REMARK 2 REMARK 2 RESOLUTION. 3.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 40227 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2010 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 49.8578 - 8.0706 0.57 3039 159 0.2124 0.2445 REMARK 3 2 8.0706 - 6.4102 0.55 2924 154 0.2419 0.2925 REMARK 3 3 6.4102 - 5.6011 0.54 2883 151 0.2485 0.2918 REMARK 3 4 5.6011 - 5.0895 0.54 2862 150 0.2317 0.2745 REMARK 3 5 5.0895 - 4.7251 0.53 2822 149 0.2033 0.2731 REMARK 3 6 4.7251 - 4.4467 0.53 2856 151 0.2117 0.2777 REMARK 3 7 4.4467 - 4.2241 0.53 2821 148 0.2211 0.2464 REMARK 3 8 4.2241 - 4.0403 0.53 2798 147 0.2376 0.3026 REMARK 3 9 4.0403 - 3.8848 0.53 2821 149 0.2445 0.2954 REMARK 3 10 3.8848 - 3.7508 0.53 2811 148 0.2458 0.2759 REMARK 3 11 3.7508 - 3.6336 0.52 2753 147 0.2405 0.3017 REMARK 3 12 3.6336 - 3.5297 0.49 2614 139 0.2608 0.3144 REMARK 3 13 3.5297 - 3.4368 0.43 2309 116 0.2585 0.3161 REMARK 3 14 3.4368 - 3.3530 0.36 1904 102 0.2525 0.2939 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.880 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 21433 REMARK 3 ANGLE : 1.578 28986 REMARK 3 CHIRALITY : 0.105 3187 REMARK 3 PLANARITY : 0.008 3693 REMARK 3 DIHEDRAL : 16.731 7939 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4IOF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-13. REMARK 100 THE RCSB ID CODE IS RCSB077006. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 278 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40227 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.353 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.200 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.11900 REMARK 200 R SYM (I) : 0.11900 REMARK 200 FOR THE DATA SET : 14.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.68800 REMARK 200 R SYM FOR SHELL (I) : 0.68800 REMARK 200 FOR SHELL : 3.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: PDB ENTRY 3CWW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, PH6.5; 0.2M REMARK 280 MGCL2; 10% PEG3000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.47750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 188.51950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.83100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 188.51950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.47750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.83100 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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 MET A 30 REMARK 465 HIS A 31 REMARK 465 HIS A 32 REMARK 465 HIS A 33 REMARK 465 HIS A 34 REMARK 465 HIS A 35 REMARK 465 HIS A 36 REMARK 465 ALA A 37 REMARK 465 ALA A 38 REMARK 465 GLY A 39 REMARK 465 ILE A 40 REMARK 465 PRO A 41 REMARK 465 MET A 42 REMARK 465 ASN A 43 REMARK 465 GLY A 209 REMARK 465 ASN A 210 REMARK 465 PRO A 211 REMARK 465 LYS A 212 REMARK 465 HIS A 213 REMARK 465 PRO A 214 REMARK 465 PHE A 215 REMARK 465 GLU A 287 REMARK 465 PHE A 288 REMARK 465 PRO A 289 REMARK 465 GLU A 290 REMARK 465 HIS A 291 REMARK 465 PRO A 292 REMARK 465 PHE A 293 REMARK 465 GLN A 294 REMARK 465 GLU A 295 REMARK 465 GLU A 296 REMARK 465 HIS A 297 REMARK 465 GLY A 366 REMARK 465 ALA A 367 REMARK 465 ARG A 368 REMARK 465 GLY A 369 REMARK 465 ASN A 966 REMARK 465 PRO A 967 REMARK 465 VAL A 968 REMARK 465 VAL A 969 REMARK 465 GLY A 970 REMARK 465 GLU A 971 REMARK 465 PHE A 972 REMARK 465 PRO A 973 REMARK 465 ALA A 974 REMARK 465 GLN A 975 REMARK 465 ASN A 976 REMARK 465 ASP A 977 REMARK 465 ILE A 978 REMARK 465 HIS A 1011 REMARK 465 ILE A 1012 REMARK 465 ASN A 1013 REMARK 465 PHE A 1014 REMARK 465 MET A 1015 REMARK 465 ALA A 1016 REMARK 465 ALA A 1017 REMARK 465 LYS A 1018 REMARK 465 LEU A 1019 REMARK 465 MET B 30 REMARK 465 HIS B 31 REMARK 465 HIS B 32 REMARK 465 HIS B 33 REMARK 465 HIS B 34 REMARK 465 HIS B 35 REMARK 465 HIS B 36 REMARK 465 ALA B 37 REMARK 465 ALA B 38 REMARK 465 GLY B 39 REMARK 465 ILE B 40 REMARK 465 PRO B 41 REMARK 465 MET B 42 REMARK 465 ASN B 43 REMARK 465 ASN B 44 REMARK 465 ALA B 104 REMARK 465 GLY B 105 REMARK 465 LEU B 106 REMARK 465 SER B 107 REMARK 465 HIS B 108 REMARK 465 ASP B 175 REMARK 465 GLU B 176 REMARK 465 SER B 177 REMARK 465 ALA B 178 REMARK 465 LYS B 179 REMARK 465 ASP B 180 REMARK 465 ARG B 181 REMARK 465 GLU B 182 REMARK 465 VAL B 183 REMARK 465 ASN B 184 REMARK 465 ALA B 185 REMARK 465 VAL B 186 REMARK 465 ASP B 187 REMARK 465 SER B 188 REMARK 465 GLU B 189 REMARK 465 HIS B 190 REMARK 465 GLU B 191 REMARK 465 LYS B 192 REMARK 465 ASN B 193 REMARK 465 VAL B 194 REMARK 465 MET B 195 REMARK 465 ASN B 196 REMARK 465 ASP B 197 REMARK 465 ALA B 198 REMARK 465 TRP B 199 REMARK 465 ARG B 200 REMARK 465 LEU B 201 REMARK 465 PHE B 202 REMARK 465 GLN B 203 REMARK 465 LEU B 204 REMARK 465 GLU B 205 REMARK 465 LYS B 206 REMARK 465 ALA B 207 REMARK 465 THR B 208 REMARK 465 GLY B 209 REMARK 465 ASN B 210 REMARK 465 PRO B 211 REMARK 465 LYS B 212 REMARK 465 HIS B 213 REMARK 465 PRO B 214 REMARK 465 PHE B 215 REMARK 465 SER B 216 REMARK 465 LYS B 217 REMARK 465 PHE B 218 REMARK 465 GLY B 219 REMARK 465 THR B 220 REMARK 465 GLY B 221 REMARK 465 ASN B 222 REMARK 465 LYS B 223 REMARK 465 TYR B 224 REMARK 465 THR B 225 REMARK 465 LEU B 226 REMARK 465 GLU B 227 REMARK 465 THR B 228 REMARK 465 ARG B 229 REMARK 465 PRO B 230 REMARK 465 ASN B 231 REMARK 465 GLN B 232 REMARK 465 GLU B 233 REMARK 465 GLY B 234 REMARK 465 ILE B 235 REMARK 465 ASP B 236 REMARK 465 VAL B 237 REMARK 465 ARG B 238 REMARK 465 GLN B 239 REMARK 465 PRO B 284 REMARK 465 LEU B 285 REMARK 465 PRO B 286 REMARK 465 GLU B 287 REMARK 465 PHE B 288 REMARK 465 PRO B 289 REMARK 465 GLU B 290 REMARK 465 HIS B 291 REMARK 465 PRO B 292 REMARK 465 PHE B 293 REMARK 465 GLN B 294 REMARK 465 GLU B 295 REMARK 465 GLU B 296 REMARK 465 HIS B 297 REMARK 465 LEU B 298 REMARK 465 ALA B 367 REMARK 465 ARG B 368 REMARK 465 LEU B 456 REMARK 465 THR B 492 REMARK 465 GLU B 493 REMARK 465 GLU B 494 REMARK 465 TRP B 495 REMARK 465 TYR B 496 REMARK 465 ASN B 966 REMARK 465 PRO B 967 REMARK 465 VAL B 968 REMARK 465 VAL B 969 REMARK 465 GLY B 970 REMARK 465 GLU B 971 REMARK 465 PHE B 972 REMARK 465 PRO B 973 REMARK 465 ALA B 974 REMARK 465 GLN B 975 REMARK 465 ASN B 976 REMARK 465 ASP B 977 REMARK 465 ILE B 978 REMARK 465 ILE B 1012 REMARK 465 ASN B 1013 REMARK 465 PHE B 1014 REMARK 465 MET B 1015 REMARK 465 ALA B 1016 REMARK 465 ALA B 1017 REMARK 465 LYS B 1018 REMARK 465 LEU B 1019 REMARK 465 MET C -25 REMARK 465 LYS C -24 REMARK 465 LYS C -23 REMARK 465 ASN C -22 REMARK 465 ILE C -21 REMARK 465 ALA C -20 REMARK 465 PHE C -19 REMARK 465 LEU C -18 REMARK 465 LEU C -17 REMARK 465 ALA C -16 REMARK 465 SER C -15 REMARK 465 MET C -14 REMARK 465 PHE C -13 REMARK 465 VAL C -12 REMARK 465 PHE C -11 REMARK 465 SER C -10 REMARK 465 ILE C -9 REMARK 465 ALA C -8 REMARK 465 THR C -7 REMARK 465 ASN C -6 REMARK 465 ALA C -5 REMARK 465 TYR C -4 REMARK 465 ALA C -3 REMARK 465 GLU C -2 REMARK 465 ILE C -1 REMARK 465 SER C 0 REMARK 465 SER C 75 REMARK 465 LYS C 76 REMARK 465 LYS C 145 REMARK 465 SER C 146 REMARK 465 THR C 147 REMARK 465 SER C 148 REMARK 465 GLY C 149 REMARK 465 GLY C 150 REMARK 465 THR C 176 REMARK 465 SER C 204 REMARK 465 LEU C 205 REMARK 465 GLY C 206 REMARK 465 THR C 207 REMARK 465 GLN C 208 REMARK 465 SER C 231 REMARK 465 CYS C 232 REMARK 465 ASP C 233 REMARK 465 LYS C 234 REMARK 465 THR C 235 REMARK 465 HIS C 236 REMARK 465 THR C 237 REMARK 465 MET D -23 REMARK 465 LYS D -22 REMARK 465 LYS D -21 REMARK 465 ASN D -20 REMARK 465 ILE D -19 REMARK 465 ALA D -18 REMARK 465 PHE D -17 REMARK 465 LEU D -16 REMARK 465 LEU D -15 REMARK 465 ALA D -14 REMARK 465 SER D -13 REMARK 465 MET D -12 REMARK 465 PHE D -11 REMARK 465 VAL D -10 REMARK 465 PHE D -9 REMARK 465 SER D -8 REMARK 465 ILE D -7 REMARK 465 ALA D -6 REMARK 465 THR D -5 REMARK 465 ASN D -4 REMARK 465 ALA D -3 REMARK 465 TYR D -2 REMARK 465 ALA D -1 REMARK 465 SER D 0 REMARK 465 ASP D 1 REMARK 465 ILE D 2 REMARK 465 GLN D 3 REMARK 465 SER D 26 REMARK 465 GLN D 27 REMARK 465 SER D 28 REMARK 465 GLY D 68 REMARK 465 GLY D 129 REMARK 465 THR D 130 REMARK 465 VAL D 151 REMARK 465 ASP D 152 REMARK 465 ASN D 153 REMARK 465 GLN D 156 REMARK 465 GLY D 213 REMARK 465 GLU D 214 REMARK 465 CYS D 215 REMARK 465 MET E -25 REMARK 465 LYS E -24 REMARK 465 LYS E -23 REMARK 465 ASN E -22 REMARK 465 ILE E -21 REMARK 465 ALA E -20 REMARK 465 PHE E -19 REMARK 465 LEU E -18 REMARK 465 LEU E -17 REMARK 465 ALA E -16 REMARK 465 SER E -15 REMARK 465 MET E -14 REMARK 465 PHE E -13 REMARK 465 VAL E -12 REMARK 465 PHE E -11 REMARK 465 SER E -10 REMARK 465 ILE E -9 REMARK 465 ALA E -8 REMARK 465 THR E -7 REMARK 465 ASN E -6 REMARK 465 ALA E -5 REMARK 465 TYR E -4 REMARK 465 ALA E -3 REMARK 465 GLU E -2 REMARK 465 ILE E -1 REMARK 465 SER E 0 REMARK 465 SER E 131 REMARK 465 SER E 143 REMARK 465 SER E 144 REMARK 465 LYS E 145 REMARK 465 SER E 146 REMARK 465 THR E 147 REMARK 465 SER E 148 REMARK 465 GLY E 149 REMARK 465 GLY E 150 REMARK 465 THR E 151 REMARK 465 ALA E 152 REMARK 465 THR E 176 REMARK 465 SER E 177 REMARK 465 PRO E 201 REMARK 465 THR E 207 REMARK 465 GLN E 208 REMARK 465 GLU E 228 REMARK 465 PRO E 229 REMARK 465 LYS E 230 REMARK 465 SER E 231 REMARK 465 CYS E 232 REMARK 465 ASP E 233 REMARK 465 LYS E 234 REMARK 465 THR E 235 REMARK 465 HIS E 236 REMARK 465 THR E 237 REMARK 465 MET F -23 REMARK 465 LYS F -22 REMARK 465 LYS F -21 REMARK 465 ASN F -20 REMARK 465 ILE F -19 REMARK 465 ALA F -18 REMARK 465 PHE F -17 REMARK 465 LEU F -16 REMARK 465 LEU F -15 REMARK 465 ALA F -14 REMARK 465 SER F -13 REMARK 465 MET F -12 REMARK 465 PHE F -11 REMARK 465 VAL F -10 REMARK 465 PHE F -9 REMARK 465 SER F -8 REMARK 465 ILE F -7 REMARK 465 ALA F -6 REMARK 465 THR F -5 REMARK 465 ASN F -4 REMARK 465 ALA F -3 REMARK 465 TYR F -2 REMARK 465 ALA F -1 REMARK 465 SER F 0 REMARK 465 ASP F 1 REMARK 465 ILE F 2 REMARK 465 GLN F 3 REMARK 465 LYS F 150 REMARK 465 VAL F 151 REMARK 465 ASP F 152 REMARK 465 ASN F 153 REMARK 465 ALA F 154 REMARK 465 LEU F 155 REMARK 465 GLY F 201 REMARK 465 LEU F 202 REMARK 465 SER F 203 REMARK 465 SER F 204 REMARK 465 ASN F 211 REMARK 465 ARG F 212 REMARK 465 GLY F 213 REMARK 465 GLU F 214 REMARK 465 CYS F 215 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 GLY A 51 N - CA - C ANGL. DEV. = -21.7 DEGREES REMARK 500 LEU A 97 CA - CB - CG ANGL. DEV. = 15.5 DEGREES REMARK 500 ASN A 280 CB - CA - C ANGL. DEV. = -30.5 DEGREES REMARK 500 VAL B 92 CB - CA - C ANGL. DEV. = -14.7 DEGREES REMARK 500 LEU B 114 CB - CA - C ANGL. DEV. = -11.6 DEGREES REMARK 500 PRO B 172 C - N - CD ANGL. DEV. = -36.7 DEGREES REMARK 500 ALA B 438 CB - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 PRO C 135 C - N - CA ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY D 64 N - CA - C ANGL. DEV. = -15.2 DEGREES REMARK 500 ASN E 220 CB - CA - C ANGL. DEV. = -18.6 DEGREES REMARK 500 VAL F 29 CB - CA - C ANGL. DEV. = -22.1 DEGREES REMARK 500 SER F 31 N - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 PRO F 93 C - N - CA ANGL. DEV. = -10.8 DEGREES REMARK 500 CYS F 195 CA - CB - SG ANGL. DEV. = 6.6 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 HIS A 93 44.72 -75.84 REMARK 500 SER A 143 -166.64 -106.58 REMARK 500 SER A 171 110.96 -162.03 REMARK 500 GLU A 227 -59.29 -131.40 REMARK 500 LYS A 281 42.74 -109.97 REMARK 500 ASN A 282 81.47 34.40 REMARK 500 GLU A 457 -36.47 -132.67 REMARK 500 PRO A 473 6.49 -63.55 REMARK 500 LYS A 566 -70.52 -134.32 REMARK 500 TYR A 584 11.63 -146.01 REMARK 500 THR A 651 19.93 -145.28 REMARK 500 ASP A 773 120.46 -34.99 REMARK 500 THR A 797 -71.19 -98.81 REMARK 500 ASP A 798 -170.77 -172.37 REMARK 500 ARG A 824 -71.39 -105.06 REMARK 500 LYS B 48 -172.75 -63.89 REMARK 500 PHE B 115 36.59 -99.50 REMARK 500 TYR B 127 -73.82 -62.95 REMARK 500 SER B 143 -164.48 -107.12 REMARK 500 SER B 171 116.79 -162.30 REMARK 500 LEU B 173 -62.69 -121.31 REMARK 500 LEU B 241 47.02 -105.75 REMARK 500 LYS B 281 -76.58 -114.66 REMARK 500 ALA B 438 6.03 82.04 REMARK 500 ASN B 515 30.23 -98.92 REMARK 500 LYS B 566 -70.44 -134.51 REMARK 500 TYR B 584 11.78 -145.94 REMARK 500 THR B 651 20.12 -145.67 REMARK 500 ASP B 773 120.44 -35.07 REMARK 500 THR B 797 -71.47 -98.06 REMARK 500 ASP B 798 -170.64 -172.76 REMARK 500 ARG B 824 -72.28 -104.68 REMARK 500 PRO B1010 -150.74 -68.31 REMARK 500 GLN C 3 158.37 176.86 REMARK 500 VAL C 48 -60.38 -106.29 REMARK 500 SER C 85 81.78 48.97 REMARK 500 ALA C 92 -179.35 -177.10 REMARK 500 PRO C 113 88.05 -68.41 REMARK 500 ASN C 171 75.48 35.53 REMARK 500 SER C 188 -7.74 -59.31 REMARK 500 ALA D 13 173.14 176.68 REMARK 500 LEU D 47 -61.12 -107.77 REMARK 500 SER D 77 56.40 -99.79 REMARK 500 ASN D 138 -90.69 -40.77 REMARK 500 PRO D 205 103.76 -56.61 REMARK 500 GLN E 3 158.36 177.32 REMARK 500 LYS E 65 -71.21 -123.08 REMARK 500 SER E 85 75.48 -111.78 REMARK 500 ALA E 92 -173.42 -178.25 REMARK 500 TYR E 103 50.65 -117.54 REMARK 500 REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 189 OE1 REMARK 620 2 HIS A 112 NE2 125.3 REMARK 620 3 HIS A 108 NE2 109.1 99.7 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1101