REMARK 2 REMARK 2 RESOLUTION. 2.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0003 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 16037 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 847 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) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1137 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3710 REMARK 3 BIN FREE R VALUE SET COUNT : 63 REMARK 3 BIN FREE R VALUE : 0.3770 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3597 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.04 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -6.02000 REMARK 3 B22 (A**2) : -6.02000 REMARK 3 B33 (A**2) : 9.02000 REMARK 3 B12 (A**2) : -3.01000 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): 0.948 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.390 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.328 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.716 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3713 ; 0.024 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5056 ; 2.386 ; 1.953 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 470 ; 9.908 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;39.189 ;23.793 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 589 ;25.326 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;25.941 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 559 ; 0.146 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2807 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1669 ; 0.288 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2485 ; 0.336 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 142 ; 0.235 ; 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): 31 ; 0.250 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.340 ; 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): 2423 ; 1.745 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3836 ; 3.059 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1514 ; 2.614 ; 3.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1220 ; 3.714 ; 4.000 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 REMARK 3 RIDING POSITIONS. FAB LIGHT AND HEAVY CHAIN ARE NUMBERED REMARK 3 ACCORDING TO THE KABAT CONVENTION. ANTIGENS RESIDUES A303 TO REMARK 3 A477 AND A513 TO A545 ARE DISORDERED IN THE CRYSTAL STRUCTURE REMARK 4 REMARK 4 2J5L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-06. REMARK 100 THE PDBE ID CODE IS EBI-29928. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.60 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) : 0.949 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18102 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 21.200 REMARK 200 R MERGE (I) : 0.25000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4 REMARK 200 DATA REDUNDANCY IN SHELL : 16.20 REMARK 200 R MERGE FOR SHELL (I) : 1.16000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.700 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 2J4W REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION TRIALS WERE REMARK 280 CARRIED OUT WITH PFAMA1 ECTOPLASMIC CONSTRUCTION REMARK 280 CORRESPONDING TO DOMAINS II-III. THE FAB FRAGMENT WAS REMARK 280 INCUBATED IN SMALL STOICHIOMETRIC EXCESS WITH THE REMARK 280 RECOMBINANT PROTEIN (1.2:1) BEFORE ADDING CRYSTALLISATION REMARK 280 BUFFERS. CRYSTALLISATION DROPS WERE PREPARED BY MIXING REMARK 280 0.8 MICROL OF PROTEIN WITH 0.8 MICROL OF RESERVOIR BUFFER REMARK 280 COMPRISING 12% PEG 6000 AND 0.1 M SODIUM ACETATE AT PH 4.6. REMARK 280 THE FINAL PROTEIN CONCENTRATION WAS 3.2 MG/ML. CRYSTALS REMARK 280 APPEARED AFTER 5 DAYS AT 17 DEGREE C. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.10000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.10000 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 22.10000 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 GENERATING THE BIOMOLECULE 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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, ASN 162 TO LYS REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 288 TO VAL REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 373 TO ASP REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 422 TO SER REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 423 TO LYS REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 499 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 GLN A 33 REMARK 465 LYS A 34 REMARK 465 SER A 35 REMARK 465 ASP A 36 REMARK 465 VAL A 37 REMARK 465 TYR A 38 REMARK 465 HIS A 39 REMARK 465 PRO A 40 REMARK 465 ILE A 41 REMARK 465 ASN A 42 REMARK 465 GLU A 43 REMARK 465 HIS A 44 REMARK 465 ARG A 45 REMARK 465 GLU A 46 REMARK 465 HIS A 47 REMARK 465 PRO A 48 REMARK 465 LYS A 49 REMARK 465 GLU A 50 REMARK 465 TYR A 51 REMARK 465 GLU A 52 REMARK 465 TYR A 53 REMARK 465 PRO A 54 REMARK 465 LEU A 55 REMARK 465 HIS A 56 REMARK 465 GLN A 57 REMARK 465 GLU A 58 REMARK 465 HIS A 59 REMARK 465 THR A 60 REMARK 465 TYR A 61 REMARK 465 GLN A 62 REMARK 465 GLN A 63 REMARK 465 GLU A 64 REMARK 465 ASP A 65 REMARK 465 SER A 66 REMARK 465 GLY A 67 REMARK 465 GLU A 68 REMARK 465 ASP A 69 REMARK 465 GLU A 70 REMARK 465 ASN A 71 REMARK 465 THR A 72 REMARK 465 LEU A 73 REMARK 465 GLN A 74 REMARK 465 HIS A 75 REMARK 465 ALA A 76 REMARK 465 TYR A 77 REMARK 465 PRO A 78 REMARK 465 ILE A 79 REMARK 465 ASP A 80 REMARK 465 HIS A 81 REMARK 465 GLU A 82 REMARK 465 GLY A 83 REMARK 465 ALA A 84 REMARK 465 GLU A 85 REMARK 465 PRO A 86 REMARK 465 ALA A 87 REMARK 465 PRO A 88 REMARK 465 GLN A 89 REMARK 465 GLU A 90 REMARK 465 GLN A 91 REMARK 465 ASN A 92 REMARK 465 LEU A 93 REMARK 465 PHE A 94 REMARK 465 SER A 95 REMARK 465 SER A 96 REMARK 465 ILE A 97 REMARK 465 GLU A 98 REMARK 465 ILE A 99 REMARK 465 VAL A 100 REMARK 465 GLU A 101 REMARK 465 ARG A 102 REMARK 465 SER A 103 REMARK 465 ASN A 104 REMARK 465 TYR A 105 REMARK 465 MET A 106 REMARK 465 GLY A 107 REMARK 465 ASN A 108 REMARK 465 PRO A 109 REMARK 465 TRP A 110 REMARK 465 THR A 111 REMARK 465 GLU A 112 REMARK 465 TYR A 113 REMARK 465 MET A 114 REMARK 465 ALA A 115 REMARK 465 LYS A 116 REMARK 465 TYR A 117 REMARK 465 ASP A 118 REMARK 465 ILE A 119 REMARK 465 GLU A 120 REMARK 465 GLU A 121 REMARK 465 VAL A 122 REMARK 465 HIS A 123 REMARK 465 GLY A 124 REMARK 465 SER A 125 REMARK 465 GLY A 126 REMARK 465 ILE A 127 REMARK 465 ARG A 128 REMARK 465 VAL A 129 REMARK 465 ASP A 130 REMARK 465 LEU A 131 REMARK 465 GLY A 132 REMARK 465 GLU A 133 REMARK 465 ASP A 134 REMARK 465 ALA A 135 REMARK 465 GLU A 136 REMARK 465 VAL A 137 REMARK 465 ALA A 138 REMARK 465 GLY A 139 REMARK 465 THR A 140 REMARK 465 GLN A 141 REMARK 465 TYR A 142 REMARK 465 ARG A 143 REMARK 465 LEU A 144 REMARK 465 PRO A 145 REMARK 465 SER A 146 REMARK 465 GLY A 147 REMARK 465 LYS A 148 REMARK 465 CYS A 149 REMARK 465 PRO A 150 REMARK 465 VAL A 151 REMARK 465 PHE A 152 REMARK 465 GLY A 153 REMARK 465 LYS A 154 REMARK 465 GLY A 155 REMARK 465 ILE A 156 REMARK 465 ILE A 157 REMARK 465 ILE A 158 REMARK 465 GLU A 159 REMARK 465 ASN A 160 REMARK 465 SER A 161 REMARK 465 ASN A 162 REMARK 465 THR A 163 REMARK 465 THR A 164 REMARK 465 PHE A 165 REMARK 465 LEU A 166 REMARK 465 LYS A 167 REMARK 465 PRO A 168 REMARK 465 VAL A 169 REMARK 465 ALA A 170 REMARK 465 THR A 171 REMARK 465 GLY A 172 REMARK 465 ASN A 173 REMARK 465 GLN A 174 REMARK 465 ASP A 175 REMARK 465 LEU A 176 REMARK 465 LYS A 177 REMARK 465 ASP A 178 REMARK 465 GLY A 179 REMARK 465 GLY A 180 REMARK 465 PHE A 181 REMARK 465 ALA A 182 REMARK 465 PHE A 183 REMARK 465 PRO A 184 REMARK 465 PRO A 185 REMARK 465 THR A 186 REMARK 465 ASN A 187 REMARK 465 PRO A 188 REMARK 465 LEU A 189 REMARK 465 ILE A 190 REMARK 465 SER A 191 REMARK 465 PRO A 192 REMARK 465 MET A 193 REMARK 465 THR A 194 REMARK 465 LEU A 195 REMARK 465 ASN A 196 REMARK 465 GLY A 197 REMARK 465 MET A 198 REMARK 465 ARG A 199 REMARK 465 ASP A 200 REMARK 465 PHE A 201 REMARK 465 TYR A 202 REMARK 465 LYS A 203 REMARK 465 ASN A 204 REMARK 465 ASN A 205 REMARK 465 GLU A 206 REMARK 465 TYR A 207 REMARK 465 VAL A 208 REMARK 465 LYS A 209 REMARK 465 ASN A 210 REMARK 465 LEU A 211 REMARK 465 ASP A 212 REMARK 465 GLU A 213 REMARK 465 LEU A 214 REMARK 465 THR A 215 REMARK 465 LEU A 216 REMARK 465 CYS A 217 REMARK 465 SER A 218 REMARK 465 ARG A 219 REMARK 465 HIS A 220 REMARK 465 ALA A 221 REMARK 465 GLY A 222 REMARK 465 ASN A 223 REMARK 465 MET A 224 REMARK 465 ASN A 225 REMARK 465 PRO A 226 REMARK 465 ASP A 227 REMARK 465 ASN A 228 REMARK 465 ASP A 229 REMARK 465 LYS A 230 REMARK 465 ASN A 231 REMARK 465 SER A 232 REMARK 465 ASN A 233 REMARK 465 TYR A 234 REMARK 465 LYS A 235 REMARK 465 TYR A 236 REMARK 465 PRO A 237 REMARK 465 ALA A 238 REMARK 465 VAL A 239 REMARK 465 TYR A 240 REMARK 465 ASP A 241 REMARK 465 TYR A 242 REMARK 465 ASN A 243 REMARK 465 ASP A 244 REMARK 465 LYS A 245 REMARK 465 LYS A 246 REMARK 465 CYS A 247 REMARK 465 HIS A 248 REMARK 465 ILE A 249 REMARK 465 LEU A 250 REMARK 465 TYR A 251 REMARK 465 ILE A 252 REMARK 465 ALA A 253 REMARK 465 ALA A 254 REMARK 465 GLN A 255 REMARK 465 GLU A 256 REMARK 465 ASN A 257 REMARK 465 ASN A 258 REMARK 465 GLY A 259 REMARK 465 PRO A 260 REMARK 465 ARG A 261 REMARK 465 TYR A 262 REMARK 465 CYS A 263 REMARK 465 ASN A 264 REMARK 465 LYS A 265 REMARK 465 ASP A 266 REMARK 465 GLN A 267 REMARK 465 SER A 268 REMARK 465 LYS A 269 REMARK 465 ARG A 270 REMARK 465 ASN A 271 REMARK 465 SER A 272 REMARK 465 MET A 273 REMARK 465 PHE A 274 REMARK 465 CYS A 275 REMARK 465 PHE A 276 REMARK 465 ARG A 277 REMARK 465 PRO A 278 REMARK 465 ALA A 279 REMARK 465 LYS A 280 REMARK 465 ASP A 281 REMARK 465 LYS A 282 REMARK 465 LEU A 283 REMARK 465 PHE A 284 REMARK 465 GLU A 285 REMARK 465 ASN A 286 REMARK 465 TYR A 287 REMARK 465 THR A 288 REMARK 465 TYR A 289 REMARK 465 LEU A 290 REMARK 465 SER A 291 REMARK 465 LYS A 292 REMARK 465 ASN A 293 REMARK 465 VAL A 294 REMARK 465 VAL A 295 REMARK 465 ASP A 296 REMARK 465 ASN A 297 REMARK 465 TRP A 298 REMARK 465 GLU A 299 REMARK 465 GLU A 300 REMARK 465 VAL A 301 REMARK 465 CYS A 302 REMARK 465 PRO A 303 REMARK 465 ARG A 304 REMARK 465 LYS A 305 REMARK 465 ASN A 306 REMARK 465 LEU A 307 REMARK 465 GLU A 308 REMARK 465 ASN A 309 REMARK 465 ALA A 310 REMARK 465 LYS A 311 REMARK 465 PHE A 312 REMARK 465 GLY A 313 REMARK 465 LEU A 314 REMARK 465 TRP A 315 REMARK 465 VAL A 316 REMARK 465 ASP A 317 REMARK 465 GLY A 318 REMARK 465 ASN A 319 REMARK 465 CYS A 320 REMARK 465 GLU A 321 REMARK 465 ASP A 322 REMARK 465 ILE A 323 REMARK 465 PRO A 324 REMARK 465 HIS A 325 REMARK 465 VAL A 326 REMARK 465 ASN A 327 REMARK 465 GLU A 328 REMARK 465 PHE A 329 REMARK 465 SER A 330 REMARK 465 ALA A 331 REMARK 465 ASN A 332 REMARK 465 ASP A 333 REMARK 465 LEU A 334 REMARK 465 PHE A 335 REMARK 465 GLU A 336 REMARK 465 CYS A 337 REMARK 465 ASN A 338 REMARK 465 LYS A 339 REMARK 465 LEU A 340 REMARK 465 VAL A 341 REMARK 465 PHE A 342 REMARK 465 GLU A 343 REMARK 465 LEU A 344 REMARK 465 SER A 345 REMARK 465 ALA A 346 REMARK 465 SER A 347 REMARK 465 ASP A 348 REMARK 465 GLN A 349 REMARK 465 PRO A 350 REMARK 465 LYS A 351 REMARK 465 GLN A 352 REMARK 465 TYR A 353 REMARK 465 GLU A 354 REMARK 465 GLN A 355 REMARK 465 HIS A 356 REMARK 465 LEU A 357 REMARK 465 THR A 358 REMARK 465 ASP A 359 REMARK 465 TYR A 360 REMARK 465 GLU A 361 REMARK 465 LYS A 362 REMARK 465 ILE A 363 REMARK 465 LYS A 364 REMARK 465 GLU A 365 REMARK 465 GLY A 366 REMARK 465 PHE A 367 REMARK 465 LYS A 368 REMARK 465 ASN A 369 REMARK 465 LYS A 370 REMARK 465 ASN A 371 REMARK 465 ALA A 372 REMARK 465 SER A 373 REMARK 465 MET A 374 REMARK 465 ILE A 375 REMARK 465 LYS A 376 REMARK 465 SER A 377 REMARK 465 ALA A 378 REMARK 465 PHE A 379 REMARK 465 LEU A 380 REMARK 465 PRO A 381 REMARK 465 THR A 382 REMARK 465 GLY A 383 REMARK 465 ALA A 384 REMARK 465 PHE A 385 REMARK 465 LYS A 386 REMARK 465 ALA A 387 REMARK 465 ASP A 388 REMARK 465 ARG A 389 REMARK 465 TYR A 390 REMARK 465 LYS A 391 REMARK 465 SER A 392 REMARK 465 HIS A 393 REMARK 465 GLY A 394 REMARK 465 LYS A 395 REMARK 465 GLY A 396 REMARK 465 TYR A 397 REMARK 465 ASN A 398 REMARK 465 TRP A 399 REMARK 465 GLY A 400 REMARK 465 ASN A 401 REMARK 465 TYR A 402 REMARK 465 ASN A 403 REMARK 465 ARG A 404 REMARK 465 GLU A 405 REMARK 465 THR A 406 REMARK 465 GLN A 407 REMARK 465 LYS A 408 REMARK 465 CYS A 409 REMARK 465 GLU A 410 REMARK 465 ILE A 411 REMARK 465 PHE A 412 REMARK 465 ASN A 413 REMARK 465 VAL A 414 REMARK 465 LYS A 415 REMARK 465 PRO A 416 REMARK 465 THR A 417 REMARK 465 CYS A 418 REMARK 465 LEU A 419 REMARK 465 ILE A 420 REMARK 465 ASN A 421 REMARK 465 ASN A 422 REMARK 465 SER A 423 REMARK 465 SER A 424 REMARK 465 TYR A 425 REMARK 465 ILE A 426 REMARK 465 ALA A 427 REMARK 465 THR A 428 REMARK 465 THR A 429 REMARK 465 ALA A 430 REMARK 465 LEU A 431 REMARK 465 SER A 432 REMARK 465 HIS A 433 REMARK 465 PRO A 434 REMARK 465 ILE A 435 REMARK 465 GLU A 436 REMARK 465 VAL A 437 REMARK 465 GLU A 438 REMARK 465 HIS A 439 REMARK 465 ASN A 440 REMARK 465 PHE A 441 REMARK 465 PRO A 442 REMARK 465 CYS A 443 REMARK 465 SER A 444 REMARK 465 LEU A 445 REMARK 465 TYR A 446 REMARK 465 LYS A 447 REMARK 465 ASP A 448 REMARK 465 GLU A 449 REMARK 465 ILE A 450 REMARK 465 LYS A 451 REMARK 465 LYS A 452 REMARK 465 GLU A 453 REMARK 465 ILE A 454 REMARK 465 GLU A 455 REMARK 465 ARG A 456 REMARK 465 GLU A 457 REMARK 465 SER A 458 REMARK 465 LYS A 459 REMARK 465 ARG A 460 REMARK 465 ILE A 461 REMARK 465 LYS A 462 REMARK 465 LEU A 463 REMARK 465 ASN A 464 REMARK 465 ASP A 465 REMARK 465 ASN A 466 REMARK 465 ASP A 467 REMARK 465 ASP A 468 REMARK 465 GLU A 469 REMARK 465 GLY A 470 REMARK 465 ASN A 471 REMARK 465 LYS A 472 REMARK 465 LYS A 473 REMARK 465 ILE A 474 REMARK 465 ILE A 475 REMARK 465 ALA A 476 REMARK 465 PRO A 477 REMARK 465 ARG A 478 REMARK 465 ARG A 513 REMARK 465 ALA A 514 REMARK 465 GLU A 515 REMARK 465 VAL A 516 REMARK 465 THR A 517 REMARK 465 SER A 518 REMARK 465 ASN A 519 REMARK 465 ASN A 520 REMARK 465 GLU A 521 REMARK 465 VAL A 522 REMARK 465 VAL A 523 REMARK 465 VAL A 524 REMARK 465 LYS A 525 REMARK 465 GLU A 526 REMARK 465 GLU A 527 REMARK 465 TYR A 528 REMARK 465 LYS A 529 REMARK 465 ASP A 530 REMARK 465 GLU A 531 REMARK 465 TYR A 532 REMARK 465 ALA A 533 REMARK 465 ASP A 534 REMARK 465 ILE A 535 REMARK 465 PRO A 536 REMARK 465 GLU A 537 REMARK 465 HIS A 538 REMARK 465 LYS A 539 REMARK 465 PRO A 540 REMARK 465 THR A 541 REMARK 465 TYR A 542 REMARK 465 ASP A 543 REMARK 465 ASN A 544 REMARK 465 MET A 545 REMARK 465 LYS A 546 REMARK 465 ILE A 547 REMARK 465 ILE A 548 REMARK 465 ILE A 549 REMARK 465 ALA A 550 REMARK 465 SER A 551 REMARK 465 SER A 552 REMARK 465 ALA A 553 REMARK 465 ALA A 554 REMARK 465 VAL A 555 REMARK 465 ALA A 556 REMARK 465 VAL A 557 REMARK 465 LEU A 558 REMARK 465 ALA A 559 REMARK 465 THR A 560 REMARK 465 ILE A 561 REMARK 465 LEU A 562 REMARK 465 MET A 563 REMARK 465 VAL A 564 REMARK 465 TYR A 565 REMARK 465 LEU A 566 REMARK 465 TYR A 567 REMARK 465 LYS A 568 REMARK 465 ARG A 569 REMARK 465 LYS A 570 REMARK 465 GLY A 571 REMARK 465 ASN A 572 REMARK 465 ALA A 573 REMARK 465 GLU A 574 REMARK 465 LYS A 575 REMARK 465 TYR A 576 REMARK 465 ASP A 577 REMARK 465 LYS A 578 REMARK 465 MET A 579 REMARK 465 ASP A 580 REMARK 465 GLN A 581 REMARK 465 PRO A 582 REMARK 465 GLN A 583 REMARK 465 HIS A 584 REMARK 465 TYR A 585 REMARK 465 GLY A 586 REMARK 465 LYS A 587 REMARK 465 SER A 588 REMARK 465 THR A 589 REMARK 465 SER A 590 REMARK 465 ARG A 591 REMARK 465 ASN A 592 REMARK 465 ASP A 593 REMARK 465 GLU A 594 REMARK 465 MET A 595 REMARK 465 LEU A 596 REMARK 465 ASP A 597 REMARK 465 PRO A 598 REMARK 465 GLU A 599 REMARK 465 ALA A 600 REMARK 465 SER A 601 REMARK 465 PHE A 602 REMARK 465 TRP A 603 REMARK 465 GLY A 604 REMARK 465 GLU A 605 REMARK 465 GLU A 606 REMARK 465 LYS A 607 REMARK 465 ARG A 608 REMARK 465 ALA A 609 REMARK 465 SER A 610 REMARK 465 HIS A 611 REMARK 465 THR A 612 REMARK 465 THR A 613 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 NH2 ARG B 61 - OE1 GLU B 81 2.13 REMARK 500 O ILE B 150 - O GLY B 152 2.17 REMARK 500 OE1 GLU C 6 - N GLY C 106 2.17 REMARK 500 O ASP C 61 - N VAL C 63 2.13 REMARK 500 O ASN C 162 - OG SER C 165 2.13 REMARK 500 O SER C 196 - OG SER C 202 2.00 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 TYR B 173 CD1 TYR B 173 CE1 0.164 REMARK 500 CYS C 208 CB CYS C 208 SG -0.096 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 LEU B 11 CA - CB - CG ANGL. DEV. = 16.1 DEGREES REMARK 500 LEU B 104 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES REMARK 500 CYS B 134 CB - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 CYS B 194 CB - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 PRO C 14 C - N - CA ANGL. DEV. = 10.9 DEGREES REMARK 500 LEU C 140 CA - CB - CG ANGL. DEV. = 14.3 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 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 LYS A 489 66.55 33.41 REMARK 500 GLN A 499 -129.44 -97.69 REMARK 500 SER A 500 -85.61 -70.58 REMARK 500 CYS A 502 114.66 154.66 REMARK 500 ARG A 503 -84.34 -105.04 REMARK 500 PHE A 504 139.58 59.15 REMARK 500 SER B 2 46.20 -89.96 REMARK 500 VAL B 3 120.34 -35.88 REMARK 500 SER B 29 151.28 -43.15 REMARK 500 TRP B 47 -65.67 -97.08 REMARK 500 THR B 51 -37.21 62.88 REMARK 500 SER B 52 14.22 -162.63 REMARK 500 SER B 76 -68.13 -17.43 REMARK 500 GLU B 79 -167.24 -103.20 REMARK 500 ALA B 84 164.89 174.29 REMARK 500 THR B 126 -53.10 -10.72 REMARK 500 ASN B 138 64.22 68.58 REMARK 500 SER B 153 83.33 -38.39 REMARK 500 LYS B 169 -37.73 -136.47 REMARK 500 THR B 182 170.88 -59.67 REMARK 500 ARG B 188 42.04 -63.52 REMARK 500 HIS B 189 118.40 -174.20 REMARK 500 PRO B 204 113.02 -31.34 REMARK 500 SER C 52 -163.03 -71.26 REMARK 500 SER C 55 55.84 75.83 REMARK 500 SER C 62 7.58 -46.52 REMARK 500 ARG C 66 -44.69 -139.69 REMARK 500 ASN C 76 76.27 38.38 REMARK 500 THR C 98 -77.00 -35.14 REMARK 500 THR C 116 105.23 -59.15 REMARK 500 SER C 128 -125.63 -43.99 REMARK 500 ALA C 129 -143.01 -75.18 REMARK 500 ALA C 130 58.90 72.78 REMARK 500 GLN C 133 -120.25 -98.69 REMARK 500 SER C 136 -26.42 77.16 REMARK 500 GLN C 179 -124.44 -116.96 REMARK 500 ASP C 183 21.61 37.23 REMARK 500 PRO C 198 2.91 -54.55 REMARK 500 SER C 216 83.01 28.99 REMARK 500 PRO C 227 155.79 -35.61 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 ILE B 75 SER B 76 141.01 REMARK 500 ASP B 170 SER B 171 -136.37 REMARK 500 SER C 215 SER C 216 -148.85 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASN B 190 21.9 L L OUTSIDE RANGE REMARK 500 ASN C 54 23.8 L L OUTSIDE RANGE REMARK 500 VAL C 109 22.6 L L OUTSIDE RANGE REMARK 500 CYS C 233 23.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED.