HEADER TRANSFERASE 27-JUL-12 4GBE
TITLE CRYSTAL STRUCTURE OF E. COLI DNA ADENINE METHYLTRANSFERASE IN COMPLEX
TITLE 2 WITH SAH
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 4GBE 1 REMARK SEQADV
REVDAT 1 26-FEB-14 4GBE 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 MIMICS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 39125
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2096
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) : 2.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2766
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : -0.03000
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): 0.348
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.258
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.172
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.089
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6285 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8519 ; 1.860 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 6.831 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 332 ;36.100 ;23.223
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1007 ;17.244 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;22.093 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 886 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4909 ; 0.009 ; 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): 3655 ; 1.150 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5874 ; 2.238 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2630 ; 3.189 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2645 ; 5.323 ; 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 4GBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073973.
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 : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41829
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 38.712
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.84800
REMARK 200 R SYM FOR SHELL (I) : 0.84800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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 (%): 66.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 1600 MM AMMONIUM SULFATE,
REMARK 280 16% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 31.85433
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 63.70867
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 63.70867
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 31.85433
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 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
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 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
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 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 HIS F 0
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 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: 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 PHE F 111 CD1 PHE F 111 CE1 0.137
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 ASP F 229 CB - CG - OD1 ANGL. DEV. = 5.9 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 TYR D 15 -51.85 -22.57
REMARK 500 PRO D 16 33.89 -98.21
REMARK 500 LEU D 17 -11.82 -142.19
REMARK 500 THR D 70 -70.14 -47.43
REMARK 500 ASN D 86 53.80 -99.57
REMARK 500 ASN D 120 19.45 53.55
REMARK 500 ARG D 137 57.49 32.14
REMARK 500 LYS D 140 92.50 -164.90
REMARK 500 HIS D 220 25.80 83.25
REMARK 500 PRO E 26 174.18 -59.22
REMARK 500 ASN E 86 54.62 -92.35
REMARK 500 TYR E 119 108.38 -32.66
REMARK 500 ASN E 120 13.18 57.56
REMARK 500 ARG E 137 64.38 39.02
REMARK 500 LYS E 139 -96.25 -29.84
REMARK 500 ASP E 181 75.05 -118.04
REMARK 500 HIS E 220 33.62 70.16
REMARK 500 ASP E 262 136.24 97.04
REMARK 500 LEU F 17 36.81 -150.70
REMARK 500 PHE F 81 41.54 -103.40
REMARK 500 ASN F 120 19.56 54.68
REMARK 500 ARG F 137 90.26 44.37
REMARK 500 LYS F 139 -78.79 -43.43
REMARK 500 SER F 200 -143.80 46.92
REMARK 500 GLN F 238 -5.69 -52.54
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 SAH D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH F 301
DBREF 4GBE D 1 278 UNP P0AEE8 DMA_ECOLI 1 278
DBREF 4GBE E 1 278 UNP P0AEE8 DMA_ECOLI 1 278
DBREF 4GBE F 1 278 UNP P0AEE8 DMA_ECOLI 1 278
SEQADV 4GBE HIS D -5 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS D -4 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS D -3 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS D -2 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS D -1 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS D 0 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E -5 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E -4 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E -3 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E -2 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E -1 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS E 0 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F -5 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F -4 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F -3 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F -2 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F -1 UNP P0AEE8 EXPRESSION TAG
SEQADV 4GBE HIS F 0 UNP P0AEE8 EXPRESSION TAG
SEQRES 1 D 284 HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE
SEQRES 2 D 284 LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP
SEQRES 3 D 284 ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU
SEQRES 4 D 284 PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP
SEQRES 5 D 284 PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU
SEQRES 6 D 284 ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU
SEQRES 7 D 284 TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR
SEQRES 8 D 284 ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE
SEQRES 9 D 284 ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE
SEQRES 10 D 284 LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG
SEQRES 11 D 284 TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG
SEQRES 12 D 284 TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS
SEQRES 13 D 284 PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU
SEQRES 14 D 284 SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER
SEQRES 15 D 284 VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA
SEQRES 16 D 284 THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR
SEQRES 17 D 284 LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY
SEQRES 18 D 284 LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS
SEQRES 19 D 284 ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS
SEQRES 20 D 284 LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN
SEQRES 21 D 284 GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU
SEQRES 22 D 284 TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS
SEQRES 1 E 284 HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE
SEQRES 2 E 284 LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP
SEQRES 3 E 284 ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU
SEQRES 4 E 284 PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP
SEQRES 5 E 284 PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU
SEQRES 6 E 284 ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU
SEQRES 7 E 284 TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR
SEQRES 8 E 284 ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE
SEQRES 9 E 284 ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE
SEQRES 10 E 284 LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG
SEQRES 11 E 284 TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG
SEQRES 12 E 284 TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS
SEQRES 13 E 284 PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU
SEQRES 14 E 284 SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER
SEQRES 15 E 284 VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA
SEQRES 16 E 284 THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR
SEQRES 17 E 284 LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY
SEQRES 18 E 284 LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS
SEQRES 19 E 284 ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS
SEQRES 20 E 284 LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN
SEQRES 21 E 284 GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU
SEQRES 22 E 284 TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS
SEQRES 1 F 284 HIS HIS HIS HIS HIS HIS MET LYS LYS ASN ARG ALA PHE
SEQRES 2 F 284 LEU LYS TRP ALA GLY GLY LYS TYR PRO LEU LEU ASP ASP
SEQRES 3 F 284 ILE LYS ARG HIS LEU PRO LYS GLY GLU CYS LEU VAL GLU
SEQRES 4 F 284 PRO PHE VAL GLY ALA GLY SER VAL PHE LEU ASN THR ASP
SEQRES 5 F 284 PHE SER ARG TYR ILE LEU ALA ASP ILE ASN SER ASP LEU
SEQRES 6 F 284 ILE SER LEU TYR ASN ILE VAL LYS MET ARG THR ASP GLU
SEQRES 7 F 284 TYR VAL GLN ALA ALA ARG GLU LEU PHE VAL PRO GLU THR
SEQRES 8 F 284 ASN CYS ALA GLU VAL TYR TYR GLN PHE ARG GLU GLU PHE
SEQRES 9 F 284 ASN LYS SER GLN ASP PRO PHE ARG ARG ALA VAL LEU PHE
SEQRES 10 F 284 LEU TYR LEU ASN ARG TYR GLY TYR ASN GLY LEU CYS ARG
SEQRES 11 F 284 TYR ASN LEU ARG GLY GLU PHE ASN VAL PRO PHE GLY ARG
SEQRES 12 F 284 TYR LYS LYS PRO TYR PHE PRO GLU ALA GLU LEU TYR HIS
SEQRES 13 F 284 PHE ALA GLU LYS ALA GLN ASN ALA PHE PHE TYR CYS GLU
SEQRES 14 F 284 SER TYR ALA ASP SER MET ALA ARG ALA ASP ASP ALA SER
SEQRES 15 F 284 VAL VAL TYR CYS ASP PRO PRO TYR ALA PRO LEU SER ALA
SEQRES 16 F 284 THR ALA ASN PHE THR ALA TYR HIS THR ASN SER PHE THR
SEQRES 17 F 284 LEU GLU GLN GLN ALA HIS LEU ALA GLU ILE ALA GLU GLY
SEQRES 18 F 284 LEU VAL GLU ARG HIS ILE PRO VAL LEU ILE SER ASN HIS
SEQRES 19 F 284 ASP THR MET LEU THR ARG GLU TRP TYR GLN ARG ALA LYS
SEQRES 20 F 284 LEU HIS VAL VAL LYS VAL ARG ARG SER ILE SER SER ASN
SEQRES 21 F 284 GLY GLY THR ARG LYS LYS VAL ASP GLU LEU LEU ALA LEU
SEQRES 22 F 284 TYR LYS PRO GLY VAL VAL SER PRO ALA LYS LYS
HET SAH D 301 26
HET SAH E 301 26
HET SAH F 301 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 4 SAH 3(C14 H20 N6 O5 S)
FORMUL 7 HOH *75(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 SER D 101 1 15
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 GLN D 156 1 13
HELIX 10 10 SER D 164 ALA D 170 1 7
HELIX 11 11 THR D 202 ARG D 219 1 18
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 LEU E 80 PHE E 81 5 2
HELIX 19 19 VAL E 82 ASN E 86 5 5
HELIX 20 20 CYS E 87 SER E 101 1 15
HELIX 21 21 ASP E 103 GLY E 118 1 16
HELIX 22 22 TYR E 119 LEU E 122 5 4
HELIX 23 23 PRO E 144 GLN E 156 1 13
HELIX 24 24 SER E 164 ALA E 170 1 7
HELIX 25 25 THR E 202 ARG E 219 1 18
HELIX 26 26 THR E 230 TYR E 237 1 8
HELIX 27 27 LYS F 14 PRO F 16 5 3
HELIX 28 28 LEU F 17 LEU F 25 1 9
HELIX 29 29 VAL F 41 THR F 45 5 5
HELIX 30 30 ASN F 56 ARG F 69 1 14
HELIX 31 31 ARG F 69 GLU F 79 1 11
HELIX 32 32 LEU F 80 PHE F 81 5 2
HELIX 33 33 VAL F 82 ASN F 86 5 5
HELIX 34 34 CYS F 87 SER F 101 1 15
HELIX 35 35 ASP F 103 GLY F 118 1 16
HELIX 36 36 TYR F 119 LEU F 122 5 4
HELIX 37 37 PRO F 144 GLN F 156 1 13
HELIX 38 38 SER F 164 ARG F 171 1 8
HELIX 39 39 THR F 202 ARG F 219 1 18
HELIX 40 40 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 PHE D 159
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 CYS D 180
SHEET 6 A 7 GLU D 263 TYR D 268 -1 O ALA D 266 N ILE D 225
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 GLU E 33 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 CYS E 180
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 CYS F 180
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 VAL F 245 O GLU F 263
SITE 1 AC1 14 TRP D 10 GLY D 12 LYS D 14 PRO D 34
SITE 2 AC1 14 PHE D 35 GLY D 37 ASP D 54 ILE D 55
SITE 3 AC1 14 TYR D 165 ASP D 181 PRO D 182 PRO D 183
SITE 4 AC1 14 TYR D 184 HOH D 406
SITE 1 AC2 13 TRP E 10 GLY E 13 LYS E 14 PRO E 34
SITE 2 AC2 13 PHE E 35 VAL E 36 ALA E 38 SER E 40
SITE 3 AC2 13 ASP E 54 ILE E 55 SER E 164 TYR E 165
SITE 4 AC2 13 ASP E 181
SITE 1 AC3 15 TRP F 10 LYS F 14 PRO F 34 PHE F 35
SITE 2 AC3 15 VAL F 36 GLY F 37 ALA F 38 GLY F 39
SITE 3 AC3 15 SER F 40 ASP F 54 ILE F 55 SER F 164
SITE 4 AC3 15 TYR F 165 ASP F 181 PRO F 183
CRYST1 161.176 161.176 95.563 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 0.006204 0.003582 0.000000 0.00000
SCALE2 0.000000 0.007164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010464 0.00000
(ATOM LINES ARE NOT SHOWN.)
END