HEADER TRANSFERASE 20-AUG-12 4GOM
TITLE CRYSTAL STRUCTURE OF E. COLI DNA ADENINE METHYLTRANSFERASE IN COMPLEX
TITLE 2 WITH AZA-SAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA ADENINE METHYLASE;
COMPND 3 CHAIN: D, E, F;
COMPND 4 SYNONYM: DNA ADENINE METHYLTRANSFERASE, DEOXYADENOSYL-
COMPND 5 METHYLTRANSFERASE, M.ECODAM;
COMPND 6 EC: 2.1.1.72;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: B3387, DAM, JW3350;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS TRANSFERASE, METHYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.HARMER,P.L.ROACH
REVDAT 2 28-FEB-24 4GOM 1 REMARK
REVDAT 1 26-FEB-14 4GOM 0
JRNL AUTH J.E.HARMER,J.C.MCKELVIE,G.HOBLEY,P.L.ROACH
JRNL TITL STRUCTURAL BASIS OF SELECTIVE N-6 ADENINE METHYLTRANSFERASE
JRNL TITL 2 INHIBITION BY TRANSITION STATE MIMIC
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 49725
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2653
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3579
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : -0.04000
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): 0.253
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.754
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6101 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8309 ; 1.853 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 7.376 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 314 ;35.818 ;23.121
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 874 ;15.279 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.796 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 880 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4829 ; 0.011 ; 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): 3670 ; 1.180 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5842 ; 2.186 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2431 ; 3.197 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2467 ; 4.913 ; 4.500
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4GOM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.924530
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49725
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.496
REMARK 200 RESOLUTION RANGE LOW (A) : 38.685
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : 0.74000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 66.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 1600 MM AMMONIUM SULFATE,
REMARK 280 14-18% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 31.76433
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 63.52867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 63.52867
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 31.76433
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 D 1
REMARK 465 LYS D 2
REMARK 465 SER D 188
REMARK 465 ALA D 189
REMARK 465 THR D 190
REMARK 465 ALA D 191
REMARK 465 ASN D 192
REMARK 465 PHE D 193
REMARK 465 THR D 194
REMARK 465 ALA D 195
REMARK 465 TYR D 196
REMARK 465 HIS D 197
REMARK 465 THR D 198
REMARK 465 VAL D 247
REMARK 465 ARG D 248
REMARK 465 ARG D 249
REMARK 465 SER D 250
REMARK 465 ILE D 251
REMARK 465 SER D 252
REMARK 465 SER D 253
REMARK 465 ASN D 254
REMARK 465 GLY D 255
REMARK 465 GLY D 256
REMARK 465 THR D 257
REMARK 465 ARG D 258
REMARK 465 LYS D 259
REMARK 465 LYS D 260
REMARK 465 GLY D 271
REMARK 465 VAL D 272
REMARK 465 VAL D 273
REMARK 465 SER D 274
REMARK 465 PRO D 275
REMARK 465 ALA D 276
REMARK 465 LYS D 277
REMARK 465 LYS D 278
REMARK 465 MET E 1
REMARK 465 LYS E 2
REMARK 465 SER E 188
REMARK 465 ALA E 189
REMARK 465 THR E 190
REMARK 465 ALA E 191
REMARK 465 ASN E 192
REMARK 465 PHE E 193
REMARK 465 THR E 194
REMARK 465 ALA E 195
REMARK 465 TYR E 196
REMARK 465 HIS E 197
REMARK 465 THR E 198
REMARK 465 ASN E 199
REMARK 465 ARG E 248
REMARK 465 ARG E 249
REMARK 465 SER E 250
REMARK 465 ILE E 251
REMARK 465 SER E 252
REMARK 465 SER E 253
REMARK 465 ASN E 254
REMARK 465 GLY E 255
REMARK 465 GLY E 256
REMARK 465 THR E 257
REMARK 465 ARG E 258
REMARK 465 LYS E 259
REMARK 465 GLY E 271
REMARK 465 VAL E 272
REMARK 465 VAL E 273
REMARK 465 SER E 274
REMARK 465 PRO E 275
REMARK 465 ALA E 276
REMARK 465 LYS E 277
REMARK 465 LYS E 278
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 SER F 188
REMARK 465 ALA F 189
REMARK 465 THR F 190
REMARK 465 ALA F 191
REMARK 465 ASN F 192
REMARK 465 PHE F 193
REMARK 465 THR F 194
REMARK 465 ALA F 195
REMARK 465 TYR F 196
REMARK 465 HIS F 197
REMARK 465 THR F 198
REMARK 465 ARG F 248
REMARK 465 ARG F 249
REMARK 465 SER F 250
REMARK 465 ILE F 251
REMARK 465 SER F 252
REMARK 465 SER F 253
REMARK 465 ASN F 254
REMARK 465 GLY F 255
REMARK 465 GLY F 256
REMARK 465 THR F 257
REMARK 465 ARG F 258
REMARK 465 LYS F 259
REMARK 465 LYS F 260
REMARK 465 GLY F 271
REMARK 465 VAL F 272
REMARK 465 VAL F 273
REMARK 465 SER F 274
REMARK 465 PRO F 275
REMARK 465 ALA F 276
REMARK 465 LYS F 277
REMARK 465 LYS F 278
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 LYS D 3 CG CD CE NZ
REMARK 470 ARG D 5 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 14 CG CD CE NZ
REMARK 470 TYR D 15 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 27 CG CD CE NZ
REMARK 470 ASP D 46 CG OD1 OD2
REMARK 470 GLU D 153 CG CD OE1 OE2
REMARK 470 ASN D 199 CG OD1 ND2
REMARK 470 SER D 200 OG
REMARK 470 LYS D 241 CG CD CE NZ
REMARK 470 LYS D 246 CG CD CE NZ
REMARK 470 LYS D 269 CG CD CE NZ
REMARK 470 LYS E 3 CG CD CE NZ
REMARK 470 LYS E 14 CG CD CE NZ
REMARK 470 ARG E 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 27 CG CD CE NZ
REMARK 470 ASP E 46 CG OD1 OD2
REMARK 470 GLN E 75 CG CD OE1 NE2
REMARK 470 GLU E 89 CG CD OE1 OE2
REMARK 470 LYS E 100 CG CD CE NZ
REMARK 470 LYS E 139 CG CD CE NZ
REMARK 470 LYS E 140 CG CD CE NZ
REMARK 470 GLU E 153 CG CD OE1 OE2
REMARK 470 LEU E 187 CG CD1 CD2
REMARK 470 SER E 200 OG
REMARK 470 GLU E 218 CG CD OE1 OE2
REMARK 470 LYS E 241 CG CD CE NZ
REMARK 470 VAL E 245 CG1 CG2
REMARK 470 LYS E 246 CG CD CE NZ
REMARK 470 VAL E 247 CG1 CG2
REMARK 470 LYS E 260 CG CD CE NZ
REMARK 470 VAL E 261 CG1 CG2
REMARK 470 LYS E 269 CG CD CE NZ
REMARK 470 LYS F 3 CG CD CE NZ
REMARK 470 ARG F 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 27 CG CD CE NZ
REMARK 470 ASP F 46 CG OD1 OD2
REMARK 470 GLN F 75 CG CD OE1 NE2
REMARK 470 GLU F 89 CG CD OE1 OE2
REMARK 470 LYS F 140 CG CD CE NZ
REMARK 470 LEU F 187 CG CD1 CD2
REMARK 470 ASN F 199 CG OD1 ND2
REMARK 470 SER F 200 OG
REMARK 470 GLU F 218 CG CD OE1 OE2
REMARK 470 LYS F 241 CG CD CE NZ
REMARK 470 LYS F 246 CG CD CE NZ
REMARK 470 VAL F 261 CG1 CG2
REMARK 470 LYS F 269 CG CD 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 LYS F 14 CD CE NZ
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 GLY F 12 N LYS F 14 1.80
REMARK 500 C GLY F 12 N LYS F 14 2.17
REMARK 500 OG SER F 164 O HOH F 411 2.19
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 PRO E 83 C - N - CA ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP E 103 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLY F 13 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 ASP F 167 CB - CG - OD1 ANGL. DEV. = 5.7 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 D 11 113.80 -32.83
REMARK 500 LYS D 14 7.57 -57.49
REMARK 500 PRO D 16 51.02 -64.56
REMARK 500 LEU D 17 -40.14 -176.72
REMARK 500 PRO D 26 -173.91 -65.59
REMARK 500 ASN D 86 60.56 -103.51
REMARK 500 ASN D 120 29.48 40.76
REMARK 500 LYS D 140 87.37 -162.59
REMARK 500 SER D 200 163.25 -46.04
REMARK 500 LYS E 14 28.78 -70.01
REMARK 500 PRO E 26 -176.22 -67.87
REMARK 500 VAL E 82 -168.39 -116.13
REMARK 500 ASN E 120 32.89 38.57
REMARK 500 ALA E 185 153.10 -49.58
REMARK 500 ALA F 11 125.72 -39.42
REMARK 500 LYS F 14 78.40 -6.57
REMARK 500 PHE F 81 40.22 -100.41
REMARK 500 GLU F 84 -7.68 -58.77
REMARK 500 ASN F 126 -172.33 -69.43
REMARK 500 ASN F 132 25.44 -140.32
REMARK 500 PRO F 144 53.44 -69.89
REMARK 500 ASP F 174 -48.09 -28.85
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 D 13 LYS D 14 -138.38
REMARK 500 GLY E 13 LYS E 14 -147.38
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 0Y0 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0Y0 E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0Y0 F 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GBE RELATED DB: PDB
REMARK 900 RELATED ID: 4GOL RELATED DB: PDB
REMARK 900 RELATED ID: 4GON RELATED DB: PDB
REMARK 900 RELATED ID: 4GOO RELATED DB: PDB
DBREF 4GOM D 1 278 UNP P0AEE8 DMA_ECOLI 1 278
DBREF 4GOM E 1 278 UNP P0AEE8 DMA_ECOLI 1 278
DBREF 4GOM F 1 278 UNP P0AEE8 DMA_ECOLI 1 278
SEQRES 1 D 278 MET LYS LYS ASN ARG ALA PHE LEU LYS TRP ALA GLY GLY
SEQRES 2 D 278 LYS TYR PRO LEU LEU ASP ASP ILE LYS ARG HIS LEU PRO
SEQRES 3 D 278 LYS GLY GLU CYS LEU VAL GLU PRO PHE VAL GLY ALA GLY
SEQRES 4 D 278 SER VAL PHE LEU ASN THR ASP PHE SER ARG TYR ILE LEU
SEQRES 5 D 278 ALA ASP ILE ASN SER ASP LEU ILE SER LEU TYR ASN ILE
SEQRES 6 D 278 VAL LYS MET ARG THR ASP GLU TYR VAL GLN ALA ALA ARG
SEQRES 7 D 278 GLU LEU PHE VAL PRO GLU THR ASN CYS ALA GLU VAL TYR
SEQRES 8 D 278 TYR GLN PHE ARG GLU GLU PHE ASN LYS SER GLN ASP PRO
SEQRES 9 D 278 PHE ARG ARG ALA VAL LEU PHE LEU TYR LEU ASN ARG TYR
SEQRES 10 D 278 GLY TYR ASN GLY LEU CYS ARG TYR ASN LEU ARG GLY GLU
SEQRES 11 D 278 PHE ASN VAL PRO PHE GLY ARG TYR LYS LYS PRO TYR PHE
SEQRES 12 D 278 PRO GLU ALA GLU LEU TYR HIS PHE ALA GLU LYS ALA GLN
SEQRES 13 D 278 ASN ALA PHE PHE TYR CYS GLU SER TYR ALA ASP SER MET
SEQRES 14 D 278 ALA ARG ALA ASP ASP ALA SER VAL VAL TYR CYS ASP PRO
SEQRES 15 D 278 PRO TYR ALA PRO LEU SER ALA THR ALA ASN PHE THR ALA
SEQRES 16 D 278 TYR HIS THR ASN SER PHE THR LEU GLU GLN GLN ALA HIS
SEQRES 17 D 278 LEU ALA GLU ILE ALA GLU GLY LEU VAL GLU ARG HIS ILE
SEQRES 18 D 278 PRO VAL LEU ILE SER ASN HIS ASP THR MET LEU THR ARG
SEQRES 19 D 278 GLU TRP TYR GLN ARG ALA LYS LEU HIS VAL VAL LYS VAL
SEQRES 20 D 278 ARG ARG SER ILE SER SER ASN GLY GLY THR ARG LYS LYS
SEQRES 21 D 278 VAL ASP GLU LEU LEU ALA LEU TYR LYS PRO GLY VAL VAL
SEQRES 22 D 278 SER PRO ALA LYS LYS
SEQRES 1 E 278 MET LYS LYS ASN ARG ALA PHE LEU LYS TRP ALA GLY GLY
SEQRES 2 E 278 LYS TYR PRO LEU LEU ASP ASP ILE LYS ARG HIS LEU PRO
SEQRES 3 E 278 LYS GLY GLU CYS LEU VAL GLU PRO PHE VAL GLY ALA GLY
SEQRES 4 E 278 SER VAL PHE LEU ASN THR ASP PHE SER ARG TYR ILE LEU
SEQRES 5 E 278 ALA ASP ILE ASN SER ASP LEU ILE SER LEU TYR ASN ILE
SEQRES 6 E 278 VAL LYS MET ARG THR ASP GLU TYR VAL GLN ALA ALA ARG
SEQRES 7 E 278 GLU LEU PHE VAL PRO GLU THR ASN CYS ALA GLU VAL TYR
SEQRES 8 E 278 TYR GLN PHE ARG GLU GLU PHE ASN LYS SER GLN ASP PRO
SEQRES 9 E 278 PHE ARG ARG ALA VAL LEU PHE LEU TYR LEU ASN ARG TYR
SEQRES 10 E 278 GLY TYR ASN GLY LEU CYS ARG TYR ASN LEU ARG GLY GLU
SEQRES 11 E 278 PHE ASN VAL PRO PHE GLY ARG TYR LYS LYS PRO TYR PHE
SEQRES 12 E 278 PRO GLU ALA GLU LEU TYR HIS PHE ALA GLU LYS ALA GLN
SEQRES 13 E 278 ASN ALA PHE PHE TYR CYS GLU SER TYR ALA ASP SER MET
SEQRES 14 E 278 ALA ARG ALA ASP ASP ALA SER VAL VAL TYR CYS ASP PRO
SEQRES 15 E 278 PRO TYR ALA PRO LEU SER ALA THR ALA ASN PHE THR ALA
SEQRES 16 E 278 TYR HIS THR ASN SER PHE THR LEU GLU GLN GLN ALA HIS
SEQRES 17 E 278 LEU ALA GLU ILE ALA GLU GLY LEU VAL GLU ARG HIS ILE
SEQRES 18 E 278 PRO VAL LEU ILE SER ASN HIS ASP THR MET LEU THR ARG
SEQRES 19 E 278 GLU TRP TYR GLN ARG ALA LYS LEU HIS VAL VAL LYS VAL
SEQRES 20 E 278 ARG ARG SER ILE SER SER ASN GLY GLY THR ARG LYS LYS
SEQRES 21 E 278 VAL ASP GLU LEU LEU ALA LEU TYR LYS PRO GLY VAL VAL
SEQRES 22 E 278 SER PRO ALA LYS LYS
SEQRES 1 F 278 MET LYS LYS ASN ARG ALA PHE LEU LYS TRP ALA GLY GLY
SEQRES 2 F 278 LYS TYR PRO LEU LEU ASP ASP ILE LYS ARG HIS LEU PRO
SEQRES 3 F 278 LYS GLY GLU CYS LEU VAL GLU PRO PHE VAL GLY ALA GLY
SEQRES 4 F 278 SER VAL PHE LEU ASN THR ASP PHE SER ARG TYR ILE LEU
SEQRES 5 F 278 ALA ASP ILE ASN SER ASP LEU ILE SER LEU TYR ASN ILE
SEQRES 6 F 278 VAL LYS MET ARG THR ASP GLU TYR VAL GLN ALA ALA ARG
SEQRES 7 F 278 GLU LEU PHE VAL PRO GLU THR ASN CYS ALA GLU VAL TYR
SEQRES 8 F 278 TYR GLN PHE ARG GLU GLU PHE ASN LYS SER GLN ASP PRO
SEQRES 9 F 278 PHE ARG ARG ALA VAL LEU PHE LEU TYR LEU ASN ARG TYR
SEQRES 10 F 278 GLY TYR ASN GLY LEU CYS ARG TYR ASN LEU ARG GLY GLU
SEQRES 11 F 278 PHE ASN VAL PRO PHE GLY ARG TYR LYS LYS PRO TYR PHE
SEQRES 12 F 278 PRO GLU ALA GLU LEU TYR HIS PHE ALA GLU LYS ALA GLN
SEQRES 13 F 278 ASN ALA PHE PHE TYR CYS GLU SER TYR ALA ASP SER MET
SEQRES 14 F 278 ALA ARG ALA ASP ASP ALA SER VAL VAL TYR CYS ASP PRO
SEQRES 15 F 278 PRO TYR ALA PRO LEU SER ALA THR ALA ASN PHE THR ALA
SEQRES 16 F 278 TYR HIS THR ASN SER PHE THR LEU GLU GLN GLN ALA HIS
SEQRES 17 F 278 LEU ALA GLU ILE ALA GLU GLY LEU VAL GLU ARG HIS ILE
SEQRES 18 F 278 PRO VAL LEU ILE SER ASN HIS ASP THR MET LEU THR ARG
SEQRES 19 F 278 GLU TRP TYR GLN ARG ALA LYS LEU HIS VAL VAL LYS VAL
SEQRES 20 F 278 ARG ARG SER ILE SER SER ASN GLY GLY THR ARG LYS LYS
SEQRES 21 F 278 VAL ASP GLU LEU LEU ALA LEU TYR LYS PRO GLY VAL VAL
SEQRES 22 F 278 SER PRO ALA LYS LYS
HET 0Y0 D 301 26
HET 0Y0 E 301 26
HET 0Y0 F 301 26
HETNAM 0Y0 5'-{[(3S)-3-AMINO-3-CARBOXYPROPYL]AMINO}-5'-
HETNAM 2 0Y0 DEOXYADENOSINE
FORMUL 4 0Y0 3(C14 H21 N7 O5)
FORMUL 7 HOH *131(H2 O)
HELIX 1 1 LEU D 17 LEU D 25 1 9
HELIX 2 2 GLY D 39 ASN D 44 1 6
HELIX 3 3 ASN D 56 ARG D 69 1 14
HELIX 4 4 ARG D 69 GLU D 79 1 11
HELIX 5 5 LEU D 80 ASN D 86 5 7
HELIX 6 6 CYS D 87 LYS D 100 1 14
HELIX 7 7 ASP D 103 GLY D 118 1 16
HELIX 8 8 TYR D 119 LEU D 122 5 4
HELIX 9 9 PRO D 144 ALA D 155 1 12
HELIX 10 10 SER D 164 ALA D 170 1 7
HELIX 11 11 THR D 202 GLU D 218 1 17
HELIX 12 12 THR D 230 TYR D 237 1 8
HELIX 13 13 LYS E 14 PRO E 16 5 3
HELIX 14 14 LEU E 17 LEU E 25 1 9
HELIX 15 15 GLY E 39 ASN E 44 1 6
HELIX 16 16 ASN E 56 ARG E 69 1 14
HELIX 17 17 ARG E 69 GLU E 79 1 11
HELIX 18 18 CYS E 87 SER E 101 1 15
HELIX 19 19 ASP E 103 GLY E 118 1 16
HELIX 20 20 TYR E 119 LEU E 122 5 4
HELIX 21 21 PRO E 144 GLN E 156 1 13
HELIX 22 22 SER E 164 ALA E 170 1 7
HELIX 23 23 THR E 202 ARG E 219 1 18
HELIX 24 24 THR E 230 TYR E 237 1 8
HELIX 25 25 LEU F 17 LEU F 25 1 9
HELIX 26 26 GLY F 39 ASN F 44 1 6
HELIX 27 27 ASN F 56 ARG F 69 1 14
HELIX 28 28 ARG F 69 GLU F 79 1 11
HELIX 29 29 LEU F 80 PHE F 81 5 2
HELIX 30 30 VAL F 82 ASN F 86 5 5
HELIX 31 31 CYS F 87 SER F 101 1 15
HELIX 32 32 ASP F 103 GLY F 118 1 16
HELIX 33 33 TYR F 119 LEU F 122 5 4
HELIX 34 34 PRO F 144 GLN F 156 1 13
HELIX 35 35 SER F 164 ARG F 171 1 8
HELIX 36 36 THR F 202 ARG F 219 1 18
HELIX 37 37 THR F 230 TYR F 237 1 8
SHEET 1 A 7 ALA D 158 CYS D 162 0
SHEET 2 A 7 ARG D 49 ASP D 54 1 N LEU D 52 O TYR D 161
SHEET 3 A 7 CYS D 30 GLU D 33 1 N LEU D 31 O ILE D 51
SHEET 4 A 7 SER D 176 CYS D 180 1 O VAL D 177 N VAL D 32
SHEET 5 A 7 VAL D 223 HIS D 228 1 O LEU D 224 N VAL D 178
SHEET 6 A 7 GLU D 263 TYR D 268 -1 O LEU D 264 N ASN D 227
SHEET 7 A 7 LYS D 241 VAL D 245 -1 N VAL D 245 O GLU D 263
SHEET 1 B 7 ALA E 158 CYS E 162 0
SHEET 2 B 7 ARG E 49 ASP E 54 1 N LEU E 52 O PHE E 159
SHEET 3 B 7 CYS E 30 GLU E 33 1 N LEU E 31 O ILE E 51
SHEET 4 B 7 SER E 176 CYS E 180 1 O VAL E 177 N VAL E 32
SHEET 5 B 7 VAL E 223 HIS E 228 1 O LEU E 224 N VAL E 178
SHEET 6 B 7 GLU E 263 TYR E 268 -1 O LEU E 264 N ASN E 227
SHEET 7 B 7 LYS E 241 VAL E 245 -1 N VAL E 245 O GLU E 263
SHEET 1 C 7 ALA F 158 TYR F 161 0
SHEET 2 C 7 ARG F 49 ALA F 53 1 N LEU F 52 O PHE F 159
SHEET 3 C 7 CYS F 30 GLU F 33 1 N GLU F 33 O ILE F 51
SHEET 4 C 7 SER F 176 CYS F 180 1 O VAL F 177 N VAL F 32
SHEET 5 C 7 VAL F 223 HIS F 228 1 O LEU F 224 N VAL F 178
SHEET 6 C 7 GLU F 263 TYR F 268 -1 O LEU F 264 N ASN F 227
SHEET 7 C 7 LYS F 241 VAL F 245 -1 N LYS F 241 O LEU F 267
SITE 1 AC1 10 TRP D 10 PHE D 35 ASP D 54 ILE D 55
SITE 2 AC1 10 SER D 164 TYR D 165 ASP D 181 PRO D 182
SITE 3 AC1 10 PRO D 183 TYR D 184
SITE 1 AC2 12 TRP E 10 ALA E 11 PRO E 34 PHE E 35
SITE 2 AC2 12 ASP E 54 ILE E 55 SER E 164 TYR E 165
SITE 3 AC2 12 ASP E 181 PRO E 182 PRO E 183 TYR E 184
SITE 1 AC3 12 TRP F 10 ALA F 11 PRO F 34 PHE F 35
SITE 2 AC3 12 GLY F 37 ASP F 54 ILE F 55 TYR F 165
SITE 3 AC3 12 ASP F 181 PRO F 182 PRO F 183 TYR F 184
CRYST1 161.038 161.038 95.293 90.00 90.00 120.00 P 31 2 1 18
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 0.006210 0.003585 0.000000 0.00000
SCALE2 0.000000 0.007170 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010494 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
