HEADER DRUG-BINDING PROTEIN 15-JAN-07 2JE5
TITLE STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN
TITLE 2 INHIBITION BY LACTIVICINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLIN-BINDING PROTEIN 1B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 72-791;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 171101;
SOURCE 4 STRAIN: R6;
SOURCE 5 ATCC: BAA-255;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS PEPTIDOGLYCAN SYNTHESIS MULTIFUNCTIONAL ENZYME, CELL WALL,
KEYWDS 2 PEPTIDOGLYCAN, GAMMA LACTAM ANTIBIOTICS, DRUG-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MACHEBOEUF,D.S.FISHER,T.J.BROWN,A.ZERVOSEN,A.LUXEN,B.JORIS,
AUTHOR 2 A.DESSEN,C.J.SCHOFIELD
REVDAT 4 13-DEC-23 2JE5 1 LINK
REVDAT 3 24-FEB-09 2JE5 1 VERSN
REVDAT 2 27-NOV-07 2JE5 1 JRNL
REVDAT 1 14-AUG-07 2JE5 0
JRNL AUTH P.MACHEBOEUF,D.S.FISHER,T.J.BROWN,A.ZERVOSEN,A.LUXEN,
JRNL AUTH 2 B.JORIS,A.DESSEN,C.J.SCHOFIELD
JRNL TITL STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN-BINDING
JRNL TITL 2 PROTEIN INHIBITION BY LACTIVICINS
JRNL REF NAT.CHEM.BIOL. V. 3 565 2007
JRNL REFN ISSN 1552-4450
JRNL PMID 17676039
JRNL DOI 10.1038/NCHEMBIO.2007.21
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 44214
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) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2315
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3228
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 187
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : 0.03000
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): 0.475
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.230
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.870
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7301 ; 0.042 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9921 ; 3.252 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 921 ; 8.796 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 339 ;40.221 ;25.221
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1161 ;22.119 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;18.478 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1081 ; 0.212 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5630 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3489 ; 0.279 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4982 ; 0.341 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 312 ; 0.171 ; 0.200
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): 27 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.148 ; 0.200
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): 4739 ; 1.676 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7296 ; 2.749 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3094 ; 4.468 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2625 ; 6.510 ; 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 : 1.20
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 2JE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1290031104.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46529
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 84.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2BG1
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MH HEPES 3.2 M SODIUM CHLORIDE 0.8
REMARK 280 M AMMONIUM SULFATE, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 49.27000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.08000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.91500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.08000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.27000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.91500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 73 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 123 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 158 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PRO 162 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 336 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 686 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 687 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 73 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 123 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 158 TO LYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, PRO 162 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ARG 336 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ARG 686 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ARG 687 TO GLN
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 GLY A 72
REMARK 465 SER A 73
REMARK 465 GLY A 74
REMARK 465 ILE A 75
REMARK 465 ALA A 76
REMARK 465 LEU A 77
REMARK 465 GLY A 78
REMARK 465 TYR A 79
REMARK 465 GLY A 80
REMARK 465 VAL A 81
REMARK 465 ALA A 82
REMARK 465 LEU A 83
REMARK 465 PHE A 84
REMARK 465 ASP A 85
REMARK 465 LYS A 86
REMARK 465 VAL A 87
REMARK 465 ARG A 88
REMARK 465 VAL A 89
REMARK 465 PRO A 90
REMARK 465 GLN A 91
REMARK 465 THR A 92
REMARK 465 GLU A 93
REMARK 465 GLU A 94
REMARK 465 LEU A 95
REMARK 465 VAL A 96
REMARK 465 ASN A 97
REMARK 465 GLN A 98
REMARK 465 VAL A 99
REMARK 465 LYS A 100
REMARK 465 ASP A 101
REMARK 465 ILE A 102
REMARK 465 SER A 103
REMARK 465 SER A 104
REMARK 465 ILE A 105
REMARK 465 VAL A 115
REMARK 465 ILE A 116
REMARK 465 ALA A 117
REMARK 465 SER A 118
REMARK 465 ILE A 119
REMARK 465 GLU A 120
REMARK 465 SER A 121
REMARK 465 ASP A 122
REMARK 465 MET A 123
REMARK 465 LEU A 124
REMARK 465 ARG A 125
REMARK 465 THR A 126
REMARK 465 SER A 127
REMARK 465 ILE A 128
REMARK 465 SER A 129
REMARK 465 SER A 130
REMARK 465 GLU A 131
REMARK 465 GLN A 132
REMARK 465 ILE A 133
REMARK 465 SER A 134
REMARK 465 GLU A 135
REMARK 465 ASN A 136
REMARK 465 LEU A 137
REMARK 465 LYS A 138
REMARK 465 LYS A 139
REMARK 465 ALA A 140
REMARK 465 ILE A 141
REMARK 465 ILE A 142
REMARK 465 ALA A 143
REMARK 465 THR A 144
REMARK 465 GLU A 145
REMARK 465 ASP A 146
REMARK 465 GLU A 147
REMARK 465 HIS A 148
REMARK 465 PHE A 149
REMARK 465 LYS A 150
REMARK 465 GLU A 151
REMARK 465 HIS A 152
REMARK 465 LYS A 153
REMARK 465 GLY A 154
REMARK 465 VAL A 155
REMARK 465 VAL A 156
REMARK 465 PRO A 157
REMARK 465 ASN A 158
REMARK 465 ALA A 159
REMARK 465 VAL A 160
REMARK 465 ILE A 161
REMARK 465 PRO A 162
REMARK 465 ALA A 163
REMARK 465 THR A 164
REMARK 465 LEU A 165
REMARK 465 GLY A 166
REMARK 465 LYS A 167
REMARK 465 PHE A 168
REMARK 465 VAL A 169
REMARK 465 GLY A 170
REMARK 465 LEU A 171
REMARK 465 GLY A 172
REMARK 465 SER A 173
REMARK 465 SER A 174
REMARK 465 SER A 175
REMARK 465 GLY A 176
REMARK 465 GLY A 177
REMARK 465 SER A 178
REMARK 465 THR A 179
REMARK 465 LEU A 180
REMARK 465 THR A 181
REMARK 465 GLN A 182
REMARK 465 GLN A 183
REMARK 465 LEU A 184
REMARK 465 ILE A 185
REMARK 465 LYS A 186
REMARK 465 GLN A 187
REMARK 465 GLN A 188
REMARK 465 VAL A 189
REMARK 465 VAL A 190
REMARK 465 GLY A 191
REMARK 465 ASP A 192
REMARK 465 ALA A 193
REMARK 465 PRO A 194
REMARK 465 THR A 195
REMARK 465 LEU A 196
REMARK 465 ALA A 197
REMARK 465 ARG A 198
REMARK 465 LYS A 199
REMARK 465 ALA A 200
REMARK 465 ALA A 201
REMARK 465 GLU A 202
REMARK 465 ILE A 203
REMARK 465 VAL A 204
REMARK 465 ASP A 205
REMARK 465 ALA A 206
REMARK 465 LEU A 207
REMARK 465 ALA A 208
REMARK 465 LEU A 209
REMARK 465 GLU A 210
REMARK 465 ARG A 211
REMARK 465 ALA A 212
REMARK 465 MET A 213
REMARK 465 ASN A 214
REMARK 465 LYS A 215
REMARK 465 ASP A 216
REMARK 465 GLU A 217
REMARK 465 ILE A 218
REMARK 465 LEU A 219
REMARK 465 THR A 220
REMARK 465 THR A 221
REMARK 465 TYR A 222
REMARK 465 LEU A 223
REMARK 465 ASN A 224
REMARK 465 VAL A 225
REMARK 465 ALA A 226
REMARK 465 PRO A 227
REMARK 465 PHE A 228
REMARK 465 GLY A 229
REMARK 465 ARG A 230
REMARK 465 ASN A 231
REMARK 465 ASN A 232
REMARK 465 LYS A 233
REMARK 465 GLY A 234
REMARK 465 GLN A 235
REMARK 465 ASN A 236
REMARK 465 ILE A 237
REMARK 465 ALA A 238
REMARK 465 GLY A 239
REMARK 465 ALA A 240
REMARK 465 ARG A 241
REMARK 465 GLN A 242
REMARK 465 ALA A 243
REMARK 465 ALA A 244
REMARK 465 GLU A 245
REMARK 465 GLY A 246
REMARK 465 ILE A 247
REMARK 465 PHE A 248
REMARK 465 GLY A 249
REMARK 465 VAL A 250
REMARK 465 ASP A 251
REMARK 465 ALA A 252
REMARK 465 SER A 253
REMARK 465 GLN A 254
REMARK 465 LEU A 255
REMARK 465 THR A 256
REMARK 465 VAL A 257
REMARK 465 PRO A 258
REMARK 465 GLN A 259
REMARK 465 ALA A 260
REMARK 465 ALA A 261
REMARK 465 PHE A 262
REMARK 465 LEU A 263
REMARK 465 ALA A 264
REMARK 465 GLY A 265
REMARK 465 LEU A 266
REMARK 465 PRO A 267
REMARK 465 GLN A 268
REMARK 465 SER A 269
REMARK 465 PRO A 270
REMARK 465 ILE A 271
REMARK 465 THR A 272
REMARK 465 TYR A 273
REMARK 465 SER A 274
REMARK 465 PRO A 275
REMARK 465 TYR A 276
REMARK 465 GLU A 277
REMARK 465 ASN A 278
REMARK 465 THR A 279
REMARK 465 GLY A 280
REMARK 465 GLU A 281
REMARK 465 LEU A 282
REMARK 465 LYS A 283
REMARK 465 SER A 284
REMARK 465 ASP A 285
REMARK 465 GLU A 286
REMARK 465 ASP A 287
REMARK 465 LEU A 288
REMARK 465 GLU A 289
REMARK 465 ILE A 290
REMARK 465 GLY A 291
REMARK 465 LEU A 292
REMARK 465 ARG A 293
REMARK 465 ARG A 294
REMARK 465 ALA A 295
REMARK 465 LYS A 296
REMARK 465 ALA A 297
REMARK 465 VAL A 298
REMARK 465 LEU A 299
REMARK 465 TYR A 300
REMARK 465 SER A 301
REMARK 465 MET A 302
REMARK 465 TYR A 303
REMARK 465 ARG A 304
REMARK 465 THR A 305
REMARK 465 GLY A 306
REMARK 465 ALA A 307
REMARK 465 LEU A 308
REMARK 465 SER A 309
REMARK 465 LYS A 310
REMARK 465 ASP A 311
REMARK 465 GLU A 312
REMARK 465 TYR A 313
REMARK 465 SER A 314
REMARK 465 GLN A 315
REMARK 465 TYR A 316
REMARK 465 LYS A 317
REMARK 465 ASP A 318
REMARK 465 TYR A 319
REMARK 465 ASP A 320
REMARK 465 LEU A 321
REMARK 465 LYS A 322
REMARK 465 GLN A 323
REMARK 465 ASP A 324
REMARK 465 PHE A 325
REMARK 465 LEU A 326
REMARK 465 PRO A 327
REMARK 465 SER A 328
REMARK 465 GLY A 329
REMARK 465 THR A 330
REMARK 465 VAL A 331
REMARK 465 THR A 332
REMARK 465 GLY A 333
REMARK 465 ILE A 334
REMARK 465 SER A 335
REMARK 465 GLN A 336
REMARK 465 SER A 789
REMARK 465 LEU A 790
REMARK 465 PRO A 791
REMARK 465 GLY B 72
REMARK 465 SER B 73
REMARK 465 GLY B 74
REMARK 465 ILE B 75
REMARK 465 ALA B 76
REMARK 465 LEU B 77
REMARK 465 GLY B 78
REMARK 465 TYR B 79
REMARK 465 GLY B 80
REMARK 465 VAL B 81
REMARK 465 ALA B 82
REMARK 465 LEU B 83
REMARK 465 PHE B 84
REMARK 465 ASP B 85
REMARK 465 LYS B 86
REMARK 465 VAL B 87
REMARK 465 ARG B 88
REMARK 465 VAL B 89
REMARK 465 PRO B 90
REMARK 465 GLN B 91
REMARK 465 THR B 92
REMARK 465 GLU B 93
REMARK 465 GLU B 94
REMARK 465 LEU B 95
REMARK 465 VAL B 96
REMARK 465 ASN B 97
REMARK 465 GLN B 98
REMARK 465 VAL B 99
REMARK 465 LYS B 100
REMARK 465 ASP B 101
REMARK 465 ILE B 102
REMARK 465 SER B 103
REMARK 465 SER B 104
REMARK 465 ILE B 105
REMARK 465 ILE B 116
REMARK 465 ALA B 117
REMARK 465 SER B 118
REMARK 465 ILE B 119
REMARK 465 GLU B 120
REMARK 465 SER B 121
REMARK 465 ASP B 122
REMARK 465 MET B 123
REMARK 465 LEU B 124
REMARK 465 ARG B 125
REMARK 465 THR B 126
REMARK 465 SER B 127
REMARK 465 ILE B 128
REMARK 465 SER B 129
REMARK 465 SER B 130
REMARK 465 GLU B 131
REMARK 465 GLN B 132
REMARK 465 ILE B 133
REMARK 465 SER B 134
REMARK 465 GLU B 135
REMARK 465 ASN B 136
REMARK 465 LEU B 137
REMARK 465 LYS B 138
REMARK 465 LYS B 139
REMARK 465 ALA B 140
REMARK 465 ILE B 141
REMARK 465 ILE B 142
REMARK 465 ALA B 143
REMARK 465 THR B 144
REMARK 465 GLU B 145
REMARK 465 ASP B 146
REMARK 465 GLU B 147
REMARK 465 HIS B 148
REMARK 465 PHE B 149
REMARK 465 LYS B 150
REMARK 465 GLU B 151
REMARK 465 HIS B 152
REMARK 465 LYS B 153
REMARK 465 GLY B 154
REMARK 465 VAL B 155
REMARK 465 VAL B 156
REMARK 465 PRO B 157
REMARK 465 ASN B 158
REMARK 465 ALA B 159
REMARK 465 VAL B 160
REMARK 465 ILE B 161
REMARK 465 PRO B 162
REMARK 465 ALA B 163
REMARK 465 THR B 164
REMARK 465 LEU B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 PHE B 168
REMARK 465 VAL B 169
REMARK 465 GLY B 170
REMARK 465 LEU B 171
REMARK 465 GLY B 172
REMARK 465 SER B 173
REMARK 465 SER B 174
REMARK 465 SER B 175
REMARK 465 GLY B 176
REMARK 465 GLY B 177
REMARK 465 SER B 178
REMARK 465 THR B 179
REMARK 465 LEU B 180
REMARK 465 THR B 181
REMARK 465 GLN B 182
REMARK 465 GLN B 183
REMARK 465 LEU B 184
REMARK 465 ILE B 185
REMARK 465 LYS B 186
REMARK 465 GLN B 187
REMARK 465 GLN B 188
REMARK 465 VAL B 189
REMARK 465 VAL B 190
REMARK 465 GLY B 191
REMARK 465 ASP B 192
REMARK 465 ALA B 193
REMARK 465 PRO B 194
REMARK 465 THR B 195
REMARK 465 LEU B 196
REMARK 465 ALA B 197
REMARK 465 ARG B 198
REMARK 465 LYS B 199
REMARK 465 ALA B 200
REMARK 465 ALA B 201
REMARK 465 GLU B 202
REMARK 465 ILE B 203
REMARK 465 VAL B 204
REMARK 465 ASP B 205
REMARK 465 ALA B 206
REMARK 465 LEU B 207
REMARK 465 ALA B 208
REMARK 465 LEU B 209
REMARK 465 GLU B 210
REMARK 465 ARG B 211
REMARK 465 ALA B 212
REMARK 465 MET B 213
REMARK 465 ASN B 214
REMARK 465 LYS B 215
REMARK 465 ASP B 216
REMARK 465 GLU B 217
REMARK 465 ILE B 218
REMARK 465 LEU B 219
REMARK 465 THR B 220
REMARK 465 THR B 221
REMARK 465 TYR B 222
REMARK 465 LEU B 223
REMARK 465 ASN B 224
REMARK 465 VAL B 225
REMARK 465 ALA B 226
REMARK 465 PRO B 227
REMARK 465 PHE B 228
REMARK 465 GLY B 229
REMARK 465 ARG B 230
REMARK 465 ASN B 231
REMARK 465 ASN B 232
REMARK 465 LYS B 233
REMARK 465 GLY B 234
REMARK 465 GLN B 235
REMARK 465 ASN B 236
REMARK 465 ILE B 237
REMARK 465 ALA B 238
REMARK 465 GLY B 239
REMARK 465 ALA B 240
REMARK 465 ARG B 241
REMARK 465 GLN B 242
REMARK 465 ALA B 243
REMARK 465 ALA B 244
REMARK 465 GLU B 245
REMARK 465 GLY B 246
REMARK 465 ILE B 247
REMARK 465 PHE B 248
REMARK 465 GLY B 249
REMARK 465 VAL B 250
REMARK 465 ASP B 251
REMARK 465 ALA B 252
REMARK 465 SER B 253
REMARK 465 GLN B 254
REMARK 465 LEU B 255
REMARK 465 THR B 256
REMARK 465 VAL B 257
REMARK 465 PRO B 258
REMARK 465 GLN B 259
REMARK 465 ALA B 260
REMARK 465 ALA B 261
REMARK 465 PHE B 262
REMARK 465 LEU B 263
REMARK 465 ALA B 264
REMARK 465 GLY B 265
REMARK 465 LEU B 266
REMARK 465 PRO B 267
REMARK 465 GLN B 268
REMARK 465 SER B 269
REMARK 465 PRO B 270
REMARK 465 ILE B 271
REMARK 465 THR B 272
REMARK 465 TYR B 273
REMARK 465 SER B 274
REMARK 465 PRO B 275
REMARK 465 TYR B 276
REMARK 465 GLU B 277
REMARK 465 ASN B 278
REMARK 465 THR B 279
REMARK 465 GLY B 280
REMARK 465 GLU B 281
REMARK 465 LEU B 282
REMARK 465 LYS B 283
REMARK 465 SER B 284
REMARK 465 ASP B 285
REMARK 465 GLU B 286
REMARK 465 ASP B 287
REMARK 465 LEU B 288
REMARK 465 GLU B 289
REMARK 465 ILE B 290
REMARK 465 GLY B 291
REMARK 465 LEU B 292
REMARK 465 ARG B 293
REMARK 465 ARG B 294
REMARK 465 ALA B 295
REMARK 465 LYS B 296
REMARK 465 ALA B 297
REMARK 465 VAL B 298
REMARK 465 LEU B 299
REMARK 465 TYR B 300
REMARK 465 SER B 301
REMARK 465 MET B 302
REMARK 465 TYR B 303
REMARK 465 ARG B 304
REMARK 465 THR B 305
REMARK 465 GLY B 306
REMARK 465 ALA B 307
REMARK 465 LEU B 308
REMARK 465 SER B 309
REMARK 465 LYS B 310
REMARK 465 ASP B 311
REMARK 465 GLU B 312
REMARK 465 TYR B 313
REMARK 465 SER B 314
REMARK 465 GLN B 315
REMARK 465 TYR B 316
REMARK 465 LYS B 317
REMARK 465 ASP B 318
REMARK 465 TYR B 319
REMARK 465 ASP B 320
REMARK 465 LEU B 321
REMARK 465 LYS B 322
REMARK 465 GLN B 323
REMARK 465 ASP B 324
REMARK 465 PHE B 325
REMARK 465 LEU B 326
REMARK 465 PRO B 327
REMARK 465 SER B 328
REMARK 465 GLY B 329
REMARK 465 THR B 330
REMARK 465 VAL B 331
REMARK 465 THR B 332
REMARK 465 GLY B 333
REMARK 465 ILE B 334
REMARK 465 SER B 335
REMARK 465 GLN B 336
REMARK 465 SER B 789
REMARK 465 LEU B 790
REMARK 465 PRO B 791
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 GLN A 601 CG CD OE1 NE2
REMARK 470 LYS A 603 CG CD CE NZ
REMARK 470 LYS A 738 CG CD CE NZ
REMARK 470 SER A 740 OG
REMARK 470 LYS A 744 CG CD CE NZ
REMARK 470 GLN B 601 CG CD OE1 NE2
REMARK 470 LYS B 603 CG CD CE NZ
REMARK 470 LYS B 738 CG CD CE NZ
REMARK 470 SER B 740 OG
REMARK 470 LYS B 744 CG 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 OE1 GLU A 382 OH TYR A 388 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 A 341 CE1 PHE A 341 CZ 0.131
REMARK 500 ALA A 345 C ALA A 345 O 0.157
REMARK 500 GLU A 346 N GLU A 346 CA 0.133
REMARK 500 GLU A 346 CB GLU A 346 CG 0.303
REMARK 500 GLU A 346 CG GLU A 346 CD 0.215
REMARK 500 GLU A 346 CD GLU A 346 OE1 -0.100
REMARK 500 TYR A 354 CD1 TYR A 354 CE1 0.178
REMARK 500 LEU A 366 CG LEU A 366 CD2 0.232
REMARK 500 GLU A 369 CD GLU A 369 OE1 0.067
REMARK 500 GLU A 384 CG GLU A 384 CD 0.125
REMARK 500 GLU A 384 CD GLU A 384 OE2 0.082
REMARK 500 GLN A 396 CG GLN A 396 CD 0.186
REMARK 500 TYR A 411 CB TYR A 411 CG -0.097
REMARK 500 TYR A 411 CE1 TYR A 411 CZ 0.091
REMARK 500 GLU A 421 CD GLU A 421 OE1 0.075
REMARK 500 VAL A 422 CA VAL A 422 CB 0.134
REMARK 500 GLU A 445 CG GLU A 445 CD 0.121
REMARK 500 ALA A 451 CA ALA A 451 CB 0.148
REMARK 500 THR A 454 CB THR A 454 CG2 0.233
REMARK 500 GLU A 511 CD GLU A 511 OE2 0.074
REMARK 500 TYR A 515 CG TYR A 515 CD1 0.078
REMARK 500 TRP A 517 CB TRP A 517 CG 0.111
REMARK 500 MET A 539 CG MET A 539 SD 0.162
REMARK 500 GLU A 548 CD GLU A 548 OE1 0.077
REMARK 500 TYR A 580 CG TYR A 580 CD2 0.086
REMARK 500 LYS A 588 CD LYS A 588 CE 0.168
REMARK 500 TYR A 600 CG TYR A 600 CD2 0.088
REMARK 500 GLN A 601 CA GLN A 601 CB 0.210
REMARK 500 VAL A 605 CB VAL A 605 CG2 0.135
REMARK 500 LYS A 633 CB LYS A 633 CG 0.171
REMARK 500 LYS A 633 CE LYS A 633 NZ 0.176
REMARK 500 SER A 638 CA SER A 638 CB -0.100
REMARK 500 LEU A 672 C LEU A 672 O 0.121
REMARK 500 TRP A 675 CB TRP A 675 CG 0.131
REMARK 500 TYR A 690 CD1 TYR A 690 CE1 0.103
REMARK 500 TYR A 696 CG TYR A 696 CD2 0.104
REMARK 500 TYR A 696 CE1 TYR A 696 CZ 0.085
REMARK 500 GLN A 706 CB GLN A 706 CG 0.211
REMARK 500 GLU A 742 CB GLU A 742 CG 0.122
REMARK 500 GLU A 742 CG GLU A 742 CD 0.112
REMARK 500 LYS A 760 CB LYS A 760 CG 0.200
REMARK 500 ILE A 786 CA ILE A 786 CB 0.162
REMARK 500 THR B 114 N THR B 114 CA 0.131
REMARK 500 VAL B 115 N VAL B 115 CA 0.121
REMARK 500 VAL B 115 CA VAL B 115 CB 0.260
REMARK 500 VAL B 115 CB VAL B 115 CG2 0.144
REMARK 500 TYR B 340 CE2 TYR B 340 CD2 0.099
REMARK 500 TYR B 354 CD1 TYR B 354 CE1 0.091
REMARK 500 LYS B 364 CD LYS B 364 CE 0.153
REMARK 500 GLU B 369 CG GLU B 369 CD 0.105
REMARK 500
REMARK 500 THIS ENTRY HAS 86 BOND DEVIATIONS.
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 GLU A 346 OE1 - CD - OE2 ANGL. DEV. = -21.3 DEGREES
REMARK 500 GLU A 346 CG - CD - OE2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 TYR A 354 CD1 - CE1 - CZ ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 376 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 376 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU A 384 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 MET A 556 CG - SD - CE ANGL. DEV. = -10.8 DEGREES
REMARK 500 ILE A 560 CB - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 VAL A 597 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 PRO A 604 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 627 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 627 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU A 639 CB - CG - CD1 ANGL. DEV. = -15.1 DEGREES
REMARK 500 MET A 697 CG - SD - CE ANGL. DEV. = -14.3 DEGREES
REMARK 500 SER A 751 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP A 778 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 THR B 114 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP B 337 CB - CG - OD1 ANGL. DEV. = 12.4 DEGREES
REMARK 500 ASP B 337 CB - CG - OD2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 MET B 351 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 THR B 371 C - N - CA ANGL. DEV. = -15.7 DEGREES
REMARK 500 THR B 371 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 ASP B 377 CB - CG - OD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASP B 377 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 LYS B 389 CD - CE - NZ ANGL. DEV. = 17.2 DEGREES
REMARK 500 ASP B 414 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 GLU B 421 CG - CD - OE1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO B 495 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG B 529 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU B 548 CG - CD - OE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 MET B 556 CG - SD - CE ANGL. DEV. = -9.7 DEGREES
REMARK 500 ILE B 560 CB - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 LEU B 574 CB - CG - CD1 ANGL. DEV. = -19.2 DEGREES
REMARK 500 LEU B 624 CB - CG - CD2 ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG B 627 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LEU B 639 CB - CG - CD1 ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU B 643 CB - CG - CD2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 LEU B 665 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU B 729 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 GLY B 750 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 SER B 751 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 ASP B 776 CB - CG - OD2 ANGL. DEV. = 6.2 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 A 110 134.36 -14.84
REMARK 500 SER A 111 -43.56 -16.30
REMARK 500 GLU A 365 -31.55 -134.41
REMARK 500 ARG A 419 123.39 -39.30
REMARK 500 ASN A 442 106.72 -175.19
REMARK 500 ASN A 446 118.23 -163.84
REMARK 500 ALA A 459 -140.45 62.62
REMARK 500 ALA A 467 -69.53 -104.90
REMARK 500 ALA A 499 -114.15 50.35
REMARK 500 THR A 504 -108.49 -125.99
REMARK 500 ASP A 534 68.28 -69.66
REMARK 500 ASN A 576 49.34 -95.09
REMARK 500 ALA A 592 -22.07 -36.77
REMARK 500 PHE A 632 -61.75 -29.34
REMARK 500 ASN A 640 86.06 -169.35
REMARK 500 GLN A 657 -6.68 62.04
REMARK 500 ASN A 681 0.08 80.95
REMARK 500 SER A 691 -74.74 -90.61
REMARK 500 LYS A 730 -32.62 -32.70
REMARK 500 SER A 740 72.44 -49.13
REMARK 500 GLU A 742 77.55 20.21
REMARK 500 LYS A 744 -149.88 141.02
REMARK 500 GLU A 745 126.25 -171.56
REMARK 500 SER A 761 -24.42 -148.22
REMARK 500 THR A 766 172.14 -48.40
REMARK 500 SER A 784 58.91 -93.37
REMARK 500 SER A 785 -60.47 -176.24
REMARK 500 ILE A 786 45.05 -78.23
REMARK 500 VAL A 787 -88.61 -141.19
REMARK 500 TYR B 110 -169.50 -51.96
REMARK 500 ASN B 360 30.05 73.23
REMARK 500 THR B 371 -76.73 101.85
REMARK 500 ASN B 442 98.25 -176.43
REMARK 500 ASN B 446 119.04 -163.22
REMARK 500 ALA B 459 -134.76 43.31
REMARK 500 ALA B 467 -76.79 -113.47
REMARK 500 ALA B 499 -111.75 61.92
REMARK 500 THR B 504 -116.53 -135.79
REMARK 500 ASN B 576 47.88 -100.99
REMARK 500 ALA B 592 -18.26 -31.43
REMARK 500 LYS B 603 71.83 -108.77
REMARK 500 ASN B 640 81.86 -170.42
REMARK 500 ALA B 644 -19.74 -47.63
REMARK 500 GLN B 657 -8.41 68.72
REMARK 500 LYS B 730 -57.94 -16.50
REMARK 500 SER B 740 90.56 -65.06
REMARK 500 GLU B 742 76.73 21.00
REMARK 500 LYS B 744 -156.63 122.49
REMARK 500 LYS B 760 -62.02 -26.11
REMARK 500 THR B 766 179.92 -48.08
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
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 THR A 109 TYR A 110 140.11
REMARK 500 ASP A 112 GLY A 113 -146.24
REMARK 500 ASP A 337 TYR A 338 145.06
REMARK 500 LYS A 760 SER A 761 -145.49
REMARK 500 SER B 666 THR B 667 147.72
REMARK 500 ASN B 759 LYS B 760 148.22
REMARK 500 LYS B 760 SER B 761 -145.65
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 L4C A1789
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L4C B1789
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1790
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1790
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1792
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BG1 RELATED DB: PDB
REMARK 900 ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA
REMARK 900 PENICILLIN-BINDING PROTEINS (PBPS)
REMARK 900 RELATED ID: 2BG3 RELATED DB: PDB
REMARK 900 ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA
REMARK 900 PENICILLIN-BINDING PROTEINS (PBPS)
REMARK 900 RELATED ID: 2BG4 RELATED DB: PDB
REMARK 900 ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA
REMARK 900 PENICILLIN-BINDING PROTEINS (PBPS)
REMARK 900 RELATED ID: 2FFF RELATED DB: PDB
REMARK 900 OPEN FORM OF A CLASS A TRANSPEPTIDASE DOMAIN
REMARK 900 RELATED ID: 2JCH RELATED DB: PDB
REMARK 900 DISRUPTION OF THE BACTERIAL PEPTIDOGLYCAN BIOSYNTHETIC MACHINERY BY
REMARK 900 NON-B-LACTAM ANTIBIOTICS
REMARK 900 RELATED ID: 2JCI RELATED DB: PDB
REMARK 900 STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM AND THE ROLE OF
REMARK 900 STREPTOCOCCUS PNEUMONIAE PBP1B
DBREF 2JE5 A 72 791 UNP O70038 O70038_STRPN 72 791
DBREF 2JE5 B 72 791 UNP O70038 O70038_STRPN 72 791
SEQADV 2JE5 SER A 73 UNP O70038 ALA 73 ENGINEERED MUTATION
SEQADV 2JE5 MET A 123 UNP O70038 LEU 123 ENGINEERED MUTATION
SEQADV 2JE5 ASN A 158 UNP O70038 LYS 158 ENGINEERED MUTATION
SEQADV 2JE5 PRO A 162 UNP O70038 ARG 162 ENGINEERED MUTATION
SEQADV 2JE5 GLN A 336 UNP O70038 ARG 336 ENGINEERED MUTATION
SEQADV 2JE5 GLN A 686 UNP O70038 ARG 686 ENGINEERED MUTATION
SEQADV 2JE5 GLN A 687 UNP O70038 ARG 687 ENGINEERED MUTATION
SEQADV 2JE5 SER B 73 UNP O70038 ALA 73 ENGINEERED MUTATION
SEQADV 2JE5 MET B 123 UNP O70038 LEU 123 ENGINEERED MUTATION
SEQADV 2JE5 ASN B 158 UNP O70038 LYS 158 ENGINEERED MUTATION
SEQADV 2JE5 PRO B 162 UNP O70038 ARG 162 ENGINEERED MUTATION
SEQADV 2JE5 GLN B 336 UNP O70038 ARG 336 ENGINEERED MUTATION
SEQADV 2JE5 GLN B 686 UNP O70038 ARG 686 ENGINEERED MUTATION
SEQADV 2JE5 GLN B 687 UNP O70038 ARG 687 ENGINEERED MUTATION
SEQRES 1 A 720 GLY SER GLY ILE ALA LEU GLY TYR GLY VAL ALA LEU PHE
SEQRES 2 A 720 ASP LYS VAL ARG VAL PRO GLN THR GLU GLU LEU VAL ASN
SEQRES 3 A 720 GLN VAL LYS ASP ILE SER SER ILE SER GLU ILE THR TYR
SEQRES 4 A 720 SER ASP GLY THR VAL ILE ALA SER ILE GLU SER ASP MET
SEQRES 5 A 720 LEU ARG THR SER ILE SER SER GLU GLN ILE SER GLU ASN
SEQRES 6 A 720 LEU LYS LYS ALA ILE ILE ALA THR GLU ASP GLU HIS PHE
SEQRES 7 A 720 LYS GLU HIS LYS GLY VAL VAL PRO ASN ALA VAL ILE PRO
SEQRES 8 A 720 ALA THR LEU GLY LYS PHE VAL GLY LEU GLY SER SER SER
SEQRES 9 A 720 GLY GLY SER THR LEU THR GLN GLN LEU ILE LYS GLN GLN
SEQRES 10 A 720 VAL VAL GLY ASP ALA PRO THR LEU ALA ARG LYS ALA ALA
SEQRES 11 A 720 GLU ILE VAL ASP ALA LEU ALA LEU GLU ARG ALA MET ASN
SEQRES 12 A 720 LYS ASP GLU ILE LEU THR THR TYR LEU ASN VAL ALA PRO
SEQRES 13 A 720 PHE GLY ARG ASN ASN LYS GLY GLN ASN ILE ALA GLY ALA
SEQRES 14 A 720 ARG GLN ALA ALA GLU GLY ILE PHE GLY VAL ASP ALA SER
SEQRES 15 A 720 GLN LEU THR VAL PRO GLN ALA ALA PHE LEU ALA GLY LEU
SEQRES 16 A 720 PRO GLN SER PRO ILE THR TYR SER PRO TYR GLU ASN THR
SEQRES 17 A 720 GLY GLU LEU LYS SER ASP GLU ASP LEU GLU ILE GLY LEU
SEQRES 18 A 720 ARG ARG ALA LYS ALA VAL LEU TYR SER MET TYR ARG THR
SEQRES 19 A 720 GLY ALA LEU SER LYS ASP GLU TYR SER GLN TYR LYS ASP
SEQRES 20 A 720 TYR ASP LEU LYS GLN ASP PHE LEU PRO SER GLY THR VAL
SEQRES 21 A 720 THR GLY ILE SER GLN ASP TYR LEU TYR PHE THR THR LEU
SEQRES 22 A 720 ALA GLU ALA GLN GLU ARG MET TYR ASP TYR LEU ALA GLN
SEQRES 23 A 720 ARG ASP ASN VAL SER ALA LYS GLU LEU LYS ASN GLU ALA
SEQRES 24 A 720 THR GLN LYS PHE TYR ARG ASP LEU ALA ALA LYS GLU ILE
SEQRES 25 A 720 GLU ASN GLY GLY TYR LYS ILE THR THR THR ILE ASP GLN
SEQRES 26 A 720 LYS ILE HIS SER ALA MET GLN SER ALA VAL ALA ASP TYR
SEQRES 27 A 720 GLY TYR LEU LEU ASP ASP GLY THR GLY ARG VAL GLU VAL
SEQRES 28 A 720 GLY ASN VAL LEU MET ASP ASN GLN THR GLY ALA ILE LEU
SEQRES 29 A 720 GLY PHE VAL GLY GLY ARG ASN TYR GLN GLU ASN GLN ASN
SEQRES 30 A 720 ASN HIS ALA PHE ASP THR LYS ARG SER PRO ALA SER THR
SEQRES 31 A 720 THR LYS PRO LEU LEU ALA TYR GLY ILE ALA ILE ASP GLN
SEQRES 32 A 720 GLY LEU MET GLY SER GLU THR ILE LEU SER ASN TYR PRO
SEQRES 33 A 720 THR ASN PHE ALA ASN GLY ASN PRO ILE MET TYR ALA ASN
SEQRES 34 A 720 SER LYS GLY THR GLY MET MET THR LEU GLY GLU ALA LEU
SEQRES 35 A 720 ASN TYR SER TRP ASN ILE PRO ALA TYR TRP THR TYR ARG
SEQRES 36 A 720 MET LEU ARG GLU ASN GLY VAL ASP VAL LYS GLY TYR MET
SEQRES 37 A 720 GLU LYS MET GLY TYR GLU ILE PRO GLU TYR GLY ILE GLU
SEQRES 38 A 720 SER LEU PRO MET GLY GLY GLY ILE GLU VAL THR VAL ALA
SEQRES 39 A 720 GLN HIS THR ASN GLY TYR GLN THR LEU ALA ASN ASN GLY
SEQRES 40 A 720 VAL TYR HIS GLN LYS HIS VAL ILE SER LYS ILE GLU ALA
SEQRES 41 A 720 ALA ASP GLY ARG VAL VAL TYR GLU TYR GLN ASP LYS PRO
SEQRES 42 A 720 VAL GLN VAL TYR SER LYS ALA THR ALA THR ILE MET GLN
SEQRES 43 A 720 GLY LEU LEU ARG GLU VAL LEU SER SER ARG VAL THR THR
SEQRES 44 A 720 THR PHE LYS SER ASN LEU THR SER LEU ASN PRO THR LEU
SEQRES 45 A 720 ALA ASN ALA ASP TRP ILE GLY LYS THR GLY THR THR ASN
SEQRES 46 A 720 GLN ASP GLU ASN MET TRP LEU MET LEU SER THR PRO ARG
SEQRES 47 A 720 LEU THR LEU GLY GLY TRP ILE GLY HIS ASP ASP ASN HIS
SEQRES 48 A 720 SER LEU SER GLN GLN ALA GLY TYR SER ASN ASN SER ASN
SEQRES 49 A 720 TYR MET ALA HIS LEU VAL ASN ALA ILE GLN GLN ALA SER
SEQRES 50 A 720 PRO SER ILE TRP GLY ASN GLU ARG PHE ALA LEU ASP PRO
SEQRES 51 A 720 SER VAL VAL LYS SER GLU VAL LEU LYS SER THR GLY GLN
SEQRES 52 A 720 LYS PRO GLY LYS VAL SER VAL GLU GLY LYS GLU VAL GLU
SEQRES 53 A 720 VAL THR GLY SER THR VAL THR SER TYR TRP ALA ASN LYS
SEQRES 54 A 720 SER GLY ALA PRO ALA THR SER TYR ARG PHE ALA ILE GLY
SEQRES 55 A 720 GLY SER ASP ALA ASP TYR GLN ASN ALA TRP SER SER ILE
SEQRES 56 A 720 VAL GLY SER LEU PRO
SEQRES 1 B 720 GLY SER GLY ILE ALA LEU GLY TYR GLY VAL ALA LEU PHE
SEQRES 2 B 720 ASP LYS VAL ARG VAL PRO GLN THR GLU GLU LEU VAL ASN
SEQRES 3 B 720 GLN VAL LYS ASP ILE SER SER ILE SER GLU ILE THR TYR
SEQRES 4 B 720 SER ASP GLY THR VAL ILE ALA SER ILE GLU SER ASP MET
SEQRES 5 B 720 LEU ARG THR SER ILE SER SER GLU GLN ILE SER GLU ASN
SEQRES 6 B 720 LEU LYS LYS ALA ILE ILE ALA THR GLU ASP GLU HIS PHE
SEQRES 7 B 720 LYS GLU HIS LYS GLY VAL VAL PRO ASN ALA VAL ILE PRO
SEQRES 8 B 720 ALA THR LEU GLY LYS PHE VAL GLY LEU GLY SER SER SER
SEQRES 9 B 720 GLY GLY SER THR LEU THR GLN GLN LEU ILE LYS GLN GLN
SEQRES 10 B 720 VAL VAL GLY ASP ALA PRO THR LEU ALA ARG LYS ALA ALA
SEQRES 11 B 720 GLU ILE VAL ASP ALA LEU ALA LEU GLU ARG ALA MET ASN
SEQRES 12 B 720 LYS ASP GLU ILE LEU THR THR TYR LEU ASN VAL ALA PRO
SEQRES 13 B 720 PHE GLY ARG ASN ASN LYS GLY GLN ASN ILE ALA GLY ALA
SEQRES 14 B 720 ARG GLN ALA ALA GLU GLY ILE PHE GLY VAL ASP ALA SER
SEQRES 15 B 720 GLN LEU THR VAL PRO GLN ALA ALA PHE LEU ALA GLY LEU
SEQRES 16 B 720 PRO GLN SER PRO ILE THR TYR SER PRO TYR GLU ASN THR
SEQRES 17 B 720 GLY GLU LEU LYS SER ASP GLU ASP LEU GLU ILE GLY LEU
SEQRES 18 B 720 ARG ARG ALA LYS ALA VAL LEU TYR SER MET TYR ARG THR
SEQRES 19 B 720 GLY ALA LEU SER LYS ASP GLU TYR SER GLN TYR LYS ASP
SEQRES 20 B 720 TYR ASP LEU LYS GLN ASP PHE LEU PRO SER GLY THR VAL
SEQRES 21 B 720 THR GLY ILE SER GLN ASP TYR LEU TYR PHE THR THR LEU
SEQRES 22 B 720 ALA GLU ALA GLN GLU ARG MET TYR ASP TYR LEU ALA GLN
SEQRES 23 B 720 ARG ASP ASN VAL SER ALA LYS GLU LEU LYS ASN GLU ALA
SEQRES 24 B 720 THR GLN LYS PHE TYR ARG ASP LEU ALA ALA LYS GLU ILE
SEQRES 25 B 720 GLU ASN GLY GLY TYR LYS ILE THR THR THR ILE ASP GLN
SEQRES 26 B 720 LYS ILE HIS SER ALA MET GLN SER ALA VAL ALA ASP TYR
SEQRES 27 B 720 GLY TYR LEU LEU ASP ASP GLY THR GLY ARG VAL GLU VAL
SEQRES 28 B 720 GLY ASN VAL LEU MET ASP ASN GLN THR GLY ALA ILE LEU
SEQRES 29 B 720 GLY PHE VAL GLY GLY ARG ASN TYR GLN GLU ASN GLN ASN
SEQRES 30 B 720 ASN HIS ALA PHE ASP THR LYS ARG SER PRO ALA SER THR
SEQRES 31 B 720 THR LYS PRO LEU LEU ALA TYR GLY ILE ALA ILE ASP GLN
SEQRES 32 B 720 GLY LEU MET GLY SER GLU THR ILE LEU SER ASN TYR PRO
SEQRES 33 B 720 THR ASN PHE ALA ASN GLY ASN PRO ILE MET TYR ALA ASN
SEQRES 34 B 720 SER LYS GLY THR GLY MET MET THR LEU GLY GLU ALA LEU
SEQRES 35 B 720 ASN TYR SER TRP ASN ILE PRO ALA TYR TRP THR TYR ARG
SEQRES 36 B 720 MET LEU ARG GLU ASN GLY VAL ASP VAL LYS GLY TYR MET
SEQRES 37 B 720 GLU LYS MET GLY TYR GLU ILE PRO GLU TYR GLY ILE GLU
SEQRES 38 B 720 SER LEU PRO MET GLY GLY GLY ILE GLU VAL THR VAL ALA
SEQRES 39 B 720 GLN HIS THR ASN GLY TYR GLN THR LEU ALA ASN ASN GLY
SEQRES 40 B 720 VAL TYR HIS GLN LYS HIS VAL ILE SER LYS ILE GLU ALA
SEQRES 41 B 720 ALA ASP GLY ARG VAL VAL TYR GLU TYR GLN ASP LYS PRO
SEQRES 42 B 720 VAL GLN VAL TYR SER LYS ALA THR ALA THR ILE MET GLN
SEQRES 43 B 720 GLY LEU LEU ARG GLU VAL LEU SER SER ARG VAL THR THR
SEQRES 44 B 720 THR PHE LYS SER ASN LEU THR SER LEU ASN PRO THR LEU
SEQRES 45 B 720 ALA ASN ALA ASP TRP ILE GLY LYS THR GLY THR THR ASN
SEQRES 46 B 720 GLN ASP GLU ASN MET TRP LEU MET LEU SER THR PRO ARG
SEQRES 47 B 720 LEU THR LEU GLY GLY TRP ILE GLY HIS ASP ASP ASN HIS
SEQRES 48 B 720 SER LEU SER GLN GLN ALA GLY TYR SER ASN ASN SER ASN
SEQRES 49 B 720 TYR MET ALA HIS LEU VAL ASN ALA ILE GLN GLN ALA SER
SEQRES 50 B 720 PRO SER ILE TRP GLY ASN GLU ARG PHE ALA LEU ASP PRO
SEQRES 51 B 720 SER VAL VAL LYS SER GLU VAL LEU LYS SER THR GLY GLN
SEQRES 52 B 720 LYS PRO GLY LYS VAL SER VAL GLU GLY LYS GLU VAL GLU
SEQRES 53 B 720 VAL THR GLY SER THR VAL THR SER TYR TRP ALA ASN LYS
SEQRES 54 B 720 SER GLY ALA PRO ALA THR SER TYR ARG PHE ALA ILE GLY
SEQRES 55 B 720 GLY SER ASP ALA ASP TYR GLN ASN ALA TRP SER SER ILE
SEQRES 56 B 720 VAL GLY SER LEU PRO
HET L4C A1789 19
HET SO4 A1790 5
HET CL A1791 1
HET CL A1792 1
HET L4C B1789 19
HET SO4 B1790 5
HET CL B1791 1
HET CL B1792 1
HETNAM L4C (2E)-2-{[(2S)-2-(ACETYLAMINO)-2-
HETNAM 2 L4C CARBOXYETHOXY]IMINO}PENTANEDIOIC ACID
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN L4C LACTIVICIN
FORMUL 3 L4C 2(C10 H14 N2 O8)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 CL 4(CL 1-)
FORMUL 11 HOH *79(H2 O)
HELIX 1 1 ASP A 337 ASP A 359 1 23
HELIX 2 2 ASN A 368 GLY A 386 1 19
HELIX 3 3 ASP A 395 GLY A 410 1 16
HELIX 4 4 TYR A 411 ASP A 414 5 4
HELIX 5 5 ASN A 442 ASN A 446 5 5
HELIX 6 6 PRO A 458 SER A 460 5 3
HELIX 7 7 THR A 461 ALA A 467 1 7
HELIX 8 8 ALA A 467 GLN A 474 1 8
HELIX 9 9 LEU A 509 SER A 516 1 8
HELIX 10 10 ASN A 518 ASN A 531 1 14
HELIX 11 11 ASP A 534 MET A 542 1 9
HELIX 12 12 SER A 553 GLY A 557 5 5
HELIX 13 13 THR A 563 ASN A 576 1 14
HELIX 14 14 SER A 609 ARG A 627 1 19
HELIX 15 15 THR A 631 ASN A 640 1 10
HELIX 16 16 ASN A 640 ASN A 645 1 6
HELIX 17 17 ASN A 656 GLU A 659 5 4
HELIX 18 18 SER A 691 SER A 708 1 18
HELIX 19 19 SER A 775 SER A 784 1 10
HELIX 20 20 ASP B 337 ASP B 359 1 23
HELIX 21 21 SER B 362 LYS B 367 1 6
HELIX 22 22 ASN B 368 GLY B 386 1 19
HELIX 23 23 ASP B 395 GLY B 410 1 16
HELIX 24 24 TYR B 411 ASP B 414 5 4
HELIX 25 25 PRO B 458 THR B 461 5 4
HELIX 26 26 THR B 462 ALA B 467 1 6
HELIX 27 27 ALA B 467 GLN B 474 1 8
HELIX 28 28 LEU B 509 SER B 516 1 8
HELIX 29 29 ASN B 518 ASN B 531 1 14
HELIX 30 30 ASP B 534 MET B 542 1 9
HELIX 31 31 THR B 563 ASN B 576 1 14
HELIX 32 32 SER B 609 ARG B 627 1 19
HELIX 33 33 THR B 631 ASN B 640 1 10
HELIX 34 34 ASN B 640 ASN B 645 1 6
HELIX 35 35 ASN B 656 GLU B 659 5 4
HELIX 36 36 SER B 691 SER B 708 1 18
HELIX 37 37 SER B 775 ALA B 782 1 8
SHEET 1 AA 4 GLU A 107 THR A 109 0
SHEET 2 AA 4 LYS A 389 THR A 392 1 O ILE A 390 N THR A 109
SHEET 3 AA 4 ILE A 586 GLU A 590 -1 N SER A 587 O THR A 391
SHEET 4 AA 4 VAL A 596 GLU A 599 -1 N VAL A 597 O ILE A 589
SHEET 1 AB 5 ILE A 434 VAL A 438 0
SHEET 2 AB 5 GLU A 421 ASP A 428 -1 O ASN A 424 N VAL A 438
SHEET 3 AB 5 LEU A 670 GLY A 677 -1 O THR A 671 N MET A 427
SHEET 4 AB 5 MET A 661 SER A 666 -1 O MET A 661 N ILE A 676
SHEET 5 AB 5 ILE A 649 THR A 654 -1 O ILE A 649 N SER A 666
SHEET 1 AC 2 ILE A 482 SER A 484 0
SHEET 2 AC 2 MET A 506 THR A 508 -1 O MET A 507 N LEU A 483
SHEET 1 AD 2 VAL A 579 TYR A 580 0
SHEET 2 AD 2 VAL A 605 GLN A 606 -1 O VAL A 605 N TYR A 580
SHEET 1 AE 2 VAL A 724 LEU A 729 0
SHEET 2 AE 2 THR A 752 TRP A 757 -1 O VAL A 753 N VAL A 728
SHEET 1 AF 2 LYS A 738 VAL A 739 0
SHEET 2 AF 2 VAL A 746 GLU A 747 -1 O VAL A 746 N VAL A 739
SHEET 1 BA 4 GLU B 107 THR B 109 0
SHEET 2 BA 4 LYS B 389 THR B 392 1 O ILE B 390 N THR B 109
SHEET 3 BA 4 ILE B 586 GLU B 590 -1 N SER B 587 O THR B 391
SHEET 4 BA 4 VAL B 596 GLU B 599 -1 N VAL B 597 O ILE B 589
SHEET 1 BB 5 ILE B 434 VAL B 438 0
SHEET 2 BB 5 GLU B 421 ASP B 428 -1 O ASN B 424 N VAL B 438
SHEET 3 BB 5 LEU B 670 GLY B 677 -1 O THR B 671 N MET B 427
SHEET 4 BB 5 MET B 661 SER B 666 -1 O MET B 661 N ILE B 676
SHEET 5 BB 5 ILE B 649 THR B 654 -1 O ILE B 649 N SER B 666
SHEET 1 BC 2 ILE B 482 SER B 484 0
SHEET 2 BC 2 MET B 506 THR B 508 -1 O MET B 507 N LEU B 483
SHEET 1 BD 2 VAL B 579 TYR B 580 0
SHEET 2 BD 2 VAL B 605 GLN B 606 -1 O VAL B 605 N TYR B 580
SHEET 1 BE 2 VAL B 724 LEU B 729 0
SHEET 2 BE 2 THR B 752 TRP B 757 -1 O VAL B 753 N VAL B 728
SHEET 1 BF 2 LYS B 738 VAL B 739 0
SHEET 2 BF 2 VAL B 746 GLU B 747 -1 O VAL B 746 N VAL B 739
LINK OG SER A 460 C4 L4C A1789 1555 1555 1.42
LINK OG SER B 460 C4 L4C B1789 1555 1555 1.42
CISPEP 1 VAL B 787 GLY B 788 0 14.25
SITE 1 AC1 10 ALA A 459 SER A 460 TYR A 498 SER A 516
SITE 2 AC1 10 ASN A 518 THR A 652 GLY A 653 THR A 654
SITE 3 AC1 10 ASN A 656 HOH A2036
SITE 1 AC2 10 ALA B 459 SER B 460 TYR B 498 SER B 516
SITE 2 AC2 10 ASN B 518 THR B 652 GLY B 653 THR B 654
SITE 3 AC2 10 ASN B 656 HOH B2042
SITE 1 AC3 3 THR B 563 LYS B 583 HOH B2043
SITE 1 AC4 2 THR A 563 LYS A 583
SITE 1 AC5 3 THR A 631 SER A 634 SER B 634
SITE 1 AC6 2 ARG A 627 LYS A 633
SITE 1 AC7 2 ARG B 627 LYS B 633
SITE 1 AC8 2 VAL B 585 ILE B 586
CRYST1 98.540 99.830 152.160 90.00 90.00 90.00 P 21 21 21 8
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 0.010148 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010017 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006572 0.00000
MTRIX1 1 -0.035000 -0.962000 0.270000 1.27003 1
MTRIX2 1 0.989000 -0.071000 -0.126000 0.49157 1
MTRIX3 1 0.141000 0.263000 0.954000 0.10928 1
(ATOM LINES ARE NOT SHOWN.)
END
