REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.56 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 32028 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) : 0.245 REMARK 3 R VALUE (WORKING SET) : 0.242 REMARK 3 FREE R VALUE : 0.299 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1708 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) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2341 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.43 REMARK 3 BIN R VALUE (WORKING SET) : 0.3420 REMARK 3 BIN FREE R VALUE SET COUNT : 111 REMARK 3 BIN FREE R VALUE : 0.3750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8359 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 173 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) : 47.91 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.79000 REMARK 3 B22 (A**2) : -0.38000 REMARK 3 B33 (A**2) : -0.22000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.21000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.504 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.437 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 53.668 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.875 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.820 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8726 ; 0.010 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11966 ; 1.333 ; 1.953 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1163 ; 7.040 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 317 ;35.604 ;24.795 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1061 ;19.885 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.970 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1413 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6675 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3955 ; 0.255 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5769 ; 0.316 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 331 ; 0.164 ; 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): 30 ; 0.303 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.124 ; 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): 5831 ; 0.432 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9213 ; 0.797 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2895 ; 0.729 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2753 ; 1.229 ; 4.500 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 3C09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JAN-08. REMARK 100 THE RCSB ID CODE IS RCSB046178. 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 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33886 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.11800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : 0.35400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: 1YY9, 3C08 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 1M NACL, PH 6.0, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 70.53650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 102.51750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.53650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 102.51750 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC 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 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 GLU L 212 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 LEU A 307 REMARK 465 GLU A 308 REMARK 465 GLU A 309 REMARK 465 SER A 501 REMARK 465 CYS A 502 REMARK 465 ARG A 503 REMARK 465 ASN A 504 REMARK 465 VAL A 505 REMARK 465 SER A 506 REMARK 465 ARG A 507 REMARK 465 GLY A 508 REMARK 465 ARG A 509 REMARK 465 GLU A 510 REMARK 465 CYS A 511 REMARK 465 VAL A 512 REMARK 465 ASP A 513 REMARK 465 LYS A 514 REMARK 465 HIS A 515 REMARK 465 HIS A 516 REMARK 465 HIS A 517 REMARK 465 HIS A 518 REMARK 465 HIS A 519 REMARK 465 HIS A 520 REMARK 465 LYS B 125 REMARK 465 SER B 126 REMARK 465 GLY B 127 REMARK 465 ALA B 143 REMARK 465 LYS B 144 REMARK 465 VAL B 145 REMARK 465 GLN B 146 REMARK 465 TRP B 147 REMARK 465 LYS B 148 REMARK 465 VAL B 149 REMARK 465 ASP B 150 REMARK 465 ASN B 151 REMARK 465 ALA B 152 REMARK 465 LEU B 153 REMARK 465 GLN B 154 REMARK 465 SER B 155 REMARK 465 LEU B 180 REMARK 465 SER B 181 REMARK 465 LYS B 182 REMARK 465 ALA B 183 REMARK 465 ASP B 184 REMARK 465 TYR B 185 REMARK 465 GLU B 186 REMARK 465 LYS B 187 REMARK 465 HIS B 188 REMARK 465 LYS B 189 REMARK 465 VAL B 190 REMARK 465 TYR B 191 REMARK 465 ALA B 192 REMARK 465 CYS B 193 REMARK 465 GLU B 194 REMARK 465 SER B 207 REMARK 465 PHE B 208 REMARK 465 ASN B 209 REMARK 465 ARG B 210 REMARK 465 GLY B 211 REMARK 465 GLU B 212 REMARK 465 VAL C 129 REMARK 465 PHE C 130 REMARK 465 PRO C 131 REMARK 465 LEU C 132 REMARK 465 ALA C 133 REMARK 465 PRO C 134 REMARK 465 SER C 135 REMARK 465 SER C 136 REMARK 465 LYS C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 THR C 143 REMARK 465 ALA C 144 REMARK 465 ALA C 145 REMARK 465 LEU C 146 REMARK 465 PRO C 193 REMARK 465 SER C 194 REMARK 465 SER C 195 REMARK 465 SER C 196 REMARK 465 LEU C 197 REMARK 465 GLY C 198 REMARK 465 THR C 199 REMARK 465 GLN C 200 REMARK 465 THR C 201 REMARK 465 VAL C 219 REMARK 465 GLU C 220 REMARK 465 PRO C 221 REMARK 465 LYS C 222 REMARK 465 SER C 223 REMARK 465 LEU D 307 REMARK 465 GLU D 308 REMARK 465 GLU D 309 REMARK 465 SER D 501 REMARK 465 CYS D 502 REMARK 465 ARG D 503 REMARK 465 ASN D 504 REMARK 465 VAL D 505 REMARK 465 SER D 506 REMARK 465 ARG D 507 REMARK 465 GLY D 508 REMARK 465 ARG D 509 REMARK 465 GLU D 510 REMARK 465 CYS D 511 REMARK 465 VAL D 512 REMARK 465 ASP D 513 REMARK 465 LYS D 514 REMARK 465 HIS D 515 REMARK 465 HIS D 516 REMARK 465 HIS D 517 REMARK 465 HIS D 518 REMARK 465 HIS D 519 REMARK 465 HIS D 520 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 ASP L 1 CG OD1 OD2 REMARK 470 ILE L 2 CG1 CG2 CD1 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 LYS L 41 CG CD CE NZ REMARK 470 SER L 66 OG REMARK 470 SER L 92 OG REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 ASP L 121 CG OD1 OD2 REMARK 470 GLU L 122 CG CD OE1 OE2 REMARK 470 LYS L 125 CG CD CE NZ REMARK 470 VAL L 131 CG1 CG2 REMARK 470 ARG L 141 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 142 CG CD OE1 OE2 REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 VAL L 145 CG1 CG2 REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 VAL L 149 CG1 CG2 REMARK 470 LEU L 153 CG CD1 CD2 REMARK 470 SER L 155 OG REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 SER L 170 OG REMARK 470 LYS L 182 CG CD CE NZ REMARK 470 LYS L 187 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 GLN L 198 CG CD OE1 NE2 REMARK 470 LEU L 200 CG CD1 CD2 REMARK 470 SER L 202 OG REMARK 470 LYS L 206 CG CD CE NZ REMARK 470 ASN L 209 CG OD1 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 LYS H 23 CG CD CE NZ REMARK 470 SER H 25 OG REMARK 470 THR H 30 OG1 CG2 REMARK 470 LYS H 63 CG CD CE NZ REMARK 470 LYS H 65 CG CD CE NZ REMARK 470 LYS H 67 CG CD CE NZ REMARK 470 SER H 75 OG REMARK 470 SER H 84 OG REMARK 470 SER H 85 OG REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 ARG H 106 CG CD NE CZ NH1 NH2 REMARK 470 SER H 121 OG REMARK 470 LYS H 125 CG CD CE NZ REMARK 470 SER H 128 OG REMARK 470 SER H 169 OG REMARK 470 SER H 195 OG REMARK 470 THR H 199 OG1 CG2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 LYS A 311 CG CD CE NZ REMARK 470 LYS A 322 CG CD CE NZ REMARK 470 LYS A 333 CG CD CE NZ REMARK 470 LYS A 336 CG CD CE NZ REMARK 470 LEU A 348 CG CD1 CD2 REMARK 470 ARG A 353 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 357 CG CD1 CD2 CE1 CE2 CZ REMARK 470 HIS A 359 CG ND1 CD2 CE1 NE2 REMARK 470 GLN A 366 CG CD OE1 NE2 REMARK 470 LYS A 372 CG CD CE NZ REMARK 470 LYS A 375 CG CD CE NZ REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 409 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 424 CG CD1 CD2 REMARK 470 LYS A 430 CG CD CE NZ REMARK 470 LYS A 443 CG CD CE NZ REMARK 470 LYS A 455 CG CD CE NZ REMARK 470 ARG A 470 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 472 CG CD OE1 OE2 REMARK 470 SER A 474 OG REMARK 470 LYS A 476 CG CD CE NZ REMARK 470 LEU A 485 CG CD1 CD2 REMARK 470 GLU A 489 CG CD OE1 OE2 REMARK 470 GLU A 495 CG CD OE1 OE2 REMARK 470 ASP B 1 CG OD1 OD2 REMARK 470 VAL B 29 CG1 CG2 REMARK 470 LYS B 41 CG CD CE NZ REMARK 470 LYS B 102 CG CD CE NZ REMARK 470 LYS B 106 CG CD CE NZ REMARK 470 ILE B 116 CG1 CG2 CD1 REMARK 470 PHE B 117 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER B 120 OG REMARK 470 ASP B 121 CG OD1 OD2 REMARK 470 GLU B 122 CG CD OE1 OE2 REMARK 470 GLN B 123 CG CD OE1 NE2 REMARK 470 LEU B 124 CG CD1 CD2 REMARK 470 THR B 128 OG1 CG2 REMARK 470 VAL B 131 CG1 CG2 REMARK 470 VAL B 132 CG1 CG2 REMARK 470 LEU B 134 CG CD1 CD2 REMARK 470 ARG B 141 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 142 CG CD OE1 OE2 REMARK 470 ASN B 157 CG OD1 REMARK 470 SER B 158 OG REMARK 470 GLN B 159 CG CD OE1 NE2 REMARK 470 LYS B 168 CG CD CE NZ REMARK 470 LEU B 174 CG CD1 CD2 REMARK 470 LEU B 178 CG CD1 CD2 REMARK 470 THR B 179 OG1 CG2 REMARK 470 VAL B 195 CG1 CG2 REMARK 470 THR B 196 OG1 CG2 REMARK 470 GLN B 198 CG CD OE1 NE2 REMARK 470 SER B 201 OG REMARK 470 SER B 202 OG REMARK 470 VAL B 204 CG1 CG2 REMARK 470 THR B 205 OG1 CG2 REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 LYS C 13 CG CD CE NZ REMARK 470 LYS C 19 CG CD CE NZ REMARK 470 LYS C 23 CG CD CE NZ REMARK 470 SER C 25 OG REMARK 470 THR C 30 OG1 CG2 REMARK 470 ARG C 57 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 62 CG CD OE1 OE2 REMARK 470 LYS C 63 CG CD CE NZ REMARK 470 LYS C 65 CG CD CE NZ REMARK 470 LYS C 67 CG CD CE NZ REMARK 470 SER C 84 OG REMARK 470 ARG C 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 89 CG CD OE1 OE2 REMARK 470 SER C 98 OG REMARK 470 ARG C 106 CG CD NE CZ NH1 NH2 REMARK 470 SER C 121 OG REMARK 470 LYS C 125 CG CD CE NZ REMARK 470 LEU C 149 CG CD1 CD2 REMARK 470 VAL C 150 CG1 CG2 REMARK 470 LYS C 151 CG CD CE NZ REMARK 470 VAL C 158 CG1 CG2 REMARK 470 SER C 161 OG REMARK 470 ASN C 163 CG OD1 REMARK 470 SER C 164 OG REMARK 470 THR C 168 OG1 CG2 REMARK 470 SER C 169 OG REMARK 470 SER C 180 OG REMARK 470 LEU C 183 CG CD1 CD2 REMARK 470 SER C 185 OG REMARK 470 LEU C 186 CG CD1 CD2 REMARK 470 VAL C 189 CG1 CG2 REMARK 470 VAL C 190 CG1 CG2 REMARK 470 TYR C 202 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE C 203 CG1 CG2 CD1 REMARK 470 ASN C 205 CG OD1 REMARK 470 VAL C 206 CG1 CG2 REMARK 470 LYS C 209 CG CD CE NZ REMARK 470 LYS C 214 CG CD CE NZ REMARK 470 VAL C 215 CG1 CG2 REMARK 470 LYS C 217 CG CD CE NZ REMARK 470 LYS C 218 CG CD CE NZ REMARK 470 LYS D 310 CG CD CE NZ REMARK 470 LYS D 311 CG CD CE NZ REMARK 470 VAL D 312 CG1 CG2 REMARK 470 LYS D 322 CG CD CE NZ REMARK 470 LEU D 325 CG CD1 CD2 REMARK 470 LYS D 333 CG CD CE NZ REMARK 470 LYS D 336 CG CD CE NZ REMARK 470 SER D 340 OG REMARK 470 ARG D 353 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 355 CG OD1 OD2 REMARK 470 PHE D 357 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU D 363 CG CD1 CD2 REMARK 470 GLN D 366 CG CD OE1 NE2 REMARK 470 LEU D 371 CG CD1 CD2 REMARK 470 LYS D 372 CG CD CE NZ REMARK 470 LYS D 375 CG CD CE NZ REMARK 470 GLU D 388 CG CD OE1 OE2 REMARK 470 ARG D 390 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 397 CG CD OE1 OE2 REMARK 470 ARG D 405 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 408 CG CD OE1 NE2 REMARK 470 GLN D 411 CG CD OE1 NE2 REMARK 470 ILE D 421 CG1 CG2 CD1 REMARK 470 SER D 423 OG REMARK 470 LEU D 424 CG CD1 CD2 REMARK 470 ARG D 427 CG CD NE CZ NH1 NH2 REMARK 470 SER D 428 OG REMARK 470 LYS D 430 CG CD CE NZ REMARK 470 LYS D 443 CG CD CE NZ REMARK 470 LEU D 445 CG CD1 CD2 REMARK 470 ILE D 451 CG1 CG2 CD1 REMARK 470 LYS D 455 CG CD CE NZ REMARK 470 LYS D 465 CG CD CE NZ REMARK 470 ILE D 466 CG1 CG2 CD1 REMARK 470 ILE D 467 CG1 CG2 CD1 REMARK 470 ARG D 470 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 472 CG CD OE1 OE2 REMARK 470 SER D 474 OG REMARK 470 LYS D 476 CG CD CE NZ REMARK 470 THR D 478 OG1 CG2 REMARK 470 VAL D 481 CG1 CG2 REMARK 470 HIS D 483 CG ND1 CD2 CE1 NE2 REMARK 470 LEU D 485 CG CD1 CD2 REMARK 470 GLU D 489 CG CD OE1 OE2 REMARK 470 GLU D 495 CG CD OE1 OE2 REMARK 470 ARG D 497 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 498 CG OD1 OD2 REMARK 470 VAL D 500 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO B 140 C - N - CD ANGL. DEV. = -19.8 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 LEU L 11 119.83 -169.09 REMARK 500 SER L 26 -77.75 -62.77 REMARK 500 ASP L 49 -30.65 75.16 REMARK 500 THR L 50 -45.98 160.49 REMARK 500 SER L 64 -158.49 -130.81 REMARK 500 ALA L 83 -177.19 177.71 REMARK 500 SER L 92 51.35 39.47 REMARK 500 HIS L 93 -6.28 85.30 REMARK 500 ASN L 137 86.42 48.39 REMARK 500 ASP L 150 64.50 34.13 REMARK 500 ASN L 151 1.70 58.76 REMARK 500 VAL L 190 93.21 52.28 REMARK 500 PRO L 203 107.91 -38.29 REMARK 500 ARG L 210 -146.44 -155.37 REMARK 500 VAL H 18 129.31 -171.12 REMARK 500 THR H 30 15.27 -63.02 REMARK 500 GLU H 62 -71.64 -28.52 REMARK 500 LYS H 67 -74.60 -57.24 REMARK 500 ASN H 77 64.68 38.09 REMARK 500 SER H 85 70.58 14.78 REMARK 500 SER H 88 -15.79 -44.79 REMARK 500 ASP H 109 107.97 -160.95 REMARK 500 SER H 121 54.79 -97.77 REMARK 500 PRO H 131 157.31 -49.55 REMARK 500 ASP H 152 87.65 64.18 REMARK 500 ASN H 163 -83.48 47.98 REMARK 500 SER H 164 70.96 -161.76 REMARK 500 ASN H 212 26.41 47.26 REMARK 500 GLU A 320 -7.42 -55.72 REMARK 500 HIS A 334 16.58 -64.94 REMARK 500 PRO A 349 -23.92 -34.18 REMARK 500 LEU A 371 3.75 -67.82 REMARK 500 GLN A 411 -46.04 -151.28 REMARK 500 LEU A 426 39.63 -93.15 REMARK 500 ASN A 442 77.46 -109.71 REMARK 500 LYS A 443 -45.64 -23.39 REMARK 500 CYS A 446 -166.92 -110.68 REMARK 500 TYR A 447 22.66 47.67 REMARK 500 ASN A 449 -161.32 -74.31 REMARK 500 THR A 450 -6.61 70.42 REMARK 500 LYS A 454 -2.27 -57.74 REMARK 500 ARG A 470 92.57 -52.11 REMARK 500 LEU A 485 -9.89 -57.40 REMARK 500 PRO A 488 -5.01 -58.50 REMARK 500 SER B 26 -71.09 -68.72 REMARK 500 LEU B 46 -60.65 -100.26 REMARK 500 THR B 50 -41.87 101.74 REMARK 500 ILE B 82 -18.14 -40.95 REMARK 500 ALA B 83 -177.63 -65.91 REMARK 500 SER B 91 138.23 -171.74 REMARK 500 REMARK 500 THIS ENTRY HAS 90 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 ARG H 99 ASP H 100 -147.94 REMARK 500 THR C 191 VAL C 192 136.35 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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE 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 ASP C 109 24.8 L L OUTSIDE RANGE REMARK 500 THR C 191 23.0 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 3281 REMARK 610 NAG A 3282 REMARK 610 BMA A 3283 REMARK 610 MAN A 3284 REMARK 610 NAG A 3371 REMARK 610 NAG A 3891 REMARK 610 NAG A 4201 REMARK 610 NAG A 4202 REMARK 610 NAG D 3281 REMARK 610 NAG D 3282 REMARK 610 BMA D 3283 REMARK 610 NAG D 3371 REMARK 610 NAG D 3891 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3281 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3282 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 3283 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3C08 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE THE FAB FRAGMENT OF MATUZUMAB/EMD72000 REMARK 900 (FAB72000)