REMARK 2 REMARK 2 RESOLUTION. 3.30 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) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.04 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 20747 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) : 0.286 REMARK 3 R VALUE (WORKING SET) : 0.282 REMARK 3 FREE R VALUE : 0.367 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1120 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) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1447 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.04 REMARK 3 BIN R VALUE (WORKING SET) : 0.3540 REMARK 3 BIN FREE R VALUE SET COUNT : 80 REMARK 3 BIN FREE R VALUE : 0.4390 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5524 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 121 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) : 60.92 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.80000 REMARK 3 B22 (A**2) : 10.75000 REMARK 3 B33 (A**2) : -7.95000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.646 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.469 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.029 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.864 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.763 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5787 ; 0.022 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7963 ; 2.647 ; 1.978 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 801 ;12.202 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;45.473 ;25.198 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 705 ;26.099 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;21.275 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 960 ; 0.161 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4366 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3403 ; 0.343 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3877 ; 0.343 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 262 ; 0.267 ; 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): 35 ; 0.372 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.169 ; 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): 4080 ; 0.794 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6328 ; 1.466 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1935 ; 2.025 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1635 ; 3.456 ; 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 3B2V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-07. REMARK 100 THE RCSB ID CODE IS RCSB045009. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21995 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 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 (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.18800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.20 REMARK 200 R MERGE FOR SHELL (I) : 0.58000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRIES 1YY9, 1CE1, AND 1DN0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.17 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12 % PEG 3350, IM NACL, 50 MM MES, PH REMARK 280 6.5, VAPOR DIFFUSION, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 78.19050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.19050 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.37150 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 133.12100 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.37150 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 133.12100 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.19050 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.37150 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 133.12100 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.19050 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.37150 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 133.12100 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6240 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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 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 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 1 REMARK 465 GLU A 2 REMARK 465 GLU A 3 REMARK 465 LYS A 4 REMARK 465 LYS A 5 REMARK 465 VAL A 6 REMARK 465 CYS A 7 REMARK 465 GLN A 8 REMARK 465 GLY A 9 REMARK 465 THR A 10 REMARK 465 SER A 11 REMARK 465 ASN A 12 REMARK 465 LYS A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 GLN A 16 REMARK 465 LEU A 17 REMARK 465 GLY A 18 REMARK 465 THR A 19 REMARK 465 PHE A 20 REMARK 465 GLU A 21 REMARK 465 ASP A 22 REMARK 465 HIS A 23 REMARK 465 PHE A 24 REMARK 465 LEU A 25 REMARK 465 SER A 26 REMARK 465 LEU A 27 REMARK 465 GLN A 28 REMARK 465 ARG A 29 REMARK 465 MET A 30 REMARK 465 PHE A 31 REMARK 465 ASN A 32 REMARK 465 ASN A 33 REMARK 465 CYS A 34 REMARK 465 GLU A 35 REMARK 465 VAL A 36 REMARK 465 VAL A 37 REMARK 465 LEU A 38 REMARK 465 GLY A 39 REMARK 465 ASN A 40 REMARK 465 LEU A 41 REMARK 465 GLU A 42 REMARK 465 ILE A 43 REMARK 465 THR A 44 REMARK 465 TYR A 45 REMARK 465 VAL A 46 REMARK 465 GLN A 47 REMARK 465 ARG A 48 REMARK 465 ASN A 49 REMARK 465 TYR A 50 REMARK 465 ASP A 51 REMARK 465 LEU A 52 REMARK 465 SER A 53 REMARK 465 PHE A 54 REMARK 465 LEU A 55 REMARK 465 LYS A 56 REMARK 465 THR A 57 REMARK 465 ILE A 58 REMARK 465 GLN A 59 REMARK 465 GLU A 60 REMARK 465 VAL A 61 REMARK 465 ALA A 62 REMARK 465 GLY A 63 REMARK 465 TYR A 64 REMARK 465 VAL A 65 REMARK 465 LEU A 66 REMARK 465 ILE A 67 REMARK 465 ALA A 68 REMARK 465 LEU A 69 REMARK 465 ASN A 70 REMARK 465 THR A 71 REMARK 465 VAL A 72 REMARK 465 GLU A 73 REMARK 465 ARG A 74 REMARK 465 ILE A 75 REMARK 465 PRO A 76 REMARK 465 LEU A 77 REMARK 465 GLU A 78 REMARK 465 ASN A 79 REMARK 465 LEU A 80 REMARK 465 GLN A 81 REMARK 465 ILE A 82 REMARK 465 ILE A 83 REMARK 465 ARG A 84 REMARK 465 GLY A 85 REMARK 465 ASN A 86 REMARK 465 MET A 87 REMARK 465 TYR A 88 REMARK 465 TYR A 89 REMARK 465 GLU A 90 REMARK 465 ASN A 91 REMARK 465 SER A 92 REMARK 465 TYR A 93 REMARK 465 ALA A 94 REMARK 465 LEU A 95 REMARK 465 ALA A 96 REMARK 465 VAL A 97 REMARK 465 LEU A 98 REMARK 465 SER A 99 REMARK 465 ASN A 100 REMARK 465 TYR A 101 REMARK 465 ASP A 102 REMARK 465 ALA A 103 REMARK 465 ASN A 104 REMARK 465 LYS A 105 REMARK 465 THR A 106 REMARK 465 GLY A 107 REMARK 465 LEU A 108 REMARK 465 LYS A 109 REMARK 465 GLU A 110 REMARK 465 LEU A 111 REMARK 465 PRO A 112 REMARK 465 MET A 113 REMARK 465 ARG A 114 REMARK 465 ASN A 115 REMARK 465 LEU A 116 REMARK 465 GLN A 117 REMARK 465 GLU A 118 REMARK 465 ILE A 119 REMARK 465 LEU A 120 REMARK 465 HIS A 121 REMARK 465 GLY A 122 REMARK 465 ALA A 123 REMARK 465 VAL A 124 REMARK 465 ARG A 125 REMARK 465 PHE A 126 REMARK 465 SER A 127 REMARK 465 ASN A 128 REMARK 465 ASN A 129 REMARK 465 PRO A 130 REMARK 465 ALA A 131 REMARK 465 LEU A 132 REMARK 465 CYS A 133 REMARK 465 ASN A 134 REMARK 465 VAL A 135 REMARK 465 GLU A 136 REMARK 465 SER A 137 REMARK 465 ILE A 138 REMARK 465 GLN A 139 REMARK 465 TRP A 140 REMARK 465 ARG A 141 REMARK 465 ASP A 142 REMARK 465 ILE A 143 REMARK 465 VAL A 144 REMARK 465 SER A 145 REMARK 465 SER A 146 REMARK 465 ASP A 147 REMARK 465 PHE A 148 REMARK 465 LEU A 149 REMARK 465 SER A 150 REMARK 465 ASN A 151 REMARK 465 MET A 152 REMARK 465 SER A 153 REMARK 465 MET A 154 REMARK 465 ASP A 155 REMARK 465 PHE A 156 REMARK 465 GLN A 157 REMARK 465 ASN A 158 REMARK 465 HIS A 159 REMARK 465 LEU A 160 REMARK 465 GLY A 161 REMARK 465 SER A 162 REMARK 465 CYS A 163 REMARK 465 GLN A 164 REMARK 465 LYS A 165 REMARK 465 CYS A 166 REMARK 465 ASP A 167 REMARK 465 PRO A 168 REMARK 465 SER A 169 REMARK 465 CYS A 170 REMARK 465 PRO A 171 REMARK 465 ASN A 172 REMARK 465 GLY A 173 REMARK 465 SER A 174 REMARK 465 CYS A 175 REMARK 465 TRP A 176 REMARK 465 GLY A 177 REMARK 465 ALA A 178 REMARK 465 GLY A 179 REMARK 465 GLU A 180 REMARK 465 GLU A 181 REMARK 465 ASN A 182 REMARK 465 CYS A 183 REMARK 465 GLN A 184 REMARK 465 LYS A 185 REMARK 465 LEU A 186 REMARK 465 THR A 187 REMARK 465 LYS A 188 REMARK 465 ILE A 189 REMARK 465 ILE A 190 REMARK 465 CYS A 191 REMARK 465 ALA A 192 REMARK 465 GLN A 193 REMARK 465 GLN A 194 REMARK 465 CYS A 195 REMARK 465 SER A 196 REMARK 465 GLY A 197 REMARK 465 ARG A 198 REMARK 465 CYS A 199 REMARK 465 ARG A 200 REMARK 465 GLY A 201 REMARK 465 LYS A 202 REMARK 465 SER A 203 REMARK 465 PRO A 204 REMARK 465 SER A 205 REMARK 465 ASP A 206 REMARK 465 CYS A 207 REMARK 465 CYS A 208 REMARK 465 HIS A 209 REMARK 465 ASN A 210 REMARK 465 GLN A 211 REMARK 465 CYS A 212 REMARK 465 ALA A 213 REMARK 465 ALA A 214 REMARK 465 GLY A 215 REMARK 465 CYS A 216 REMARK 465 THR A 217 REMARK 465 GLY A 218 REMARK 465 PRO A 219 REMARK 465 ARG A 220 REMARK 465 GLU A 221 REMARK 465 SER A 222 REMARK 465 ASP A 223 REMARK 465 CYS A 224 REMARK 465 LEU A 225 REMARK 465 VAL A 226 REMARK 465 CYS A 227 REMARK 465 ARG A 228 REMARK 465 LYS A 229 REMARK 465 PHE A 230 REMARK 465 ARG A 231 REMARK 465 ASP A 232 REMARK 465 GLU A 233 REMARK 465 ALA A 234 REMARK 465 THR A 235 REMARK 465 CYS A 236 REMARK 465 LYS A 237 REMARK 465 ASP A 238 REMARK 465 THR A 614 REMARK 465 ASN A 615 REMARK 465 GLY A 616 REMARK 465 PRO A 617 REMARK 465 LYS A 618 REMARK 465 HIS A 619 REMARK 465 HIS A 620 REMARK 465 HIS A 621 REMARK 465 HIS A 622 REMARK 465 HIS A 623 REMARK 465 HIS A 624 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 GLU L 17 CG CD OE1 OE2 REMARK 470 ARG L 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 38 CG CD OE1 NE2 REMARK 470 ARG L 54 CG CD NE CZ NH1 NH2 REMARK 470 ILE L 75 CG1 CG2 CD1 REMARK 470 LEU L 78 CG CD1 CD2 REMARK 470 HIS L 89 CG ND1 CD2 CE1 NE2 REMARK 470 LYS L 103 CG CD CE NZ REMARK 470 GLU L 105 CG CD OE1 OE2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 ARG L 108 CG CD NE CZ NH1 NH2 REMARK 470 PHE L 118 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU L 123 CG CD OE1 OE2 REMARK 470 GLN L 124 CG CD OE1 NE2 REMARK 470 LEU L 125 CG CD1 CD2 REMARK 470 LYS L 126 CG CD CE NZ REMARK 470 VAL L 132 CG1 CG2 REMARK 470 VAL L 133 CG1 CG2 REMARK 470 GLU L 143 CG CD OE1 OE2 REMARK 470 LYS L 145 CG CD CE NZ REMARK 470 GLN L 147 CG CD OE1 NE2 REMARK 470 TRP L 148 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP L 148 CZ3 CH2 REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 VAL L 150 CG1 CG2 REMARK 470 ASP L 151 CG OD1 OD2 REMARK 470 ASN L 152 CG OD1 REMARK 470 GLN L 155 CG CD OE1 NE2 REMARK 470 GLN L 160 CG CD OE1 NE2 REMARK 470 GLU L 161 CG CD OE1 OE2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LEU L 179 CG CD1 CD2 REMARK 470 LEU L 181 CG CD1 CD2 REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 TYR L 186 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU L 187 CG CD OE1 OE2 REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 VAL L 191 CG1 CG2 REMARK 470 TYR L 192 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU L 195 CG CD OE1 OE2 REMARK 470 VAL L 196 CG1 CG2 REMARK 470 HIS L 198 CG ND1 CD2 CE1 NE2 REMARK 470 LEU L 201 CG CD1 CD2 REMARK 470 SER L 202 OG REMARK 470 PHE L 209 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG L 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 5 CG CD OE1 NE2 REMARK 470 LEU H 18 CG CD1 CD2 REMARK 470 LYS H 45 CG CD CE NZ REMARK 470 TYR H 54 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 77 CG CD CE NZ REMARK 470 GLN H 113 CG CD OE1 NE2 REMARK 470 PHE H 130 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER H 136 OG REMARK 470 PHE H 174 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU H 183 CG CD1 CD2 REMARK 470 TYR H 184 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU H 197 CG CD1 CD2 REMARK 470 TYR H 202 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE H 203 CG1 CG2 CD1 REMARK 470 ASN H 205 CG OD1 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 VAL H 215 CG1 CG2 REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 GLU H 220 CG CD OE1 OE2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 LEU A 243 CG CD1 CD2 REMARK 470 MET A 244 CB CG SD CE REMARK 470 LEU A 245 CG CD1 CD2 REMARK 470 GLN A 252 CG CD OE1 NE2 REMARK 470 MET A 253 CG SD CE REMARK 470 VAL A 255 CG1 CG2 REMARK 470 ASN A 256 CG OD1 REMARK 470 GLU A 258 CG CD OE1 OE2 REMARK 470 LYS A 260 CG CD CE NZ REMARK 470 TYR A 261 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE A 263 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 269 CG CD CE NZ REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 274 CG OD1 REMARK 470 TYR A 275 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS A 280 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 285 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 301 CG CD CE NZ REMARK 470 LYS A 303 CG CD CE NZ REMARK 470 LYS A 304 CG CD CE NZ REMARK 470 ARG A 310 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 311 CG CD CE NZ REMARK 470 ILE A 316 CG1 CG2 CD1 REMARK 470 ILE A 318 CG1 CG2 CD1 REMARK 470 GLU A 320 CG CD OE1 OE2 REMARK 470 PHE A 321 CG CD1 CD2 CE1 CE2 CZ 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 VAL A 350 CG1 CG2 REMARK 470 PHE A 357 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 367 CG CD OE1 OE2 REMARK 470 ASP A 369 CG OD1 OD2 REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 408 CG CD OE1 NE2 REMARK 470 ARG A 427 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 430 CG CD CE NZ REMARK 470 GLU A 431 CG CD OE1 OE2 REMARK 470 LYS A 455 CG CD CE NZ REMARK 470 GLN A 462 CG CD OE1 NE2 REMARK 470 LYS A 463 CG CD CE NZ REMARK 470 LYS A 465 CG CD CE NZ REMARK 470 SER A 474 OG REMARK 470 LYS A 476 CG CD CE NZ REMARK 470 ARG A 503 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 509 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 513 CG OD1 OD2 REMARK 470 GLU A 519 CG CD OE1 OE2 REMARK 470 ARG A 523 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 550 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 553 CG OD1 OD2 REMARK 470 HIS A 560 CG ND1 CD2 CE1 NE2 REMARK 470 TYR A 561 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 569 CG CD CE NZ REMARK 470 MET A 576 CG SD CE REMARK 470 ASN A 579 CG OD1 REMARK 470 ASN A 580 CG OD1 REMARK 470 THR A 581 OG1 CG2 REMARK 470 LEU A 582 CG CD1 CD2 REMARK 470 TRP A 584 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 584 CZ3 CH2 REMARK 470 LYS A 585 CG CD CE NZ REMARK 470 TYR A 586 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS A 591 CG ND1 CD2 CE1 NE2 REMARK 470 VAL A 592 CG1 CG2 REMARK 470 HIS A 594 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 595 CG CD1 CD2 REMARK 470 TYR A 602 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 609 CG CD1 CD2 REMARK 470 GLU A 610 CG CD OE1 OE2 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 CG2 VAL H 24 O ASN H 78 1.79 REMARK 500 NE2 GLN L 6 O TYR L 86 1.93 REMARK 500 O LYS A 311 CG2 THR A 339 2.02 REMARK 500 O SER H 181 N LEU H 183 2.04 REMARK 500 NH2 ARG H 68 OD1 ASP H 91 2.04 REMARK 500 OD1 ASN A 328 N THR A 330 2.05 REMARK 500 O GLN A 366 N LEU A 368 2.11 REMARK 500 O SER H 28 N SER H 30 2.11 REMARK 500 ND2 ASN A 328 C2 NAG A 3281 2.13 REMARK 500 OG SER L 65 O THR L 72 2.13 REMARK 500 CG ASN A 504 C1 NAG A 5041 2.16 REMARK 500 O SER H 180 N GLY H 182 2.19 REMARK 500 CG2 VAL A 505 O SER A 529 2.19 REMARK 500 O TYR A 447 N ASN A 449 2.19 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 CYS A 534 CB CYS A 534 SG -0.134 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 PRO L 15 C - N - CA ANGL. DEV. = 11.5 DEGREES REMARK 500 CYS L 23 CB - CA - C ANGL. DEV. = -13.3 DEGREES REMARK 500 CYS L 23 CA - CB - SG ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP L 82 CB - CG - OD1 ANGL. DEV. = -6.8 DEGREES REMARK 500 CYS L 88 CB - CA - C ANGL. DEV. = -12.8 DEGREES REMARK 500 CYS L 88 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 PRO L 113 C - N - CA ANGL. DEV. = 9.9 DEGREES REMARK 500 ASN L 138 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 PRO H 9 C - N - CA ANGL. DEV. = 10.0 DEGREES REMARK 500 VAL H 24 CB - CA - C ANGL. DEV. = -14.0 DEGREES REMARK 500 VAL H 24 N - CA - C ANGL. DEV. = -18.7 DEGREES REMARK 500 CYS H 204 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 LEU A 371 CA - CB - CG ANGL. DEV. = -16.2 DEGREES REMARK 500 LEU A 382 CA - CB - CG ANGL. DEV. = -20.6 DEGREES REMARK 500 PRO A 494 C - N - CA ANGL. DEV. = 10.1 DEGREES REMARK 500 PRO A 540 C - N - CA ANGL. DEV. = 13.0 DEGREES REMARK 500 PRO A 572 C - N - CA ANGL. DEV. = 9.7 DEGREES REMARK 500 PRO A 598 C - N - CA ANGL. DEV. = 12.4 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 VAL L 3 113.70 -20.82 REMARK 500 THR L 5 69.92 -119.58 REMARK 500 ALA L 9 -62.12 40.85 REMARK 500 PRO L 15 154.21 -14.60 REMARK 500 SER L 22 125.90 -172.26 REMARK 500 VAL L 29 37.65 -87.19 REMARK 500 SER L 30 -96.46 32.83 REMARK 500 TYR L 32 88.03 -35.53 REMARK 500 PRO L 40 142.05 -25.75 REMARK 500 ALA L 43 -163.12 -161.29 REMARK 500 PRO L 44 170.75 -48.92 REMARK 500 LEU L 47 -47.06 -144.62 REMARK 500 ASP L 50 118.10 55.46 REMARK 500 ALA L 51 -89.51 40.41 REMARK 500 SER L 52 -59.27 162.37 REMARK 500 ALA L 55 -171.82 -65.71 REMARK 500 SER L 65 116.77 117.39 REMARK 500 SER L 77 102.62 -174.12 REMARK 500 GLU L 81 25.48 -72.77 REMARK 500 HIS L 89 25.64 -168.04 REMARK 500 GLN L 90 146.99 -14.90 REMARK 500 ARG L 108 -166.03 -101.71 REMARK 500 THR L 109 -106.71 -57.78 REMARK 500 PRO L 113 71.22 -48.62 REMARK 500 SER L 114 70.05 -59.03 REMARK 500 PRO L 120 -177.11 -58.72 REMARK 500 SER L 127 -93.24 -79.51 REMARK 500 THR L 129 -90.82 -125.47 REMARK 500 ALA L 130 155.25 88.82 REMARK 500 LEU L 135 -143.75 -92.72 REMARK 500 LEU L 136 68.58 147.08 REMARK 500 ASN L 138 68.63 -152.87 REMARK 500 PRO L 141 -153.94 -86.89 REMARK 500 ARG L 142 -101.70 -61.29 REMARK 500 ALA L 144 58.42 -171.93 REMARK 500 ASP L 151 -31.69 57.86 REMARK 500 ASN L 152 -166.64 -164.47 REMARK 500 ALA L 153 143.12 -34.45 REMARK 500 LEU L 154 -174.87 59.95 REMARK 500 GLN L 155 152.56 98.88 REMARK 500 ASN L 158 63.37 176.69 REMARK 500 SER L 159 130.92 170.04 REMARK 500 ASP L 170 -5.31 164.32 REMARK 500 TYR L 173 -148.53 -98.42 REMARK 500 SER L 174 115.29 171.96 REMARK 500 SER L 176 115.80 -160.65 REMARK 500 THR L 180 -74.67 -94.02 REMARK 500 LEU L 181 138.95 58.91 REMARK 500 LYS L 183 25.78 -60.21 REMARK 500 ALA L 184 -30.82 -131.33 REMARK 500 REMARK 500 THIS ENTRY HAS 214 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 CYS L 23 ARG L 24 149.89 REMARK 500 GLN L 42 ALA L 43 146.56 REMARK 500 ALA L 43 PRO L 44 -110.84 REMARK 500 ALA L 55 THR L 56 -142.04 REMARK 500 THR L 56 GLY L 57 -32.18 REMARK 500 GLY L 57 ILE L 58 143.18 REMARK 500 GLU L 79 PRO L 80 148.53 REMARK 500 GLY L 101 THR L 102 145.95 REMARK 500 THR H 23 VAL H 24 -72.40 REMARK 500 VAL H 69 THR H 70 148.47 REMARK 500 LEU H 82 LYS H 83 146.24 REMARK 500 GLY H 104 VAL H 105 143.02 REMARK 500 GLU H 156 PRO H 157 31.96 REMARK 500 ALA A 289 ASP A 290 -146.67 REMARK 500 GLY A 317 ILE A 318 33.19 REMARK 500 ASN A 328 ALA A 329 46.16 REMARK 500 CYS A 338 THR A 339 148.74 REMARK 500 SER A 340 ILE A 341 -148.33 REMARK 500 VAL A 350 ALA A 351 -149.45 REMARK 500 PRO A 387 GLU A 388 -149.40 REMARK 500 GLY A 404 ARG A 405 -42.76 REMARK 500 ILE A 421 THR A 422 -149.56 REMARK 500 LYS A 443 ASN A 444 149.37 REMARK 500 GLN A 557 CYS A 558 -148.58 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 VAL L 3 24.7 L L OUTSIDE RANGE REMARK 500 ALA L 43 23.6 L L OUTSIDE RANGE REMARK 500 SER L 52 24.2 L L OUTSIDE RANGE REMARK 500 HIS L 89 24.8 L L OUTSIDE RANGE REMARK 500 GLU A 320 20.8 L L OUTSIDE RANGE REMARK 500 PHE A 321 22.1 L L OUTSIDE RANGE REMARK 500 ILE A 370 21.9 L L OUTSIDE RANGE REMARK 500 LYS A 375 24.8 L L OUTSIDE RANGE REMARK 500 THR A 464 24.6 L L OUTSIDE RANGE REMARK 500 ILE A 467 24.7 L L OUTSIDE RANGE REMARK 500 CYS A 502 24.0 L L OUTSIDE RANGE REMARK 500 ILE A 556 24.5 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 5041 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 NDG A 3371 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3372 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3891 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5041 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3B2U RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ISOLATED DOMAIN III OF THE REMARK 900 EXTRACELLULAR REGION OF THE EPIDERMAL GROWTH FACTOR REMARK 900 RECEPTOR IN COMPLEX WITH THE FAB FRAGMENT OF IMC-11F8