HEADER TRANSFERASE 22-JAN-14 4CND
TITLE CRYSTAL STRUCTURE OF E.COLI TRMJ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA (CYTIDINE/URIDINE-2'-O-)-METHYLTRANSFERASE TRMJ;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRNA (CYTIDINE(32)/URIDINE(32)-2'-O)-METHYLTRANSFERASE, TRNA
COMPND 5 CM32/UM32 METHYLTRANSFERASE, TRMJ;
COMPND 6 EC: 2.1.1.200;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET28B
KEYWDS TRANSFERASE, SPOUT
EXPDTA X-RAY DIFFRACTION
AUTHOR B.VAN LAER,J.SOMME,M.ROOVERS,J.STEYAERT,L.DROOGMANS,W.VERSEES
REVDAT 3 20-DEC-23 4CND 1 REMARK
REVDAT 2 30-JUL-14 4CND 1 JRNL
REVDAT 1 02-JUL-14 4CND 0
JRNL AUTH J.SOMME,B.VAN LAER,M.ROOVERS,J.STEYAERT,W.VERSEES,
JRNL AUTH 2 L.DROOGMANS
JRNL TITL CHARACTERIZATION OF TWO HOMOLOGOUS 2'-O-METHYLTRANSFERASES
JRNL TITL 2 SHOWING DIFFERENT SPECIFICITIES FOR THEIR TRNA SUBSTRATES.
JRNL REF RNA V. 20 1257 2014
JRNL REFN ISSN 1355-8382
JRNL PMID 24951554
JRNL DOI 10.1261/RNA.044503.114
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 46569
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2451
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2789
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.39000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.76000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2539 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2504 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3459 ; 1.712 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5731 ; 3.647 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 6.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;36.083 ;24.082
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 416 ;13.562 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.536 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 419 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2865 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 541 ; 0.019 ; 0.020
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): 1326 ; 2.082 ; 1.788
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1325 ; 2.079 ; 1.786
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1651 ; 2.818 ; 2.668
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1213 ; 3.038 ; 2.123
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4CND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059518.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49018
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.88000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 3ILK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M NA/KPO4, 0.1M MES PH6.5, 19%
REMARK 280 PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 36.51500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.5 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 -16
REMARK 465 ARG A -15
REMARK 465 GLY A -14
REMARK 465 SER A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 THR A -6
REMARK 465 GLU A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 GLU A 168
REMARK 465 GLN A 169
REMARK 465 VAL A 170
REMARK 465 GLU A 171
REMARK 465 HIS A 172
REMARK 465 GLU A 173
REMARK 465 GLU A 174
REMARK 465 THR A 175
REMARK 465 PRO A 176
REMARK 465 TYR A 177
REMARK 465 PRO A 178
REMARK 465 LEU A 179
REMARK 465 VAL A 180
REMARK 465 ASP A 181
REMARK 465 ASP A 182
REMARK 465 LEU A 183
REMARK 465 GLU A 184
REMARK 465 ARG A 185
REMARK 465 PHE A 186
REMARK 465 TYR A 187
REMARK 465 GLY A 188
REMARK 465 HIS A 189
REMARK 465 LEU A 190
REMARK 465 GLU A 191
REMARK 465 GLN A 192
REMARK 465 THR A 193
REMARK 465 LEU A 194
REMARK 465 LEU A 195
REMARK 465 ALA A 196
REMARK 465 THR A 197
REMARK 465 GLY A 198
REMARK 465 PHE A 199
REMARK 465 ILE A 200
REMARK 465 ARG A 201
REMARK 465 GLU A 202
REMARK 465 ASN A 203
REMARK 465 HIS A 204
REMARK 465 PRO A 205
REMARK 465 GLY A 206
REMARK 465 GLN A 207
REMARK 465 VAL A 208
REMARK 465 MET A 209
REMARK 465 ASN A 210
REMARK 465 LYS A 211
REMARK 465 LEU A 212
REMARK 465 ARG A 213
REMARK 465 ARG A 214
REMARK 465 LEU A 215
REMARK 465 PHE A 216
REMARK 465 THR A 217
REMARK 465 ARG A 218
REMARK 465 ALA A 219
REMARK 465 ARG A 220
REMARK 465 PRO A 221
REMARK 465 GLU A 222
REMARK 465 SER A 223
REMARK 465 GLN A 224
REMARK 465 GLU A 225
REMARK 465 LEU A 226
REMARK 465 ASN A 227
REMARK 465 ILE A 228
REMARK 465 LEU A 229
REMARK 465 ARG A 230
REMARK 465 GLY A 231
REMARK 465 ILE A 232
REMARK 465 LEU A 233
REMARK 465 ALA A 234
REMARK 465 SER A 235
REMARK 465 ILE A 236
REMARK 465 GLU A 237
REMARK 465 GLN A 238
REMARK 465 GLN A 239
REMARK 465 ASN A 240
REMARK 465 LYS A 241
REMARK 465 GLY A 242
REMARK 465 ASN A 243
REMARK 465 LYS A 244
REMARK 465 ALA A 245
REMARK 465 GLU A 246
REMARK 465 GLY A 247
REMARK 465 LEU A 248
REMARK 465 CYS A 249
REMARK 465 GLY A 250
REMARK 465 ARG A 251
REMARK 465 MET B -16
REMARK 465 ARG B -15
REMARK 465 GLY B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 THR B -6
REMARK 465 SER B 44
REMARK 465 GLN B 45
REMARK 465 ALA B 46
REMARK 465 ILE B 47
REMARK 465 ALA B 48
REMARK 465 LEU B 49
REMARK 465 ALA B 50
REMARK 465 GLU B 165
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 GLU B 168
REMARK 465 GLN B 169
REMARK 465 VAL B 170
REMARK 465 GLU B 171
REMARK 465 HIS B 172
REMARK 465 GLU B 173
REMARK 465 GLU B 174
REMARK 465 THR B 175
REMARK 465 PRO B 176
REMARK 465 TYR B 177
REMARK 465 PRO B 178
REMARK 465 LEU B 179
REMARK 465 VAL B 180
REMARK 465 ASP B 181
REMARK 465 ASP B 182
REMARK 465 LEU B 183
REMARK 465 GLU B 184
REMARK 465 ARG B 185
REMARK 465 PHE B 186
REMARK 465 TYR B 187
REMARK 465 GLY B 188
REMARK 465 HIS B 189
REMARK 465 LEU B 190
REMARK 465 GLU B 191
REMARK 465 GLN B 192
REMARK 465 THR B 193
REMARK 465 LEU B 194
REMARK 465 LEU B 195
REMARK 465 ALA B 196
REMARK 465 THR B 197
REMARK 465 GLY B 198
REMARK 465 PHE B 199
REMARK 465 ILE B 200
REMARK 465 ARG B 201
REMARK 465 GLU B 202
REMARK 465 ASN B 203
REMARK 465 HIS B 204
REMARK 465 PRO B 205
REMARK 465 GLY B 206
REMARK 465 GLN B 207
REMARK 465 VAL B 208
REMARK 465 MET B 209
REMARK 465 ASN B 210
REMARK 465 LYS B 211
REMARK 465 LEU B 212
REMARK 465 ARG B 213
REMARK 465 ARG B 214
REMARK 465 LEU B 215
REMARK 465 PHE B 216
REMARK 465 THR B 217
REMARK 465 ARG B 218
REMARK 465 ALA B 219
REMARK 465 ARG B 220
REMARK 465 PRO B 221
REMARK 465 GLU B 222
REMARK 465 SER B 223
REMARK 465 GLN B 224
REMARK 465 GLU B 225
REMARK 465 LEU B 226
REMARK 465 ASN B 227
REMARK 465 ILE B 228
REMARK 465 LEU B 229
REMARK 465 ARG B 230
REMARK 465 GLY B 231
REMARK 465 ILE B 232
REMARK 465 LEU B 233
REMARK 465 ALA B 234
REMARK 465 SER B 235
REMARK 465 ILE B 236
REMARK 465 GLU B 237
REMARK 465 GLN B 238
REMARK 465 GLN B 239
REMARK 465 ASN B 240
REMARK 465 LYS B 241
REMARK 465 GLY B 242
REMARK 465 ASN B 243
REMARK 465 LYS B 244
REMARK 465 ALA B 245
REMARK 465 GLU B 246
REMARK 465 GLY B 247
REMARK 465 LEU B 248
REMARK 465 CYS B 249
REMARK 465 GLY B 250
REMARK 465 ARG B 251
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 43 -163.99 -124.23
REMARK 500 ALA A 51 -121.57 52.77
REMARK 500 SER A 80 144.51 -170.40
REMARK 500 ARG A 117 -55.64 67.71
REMARK 500 TYR A 140 78.97 -160.71
REMARK 500 LYS B 41 151.95 -46.98
REMARK 500 ARG B 117 -49.15 76.46
REMARK 500 TYR B 140 87.54 -164.29
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 TYR A 140 SER A 141 -149.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2001 DISTANCE = 6.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1165
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CNE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E.COLI TRMJ IN COMPLEX WITH S- ADENOSYL-L-
REMARK 900 HOMOCYSTEINE
DBREF 4CND A 1 246 UNP P0AE01 TRMJ_ECOLI 1 246
DBREF 4CND B 1 246 UNP P0AE01 TRMJ_ECOLI 1 246
SEQADV 4CND MET A -16 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG A -15 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND GLY A -14 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND SER A -13 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -12 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -11 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -10 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -9 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -8 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS A -7 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND THR A -6 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ASP A -5 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND PRO A -4 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ALA A -3 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND LEU A -2 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG A -1 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ALA A 1 UNP P0AE01 MET 1 ENGINEERED MUTATION
SEQADV 4CND GLY A 247 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND LEU A 248 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND CYS A 249 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND GLY A 250 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG A 251 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND MET B -16 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG B -15 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND GLY B -14 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND SER B -13 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -12 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -11 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -10 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -9 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -8 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND HIS B -7 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND THR B -6 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ASP B -5 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND PRO B -4 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ALA B -3 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND LEU B -2 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG B -1 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ALA B 1 UNP P0AE01 MET 1 ENGINEERED MUTATION
SEQADV 4CND GLY B 247 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND LEU B 248 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND CYS B 249 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND GLY B 250 UNP P0AE01 EXPRESSION TAG
SEQADV 4CND ARG B 251 UNP P0AE01 EXPRESSION TAG
SEQRES 1 A 267 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 A 267 ALA LEU ARG ALA LEU GLN ASN ILE ARG ILE VAL LEU VAL
SEQRES 3 A 267 GLU THR SER HIS THR GLY ASN MET GLY SER VAL ALA ARG
SEQRES 4 A 267 ALA MET LYS THR MET GLY LEU THR ASN LEU TRP LEU VAL
SEQRES 5 A 267 ASN PRO LEU VAL LYS PRO ASP SER GLN ALA ILE ALA LEU
SEQRES 6 A 267 ALA ALA GLY ALA SER ASP VAL ILE GLY ASN ALA HIS ILE
SEQRES 7 A 267 VAL ASP THR LEU ASP GLU ALA LEU ALA GLY CYS SER LEU
SEQRES 8 A 267 VAL VAL GLY THR SER ALA ARG SER ARG THR LEU PRO TRP
SEQRES 9 A 267 PRO MET LEU ASP PRO ARG GLU CYS GLY LEU LYS SER VAL
SEQRES 10 A 267 ALA GLU ALA ALA ASN THR PRO VAL ALA LEU VAL PHE GLY
SEQRES 11 A 267 ARG GLU ARG VAL GLY LEU THR ASN GLU GLU LEU GLN LYS
SEQRES 12 A 267 CYS HIS TYR HIS VAL ALA ILE ALA ALA ASN PRO GLU TYR
SEQRES 13 A 267 SER SER LEU ASN LEU ALA MET ALA VAL GLN VAL ILE ALA
SEQRES 14 A 267 TYR GLU VAL ARG MET ALA TRP LEU ALA THR GLN GLU ASN
SEQRES 15 A 267 GLY GLU GLN VAL GLU HIS GLU GLU THR PRO TYR PRO LEU
SEQRES 16 A 267 VAL ASP ASP LEU GLU ARG PHE TYR GLY HIS LEU GLU GLN
SEQRES 17 A 267 THR LEU LEU ALA THR GLY PHE ILE ARG GLU ASN HIS PRO
SEQRES 18 A 267 GLY GLN VAL MET ASN LYS LEU ARG ARG LEU PHE THR ARG
SEQRES 19 A 267 ALA ARG PRO GLU SER GLN GLU LEU ASN ILE LEU ARG GLY
SEQRES 20 A 267 ILE LEU ALA SER ILE GLU GLN GLN ASN LYS GLY ASN LYS
SEQRES 21 A 267 ALA GLU GLY LEU CYS GLY ARG
SEQRES 1 B 267 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 B 267 ALA LEU ARG ALA LEU GLN ASN ILE ARG ILE VAL LEU VAL
SEQRES 3 B 267 GLU THR SER HIS THR GLY ASN MET GLY SER VAL ALA ARG
SEQRES 4 B 267 ALA MET LYS THR MET GLY LEU THR ASN LEU TRP LEU VAL
SEQRES 5 B 267 ASN PRO LEU VAL LYS PRO ASP SER GLN ALA ILE ALA LEU
SEQRES 6 B 267 ALA ALA GLY ALA SER ASP VAL ILE GLY ASN ALA HIS ILE
SEQRES 7 B 267 VAL ASP THR LEU ASP GLU ALA LEU ALA GLY CYS SER LEU
SEQRES 8 B 267 VAL VAL GLY THR SER ALA ARG SER ARG THR LEU PRO TRP
SEQRES 9 B 267 PRO MET LEU ASP PRO ARG GLU CYS GLY LEU LYS SER VAL
SEQRES 10 B 267 ALA GLU ALA ALA ASN THR PRO VAL ALA LEU VAL PHE GLY
SEQRES 11 B 267 ARG GLU ARG VAL GLY LEU THR ASN GLU GLU LEU GLN LYS
SEQRES 12 B 267 CYS HIS TYR HIS VAL ALA ILE ALA ALA ASN PRO GLU TYR
SEQRES 13 B 267 SER SER LEU ASN LEU ALA MET ALA VAL GLN VAL ILE ALA
SEQRES 14 B 267 TYR GLU VAL ARG MET ALA TRP LEU ALA THR GLN GLU ASN
SEQRES 15 B 267 GLY GLU GLN VAL GLU HIS GLU GLU THR PRO TYR PRO LEU
SEQRES 16 B 267 VAL ASP ASP LEU GLU ARG PHE TYR GLY HIS LEU GLU GLN
SEQRES 17 B 267 THR LEU LEU ALA THR GLY PHE ILE ARG GLU ASN HIS PRO
SEQRES 18 B 267 GLY GLN VAL MET ASN LYS LEU ARG ARG LEU PHE THR ARG
SEQRES 19 B 267 ALA ARG PRO GLU SER GLN GLU LEU ASN ILE LEU ARG GLY
SEQRES 20 B 267 ILE LEU ALA SER ILE GLU GLN GLN ASN LYS GLY ASN LYS
SEQRES 21 B 267 ALA GLU GLY LEU CYS GLY ARG
HET PEG B1165 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 PEG C4 H10 O3
FORMUL 4 HOH *207(H2 O)
HELIX 1 1 ALA A -3 GLN A 3 1 6
HELIX 2 2 HIS A 14 MET A 28 1 15
HELIX 3 3 ASP A 43 ALA A 51 1 9
HELIX 4 4 ALA A 53 ASN A 59 1 7
HELIX 5 5 THR A 65 ALA A 71 1 7
HELIX 6 6 ASP A 92 ALA A 105 1 14
HELIX 7 7 THR A 121 GLN A 126 1 6
HELIX 8 8 ASN A 144 THR A 163 1 20
HELIX 9 9 ALA B -3 GLN B 3 1 6
HELIX 10 10 HIS B 14 MET B 28 1 15
HELIX 11 11 ALA B 53 ASN B 59 1 7
HELIX 12 12 THR B 65 ALA B 71 1 7
HELIX 13 13 ASP B 92 ALA B 105 1 14
HELIX 14 14 THR B 121 GLN B 126 1 6
HELIX 15 15 ASN B 144 THR B 163 1 20
SHEET 1 AA 7 HIS A 61 VAL A 63 0
SHEET 2 AA 7 ASN A 32 VAL A 36 1 O LEU A 33 N HIS A 61
SHEET 3 AA 7 ILE A 5 VAL A 10 1 O ILE A 5 N ASN A 32
SHEET 4 AA 7 VAL A 109 PHE A 113 1 O VAL A 109 N ARG A 6
SHEET 5 AA 7 LEU A 75 THR A 79 1 O LEU A 75 N ALA A 110
SHEET 6 AA 7 TYR A 130 VAL A 132 1 O TYR A 130 N GLY A 78
SHEET 7 AA 7 MET A 90 LEU A 91 1 N LEU A 91 O HIS A 131
SHEET 1 BA 7 HIS B 61 VAL B 63 0
SHEET 2 BA 7 ASN B 32 VAL B 36 1 O LEU B 33 N HIS B 61
SHEET 3 BA 7 ILE B 5 VAL B 10 1 O ILE B 5 N ASN B 32
SHEET 4 BA 7 VAL B 109 PHE B 113 1 O VAL B 109 N ARG B 6
SHEET 5 BA 7 LEU B 75 THR B 79 1 O LEU B 75 N ALA B 110
SHEET 6 BA 7 TYR B 130 VAL B 132 1 O TYR B 130 N GLY B 78
SHEET 7 BA 7 MET B 90 LEU B 91 1 N LEU B 91 O HIS B 131
SITE 1 AC1 3 PRO B 89 HIS B 129 TYR B 130
CRYST1 42.400 73.030 53.330 90.00 105.13 90.00 P 1 21 1 4
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 0.023585 0.000000 0.006377 0.00000
SCALE2 0.000000 0.013693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019425 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
