REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.41 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 19042 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.242 REMARK 3 R VALUE (WORKING SET) : 0.238 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.790 REMARK 3 FREE R VALUE TEST SET COUNT : 1864 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 44.4130 - 7.9810 0.97 1428 150 0.2640 0.2820 REMARK 3 2 7.9810 - 6.3400 1.00 1416 129 0.2520 0.3080 REMARK 3 3 6.3400 - 5.5410 0.99 1406 141 0.2370 0.2880 REMARK 3 4 5.5410 - 5.0350 1.00 1380 140 0.2000 0.2470 REMARK 3 5 5.0350 - 4.6740 0.99 1383 141 0.1830 0.2110 REMARK 3 6 4.6740 - 4.3990 0.99 1308 160 0.1840 0.2480 REMARK 3 7 4.3990 - 4.1790 0.99 1368 153 0.1920 0.2070 REMARK 3 8 4.1790 - 3.9970 0.98 1332 156 0.2110 0.2630 REMARK 3 9 3.9970 - 3.8430 0.96 1314 157 0.2300 0.2860 REMARK 3 10 3.8430 - 3.7110 0.94 1248 147 0.2290 0.2790 REMARK 3 11 3.7110 - 3.5950 0.92 1281 144 0.2530 0.2810 REMARK 3 12 3.5950 - 3.4920 0.89 1177 111 0.2560 0.2660 REMARK 3 13 3.4920 - 3.4000 0.82 1137 135 0.2680 0.2930 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 : 0.32 REMARK 3 B_SOL : 119.22 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -11.73000 REMARK 3 B22 (A**2) : 11.60200 REMARK 3 B33 (A**2) : -0.03500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 10.72000 REMARK 3 B23 (A**2) : -0.00000 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 : 0.003 5088 REMARK 3 ANGLE : 0.669 6919 REMARK 3 CHIRALITY : 0.042 802 REMARK 3 PLANARITY : 0.003 869 REMARK 3 DIHEDRAL : 16.331 1746 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 35-62 REMARK 3 ORIGIN FOR THE GROUP (A): 25.0397 38.4713 42.3780 REMARK 3 T TENSOR REMARK 3 T11: 0.6752 T22: 0.7989 REMARK 3 T33: 3.0352 T12: -0.1732 REMARK 3 T13: -0.0342 T23: -0.6125 REMARK 3 L TENSOR REMARK 3 L11: -4.6032 L22: -4.3464 REMARK 3 L33: 0.6586 L12: -2.3268 REMARK 3 L13: -3.1854 L23: -0.7052 REMARK 3 S TENSOR REMARK 3 S11: -0.1245 S12: 0.3235 S13: -0.1314 REMARK 3 S21: 0.6725 S22: -1.0954 S23: -0.2915 REMARK 3 S31: -0.6206 S32: 0.2059 S33: 0.9997 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 63-91 REMARK 3 ORIGIN FOR THE GROUP (A): 24.6046 45.5368 48.4296 REMARK 3 T TENSOR REMARK 3 T11: 0.7164 T22: 1.5075 REMARK 3 T33: 2.8632 T12: -0.1991 REMARK 3 T13: 0.0173 T23: -0.3087 REMARK 3 L TENSOR REMARK 3 L11: 1.0547 L22: 0.5994 REMARK 3 L33: -1.0892 L12: -0.4899 REMARK 3 L13: -0.8407 L23: -0.1266 REMARK 3 S TENSOR REMARK 3 S11: -0.4830 S12: -0.7179 S13: 1.2397 REMARK 3 S21: 0.1854 S22: 0.3520 S23: 0.1978 REMARK 3 S31: 0.1595 S32: 0.5998 S33: 0.2010 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 108-144 REMARK 3 ORIGIN FOR THE GROUP (A): 29.1806 57.2118 50.9754 REMARK 3 T TENSOR REMARK 3 T11: 0.7750 T22: 1.8231 REMARK 3 T33: 2.2243 T12: 0.2289 REMARK 3 T13: -0.2698 T23: -0.6768 REMARK 3 L TENSOR REMARK 3 L11: -0.3834 L22: 1.8729 REMARK 3 L33: -0.1018 L12: 0.5545 REMARK 3 L13: 0.8457 L23: -1.0988 REMARK 3 S TENSOR REMARK 3 S11: 1.6994 S12: 0.8643 S13: -0.6789 REMARK 3 S21: 0.0369 S22: -1.4996 S23: 1.9728 REMARK 3 S31: 0.1142 S32: -0.2409 S33: -0.1328 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 145-164 REMARK 3 ORIGIN FOR THE GROUP (A): 24.8074 54.3706 59.2464 REMARK 3 T TENSOR REMARK 3 T11: 1.1877 T22: 1.3851 REMARK 3 T33: 1.7187 T12: -0.0514 REMARK 3 T13: 0.5217 T23: -0.0394 REMARK 3 L TENSOR REMARK 3 L11: 8.9951 L22: 6.8093 REMARK 3 L33: 2.6691 L12: -4.0022 REMARK 3 L13: 0.7340 L23: 0.5329 REMARK 3 S TENSOR REMARK 3 S11: 0.2058 S12: -0.8124 S13: -0.0283 REMARK 3 S21: 0.0694 S22: -0.4698 S23: 1.2363 REMARK 3 S31: -0.7261 S32: 0.6089 S33: -0.0218 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 203-242 REMARK 3 ORIGIN FOR THE GROUP (A): 40.5198 63.7908 43.0775 REMARK 3 T TENSOR REMARK 3 T11: 0.8236 T22: 0.5905 REMARK 3 T33: 0.5146 T12: 0.0584 REMARK 3 T13: -0.4432 T23: -0.4189 REMARK 3 L TENSOR REMARK 3 L11: 0.4770 L22: 3.0786 REMARK 3 L33: 2.3541 L12: 0.3437 REMARK 3 L13: -0.1856 L23: 1.0693 REMARK 3 S TENSOR REMARK 3 S11: -0.5638 S12: -0.2722 S13: 0.0947 REMARK 3 S21: -0.9087 S22: -0.6241 S23: 0.2279 REMARK 3 S31: -0.2633 S32: 0.3858 S33: 0.5890 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 263-291 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4408 56.4628 39.6897 REMARK 3 T TENSOR REMARK 3 T11: 1.3154 T22: 2.0932 REMARK 3 T33: 1.7483 T12: 0.1000 REMARK 3 T13: 0.0261 T23: -0.4017 REMARK 3 L TENSOR REMARK 3 L11: -1.1721 L22: 2.3415 REMARK 3 L33: 0.7611 L12: 0.6583 REMARK 3 L13: -0.1181 L23: -0.6697 REMARK 3 S TENSOR REMARK 3 S11: -0.1813 S12: 0.2557 S13: 0.2619 REMARK 3 S21: 0.0698 S22: -0.5127 S23: 1.3272 REMARK 3 S31: 0.2710 S32: -0.8798 S33: 0.6791 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 307-346 REMARK 3 ORIGIN FOR THE GROUP (A): 30.8927 42.5099 38.1328 REMARK 3 T TENSOR REMARK 3 T11: 1.1562 T22: 1.8727 REMARK 3 T33: 2.3250 T12: -0.1382 REMARK 3 T13: 0.2259 T23: -0.7549 REMARK 3 L TENSOR REMARK 3 L11: 1.6158 L22: 1.0424 REMARK 3 L33: 2.2741 L12: 0.2620 REMARK 3 L13: 0.4083 L23: -1.1153 REMARK 3 S TENSOR REMARK 3 S11: -0.4893 S12: -0.3475 S13: 0.0508 REMARK 3 S21: 0.5094 S22: -0.3919 S23: -0.6606 REMARK 3 S31: -0.7024 S32: 0.5038 S33: 0.4840 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN L REMARK 3 ORIGIN FOR THE GROUP (A): 85.8585 54.5149 17.8111 REMARK 3 T TENSOR REMARK 3 T11: 0.7044 T22: 0.5884 REMARK 3 T33: 0.5257 T12: -0.0437 REMARK 3 T13: -0.0164 T23: -0.0226 REMARK 3 L TENSOR REMARK 3 L11: 1.7062 L22: 1.1648 REMARK 3 L33: 1.5040 L12: -0.0371 REMARK 3 L13: -1.6949 L23: 0.1006 REMARK 3 S TENSOR REMARK 3 S11: 0.1976 S12: -0.1295 S13: 0.3998 REMARK 3 S21: -0.4164 S22: 0.0135 S23: -0.1964 REMARK 3 S31: -0.3169 S32: 0.1400 S33: -0.1672 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN H REMARK 3 ORIGIN FOR THE GROUP (A): 73.1850 42.6539 19.2703 REMARK 3 T TENSOR REMARK 3 T11: 0.6485 T22: 0.5867 REMARK 3 T33: 0.5761 T12: -0.0799 REMARK 3 T13: -0.0394 T23: -0.0602 REMARK 3 L TENSOR REMARK 3 L11: 0.9809 L22: 1.2225 REMARK 3 L33: 1.9803 L12: -0.8191 REMARK 3 L13: -0.9582 L23: 0.3143 REMARK 3 S TENSOR REMARK 3 S11: -0.0823 S12: 0.1581 S13: -0.2583 REMARK 3 S21: -0.1631 S22: -0.1835 S23: 0.0957 REMARK 3 S31: 0.3108 S32: -0.2583 S33: 0.2299 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 3KJ6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-09. REMARK 100 THE RCSB ID CODE IS RCSB056057. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-AUG-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19946 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.11700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.38300 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4, PH 7, BICELLES, 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 169.30000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.30000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 169.30000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.30000 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 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 GLY A 0 REMARK 465 PHE A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 ASN A 15 REMARK 465 ARG A 16 REMARK 465 SER A 17 REMARK 465 HIS A 18 REMARK 465 ALA A 19 REMARK 465 PRO A 20 REMARK 465 ASP A 21 REMARK 465 HIS A 22 REMARK 465 ASP A 23 REMARK 465 VAL A 24 REMARK 465 THR A 25 REMARK 465 GLN A 26 REMARK 465 GLN A 27 REMARK 465 ARG A 28 REMARK 465 ASP A 29 REMARK 465 GLU A 30 REMARK 465 VAL A 31 REMARK 465 TRP A 32 REMARK 465 VAL A 33 REMARK 465 VAL A 34 REMARK 465 LYS A 60 REMARK 465 ALA A 92 REMARK 465 HIS A 93 REMARK 465 ILE A 94 REMARK 465 LEU A 95 REMARK 465 MET A 96 REMARK 465 LYS A 97 REMARK 465 MET A 98 REMARK 465 TRP A 99 REMARK 465 THR A 100 REMARK 465 PHE A 101 REMARK 465 GLY A 102 REMARK 465 ASN A 103 REMARK 465 PHE A 104 REMARK 465 TRP A 105 REMARK 465 CYS A 106 REMARK 465 GLU A 107 REMARK 465 SER A 165 REMARK 465 PHE A 166 REMARK 465 LEU A 167 REMARK 465 PRO A 168 REMARK 465 ILE A 169 REMARK 465 GLN A 170 REMARK 465 MET A 171 REMARK 465 HIS A 172 REMARK 465 TRP A 173 REMARK 465 TYR A 174 REMARK 465 ARG A 175 REMARK 465 ALA A 176 REMARK 465 THR A 177 REMARK 465 HIS A 178 REMARK 465 GLN A 179 REMARK 465 GLU A 180 REMARK 465 ALA A 181 REMARK 465 ILE A 182 REMARK 465 ASN A 183 REMARK 465 CYS A 184 REMARK 465 TYR A 185 REMARK 465 ALA A 186 REMARK 465 GLU A 187 REMARK 465 GLU A 188 REMARK 465 THR A 189 REMARK 465 CYS A 190 REMARK 465 CYS A 191 REMARK 465 ASP A 192 REMARK 465 PHE A 193 REMARK 465 PHE A 194 REMARK 465 THR A 195 REMARK 465 ASN A 196 REMARK 465 GLN A 197 REMARK 465 ALA A 198 REMARK 465 TYR A 199 REMARK 465 ALA A 200 REMARK 465 ILE A 201 REMARK 465 ALA A 202 REMARK 465 GLN A 243 REMARK 465 ASN A 244 REMARK 465 LEU A 245 REMARK 465 SER A 246 REMARK 465 GLN A 247 REMARK 465 VAL A 248 REMARK 465 GLU A 249 REMARK 465 GLN A 250 REMARK 465 ASP A 251 REMARK 465 GLY A 252 REMARK 465 ARG A 253 REMARK 465 THR A 254 REMARK 465 GLY A 255 REMARK 465 HIS A 256 REMARK 465 GLY A 257 REMARK 465 LEU A 258 REMARK 465 ARG A 259 REMARK 465 ARG A 260 REMARK 465 SER A 261 REMARK 465 SER A 262 REMARK 465 VAL A 292 REMARK 465 ASN A 293 REMARK 465 ILE A 294 REMARK 465 VAL A 295 REMARK 465 HIS A 296 REMARK 465 VAL A 297 REMARK 465 ILE A 298 REMARK 465 GLN A 299 REMARK 465 ASP A 300 REMARK 465 ASN A 301 REMARK 465 LEU A 302 REMARK 465 ILE A 303 REMARK 465 ARG A 304 REMARK 465 LYS A 305 REMARK 465 GLU A 306 REMARK 465 LEU A 347 REMARK 465 LYS A 348 REMARK 465 ALA A 349 REMARK 465 TYR A 350 REMARK 465 GLY A 351 REMARK 465 ASN A 352 REMARK 465 GLY A 353 REMARK 465 TYR A 354 REMARK 465 SER A 355 REMARK 465 SER A 356 REMARK 465 ASN A 357 REMARK 465 GLY A 358 REMARK 465 ASN A 359 REMARK 465 THR A 360 REMARK 465 GLY A 361 REMARK 465 GLU A 362 REMARK 465 GLN A 363 REMARK 465 SER A 364 REMARK 465 GLY A 365 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 MET A 36 CG SD CE REMARK 470 VAL A 39 CG1 CG2 REMARK 470 LEU A 42 CG CD1 CD2 REMARK 470 PHE A 49 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 53 CG CD1 CD2 REMARK 470 ILE A 55 CG1 CG2 CD1 REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 69 CG OD1 ND2 REMARK 470 CYS A 77 SG REMARK 470 ILE A 112 CG1 CG2 CD1 REMARK 470 VAL A 114 CG1 CG2 REMARK 470 SER A 120 OG REMARK 470 GLU A 122 CG CD OE1 OE2 REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 147 CG CD CE NZ REMARK 470 MET A 156 CG SD CE REMARK 470 TYR A 209 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 227 CG CD CE NZ REMARK 470 LYS A 232 CG CD CE NZ REMARK 470 LYS A 263 CG CD CE NZ REMARK 470 MET A 279 CG SD CE REMARK 470 LEU A 287 CG CD1 CD2 REMARK 470 TYR A 308 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE A 309 CG1 CG2 CD1 REMARK 470 PHE A 321 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 324 CG CD1 CD2 REMARK 470 TYR A 326 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE A 332 CG CD1 CD2 CE1 CE2 CZ 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 PHE A 139 -93.57 -88.15 REMARK 500 TYR A 141 82.89 -68.10 REMARK 500 PHE A 208 -59.88 -126.23 REMARK 500 HIS A 241 -73.78 -34.66 REMARK 500 ASN A 318 1.86 -69.14 REMARK 500 CYS A 327 -73.91 -104.35 REMARK 500 SER A 329 -56.29 -153.55 REMARK 500 PRO A 330 -165.72 -104.31 REMARK 500 LEU A 339 -9.08 -58.02 REMARK 500 ARG A 343 -78.83 -34.39 REMARK 500 ARG A 344 -38.56 -141.45 REMARK 500 GLN L 6 81.93 -160.62 REMARK 500 SER L 31 16.91 50.58 REMARK 500 ALA L 51 -34.77 78.95 REMARK 500 ASN L 52 -10.05 -146.28 REMARK 500 SER L 60 1.04 -67.98 REMARK 500 SER L 77 78.07 54.95 REMARK 500 ASP L 82 51.15 -91.87 REMARK 500 ASN L 138 74.63 44.04 REMARK 500 GLN L 156 32.51 -141.40 REMARK 500 SER L 162 131.21 -172.09 REMARK 500 ASN L 212 -70.37 -76.65 REMARK 500 SER H 25 110.13 -163.70 REMARK 500 THR H 30 35.54 -86.89 REMARK 500 SER H 55 -81.38 -77.46 REMARK 500 LYS H 65 -70.42 -46.07 REMARK 500 LYS H 67 -65.79 -99.82 REMARK 500 SER H 75 -70.95 -71.70 REMARK 500 ALA H 92 -175.89 -179.05 REMARK 500 ARG H 98 45.58 -90.17 REMARK 500 LEU H 138 -161.79 -101.14 REMARK 500 PRO H 149 -169.65 -116.60 REMARK 500 SER H 160 -51.87 -139.55 REMARK 500 SER H 172 50.57 72.24 REMARK 500 ASP H 173 -6.96 76.71 REMARK 500 THR H 187 -59.08 -133.12 REMARK 500 PRO H 212 -87.37 -43.74 REMARK 500 CYS H 215 -44.88 110.30 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001