 112 MET SELENOMETHIONINE
MODRES 4FXS MSE A 155 MET SELENOMETHIONINE
MODRES 4FXS MSE A 177 MET SELENOMETHIONINE
MODRES 4FXS MSE A 197 MET SELENOMETHIONINE
MODRES 4FXS MSE A 361 MET SELENOMETHIONINE
MODRES 4FXS MSE A 365 MET SELENOMETHIONINE
MODRES 4FXS MSE A 390 MET SELENOMETHIONINE
MODRES 4FXS MSE A 396 MET SELENOMETHIONINE
MODRES 4FXS MSE A 437 MET SELENOMETHIONINE
MODRES 4FXS MSE A 444 MET SELENOMETHIONINE
MODRES 4FXS MSE A 469 MET SELENOMETHIONINE
HET MSE A 3 8
HET MSE A 46 8
HET MSE A 51 8
HET MSE A 76 8
HET MSE A 112 8
HET MSE A 155 8
HET MSE A 177 8
HET MSE A 197 8
HET MSE A 361 8
HET MSE A 365 8
HET MSE A 390 8
HET MSE A 396 8
HET MSE A 437 8
HET MSE A 444 8
HET MSE A 469 8
HET IMP A 701 23
HET MOA A 702 23
HET K A 703 1
HETNAM MSE SELENOMETHIONINE
HETNAM IMP INOSINIC ACID
HETNAM MOA MYCOPHENOLIC ACID
HETNAM K POTASSIUM ION
HETSYN MOA 6-(1,3-DIHYDRO-7-HYDROXY-5-METHOXY-4-METHYL-1-
HETSYN 2 MOA OXOISOBENZOFURAN-6-YL)-4-METHYL-4-HEXANOIC ACID
FORMUL 1 MSE 15(C5 H11 N O2 SE)
FORMUL 2 IMP C10 H13 N4 O8 P
FORMUL 3 MOA C17 H20 O6
FORMUL 4 K K 1+
FORMUL 5 HOH *87(H2 O)
HELIX 1 1 THR A 12 ASP A 14 5 3
HELIX 2 2 LEU A 26 ALA A 30 5 5
HELIX 3 3 GLU A 56 GLY A 67 1 12
HELIX 4 4 SER A 77 PHE A 91 1 15
HELIX 5 5 THR A 107 HIS A 116 1 10
HELIX 6 6 GLY A 138 ARG A 142 1 5
HELIX 7 7 SER A 150 VAL A 154 5 5
HELIX 8 8 GLU A 159 LEU A 161 5 3
HELIX 9 9 GLU A 172 LYS A 176 5 5
HELIX 10 10 ASN A 232 ALA A 242 1 11
HELIX 11 11 SER A 256 TYR A 270 1 15
HELIX 12 12 THR A 282 GLY A 293 1 12
HELIX 13 13 THR A 308 GLY A 314 1 7
HELIX 14 14 PRO A 318 ASN A 331 1 14
HELIX 15 15 GLU A 332 GLY A 334 5 3
HELIX 16 16 PHE A 345 ALA A 355 1 11
HELIX 17 17 SER A 392 LYS A 398 1 7
HELIX 18 18 HIS A 428 GLY A 448 1 21
HELIX 19 19 THR A 451 ALA A 459 1 9
HELIX 20 20 SER A 465 HIS A 473 1 9
SHEET 1 A 2 VAL A 16 LEU A 18 0
SHEET 2 A 2 PHE A 461 ARG A 463 -1 O VAL A 462 N LEU A 17
SHEET 1 B 2 THR A 34 THR A 37 0
SHEET 2 B 2 ILE A 40 LEU A 42 -1 O LEU A 42 N THR A 34
SHEET 1 C 9 MSE A 46 SER A 48 0
SHEET 2 C 9 ILE A 69 ILE A 72 1 O ILE A 69 N SER A 48
SHEET 3 C 9 GLY A 223 ALA A 225 1 O ALA A 225 N ILE A 72
SHEET 4 C 9 VAL A 246 ASP A 250 1 O LEU A 248 N ALA A 224
SHEET 5 C 9 ILE A 275 VAL A 280 1 O ILE A 276 N LEU A 247
SHEET 6 C 9 ALA A 296 VAL A 299 1 O LYS A 298 N GLY A 277
SHEET 7 C 9 VAL A 337 ASP A 340 1 O ILE A 338 N VAL A 299
SHEET 8 C 9 CYS A 359 VAL A 362 1 O MSE A 361 N ALA A 339
SHEET 9 C 9 MSE A 46 SER A 48 1 N VAL A 47 O VAL A 360
SHEET 1 D 3 GLY A 122 VAL A 126 0
SHEET 2 D 3 LEU A 132 THR A 137 -1 O ILE A 136 N PHE A 123
SHEET 3 D 3 THR A 156 PRO A 157 -1 O THR A 156 N ILE A 135
SHEET 1 E 3 THR A 163 LYS A 165 0
SHEET 2 E 3 ILE A 185 VAL A 188 1 O VAL A 188 N VAL A 164
SHEET 3 E 3 GLY A 196 ILE A 198 -1 O ILE A 198 N ILE A 185
SHEET 1 F 3 ILE A 377 LEU A 378 0
SHEET 2 F 3 SER A 383 ARG A 388 -1 O TYR A 384 N ILE A 377
SHEET 3 F 3 GLU A 420 ALA A 424 -1 O ILE A 423 N LYS A 385
LINK C MSE A 3 N LEU A 4 1555 1555 1.35
LINK C PRO A 45 N MSE A 46 1555 1555 1.34
LINK C MSE A 46 N VAL A 47 1555 1555 1.33
LINK C SER A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N ASP A 52 1555 1555 1.34
LINK C ASN A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N SER A 77 1555 1555 1.32
LINK C VAL A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N GLU A 113 1555 1555 1.35
LINK C VAL A 154 N MSE A 155 1555 1555 1.33
LINK C MSE A 155 N THR A 156 1555 1555 1.33
LINK C LYS A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N HIS A 178 1555 1555 1.34
LINK C GLY A 196 N MSE A 197 1555 1555 1.33
LINK C MSE A 197 N ILE A 198 1555 1555 1.33
LINK C VAL A 360 N MSE A 361 1555 1555 1.32
LINK C MSE A 361 N VAL A 362 1555 1555 1.34
LINK C SER A 364 N MSE A 365 1555 1555 1.33
LINK C MSE A 365 N PHE A 366 1555 1555 1.33
LINK C GLY A 389 N MSE A 390 1555 1555 1.33
LINK C MSE A 390 N GLY A 391 1555 1555 1.33
LINK C ALA A 395 N MSE A 396 1555 1555 1.32
LINK C MSE A 396 N SER A 397 1555 1555 1.33
LINK C GLN A 436 N MSE A 437 1555 1555 1.33
LINK C MSE A 437 N GLY A 438 1555 1555 1.32
LINK C CYS A 443 N MSE A 444 1555 1555 1.34
LINK C MSE A 444 N GLY A 445 1555 1555 1.33
LINK C GLY A 468 N MSE A 469 1555 1555 1.34
LINK C MSE A 469 N LYS A 470 1555 1555 1.34
LINK O CYS A 307 K K A 703 1555 1555 2.86
LINK O GLY A 304 K K A 703 1555 1555 2.88
LINK O GLY A 302 K K A 703 1555 1555 3.05
LINK K K A 703 O HOH A 828 1555 1555 3.25
CISPEP 1 ASN A 129 ASN A 130 0 -15.16
CISPEP 2 GLY A 278 ASN A 279 0 8.22
SITE 1 AC1 24 ALA A 49 MSE A 51 GLY A 304 SER A 305
SITE 2 AC1 24 ILE A 306 CYS A 307 ASP A 340 GLY A 341
SITE 3 AC1 24 GLY A 342 MSE A 361 GLY A 363 SER A 364
SITE 4 AC1 24 TYR A 387 GLY A 389 MSE A 390 GLY A 391
SITE 5 AC1 24 GLU A 417 GLY A 418 MOA A 702 HOH A 805
SITE 6 AC1 24 HOH A 812 HOH A 819 HOH A 820 HOH A 845
SITE 1 AC2 10 ASP A 250 SER A 251 SER A 252 ASN A 279
SITE 2 AC2 10 GLY A 300 ILE A 301 GLY A 302 CYS A 307
SITE 3 AC2 10 THR A 309 IMP A 701
SITE 1 AC3 6 GLY A 302 GLY A 304 CYS A 307 GLU A 471
SITE 2 AC3 6 SER A 472 HIS A 473
CRYST1 111.960 111.960 188.994 90.00 90.00 90.00 I 4 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 0.008932 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005291 0.00000
HETATM 1 N MSE A 3 15.736 -5.597 47.753 1.00 75.96 N
ANISOU 1 N MSE A 3 9058 9171 10632 63 129 1298 N
HETATM 2 CA MSE A 3 16.886 -6.195 47.008 1.00 74.73 C
ANISOU 2 CA MSE A 3 8800 8975 10617 155 158 1368 C
HETATM 3 C MSE A 3 17.251 -5.367 45.749 1.00 76.10 C
ANISOU 3 C MSE A 3 8954 9176 10786 170 167 1248 C
HETATM 4 O MSE A 3 18.338 -4.752 45.706 1.00 70.71 O
ANISOU 4 O MSE A 3 8207 8577 10082 168 103 1317 O
HETATM 5 CB MSE A 3 16.589 -7.657 46.671 1.00 92.59 C
ANISOU 5 CB MSE A 3 11048 11091 13041 234 269 1378 C
HETATM 6 CG MSE A 3 17.837 -8.518 46.449 1.00100.87 C
ANISOU 6 CG MSE A 3 11985 12092 14247 331 296 1518 C
HETATM 7 SE MSE A 3 19.238 -8.427 47.844 0.60108.50 SE
ANISOU 7 SE MSE A 3 12852 13179 15191 321 157 1798 SE
HETATM 8 CE MSE A 3 20.536 -7.158 47.136 1.00 84.68 C
ANISOU 8 CE MSE A 3 9749 10291 12132 316 83 1790 C
(ATOM LINES ARE NOT SHOWN.)
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