REMARK 2 REMARK 2 RESOLUTION. 1.55 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) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 183666 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.173 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.186 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 9196 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 49.1752 - 4.8148 0.98 6228 324 0.1581 0.1668 REMARK 3 2 4.8148 - 3.8221 1.00 6172 298 0.1408 0.1498 REMARK 3 3 3.8221 - 3.3391 1.00 6105 313 0.1745 0.1792 REMARK 3 4 3.3391 - 3.0338 1.00 6093 309 0.1830 0.1922 REMARK 3 5 3.0338 - 2.8164 1.00 6050 331 0.1815 0.1937 REMARK 3 6 2.8164 - 2.6504 1.00 6037 293 0.1785 0.1974 REMARK 3 7 2.6504 - 2.5176 1.00 6010 323 0.1808 0.1964 REMARK 3 8 2.5176 - 2.4081 1.00 5983 321 0.1786 0.1935 REMARK 3 9 2.4081 - 2.3154 1.00 6032 293 0.1714 0.1887 REMARK 3 10 2.3154 - 2.2355 1.00 5982 327 0.1708 0.1916 REMARK 3 11 2.2355 - 2.1656 0.99 5958 304 0.1655 0.1748 REMARK 3 12 2.1656 - 2.1037 0.99 5954 307 0.1614 0.1908 REMARK 3 13 2.1037 - 2.0483 0.99 5940 302 0.1646 0.1817 REMARK 3 14 2.0483 - 1.9983 0.99 5935 324 0.1715 0.2035 REMARK 3 15 1.9983 - 1.9529 0.99 5926 328 0.1710 0.1863 REMARK 3 16 1.9529 - 1.9113 0.99 5902 316 0.1667 0.1750 REMARK 3 17 1.9113 - 1.8731 0.99 5904 313 0.1639 0.1910 REMARK 3 18 1.8731 - 1.8377 0.99 5922 326 0.1658 0.1832 REMARK 3 19 1.8377 - 1.8049 0.99 5918 292 0.1721 0.1956 REMARK 3 20 1.8049 - 1.7743 0.99 5810 334 0.1815 0.2094 REMARK 3 21 1.7743 - 1.7457 0.99 5919 295 0.1847 0.2188 REMARK 3 22 1.7457 - 1.7188 0.99 5863 307 0.1784 0.1914 REMARK 3 23 1.7188 - 1.6936 0.98 5822 356 0.1841 0.2059 REMARK 3 24 1.6936 - 1.6697 0.98 5854 309 0.1896 0.1991 REMARK 3 25 1.6697 - 1.6471 0.98 5821 325 0.2038 0.2207 REMARK 3 26 1.6471 - 1.6257 0.98 5792 333 0.2150 0.2188 REMARK 3 27 1.6257 - 1.6054 0.93 5539 260 0.2419 0.2638 REMARK 3 28 1.6054 - 1.5861 0.85 5029 241 0.2412 0.2456 REMARK 3 29 1.5861 - 1.5676 0.78 4617 254 0.2478 0.2528 REMARK 3 30 1.5676 - 1.5500 0.73 4353 238 0.2682 0.2935 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) : 0.130 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.020 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.10 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 : 0.009 6900 REMARK 3 ANGLE : 1.263 9437 REMARK 3 CHIRALITY : 0.085 1082 REMARK 3 PLANARITY : 0.007 1193 REMARK 3 DIHEDRAL : 14.166 2495 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain H and resid 1:123 REMARK 3 ORIGIN FOR THE GROUP (A): 35.9710 15.0688 17.0715 REMARK 3 T TENSOR REMARK 3 T11: 0.0826 T22: 0.0926 REMARK 3 T33: 0.1168 T12: 0.0106 REMARK 3 T13: -0.0071 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 0.9358 L22: 0.5403 REMARK 3 L33: 2.7555 L12: -0.0444 REMARK 3 L13: -0.9392 L23: 0.4297 REMARK 3 S TENSOR REMARK 3 S11: -0.0543 S12: 0.0231 S13: 0.0273 REMARK 3 S21: 0.0578 S22: 0.0378 S23: -0.0093 REMARK 3 S31: 0.0867 S32: 0.0351 S33: 0.0198 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain H and resid 124:209 REMARK 3 ORIGIN FOR THE GROUP (A): 33.5976 -4.1702 43.4610 REMARK 3 T TENSOR REMARK 3 T11: 0.2820 T22: 0.3445 REMARK 3 T33: 0.6612 T12: 0.0801 REMARK 3 T13: 0.1823 T23: 0.2446 REMARK 3 L TENSOR REMARK 3 L11: 1.1663 L22: 1.8459 REMARK 3 L33: 1.1998 L12: 0.5326 REMARK 3 L13: -0.2881 L23: 0.2172 REMARK 3 S TENSOR REMARK 3 S11: -0.1698 S12: -0.4579 S13: -0.7533 REMARK 3 S21: -0.2296 S22: -0.2782 S23: -0.9165 REMARK 3 S31: 0.3102 S32: 0.4641 S33: 0.2874 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain L and resid 1:109 REMARK 3 ORIGIN FOR THE GROUP (A): 24.9070 -0.2588 6.5246 REMARK 3 T TENSOR REMARK 3 T11: 0.2354 T22: 0.2026 REMARK 3 T33: 0.1602 T12: -0.0937 REMARK 3 T13: 0.0501 T23: -0.0466 REMARK 3 L TENSOR REMARK 3 L11: 1.3619 L22: 1.8903 REMARK 3 L33: 2.5433 L12: 1.0951 REMARK 3 L13: -0.2797 L23: 0.2507 REMARK 3 S TENSOR REMARK 3 S11: -0.1108 S12: 0.1799 S13: -0.1480 REMARK 3 S21: -0.0069 S22: -0.0221 S23: 0.0950 REMARK 3 S31: 0.6153 S32: -0.3307 S33: 0.0562 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain L and resid 110:209 REMARK 3 ORIGIN FOR THE GROUP (A): 17.3828 -9.3318 43.6578 REMARK 3 T TENSOR REMARK 3 T11: 0.2634 T22: 0.1555 REMARK 3 T33: 0.1867 T12: -0.0303 REMARK 3 T13: 0.0747 T23: 0.0347 REMARK 3 L TENSOR REMARK 3 L11: 2.0608 L22: 2.5878 REMARK 3 L33: 2.9801 L12: 1.2463 REMARK 3 L13: -0.8861 L23: -0.6089 REMARK 3 S TENSOR REMARK 3 S11: -0.2158 S12: -0.0582 S13: -0.2811 REMARK 3 S21: -0.5899 S22: 0.0107 S23: -0.3422 REMARK 3 S31: 0.1403 S32: 0.1153 S33: 0.0953 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain I and resid 1:123 REMARK 3 ORIGIN FOR THE GROUP (A): 54.5971 15.1167 -14.2791 REMARK 3 T TENSOR REMARK 3 T11: 0.0837 T22: 0.0972 REMARK 3 T33: 0.1369 T12: -0.0085 REMARK 3 T13: 0.0003 T23: -0.0115 REMARK 3 L TENSOR REMARK 3 L11: 0.8524 L22: 0.4406 REMARK 3 L33: 2.8973 L12: 0.0409 REMARK 3 L13: -0.7418 L23: -0.2895 REMARK 3 S TENSOR REMARK 3 S11: -0.0542 S12: -0.0534 S13: 0.0417 REMARK 3 S21: -0.0464 S22: 0.0336 S23: -0.0003 REMARK 3 S31: 0.0593 S32: 0.0029 S33: 0.0236 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain I and resid 124:209 REMARK 3 ORIGIN FOR THE GROUP (A): 57.8786 -6.0149 -40.1282 REMARK 3 T TENSOR REMARK 3 T11: 0.1979 T22: 0.1634 REMARK 3 T33: 0.3646 T12: 0.0087 REMARK 3 T13: 0.0858 T23: -0.0357 REMARK 3 L TENSOR REMARK 3 L11: 1.2998 L22: 3.7330 REMARK 3 L33: 2.0675 L12: -0.1493 REMARK 3 L13: 0.2058 L23: 0.3809 REMARK 3 S TENSOR REMARK 3 S11: -0.0169 S12: 0.0353 S13: -0.2866 REMARK 3 S21: 0.1526 S22: -0.1129 S23: 0.8245 REMARK 3 S31: 0.2873 S32: -0.1779 S33: 0.0650 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain M and resid 1:109 REMARK 3 ORIGIN FOR THE GROUP (A): 66.3631 0.4093 -3.6137 REMARK 3 T TENSOR REMARK 3 T11: 0.2080 T22: 0.2526 REMARK 3 T33: 0.1630 T12: 0.1029 REMARK 3 T13: 0.0265 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 1.2147 L22: 1.6113 REMARK 3 L33: 2.8445 L12: -1.0709 REMARK 3 L13: -0.2158 L23: 0.0415 REMARK 3 S TENSOR REMARK 3 S11: -0.0672 S12: -0.1639 S13: -0.0629 REMARK 3 S21: 0.0655 S22: -0.0124 S23: -0.1367 REMARK 3 S31: 0.5389 S32: 0.4542 S33: 0.0265 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain M and resid 110:209 REMARK 3 ORIGIN FOR THE GROUP (A): 73.5848 -9.5158 -40.5857 REMARK 3 T TENSOR REMARK 3 T11: 0.1794 T22: 0.1859 REMARK 3 T33: 0.1463 T12: 0.0933 REMARK 3 T13: 0.0254 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 1.3159 L22: 1.8327 REMARK 3 L33: 4.0362 L12: -0.5943 REMARK 3 L13: -0.4294 L23: 0.3641 REMARK 3 S TENSOR REMARK 3 S11: -0.1815 S12: -0.1563 S13: -0.0701 REMARK 3 S21: 0.3290 S22: 0.1794 S23: 0.0680 REMARK 3 S31: 0.1122 S32: 0.1833 S33: -0.0117 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 4M5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-13. REMARK 100 THE RCSB ID CODE IS RCSB081507. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-NOV-12 REMARK 200 TEMPERATURE (KELVIN) : 77 REMARK 200 PH : 8 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-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED REMARK 200 SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 183997 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 7.300 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : 0.04600 REMARK 200 FOR THE DATA SET : 21.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57 REMARK 200 COMPLETENESS FOR SHELL (%) : 72.5 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.91000 REMARK 200 R SYM FOR SHELL (I) : 0.91000 REMARK 200 FOR SHELL : 1.800 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: PDB ENTRY 3MLY CHAINS H AND L REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 11% PEG3350, PH REMARK 280 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 45.28650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.16650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.99150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.16650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.28650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.99150 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M 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 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 REMARK 465 LYS I 214 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 HIS I 217 REMARK 465 HIS I 218 REMARK 465 HIS I 219 REMARK 465 HIS I 220 REMARK 465 HIS I 221 REMARK 465 HIS I 222 REMARK 465 GLU M 210 REMARK 465 CYS M 211 REMARK 465 SER M 212 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 OG SER H 70 O4 PG4 H 305 2.12 REMARK 500 O4 PEG I 302 O HOH I 575 2.14 REMARK 500 OE1 GLU H 46 O HOH H 536 2.14 REMARK 500 O HOH H 460 O HOH H 507 2.15 REMARK 500 O5 PG4 H 305 O HOH H 472 2.18 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 SER H 15 -4.66 79.26 REMARK 500 TYR H 33 158.39 77.35 REMARK 500 PRO L 40 122.66 -39.70 REMARK 500 ASP L 51 -45.31 72.30 REMARK 500 ASP L 151 -114.61 53.63 REMARK 500 SER L 168 -16.28 75.41 REMARK 500 ASN L 170 -2.18 76.44 REMARK 500 SER I 15 -9.75 84.82 REMARK 500 TYR I 33 158.43 73.74 REMARK 500 ASP I 144 60.45 65.62 REMARK 500 ASP M 51 -45.18 73.48 REMARK 500 ASP M 151 -114.09 50.96 REMARK 500 ASN M 170 -2.74 74.20 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 PEG H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 H 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG M 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG M 302 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4M4Y RELATED DB: PDB REMARK 900 RELATED ID: 4M5Z RELATED DB: PDB