REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.K.SOHI,A.L.CORPER,T.WAN,M.STEINITZ,R.JEFFERIS, REMARK 1 AUTH 2 D.BEALE,M.HE,A.FEINSTEIN,B.J.SUTTON,M.J.TAUSSIG REMARK 1 TITL CRYSTALLIZATION OF A COMPLEX BETWEEN THE FAB REMARK 1 TITL 2 FRAGMENT OF A HUMAN IMMUNOGLOBULIN M (IGM) REMARK 1 TITL 3 RHEUMATOID FACTOR (RF-AN) AND THE FC FRAGMENT OF REMARK 1 TITL 4 HUMAN IGG4 REMARK 1 REF IMMUNOLOGY V. 88 636 1996 REMARK 1 REFN ISSN 0019-2805 REMARK 2 REMARK 2 RESOLUTION. 3.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 80.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.0 REMARK 3 NUMBER OF REFLECTIONS : 11603 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 SET) : 0.225 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.600 REMARK 3 FREE R VALUE TEST SET COUNT : 756 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.15 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.26 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 902 REMARK 3 BIN R VALUE (WORKING SET) : 0.2880 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 53 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.050 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4977 REMARK 3 NUCLEIC ACID ATOMS : NULL REMARK 3 HETEROGEN ATOMS : NULL REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.41 REMARK 3 ESD FROM SIGMAA (A) : 0.45 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.52 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.18 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.47 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.06 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED B-FACTOR REFINEMENT REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGION A263-A300 WAS REMARK 3 MODELED STEREOCHEMICALLY. FAB IN COMPLEX WITH ITS AUTOANTIGEN REMARK 3 IGG FC. CONSTANT DOMAINS OF RF-AN SHOWED SIGNIFICANT DISORDER REMARK 3 AND WERE PARTLY MODELED STEREOCHEMICALLY. RESIDUES L51 AND REMARK 3 L171 OCCUR IN WELL DEFINED REGIONS OF THE STRUCTURE (OCCUPANCY REMARK 3 = 1). BOTH OCCUR IN LOOP REGIONS AND CONTINUE TO HAVE REMARK 3 DISALLOWED PHI/PSI VALUES EVEN AFTER REBUILDING. REMARK 4 REMARK 4 1ADQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : JUN-94 REMARK 200 TEMPERATURE (KELVIN) : 278 REMARK 200 PH : APPROX. REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : CCP4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14109 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.11300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.26500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1FC1, 2IG2 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY HANGING DROP REMARK 280 VAPOR DIFFUSION. THE HANGING DROPS CONSISTED OF 2UL OF PROTEIN REMARK 280 SOLUTION CONTAINING EACH PROTEIN AT 1MG/ML IN 0.1 % SODIUM REMARK 280 AZIDE, 20MM TRIS-HCL AT PH 7.0, MIXED WITH AN EQUAL VOLUME OF REMARK 280 THE RESERVOIR SOLUTION TO BE SCREENED. CRYSTALS WERE OBTAINED REMARK 280 WITH RESERVOIR SOLUTIONS CONTAINING 17.5 - 22.5 % (W/V) REMARK 280 POLYETHYLENE GLYCOL (MEAN MW 8000) IN 0.1 % SODIUM AZIDE, REMARK 280 100MM TRIS-HCL, PH 7.0, AT TEMPERATURES BETWEEN 17.5 AND 21.5 REMARK 280 (CELSIUS)., VAPOR DIFFUSION - HANGING DROP 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 80.17500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.97500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.17500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.97500 REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: A, L, H 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 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 PRO A 238 REMARK 475 VAL A 263 REMARK 475 VAL A 264 REMARK 475 ASP A 265 REMARK 475 VAL A 266 REMARK 475 SER A 267 REMARK 475 GLN A 268 REMARK 475 GLU A 269 REMARK 475 ASP A 270 REMARK 475 PRO A 271 REMARK 475 GLN A 272 REMARK 475 VAL A 273 REMARK 475 GLN A 274 REMARK 475 PHE A 275 REMARK 475 ASN A 276 REMARK 475 TRP A 277 REMARK 475 TYR A 278 REMARK 475 VAL A 279 REMARK 475 ASP A 280 REMARK 475 GLY A 281 REMARK 475 VAL A 282 REMARK 475 GLN A 283 REMARK 475 VAL A 284 REMARK 475 HIS A 285 REMARK 475 ASN A 286 REMARK 475 ALA A 287 REMARK 475 LYS A 288 REMARK 475 THR A 289 REMARK 475 LYS A 290 REMARK 475 PRO A 291 REMARK 475 ARG A 292 REMARK 475 GLU A 293 REMARK 475 GLN A 294 REMARK 475 GLN A 295 REMARK 475 PHE A 296 REMARK 475 ASN A 297 REMARK 475 SER A 298 REMARK 475 THR A 299 REMARK 475 TYR A 300 REMARK 475 GLY A 327 REMARK 475 GLN L 167 REMARK 475 GLU L 213 REMARK 475 CYS L 214 REMARK 475 SER L 215 REMARK 475 GLY H 114 REMARK 475 CYS H 127 REMARK 475 GLU H 128 REMARK 475 ASN H 129 REMARK 475 SER H 130 REMARK 475 ASN H 133 REMARK 475 PRO H 134 REMARK 475 SER H 135 REMARK 475 SER H 136 REMARK 475 THR H 137 REMARK 475 VAL H 138 REMARK 475 ALA H 139 REMARK 475 TYR H 159 REMARK 475 LYS H 160 REMARK 475 ASN H 161 REMARK 475 ASN H 162 REMARK 475 SER H 163 REMARK 475 ASP H 164 REMARK 475 ILE H 165 REMARK 475 SER H 168 REMARK 475 ARG H 179 REMARK 475 GLY H 180 REMARK 475 GLY H 183 REMARK 475 LYS H 184 REMARK 475 PRO H 194 REMARK 475 SER H 195 REMARK 475 LYS H 196 REMARK 475 ASP H 197 REMARK 475 VAL H 198 REMARK 475 MET H 199 REMARK 475 GLN H 200 REMARK 475 GLY H 201 REMARK 475 THR H 202 REMARK 475 ASN H 203 REMARK 475 GLU H 204 REMARK 475 HIS H 205 REMARK 475 HIS H 213 REMARK 475 PRO H 214 REMARK 475 ASN H 215 REMARK 475 GLY H 216 REMARK 475 ASN H 217 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 VAL A 262 CG1 CG2 REMARK 480 GLN A 311 OE1 NE2 REMARK 480 LYS A 320 CB CG CD CE NZ REMARK 480 LYS A 322 CB CG CD CE NZ REMARK 480 VAL A 323 CG1 CG2 REMARK 480 LYS A 326 CA C O CB CG CD CE REMARK 480 LYS A 326 NZ REMARK 480 SER A 331 CB OG REMARK 480 ILE A 332 CD1 REMARK 480 LYS A 334 CB CG CD CE NZ REMARK 480 ALA A 339 CB REMARK 480 LYS A 340 CB CG CD CE NZ REMARK 480 GLN A 347 CG CD OE1 NE2 REMARK 480 SER A 354 OG REMARK 480 GLN A 355 CD OE1 NE2 REMARK 480 GLN A 386 CB CG CD OE1 NE2 REMARK 480 SER A 400 CB OG REMARK 480 TYR L 2 CB OH REMARK 480 VAL L 13 CG1 REMARK 480 GLN L 17 CB CG CD OE1 NE2 REMARK 480 ARG L 20 CG CD NE CZ NH1 NH2 REMARK 480 ASN L 26 CB CG OD1 ND2 REMARK 480 ASN L 27 O CB CG OD1 ND2 REMARK 480 ILE L 28 O REMARK 480 SER L 30 C O CB OG REMARK 480 GLN L 42 CB CG CD OE1 NE2 REMARK 480 SER L 52 OG REMARK 480 ILE L 58 CD1 REMARK 480 ASN L 69 CB CG OD1 ND2 REMARK 480 THR L 70 O REMARK 480 SER L 76 CB OG REMARK 480 ARG L 77 CB CG CD NE CZ NH1 NH2 REMARK 480 VAL L 90 CG2 REMARK 480 SER L 93 CB OG REMARK 480 SER L 94 CB OG REMARK 480 HIS L 95B CB CG ND1 CD2 CE1 NE2 REMARK 480 GLY L 107 CA C O REMARK 480 GLN L 108 CB CG CD OE1 NE2 REMARK 480 LYS L 110 O CG CD CE NZ REMARK 480 ALA L 111 N CB REMARK 480 THR L 116 CG2 REMARK 480 PRO L 119 CB REMARK 480 GLU L 123 CB CG CD OE1 OE2 REMARK 480 GLU L 124 C O CB CG CD OE1 OE2 REMARK 480 LEU L 125 CB CG CD1 CD2 REMARK 480 GLN L 126 CB CG CD OE1 NE2 REMARK 480 LYS L 129 CB CG CD CE NZ REMARK 480 VAL L 133 CG1 CG2 REMARK 480 ASP L 138 OD2 REMARK 480 TYR L 140 CB CG CD1 CD2 CE1 CE2 CZ REMARK 480 TYR L 140 OH REMARK 480 ALA L 143 CB REMARK 480 ALA L 150 CB REMARK 480 SER L 153 OG REMARK 480 VAL L 155 CB CG1 CG2 REMARK 480 LYS L 156 CG CD CE NZ REMARK 480 GLU L 160 CG CD OE1 OE2 REMARK 480 THR L 163 OG1 CG2 REMARK 480 LYS L 166 CG CD CE NZ REMARK 480 SER L 168 N CB OG REMARK 480 ASN L 170 CB CG OD1 ND2 REMARK 480 TYR L 173 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 SER L 180 CB OG REMARK 480 GLU L 184 CD OE1 OE2 REMARK 480 GLN L 185 CB CG CD OE1 NE2 REMARK 480 GLN L 195 OE1 REMARK 480 THR L 208 CB OG1 CG2 REMARK 480 GLN H 13 CB CG CD OE1 NE2 REMARK 480 ARG H 16 CB CG CD NE CZ NH1 NH2 REMARK 480 SER H 25 CB OG REMARK 480 LYS H 43 CB CG CD CE NZ REMARK 480 GLU H 46 CB CG CD OE1 OE2 REMARK 480 SER H 52 OG REMARK 480 THR H 54 OG1 CG2 REMARK 480 VAL H 63 CG1 REMARK 480 LYS H 64 C O CD CE NZ REMARK 480 ALA H 88 CB REMARK 480 GLN H 105 CB CG CD OE1 NE2 REMARK 480 ILE H 107 CG2 CD1 REMARK 480 SER H 113 OG REMARK 480 SER H 115 CA REMARK 480 ALA H 116 CA CB REMARK 480 SER H 117 OG REMARK 480 ALA H 118 CA C O CB REMARK 480 THR H 120 N CG2 REMARK 480 LEU H 121 CG CD1 CD2 REMARK 480 SER H 126 CA C O CB OG REMARK 480 VAL H 140 CG1 REMARK 480 GLN H 145 CB CG CD OE1 NE2 REMARK 480 ASP H 146 N CB CG OD1 OD2 REMARK 480 LEU H 148 CB CG CD1 CD2 REMARK 480 ASP H 150 C O CG OD2 REMARK 480 SER H 151 N CB OG REMARK 480 ILE H 152 CG1 CG2 CD1 REMARK 480 THR H 153 CB OG1 CG2 REMARK 480 PHE H 154 CB CG CD1 CD2 CE1 CE2 CZ REMARK 480 SER H 156 CB OG REMARK 480 LYS H 158 CA C O CB CG CD CE REMARK 480 LYS H 158 NZ REMARK 480 SER H 169 O CB OG REMARK 480 ARG H 172 CG CD NE CZ NH1 NH2 REMARK 480 VAL H 177 CG2 REMARK 480 LEU H 178 C O REMARK 480 TYR H 185 CB CG CD1 CD2 CE1 CE2 CZ REMARK 480 TYR H 185 OH REMARK 480 ALA H 186 CB REMARK 480 SER H 189 OG REMARK 480 GLN H 190 CG CD OE1 NE2 REMARK 480 LEU H 192 CG CD1 CD2 REMARK 480 LEU H 193 C O CB CG CD1 CD2 REMARK 480 VAL H 207 CG1 CG2 REMARK 480 LYS H 209 CB CG CD CE NZ REMARK 480 GLN H 212 CB CG CD OE1 NE2 REMARK 480 LYS H 218 CB CG CD CE NZ REMARK 480 GLU H 220 CB CG CD OE1 OE2 REMARK 480 LYS H 221 CG CD CE NZ REMARK 480 ASP H 222 CG OD1 OD2 REMARK 480 VAL H 223 CB CG1 CG2 REMARK 480 PRO H 223A CB CG CD REMARK 480 LEU H 223B CB CG CD1 CD2 OXT REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 265 76.73 64.84 REMARK 500 GLU A 269 -125.65 -177.37 REMARK 500 PRO A 271 35.63 -72.51 REMARK 500 ASP A 280 51.89 34.13 REMARK 500 HIS A 285 -68.25 62.80 REMARK 500 ALA A 287 -129.63 58.90 REMARK 500 PRO A 291 87.06 -66.15 REMARK 500 ARG A 292 86.09 -68.12 REMARK 500 GLU A 293 89.72 -55.66 REMARK 500 ASN A 297 -95.63 70.37 REMARK 500 TYR A 300 115.53 174.93 REMARK 500 HIS A 310 -63.34 -26.89 REMARK 500 ASN A 325 148.00 -173.22 REMARK 500 LYS A 326 81.75 -67.99 REMARK 500 ALA A 339 98.75 -52.74 REMARK 500 SER A 383 -105.81 -94.64 REMARK 500 ASP A 401 10.28 -68.59 REMARK 500 THR A 437 144.04 -175.90 REMARK 500 ASP L 51 -58.91 75.27 REMARK 500 ARG L 61 -9.87 -58.54 REMARK 500 ALA L 84 -169.58 -169.77 REMARK 500 ALA L 143 119.01 -164.96 REMARK 500 GLN L 167 -74.78 52.37 REMARK 500 SER L 168 -32.02 -167.34 REMARK 500 ASN L 171 -50.31 74.53 REMARK 500 SER L 188 30.71 -93.94 REMARK 500 HIS L 198 77.24 -104.26 REMARK 500 GLU L 199 79.37 61.83 REMARK 500 PRO L 211 -5.57 -57.07 REMARK 500 SER H 7 -86.24 -129.44 REMARK 500 PRO H 14 152.60 -44.43 REMARK 500 PRO H 41 88.98 -45.18 REMARK 500 THR H 54 -14.73 71.13 REMARK 500 VAL H 63 -27.83 -145.95 REMARK 500 ARG H 96 84.34 -156.37 REMARK 500 SER H 113 -79.30 -79.19 REMARK 500 SER H 115 -84.98 -81.86 REMARK 500 SER H 126 -96.44 -106.48 REMARK 500 SER H 130 -57.35 -173.74 REMARK 500 ALA H 139 -115.53 54.55 REMARK 500 ASP H 150 -116.14 -54.82 REMARK 500 SER H 163 90.08 -69.58 REMARK 500 ASP H 164 -72.76 -56.68 REMARK 500 SER H 195 179.27 62.21 REMARK 500 GLN H 200 -62.55 72.06 REMARK 500 HIS H 205 139.49 -172.19 REMARK 500 ASN H 215 95.89 67.35 REMARK 500 PRO H 223A -161.81 -64.53 REMARK 500 REMARK 500 REMARK: NULL