Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE 05-AUG-14 4U97 TITLE CRYSTAL STRUCTURE OF ASYMMETRIC IRAK4 DIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE 4; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: IRAK-4,RENAL CARCINOMA ANTIGEN NY-REN-64; COMPND 5 EC: 2.7.11.1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: IRAK4; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS KINASE, AUTOPHOSPHORYLATION, DIMER, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR R.FERRAO,H.WU REVDAT 2 01-OCT-14 4U97 1 JRNL REVDAT 1 24-SEP-14 4U97 0 JRNL AUTH R.FERRAO,H.ZHOU,Y.SHAN,Q.LIU,Q.LI,D.E.SHAW,X.LI,H.WU JRNL TITL IRAK4 DIMERIZATION AND TRANS-AUTOPHOSPHORYLATION ARE INDUCED JRNL TITL 2 BY MYDDOSOME ASSEMBLY. JRNL REF MOL.CELL V. 55 891 2014 JRNL REFN ISSN 1097-2765 JRNL PMID 25201411 JRNL DOI 10.1016/J.MOLCEL.2014.08.006 REMARK 2 REMARK 2 RESOLUTION. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.81 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 29121 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.870 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 41.8124 - 6.3799 1.00 2186 161 0.2171 0.2428 REMARK 3 2 6.3799 - 5.0667 1.00 2011 149 0.2030 0.2701 REMARK 3 3 5.0667 - 4.4270 1.00 1984 146 0.1614 0.2011 REMARK 3 4 4.4270 - 4.0226 1.00 1945 144 0.1582 0.2115 REMARK 3 5 4.0226 - 3.7345 1.00 1941 142 0.1730 0.2055 REMARK 3 6 3.7345 - 3.5144 1.00 1913 142 0.1935 0.2245 REMARK 3 7 3.5144 - 3.3385 1.00 1925 141 0.2104 0.2898 REMARK 3 8 3.3385 - 3.1932 1.00 1903 141 0.2328 0.2742 REMARK 3 9 3.1932 - 3.0704 1.00 1911 141 0.2327 0.3110 REMARK 3 10 3.0704 - 2.9644 1.00 1885 138 0.2254 0.2853 REMARK 3 11 2.9644 - 2.8718 1.00 1888 140 0.2506 0.2811 REMARK 3 12 2.8718 - 2.7897 1.00 1893 139 0.2416 0.3240 REMARK 3 13 2.7897 - 2.7163 1.00 1872 138 0.2438 0.3275 REMARK 3 14 2.7163 - 2.6500 1.00 1864 138 0.2707 0.3173 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) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.970 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 : 0.008 4430 REMARK 3 ANGLE : 1.111 5994 REMARK 3 CHIRALITY : 0.039 671 REMARK 3 PLANARITY : 0.005 753 REMARK 3 DIHEDRAL : 14.712 1624 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 166 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.5052 10.9806 26.4227 REMARK 3 T TENSOR REMARK 3 T11: 1.3100 T22: 1.0200 REMARK 3 T33: 0.9180 T12: 0.4622 REMARK 3 T13: 0.0094 T23: 0.1943 REMARK 3 L TENSOR REMARK 3 L11: 5.2449 L22: 0.1504 REMARK 3 L33: 2.7248 L12: -0.3081 REMARK 3 L13: 0.3042 L23: -0.6113 REMARK 3 S TENSOR REMARK 3 S11: -0.3311 S12: 0.0619 S13: -1.0817 REMARK 3 S21: -0.3603 S22: -0.1654 S23: -0.6251 REMARK 3 S31: 1.5483 S32: 0.5417 S33: 0.1664 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 198 THROUGH 226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 90.8955 14.9537 27.5354 REMARK 3 T TENSOR REMARK 3 T11: 0.9673 T22: 0.9186 REMARK 3 T33: 0.8826 T12: 0.5081 REMARK 3 T13: -0.0411 T23: 0.3176 REMARK 3 L TENSOR REMARK 3 L11: 0.9400 L22: 2.9489 REMARK 3 L33: 1.7191 L12: -0.0474 REMARK 3 L13: -0.2773 L23: -0.4281 REMARK 3 S TENSOR REMARK 3 S11: 0.0700 S12: -0.4065 S13: -0.5956 REMARK 3 S21: -0.2339 S22: -0.0787 S23: -0.2328 REMARK 3 S31: 0.8090 S32: 0.7163 S33: 0.7689 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 227 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 102.2327 25.3167 24.4977 REMARK 3 T TENSOR REMARK 3 T11: 0.5645 T22: 1.4888 REMARK 3 T33: 1.1601 T12: 0.3555 REMARK 3 T13: 0.0527 T23: 0.4536 REMARK 3 L TENSOR REMARK 3 L11: 1.1722 L22: 1.1768 REMARK 3 L33: 1.9344 L12: 0.3764 REMARK 3 L13: -0.6183 L23: 0.1774 REMARK 3 S TENSOR REMARK 3 S11: 0.1747 S12: -0.3063 S13: -0.5380 REMARK 3 S21: -0.1780 S22: -0.3252 S23: -1.1383 REMARK 3 S31: 0.5930 S32: 0.8929 S33: 0.5106 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 350 ) REMARK 3 ORIGIN FOR THE GROUP (A): 90.9866 31.5539 23.4117 REMARK 3 T TENSOR REMARK 3 T11: 0.1650 T22: 0.9497 REMARK 3 T33: 0.4751 T12: 0.1268 REMARK 3 T13: 0.0196 T23: 0.1746 REMARK 3 L TENSOR REMARK 3 L11: 2.6467 L22: 2.9210 REMARK 3 L33: 2.4749 L12: 0.2392 REMARK 3 L13: -0.3002 L23: 0.2320 REMARK 3 S TENSOR REMARK 3 S11: 0.1851 S12: -0.4209 S13: -0.2360 REMARK 3 S21: -0.3680 S22: -0.2843 S23: -0.7998 REMARK 3 S31: 0.3887 S32: 1.0585 S33: -0.0286 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 351 THROUGH 395 ) REMARK 3 ORIGIN FOR THE GROUP (A): 87.6108 38.2265 10.3592 REMARK 3 T TENSOR REMARK 3 T11: 0.2543 T22: 0.7473 REMARK 3 T33: 0.3758 T12: 0.1415 REMARK 3 T13: 0.1295 T23: 0.1246 REMARK 3 L TENSOR REMARK 3 L11: 4.6496 L22: 1.8008 REMARK 3 L33: 0.8126 L12: -0.5063 REMARK 3 L13: -1.3664 L23: 0.3510 REMARK 3 S TENSOR REMARK 3 S11: 0.2602 S12: 0.6764 S13: -0.1440 REMARK 3 S21: -0.5445 S22: -0.3895 S23: -0.2658 REMARK 3 S31: 0.2424 S32: 0.4452 S33: -0.1457 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 396 THROUGH 413 ) REMARK 3 ORIGIN FOR THE GROUP (A): 78.5720 49.7272 9.1607 REMARK 3 T TENSOR REMARK 3 T11: 0.4883 T22: 0.7363 REMARK 3 T33: 0.5344 T12: 0.1329 REMARK 3 T13: 0.1914 T23: 0.1196 REMARK 3 L TENSOR REMARK 3 L11: 7.9392 L22: 6.7848 REMARK 3 L33: 4.0300 L12: -1.0029 REMARK 3 L13: -0.7462 L23: -0.7030 REMARK 3 S TENSOR REMARK 3 S11: 1.0998 S12: 0.6291 S13: 1.4422 REMARK 3 S21: -0.8642 S22: -0.4760 S23: 0.0161 REMARK 3 S31: -1.0339 S32: 0.3237 S33: -0.2778 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 414 THROUGH 458 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.0282 48.6804 19.9053 REMARK 3 T TENSOR REMARK 3 T11: 0.3507 T22: 0.7227 REMARK 3 T33: 0.5264 T12: -0.1134 REMARK 3 T13: 0.1859 T23: 0.0176 REMARK 3 L TENSOR REMARK 3 L11: 5.6777 L22: 2.5271 REMARK 3 L33: 1.3402 L12: 0.9777 REMARK 3 L13: -0.1091 L23: 0.1560 REMARK 3 S TENSOR REMARK 3 S11: 0.5809 S12: -0.5324 S13: 0.8506 REMARK 3 S21: -0.1393 S22: -0.3391 S23: -0.5654 REMARK 3 S31: -0.8984 S32: 0.5427 S33: -0.2017 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 166 THROUGH 177 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.6256 15.7454 -35.5114 REMARK 3 T TENSOR REMARK 3 T11: 1.3495 T22: 0.8615 REMARK 3 T33: 1.2596 T12: -0.4301 REMARK 3 T13: -0.4517 T23: 0.0310 REMARK 3 L TENSOR REMARK 3 L11: 5.4888 L22: 3.1822 REMARK 3 L33: 8.9107 L12: -4.0519 REMARK 3 L13: -3.3915 L23: 3.6366 REMARK 3 S TENSOR REMARK 3 S11: 0.4372 S12: 0.1035 S13: -0.7613 REMARK 3 S21: 0.1239 S22: -0.7421 S23: 2.8464 REMARK 3 S31: 2.5424 S32: -1.4548 S33: 0.0530 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 100.6248 14.9463 -28.8418 REMARK 3 T TENSOR REMARK 3 T11: 1.1323 T22: 0.5164 REMARK 3 T33: 0.6187 T12: 0.0088 REMARK 3 T13: 0.0554 T23: -0.0731 REMARK 3 L TENSOR REMARK 3 L11: 5.1644 L22: 9.3128 REMARK 3 L33: 7.0921 L12: 2.8012 REMARK 3 L13: 3.4051 L23: 1.9680 REMARK 3 S TENSOR REMARK 3 S11: -0.3852 S12: 0.0084 S13: -1.5784 REMARK 3 S21: -0.2899 S22: 0.4865 S23: -0.3075 REMARK 3 S31: 3.2274 S32: -0.0601 S33: -0.2495 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 185 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.6922 21.9053 -24.7926 REMARK 3 T TENSOR REMARK 3 T11: 0.7071 T22: 0.8066 REMARK 3 T33: 0.6407 T12: -0.0604 REMARK 3 T13: 0.0615 T23: 0.1312 REMARK 3 L TENSOR REMARK 3 L11: 6.4653 L22: 5.5760 REMARK 3 L33: 5.4952 L12: -5.9848 REMARK 3 L13: -5.9496 L23: 5.5080 REMARK 3 S TENSOR REMARK 3 S11: -1.1153 S12: -0.9434 S13: -1.0121 REMARK 3 S21: 1.1429 S22: 0.2802 S23: 0.4827 REMARK 3 S31: 1.9912 S32: -0.4939 S33: 0.9193 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 92.7031 21.9118 -31.4286 REMARK 3 T TENSOR REMARK 3 T11: 0.6654 T22: 0.6885 REMARK 3 T33: 0.5917 T12: -0.3084 REMARK 3 T13: -0.0811 T23: 0.1240 REMARK 3 L TENSOR REMARK 3 L11: 6.0063 L22: 3.8574 REMARK 3 L33: 3.4349 L12: -1.6979 REMARK 3 L13: -1.0292 L23: -0.4305 REMARK 3 S TENSOR REMARK 3 S11: -0.1668 S12: 0.4159 S13: 0.4239 REMARK 3 S21: -1.0561 S22: 0.7728 S23: 1.4869 REMARK 3 S31: 2.0146 S32: -1.0910 S33: -0.3583 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 80.8660 29.5957 -24.6522 REMARK 3 T TENSOR REMARK 3 T11: 0.4881 T22: 1.6943 REMARK 3 T33: 1.1061 T12: -0.0562 REMARK 3 T13: 0.0131 T23: 0.1252 REMARK 3 L TENSOR REMARK 3 L11: 0.1136 L22: 5.7254 REMARK 3 L33: 4.5045 L12: -0.7210 REMARK 3 L13: 0.1002 L23: 1.6774 REMARK 3 S TENSOR REMARK 3 S11: 0.1545 S12: 0.1149 S13: -0.2942 REMARK 3 S21: 0.3297 S22: -0.1019 S23: 2.3000 REMARK 3 S31: 0.7246 S32: -1.7735 S33: -0.2856 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 324 ) REMARK 3 ORIGIN FOR THE GROUP (A): 93.8606 37.1519 -24.8345 REMARK 3 T TENSOR REMARK 3 T11: 0.1317 T22: 0.8627 REMARK 3 T33: 0.3660 T12: 0.0994 REMARK 3 T13: 0.0829 T23: 0.1178 REMARK 3 L TENSOR REMARK 3 L11: 2.7691 L22: 2.4848 REMARK 3 L33: 2.4751 L12: -0.4437 REMARK 3 L13: -0.8976 L23: -0.2474 REMARK 3 S TENSOR REMARK 3 S11: -0.0392 S12: 0.1504 S13: -0.1206 REMARK 3 S21: -0.1505 S22: 0.2481 S23: 0.5098 REMARK 3 S31: 0.0356 S32: -1.1099 S33: -0.1111 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 354 ) REMARK 3 ORIGIN FOR THE GROUP (A): 92.2186 31.4359 -7.9630 REMARK 3 T TENSOR REMARK 3 T11: 0.4535 T22: 1.0993 REMARK 3 T33: 0.8415 T12: 0.0584 REMARK 3 T13: 0.1221 T23: 0.2241 REMARK 3 L TENSOR REMARK 3 L11: 0.9617 L22: 1.5848 REMARK 3 L33: 1.1987 L12: -0.8696 REMARK 3 L13: -0.7551 L23: 1.3771 REMARK 3 S TENSOR REMARK 3 S11: -0.0341 S12: -0.3660 S13: -1.0016 REMARK 3 S21: 0.5702 S22: 0.5160 S23: 0.4997 REMARK 3 S31: 0.5173 S32: -0.7458 S33: -0.6509 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 355 THROUGH 458 ) REMARK 3 ORIGIN FOR THE GROUP (A): 98.3666 47.3032 -10.2223 REMARK 3 T TENSOR REMARK 3 T11: 0.3805 T22: 0.8549 REMARK 3 T33: 0.3401 T12: 0.2150 REMARK 3 T13: 0.2520 T23: 0.0013 REMARK 3 L TENSOR REMARK 3 L11: 4.4286 L22: 2.0469 REMARK 3 L33: 3.2349 L12: -0.1651 REMARK 3 L13: -1.7526 L23: -0.8660 REMARK 3 S TENSOR REMARK 3 S11: 0.2190 S12: -0.6282 S13: 0.3746 REMARK 3 S21: 0.5685 S22: -0.0333 S23: 0.1009 REMARK 3 S31: -1.1294 S32: -0.4007 S33: -0.5274 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 4U97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-14. REMARK 100 THE DEPOSITION ID IS D_1000203028. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUN-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X29A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29127 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650 REMARK 200 RESOLUTION RANGE LOW (A) : 41.810 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 83.20 REMARK 200 R MERGE (I) : 0.12100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> 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: COOT REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SET UP AT 10 MG/ML WITH STAUROSPORINE REMARK 280 AT A 2:1 MOLAR RATIO. MIXED WITH EQUAL VOLUMES 1.6-1.9 M REMARK 280 AMMONIUM SULFATE, 100 MM HEPES-NAOH AT PH7. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 140.52667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 281.05333 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 210.79000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 351.31667 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.26333 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 140.52667 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 281.05333 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 351.31667 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 210.79000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 70.26333 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 609 LIES ON A SPECIAL POSITION. 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 149 REMARK 465 ALA A 150 REMARK 465 MET A 151 REMARK 465 GLY A 152 REMARK 465 SER A 153 REMARK 465 GLU A 154 REMARK 465 ASN A 155 REMARK 465 LYS A 156 REMARK 465 SER A 157 REMARK 465 LEU A 158 REMARK 465 GLU A 159 REMARK 465 VAL A 160 REMARK 465 SER A 161 REMARK 465 ASP A 162 REMARK 465 THR A 163 REMARK 465 ARG A 164 REMARK 465 PHE A 165 REMARK 465 MET A 218 REMARK 465 VAL A 219 REMARK 465 ASP A 220 REMARK 465 ILE A 221 REMARK 465 THR A 222 REMARK 465 THR A 223 REMARK 465 GLU A 224 REMARK 465 GLU A 225 REMARK 465 SER A 253 REMARK 465 ASP A 254 REMARK 465 GLY A 255 REMARK 465 ASP A 256 REMARK 465 ASP A 257 REMARK 465 ARG A 334 REMARK 465 ALA A 335 REMARK 465 SER A 336 REMARK 465 GLU A 337 REMARK 465 LYS A 338 REMARK 465 PHE A 339 REMARK 465 ALA A 340 REMARK 465 GLN A 341 REMARK 465 ALA A 459 REMARK 465 SER A 460 REMARK 465 GLY B 149 REMARK 465 ALA B 150 REMARK 465 MET B 151 REMARK 465 GLY B 152 REMARK 465 SER B 153 REMARK 465 GLU B 154 REMARK 465 ASN B 155 REMARK 465 LYS B 156 REMARK 465 SER B 157 REMARK 465 LEU B 158 REMARK 465 GLU B 159 REMARK 465 VAL B 160 REMARK 465 SER B 161 REMARK 465 ASP B 162 REMARK 465 THR B 163 REMARK 465 ARG B 164 REMARK 465 PHE B 165 REMARK 465 MET B 218 REMARK 465 VAL B 219 REMARK 465 ASP B 220 REMARK 465 ILE B 221 REMARK 465 THR B 222 REMARK 465 THR B 223 REMARK 465 GLU B 224 REMARK 465 GLU B 225 REMARK 465 GLY B 255 REMARK 465 ASP B 256 REMARK 465 ASP B 257 REMARK 465 GLY B 331 REMARK 465 LEU B 332 REMARK 465 ALA B 333 REMARK 465 ARG B 334 REMARK 465 ALA B 335 REMARK 465 SER B 336 REMARK 465 GLU B 337 REMARK 465 LYS B 338 REMARK 465 PHE B 339 REMARK 465 ALA B 340 REMARK 465 GLN B 341 REMARK 465 THR B 342 REMARK 465 ALA B 459 REMARK 465 SER B 460 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 O HOH A 613 O HOH A 635 1.73 REMARK 500 O HOH B 624 O HOH B 628 1.81 REMARK 500 O THR B 209 O HOH B 625 1.96 REMARK 500 O HOH B 636 O HOH B 637 2.02 REMARK 500 O LEU A 274 O HOH A 628 2.02 REMARK 500 O HOH B 619 O HOH B 620 2.05 REMARK 500 OE1 GLN B 394 O HOH B 639 2.06 REMARK 500 N GLU B 389 O HOH B 612 2.09 REMARK 500 NH1 ARG A 273 OG1 THR A 280 2.12 REMARK 500 O HOH A 621 O HOH A 625 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 607 O HOH B 606 6545 2.06 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 ASN A 206 -130.14 51.10 REMARK 500 ASN A 311 40.27 -145.70 REMARK 500 PHE A 330 30.58 -75.86 REMARK 500 GLU A 406 17.34 56.18 REMARK 500 LYS A 417 42.06 -76.11 REMARK 500 ASN B 178 51.34 71.11 REMARK 500 ARG B 310 -13.24 83.45 REMARK 500 ASN B 311 33.21 -142.68 REMARK 500 MET B 344 -148.38 -103.08 REMARK 500 THR B 351 91.30 -64.15 REMARK 500 LYS B 417 36.92 -88.08 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 STU A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue STU B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 504 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4U9A RELATED DB: PDB DBREF 4U97 A 154 460 UNP Q9NWZ3 IRAK4_HUMAN 154 460 DBREF 4U97 B 154 460 UNP Q9NWZ3 IRAK4_HUMAN 154 460 SEQADV 4U97 GLY A 149 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 ALA A 150 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 MET A 151 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 GLY A 152 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 SER A 153 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 ASN A 311 UNP Q9NWZ3 ASP 311 ENGINEERED MUTATION SEQADV 4U97 GLY B 149 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 ALA B 150 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 MET B 151 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 GLY B 152 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 SER B 153 UNP Q9NWZ3 EXPRESSION TAG SEQADV 4U97 ASN B 311 UNP Q9NWZ3 ASP 311 ENGINEERED MUTATION SEQRES 1 A 312 GLY ALA MET GLY SER GLU ASN LYS SER LEU GLU VAL SER SEQRES 2 A 312 ASP THR ARG PHE HIS SER PHE SER PHE TYR GLU LEU LYS SEQRES 3 A 312 ASN VAL THR ASN ASN PHE ASP GLU ARG PRO ILE SER VAL SEQRES 4 A 312 GLY GLY ASN LYS MET GLY GLU GLY GLY PHE GLY VAL VAL SEQRES 5 A 312 TYR LYS GLY TYR VAL ASN ASN THR THR VAL ALA VAL LYS SEQRES 6 A 312 LYS LEU ALA ALA MET VAL ASP ILE THR THR GLU GLU LEU SEQRES 7 A 312 LYS GLN GLN PHE ASP GLN GLU ILE LYS VAL MET ALA LYS SEQRES 8 A 312 CYS GLN HIS GLU ASN LEU VAL GLU LEU LEU GLY PHE SER SEQRES 9 A 312 SER ASP GLY ASP ASP LEU CYS LEU VAL TYR VAL TYR MET SEQRES 10 A 312 PRO ASN GLY SER LEU LEU ASP ARG LEU SER CYS LEU ASP SEQRES 11 A 312 GLY THR PRO PRO LEU SER TRP HIS MET ARG CYS LYS ILE SEQRES 12 A 312 ALA GLN GLY ALA ALA ASN GLY ILE ASN PHE LEU HIS GLU SEQRES 13 A 312 ASN HIS HIS ILE HIS ARG ASN ILE LYS SER ALA ASN ILE SEQRES 14 A 312 LEU LEU ASP GLU ALA PHE THR ALA LYS ILE SER ASP PHE SEQRES 15 A 312 GLY LEU ALA ARG ALA SER GLU LYS PHE ALA GLN THR VAL SEQRES 16 A 312 MET THR SER ARG ILE VAL GLY THR THR ALA TYR MET ALA SEQRES 17 A 312 PRO GLU ALA LEU ARG GLY GLU ILE THR PRO LYS SER ASP SEQRES 18 A 312 ILE TYR SER PHE GLY VAL VAL LEU LEU GLU ILE ILE THR SEQRES 19 A 312 GLY LEU PRO ALA VAL ASP GLU HIS ARG GLU PRO GLN LEU SEQRES 20 A 312 LEU LEU ASP ILE LYS GLU GLU ILE GLU ASP GLU GLU LYS SEQRES 21 A 312 THR ILE GLU ASP TYR ILE ASP LYS LYS MET ASN ASP ALA SEQRES 22 A 312 ASP SER THR SER VAL GLU ALA MET TYR SER VAL ALA SER SEQRES 23 A 312 GLN CYS LEU HIS GLU LYS LYS ASN LYS ARG PRO ASP ILE SEQRES 24 A 312 LYS LYS VAL GLN GLN LEU LEU GLN GLU MET THR ALA SER SEQRES 1 B 312 GLY ALA MET GLY SER GLU ASN LYS SER LEU GLU VAL SER SEQRES 2 B 312 ASP THR ARG PHE HIS SER PHE SER PHE TYR GLU LEU LYS SEQRES 3 B 312 ASN VAL THR ASN ASN PHE ASP GLU ARG PRO ILE SER VAL SEQRES 4 B 312 GLY GLY ASN LYS MET GLY GLU GLY GLY PHE GLY VAL VAL SEQRES 5 B 312 TYR LYS GLY TYR VAL ASN ASN THR THR VAL ALA VAL LYS SEQRES 6 B 312 LYS LEU ALA ALA MET VAL ASP ILE THR THR GLU GLU LEU SEQRES 7 B 312 LYS GLN GLN PHE ASP GLN GLU ILE LYS VAL MET ALA LYS SEQRES 8 B 312 CYS GLN HIS GLU ASN LEU VAL GLU LEU LEU GLY PHE SER SEQRES 9 B 312 SER ASP GLY ASP ASP LEU CYS LEU VAL TYR VAL TYR MET SEQRES 10 B 312 PRO ASN GLY SER LEU LEU ASP ARG LEU SER CYS LEU ASP SEQRES 11 B 312 GLY THR PRO PRO LEU SER TRP HIS MET ARG CYS LYS ILE SEQRES 12 B 312 ALA GLN GLY ALA ALA ASN GLY ILE ASN PHE LEU HIS GLU SEQRES 13 B 312 ASN HIS HIS ILE HIS ARG ASN ILE LYS SER ALA ASN ILE SEQRES 14 B 312 LEU LEU ASP GLU ALA PHE THR ALA LYS ILE SER ASP PHE SEQRES 15 B 312 GLY LEU ALA ARG ALA SER GLU LYS PHE ALA GLN THR VAL SEQRES 16 B 312 MET THR SER ARG ILE VAL GLY THR THR ALA TYR MET ALA SEQRES 17 B 312 PRO GLU ALA LEU ARG GLY GLU ILE THR PRO LYS SER ASP SEQRES 18 B 312 ILE TYR SER PHE GLY VAL VAL LEU LEU GLU ILE ILE THR SEQRES 19 B 312 GLY LEU PRO ALA VAL ASP GLU HIS ARG GLU PRO GLN LEU SEQRES 20 B 312 LEU LEU ASP ILE LYS GLU GLU ILE GLU ASP GLU GLU LYS SEQRES 21 B 312 THR ILE GLU ASP TYR ILE ASP LYS LYS MET ASN ASP ALA SEQRES 22 B 312 ASP SER THR SER VAL GLU ALA MET TYR SER VAL ALA SER SEQRES 23 B 312 GLN CYS LEU HIS GLU LYS LYS ASN LYS ARG PRO ASP ILE SEQRES 24 B 312 LYS LYS VAL GLN GLN LEU LEU GLN GLU MET THR ALA SER HET STU A 501 35 HET STU B 501 35 HET SO4 B 502 5 HET SO4 B 503 5 HET SO4 B 504 5 HETNAM STU STAUROSPORINE HETNAM SO4 SULFATE ION FORMUL 3 STU 2(C28 H26 N4 O3) FORMUL 5 SO4 3(O4 S 2-) FORMUL 8 HOH *97(H2 O) HELIX 1 AA1 SER A 169 THR A 177 1 9 HELIX 2 AA2 PRO A 184 GLY A 188 5 5 HELIX 3 AA3 LYS A 227 CYS A 240 1 14 HELIX 4 AA4 SER A 269 SER A 275 1 7 HELIX 5 AA5 CYS A 276 THR A 280 5 5 HELIX 6 AA6 SER A 284 ASN A 305 1 22 HELIX 7 AA7 LYS A 313 ALA A 315 5 3 HELIX 8 AA8 ALA A 353 MET A 355 5 3 HELIX 9 AA9 ALA A 356 GLY A 362 1 7 HELIX 10 AB1 THR A 365 GLY A 383 1 19 HELIX 11 AB2 LEU A 395 LEU A 397 5 3 HELIX 12 AB3 ASP A 398 ASP A 405 1 8 HELIX 13 AB4 THR A 409 ILE A 414 1 6 HELIX 14 AB5 ASP A 422 LEU A 437 1 16 HELIX 15 AB6 LYS A 440 ARG A 444 5 5 HELIX 16 AB7 ASP A 446 MET A 457 1 12 HELIX 17 AB8 SER B 169 VAL B 176 1 8 HELIX 18 AB9 PRO B 184 GLY B 188 5 5 HELIX 19 AC1 LYS B 227 CYS B 240 1 14 HELIX 20 AC2 SER B 269 SER B 275 1 7 HELIX 21 AC3 CYS B 276 THR B 280 5 5 HELIX 22 AC4 SER B 284 ASN B 305 1 22 HELIX 23 AC5 ALA B 356 GLY B 362 1 7 HELIX 24 AC6 THR B 365 GLY B 383 1 19 HELIX 25 AC7 LEU B 395 LEU B 397 5 3 HELIX 26 AC8 ASP B 398 ASP B 405 1 8 HELIX 27 AC9 ILE B 410 ILE B 414 5 5 HELIX 28 AD1 ASP B 422 LEU B 437 1 16 HELIX 29 AD2 LYS B 440 ARG B 444 5 5 HELIX 30 AD3 ASP B 446 MET B 457 1 12 SHEET 1 AA1 5 LYS A 191 GLY A 195 0 SHEET 2 AA1 5 GLY A 198 VAL A 205 -1 O VAL A 200 N MET A 192 SHEET 3 AA1 5 THR A 208 LEU A 215 -1 O VAL A 212 N TYR A 201 SHEET 4 AA1 5 CYS A 259 VAL A 263 -1 O LEU A 260 N LYS A 213 SHEET 5 AA1 5 LEU A 248 PHE A 251 -1 N LEU A 249 O VAL A 261 SHEET 1 AA2 2 ILE A 317 LEU A 319 0 SHEET 2 AA2 2 ALA A 325 ILE A 327 -1 O LYS A 326 N LEU A 318 SHEET 1 AA3 2 VAL A 349 THR A 351 0 SHEET 2 AA3 2 THR B 345 ARG B 347 -1 O SER B 346 N GLY A 350 SHEET 1 AA4 5 LYS B 191 GLY B 195 0 SHEET 2 AA4 5 GLY B 198 TYR B 204 -1 O VAL B 200 N MET B 192 SHEET 3 AA4 5 THR B 209 LEU B 215 -1 O VAL B 212 N TYR B 201 SHEET 4 AA4 5 CYS B 259 VAL B 263 -1 O TYR B 262 N ALA B 211 SHEET 5 AA4 5 LEU B 248 SER B 252 -1 N LEU B 249 O VAL B 261 SHEET 1 AA5 2 ILE B 317 LEU B 319 0 SHEET 2 AA5 2 ALA B 325 ILE B 327 -1 O LYS B 326 N LEU B 318 CISPEP 1 GLU A 392 PRO A 393 0 -0.80 CISPEP 2 GLU B 392 PRO B 393 0 0.64 SITE 1 AC1 13 MET A 192 GLY A 193 GLU A 194 GLY A 195 SITE 2 AC1 13 VAL A 200 ALA A 211 VAL A 263 TYR A 264 SITE 3 AC1 13 MET A 265 ALA A 315 ASN A 316 LEU A 318 SITE 4 AC1 13 SER A 328 SITE 1 AC2 15 MET B 192 GLY B 193 GLU B 194 GLY B 195 SITE 2 AC2 15 VAL B 200 ALA B 211 VAL B 263 TYR B 264 SITE 3 AC2 15 MET B 265 GLY B 268 ALA B 315 ASN B 316 SITE 4 AC2 15 LEU B 318 SER B 328 SO4 B 503 SITE 1 AC3 4 LYS A 313 HOH A 636 THR B 345 HOH B 621 SITE 1 AC4 3 ALA B 315 STU B 501 HOH B 642 SITE 1 AC5 3 THR B 365 LYS B 367 LYS B 441 CRYST1 87.580 87.580 421.580 90.00 90.00 120.00 P 61 2 2 24 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011418 0.006592 0.000000 0.00000 SCALE2 0.000000 0.013185 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002372 0.00000 ATOM 1 N HIS A 166 103.927 18.304 33.313 1.00 93.14 N ANISOU 1 N HIS A 166 9597 14700 11094 5582 -784 3662 N ATOM 2 CA HIS A 166 103.552 17.037 33.933 1.00 94.41 C ANISOU 2 CA HIS A 166 9972 14726 11175 5777 -657 3754 C ATOM 3 C HIS A 166 103.279 15.955 32.890 1.00 95.43 C ANISOU 3 C HIS A 166 10398 14594 11265 6036 -408 3810 C ATOM 4 O HIS A 166 102.945 16.255 31.749 1.00 94.24 O ANISOU 4 O HIS A 166 10330 14360 11117 6013 -370 3724 O ATOM 5 CB HIS A 166 102.325 17.215 34.827 1.00 92.29 C ANISOU 5 CB HIS A 166 9783 14398 10885 5577 -839 3634 C ATOM 6 CG HIS A 166 102.002 16.012 35.665 1.00 93.90 C ANISOU 6 CG HIS A 166 10148 14513 11018 5742 -742 3767 C ATOM 7 ND1 HIS A 166 101.349 14.906 35.164 1.00 94.51 N ANISOU 7 ND1 HIS A 166 10547 14290 11072 5918 -569 3829 N ATOM 8 CD2 HIS A 166 102.232 15.749 36.975 1.00 98.19 C ANISOU 8 CD2 HIS A 166 10568 15225 11515 5755 -795 3862 C ATOM 9 CE1 HIS A 166 101.195 14.012 36.126 1.00 97.29 C ANISOU 9 CE1 HIS A 166 10967 14606 11391 6022 -526 3974 C ATOM 10 NE2 HIS A 166 101.724 14.498 37.235 1.00 98.24 N ANISOU 10 NE2 HIS A 166 10811 15033 11484 5930 -656 4005 N ATOM 11 N SER A 167 103.418 14.697 33.302 1.00101.24 N ANISOU 11 N SER A 167 11294 15198 11974 6289 -240 3953 N ATOM 12 CA SER A 167 103.287 13.544 32.410 1.00104.07 C ANISOU 12 CA SER A 167 11950 15265 12326 6582 13 3999 C ATOM 13 C SER A 167 102.266 12.511 32.911 1.00103.99 C ANISOU 13 C SER A 167 12244 14945 12322 6647 58 4031 C ATOM 14 O SER A 167 102.402 11.959 34.008 1.00108.78 O ANISOU 14 O SER A 167 12817 15574 12939 6694 49 4175 O ATOM 15 CB SER A 167 104.649 12.868 32.225 1.00103.47 C ANISOU 15 CB SER A 167 11792 15267 12255 6891 222 4167 C ATOM 16 OG SER A 167 104.508 11.622 31.572 1.00105.85 O ANISOU 16 OG SER A 167 12399 15241 12577 7199 464 4198 O ATOM 17 N PHE A 168 101.256 12.242 32.088 1.00101.91 N ANISOU 17 N PHE A 168 12273 14400 12049 6653 112 3911 N ATOM 18 CA PHE A 168 100.193 11.305 32.442 1.00101.04 C ANISOU 18 CA PHE A 168 12479 13958 11953 6689 150 3937 C ATOM 19 C PHE A 168 100.391 9.917 31.836 1.00102.86 C ANISOU 19 C PHE A 168 13016 13806 12260 7037 430 4003 C ATOM 20 O PHE A 168 101.022 9.761 30.793 1.00104.29 O ANISOU 20 O PHE A 168 13232 13948 12446 7244 599 3946 O ATOM 21 CB PHE A 168 98.834 11.859 31.998 1.00 95.93 C ANISOU 21 CB PHE A 168 11995 13212 11243 6460 22 3753 C ATOM 22 CG PHE A 168 98.456 13.146 32.671 1.00 94.81 C ANISOU 22 CG PHE A 168 11589 13378 11055 6113 -262 3662 C ATOM 23 CD1 PHE A 168 97.829 13.139 33.909 1.00 94.30 C ANISOU 23 CD1 PHE A 168 11487 13380 10961 5954 -419 3702 C ATOM 24 CD2 PHE A 168 98.726 14.365 32.069 1.00 91.95 C ANISOU 24 CD2 PHE A 168 11011 13235 10690 5950 -373 3534 C ATOM 25 CE1 PHE A 168 97.486 14.322 34.533 1.00 89.37 C ANISOU 25 CE1 PHE A 168 10626 13028 10302 5655 -675 3577 C ATOM 26 CE2 PHE A 168 98.385 15.551 32.690 1.00 88.09 C ANISOU 26 CE2 PHE A 168 10295 12971 10203 5635 -635 3425 C ATOM 27 CZ PHE A 168 97.767 15.529 33.923 1.00 87.45 C ANISOU 27 CZ PHE A 168 10191 12946 10090 5497 -784 3426 C ATOM 28 N SER A 169 99.835 8.911 32.499 1.00104.53 N ANISOU 28 N SER A 169 13445 13731 12539 7098 477 4119 N ATOM 29 CA SER A 169 99.760 7.575 31.934 1.00107.94 C ANISOU 29 CA SER A 169 14231 13689 13091 7386 724 4141 C ATOM 30 C SER A 169 98.702 7.512 30.843 1.00106.54 C ANISOU 30 C SER A 169 14400 13195 12887 7361 782 3913 C ATOM 31 O SER A 169 97.609 8.041 31.013 1.00107.30 O ANISOU 31 O SER A 169 14564 13308 12899 7103 618 3838 O ATOM 32 CB SER A 169 99.438 6.554 33.022 1.00110.35 C ANISOU 32 CB SER A 169 14654 13766 13509 7421 738 4362 C ATOM 33 OG SER A 169 99.265 5.263 32.464 1.00118.28 O ANISOU 33 OG SER A 169 16029 14232 14679 7665 967 4360 O ATOM 34 N PHE A 170 99.011 6.864 29.725 1.00108.99 N ANISOU 34 N PHE A 170 14932 13227 13253 7635 1018 3786 N ATOM 35 CA PHE A 170 97.999 6.670 28.693 1.00108.28 C ANISOU 35 CA PHE A 170 15213 12796 13132 7641 1103 3541 C ATOM 36 C PHE A 170 96.894 5.750 29.195 1.00109.27 C ANISOU 36 C PHE A 170 15709 12441 13367 7568 1117 3579 C ATOM 37 O PHE A 170 95.773 5.779 28.697 1.00111.51 O ANISOU 37 O PHE A 170 16286 12492 13592 7420 1103 3392 O ATOM 38 CB PHE A 170 98.594 6.095 27.409 1.00111.29 C ANISOU 38 CB PHE A 170 15755 12982 13549 7972 1372 3348 C ATOM 39 CG PHE A 170 97.570 5.876 26.333 1.00110.91 C ANISOU 39 CG PHE A 170 16088 12599 13452 7937 1473 3021 C ATOM 40 CD1 PHE A 170 97.136 6.936 25.545 1.00110.14 C ANISOU 40 CD1 PHE A 170 15875 12824 13149 7619 1366 2787 C ATOM 41 CD2 PHE A 170 97.008 4.624 26.135 1.00114.08 C ANISOU 41 CD2 PHE A 170 16914 12420 14013 7967 1641 2860 C ATOM 42 CE1 PHE A 170 96.179 6.743 24.562 1.00107.31 C ANISOU 42 CE1 PHE A 170 15804 12261 12707 7349 1434 2399 C ATOM 43 CE2 PHE A 170 96.049 4.423 25.156 1.00113.92 C ANISOU 43 CE2 PHE A 170 17192 12169 13922 7681 1702 2441 C ATOM 44 CZ PHE A 170 95.633 5.484 24.369 1.00111.99 C ANISOU 44 CZ PHE A 170 16816 12301 13435 7375 1601 2211 C ATOM 45 N TYR A 171 97.213 4.923 30.178 1.00112.83 N ANISOU 45 N TYR A 171 16140 12756 13974 7634 1143 3820 N ATOM 46 CA TYR A 171 96.203 4.059 30.759 1.00115.23 C ANISOU 46 CA TYR A 171 16749 12632 14400 7535 1140 3919 C ATOM 47 C TYR A 171 95.158 4.905 31.464 1.00109.15 C ANISOU 47 C TYR A 171 15891 12123 13460 7180 877 3972 C ATOM 48 O TYR A 171 93.958 4.702 31.284 1.00108.24 O ANISOU 48 O TYR A 171 16097 11711 13320 7027 854 3892 O ATOM 49 CB TYR A 171 96.827 3.061 31.734 1.00117.35 C ANISOU 49 CB TYR A 171 16947 12770 14871 7679 1203 4218 C ATOM 50 CG TYR A 171 95.809 2.235 32.489 1.00118.75 C ANISOU 50 CG TYR A 171 17369 12570 15180 7538 1169 4395 C ATOM 51 CD1 TYR A 171 95.238 2.705 33.667 1.00116.48 C ANISOU 51 CD1 TYR A 171 16879 12604 14773 7275 940 4610 C ATOM 52 CD2 TYR A 171 95.414 0.988 32.023 1.00122.62 C ANISOU 52 CD2 TYR A 171 18282 12389 15919 7654 1364 4335 C ATOM 53 CE1 TYR A 171 94.303 1.958 34.359 1.00117.94 C ANISOU 53 CE1 TYR A 171 17262 12489 15060 7136 905 4807 C ATOM 54 CE2 TYR A 171 94.482 0.231 32.710 1.00124.18 C ANISOU 54 CE2 TYR A 171 18694 12230 16257 7493 1328 4526 C ATOM 55 CZ TYR A 171 93.929 0.720 33.878 1.00124.63 C ANISOU 55 CZ TYR A 171 18530 12655 16170 7237 1099 4786 C ATOM 56 OH TYR A 171 93.002 -0.032 34.569 1.00126.73 O ANISOU 56 OH TYR A 171 18983 12610 16560 7068 1060 5013 O ATOM 57 N GLU A 172 95.623 5.858 32.264 1.00106.87 N ANISOU 57 N GLU A 172 15170 12386 13049 7042 678 4085 N ATOM 58 CA GLU A 172 94.726 6.690 33.055 1.00103.30 C ANISOU 58 CA GLU A 172 14576 12235 12439 6712 415 4114 C ATOM 59 C GLU A 172 93.768 7.458 32.149 1.00 99.83 C ANISOU 59 C GLU A 172 14300 11787 11843 6543 336 3856 C ATOM 60 O GLU A 172 92.550 7.321 32.276 1.00101.37 O ANISOU 60 O GLU A 172 14726 11815 11975 6321 262 3812 O ATOM 61 CB GLU A 172 95.526 7.652 33.946 1.00103.78 C ANISOU 61 CB GLU A 172 14144 12872 12416 6607 233 4191 C ATOM 62 CG GLU A 172 94.686 8.372 35.005 1.00 99.03 C ANISOU 62 CG GLU A 172 13363 12588 11675 6291 -34 4219 C ATOM 63 CD GLU A 172 95.529 9.102 36.038 1.00 98.61 C ANISOU 63 CD GLU A 172 12862 13031 11575 6217 -182 4287 C ATOM 64 OE1 GLU A 172 96.770 9.146 35.879 1.00100.14 O ANISOU 64 OE1 GLU A 172 12878 13342 11828 6387 -88 4320 O ATOM 65 OE2 GLU A 172 94.949 9.625 37.012 1.00 96.97 O1+ ANISOU 65 OE2 GLU A 172 12485 13099 11259 5990 -386 4295 O1+ ATOM 66 N LEU A 173 94.329 8.243 31.230 1.00 98.39 N ANISOU 66 N LEU A 173 13980 11808 11596 6597 353 3677 N ATOM 67 CA LEU A 173 93.554 9.040 30.272 1.00 98.91 C ANISOU 67 CA LEU A 173 14127 11936 11520 6333 284 3371 C ATOM 68 C LEU A 173 92.455 8.228 29.599 1.00 98.65 C ANISOU 68 C LEU A 173 14532 11454 11498 6109 409 3116 C ATOM 69 O LEU A 173 91.296 8.643 29.563 1.00 93.71 O ANISOU 69 O LEU A 173 13991 10865 10750 5728 274 2950 O ATOM 70 CB LEU A 173 94.478 9.629 29.200 1.00 95.19 C ANISOU 70 CB LEU A 173 13486 11658 11024 6484 371 3246 C ATOM 71 CG LEU A 173 95.138 10.991 29.420 1.00 92.71 C ANISOU 71 CG LEU A 173 12717 11863 10647 6434 175 3318 C ATOM 72 CD1 LEU A 173 95.534 11.197 30.864 1.00 92.63 C ANISOU 72 CD1 LEU A 173 12411 12098 10687 6297 19 3484 C ATOM 73 CD2 LEU A 173 96.350 11.120 28.523 1.00 94.28 C ANISOU 73 CD2 LEU A 173 12755 12192 10876 6656 331 3292 C ATOM 74 N LYS A 174 92.843 7.072 29.065 1.00100.02 N ANISOU 74 N LYS A 174 14972 11209 11823 6356 665 3074 N ATOM 75 CA LYS A 174 91.933 6.161 28.384 1.00101.76 C ANISOU 75 CA LYS A 174 15618 10952 12093 6180 806 2808 C ATOM 76 C LYS A 174 90.668 5.947 29.204 1.00100.72 C ANISOU 76 C LYS A 174 15632 10700 11939 5836 660 2880 C ATOM 77 O LYS A 174 89.550 6.058 28.699 1.00 99.26 O ANISOU 77 O LYS A 174 15636 10435 11644 5468 618 2614 O ATOM 78 CB LYS A 174 92.634 4.824 28.132 1.00106.80 C ANISOU 78 CB LYS A 174 16489 11118 12971 6560 1075 2846 C ATOM 79 CG LYS A 174 92.048 3.964 27.019 1.00111.84 C ANISOU 79 CG LYS A 174 17535 11287 13672 6459 1269 2454 C ATOM 80 CD LYS A 174 92.743 2.594 26.981 1.00116.36 C ANISOU 80 CD LYS A 174 18331 11341 14539 6863 1515 2520 C ATOM 81 CE LYS A 174 92.479 1.840 25.680 1.00118.82 C ANISOU 81 CE LYS A 174 18989 11249 14909 6852 1730 2053 C ATOM 82 NZ LYS A 174 93.110 2.504 24.501 1.00117.67 N1+ ANISOU 82 NZ LYS A 174 18680 11461 14568 6971 1812 1772 N1+ ATOM 83 N ASN A 175 90.862 5.681 30.489 1.00101.66 N ANISOU 83 N ASN A 175 15626 10863 12136 5959 577 3259 N ATOM 84 CA ASN A 175 89.777 5.261 31.361 1.00102.68 C ANISOU 84 CA ASN A 175 15885 10863 12264 5694 468 3402 C ATOM 85 C ASN A 175 88.985 6.405 31.966 1.00 97.30 C ANISOU 85 C ASN A 175 14969 10659 11343 5363 187 3396 C ATOM 86 O ASN A 175 87.767 6.311 32.102 1.00 96.47 O ANISOU 86 O ASN A 175 15022 10481 11152 5013 102 3311 O ATOM 87 CB ASN A 175 90.332 4.378 32.470 1.00104.99 C ANISOU 87 CB ASN A 175 16138 11006 12747 5991 517 3847 C ATOM 88 CG ASN A 175 90.976 3.121 31.930 1.00112.98 C ANISOU 88 CG ASN A 175 17424 11461 14043 6316 797 3855 C ATOM 89 OD1 ASN A 175 90.392 2.038 31.986 1.00117.59 O ANISOU 89 OD1 ASN A 175 18325 11539 14815 6242 896 3890 O ATOM 90 ND2 ASN A 175 92.179 3.260 31.381 1.00112.12 N ANISOU 90 ND2 ASN A 175 17189 11434 13978 6677 924 3813 N ATOM 91 N VAL A 176 89.669 7.486 32.326 1.00 94.95 N ANISOU 91 N VAL A 176 14287 10847 10941 5472 40 3476 N ATOM 92 CA VAL A 176 88.991 8.629 32.935 1.00 91.18 C ANISOU 92 CA VAL A 176 13561 10824 10260 5193 -237 3444 C ATOM 93 C VAL A 176 88.157 9.394 31.910 1.00 88.21 C ANISOU 93 C VAL A 176 13270 10501 9744 4855 -292 3063 C ATOM 94 O VAL A 176 87.359 10.261 32.269 1.00 85.26 O ANISOU 94 O VAL A 176 12758 10426 9212 4583 -507 2983 O ATOM 95 CB VAL A 176 89.993 9.582 33.611 1.00 89.92 C ANISOU 95 CB VAL A 176 12954 11150 10061 5400 -389 3609 C ATOM 96 CG1 VAL A 176 90.535 8.950 34.890 1.00 92.47 C ANISOU 96 CG1 VAL A 176 13124 11550 10460 5615 -394 3984 C ATOM 97 CG2 VAL A 176 91.124 9.921 32.665 1.00 90.18 C ANISOU 97 CG2 VAL A 176 12890 11209 10167 5633 -267 3513 C ATOM 98 N THR A 177 88.339 9.060 30.635 1.00 89.51 N ANISOU 98 N THR A 177 13651 10396 9962 4888 -95 2828 N ATOM 99 CA THR A 177 87.517 9.607 29.560 1.00 87.07 C ANISOU 99 CA THR A 177 13452 10116 9516 4575 -111 2481 C ATOM 100 C THR A 177 86.591 8.530 29.010 1.00 89.09 C ANISOU 100 C THR A 177 14128 9928 9793 4381 39 2300 C ATOM 101 O THR A 177 86.048 8.664 27.918 1.00 88.46 O ANISOU 101 O THR A 177 14197 9795 9617 4178 100 1991 O ATOM 102 CB THR A 177 88.375 10.168 28.418 1.00 86.73 C ANISOU 102 CB THR A 177 13290 10196 9469 4723 -14 2322 C ATOM 103 OG1 THR A 177 89.231 9.138 27.910 1.00 96.63 O ANISOU 103 OG1 THR A 177 14714 11129 10872 5044 245 2330 O ATOM 104 CG2 THR A 177 89.228 11.325 28.908 1.00 84.75 C ANISOU 104 CG2 THR A 177 12609 10382 9210 4857 -184 2485 C ATOM 105 N ASN A 178 86.430 7.455 29.776 1.00 91.81 N ANISOU 105 N ASN A 178 14648 9963 10272 4443 96 2508 N ATOM 106 CA ASN A 178 85.596 6.326 29.380 1.00 94.39 C ANISOU 106 CA ASN A 178 15376 9811 10678 4260 232 2371 C ATOM 107 C ASN A 178 86.016 5.756 28.029 1.00101.30 C ANISOU 107 C ASN A 178 16486 10362 11641 4384 477 2063 C ATOM 108 O ASN A 178 85.232 5.742 27.073 1.00 99.98 O ANISOU 108 O ASN A 178 16511 10112 11365 4110 520 1723 O ATOM 109 CB ASN A 178 84.122 6.741 29.367 1.00 91.88 C ANISOU 109 CB ASN A 178 15128 9629 10155 3790 75 2211 C ATOM 110 CG ASN A 178 83.618 7.126 30.757 1.00 96.80 C ANISOU 110 CG ASN A 178 15542 10553 10686 3676 -153 2503 C ATOM 111 OD1 ASN A 178 83.345 6.262 31.593 1.00 99.71 O ANISOU 111 OD1 ASN A 178 16013 10716 11155 3673 -144 2758 O ATOM 112 ND2 ASN A 178 83.514 8.427 31.015 1.00 86.48 N ANISOU 112 ND2 ASN A 178 13923 9743 9194 3593 -361 2472 N ATOM 113 N ASN A 179 87.264 5.289 27.974 1.00 99.47 N ANISOU 113 N ASN A 179 16218 9986 11589 4808 634 2183 N ATOM 114 CA ASN A 179 87.877 4.779 26.750 1.00102.14 C ANISOU 114 CA ASN A 179 16722 10079 12006 5014 873 1902 C ATOM 115 C ASN A 179 87.619 5.686 25.557 1.00 99.57 C ANISOU 115 C ASN A 179 16321 10068 11443 4823 858 1551 C ATOM 116 O ASN A 179 87.338 5.220 24.454 1.00101.37 O ANISOU 116 O ASN A 179 16781 10090 11643 4748 1012 1199 O ATOM 117 CB ASN A 179 87.387 3.363 26.459 1.00106.52 C ANISOU 117 CB ASN A 179 17702 10006 12764 4970 1050 1753 C ATOM 118 CG ASN A 179 87.814 2.373 27.529 1.00116.19 C ANISOU 118 CG ASN A 179 18997 10874 14278 5225 1102 2138 C ATOM 119 OD1 ASN A 179 86.977 1.763 28.197 1.00118.17 O ANISOU 119 OD1 ASN A 179 19417 10859 14624 5007 1047 2283 O ATOM 120 ND2 ASN A 179 89.124 2.216 27.704 1.00116.61 N ANISOU 120 ND2 ASN A 179 18898 10942 14467 5689 1208 2336 N ATOM 121 N PHE A 180 87.722 6.988 25.797 1.00 95.62 N ANISOU 121 N PHE A 180 15479 10075 10777 4745 666 1654 N ATOM 122 CA PHE A 180 87.457 7.975 24.769 1.00 93.04 C ANISOU 122 CA PHE A 180 15028 10087 10237 4553 623 1401 C ATOM 123 C PHE A 180 86.074 7.752 24.182 1.00 92.65 C ANISOU 123 C PHE A 180 15243 9907 10052 4141 618 1101 C ATOM 124 O PHE A 180 85.923 7.487 22.985 1.00 94.05 O ANISOU 124 O PHE A 180 15572 10013 10150 4086 767 778 O ATOM 125 CB PHE A 180 88.528 7.914 23.685 1.00 94.98 C ANISOU 125 CB PHE A 180 15214 10383 10493 4854 820 1261 C ATOM 126 CG PHE A 180 89.913 8.128 24.207 1.00 95.58 C ANISOU 126 CG PHE A 180 15014 10614 10687 5257 831 1558 C ATOM 127 CD1 PHE A 180 90.328 9.385 24.607 1.00 92.41 C ANISOU 127 CD1 PHE A 180 14224 10670 10217 5249 639 1754 C ATOM 128 CD2 PHE A 180 90.796 7.073 24.319 1.00 99.54 C ANISOU 128 CD2 PHE A 180 15636 10801 11385 5644 1029 1642 C ATOM 129 CE1 PHE A 180 91.608 9.586 25.102 1.00 95.25 C ANISOU 129 CE1 PHE A 180 14312 11199 10679 5601 641 2025 C ATOM 130 CE2 PHE A 180 92.079 7.266 24.813 1.00100.22 C ANISOU 130 CE2 PHE A 180 15448 11068 11563 6021 1039 1933 C ATOM 131 CZ PHE A 180 92.485 8.523 25.204 1.00 96.98 C ANISOU 131 CZ PHE A 180 14644 11143 11062 5989 844 2123 C ATOM 132 N ASP A 181 85.068 7.835 25.048 1.00 94.49 N ANISOU 132 N ASP A 181 15516 10142 10245 3858 446 1211 N ATOM 133 CA ASP A 181 83.677 7.740 24.628 1.00 94.23 C ANISOU 133 CA ASP A 181 15688 10055 10058 3434 406 968 C ATOM 134 C ASP A 181 83.389 8.800 23.572 1.00 87.68 C ANISOU 134 C ASP A 181 14703 9614 8996 3257 360 736 C ATOM 135 O ASP A 181 83.543 9.993 23.820 1.00 84.47 O ANISOU 135 O ASP A 181 13982 9606 8506 3243 190 864 O ATOM 136 CB ASP A 181 82.738 7.901 25.822 1.00 93.20 C ANISOU 136 CB ASP A 181 15527 9998 9885 3185 196 1175 C ATOM 137 CG ASP A 181 81.325 7.433 25.523 1.00 95.14 C ANISOU 137 CG ASP A 181 16043 10086 10021 2771 188 967 C ATOM 138 OD1 ASP A 181 81.007 7.199 24.335 1.00 93.71 O ANISOU 138 OD1 ASP A 181 16035 9812 9757 2640 316 632 O ATOM 139 OD2 ASP A 181 80.531 7.304 26.480 1.00 94.22 O1+ ANISOU 139 OD2 ASP A 181 15945 9973 9882 2573 50 1142 O1+ ATOM 140 N GLU A 182 82.969 8.342 22.398 1.00 95.45 N ANISOU 140 N GLU A 182 15903 10477 9886 3121 512 395 N ATOM 141 CA GLU A 182 82.839 9.186 21.214 1.00 93.13 C ANISOU 141 CA GLU A 182 15464 10551 9371 3004 521 177 C ATOM 142 C GLU A 182 81.540 9.989 21.184 1.00 84.72 C ANISOU 142 C GLU A 182 14335 9769 8085 2587 335 118 C ATOM 143 O GLU A 182 81.384 10.904 20.375 1.00 82.93 O ANISOU 143 O GLU A 182 13921 9909 7679 2480 295 24 O ATOM 144 CB GLU A 182 82.936 8.318 19.953 1.00 97.26 C ANISOU 144 CB GLU A 182 16225 10875 9855 3046 767 -189 C ATOM 145 CG GLU A 182 83.582 9.004 18.767 1.00 97.14 C ANISOU 145 CG GLU A 182 15985 11240 9682 3175 852 -316 C ATOM 146 CD GLU A 182 85.066 9.217 18.973 1.00100.59 C ANISOU 146 CD GLU A 182 16197 11755 10268 3610 907 -87 C ATOM 147 OE1 GLU A 182 85.647 8.521 19.838 1.00102.80 O ANISOU 147 OE1 GLU A 182 16570 11709 10780 3854 945 88 O ATOM 148 OE2 GLU A 182 85.644 10.080 18.273 1.00 98.75 O1+ ANISOU 148 OE2 GLU A 182 15679 11923 9919 3702 910 -58 O1+ ATOM 149 N ARG A 183 80.606 9.630 22.058 1.00 87.85 N ANISOU 149 N ARG A 183 14875 10009 8494 2359 225 191 N ATOM 150 CA ARG A 183 79.318 10.319 22.133 1.00 84.81 C ANISOU 150 CA ARG A 183 14434 9891 7896 1974 47 145 C ATOM 151 C ARG A 183 79.444 11.719 22.746 1.00 86.38 C ANISOU 151 C ARG A 183 14263 10500 8056 2001 -183 368 C ATOM 152 O ARG A 183 80.189 11.916 23.712 1.00 81.88 O ANISOU 152 O ARG A 183 13536 9934 7642 2235 -263 621 O ATOM 153 CB ARG A 183 78.319 9.489 22.943 1.00 89.26 C ANISOU 153 CB ARG A 183 15240 10190 8485 1733 -3 184 C ATOM 154 CG ARG A 183 77.779 8.271 22.221 1.00 92.23 C ANISOU 154 CG ARG A 183 15983 10195 8866 1560 177 -102 C ATOM 155 CD ARG A 183 77.856 7.028 23.098 1.00 99.12 C ANISOU 155 CD ARG A 183 17099 10571 9990 1629 236 49 C ATOM 156 NE ARG A 183 77.417 7.261 24.474 1.00 98.56 N ANISOU 156 NE ARG A 183 16914 10601 9934 1548 40 385 N ATOM 157 CZ ARG A 183 76.154 7.474 24.838 1.00 98.63 C ANISOU 157 CZ ARG A 183 16929 10779 9767 1181 -110 396 C ATOM 158 NH1 ARG A 183 75.189 7.510 23.926 1.00 96.78 N1+ ANISOU 158 NH1 ARG A 183 16810 10630 9330 847 -91 99 N1+ ATOM 159 NH2 ARG A 183 75.855 7.661 26.117 1.00 96.61 N ANISOU 159 NH2 ARG A 183 16541 10650 9514 1154 -280 704 N ATOM 160 N PRO A 184 78.715 12.697 22.176 1.00 83.50 N ANISOU 160 N PRO A 184 13750 10485 7493 1763 -290 269 N ATOM 161 CA PRO A 184 78.650 14.074 22.679 1.00 71.91 C ANISOU 161 CA PRO A 184 11942 9379 6002 1745 -523 434 C ATOM 162 C PRO A 184 78.231 14.144 24.139 1.00 70.66 C ANISOU 162 C PRO A 184 11736 9222 5891 1704 -713 618 C ATOM 163 O PRO A 184 77.424 13.325 24.575 1.00 72.49 O ANISOU 163 O PRO A 184 12195 9278 6070 1529 -702 593 O ATOM 164 CB PRO A 184 77.590 14.725 21.782 1.00 70.49 C ANISOU 164 CB PRO A 184 11722 9475 5586 1433 -571 260 C ATOM 165 CG PRO A 184 76.912 13.595 21.066 1.00 73.00 C ANISOU 165 CG PRO A 184 12379 9582 5777 1237 -394 8 C ATOM 166 CD PRO A 184 77.947 12.543 20.932 1.00 76.10 C ANISOU 166 CD PRO A 184 12948 9621 6345 1511 -187 -22 C ATOM 167 N ILE A 185 78.769 15.106 24.883 1.00 75.82 N ANISOU 167 N ILE A 185 12082 10088 6637 1858 -889 798 N ATOM 168 CA ILE A 185 78.391 15.265 26.284 1.00 77.54 C ANISOU 168 CA ILE A 185 12205 10390 6867 1836 -1083 953 C ATOM 169 C ILE A 185 76.905 15.558 26.403 1.00 76.19 C ANISOU 169 C ILE A 185 12071 10392 6486 1494 -1216 851 C ATOM 170 O ILE A 185 76.287 15.251 27.429 1.00 74.92 O ANISOU 170 O ILE A 185 11941 10253 6271 1406 -1320 940 O ATOM 171 CB ILE A 185 79.163 16.400 26.987 1.00 79.20 C ANISOU 171 CB ILE A 185 12044 10849 7198 2034 -1272 1100 C ATOM 172 CG1 ILE A 185 80.628 16.403 26.562 1.00 81.98 C ANISOU 172 CG1 ILE A 185 12296 11122 7729 2342 -1148 1182 C ATOM 173 CG2 ILE A 185 79.020 16.286 28.509 1.00 79.06 C ANISOU 173 CG2 ILE A 185 11940 10906 7195 2086 -1431 1261 C ATOM 174 CD1 ILE A 185 80.906 17.360 25.444 1.00 79.89 C ANISOU 174 CD1 ILE A 185 11857 11032 7465 2320 -1144 1104 C ATOM 175 N SER A 186 76.344 16.172 25.359 1.00 73.56 N ANISOU 175 N SER A 186 11707 10220 6021 1310 -1213 686 N ATOM 176 CA SER A 186 74.909 16.416 25.298 1.00 63.92 C ANISOU 176 CA SER A 186 10527 9179 4579 982 -1315 577 C ATOM 177 C SER A 186 74.154 15.126 25.608 1.00 80.31 C ANISOU 177 C SER A 186 12919 11028 6567 798 -1226 547 C ATOM 178 O SER A 186 73.171 15.129 26.353 1.00 80.45 O ANISOU 178 O SER A 186 12934 11177 6456 610 -1360 585 O ATOM 179 CB SER A 186 74.514 16.943 23.926 1.00 65.38 C ANISOU 179 CB SER A 186 10688 9521 4630 824 -1255 411 C ATOM 180 OG SER A 186 74.644 15.938 22.938 1.00 65.78 O ANISOU 180 OG SER A 186 11004 9353 4635 782 -1015 262 O ATOM 181 N VAL A 187 74.649 14.020 25.054 1.00 82.43 N ANISOU 181 N VAL A 187 13447 10952 6920 863 -1002 483 N ATOM 182 CA VAL A 187 74.028 12.709 25.223 1.00 79.74 C ANISOU 182 CA VAL A 187 13428 10312 6558 686 -898 446 C ATOM 183 C VAL A 187 74.565 11.952 26.439 1.00 80.77 C ANISOU 183 C VAL A 187 13609 10204 6878 876 -901 695 C ATOM 184 O VAL A 187 74.046 10.898 26.798 1.00 85.63 O ANISOU 184 O VAL A 187 14458 10565 7514 733 -844 738 O ATOM 185 CB VAL A 187 74.235 11.837 23.977 1.00 81.37 C ANISOU 185 CB VAL A 187 13902 10232 6781 654 -653 210 C ATOM 186 CG1 VAL A 187 73.289 10.647 24.007 1.00 84.84 C ANISOU 186 CG1 VAL A 187 14664 10394 7176 367 -579 113 C ATOM 187 CG2 VAL A 187 74.025 12.664 22.723 1.00 79.58 C ANISOU 187 CG2 VAL A 187 13560 10299 6378 552 -632 6 C ATOM 188 N GLY A 188 75.607 12.484 27.069 1.00 77.88 N ANISOU 188 N GLY A 188 13008 9929 6653 1191 -968 875 N ATOM 189 CA GLY A 188 76.182 11.844 28.240 1.00 76.31 C ANISOU 189 CA GLY A 188 12807 9573 6615 1397 -976 1140 C ATOM 190 C GLY A 188 77.509 11.155 27.975 1.00 79.92 C ANISOU 190 C GLY A 188 13355 9702 7308 1729 -781 1202 C ATOM 191 O GLY A 188 78.069 10.504 28.860 1.00 79.27 O ANISOU 191 O GLY A 188 13285 9453 7379 1928 -756 1442 O ATOM 192 N GLY A 189 78.003 11.290 26.746 1.00 82.16 N ANISOU 192 N GLY A 189 13685 9922 7609 1797 -639 998 N ATOM 193 CA GLY A 189 79.319 10.801 26.383 1.00 78.04 C ANISOU 193 CA GLY A 189 13202 9163 7285 2141 -457 1030 C ATOM 194 C GLY A 189 80.387 11.795 26.801 1.00 76.22 C ANISOU 194 C GLY A 189 12619 9211 7129 2423 -563 1199 C ATOM 195 O GLY A 189 80.152 12.640 27.662 1.00 73.89 O ANISOU 195 O GLY A 189 12079 9216 6780 2381 -781 1323 O ATOM 196 N ASN A 190 81.555 11.705 26.176 1.00 77.49 N ANISOU 196 N ASN A 190 12743 9289 7411 2707 -413 1187 N ATOM 197 CA ASN A 190 82.711 12.492 26.590 1.00 76.44 C ANISOU 197 CA ASN A 190 12282 9381 7380 2993 -493 1372 C ATOM 198 C ASN A 190 83.272 13.375 25.492 1.00 75.38 C ANISOU 198 C ASN A 190 11963 9462 7214 3048 -462 1259 C ATOM 199 O ASN A 190 84.222 14.124 25.719 1.00 74.54 O ANISOU 199 O ASN A 190 11564 9559 7199 3251 -536 1403 O ATOM 200 CB ASN A 190 83.819 11.568 27.095 1.00 83.31 C ANISOU 200 CB ASN A 190 13206 9998 8449 3349 -353 1569 C ATOM 201 CG ASN A 190 83.501 10.965 28.439 1.00 80.18 C ANISOU 201 CG ASN A 190 12857 9501 8105 3351 -434 1802 C ATOM 202 OD1 ASN A 190 82.822 9.941 28.534 1.00 82.15 O ANISOU 202 OD1 ASN A 190 13399 9441 8375 3221 -348 1785 O ATOM 203 ND2 ASN A 190 83.980 11.606 29.494 1.00 78.91 N ANISOU 203 ND2 ASN A 190 12391 9624 7966 3488 -607 2024 N ATOM 204 N LYS A 191 82.693 13.272 24.302 1.00 75.67 N ANISOU 204 N LYS A 191 12156 9476 7121 2860 -353 1012 N ATOM 205 CA LYS A 191 83.182 14.015 23.149 1.00 76.75 C ANISOU 205 CA LYS A 191 12118 9839 7204 2904 -299 922 C ATOM 206 C LYS A 191 82.799 15.482 23.240 1.00 71.85 C ANISOU 206 C LYS A 191 11187 9588 6526 2738 -534 980 C ATOM 207 O LYS A 191 81.626 15.828 23.158 1.00 70.29 O ANISOU 207 O LYS A 191 11032 9491 6183 2440 -638 873 O ATOM 208 CB LYS A 191 82.642 13.409 21.853 1.00 78.16 C ANISOU 208 CB LYS A 191 12544 9923 7231 2753 -108 632 C ATOM 209 CG LYS A 191 83.101 14.126 20.601 1.00 77.50 C ANISOU 209 CG LYS A 191 12263 10131 7054 2793 -40 555 C ATOM 210 CD LYS A 191 82.748 13.328 19.361 1.00 80.17 C ANISOU 210 CD LYS A 191 12847 10380 7235 2708 180 246 C ATOM 211 CE LYS A 191 83.191 14.033 18.096 1.00 79.34 C ANISOU 211 CE LYS A 191 12512 10635 6999 2750 252 192 C ATOM 212 NZ LYS A 191 83.253 13.061 16.977 1.00 82.89 N1+ ANISOU 212 NZ LYS A 191 13183 10988 7325 2797 505 -116 N1+ ATOM 213 N MET A 192 83.802 16.337 23.400 1.00 71.06 N ANISOU 213 N MET A 192 10768 9679 6552 2933 -617 1150 N ATOM 214 CA MET A 192 83.579 17.763 23.591 1.00 68.34 C ANISOU 214 CA MET A 192 10105 9633 6227 2809 -856 1220 C ATOM 215 C MET A 192 83.759 18.571 22.308 1.00 68.01 C ANISOU 215 C MET A 192 9885 9812 6141 2752 -818 1189 C ATOM 216 O MET A 192 83.253 19.680 22.192 1.00 66.03 O ANISOU 216 O MET A 192 9430 9772 5885 2578 -992 1207 O ATOM 217 CB MET A 192 84.529 18.300 24.663 1.00 67.83 C ANISOU 217 CB MET A 192 9764 9653 6357 3024 -1008 1432 C ATOM 218 CG MET A 192 84.080 18.080 26.089 1.00 67.21 C ANISOU 218 CG MET A 192 9715 9532 6289 3001 -1161 1489 C ATOM 219 SD MET A 192 85.468 18.373 27.202 1.00 77.35 S ANISOU 219 SD MET A 192 10698 10915 7777 3321 -1263 1725 S ATOM 220 CE MET A 192 86.077 19.940 26.591 1.00 66.34 C ANISOU 220 CE MET A 192 8909 9787 6511 3306 -1407 1758 C ATOM 221 N GLY A 193 84.502 18.025 21.355 1.00 70.20 N ANISOU 221 N GLY A 193 10221 10058 6394 2915 -592 1155 N ATOM 222 CA GLY A 193 84.815 18.767 20.154 1.00 70.30 C ANISOU 222 CA GLY A 193 10020 10335 6355 2894 -547 1174 C ATOM 223 C GLY A 193 85.835 18.103 19.256 1.00 73.13 C ANISOU 223 C GLY A 193 10407 10694 6686 3143 -294 1151 C ATOM 224 O GLY A 193 86.420 17.088 19.600 1.00 79.89 O ANISOU 224 O GLY A 193 11441 11314 7601 3368 -154 1128 O ATOM 225 N GLU A 194 86.022 18.682 18.078 1.00 76.68 N ANISOU 225 N GLU A 194 10666 11430 7039 3107 -233 1165 N ATOM 226 CA GLU A 194 87.039 18.246 17.139 1.00 81.79 C ANISOU 226 CA GLU A 194 11259 12184 7633 3352 -7 1158 C ATOM 227 C GLU A 194 87.816 19.468 16.698 1.00 81.85 C ANISOU 227 C GLU A 194 10830 12543 7725 3400 -96 1427 C ATOM 228 O GLU A 194 87.226 20.463 16.264 1.00 82.89 O ANISOU 228 O GLU A 194 10773 12901 7820 3170 -225 1498 O ATOM 229 CB GLU A 194 86.425 17.551 15.930 1.00 83.33 C ANISOU 229 CB GLU A 194 11668 12435 7559 3247 199 869 C ATOM 230 CG GLU A 194 85.452 16.441 16.252 1.00 87.29 C ANISOU 230 CG GLU A 194 12594 12593 7979 3113 264 589 C ATOM 231 CD GLU A 194 85.047 15.674 15.007 1.00 93.96 C ANISOU 231 CD GLU A 194 13634 13493 8572 3047 486 265 C ATOM 232 OE1 GLU A 194 83.880 15.811 14.571 1.00 94.41 O ANISOU 232 OE1 GLU A 194 13777 13654 8440 2735 447 105 O ATOM 233 OE2 GLU A 194 85.905 14.947 14.458 1.00 95.40 O1+ ANISOU 233 OE2 GLU A 194 13869 13641 8738 3316 697 158 O1+ ATOM 234 N GLY A 195 89.134 19.403 16.814 1.00 77.33 N ANISOU 234 N GLY A 195 10086 12016 7280 3696 -32 1597 N ATOM 235 CA GLY A 195 89.964 20.540 16.487 1.00 77.17 C ANISOU 235 CA GLY A 195 9633 12312 7376 3740 -127 1887 C ATOM 236 C GLY A 195 91.334 20.349 17.082 1.00 78.47 C ANISOU 236 C GLY A 195 9654 12446 7715 4060 -99 2070 C ATOM 237 O GLY A 195 91.621 19.289 17.632 1.00 79.68 O ANISOU 237 O GLY A 195 10052 12345 7879 4265 17 1968 O ATOM 238 N GLY A 196 92.177 21.371 16.968 1.00 78.45 N ANISOU 238 N GLY A 196 9245 12703 7861 4099 -208 2357 N ATOM 239 CA GLY A 196 93.550 21.298 17.439 1.00 82.25 C ANISOU 239 CA GLY A 196 9528 13231 8494 4392 -187 2560 C ATOM 240 C GLY A 196 94.263 20.035 16.995 1.00 82.97 C ANISOU 240 C GLY A 196 9795 13288 8440 4721 108 2451 C ATOM 241 O GLY A 196 95.167 19.562 17.678 1.00 89.65 O ANISOU 241 O GLY A 196 10626 14043 9394 4994 149 2543 O ATOM 242 N PHE A 197 93.832 19.493 15.856 1.00 88.57 N ANISOU 242 N PHE A 197 10667 14080 8904 4701 310 2240 N ATOM 243 CA PHE A 197 94.385 18.270 15.266 1.00 87.81 C ANISOU 243 CA PHE A 197 10759 13950 8656 5007 605 2059 C ATOM 244 C PHE A 197 94.273 17.048 16.183 1.00 91.10 C ANISOU 244 C PHE A 197 11562 13904 9148 5171 683 1884 C ATOM 245 O PHE A 197 95.264 16.380 16.492 1.00 90.70 O ANISOU 245 O PHE A 197 11518 13772 9171 5515 808 1946 O ATOM 246 CB PHE A 197 95.832 18.508 14.851 1.00 90.12 C ANISOU 246 CB PHE A 197 10695 14577 8970 5300 695 2308 C ATOM 247 CG PHE A 197 95.968 19.518 13.756 1.00 91.36 C ANISOU 247 CG PHE A 197 10481 15212 9021 5162 670 2485 C ATOM 248 CD1 PHE A 197 95.671 19.178 12.440 1.00 94.73 C ANISOU 248 CD1 PHE A 197 10947 15891 9154 5155 867 2295 C ATOM 249 CD2 PHE A 197 96.364 20.813 14.035 1.00 88.86 C ANISOU 249 CD2 PHE A 197 9763 15098 8900 5029 444 2842 C ATOM 250 CE1 PHE A 197 95.784 20.104 11.422 1.00 92.85 C ANISOU 250 CE1 PHE A 197 10340 16137 8802 5029 848 2499 C ATOM 251 CE2 PHE A 197 96.477 21.748 13.020 1.00 93.50 C ANISOU 251 CE2 PHE A 197 9995 16114 9418 4892 419 3054 C ATOM 252 CZ PHE A 197 96.187 21.391 11.711 1.00 91.36 C ANISOU 252 CZ PHE A 197 9752 16128 8834 4896 624 2902 C ATOM 253 N GLY A 198 93.041 16.760 16.594 1.00 74.41 N ANISOU 253 N GLY A 198 11063 8526 8681 5360 351 1958 N ATOM 254 CA GLY A 198 92.731 15.595 17.395 1.00 75.24 C ANISOU 254 CA GLY A 198 11166 8539 8884 5336 250 2039 C ATOM 255 C GLY A 198 91.302 15.723 17.851 1.00 73.56 C ANISOU 255 C GLY A 198 11005 8228 8717 5102 49 2053 C ATOM 256 O GLY A 198 90.599 16.624 17.406 1.00 72.00 O ANISOU 256 O GLY A 198 10872 8010 8475 4978 -10 1989 O ATOM 257 N VAL A 199 90.856 14.841 18.734 1.00 74.00 N ANISOU 257 N VAL A 199 11030 8219 8869 5042 -52 2142 N ATOM 258 CA VAL A 199 89.512 14.978 19.282 1.00 77.65 C ANISOU 258 CA VAL A 199 11501 8606 9398 4820 -223 2175 C ATOM 259 C VAL A 199 89.590 15.271 20.784 1.00 78.16 C ANISOU 259 C VAL A 199 11266 8923 9510 4745 -253 2302 C ATOM 260 O VAL A 199 90.395 14.669 21.502 1.00 73.01 O ANISOU 260 O VAL A 199 10487 8375 8879 4852 -206 2386 O ATOM 261 CB VAL A 199 88.665 13.718 19.021 1.00 74.03 C ANISOU 261 CB VAL A 199 11297 7814 9016 4778 -328 2172 C ATOM 262 CG1 VAL A 199 87.300 13.848 19.671 1.00 72.53 C ANISOU 262 CG1 VAL A 199 11077 7559 8924 4554 -491 2227 C ATOM 263 CG2 VAL A 199 88.515 13.487 17.530 1.00 74.68 C ANISOU 263 CG2 VAL A 199 11705 7641 9029 4829 -319 2034 C ATOM 264 N VAL A 200 88.769 16.205 21.259 1.00 69.83 N ANISOU 264 N VAL A 200 10107 7962 8464 4565 -332 2317 N ATOM 265 CA VAL A 200 88.831 16.604 22.662 1.00 69.11 C ANISOU 265 CA VAL A 200 9756 8113 8387 4488 -350 2426 C ATOM 266 C VAL A 200 87.764 15.927 23.530 1.00 85.50 C ANISOU 266 C VAL A 200 11866 10058 10563 4357 -461 2519 C ATOM 267 O VAL A 200 86.565 16.117 23.312 1.00 82.75 O ANISOU 267 O VAL A 200 11613 9556 10272 4212 -549 2501 O ATOM 268 CB VAL A 200 88.699 18.123 22.810 1.00 67.14 C ANISOU 268 CB VAL A 200 9347 8085 8077 4384 -339 2398 C ATOM 269 CG1 VAL A 200 88.690 18.505 24.276 1.00 66.57 C ANISOU 269 CG1 VAL A 200 9044 8244 8005 4295 -363 2506 C ATOM 270 CG2 VAL A 200 89.840 18.816 22.105 1.00 67.26 C ANISOU 270 CG2 VAL A 200 9295 8258 8001 4517 -216 2329 C ATOM 271 N TYR A 201 88.213 15.155 24.518 1.00 70.37 N ANISOU 271 N TYR A 201 9866 8202 8670 4415 -454 2627 N ATOM 272 CA TYR A 201 87.318 14.467 25.450 1.00 74.61 C ANISOU 272 CA TYR A 201 10431 8626 9292 4311 -535 2735 C ATOM 273 C TYR A 201 87.366 15.065 26.858 1.00 73.25 C ANISOU 273 C TYR A 201 10042 8710 9079 4236 -535 2838 C ATOM 274 O TYR A 201 88.419 15.506 27.326 1.00 70.20 O ANISOU 274 O TYR A 201 9484 8579 8609 4314 -484 2855 O ATOM 275 CB TYR A 201 87.666 12.971 25.526 1.00 72.95 C ANISOU 275 CB TYR A 201 10344 8238 9135 4433 -536 2791 C ATOM 276 CG TYR A 201 87.710 12.298 24.175 1.00 75.76 C ANISOU 276 CG TYR A 201 10936 8337 9514 4523 -524 2690 C ATOM 277 CD1 TYR A 201 88.848 12.363 23.383 1.00 76.96 C ANISOU 277 CD1 TYR A 201 11097 8551 9592 4697 -420 2613 C ATOM 278 CD2 TYR A 201 86.609 11.607 23.685 1.00 76.23 C ANISOU 278 CD2 TYR A 201 11214 8085 9666 4433 -613 2674 C ATOM 279 CE1 TYR A 201 88.889 11.757 22.145 1.00 78.76 C ANISOU 279 CE1 TYR A 201 11571 8536 9818 4786 -395 2516 C ATOM 280 CE2 TYR A 201 86.641 10.999 22.446 1.00 75.52 C ANISOU 280 CE2 TYR A 201 11365 7751 9576 4508 -610 2574 C ATOM 281 CZ TYR A 201 87.783 11.078 21.683 1.00 76.22 C ANISOU 281 CZ TYR A 201 11484 7906 9570 4688 -496 2492 C ATOM 282 OH TYR A 201 87.822 10.474 20.450 1.00 84.07 O ANISOU 282 OH TYR A 201 12748 8652 10543 4769 -478 2387 O ATOM 283 N LYS A 202 86.219 15.070 27.531 1.00 69.45 N ANISOU 283 N LYS A 202 9577 8154 8658 4087 -591 2909 N ATOM 284 CA LYS A 202 86.164 15.447 28.933 1.00 69.20 C ANISOU 284 CA LYS A 202 9392 8323 8579 4022 -583 3020 C ATOM 285 C LYS A 202 86.662 14.285 29.795 1.00 71.18 C ANISOU 285 C LYS A 202 9661 8553 8832 4116 -589 3135 C ATOM 286 O LYS A 202 86.280 13.135 29.580 1.00 72.45 O ANISOU 286 O LYS A 202 9982 8463 9083 4143 -620 3168 O ATOM 287 CB LYS A 202 84.742 15.850 29.324 1.00 68.12 C ANISOU 287 CB LYS A 202 9271 8100 8510 3845 -614 3066 C ATOM 288 CG LYS A 202 84.483 15.853 30.819 1.00 75.94 C ANISOU 288 CG LYS A 202 10177 9212 9466 3787 -595 3208 C ATOM 289 CD LYS A 202 83.042 16.242 31.146 1.00 73.81 C ANISOU 289 CD LYS A 202 9920 8843 9284 3624 -596 3264 C ATOM 290 CE LYS A 202 82.795 17.729 30.915 1.00 72.83 C ANISOU 290 CE LYS A 202 9678 8879 9116 3539 -567 3192 C ATOM 291 NZ LYS A 202 81.426 18.130 31.334 1.00 69.56 N1+ ANISOU 291 NZ LYS A 202 9249 8382 8799 3393 -549 3266 N1+ ATOM 292 N GLY A 203 87.530 14.589 30.758 1.00 79.98 N ANISOU 292 N GLY A 203 10617 9926 9844 4165 -569 3198 N ATOM 293 CA GLY A 203 88.089 13.579 31.642 1.00 73.62 C ANISOU 293 CA GLY A 203 9818 9128 9024 4262 -585 3314 C ATOM 294 C GLY A 203 88.171 14.045 33.086 1.00 73.70 C ANISOU 294 C GLY A 203 9707 9364 8931 4207 -596 3424 C ATOM 295 O GLY A 203 88.032 15.228 33.382 1.00 72.25 O ANISOU 295 O GLY A 203 9408 9372 8672 4113 -582 3400 O ATOM 296 N TYR A 204 88.402 13.102 33.989 1.00 76.69 N ANISOU 296 N TYR A 204 10128 9715 9297 4270 -622 3548 N ATOM 297 CA TYR A 204 88.477 13.387 35.419 1.00 76.11 C ANISOU 297 CA TYR A 204 9981 9829 9107 4229 -641 3667 C ATOM 298 C TYR A 204 89.779 12.844 36.027 1.00 82.21 C ANISOU 298 C TYR A 204 10679 10743 9813 4382 -686 3735 C ATOM 299 O TYR A 204 89.932 11.643 36.231 1.00 82.95 O ANISOU 299 O TYR A 204 10877 10685 9955 4477 -706 3814 O ATOM 300 CB TYR A 204 87.259 12.795 36.131 1.00 76.48 C ANISOU 300 CB TYR A 204 10173 9690 9196 4133 -630 3785 C ATOM 301 CG TYR A 204 85.959 13.034 35.375 1.00 90.44 C ANISOU 301 CG TYR A 204 12023 11255 11085 4003 -599 3729 C ATOM 302 CD1 TYR A 204 85.204 14.183 35.593 1.00 89.56 C ANISOU 302 CD1 TYR A 204 11843 11243 10944 3864 -560 3716 C ATOM 303 CD2 TYR A 204 85.500 12.120 34.424 1.00 90.61 C ANISOU 303 CD2 TYR A 204 12191 10982 11254 4022 -615 3690 C ATOM 304 CE1 TYR A 204 84.021 14.411 34.905 1.00 84.77 C ANISOU 304 CE1 TYR A 204 11293 10450 10465 3749 -542 3673 C ATOM 305 CE2 TYR A 204 84.320 12.339 33.725 1.00 85.68 C ANISOU 305 CE2 TYR A 204 11637 10170 10749 3899 -613 3642 C ATOM 306 CZ TYR A 204 83.586 13.489 33.967 1.00 85.94 C ANISOU 306 CZ TYR A 204 11580 10309 10764 3765 -579 3636 C ATOM 307 OH TYR A 204 82.414 13.716 33.279 1.00 80.52 O ANISOU 307 OH TYR A 204 10945 9435 10212 3647 -586 3598 O ATOM 308 N VAL A 205 90.726 13.743 36.286 1.00 82.86 N ANISOU 308 N VAL A 205 10578 11113 9794 4406 -707 3705 N ATOM 309 CA VAL A 205 91.966 13.394 36.967 1.00 84.52 C ANISOU 309 CA VAL A 205 10683 11491 9941 4535 -771 3778 C ATOM 310 C VAL A 205 91.963 14.007 38.360 1.00 85.40 C ANISOU 310 C VAL A 205 10734 11819 9895 4453 -828 3872 C ATOM 311 O VAL A 205 91.522 15.150 38.547 1.00 78.74 O ANISOU 311 O VAL A 205 9835 11111 8973 4320 -809 3831 O ATOM 312 CB VAL A 205 93.212 13.879 36.206 1.00 86.04 C ANISOU 312 CB VAL A 205 10693 11852 10146 4640 -765 3684 C ATOM 313 CG1 VAL A 205 94.476 13.524 36.997 1.00 91.28 C ANISOU 313 CG1 VAL A 205 11226 12695 10761 4769 -848 3775 C ATOM 314 CG2 VAL A 205 93.264 13.264 34.825 1.00 83.88 C ANISOU 314 CG2 VAL A 205 10503 11362 10005 4737 -695 3594 C ATOM 315 N ASN A 206 92.482 13.255 39.329 1.00 86.76 N ANISOU 315 N ASN A 206 10928 12025 10013 4537 -901 3998 N ATOM 316 CA ASN A 206 92.302 13.603 40.731 1.00 88.22 C ANISOU 316 CA ASN A 206 11127 12356 10034 4460 -957 4109 C ATOM 317 C ASN A 206 90.817 13.840 40.996 1.00 91.36 C ANISOU 317 C ASN A 206 11674 12622 10418 4305 -874 4135 C ATOM 318 O ASN A 206 89.971 13.023 40.615 1.00 91.72 O ANISOU 318 O ASN A 206 11869 12399 10582 4298 -816 4158 O ATOM 319 CB ASN A 206 93.135 14.834 41.108 1.00 83.18 C ANISOU 319 CB ASN A 206 10290 12047 9266 4422 -1024 4066 C ATOM 320 CG ASN A 206 94.544 14.468 41.574 1.00 99.44 C ANISOU 320 CG ASN A 206 12220 14268 11293 4561 -1148 4124 C ATOM 321 OD1 ASN A 206 94.738 13.973 42.690 1.00 87.77 O ANISOU 321 OD1 ASN A 206 10804 12825 9719 4592 -1237 4252 O ATOM 322 ND2 ASN A 206 95.533 14.718 40.721 1.00 98.93 N ANISOU 322 ND2 ASN A 206 11974 14302 11312 4648 -1152 4035 N ATOM 323 N ASN A 207 90.495 14.962 41.628 1.00 89.98 N ANISOU 323 N ASN A 207 11453 12628 10106 4181 -867 4135 N ATOM 324 CA ASN A 207 89.104 15.324 41.836 1.00 88.74 C ANISOU 324 CA ASN A 207 11410 12363 9945 4038 -768 4161 C ATOM 325 C ASN A 207 88.792 16.566 41.015 1.00 85.19 C ANISOU 325 C ASN A 207 10855 11992 9520 3941 -714 4023 C ATOM 326 O ASN A 207 87.886 17.344 41.337 1.00 75.78 O ANISOU 326 O ASN A 207 9693 10823 8277 3814 -644 4035 O ATOM 327 CB ASN A 207 88.816 15.554 43.324 1.00 95.62 C ANISOU 327 CB ASN A 207 12359 13347 10624 3973 -774 4294 C ATOM 328 CG ASN A 207 87.337 15.427 43.661 1.00 99.77 C ANISOU 328 CG ASN A 207 13042 13685 11179 3862 -647 4376 C ATOM 329 OD1 ASN A 207 86.481 15.468 42.774 1.00103.97 O ANISOU 329 OD1 ASN A 207 13590 14042 11872 3807 -566 4317 O ATOM 330 ND2 ASN A 207 87.030 15.277 44.945 1.00 99.84 N ANISOU 330 ND2 ASN A 207 13171 13725 11036 3829 -629 4517 N ATOM 331 N THR A 208 89.564 16.744 39.947 1.00 82.81 N ANISOU 331 N THR A 208 10434 11730 9298 4009 -738 3899 N ATOM 332 CA THR A 208 89.419 17.898 39.064 1.00 78.89 C ANISOU 332 CA THR A 208 9837 11310 8826 3935 -695 3763 C ATOM 333 C THR A 208 89.132 17.481 37.611 1.00 73.17 C ANISOU 333 C THR A 208 9158 10360 8284 3972 -650 3659 C ATOM 334 O THR A 208 89.683 16.501 37.109 1.00 74.34 O ANISOU 334 O THR A 208 9338 10391 8517 4096 -671 3654 O ATOM 335 CB THR A 208 90.685 18.785 39.110 1.00 77.02 C ANISOU 335 CB THR A 208 9404 11374 8486 3965 -759 3701 C ATOM 336 OG1 THR A 208 91.164 19.010 37.778 1.00 73.41 O ANISOU 336 OG1 THR A 208 8859 10897 8137 4019 -731 3571 O ATOM 337 CG2 THR A 208 91.781 18.116 39.935 1.00 76.88 C ANISOU 337 CG2 THR A 208 9339 11472 8399 4076 -863 3792 C ATOM 338 N THR A 209 88.266 18.229 36.935 1.00 72.94 N ANISOU 338 N THR A 209 9141 10265 8308 3868 -591 3580 N ATOM 339 CA THR A 209 87.924 17.907 35.550 1.00 70.30 C ANISOU 339 CA THR A 209 8872 9712 8127 3890 -565 3477 C ATOM 340 C THR A 209 88.909 18.525 34.547 1.00 69.69 C ANISOU 340 C THR A 209 8676 9760 8044 3957 -563 3346 C ATOM 341 O THR A 209 89.353 19.662 34.701 1.00 68.92 O ANISOU 341 O THR A 209 8438 9899 7850 3915 -560 3304 O ATOM 342 CB THR A 209 86.494 18.349 35.228 1.00 68.70 C ANISOU 342 CB THR A 209 8745 9353 8004 3752 -517 3460 C ATOM 343 OG1 THR A 209 85.586 17.565 36.005 1.00 69.59 O ANISOU 343 OG1 THR A 209 8976 9304 8160 3708 -502 3590 O ATOM 344 CG2 THR A 209 86.187 18.126 33.771 1.00 67.91 C ANISOU 344 CG2 THR A 209 8717 9042 8041 3766 -517 3344 C ATOM 345 N VAL A 210 89.264 17.755 33.525 1.00 70.23 N ANISOU 345 N VAL A 210 8807 9666 8211 4064 -556 3288 N ATOM 346 CA VAL A 210 90.258 18.198 32.561 1.00 70.04 C ANISOU 346 CA VAL A 210 8684 9744 8184 4154 -530 3181 C ATOM 347 C VAL A 210 89.812 17.919 31.144 1.00 69.36 C ANISOU 347 C VAL A 210 8735 9415 8201 4177 -493 3077 C ATOM 348 O VAL A 210 88.942 17.087 30.914 1.00 69.56 O ANISOU 348 O VAL A 210 8931 9181 8316 4153 -510 3096 O ATOM 349 CB VAL A 210 91.638 17.513 32.778 1.00 72.17 C ANISOU 349 CB VAL A 210 8863 10117 8441 4322 -550 3223 C ATOM 350 CG1 VAL A 210 92.204 17.845 34.151 1.00 73.10 C ANISOU 350 CG1 VAL A 210 8840 10492 8443 4302 -614 3320 C ATOM 351 CG2 VAL A 210 91.532 16.018 32.567 1.00 73.72 C ANISOU 351 CG2 VAL A 210 9221 10057 8733 4427 -556 3270 C ATOM 352 N ALA A 211 90.430 18.621 30.202 1.00 68.73 N ANISOU 352 N ALA A 211 8587 9422 8104 4224 -447 2972 N ATOM 353 CA ALA A 211 90.174 18.430 28.782 1.00 68.30 C ANISOU 353 CA ALA A 211 8676 9157 8116 4267 -409 2867 C ATOM 354 C ALA A 211 91.293 17.616 28.158 1.00 70.06 C ANISOU 354 C ALA A 211 8912 9343 8363 4462 -363 2849 C ATOM 355 O ALA A 211 92.457 17.999 28.240 1.00 70.73 O ANISOU 355 O ALA A 211 8824 9649 8403 4555 -322 2849 O ATOM 356 CB ALA A 211 90.039 19.771 28.088 1.00 66.53 C ANISOU 356 CB ALA A 211 8399 9031 7849 4198 -371 2766 C ATOM 357 N VAL A 212 90.940 16.495 27.537 1.00 70.97 N ANISOU 357 N VAL A 212 9229 9178 8556 4525 -366 2837 N ATOM 358 CA VAL A 212 91.937 15.577 26.990 1.00 72.93 C ANISOU 358 CA VAL A 212 9518 9361 8833 4724 -309 2831 C ATOM 359 C VAL A 212 91.878 15.480 25.479 1.00 72.87 C ANISOU 359 C VAL A 212 9689 9158 8841 4795 -244 2711 C ATOM 360 O VAL A 212 90.914 14.948 24.929 1.00 72.69 O ANISOU 360 O VAL A 212 9887 8863 8867 4739 -287 2674 O ATOM 361 CB VAL A 212 91.762 14.157 27.541 1.00 74.69 C ANISOU 361 CB VAL A 212 9855 9404 9120 4776 -356 2926 C ATOM 362 CG1 VAL A 212 92.941 13.299 27.135 1.00 76.94 C ANISOU 362 CG1 VAL A 212 10140 9664 9428 4996 -289 2934 C ATOM 363 CG2 VAL A 212 91.596 14.182 29.051 1.00 74.81 C ANISOU 363 CG2 VAL A 212 9754 9564 9106 4693 -428 3051 C ATOM 364 N LYS A 213 92.915 15.972 24.806 1.00 75.92 N ANISOU 364 N LYS A 213 9985 9677 9186 4921 -141 2652 N ATOM 365 CA LYS A 213 92.974 15.901 23.345 1.00 75.04 C ANISOU 365 CA LYS A 213 10063 9385 9063 5012 -56 2538 C ATOM 366 C LYS A 213 93.772 14.686 22.886 1.00 75.91 C ANISOU 366 C LYS A 213 10273 9359 9211 5220 22 2547 C ATOM 367 O LYS A 213 94.956 14.579 23.188 1.00 77.34 O ANISOU 367 O LYS A 213 10271 9715 9399 5362 95 2596 O ATOM 368 CB LYS A 213 93.593 17.173 22.762 1.00 72.56 C ANISOU 368 CB LYS A 213 9620 9270 8679 5038 40 2467 C ATOM 369 CG LYS A 213 93.487 17.257 21.248 1.00 72.58 C ANISOU 369 CG LYS A 213 9857 9077 8646 5111 125 2344 C ATOM 370 CD LYS A 213 94.089 18.554 20.705 1.00 75.25 C ANISOU 370 CD LYS A 213 10067 9610 8913 5138 233 2283 C ATOM 371 CE LYS A 213 95.614 18.553 20.817 1.00 77.17 C ANISOU 371 CE LYS A 213 10078 10072 9170 5317 371 2324 C ATOM 372 NZ LYS A 213 96.216 19.815 20.296 1.00 74.53 N1+ ANISOU 372 NZ LYS A 213 9603 9930 8786 5340 490 2271 N1+ ATOM 373 N LYS A 214 93.124 13.768 22.171 1.00 76.59 N ANISOU 373 N LYS A 214 10645 9128 9327 5237 3 2500 N ATOM 374 CA LYS A 214 93.845 12.669 21.532 1.00 86.51 C ANISOU 374 CA LYS A 214 12041 10224 10605 5442 99 2486 C ATOM 375 C LYS A 214 94.109 12.994 20.071 1.00 88.12 C ANISOU 375 C LYS A 214 12419 10322 10741 5538 223 2354 C ATOM 376 O LYS A 214 93.173 13.197 19.297 1.00 78.20 O ANISOU 376 O LYS A 214 11391 8872 9449 5436 171 2263 O ATOM 377 CB LYS A 214 93.078 11.352 21.634 1.00 86.83 C ANISOU 377 CB LYS A 214 12310 9968 10713 5418 13 2517 C ATOM 378 CG LYS A 214 93.939 10.134 21.274 1.00 86.86 C ANISOU 378 CG LYS A 214 12418 9838 10746 5641 112 2532 C ATOM 379 CD LYS A 214 93.142 8.840 21.319 1.00 90.79 C ANISOU 379 CD LYS A 214 13162 10024 11311 5610 27 2557 C ATOM 380 CE LYS A 214 91.992 8.873 20.315 1.00 93.81 C ANISOU 380 CE LYS A 214 13834 10135 11674 5483 -38 2441 C ATOM 381 NZ LYS A 214 91.199 7.610 20.329 1.00 96.97 N1+ ANISOU 381 NZ LYS A 214 14470 10221 12152 5440 -127 2466 N1+ ATOM 382 N LEU A 215 95.385 13.016 19.694 1.00 89.13 N ANISOU 382 N LEU A 215 12445 10568 10853 5735 386 2349 N ATOM 383 CA LEU A 215 95.786 13.555 18.396 1.00 90.63 C ANISOU 383 CA LEU A 215 12756 10715 10963 5832 539 2233 C ATOM 384 C LEU A 215 95.280 12.745 17.196 1.00 92.75 C ANISOU 384 C LEU A 215 13431 10622 11189 5884 565 2127 C ATOM 385 O LEU A 215 95.221 11.513 17.230 1.00 83.74 O ANISOU 385 O LEU A 215 12440 9283 10093 5953 547 2151 O ATOM 386 CB LEU A 215 97.311 13.688 18.341 1.00 87.50 C ANISOU 386 CB LEU A 215 12130 10530 10585 6035 725 2267 C ATOM 387 CG LEU A 215 97.834 15.065 18.776 1.00 86.94 C ANISOU 387 CG LEU A 215 11729 10802 10503 5977 753 2292 C ATOM 388 CD1 LEU A 215 97.387 15.388 20.194 1.00 85.14 C ANISOU 388 CD1 LEU A 215 11279 10760 10309 5801 570 2390 C ATOM 389 CD2 LEU A 215 99.357 15.165 18.656 1.00 87.49 C ANISOU 389 CD2 LEU A 215 11554 11071 10616 6169 939 2326 C ATOM 390 N ALA A 216 94.907 13.470 16.144 1.00 95.54 N ANISOU 390 N ALA A 216 13971 10887 11444 5844 601 2008 N ATOM 391 CA ALA A 216 94.403 12.886 14.900 1.00100.78 C ANISOU 391 CA ALA A 216 15048 11212 12031 5872 613 1887 C ATOM 392 C ALA A 216 94.469 13.916 13.761 1.00104.44 C ANISOU 392 C ALA A 216 15651 11667 12364 5882 714 1768 C ATOM 393 O ALA A 216 94.633 15.108 14.012 1.00105.86 O ANISOU 393 O ALA A 216 15612 12083 12529 5827 735 1782 O ATOM 394 CB ALA A 216 92.975 12.380 15.088 1.00 99.73 C ANISOU 394 CB ALA A 216 15105 10850 11938 5674 384 1879 C ATOM 395 N ALA A 217 94.339 13.462 12.515 1.00108.38 N ANISOU 395 N ALA A 217 16530 11890 12760 5950 776 1649 N ATOM 396 CA ALA A 217 94.442 14.362 11.362 1.00107.36 C ANISOU 396 CA ALA A 217 16583 11724 12485 5972 886 1532 C ATOM 397 C ALA A 217 93.093 14.972 10.979 1.00105.10 C ANISOU 397 C ALA A 217 16498 11297 12137 5749 672 1456 C ATOM 398 O ALA A 217 92.085 14.271 10.885 1.00105.03 O ANISOU 398 O ALA A 217 16706 11052 12147 5627 480 1428 O ATOM 399 CB ALA A 217 95.047 13.628 10.170 1.00110.01 C ANISOU 399 CB ALA A 217 17245 11838 12714 6157 1076 1436 C ATOM 400 N LEU A 226 102.500 14.646 12.395 1.00 92.41 N ANISOU 400 N LEU A 226 13027 11087 10999 6984 2155 1901 N ATOM 401 CA LEU A 226 101.715 14.480 13.616 1.00 99.53 C ANISOU 401 CA LEU A 226 13807 12051 11958 6836 1866 1984 C ATOM 402 C LEU A 226 102.566 14.703 14.875 1.00104.19 C ANISOU 402 C LEU A 226 13909 12982 12697 6839 1819 2125 C ATOM 403 O LEU A 226 102.315 15.646 15.630 1.00100.69 O ANISOU 403 O LEU A 226 13225 12765 12266 6682 1690 2162 O ATOM 404 CB LEU A 226 101.066 13.087 13.656 1.00100.60 C ANISOU 404 CB LEU A 226 14238 11893 12092 6864 1746 1985 C ATOM 405 CG LEU A 226 99.840 12.846 14.553 1.00 89.32 C ANISOU 405 CG LEU A 226 12853 10404 10682 6670 1453 2025 C ATOM 406 CD1 LEU A 226 100.023 13.500 15.902 1.00 92.34 C ANISOU 406 CD1 LEU A 226 12816 11115 11153 6562 1326 2143 C ATOM 407 CD2 LEU A 226 98.538 13.320 13.912 1.00 87.18 C ANISOU 407 CD2 LEU A 226 12895 9938 10292 6497 1333 1912 C ATOM 408 N LYS A 227 103.554 13.835 15.106 1.00114.70 N ANISOU 408 N LYS A 227 11126 16117 16337 6079 2793 4007 N ATOM 409 CA LYS A 227 104.422 13.961 16.279 1.00103.80 C ANISOU 409 CA LYS A 227 9475 14869 15095 6049 2549 4190 C ATOM 410 C LYS A 227 105.079 15.339 16.349 1.00106.05 C ANISOU 410 C LYS A 227 9483 15441 15369 5854 2482 4173 C ATOM 411 O LYS A 227 105.260 15.877 17.444 1.00105.40 O ANISOU 411 O LYS A 227 9224 15541 15281 5707 2226 4289 O ATOM 412 CB LYS A 227 105.498 12.875 16.283 1.00107.71 C ANISOU 412 CB LYS A 227 9911 15187 15826 6288 2623 4263 C ATOM 413 CG LYS A 227 106.634 13.123 17.275 1.00109.53 C ANISOU 413 CG LYS A 227 9826 15587 16205 6260 2412 4416 C ATOM 414 CD LYS A 227 106.221 12.814 18.709 1.00111.93 C ANISOU 414 CD LYS A 227 10137 15919 16473 6196 2104 4594 C ATOM 415 CE LYS A 227 107.376 13.012 19.687 1.00111.23 C ANISOU 415 CE LYS A 227 9742 15999 16520 6174 1899 4735 C ATOM 416 NZ LYS A 227 108.583 12.233 19.305 1.00115.17 N1+ ANISOU 416 NZ LYS A 227 10131 16379 17248 6421 2037 4759 N1+ ATOM 417 N GLN A 228 105.437 15.901 15.190 1.00105.81 N ANISOU 417 N GLN A 228 9432 15442 15330 5845 2714 4024 N ATOM 418 CA GLN A 228 105.988 17.257 15.140 1.00102.09 C ANISOU 418 CA GLN A 228 8737 15219 14834 5651 2680 3992 C ATOM 419 C GLN A 228 104.999 18.202 15.792 1.00 98.84 C ANISOU 419 C GLN A 228 8348 14983 14222 5410 2483 4006 C ATOM 420 O GLN A 228 105.351 18.969 16.687 1.00 99.18 O ANISOU 420 O GLN A 228 8190 15223 14271 5246 2278 4088 O ATOM 421 CB GLN A 228 106.279 17.714 13.706 1.00102.31 C ANISOU 421 CB GLN A 228 8808 15229 14837 5660 2970 3818 C ATOM 422 CG GLN A 228 107.554 17.158 13.090 1.00119.05 C ANISOU 422 CG GLN A 228 10814 17253 17167 5843 3150 3799 C ATOM 423 CD GLN A 228 108.827 17.525 13.862 1.00123.38 C ANISOU 423 CD GLN A 228 11022 17965 17889 5816 3002 3916 C ATOM 424 OE1 GLN A 228 108.940 17.269 15.066 1.00120.61 O ANISOU 424 OE1 GLN A 228 10561 17669 17595 5810 2759 4067 O ATOM 425 NE2 GLN A 228 109.796 18.114 13.159 1.00119.89 N ANISOU 425 NE2 GLN A 228 10420 17607 17527 5797 3150 3842 N ATOM 426 N GLN A 229 103.754 18.127 15.334 1.00 96.51 N ANISOU 426 N GLN A 229 8305 14618 13747 5392 2553 3915 N ATOM 427 CA GLN A 229 102.673 18.926 15.884 1.00 93.26 C ANISOU 427 CA GLN A 229 7951 14356 13129 5174 2377 3910 C ATOM 428 C GLN A 229 102.632 18.798 17.409 1.00102.91 C ANISOU 428 C GLN A 229 9057 15662 14381 5098 2061 4088 C ATOM 429 O GLN A 229 102.429 19.783 18.117 1.00101.59 O ANISOU 429 O GLN A 229 8782 15698 14121 4875 1876 4117 O ATOM 430 CB GLN A 229 101.339 18.499 15.265 1.00 91.55 C ANISOU 430 CB GLN A 229 8142 13962 12681 5083 2438 3733 C ATOM 431 CG GLN A 229 100.124 19.283 15.749 1.00 88.29 C ANISOU 431 CG GLN A 229 7870 13664 12013 4788 2244 3669 C ATOM 432 CD GLN A 229 99.979 20.635 15.075 1.00 86.49 C ANISOU 432 CD GLN A 229 7600 13605 11657 4638 2330 3559 C ATOM 433 OE1 GLN A 229 100.659 20.930 14.091 1.00 87.54 O ANISOU 433 OE1 GLN A 229 7653 13747 11861 4742 2561 3505 O ATOM 434 NE2 GLN A 229 99.084 21.468 15.607 1.00 83.86 N ANISOU 434 NE2 GLN A 229 7328 13402 11134 4393 2152 3528 N ATOM 435 N PHE A 230 102.851 17.585 17.910 1.00 95.15 N ANISOU 435 N PHE A 230 8116 14514 13520 5269 2003 4199 N ATOM 436 CA PHE A 230 102.800 17.335 19.344 1.00 95.30 C ANISOU 436 CA PHE A 230 8069 14587 13552 5194 1704 4365 C ATOM 437 C PHE A 230 103.945 18.012 20.090 1.00 96.52 C ANISOU 437 C PHE A 230 7922 14937 13813 5081 1556 4446 C ATOM 438 O PHE A 230 103.726 18.698 21.086 1.00 96.80 O ANISOU 438 O PHE A 230 7871 15148 13759 4867 1323 4504 O ATOM 439 CB PHE A 230 102.818 15.834 19.623 1.00103.06 C ANISOU 439 CB PHE A 230 9192 15322 14645 5418 1700 4466 C ATOM 440 CG PHE A 230 103.019 15.488 21.072 1.00103.89 C ANISOU 440 CG PHE A 230 9216 15471 14788 5362 1408 4647 C ATOM 441 CD1 PHE A 230 101.942 15.441 21.941 1.00100.88 C ANISOU 441 CD1 PHE A 230 8979 15110 14242 5215 1195 4706 C ATOM 442 CD2 PHE A 230 104.282 15.209 21.564 1.00101.35 C ANISOU 442 CD2 PHE A 230 8681 15174 14654 5444 1344 4750 C ATOM 443 CE1 PHE A 230 102.122 15.115 23.271 1.00100.49 C ANISOU 443 CE1 PHE A 230 8870 15098 14211 5152 933 4868 C ATOM 444 CE2 PHE A 230 104.464 14.893 22.891 1.00102.32 C ANISOU 444 CE2 PHE A 230 8738 15343 14795 5390 1077 4910 C ATOM 445 CZ PHE A 230 103.385 14.845 23.746 1.00100.33 C ANISOU 445 CZ PHE A 230 8643 15104 14375 5239 875 4967 C ATOM 446 N ASP A 231 105.168 17.809 19.618 1.00 99.23 N ANISOU 446 N ASP A 231 8111 15249 14343 5220 1692 4443 N ATOM 447 CA ASP A 231 106.324 18.400 20.281 1.00106.75 C ANISOU 447 CA ASP A 231 8768 16386 15404 5133 1563 4514 C ATOM 448 C ASP A 231 106.289 19.916 20.166 1.00104.71 C ANISOU 448 C ASP A 231 8397 16353 15035 4881 1551 4428 C ATOM 449 O ASP A 231 106.685 20.630 21.090 1.00104.83 O ANISOU 449 O ASP A 231 8232 16557 15043 4704 1357 4489 O ATOM 450 CB ASP A 231 107.627 17.859 19.693 1.00104.25 C ANISOU 450 CB ASP A 231 8309 15992 15310 5347 1730 4516 C ATOM 451 CG ASP A 231 107.748 16.358 19.835 1.00111.75 C ANISOU 451 CG ASP A 231 9368 16708 16385 5606 1747 4605 C ATOM 452 OD1 ASP A 231 107.973 15.884 20.972 1.00112.93 O ANISOU 452 OD1 ASP A 231 9451 16875 16584 5619 1524 4755 O ATOM 453 OD2 ASP A 231 107.621 15.653 18.808 1.00112.97 O1+ ANISOU 453 OD2 ASP A 231 9687 16655 16583 5793 1989 4522 O1+ ATOM 454 N GLN A 232 105.804 20.400 19.026 1.00103.26 N ANISOU 454 N GLN A 232 8335 16141 14758 4863 1764 4283 N ATOM 455 CA GLN A 232 105.756 21.832 18.774 1.00102.06 C ANISOU 455 CA GLN A 232 8107 16172 14500 4640 1786 4194 C ATOM 456 C GLN A 232 104.749 22.484 19.701 1.00 92.32 C ANISOU 456 C GLN A 232 6929 15067 13083 4411 1560 4221 C ATOM 457 O GLN A 232 104.973 23.586 20.193 1.00 97.83 O ANISOU 457 O GLN A 232 7488 15949 13735 4198 1455 4218 O ATOM 458 CB GLN A 232 105.410 22.125 17.307 1.00103.48 C ANISOU 458 CB GLN A 232 8437 16275 14605 4684 2071 4033 C ATOM 459 CG GLN A 232 106.544 21.819 16.325 1.00111.89 C ANISOU 459 CG GLN A 232 9417 17257 15839 4850 2308 3979 C ATOM 460 CD GLN A 232 106.247 22.274 14.899 1.00115.68 C ANISOU 460 CD GLN A 232 10048 17685 16221 4849 2579 3812 C ATOM 461 OE1 GLN A 232 105.126 22.695 14.585 1.00115.22 O ANISOU 461 OE1 GLN A 232 10178 17634 15965 4753 2601 3736 O ATOM 462 NE2 GLN A 232 107.256 22.191 14.028 1.00114.60 N ANISOU 462 NE2 GLN A 232 9829 17500 16214 4952 2785 3753 N ATOM 463 N GLU A 233 103.642 21.798 19.953 1.00 90.99 N ANISOU 463 N GLU A 233 6967 14797 12809 4451 1488 4243 N ATOM 464 CA GLU A 233 102.596 22.383 20.776 1.00 88.30 C ANISOU 464 CA GLU A 233 6697 14573 12281 4232 1282 4255 C ATOM 465 C GLU A 233 103.066 22.532 22.221 1.00 89.04 C ANISOU 465 C GLU A 233 6628 14792 12411 4091 1007 4382 C ATOM 466 O GLU A 233 102.653 23.460 22.915 1.00 87.23 O ANISOU 466 O GLU A 233 6368 14721 12054 3850 852 4372 O ATOM 467 CB GLU A 233 101.315 21.551 20.708 1.00 86.95 C ANISOU 467 CB GLU A 233 6784 14264 11988 4312 1267 4249 C ATOM 468 CG GLU A 233 100.436 21.742 21.930 1.00 92.47 C ANISOU 468 CG GLU A 233 7563 15042 12530 4090 988 4296 C ATOM 469 CD GLU A 233 98.954 21.750 21.614 1.00 88.65 C ANISOU 469 CD GLU A 233 7429 14458 11798 3930 991 4131 C ATOM 470 OE1 GLU A 233 98.572 21.306 20.509 1.00 88.79 O ANISOU 470 OE1 GLU A 233 7657 14310 11770 4022 1193 3997 O ATOM 471 OE2 GLU A 233 98.178 22.204 22.482 1.00 80.72 O1+ ANISOU 471 OE2 GLU A 233 6480 13551 10639 3710 791 4131 O1+ ATOM 472 N ILE A 234 103.943 21.631 22.663 1.00 96.48 N ANISOU 472 N ILE A 234 7471 15664 13523 4242 955 4493 N ATOM 473 CA ILE A 234 104.474 21.684 24.026 1.00 95.94 C ANISOU 473 CA ILE A 234 7249 15713 13490 4127 699 4615 C ATOM 474 C ILE A 234 105.549 22.749 24.154 1.00 93.87 C ANISOU 474 C ILE A 234 6728 15641 13296 3997 693 4594 C ATOM 475 O ILE A 234 105.643 23.436 25.170 1.00 93.42 O ANISOU 475 O ILE A 234 6570 15749 13178 3784 497 4629 O ATOM 476 CB ILE A 234 105.065 20.343 24.469 1.00 95.92 C ANISOU 476 CB ILE A 234 7231 15573 13643 4345 641 4748 C ATOM 477 CG1 ILE A 234 104.161 19.194 24.037 1.00 95.57 C ANISOU 477 CG1 ILE A 234 7452 15292 13567 4526 722 4755 C ATOM 478 CG2 ILE A 234 105.262 20.335 25.971 1.00 96.62 C ANISOU 478 CG2 ILE A 234 7228 15775 13708 4205 351 4871 C ATOM 479 CD1 ILE A 234 104.575 17.863 24.596 1.00 98.33 C ANISOU 479 CD1 ILE A 234 7829 15485 14047 4724 645 4896 C ATOM 480 N LYS A 235 106.360 22.873 23.110 1.00 95.26 N ANISOU 480 N LYS A 235 6807 15789 13596 4122 917 4530 N ATOM 481 CA LYS A 235 107.414 23.878 23.046 1.00 96.29 C ANISOU 481 CA LYS A 235 6699 16087 13801 4013 949 4496 C ATOM 482 C LYS A 235 106.840 25.292 23.150 1.00 93.54 C ANISOU 482 C LYS A 235 6367 15890 13284 3733 914 4410 C ATOM 483 O LYS A 235 107.407 26.155 23.824 1.00 93.91 O ANISOU 483 O LYS A 235 6240 16110 13333 3550 800 4423 O ATOM 484 CB LYS A 235 108.212 23.712 21.747 1.00103.10 C ANISOU 484 CB LYS A 235 7503 16865 14805 4198 1226 4423 C ATOM 485 CG LYS A 235 109.176 24.847 21.420 1.00104.87 C ANISOU 485 CG LYS A 235 7513 17246 15086 4076 1310 4358 C ATOM 486 CD LYS A 235 109.299 25.044 19.900 1.00104.82 C ANISOU 486 CD LYS A 235 7576 17149 15103 4170 1616 4228 C ATOM 487 CE LYS A 235 107.923 25.258 19.243 1.00100.37 C ANISOU 487 CE LYS A 235 7292 16498 14346 4126 1712 4135 C ATOM 488 NZ LYS A 235 107.699 26.641 18.716 1.00 96.34 N1+ ANISOU 488 NZ LYS A 235 6797 16091 13716 3926 1806 4025 N1+ ATOM 489 N VAL A 236 105.705 25.516 22.487 1.00 98.86 N ANISOU 489 N VAL A 236 7256 16499 13810 3705 1015 4320 N ATOM 490 CA VAL A 236 105.007 26.805 22.531 1.00 94.46 C ANISOU 490 CA VAL A 236 6748 16063 13080 3459 991 4236 C ATOM 491 C VAL A 236 104.273 26.994 23.862 1.00 86.71 C ANISOU 491 C VAL A 236 5811 15171 11965 3262 721 4292 C ATOM 492 O VAL A 236 104.153 28.110 24.368 1.00 85.49 O ANISOU 492 O VAL A 236 5605 15161 11717 3026 634 4257 O ATOM 493 CB VAL A 236 104.004 26.945 21.354 1.00 86.09 C ANISOU 493 CB VAL A 236 5908 14907 11894 3508 1189 4118 C ATOM 494 CG1 VAL A 236 103.138 28.188 21.519 1.00 83.30 C ANISOU 494 CG1 VAL A 236 5628 14673 11351 3264 1138 4043 C ATOM 495 CG2 VAL A 236 104.745 26.987 20.019 1.00 88.92 C ANISOU 495 CG2 VAL A 236 6235 15194 12357 3652 1468 4039 C ATOM 496 N MET A 237 103.796 25.897 24.434 1.00 86.94 N ANISOU 496 N MET A 237 5945 15105 11985 3356 594 4376 N ATOM 497 CA MET A 237 103.112 25.956 25.718 1.00 85.76 C ANISOU 497 CA MET A 237 5854 15024 11706 3172 339 4429 C ATOM 498 C MET A 237 104.091 26.269 26.845 1.00 93.36 C ANISOU 498 C MET A 237 6607 16127 12739 3048 162 4508 C ATOM 499 O MET A 237 103.729 26.922 27.831 1.00 86.44 O ANISOU 499 O MET A 237 5732 15370 11741 2812 -14 4506 O ATOM 500 CB MET A 237 102.390 24.642 25.994 1.00 85.80 C ANISOU 500 CB MET A 237 6039 14876 11687 3311 263 4501 C ATOM 501 CG MET A 237 100.889 24.781 26.066 1.00 86.90 C ANISOU 501 CG MET A 237 6403 14997 11616 3195 207 4440 C ATOM 502 SD MET A 237 100.249 25.945 24.862 1.00 80.37 S ANISOU 502 SD MET A 237 5643 14225 10670 3124 410 4275 S ATOM 503 CE MET A 237 98.937 24.969 24.122 1.00102.66 C ANISOU 503 CE MET A 237 8739 16881 13386 3292 494 4237 C ATOM 504 N ALA A 238 105.332 25.805 26.679 1.00 91.92 N ANISOU 504 N ALA A 238 6245 15933 12748 3211 216 4568 N ATOM 505 CA ALA A 238 106.378 25.958 27.686 1.00 92.76 C ANISOU 505 CA ALA A 238 6133 16174 12937 3135 54 4650 C ATOM 506 C ALA A 238 106.779 27.417 27.882 1.00 92.19 C ANISOU 506 C ALA A 238 5917 16292 12820 2890 43 4577 C ATOM 507 O ALA A 238 106.932 27.878 29.012 1.00 92.42 O ANISOU 507 O ALA A 238 5869 16456 12789 2697 -149 4611 O ATOM 508 CB ALA A 238 107.583 25.130 27.307 1.00 96.10 C ANISOU 508 CB ALA A 238 6397 16539 13579 3387 138 4719 C ATOM 509 N LYS A 239 106.946 28.139 26.776 1.00 92.26 N ANISOU 509 N LYS A 239 5901 16304 12851 2895 257 4474 N ATOM 510 CA LYS A 239 107.222 29.577 26.827 1.00103.11 C ANISOU 510 CA LYS A 239 7171 17832 14174 2662 277 4393 C ATOM 511 C LYS A 239 105.999 30.402 27.255 1.00103.49 C ANISOU 511 C LYS A 239 7389 17924 14008 2427 193 4329 C ATOM 512 O LYS A 239 106.142 31.399 27.965 1.00106.84 O ANISOU 512 O LYS A 239 7738 18490 14368 2193 94 4303 O ATOM 513 CB LYS A 239 107.721 30.081 25.467 1.00 91.20 C ANISOU 513 CB LYS A 239 5611 16294 12745 2740 545 4301 C ATOM 514 CG LYS A 239 109.226 29.926 25.227 1.00 96.21 C ANISOU 514 CG LYS A 239 5992 16978 13584 2850 618 4329 C ATOM 515 CD LYS A 239 110.051 30.837 26.141 1.00 97.97 C ANISOU 515 CD LYS A 239 5997 17403 13825 2634 481 4340 C ATOM 516 CE LYS A 239 111.557 30.680 25.901 1.00101.94 C ANISOU 516 CE LYS A 239 6229 17972 14531 2744 550 4362 C ATOM 517 NZ LYS A 239 112.373 31.616 26.735 1.00100.66 N1+ ANISOU 517 NZ LYS A 239 5847 18017 14382 2525 429 4359 N1+ ATOM 518 N CYS A 240 104.804 29.986 26.837 1.00 85.56 N ANISOU 518 N CYS A 240 5346 15535 11628 2489 234 4299 N ATOM 519 CA CYS A 240 103.615 30.815 27.017 1.00 85.17 C ANISOU 519 CA CYS A 240 5458 15523 11380 2288 194 4219 C ATOM 520 C CYS A 240 102.625 30.313 28.058 1.00 85.43 C ANISOU 520 C CYS A 240 5640 15541 11279 2202 -17 4261 C ATOM 521 O CYS A 240 101.725 29.537 27.737 1.00 80.23 O ANISOU 521 O CYS A 240 5158 14764 10561 2315 0 4261 O ATOM 522 CB CYS A 240 102.866 30.958 25.692 1.00 83.27 C ANISOU 522 CB CYS A 240 5375 15185 11079 2388 409 4125 C ATOM 523 SG CYS A 240 103.887 31.366 24.269 1.00 94.12 S ANISOU 523 SG CYS A 240 6635 16530 12595 2518 697 4063 S ATOM 524 N GLN A 241 102.778 30.768 29.298 1.00 86.53 N ANISOU 524 N GLN A 241 5716 15798 11364 1992 -209 4287 N ATOM 525 CA GLN A 241 101.718 30.610 30.291 1.00 84.35 C ANISOU 525 CA GLN A 241 5603 15522 10924 1844 -391 4291 C ATOM 526 C GLN A 241 101.358 31.973 30.853 1.00 81.25 C ANISOU 526 C GLN A 241 5219 15258 10395 1557 -447 4204 C ATOM 527 O GLN A 241 102.238 32.743 31.246 1.00 82.43 O ANISOU 527 O GLN A 241 5201 15525 10592 1435 -470 4202 O ATOM 528 CB GLN A 241 102.130 29.661 31.413 1.00 81.96 C ANISOU 528 CB GLN A 241 5258 15216 10669 1869 -584 4411 C ATOM 529 CG GLN A 241 102.215 28.211 30.991 1.00101.89 C ANISOU 529 CG GLN A 241 7830 17584 13300 2147 -550 4500 C ATOM 530 CD GLN A 241 102.372 27.284 32.177 1.00107.16 C ANISOU 530 CD GLN A 241 8505 18234 13977 2155 -754 4619 C ATOM 531 OE1 GLN A 241 102.171 27.687 33.325 1.00106.74 O ANISOU 531 OE1 GLN A 241 8464 18275 13817 1937 -924 4621 O ATOM 532 NE2 GLN A 241 102.737 26.034 31.909 1.00109.62 N ANISOU 532 NE2 GLN A 241 8817 18416 14416 2408 -730 4717 N ATOM 533 N HIS A 242 100.062 32.268 30.870 1.00 75.96 N ANISOU 533 N HIS A 242 4745 14563 9555 1453 -462 4127 N ATOM 534 CA HIS A 242 99.571 33.562 31.308 1.00 74.38 C ANISOU 534 CA HIS A 242 4582 14461 9217 1196 -492 4032 C ATOM 535 C HIS A 242 98.166 33.358 31.837 1.00 72.26 C ANISOU 535 C HIS A 242 4536 14153 8769 1093 -595 3986 C ATOM 536 O HIS A 242 97.559 32.316 31.598 1.00 71.86 O ANISOU 536 O HIS A 242 4608 13994 8701 1233 -606 4014 O ATOM 537 CB HIS A 242 99.613 34.563 30.150 1.00 73.50 C ANISOU 537 CB HIS A 242 4445 14366 9114 1209 -287 3945 C ATOM 538 CG HIS A 242 99.238 35.967 30.522 1.00 72.19 C ANISOU 538 CG HIS A 242 4304 14297 8829 960 -296 3852 C ATOM 539 ND1 HIS A 242 97.963 36.468 30.354 1.00 69.76 N ANISOU 539 ND1 HIS A 242 4175 13973 8358 878 -275 3762 N ATOM 540 CD2 HIS A 242 99.979 36.990 31.008 1.00 73.12 C ANISOU 540 CD2 HIS A 242 4290 14524 8970 782 -314 3830 C ATOM 541 CE1 HIS A 242 97.934 37.730 30.737 1.00 69.26 C ANISOU 541 CE1 HIS A 242 4092 13996 8227 665 -277 3693 C ATOM 542 NE2 HIS A 242 99.143 38.075 31.136 1.00 71.25 N ANISOU 542 NE2 HIS A 242 4162 14322 8588 598 -299 3730 N ATOM 543 N GLU A 243 97.668 34.344 32.574 1.00 79.53 N ANISOU 543 N GLU A 243 5507 15155 9557 847 -666 3911 N ATOM 544 CA GLU A 243 96.331 34.312 33.172 1.00 69.13 C ANISOU 544 CA GLU A 243 4396 13809 8061 713 -759 3845 C ATOM 545 C GLU A 243 95.220 34.084 32.136 1.00 79.21 C ANISOU 545 C GLU A 243 5836 15002 9259 830 -651 3778 C ATOM 546 O GLU A 243 94.212 33.419 32.403 1.00 66.12 O ANISOU 546 O GLU A 243 4349 13275 7498 823 -721 3755 O ATOM 547 CB GLU A 243 96.094 35.625 33.924 1.00 68.31 C ANISOU 547 CB GLU A 243 4301 13808 7846 442 -803 3758 C ATOM 548 CG GLU A 243 94.667 35.900 34.299 1.00 66.09 C ANISOU 548 CG GLU A 243 4228 13504 7381 302 -843 3655 C ATOM 549 CD GLU A 243 94.134 34.915 35.309 1.00 66.20 C ANISOU 549 CD GLU A 243 4361 13457 7335 254 -994 3682 C ATOM 550 OE1 GLU A 243 94.906 34.037 35.755 1.00 81.46 O ANISOU 550 OE1 GLU A 243 6211 15373 9367 332 -1078 3793 O ATOM 551 OE2 GLU A 243 92.940 35.019 35.654 1.00 64.52 O1+ ANISOU 551 OE2 GLU A 243 4324 13211 6979 140 -1024 3589 O1+ ATOM 552 N ASN A 244 95.431 34.623 30.940 1.00 66.84 N ANISOU 552 N ASN A 244 4215 13443 7738 939 -475 3745 N ATOM 553 CA ASN A 244 94.432 34.576 29.895 1.00 65.11 C ANISOU 553 CA ASN A 244 4136 13170 7433 1048 -360 3675 C ATOM 554 C ASN A 244 94.745 33.574 28.787 1.00 65.92 C ANISOU 554 C ASN A 244 4226 13177 7646 1330 -238 3729 C ATOM 555 O ASN A 244 94.289 33.729 27.668 1.00 64.99 O ANISOU 555 O ASN A 244 4169 13031 7492 1448 -87 3672 O ATOM 556 CB ASN A 244 94.259 35.975 29.315 1.00 64.03 C ANISOU 556 CB ASN A 244 3981 13104 7242 964 -233 3585 C ATOM 557 CG ASN A 244 93.767 36.972 30.352 1.00 63.08 C ANISOU 557 CG ASN A 244 3905 13065 6997 695 -339 3517 C ATOM 558 OD1 ASN A 244 94.536 37.759 30.907 1.00 64.01 O ANISOU 558 OD1 ASN A 244 3901 13258 7161 552 -361 3525 O ATOM 559 ND2 ASN A 244 92.466 36.936 30.621 1.00 77.66 N ANISOU 559 ND2 ASN A 244 5933 14893 8681 621 -402 3441 N ATOM 560 N LEU A 245 95.516 32.539 29.104 1.00 67.79 N ANISOU 560 N LEU A 245 4387 13359 8012 1443 -295 3835 N ATOM 561 CA LEU A 245 95.773 31.464 28.147 1.00 68.74 C ANISOU 561 CA LEU A 245 4512 13367 8237 1718 -182 3887 C ATOM 562 C LEU A 245 95.436 30.114 28.734 1.00 69.32 C ANISOU 562 C LEU A 245 4687 13345 8307 1790 -315 3963 C ATOM 563 O LEU A 245 95.665 29.879 29.913 1.00 70.12 O ANISOU 563 O LEU A 245 4763 13468 8412 1671 -482 4021 O ATOM 564 CB LEU A 245 97.233 31.452 27.699 1.00 75.66 C ANISOU 564 CB LEU A 245 5184 14245 9317 1846 -70 3950 C ATOM 565 CG LEU A 245 97.879 32.751 27.241 1.00 71.06 C ANISOU 565 CG LEU A 245 4474 13753 8772 1761 59 3893 C ATOM 566 CD1 LEU A 245 99.361 32.497 27.039 1.00 73.67 C ANISOU 566 CD1 LEU A 245 4602 14081 9307 1875 126 3964 C ATOM 567 CD2 LEU A 245 97.207 33.292 25.978 1.00 69.47 C ANISOU 567 CD2 LEU A 245 4377 13526 8494 1828 257 3792 C ATOM 568 N VAL A 246 94.905 29.219 27.913 1.00 69.07 N ANISOU 568 N VAL A 246 4777 13203 8265 1987 -234 3964 N ATOM 569 CA VAL A 246 94.599 27.891 28.400 1.00 69.81 C ANISOU 569 CA VAL A 246 4981 13186 8360 2068 -344 4044 C ATOM 570 C VAL A 246 95.889 27.166 28.740 1.00 73.83 C ANISOU 570 C VAL A 246 5334 13648 9070 2199 -366 4176 C ATOM 571 O VAL A 246 96.761 26.985 27.899 1.00 73.92 O ANISOU 571 O VAL A 246 5230 13620 9237 2394 -212 4205 O ATOM 572 CB VAL A 246 93.799 27.065 27.400 1.00 69.20 C ANISOU 572 CB VAL A 246 5146 12927 8222 2211 -213 3958 C ATOM 573 CG1 VAL A 246 93.779 25.614 27.842 1.00 70.61 C ANISOU 573 CG1 VAL A 246 5416 12965 8449 2327 -298 4063 C ATOM 574 CG2 VAL A 246 92.389 27.604 27.291 1.00 66.70 C ANISOU 574 CG2 VAL A 246 5050 12614 7678 2033 -221 3795 C ATOM 575 N GLU A 247 95.974 26.764 29.998 1.00 73.33 N ANISOU 575 N GLU A 247 5277 13590 8995 2086 -557 4248 N ATOM 576 CA GLU A 247 97.137 26.123 30.569 1.00 76.00 C ANISOU 576 CA GLU A 247 5471 13908 9499 2178 -624 4378 C ATOM 577 C GLU A 247 97.205 24.642 30.202 1.00 77.53 C ANISOU 577 C GLU A 247 5744 13924 9788 2442 -589 4478 C ATOM 578 O GLU A 247 96.266 23.885 30.456 1.00 76.86 O ANISOU 578 O GLU A 247 5858 13744 9601 2442 -661 4493 O ATOM 579 CB GLU A 247 97.092 26.307 32.083 1.00 76.24 C ANISOU 579 CB GLU A 247 5498 14016 9453 1946 -841 4409 C ATOM 580 CG GLU A 247 98.287 25.837 32.859 1.00 79.04 C ANISOU 580 CG GLU A 247 5690 14392 9949 1999 -942 4538 C ATOM 581 CD GLU A 247 98.076 26.011 34.359 1.00 90.40 C ANISOU 581 CD GLU A 247 7160 15907 11281 1761 -1153 4556 C ATOM 582 OE1 GLU A 247 97.022 26.576 34.744 1.00 88.12 O ANISOU 582 OE1 GLU A 247 7013 15651 10816 1549 -1200 4454 O ATOM 583 OE2 GLU A 247 98.955 25.585 35.149 1.00 91.05 O1+ ANISOU 583 OE2 GLU A 247 7127 16018 11451 1789 -1265 4667 O1+ ATOM 584 N LEU A 248 98.317 24.240 29.585 1.00 78.98 N ANISOU 584 N LEU A 248 5992 14128 9890 2174 -419 2584 N ATOM 585 CA LEU A 248 98.588 22.828 29.341 1.00 76.27 C ANISOU 585 CA LEU A 248 5661 13651 9667 2489 -401 2722 C ATOM 586 C LEU A 248 99.049 22.181 30.636 1.00 70.91 C ANISOU 586 C LEU A 248 4881 13076 8986 2550 -596 2885 C ATOM 587 O LEU A 248 100.042 22.605 31.224 1.00 73.29 O ANISOU 587 O LEU A 248 4949 13585 9314 2506 -688 2901 O ATOM 588 CB LEU A 248 99.644 22.644 28.254 1.00 70.18 C ANISOU 588 CB LEU A 248 4731 12863 9072 2701 -242 2697 C ATOM 589 CG LEU A 248 99.979 21.191 27.888 1.00 75.54 C ANISOU 589 CG LEU A 248 5428 13373 9900 3053 -195 2816 C ATOM 590 CD1 LEU A 248 98.821 20.516 27.144 1.00 70.64 C ANISOU 590 CD1 LEU A 248 5110 12479 9252 3153 -93 2796 C ATOM 591 CD2 LEU A 248 101.268 21.106 27.078 1.00 75.96 C ANISOU 591 CD2 LEU A 248 5252 13473 10138 3247 -53 2788 C ATOM 592 N LEU A 249 98.315 21.167 31.081 1.00 70.93 N ANISOU 592 N LEU A 249 5063 12931 8956 2647 -666 3007 N ATOM 593 CA LEU A 249 98.615 20.487 32.334 1.00 73.77 C ANISOU 593 CA LEU A 249 5369 13369 9292 2708 -859 3183 C ATOM 594 C LEU A 249 99.701 19.436 32.147 1.00 79.69 C ANISOU 594 C LEU A 249 5973 14071 10236 3040 -871 3318 C ATOM 595 O LEU A 249 100.594 19.298 32.987 1.00 82.51 O ANISOU 595 O LEU A 249 6135 14595 10619 3093 -1023 3424 O ATOM 596 CB LEU A 249 97.351 19.841 32.907 1.00 72.29 C ANISOU 596 CB LEU A 249 5444 13031 8994 2663 -924 3268 C ATOM 597 CG LEU A 249 96.325 20.772 33.552 1.00 69.12 C ANISOU 597 CG LEU A 249 5154 12720 8391 2333 -966 3171 C ATOM 598 CD1 LEU A 249 95.180 19.965 34.115 1.00 68.43 C ANISOU 598 CD1 LEU A 249 5298 12479 8223 2323 -1026 3278 C ATOM 599 CD2 LEU A 249 96.966 21.639 34.631 1.00 70.45 C ANISOU 599 CD2 LEU A 249 5138 13178 8454 2147 -1100 3157 C ATOM 600 N GLY A 250 99.623 18.704 31.040 1.00 78.05 N ANISOU 600 N GLY A 250 5860 13630 10164 3269 -713 3306 N ATOM 601 CA GLY A 250 100.549 17.622 30.773 1.00 82.10 C ANISOU 601 CA GLY A 250 6267 14048 10880 3609 -698 3419 C ATOM 602 C GLY A 250 100.284 16.912 29.459 1.00 83.33 C ANISOU 602 C GLY A 250 6577 13921 11164 3835 -489 3362 C ATOM 603 O GLY A 250 99.629 17.463 28.568 1.00 79.29 O ANISOU 603 O GLY A 250 6193 13340 10595 3727 -336 3211 O ATOM 604 N PHE A 251 100.791 15.685 29.345 1.00 88.72 N ANISOU 604 N PHE A 251 7258 14433 12020 4155 -487 3479 N ATOM 605 CA PHE A 251 100.740 14.928 28.095 1.00 88.67 C ANISOU 605 CA PHE A 251 7379 14149 12161 4410 -277 3413 C ATOM 606 C PHE A 251 100.838 13.423 28.321 1.00 91.49 C ANISOU 606 C PHE A 251 7849 14244 12668 4716 -330 3572 C ATOM 607 O PHE A 251 100.947 12.958 29.453 1.00 91.35 O ANISOU 607 O PHE A 251 7810 14265 12636 4735 -537 3751 O ATOM 608 CB PHE A 251 101.869 15.375 27.164 1.00 87.49 C ANISOU 608 CB PHE A 251 6983 14115 12144 4514 -103 3293 C ATOM 609 CG PHE A 251 103.217 15.374 27.818 1.00 95.53 C ANISOU 609 CG PHE A 251 7662 15352 13285 4609 -221 3383 C ATOM 610 CD1 PHE A 251 103.936 14.191 27.958 1.00101.66 C ANISOU 610 CD1 PHE A 251 8363 16003 14259 4939 -260 3509 C ATOM 611 CD2 PHE A 251 103.761 16.548 28.313 1.00 91.19 C ANISOU 611 CD2 PHE A 251 6867 15121 12661 4371 -304 3339 C ATOM 612 CE1 PHE A 251 105.179 14.180 28.571 1.00100.23 C ANISOU 612 CE1 PHE A 251 7852 16029 14200 5040 -388 3594 C ATOM 613 CE2 PHE A 251 105.004 16.543 28.929 1.00103.31 C ANISOU 613 CE2 PHE A 251 8078 16860 14316 4458 -430 3416 C ATOM 614 CZ PHE A 251 105.714 15.356 29.056 1.00 99.79 C ANISOU 614 CZ PHE A 251 7544 16305 14068 4798 -476 3546 C ATOM 615 N SER A 252 100.824 12.671 27.227 1.00 92.54 N ANISOU 615 N SER A 252 8113 14103 12945 4960 -139 3500 N ATOM 616 CA SER A 252 100.885 11.218 27.296 1.00 96.61 C ANISOU 616 CA SER A 252 8768 14312 13626 5263 -161 3625 C ATOM 617 C SER A 252 101.133 10.604 25.918 1.00 99.75 C ANISOU 617 C SER A 252 9253 14453 14195 5530 95 3484 C ATOM 618 O SER A 252 100.832 11.218 24.890 1.00 97.89 O ANISOU 618 O SER A 252 9078 14219 13897 5449 289 3294 O ATOM 619 CB SER A 252 99.593 10.669 27.902 1.00 91.98 C ANISOU 619 CB SER A 252 8504 13512 12933 5161 -279 3727 C ATOM 620 OG SER A 252 99.434 9.291 27.619 1.00 97.20 O ANISOU 620 OG SER A 252 9381 13790 13760 5437 -238 3794 O ATOM 621 N LEU A 258 98.576 8.742 21.571 1.00 98.76 N ANISOU 621 N LEU A 258 10252 13113 14158 5918 855 2870 N ATOM 622 CA LEU A 258 99.220 10.022 21.878 1.00 97.80 C ANISOU 622 CA LEU A 258 9797 13426 13935 5733 817 2883 C ATOM 623 C LEU A 258 98.217 11.155 22.247 1.00102.46 C ANISOU 623 C LEU A 258 10439 14208 14285 5372 710 2869 C ATOM 624 O LEU A 258 97.288 11.454 21.488 1.00100.28 O ANISOU 624 O LEU A 258 10391 13819 13894 5277 810 2723 O ATOM 625 CB LEU A 258 100.088 10.439 20.695 1.00 91.99 C ANISOU 625 CB LEU A 258 8919 12788 13247 5846 1076 2702 C ATOM 626 CG LEU A 258 101.145 11.481 21.044 1.00 92.97 C ANISOU 626 CG LEU A 258 8644 13319 13360 5733 1045 2736 C ATOM 627 CD1 LEU A 258 102.251 11.497 20.009 1.00 95.38 C ANISOU 627 CD1 LEU A 258 8778 13668 13793 5927 1299 2599 C ATOM 628 CD2 LEU A 258 100.487 12.845 21.160 1.00 94.27 C ANISOU 628 CD2 LEU A 258 8799 13724 13293 5379 994 2688 C ATOM 629 N CYS A 259 98.432 11.798 23.401 1.00 98.46 N ANISOU 629 N CYS A 259 9717 13991 13701 5177 508 3007 N ATOM 630 CA CYS A 259 97.432 12.702 23.997 1.00 90.83 C ANISOU 630 CA CYS A 259 8811 13175 12524 4840 373 3015 C ATOM 631 C CYS A 259 97.983 13.992 24.622 1.00 79.37 C ANISOU 631 C CYS A 259 7063 12128 10965 4597 281 3028 C ATOM 632 O CYS A 259 99.160 14.079 24.966 1.00 86.80 O ANISOU 632 O CYS A 259 7728 13253 11998 4675 249 3089 O ATOM 633 CB CYS A 259 96.647 11.958 25.079 1.00 80.70 C ANISOU 633 CB CYS A 259 7700 11742 11222 4794 170 3188 C ATOM 634 SG CYS A 259 95.776 10.490 24.520 1.00 98.74 S ANISOU 634 SG CYS A 259 10380 13512 13623 5007 242 3180 S ATOM 635 N LEU A 260 97.104 14.978 24.792 1.00 75.37 N ANISOU 635 N LEU A 260 6619 11745 10273 4299 230 2963 N ATOM 636 CA LEU A 260 97.431 16.226 25.482 1.00 73.94 C ANISOU 636 CA LEU A 260 6211 11909 9975 4026 128 2959 C ATOM 637 C LEU A 260 96.332 16.615 26.472 1.00 76.71 C ANISOU 637 C LEU A 260 6679 12312 10156 3749 -48 3003 C ATOM 638 O LEU A 260 95.144 16.360 26.229 1.00 68.84 O ANISOU 638 O LEU A 260 5936 11121 9099 3702 -38 2967 O ATOM 639 CB LEU A 260 97.652 17.354 24.483 1.00 72.13 C ANISOU 639 CB LEU A 260 5899 11814 9694 3918 297 2782 C ATOM 640 CG LEU A 260 99.043 17.427 23.867 1.00 75.22 C ANISOU 640 CG LEU A 260 6047 12307 10227 4086 440 2746 C ATOM 641 CD1 LEU A 260 99.048 18.375 22.691 1.00 73.45 C ANISOU 641 CD1 LEU A 260 5825 12139 9943 3999 643 2573 C ATOM 642 CD2 LEU A 260 100.048 17.871 24.911 1.00 77.20 C ANISOU 642 CD2 LEU A 260 5989 12833 10509 3995 285 2839 C ATOM 643 N VAL A 261 96.730 17.239 27.583 1.00 76.22 N ANISOU 643 N VAL A 261 6432 12511 10016 3566 -205 3069 N ATOM 644 CA VAL A 261 95.804 17.488 28.696 1.00 75.67 C ANISOU 644 CA VAL A 261 6461 12501 9789 3323 -372 3124 C ATOM 645 C VAL A 261 95.762 18.947 29.146 1.00 67.12 C ANISOU 645 C VAL A 261 5252 11695 8557 3000 -420 3020 C ATOM 646 O VAL A 261 96.796 19.542 29.433 1.00 68.66 O ANISOU 646 O VAL A 261 5210 12109 8769 2960 -449 3013 O ATOM 647 CB VAL A 261 96.163 16.616 29.915 1.00 72.60 C ANISOU 647 CB VAL A 261 6034 12124 9426 3416 -550 3335 C ATOM 648 CG1 VAL A 261 95.341 17.036 31.117 1.00 73.98 C ANISOU 648 CG1 VAL A 261 6278 12417 9414 3141 -706 3381 C ATOM 649 CG2 VAL A 261 95.944 15.146 29.597 1.00 74.69 C ANISOU 649 CG2 VAL A 261 6489 12060 9829 3701 -521 3445 C ATOM 650 N TYR A 262 94.561 19.513 29.223 1.00 63.68 N ANISOU 650 N TYR A 262 4977 11233 7985 2772 -430 2932 N ATOM 651 CA TYR A 262 94.413 20.932 29.532 1.00 61.38 C ANISOU 651 CA TYR A 262 4605 11155 7563 2468 -453 2804 C ATOM 652 C TYR A 262 93.495 21.210 30.712 1.00 59.93 C ANISOU 652 C TYR A 262 4509 11037 7226 2228 -587 2824 C ATOM 653 O TYR A 262 92.684 20.375 31.103 1.00 59.88 O ANISOU 653 O TYR A 262 4667 10886 7200 2264 -643 2917 O ATOM 654 CB TYR A 262 93.858 21.697 28.332 1.00 58.43 C ANISOU 654 CB TYR A 262 4319 10712 7168 2391 -306 2626 C ATOM 655 CG TYR A 262 94.504 21.426 27.001 1.00 59.49 C ANISOU 655 CG TYR A 262 4423 10754 7428 2622 -134 2584 C ATOM 656 CD1 TYR A 262 94.130 20.327 26.245 1.00 60.05 C ANISOU 656 CD1 TYR A 262 4663 10572 7582 2867 -51 2613 C ATOM 657 CD2 TYR A 262 95.454 22.292 26.482 1.00 60.07 C ANISOU 657 CD2 TYR A 262 4312 10979 7533 2587 -43 2504 C ATOM 658 CE1 TYR A 262 94.699 20.081 25.020 1.00 61.22 C ANISOU 658 CE1 TYR A 262 4801 10631 7830 3083 129 2556 C ATOM 659 CE2 TYR A 262 96.029 22.054 25.258 1.00 61.25 C ANISOU 659 CE2 TYR A 262 4435 11050 7786 2793 138 2461 C ATOM 660 CZ TYR A 262 95.642 20.945 24.536 1.00 61.81 C ANISOU 660 CZ TYR A 262 4681 10879 7925 3044 228 2482 C ATOM 661 OH TYR A 262 96.199 20.694 23.322 1.00 63.20 O ANISOU 661 OH TYR A 262 4851 10972 8190 3254 428 2421 O ATOM 662 N VAL A 263 93.624 22.410 31.261 1.00 58.92 N ANISOU 662 N VAL A 263 4278 11117 6992 1978 -628 2729 N ATOM 663 CA VAL A 263 92.644 22.923 32.193 1.00 57.08 C ANISOU 663 CA VAL A 263 4139 10944 6605 1723 -708 2689 C ATOM 664 C VAL A 263 91.295 23.043 31.477 1.00 62.97 C ANISOU 664 C VAL A 263 5091 11507 7327 1647 -629 2578 C ATOM 665 O VAL A 263 91.185 23.654 30.407 1.00 52.02 O ANISOU 665 O VAL A 263 3726 10067 5974 1632 -520 2442 O ATOM 666 CB VAL A 263 93.046 24.295 32.765 1.00 56.63 C ANISOU 666 CB VAL A 263 3952 11114 6453 1477 -741 2570 C ATOM 667 CG1 VAL A 263 91.930 24.848 33.664 1.00 54.70 C ANISOU 667 CG1 VAL A 263 3823 10911 6052 1221 -794 2503 C ATOM 668 CG2 VAL A 263 94.373 24.220 33.499 1.00 60.11 C ANISOU 668 CG2 VAL A 263 4173 11749 6916 1541 -842 2670 C ATOM 669 N TYR A 264 90.278 22.447 32.084 1.00 53.31 N ANISOU 669 N TYR A 264 4013 10194 6047 1600 -693 2645 N ATOM 670 CA TYR A 264 88.935 22.446 31.555 1.00 50.64 C ANISOU 670 CA TYR A 264 3860 9686 5693 1526 -649 2557 C ATOM 671 C TYR A 264 88.206 23.754 31.864 1.00 54.97 C ANISOU 671 C TYR A 264 4418 10341 6129 1231 -644 2382 C ATOM 672 O TYR A 264 88.190 24.211 33.018 1.00 48.48 O ANISOU 672 O TYR A 264 3541 9681 5198 1059 -712 2388 O ATOM 673 CB TYR A 264 88.165 21.256 32.121 1.00 51.55 C ANISOU 673 CB TYR A 264 4123 9658 5804 1589 -722 2712 C ATOM 674 CG TYR A 264 86.706 21.235 31.767 1.00 50.36 C ANISOU 674 CG TYR A 264 4152 9351 5633 1484 -704 2633 C ATOM 675 CD1 TYR A 264 86.295 21.101 30.450 1.00 47.75 C ANISOU 675 CD1 TYR A 264 3926 8831 5387 1593 -625 2542 C ATOM 676 CD2 TYR A 264 85.733 21.348 32.750 1.00 54.38 C ANISOU 676 CD2 TYR A 264 4721 9911 6031 1277 -769 2649 C ATOM 677 CE1 TYR A 264 84.959 21.080 30.130 1.00 58.43 C ANISOU 677 CE1 TYR A 264 5433 10046 6723 1497 -633 2470 C ATOM 678 CE2 TYR A 264 84.392 21.328 32.439 1.00 46.50 C ANISOU 678 CE2 TYR A 264 3865 8782 5022 1174 -760 2580 C ATOM 679 CZ TYR A 264 84.009 21.189 31.132 1.00 59.43 C ANISOU 679 CZ TYR A 264 5599 10228 6753 1284 -703 2492 C ATOM 680 OH TYR A 264 82.666 21.175 30.808 1.00 62.11 O ANISOU 680 OH TYR A 264 6071 10442 7085 1181 -717 2422 O ATOM 681 N MET A 265 87.607 24.341 30.824 1.00 45.64 N ANISOU 681 N MET A 265 3313 9058 4971 1187 -563 2226 N ATOM 682 CA MET A 265 86.842 25.576 30.950 1.00 43.23 C ANISOU 682 CA MET A 265 3040 8800 4587 934 -549 2048 C ATOM 683 C MET A 265 85.338 25.336 30.827 1.00 56.95 C ANISOU 683 C MET A 265 4936 10392 6310 857 -563 1996 C ATOM 684 O MET A 265 84.815 25.298 29.717 1.00 42.22 O ANISOU 684 O MET A 265 3161 8378 4502 923 -520 1920 O ATOM 685 CB MET A 265 87.264 26.581 29.886 1.00 45.18 C ANISOU 685 CB MET A 265 3251 9047 4868 920 -460 1907 C ATOM 686 CG MET A 265 88.733 26.651 29.637 1.00 45.74 C ANISOU 686 CG MET A 265 3166 9224 4991 1040 -426 1963 C ATOM 687 SD MET A 265 89.672 26.720 31.167 1.00 57.93 S ANISOU 687 SD MET A 265 4549 10991 6471 965 -530 2061 S ATOM 688 CE MET A 265 89.662 28.458 31.518 1.00 46.56 C ANISOU 688 CE MET A 265 3076 9666 4949 685 -523 1871 C ATOM 689 N PRO A 266 84.631 25.231 31.970 1.00 49.59 N ANISOU 689 N PRO A 266 4030 9518 5293 708 -626 2033 N ATOM 690 CA PRO A 266 83.217 24.827 32.031 1.00 40.34 C ANISOU 690 CA PRO A 266 2987 8228 4111 633 -654 2020 C ATOM 691 C PRO A 266 82.260 25.703 31.240 1.00 49.10 C ANISOU 691 C PRO A 266 4165 9249 5240 516 -613 1813 C ATOM 692 O PRO A 266 81.139 25.264 30.988 1.00 47.90 O ANISOU 692 O PRO A 266 4114 8976 5110 494 -642 1800 O ATOM 693 CB PRO A 266 82.872 24.932 33.522 1.00 41.14 C ANISOU 693 CB PRO A 266 3055 8489 4088 453 -704 2075 C ATOM 694 CG PRO A 266 84.129 25.202 34.231 1.00 42.96 C ANISOU 694 CG PRO A 266 3153 8902 4267 468 -723 2136 C ATOM 695 CD PRO A 266 85.107 25.753 33.261 1.00 55.21 C ANISOU 695 CD PRO A 266 4638 10441 5897 566 -667 2054 C ATOM 696 N ASN A 267 82.637 26.921 30.881 1.00 36.68 N ANISOU 696 N ASN A 267 2547 7728 3661 436 -558 1660 N ATOM 697 CA ASN A 267 81.664 27.771 30.188 1.00 40.70 C ANISOU 697 CA ASN A 267 3136 8134 4194 329 -531 1470 C ATOM 698 C ASN A 267 81.861 27.827 28.673 1.00 33.78 C ANISOU 698 C ASN A 267 2300 7139 3395 474 -492 1418 C ATOM 699 O ASN A 267 81.145 28.547 27.979 1.00 51.35 O ANISOU 699 O ASN A 267 4590 9280 5642 407 -480 1271 O ATOM 700 CB ASN A 267 81.668 29.186 30.786 1.00 41.17 C ANISOU 700 CB ASN A 267 3166 8284 4193 132 -500 1324 C ATOM 701 CG ASN A 267 80.913 29.252 32.110 1.00 41.36 C ANISOU 701 CG ASN A 267 3193 8395 4127 -35 -527 1318 C ATOM 702 OD1 ASN A 267 79.753 28.850 32.190 1.00 41.59 O ANISOU 702 OD1 ASN A 267 3284 8353 4165 -88 -549 1301 O ATOM 703 ND2 ASN A 267 81.572 29.739 33.154 1.00 44.87 N ANISOU 703 ND2 ASN A 267 3561 9008 4478 -121 -527 1334 N ATOM 704 N GLY A 268 82.790 27.030 28.159 1.00 35.18 N ANISOU 704 N GLY A 268 2445 7309 3613 687 -471 1544 N ATOM 705 CA GLY A 268 82.919 26.813 26.735 1.00 34.97 C ANISOU 705 CA GLY A 268 2471 7174 3641 866 -426 1522 C ATOM 706 C GLY A 268 83.414 28.035 25.997 1.00 34.19 C ANISOU 706 C GLY A 268 2323 7133 3533 820 -352 1410 C ATOM 707 O GLY A 268 84.112 28.850 26.589 1.00 47.29 O ANISOU 707 O GLY A 268 3885 8918 5163 705 -330 1391 O ATOM 708 N SER A 269 83.064 28.175 24.717 1.00 33.45 N ANISOU 708 N SER A 269 2305 6949 3455 914 -321 1343 N ATOM 709 CA SER A 269 83.663 29.214 23.896 1.00 33.18 C ANISOU 709 CA SER A 269 2219 6980 3409 909 -237 1280 C ATOM 710 C SER A 269 82.897 30.522 23.980 1.00 36.30 C ANISOU 710 C SER A 269 2648 7361 3783 686 -265 1130 C ATOM 711 O SER A 269 81.694 30.542 24.248 1.00 30.34 O ANISOU 711 O SER A 269 1984 6511 3033 584 -340 1049 O ATOM 712 CB SER A 269 83.779 28.763 22.427 1.00 33.65 C ANISOU 712 CB SER A 269 2342 6974 3470 1154 -171 1297 C ATOM 713 OG SER A 269 82.539 28.799 21.748 1.00 32.41 O ANISOU 713 OG SER A 269 2337 6692 3285 1154 -245 1204 O ATOM 714 N LEU A 270 83.622 31.618 23.762 1.00 31.59 N ANISOU 714 N LEU A 270 1976 6850 3178 616 -201 1096 N ATOM 715 CA LEU A 270 83.003 32.929 23.639 1.00 31.78 C ANISOU 715 CA LEU A 270 2039 6836 3200 444 -214 964 C ATOM 716 C LEU A 270 81.952 32.906 22.532 1.00 29.33 C ANISOU 716 C LEU A 270 1837 6419 2888 511 -247 902 C ATOM 717 O LEU A 270 80.928 33.582 22.632 1.00 30.91 O ANISOU 717 O LEU A 270 2107 6530 3107 381 -307 787 O ATOM 718 CB LEU A 270 84.062 34.011 23.361 1.00 31.00 C ANISOU 718 CB LEU A 270 1841 6833 3105 392 -136 962 C ATOM 719 CG LEU A 270 83.480 35.383 23.011 1.00 29.99 C ANISOU 719 CG LEU A 270 1753 6650 2992 250 -139 844 C ATOM 720 CD1 LEU A 270 82.542 35.878 24.104 1.00 28.95 C ANISOU 720 CD1 LEU A 270 1692 6432 2877 77 -217 727 C ATOM 721 CD2 LEU A 270 84.540 36.406 22.704 1.00 30.96 C ANISOU 721 CD2 LEU A 270 1775 6853 3137 192 -57 852 C ATOM 722 N LEU A 271 82.194 32.125 21.485 1.00 30.04 N ANISOU 722 N LEU A 271 1952 6509 2953 736 -216 974 N ATOM 723 CA LEU A 271 81.231 32.001 20.383 1.00 34.67 C ANISOU 723 CA LEU A 271 2720 6950 3502 820 -268 905 C ATOM 724 C LEU A 271 79.912 31.390 20.876 1.00 33.39 C ANISOU 724 C LEU A 271 2658 6664 3365 756 -412 841 C ATOM 725 O LEU A 271 78.834 31.920 20.603 1.00 27.79 O ANISOU 725 O LEU A 271 2048 5848 2664 659 -494 723 O ATOM 726 CB LEU A 271 81.824 31.171 19.230 1.00 31.06 C ANISOU 726 CB LEU A 271 2426 6374 3000 1046 -152 941 C ATOM 727 CG LEU A 271 80.933 30.797 18.028 1.00 30.76 C ANISOU 727 CG LEU A 271 2701 6087 2900 1123 -182 835 C ATOM 728 CD1 LEU A 271 80.449 32.014 17.291 1.00 34.75 C ANISOU 728 CD1 LEU A 271 3300 6548 3355 1027 -199 750 C ATOM 729 CD2 LEU A 271 81.617 29.865 17.063 1.00 32.41 C ANISOU 729 CD2 LEU A 271 3060 6198 3056 1348 -53 862 C ATOM 730 N ASP A 272 80.020 30.282 21.604 1.00 36.52 N ANISOU 730 N ASP A 272 3029 7060 3785 806 -433 924 N ATOM 731 CA ASP A 272 78.875 29.645 22.229 1.00 35.99 C ANISOU 731 CA ASP A 272 3036 6885 3753 719 -540 884 C ATOM 732 C ASP A 272 78.083 30.615 23.114 1.00 41.71 C ANISOU 732 C ASP A 272 3729 7595 4523 465 -565 763 C ATOM 733 O ASP A 272 76.840 30.671 23.026 1.00 36.63 O ANISOU 733 O ASP A 272 3161 6841 3914 385 -651 658 O ATOM 734 CB ASP A 272 79.308 28.449 23.092 1.00 50.12 C ANISOU 734 CB ASP A 272 4786 8696 5563 786 -535 1025 C ATOM 735 CG ASP A 272 79.930 27.314 22.290 1.00 49.29 C ANISOU 735 CG ASP A 272 4789 8481 5457 1043 -478 1113 C ATOM 736 OD1 ASP A 272 79.677 27.225 21.073 1.00 40.92 O ANISOU 736 OD1 ASP A 272 3925 7243 4379 1129 -445 1013 O ATOM 737 OD2 ASP A 272 80.664 26.497 22.909 1.00 56.76 O1+ ANISOU 737 OD2 ASP A 272 5655 9486 6426 1151 -457 1266 O1+ ATOM 738 N ARG A 273 78.790 31.348 23.987 1.00 29.63 N ANISOU 738 N ARG A 273 2098 6168 2991 352 -491 773 N ATOM 739 CA ARG A 273 78.114 32.264 24.909 1.00 26.76 C ANISOU 739 CA ARG A 273 1734 5779 2655 150 -495 660 C ATOM 740 C ARG A 273 77.490 33.467 24.176 1.00 39.84 C ANISOU 740 C ARG A 273 3438 7347 4351 93 -509 526 C ATOM 741 O ARG A 273 76.387 33.916 24.545 1.00 25.17 O ANISOU 741 O ARG A 273 1623 5389 2551 -13 -547 412 O ATOM 742 CB ARG A 273 79.052 32.775 26.003 1.00 27.31 C ANISOU 742 CB ARG A 273 1718 5974 2685 64 -433 696 C ATOM 743 CG ARG A 273 79.420 31.753 27.072 1.00 30.23 C ANISOU 743 CG ARG A 273 2039 6437 3011 77 -444 819 C ATOM 744 CD ARG A 273 78.233 30.889 27.505 1.00 30.38 C ANISOU 744 CD ARG A 273 2109 6390 3045 44 -507 821 C ATOM 745 NE ARG A 273 78.347 29.549 26.927 1.00 33.50 N ANISOU 745 NE ARG A 273 2522 6753 3454 211 -548 946 N ATOM 746 CZ ARG A 273 77.327 28.895 26.408 1.00 35.12 C ANISOU 746 CZ ARG A 273 2805 6842 3698 242 -622 922 C ATOM 747 NH1 ARG A 273 76.134 29.461 26.432 1.00 42.59 N1+ ANISOU 747 NH1 ARG A 273 3791 7709 4683 107 -655 775 N1+ ATOM 748 NH2 ARG A 273 77.489 27.692 25.873 1.00 32.54 N ANISOU 748 NH2 ARG A 273 2522 6467 3376 418 -664 1042 N ATOM 749 N LEU A 274 78.166 33.984 23.147 1.00 26.04 N ANISOU 749 N LEU A 274 1674 5644 2577 174 -475 550 N ATOM 750 CA LEU A 274 77.602 35.115 22.406 1.00 25.48 C ANISOU 750 CA LEU A 274 1643 5504 2534 132 -503 452 C ATOM 751 C LEU A 274 76.318 34.712 21.713 1.00 25.07 C ANISOU 751 C LEU A 274 1709 5311 2506 177 -621 379 C ATOM 752 O LEU A 274 75.382 35.498 21.605 1.00 25.68 O ANISOU 752 O LEU A 274 1826 5282 2649 102 -677 269 O ATOM 753 CB LEU A 274 78.590 35.668 21.378 1.00 26.10 C ANISOU 753 CB LEU A 274 1669 5692 2554 220 -444 522 C ATOM 754 CG LEU A 274 79.665 36.534 22.029 1.00 50.51 C ANISOU 754 CG LEU A 274 4643 8891 5657 114 -344 545 C ATOM 755 CD1 LEU A 274 80.792 36.851 21.045 1.00 27.55 C ANISOU 755 CD1 LEU A 274 1645 6120 2703 208 -251 644 C ATOM 756 CD2 LEU A 274 79.008 37.809 22.679 1.00 25.95 C ANISOU 756 CD2 LEU A 274 1550 5690 2621 -61 -365 413 C ATOM 757 N SER A 275 76.285 33.480 21.241 1.00 25.52 N ANISOU 757 N SER A 275 1827 5357 2514 310 -668 438 N ATOM 758 CA SER A 275 75.127 32.991 20.543 1.00 31.17 C ANISOU 758 CA SER A 275 2674 5936 3233 354 -799 361 C ATOM 759 C SER A 275 74.113 32.359 21.489 1.00 32.83 C ANISOU 759 C SER A 275 2872 6067 3535 242 -852 307 C ATOM 760 O SER A 275 73.100 31.854 21.051 1.00 33.81 O ANISOU 760 O SER A 275 3077 6085 3682 251 -969 237 O ATOM 761 CB SER A 275 75.553 31.980 19.491 1.00 34.93 C ANISOU 761 CB SER A 275 3320 6332 3621 546 -786 416 C ATOM 762 OG SER A 275 75.997 30.788 20.111 1.00 31.91 O ANISOU 762 OG SER A 275 2905 5975 3245 601 -747 509 O ATOM 763 N CYS A 276 74.399 32.393 22.785 1.00 29.48 N ANISOU 763 N CYS A 276 2349 5709 3144 135 -770 341 N ATOM 764 CA CYS A 276 73.518 31.822 23.806 1.00 33.19 C ANISOU 764 CA CYS A 276 2796 6145 3671 26 -796 313 C ATOM 765 C CYS A 276 73.122 30.393 23.461 1.00 35.11 C ANISOU 765 C CYS A 276 3084 6360 3896 103 -892 368 C ATOM 766 O CYS A 276 71.980 29.996 23.658 1.00 40.40 O ANISOU 766 O CYS A 276 3762 6957 4631 20 -968 298 O ATOM 767 CB CYS A 276 72.275 32.692 23.992 1.00 24.52 C ANISOU 767 CB CYS A 276 1710 4927 2678 -89 -826 160 C ATOM 768 SG CYS A 276 72.664 34.356 24.443 1.00 27.92 S ANISOU 768 SG CYS A 276 2103 5374 3133 -162 -731 102 S ATOM 769 N LEU A 277 74.072 29.627 22.944 1.00 26.50 N ANISOU 769 N LEU A 277 2019 5325 2724 270 -885 496 N ATOM 770 CA LEU A 277 73.836 28.231 22.620 1.00 27.48 C ANISOU 770 CA LEU A 277 2288 5292 2860 361 -913 538 C ATOM 771 C LEU A 277 73.344 27.458 23.840 1.00 44.21 C ANISOU 771 C LEU A 277 4341 7435 5022 244 -926 606 C ATOM 772 O LEU A 277 73.816 27.676 24.965 1.00 49.05 O ANISOU 772 O LEU A 277 4793 8248 5597 175 -888 706 O ATOM 773 CB LEU A 277 75.120 27.599 22.067 1.00 39.56 C ANISOU 773 CB LEU A 277 3898 6800 4333 568 -822 657 C ATOM 774 CG LEU A 277 74.992 26.180 21.512 1.00 38.90 C ANISOU 774 CG LEU A 277 4021 6484 4274 693 -823 672 C ATOM 775 CD1 LEU A 277 74.088 26.197 20.257 1.00 40.58 C ANISOU 775 CD1 LEU A 277 4436 6493 4488 702 -901 497 C ATOM 776 CD2 LEU A 277 76.370 25.581 21.215 1.00 30.91 C ANISOU 776 CD2 LEU A 277 3036 5482 3224 909 -708 803 C ATOM 777 N ASP A 278 72.394 26.553 23.617 1.00 46.93 N ANISOU 777 N ASP A 278 4815 7580 5437 211 -980 554 N ATOM 778 CA ASP A 278 71.835 25.732 24.689 1.00 50.54 C ANISOU 778 CA ASP A 278 5238 8024 5940 88 -978 625 C ATOM 779 C ASP A 278 71.085 26.536 25.751 1.00 48.38 C ANISOU 779 C ASP A 278 4777 7924 5682 -126 -985 569 C ATOM 780 O ASP A 278 70.732 26.018 26.809 1.00 52.92 O ANISOU 780 O ASP A 278 5300 8547 6261 -247 -956 646 O ATOM 781 CB ASP A 278 72.938 24.912 25.330 1.00 40.76 C ANISOU 781 CB ASP A 278 3997 6842 4648 194 -907 843 C ATOM 782 CG ASP A 278 73.387 23.785 24.435 1.00 47.18 C ANISOU 782 CG ASP A 278 5016 7422 5488 389 -888 888 C ATOM 783 OD1 ASP A 278 72.690 23.557 23.431 1.00 49.98 O ANISOU 783 OD1 ASP A 278 5524 7572 5892 400 -937 740 O ATOM 784 OD2 ASP A 278 74.406 23.123 24.729 1.00 54.18 O1+ ANISOU 784 OD2 ASP A 278 5909 8328 6349 533 -829 1061 O1+ ATOM 785 N GLY A 279 70.829 27.801 25.453 1.00 42.82 N ANISOU 785 N GLY A 279 3983 7302 4983 -169 -1013 432 N ATOM 786 CA GLY A 279 69.894 28.575 26.232 1.00 41.94 C ANISOU 786 CA GLY A 279 3793 7200 4941 -339 -973 305 C ATOM 787 C GLY A 279 70.516 29.335 27.379 1.00 33.71 C ANISOU 787 C GLY A 279 2702 6270 3836 -391 -839 337 C ATOM 788 O GLY A 279 69.795 29.895 28.209 1.00 37.12 O ANISOU 788 O GLY A 279 3100 6703 4302 -511 -780 248 O ATOM 789 N THR A 280 71.841 29.377 27.431 1.00 33.88 N ANISOU 789 N THR A 280 2722 6388 3763 -296 -792 456 N ATOM 790 CA THR A 280 72.516 30.149 28.474 1.00 29.64 C ANISOU 790 CA THR A 280 2143 5966 3152 -353 -688 473 C ATOM 791 C THR A 280 72.187 31.631 28.334 1.00 32.92 C ANISOU 791 C THR A 280 2587 6295 3626 -395 -644 302 C ATOM 792 O THR A 280 71.903 32.112 27.252 1.00 28.01 O ANISOU 792 O THR A 280 2013 5547 3083 -337 -686 217 O ATOM 793 CB THR A 280 74.026 29.979 28.419 1.00 27.22 C ANISOU 793 CB THR A 280 1817 5764 2761 -242 -656 614 C ATOM 794 OG1 THR A 280 74.512 30.578 27.212 1.00 26.54 O ANISOU 794 OG1 THR A 280 1772 5601 2710 -138 -656 559 O ATOM 795 CG2 THR A 280 74.387 28.516 28.433 1.00 28.38 C ANISOU 795 CG2 THR A 280 1947 5961 2874 -146 -711 807 C ATOM 796 N PRO A 281 72.240 32.361 29.447 1.00 36.72 N ANISOU 796 N PRO A 281 3040 6855 4058 -488 -570 265 N ATOM 797 CA PRO A 281 71.921 33.797 29.468 1.00 33.44 C ANISOU 797 CA PRO A 281 2643 6359 3703 -523 -534 118 C ATOM 798 C PRO A 281 72.910 34.661 28.682 1.00 29.84 C ANISOU 798 C PRO A 281 2207 5881 3251 -453 -522 116 C ATOM 799 O PRO A 281 74.109 34.401 28.684 1.00 34.58 O ANISOU 799 O PRO A 281 2783 6589 3765 -411 -501 223 O ATOM 800 CB PRO A 281 71.965 34.138 30.963 1.00 26.15 C ANISOU 800 CB PRO A 281 1679 5579 2678 -633 -465 107 C ATOM 801 CG PRO A 281 72.727 33.042 31.591 1.00 27.05 C ANISOU 801 CG PRO A 281 1754 5870 2655 -639 -467 278 C ATOM 802 CD PRO A 281 72.526 31.822 30.786 1.00 27.06 C ANISOU 802 CD PRO A 281 1761 5814 2707 -569 -533 369 C ATOM 803 N PRO A 282 72.404 35.683 27.989 1.00 39.02 N ANISOU 803 N PRO A 282 3398 6911 4518 -443 -541 7 N ATOM 804 CA PRO A 282 73.322 36.565 27.263 1.00 24.13 C ANISOU 804 CA PRO A 282 1514 5028 2627 -400 -526 14 C ATOM 805 C PRO A 282 74.348 37.190 28.193 1.00 32.48 C ANISOU 805 C PRO A 282 2528 6212 3600 -460 -455 33 C ATOM 806 O PRO A 282 73.958 37.560 29.292 1.00 36.86 O ANISOU 806 O PRO A 282 3067 6799 4137 -544 -425 -29 O ATOM 807 CB PRO A 282 72.410 37.638 26.667 1.00 23.79 C ANISOU 807 CB PRO A 282 1491 4837 2710 -406 -565 -104 C ATOM 808 CG PRO A 282 70.993 37.207 26.950 1.00 27.98 C ANISOU 808 CG PRO A 282 2030 5274 3327 -432 -607 -169 C ATOM 809 CD PRO A 282 71.003 35.840 27.565 1.00 27.43 C ANISOU 809 CD PRO A 282 1950 5291 3182 -449 -599 -96 C ATOM 810 N LEU A 283 75.614 37.291 27.779 1.00 37.27 N ANISOU 810 N LEU A 283 3106 6904 4151 -420 -433 112 N ATOM 811 CA LEU A 283 76.632 37.986 28.567 1.00 25.57 C ANISOU 811 CA LEU A 283 1573 5537 2605 -484 -386 117 C ATOM 812 C LEU A 283 76.355 39.470 28.625 1.00 31.68 C ANISOU 812 C LEU A 283 2345 6238 3455 -555 -371 -10 C ATOM 813 O LEU A 283 76.037 40.080 27.608 1.00 25.13 O ANISOU 813 O LEU A 283 1529 5304 2714 -527 -390 -48 O ATOM 814 CB LEU A 283 78.009 37.790 27.966 1.00 32.44 C ANISOU 814 CB LEU A 283 2393 6506 3428 -422 -368 227 C ATOM 815 CG LEU A 283 78.435 36.391 27.569 1.00 34.06 C ANISOU 815 CG LEU A 283 2584 6773 3584 -313 -380 366 C ATOM 816 CD1 LEU A 283 79.537 36.498 26.556 1.00 26.71 C ANISOU 816 CD1 LEU A 283 1604 5901 2646 -229 -351 443 C ATOM 817 CD2 LEU A 283 78.877 35.616 28.806 1.00 27.21 C ANISOU 817 CD2 LEU A 283 1673 6041 2627 -337 -380 451 C ATOM 818 N SER A 284 76.501 40.069 29.798 1.00 26.24 N ANISOU 818 N SER A 284 1627 5619 2723 -648 -343 -70 N ATOM 819 CA SER A 284 76.314 41.516 29.920 1.00 26.53 C ANISOU 819 CA SER A 284 1648 5594 2839 -718 -326 -194 C ATOM 820 C SER A 284 77.405 42.301 29.190 1.00 27.81 C ANISOU 820 C SER A 284 1764 5771 3032 -726 -313 -170 C ATOM 821 O SER A 284 78.425 41.738 28.802 1.00 27.16 O ANISOU 821 O SER A 284 1652 5778 2889 -683 -308 -61 O ATOM 822 CB SER A 284 76.319 41.917 31.381 1.00 27.51 C ANISOU 822 CB SER A 284 1743 5826 2883 -820 -296 -269 C ATOM 823 OG SER A 284 77.621 41.768 31.897 1.00 28.46 O ANISOU 823 OG SER A 284 1811 6110 2891 -852 -290 -200 O ATOM 824 N TRP A 285 77.227 43.609 29.057 1.00 27.30 N ANISOU 824 N TRP A 285 1677 5632 3064 -789 -302 -270 N ATOM 825 CA TRP A 285 78.240 44.423 28.414 1.00 27.97 C ANISOU 825 CA TRP A 285 1702 5737 3188 -825 -280 -250 C ATOM 826 C TRP A 285 79.505 44.524 29.284 1.00 39.17 C ANISOU 826 C TRP A 285 3054 7306 4521 -896 -256 -230 C ATOM 827 O TRP A 285 80.625 44.516 28.783 1.00 41.27 O ANISOU 827 O TRP A 285 3261 7644 4778 -893 -238 -152 O ATOM 828 CB TRP A 285 77.698 45.814 28.116 1.00 35.76 C ANISOU 828 CB TRP A 285 2668 6606 4312 -892 -275 -362 C ATOM 829 CG TRP A 285 78.759 46.724 27.563 1.00 42.79 C ANISOU 829 CG TRP A 285 3483 7524 5253 -965 -237 -345 C ATOM 830 CD1 TRP A 285 79.326 47.796 28.189 1.00 42.79 C ANISOU 830 CD1 TRP A 285 3422 7540 5294 -1091 -203 -426 C ATOM 831 CD2 TRP A 285 79.401 46.623 26.279 1.00 42.95 C ANISOU 831 CD2 TRP A 285 3468 7572 5280 -929 -216 -238 C ATOM 832 NE1 TRP A 285 80.282 48.362 27.382 1.00 45.63 N ANISOU 832 NE1 TRP A 285 3712 7917 5708 -1145 -160 -373 N ATOM 833 CE2 TRP A 285 80.346 47.663 26.201 1.00 41.63 C ANISOU 833 CE2 TRP A 285 3216 7428 5175 -1047 -158 -252 C ATOM 834 CE3 TRP A 285 79.274 45.745 25.195 1.00 41.08 C ANISOU 834 CE3 TRP A 285 3256 7360 4994 -814 -233 -129 C ATOM 835 CZ2 TRP A 285 81.156 47.864 25.077 1.00 40.76 C ANISOU 835 CZ2 TRP A 285 3042 7363 5082 -1060 -97 -150 C ATOM 836 CZ3 TRP A 285 80.085 45.933 24.091 1.00 41.14 C ANISOU 836 CZ3 TRP A 285 3199 7437 4993 -814 -180 -28 C ATOM 837 CH2 TRP A 285 81.016 46.993 24.035 1.00 40.31 C ANISOU 837 CH2 TRP A 285 3008 7354 4955 -940 -102 -33 C ATOM 838 N HIS A 286 79.305 44.636 30.594 1.00 43.36 N ANISOU 838 N HIS A 286 3584 7903 4987 -964 -256 -305 N ATOM 839 CA HIS A 286 80.398 44.717 31.543 1.00 31.25 C ANISOU 839 CA HIS A 286 1979 6537 3356 -1040 -254 -297 C ATOM 840 C HIS A 286 81.255 43.460 31.452 1.00 31.65 C ANISOU 840 C HIS A 286 2004 6714 3308 -961 -273 -142 C ATOM 841 O HIS A 286 82.479 43.520 31.425 1.00 56.21 O ANISOU 841 O HIS A 286 5028 9929 6400 -980 -275 -85 O ATOM 842 CB HIS A 286 79.861 44.919 32.964 1.00 31.99 C ANISOU 842 CB HIS A 286 2080 6714 3361 -1124 -249 -405 C ATOM 843 CG HIS A 286 80.916 44.831 34.019 1.00 58.05 C ANISOU 843 CG HIS A 286 5300 10233 6522 -1204 -262 -390 C ATOM 844 ND1 HIS A 286 80.990 43.781 34.908 1.00 65.99 N ANISOU 844 ND1 HIS A 286 6298 11411 7364 -1194 -281 -315 N ATOM 845 CD2 HIS A 286 81.948 45.653 34.319 1.00 60.36 C ANISOU 845 CD2 HIS A 286 5505 10608 6821 -1302 -265 -435 C ATOM 846 CE1 HIS A 286 82.020 43.963 35.718 1.00 62.20 C ANISOU 846 CE1 HIS A 286 5727 11118 6788 -1276 -303 -312 C ATOM 847 NE2 HIS A 286 82.619 45.091 35.380 1.00 53.97 N ANISOU 847 NE2 HIS A 286 4633 10027 5846 -1345 -295 -391 N ATOM 848 N MET A 287 80.594 42.321 31.377 1.00 44.14 N ANISOU 848 N MET A 287 3647 8282 4842 -874 -287 -73 N ATOM 849 CA MET A 287 81.264 41.035 31.292 1.00 41.84 C ANISOU 849 CA MET A 287 3330 8100 4468 -789 -305 80 C ATOM 850 C MET A 287 81.951 40.922 29.930 1.00 39.35 C ANISOU 850 C MET A 287 2986 7746 4219 -705 -290 163 C ATOM 851 O MET A 287 83.094 40.474 29.857 1.00 38.58 O ANISOU 851 O MET A 287 2806 7769 4084 -667 -289 264 O ATOM 852 CB MET A 287 80.240 39.903 31.531 1.00 36.80 C ANISOU 852 CB MET A 287 2761 7438 3782 -734 -319 122 C ATOM 853 CG MET A 287 80.811 38.532 31.766 1.00 40.54 C ANISOU 853 CG MET A 287 3198 8041 4163 -662 -339 281 C ATOM 854 SD MET A 287 82.256 38.499 32.863 1.00 77.93 S ANISOU 854 SD MET A 287 7807 13020 8782 -715 -361 354 S ATOM 855 CE MET A 287 81.559 39.076 34.414 1.00 55.39 C ANISOU 855 CE MET A 287 4963 10263 5819 -865 -360 235 C ATOM 856 N ARG A 288 81.275 41.367 28.866 1.00 29.17 N ANISOU 856 N ARG A 288 1749 6311 3024 -678 -275 121 N ATOM 857 CA ARG A 288 81.890 41.398 27.535 1.00 29.20 C ANISOU 857 CA ARG A 288 1715 6309 3069 -613 -247 196 C ATOM 858 C ARG A 288 83.157 42.245 27.528 1.00 36.67 C ANISOU 858 C ARG A 288 2551 7336 4047 -687 -210 199 C ATOM 859 O ARG A 288 84.137 41.909 26.870 1.00 35.42 O ANISOU 859 O ARG A 288 2318 7259 3884 -630 -175 300 O ATOM 860 CB ARG A 288 80.918 41.936 26.469 1.00 33.65 C ANISOU 860 CB ARG A 288 2335 6733 3716 -596 -246 144 C ATOM 861 CG ARG A 288 79.869 40.926 25.955 1.00 27.03 C ANISOU 861 CG ARG A 288 1581 5825 2863 -492 -285 171 C ATOM 862 CD ARG A 288 78.759 41.622 25.199 1.00 26.35 C ANISOU 862 CD ARG A 288 1541 5605 2866 -497 -316 90 C ATOM 863 NE ARG A 288 77.494 40.886 25.280 1.00 25.78 N ANISOU 863 NE ARG A 288 1550 5435 2811 -447 -374 54 N ATOM 864 CZ ARG A 288 76.697 40.598 24.247 1.00 26.53 C ANISOU 864 CZ ARG A 288 1690 5455 2935 -369 -433 55 C ATOM 865 NH1 ARG A 288 77.012 40.973 23.012 1.00 25.21 N1+ ANISOU 865 NH1 ARG A 288 1499 5323 2755 -320 -443 104 N1+ ATOM 866 NH2 ARG A 288 75.574 39.930 24.449 1.00 24.37 N ANISOU 866 NH2 ARG A 288 1479 5084 2694 -342 -490 12 N ATOM 867 N CYS A 289 83.149 43.344 28.275 1.00 39.46 N ANISOU 867 N CYS A 289 2883 7670 4442 -815 -211 85 N ATOM 868 CA CYS A 289 84.293 44.225 28.282 1.00 32.91 C ANISOU 868 CA CYS A 289 1940 6900 3665 -907 -178 72 C ATOM 869 C CYS A 289 85.452 43.535 28.960 1.00 44.81 C ANISOU 869 C CYS A 289 3351 8581 5092 -891 -200 151 C ATOM 870 O CYS A 289 86.587 43.588 28.481 1.00 35.47 O ANISOU 870 O CYS A 289 2057 7473 3948 -886 -164 219 O ATOM 871 CB CYS A 289 83.955 45.542 28.963 1.00 33.53 C ANISOU 871 CB CYS A 289 2016 6915 3809 -1051 -178 -78 C ATOM 872 SG CYS A 289 83.000 46.632 27.892 1.00 35.47 S ANISOU 872 SG CYS A 289 2309 6967 4199 -1085 -139 -148 S ATOM 873 N LYS A 290 85.155 42.858 30.068 1.00 42.29 N ANISOU 873 N LYS A 290 3063 8339 4667 -882 -253 152 N ATOM 874 CA LYS A 290 86.193 42.124 30.786 1.00 44.11 C ANISOU 874 CA LYS A 290 3191 8756 4812 -862 -288 243 C ATOM 875 C LYS A 290 86.807 41.069 29.858 1.00 46.70 C ANISOU 875 C LYS A 290 3475 9121 5146 -714 -268 397 C ATOM 876 O LYS A 290 88.032 40.893 29.841 1.00 47.07 O ANISOU 876 O LYS A 290 3385 9292 5207 -694 -266 470 O ATOM 877 CB LYS A 290 85.637 41.478 32.061 1.00 35.72 C ANISOU 877 CB LYS A 290 2172 7782 3618 -876 -338 242 C ATOM 878 CG LYS A 290 86.415 40.228 32.507 1.00 63.56 C ANISOU 878 CG LYS A 290 5617 11482 7052 -793 -379 397 C ATOM 879 CD LYS A 290 85.885 39.618 33.828 1.00 64.87 C ANISOU 879 CD LYS A 290 5809 11765 7075 -828 -421 414 C ATOM 880 CE LYS A 290 86.957 38.760 34.539 1.00 64.95 C ANISOU 880 CE LYS A 290 5685 11995 6998 -790 -478 557 C ATOM 881 NZ LYS A 290 86.402 37.668 35.411 1.00 60.93 N1+ ANISOU 881 NZ LYS A 290 5204 11583 6364 -763 -508 656 N1+ ATOM 882 N ILE A 291 85.963 40.386 29.081 1.00 34.64 N ANISOU 882 N ILE A 291 2052 7493 3617 -608 -252 439 N ATOM 883 CA ILE A 291 86.434 39.310 28.219 1.00 34.14 C ANISOU 883 CA ILE A 291 1955 7468 3550 -454 -226 580 C ATOM 884 C ILE A 291 87.321 39.855 27.101 1.00 40.08 C ANISOU 884 C ILE A 291 2615 8227 4385 -436 -151 607 C ATOM 885 O ILE A 291 88.308 39.234 26.718 1.00 36.19 O ANISOU 885 O ILE A 291 2017 7830 3902 -338 -117 715 O ATOM 886 CB ILE A 291 85.259 38.521 27.624 1.00 32.40 C ANISOU 886 CB ILE A 291 1863 7138 3311 -357 -228 602 C ATOM 887 CG1 ILE A 291 84.561 37.724 28.724 1.00 32.07 C ANISOU 887 CG1 ILE A 291 1878 7113 3193 -363 -284 611 C ATOM 888 CG2 ILE A 291 85.726 37.576 26.556 1.00 32.66 C ANISOU 888 CG2 ILE A 291 1861 7200 3349 -190 -186 730 C ATOM 889 CD1 ILE A 291 83.178 37.235 28.350 1.00 30.42 C ANISOU 889 CD1 ILE A 291 1796 6770 2994 -323 -294 583 C ATOM 890 N ALA A 292 86.975 41.026 26.582 1.00 35.73 N ANISOU 890 N ALA A 292 2094 7578 3905 -532 -112 515 N ATOM 891 CA ALA A 292 87.795 41.651 25.559 1.00 35.55 C ANISOU 891 CA ALA A 292 1978 7566 3963 -544 -16 546 C ATOM 892 C ALA A 292 89.166 42.058 26.125 1.00 37.79 C ANISOU 892 C ALA A 292 2094 7966 4298 -622 -3 548 C ATOM 893 O ALA A 292 90.174 41.888 25.447 1.00 39.17 O ANISOU 893 O ALA A 292 2151 8210 4522 -569 78 629 O ATOM 894 CB ALA A 292 87.081 42.843 24.968 1.00 34.85 C ANISOU 894 CB ALA A 292 1950 7349 3942 -644 24 460 C ATOM 895 N GLN A 293 89.204 42.566 27.366 1.00 38.37 N ANISOU 895 N GLN A 293 2147 8072 4359 -744 -77 459 N ATOM 896 CA GLN A 293 90.472 42.925 28.025 1.00 40.75 C ANISOU 896 CA GLN A 293 2275 8507 4702 -827 -90 453 C ATOM 897 C GLN A 293 91.307 41.678 28.277 1.00 54.33 C ANISOU 897 C GLN A 293 3890 10382 6369 -695 -123 582 C ATOM 898 O GLN A 293 92.533 41.685 28.058 1.00 55.86 O ANISOU 898 O GLN A 293 3909 10678 6638 -686 -84 633 O ATOM 899 CB GLN A 293 90.255 43.663 29.355 1.00 41.30 C ANISOU 899 CB GLN A 293 2350 8603 4739 -978 -169 330 C ATOM 900 CG GLN A 293 89.804 45.124 29.249 1.00 53.40 C ANISOU 900 CG GLN A 293 3922 10003 6366 -1133 -131 192 C ATOM 901 CD GLN A 293 89.060 45.631 30.510 1.00 53.81 C ANISOU 901 CD GLN A 293 4046 10048 6351 -1236 -202 61 C ATOM 902 OE1 GLN A 293 88.944 44.921 31.522 1.00 56.31 O ANISOU 902 OE1 GLN A 293 4377 10482 6538 -1209 -274 76 O ATOM 903 NE2 GLN A 293 88.543 46.861 30.438 1.00 60.10 N ANISOU 903 NE2 GLN A 293 4882 10716 7235 -1356 -170 -62 N ATOM 904 N GLY A 294 90.641 40.615 28.730 1.00 40.78 N ANISOU 904 N GLY A 294 2270 8681 4542 -595 -186 637 N ATOM 905 CA GLY A 294 91.303 39.354 29.008 1.00 41.92 C ANISOU 905 CA GLY A 294 2326 8960 4641 -457 -220 774 C ATOM 906 C GLY A 294 91.959 38.779 27.770 1.00 49.62 C ANISOU 906 C GLY A 294 3227 9938 5689 -304 -126 879 C ATOM 907 O GLY A 294 93.147 38.439 27.779 1.00 50.79 O ANISOU 907 O GLY A 294 3198 10211 5890 -244 -112 953 O ATOM 908 N ALA A 295 91.190 38.685 26.689 1.00 40.74 N ANISOU 908 N ALA A 295 2227 8684 4568 -236 -56 882 N ATOM 909 CA ALA A 295 91.691 38.094 25.455 1.00 41.30 C ANISOU 909 CA ALA A 295 2249 8759 4684 -74 55 980 C ATOM 910 C ALA A 295 92.899 38.872 24.954 1.00 43.37 C ANISOU 910 C ALA A 295 2340 9078 5060 -133 158 971 C ATOM 911 O ALA A 295 93.889 38.292 24.527 1.00 45.18 O ANISOU 911 O ALA A 295 2433 9392 5344 -12 232 1058 O ATOM 912 CB ALA A 295 90.603 38.053 24.398 1.00 39.28 C ANISOU 912 CB ALA A 295 2155 8371 4397 -16 111 970 C ATOM 913 N ALA A 296 92.811 40.193 25.033 1.00 43.31 N ANISOU 913 N ALA A 296 2335 9016 5104 -321 173 863 N ATOM 914 CA ALA A 296 93.892 41.051 24.598 1.00 45.41 C ANISOU 914 CA ALA A 296 2440 9319 5497 -414 283 846 C ATOM 915 C ALA A 296 95.148 40.918 25.478 1.00 48.93 C ANISOU 915 C ALA A 296 2667 9925 6000 -442 228 861 C ATOM 916 O ALA A 296 96.259 41.024 24.969 1.00 52.64 O ANISOU 916 O ALA A 296 2959 10461 6580 -429 336 896 O ATOM 917 CB ALA A 296 93.422 42.483 24.555 1.00 44.87 C ANISOU 917 CB ALA A 296 2431 9139 5480 -612 307 731 C ATOM 918 N ASN A 297 94.992 40.683 26.780 1.00 48.04 N ANISOU 918 N ASN A 297 2556 9885 5812 -480 72 837 N ATOM 919 CA ASN A 297 96.165 40.516 27.635 1.00 50.79 C ANISOU 919 CA ASN A 297 2686 10410 6201 -499 2 862 C ATOM 920 C ASN A 297 96.893 39.225 27.282 1.00 52.13 C ANISOU 920 C ASN A 297 2739 10680 6390 -282 30 1004 C ATOM 921 O ASN A 297 98.124 39.155 27.341 1.00 70.10 O ANISOU 921 O ASN A 297 4782 13083 8770 -263 50 1039 O ATOM 922 CB ASN A 297 95.791 40.519 29.128 1.00 50.71 C ANISOU 922 CB ASN A 297 2714 10477 6078 -584 -164 816 C ATOM 923 CG ASN A 297 95.243 41.868 29.606 1.00 52.67 C ANISOU 923 CG ASN A 297 3041 10646 6327 -799 -186 659 C ATOM 924 OD1 ASN A 297 95.399 42.891 28.943 1.00 52.46 O ANISOU 924 OD1 ASN A 297 2990 10527 6415 -905 -92 590 O ATOM 925 ND2 ASN A 297 94.602 41.865 30.767 1.00 49.85 N ANISOU 925 ND2 ASN A 297 2773 10323 5843 -861 -298 607 N ATOM 926 N GLY A 298 96.132 38.207 26.902 1.00 50.36 N ANISOU 926 N GLY A 298 2664 10390 6079 -115 36 1082 N ATOM 927 CA GLY A 298 96.698 36.926 26.522 1.00 51.60 C ANISOU 927 CA GLY A 298 2735 10611 6259 115 72 1217 C ATOM 928 C GLY A 298 97.366 36.954 25.162 1.00 52.70 C ANISOU 928 C GLY A 298 2789 10725 6511 208 264 1244 C ATOM 929 O GLY A 298 98.330 36.222 24.925 1.00 55.00 O ANISOU 929 O GLY A 298 2911 11105 6882 364 318 1327 O ATOM 930 N ILE A 299 96.856 37.790 24.257 1.00 51.31 N ANISOU 930 N ILE A 299 2726 10427 6343 122 378 1177 N ATOM 931 CA ILE A 299 97.529 38.000 22.977 1.00 57.09 C ANISOU 931 CA ILE A 299 3379 11142 7170 174 591 1196 C ATOM 932 C ILE A 299 98.796 38.833 23.182 1.00 62.73 C ANISOU 932 C ILE A 299 3846 11954 8034 33 644 1152 C ATOM 933 O ILE A 299 99.827 38.562 22.576 1.00 60.24 O ANISOU 933 O ILE A 299 3357 11705 7826 121 787 1195 O ATOM 934 CB ILE A 299 96.629 38.695 21.946 1.00 54.63 C ANISOU 934 CB ILE A 299 3261 10683 6813 114 705 1153 C ATOM 935 CG1 ILE A 299 95.396 37.829 21.635 1.00 48.18 C ANISOU 935 CG1 ILE A 299 2666 9779 5862 266 660 1194 C ATOM 936 CG2 ILE A 299 97.437 39.017 20.683 1.00 52.67 C ANISOU 936 CG2 ILE A 299 2930 10430 6651 141 954 1175 C ATOM 937 CD1 ILE A 299 94.386 38.484 20.697 1.00 46.28 C ANISOU 937 CD1 ILE A 299 2615 9407 5561 214 742 1157 C ATOM 938 N ASN A 300 98.717 39.841 24.049 1.00 63.56 N ANISOU 938 N ASN A 300 3929 12065 8156 -186 537 1059 N ATOM 939 CA ASN A 300 99.885 40.646 24.378 1.00 66.23 C ANISOU 939 CA ASN A 300 4022 12498 8645 -337 564 1008 C ATOM 940 C ASN A 300 100.988 39.791 24.964 1.00 61.20 C ANISOU 940 C ASN A 300 3141 12043 8070 -218 496 1076 C ATOM 941 O ASN A 300 102.157 40.089 24.784 1.00 64.22 O ANISOU 941 O ASN A 300 3276 12516 8610 -258 583 1069 O ATOM 942 CB ASN A 300 99.534 41.774 25.356 1.00 65.25 C ANISOU 942 CB ASN A 300 3929 12350 8513 -574 437 892 C ATOM 943 CG ASN A 300 100.780 42.499 25.883 1.00 68.70 C ANISOU 943 CG ASN A 300 4088 12907 9106 -728 430 840 C ATOM 944 OD1 ASN A 300 101.334 43.383 25.219 1.00 70.03 O ANISOU 944 OD1 ASN A 300 4156 13030 9420 -852 589 803 O ATOM 945 ND2 ASN A 300 101.218 42.125 27.083 1.00 62.77 N ANISOU 945 ND2 ASN A 300 3210 12313 8326 -727 249 844 N ATOM 946 N PHE A 301 100.621 38.719 25.652 1.00 60.42 N ANISOU 946 N PHE A 301 3101 11996 7858 -72 347 1149 N ATOM 947 CA PHE A 301 101.640 37.852 26.210 1.00 63.26 C ANISOU 947 CA PHE A 301 3230 12528 8280 61 274 1232 C ATOM 948 C PHE A 301 102.296 37.010 25.127 1.00 64.81 C ANISOU 948 C PHE A 301 3324 12731 8572 285 449 1317 C ATOM 949 O PHE A 301 103.477 36.702 25.212 1.00 68.11 O ANISOU 949 O PHE A 301 3472 13281 9126 357 472 1352 O ATOM 950 CB PHE A 301 101.076 36.943 27.297 1.00 62.34 C ANISOU 950 CB PHE A 301 3208 12462 8017 150 74 1301 C ATOM 951 CG PHE A 301 102.128 36.112 27.981 1.00 65.60 C ANISOU 951 CG PHE A 301 3374 13058 8493 280 -25 1397 C ATOM 952 CD1 PHE A 301 102.866 36.633 29.036 1.00 68.04 C ANISOU 952 CD1 PHE A 301 3483 13531 8840 141 -165 1358 C ATOM 953 CD2 PHE A 301 102.395 34.818 27.557 1.00 67.62 C ANISOU 953 CD2 PHE A 301 3590 13322 8781 550 20 1524 C ATOM 954 CE1 PHE A 301 103.841 35.878 29.659 1.00 71.34 C ANISOU 954 CE1 PHE A 301 3658 14128 9322 267 -272 1451 C ATOM 955 CE2 PHE A 301 103.373 34.055 28.184 1.00 69.82 C ANISOU 955 CE2 PHE A 301 3630 13762 9136 685 -79 1619 C ATOM 956 CZ PHE A 301 104.092 34.589 29.235 1.00 72.23 C ANISOU 956 CZ PHE A 301 3730 14240 9475 544 -231 1585 C ATOM 957 N LEU A 302 101.531 36.639 24.110 1.00 62.67 N ANISOU 957 N LEU A 302 3261 12319 8232 399 577 1343 N ATOM 958 CA LEU A 302 102.083 35.858 23.014 1.00 64.20 C ANISOU 958 CA LEU A 302 3388 12505 8500 620 771 1408 C ATOM 959 C LEU A 302 103.077 36.697 22.220 1.00 67.22 C ANISOU 959 C LEU A 302 3584 12917 9038 519 983 1351 C ATOM 960 O LEU A 302 104.188 36.251 21.919 1.00 69.85 O ANISOU 960 O LEU A 302 3683 13347 9511 639 1091 1382 O ATOM 961 CB LEU A 302 100.973 35.336 22.104 1.00 61.45 C ANISOU 961 CB LEU A 302 3323 12000 8025 753 860 1437 C ATOM 962 CG LEU A 302 99.959 34.388 22.759 1.00 63.38 C ANISOU 962 CG LEU A 302 3752 12197 8133 867 685 1499 C ATOM 963 CD1 LEU A 302 98.753 34.122 21.857 1.00 56.42 C ANISOU 963 CD1 LEU A 302 3149 11155 7134 948 764 1499 C ATOM 964 CD2 LEU A 302 100.628 33.078 23.173 1.00 63.68 C ANISOU 964 CD2 LEU A 302 3650 12318 8227 1103 634 1610 C ATOM 965 N HIS A 303 102.679 37.922 21.901 1.00 65.43 N ANISOU 965 N HIS A 303 3455 12604 8801 296 1049 1266 N ATOM 966 CA HIS A 303 103.506 38.808 21.089 1.00 67.70 C ANISOU 966 CA HIS A 303 3600 12893 9231 172 1278 1215 C ATOM 967 C HIS A 303 104.752 39.313 21.816 1.00 72.91 C ANISOU 967 C HIS A 303 3926 13701 10074 40 1234 1174 C ATOM 968 O HIS A 303 105.819 39.405 21.212 1.00 77.74 O ANISOU 968 O HIS A 303 4318 14376 10844 50 1427 1168 O ATOM 969 CB HIS A 303 102.665 39.973 20.593 1.00 65.53 C ANISOU 969 CB HIS A 303 3537 12467 8895 -27 1353 1152 C ATOM 970 CG HIS A 303 101.601 39.557 19.628 1.00 62.93 C ANISOU 970 CG HIS A 303 3497 12005 8408 102 1444 1193 C ATOM 971 ND1 HIS A 303 100.794 40.457 18.974 1.00 61.16 N ANISOU 971 ND1 HIS A 303 3480 11643 8116 -29 1534 1160 N ATOM 972 CD2 HIS A 303 101.222 38.329 19.205 1.00 62.07 C ANISOU 972 CD2 HIS A 303 3501 11880 8202 358 1458 1266 C ATOM 973 CE1 HIS A 303 99.958 39.800 18.188 1.00 59.32 C ANISOU 973 CE1 HIS A 303 3471 11329 7739 139 1590 1210 C ATOM 974 NE2 HIS A 303 100.199 38.508 18.309 1.00 59.82 N ANISOU 974 NE2 HIS A 303 3484 11458 7785 373 1549 1269 N ATOM 975 N GLU A 304 104.621 39.635 23.102 1.00 73.24 N ANISOU 975 N GLU A 304 3930 13805 10095 -85 989 1139 N ATOM 976 CA GLU A 304 105.786 39.921 23.933 1.00 74.44 C ANISOU 976 CA GLU A 304 3755 14124 10403 -179 900 1110 C ATOM 977 C GLU A 304 106.802 38.787 23.840 1.00 77.28 C ANISOU 977 C GLU A 304 3868 14627 10867 56 929 1192 C ATOM 978 O GLU A 304 107.997 39.036 23.754 1.00 81.13 O ANISOU 978 O GLU A 304 4047 15228 11552 15 1015 1168 O ATOM 979 CB GLU A 304 105.389 40.126 25.391 1.00 73.38 C ANISOU 979 CB GLU A 304 3655 14052 10173 -289 612 1078 C ATOM 980 CG GLU A 304 104.927 41.519 25.761 1.00 72.31 C ANISOU 980 CG GLU A 304 3613 13832 10030 -571 575 961 C ATOM 981 CD GLU A 304 104.567 41.612 27.247 1.00 81.14 C ANISOU 981 CD GLU A 304 4766 15033 11032 -657 301 924 C ATOM 982 OE1 GLU A 304 104.962 40.695 28.011 1.00 79.74 O ANISOU 982 OE1 GLU A 304 4471 15012 10816 -526 148 996 O ATOM 983 OE2 GLU A 304 103.884 42.586 27.648 1.00 70.28 O1+ ANISOU 983 OE2 GLU A 304 3536 13566 9600 -851 248 828 O1+ ATOM 984 N ASN A 305 106.319 37.547 23.851 1.00 75.93 N ANISOU 984 N ASN A 305 3826 14444 10579 304 864 1288 N ATOM 985 CA ASN A 305 107.186 36.374 23.763 1.00 78.79 C ANISOU 985 CA ASN A 305 3977 14918 11041 562 888 1375 C ATOM 986 C ASN A 305 107.307 35.827 22.349 1.00 79.19 C ANISOU 986 C ASN A 305 4077 14884 11128 751 1169 1401 C ATOM 987 O ASN A 305 107.539 34.636 22.158 1.00 80.31 O ANISOU 987 O ASN A 305 4180 15046 11288 1021 1191 1483 O ATOM 988 CB ASN A 305 106.690 35.266 24.689 1.00 79.89 C ANISOU 988 CB ASN A 305 4209 15091 11053 736 654 1477 C ATOM 989 CG ASN A 305 106.862 35.612 26.153 1.00 83.40 C ANISOU 989 CG ASN A 305 4545 15672 11471 590 385 1464 C ATOM 990 OD1 ASN A 305 106.044 36.332 26.729 1.00 84.22 O ANISOU 990 OD1 ASN A 305 4832 15724 11442 395 273 1403 O ATOM 991 ND2 ASN A 305 107.925 35.094 26.769 1.00 82.32 N ANISOU 991 ND2 ASN A 305 4107 15713 11458 691 280 1519 N ATOM 992 N HIS A 306 107.112 36.708 21.370 1.00 84.44 N ANISOU 992 N HIS A 306 4845 15446 11794 609 1388 1332 N ATOM 993 CA HIS A 306 107.458 36.463 19.965 1.00 86.29 C ANISOU 993 CA HIS A 306 5087 15626 12074 731 1705 1332 C ATOM 994 C HIS A 306 106.827 35.208 19.359 1.00 78.26 C ANISOU 994 C HIS A 306 4285 14519 10930 1026 1756 1407 C ATOM 995 O HIS A 306 107.448 34.495 18.566 1.00 80.64 O ANISOU 995 O HIS A 306 4498 14835 11305 1231 1957 1425 O ATOM 996 CB HIS A 306 108.984 36.413 19.818 1.00 84.58 C ANISOU 996 CB HIS A 306 4479 15562 12097 763 1844 1310 C ATOM 997 CG HIS A 306 109.678 37.585 20.439 1.00 86.52 C ANISOU 997 CG HIS A 306 4483 15897 12493 479 1791 1234 C ATOM 998 ND1 HIS A 306 109.713 38.829 19.846 1.00 86.63 N ANISOU 998 ND1 HIS A 306 4528 15837 12551 226 1979 1156 N ATOM 999 CD2 HIS A 306 110.341 37.709 21.613 1.00 88.59 C ANISOU 999 CD2 HIS A 306 4478 16311 12871 407 1570 1225 C ATOM 1000 CE1 HIS A 306 110.379 39.666 20.622 1.00 90.02 C ANISOU 1000 CE1 HIS A 306 4712 16358 13135 10 1882 1099 C ATOM 1001 NE2 HIS A 306 110.768 39.012 21.702 1.00 92.25 N ANISOU 1001 NE2 HIS A 306 4809 16785 13455 114 1627 1135 N ATOM 1002 N HIS A 307 105.575 34.967 19.722 1.00 81.81 N ANISOU 1002 N HIS A 307 5020 14868 11197 1042 1586 1440 N ATOM 1003 CA HIS A 307 104.788 33.911 19.101 1.00 82.21 C ANISOU 1003 CA HIS A 307 5316 14801 11120 1288 1637 1499 C ATOM 1004 C HIS A 307 103.627 34.492 18.336 1.00 69.52 C ANISOU 1004 C HIS A 307 4027 13039 9346 1190 1719 1463 C ATOM 1005 O HIS A 307 103.173 35.591 18.632 1.00 71.83 O ANISOU 1005 O HIS A 307 4386 13305 9600 942 1647 1410 O ATOM 1006 CB HIS A 307 104.287 32.920 20.146 1.00 71.55 C ANISOU 1006 CB HIS A 307 4021 13460 9706 1427 1377 1581 C ATOM 1007 CG HIS A 307 105.328 31.934 20.553 1.00 80.21 C ANISOU 1007 CG HIS A 307 4859 14669 10949 1640 1344 1649 C ATOM 1008 ND1 HIS A 307 106.646 32.291 20.749 1.00 82.94 N ANISOU 1008 ND1 HIS A 307 4859 15169 11484 1588 1387 1621 N ATOM 1009 CD2 HIS A 307 105.264 30.599 20.762 1.00 83.36 C ANISOU 1009 CD2 HIS A 307 5283 15039 11349 1915 1281 1742 C ATOM 1010 CE1 HIS A 307 107.344 31.223 21.082 1.00 87.94 C ANISOU 1010 CE1 HIS A 307 5310 15875 12227 1828 1339 1696 C ATOM 1011 NE2 HIS A 307 106.528 30.181 21.096 1.00 86.80 N ANISOU 1011 NE2 HIS A 307 5394 15614 11973 2032 1277 1774 N ATOM 1012 N ILE A 308 103.158 33.756 17.341 1.00 68.91 N ANISOU 1012 N ILE A 308 4149 12857 9177 1395 1871 1487 N ATOM 1013 CA ILE A 308 101.966 34.160 16.621 1.00 65.91 C ANISOU 1013 CA ILE A 308 4087 12335 8623 1339 1925 1464 C ATOM 1014 C ILE A 308 100.937 33.042 16.708 1.00 63.69 C ANISOU 1014 C ILE A 308 4027 11957 8217 1551 1812 1514 C ATOM 1015 O ILE A 308 101.263 31.868 16.574 1.00 65.20 O ANISOU 1015 O ILE A 308 4187 12139 8445 1807 1854 1558 O ATOM 1016 CB ILE A 308 102.297 34.511 15.167 1.00 67.50 C ANISOU 1016 CB ILE A 308 4362 12486 8798 1354 2253 1429 C ATOM 1017 CG1 ILE A 308 103.474 35.485 15.143 1.00 72.79 C ANISOU 1017 CG1 ILE A 308 4767 13261 9628 1154 2383 1384 C ATOM 1018 CG2 ILE A 308 101.116 35.136 14.480 1.00 64.72 C ANISOU 1018 CG2 ILE A 308 4325 12002 8265 1259 2293 1410 C ATOM 1019 CD1 ILE A 308 103.878 35.928 13.762 1.00 76.61 C ANISOU 1019 CD1 ILE A 308 5317 13710 10083 1128 2725 1351 C ATOM 1020 N HIS A 309 99.692 33.411 16.961 1.00 60.32 N ANISOU 1020 N HIS A 309 3814 11448 7657 1442 1668 1502 N ATOM 1021 CA HIS A 309 98.644 32.425 17.160 1.00 59.42 C ANISOU 1021 CA HIS A 309 3896 11243 7437 1607 1544 1541 C ATOM 1022 C HIS A 309 98.093 31.888 15.843 1.00 57.91 C ANISOU 1022 C HIS A 309 3947 10922 7132 1801 1740 1527 C ATOM 1023 O HIS A 309 97.999 30.669 15.647 1.00 58.53 O ANISOU 1023 O HIS A 309 4099 10937 7204 2057 1769 1558 O ATOM 1024 CB HIS A 309 97.519 33.026 17.987 1.00 54.96 C ANISOU 1024 CB HIS A 309 3448 10651 6784 1409 1317 1517 C ATOM 1025 CG HIS A 309 96.519 32.017 18.439 1.00 53.09 C ANISOU 1025 CG HIS A 309 3364 10341 6465 1545 1167 1557 C ATOM 1026 ND1 HIS A 309 95.402 31.698 17.701 1.00 51.20 N ANISOU 1026 ND1 HIS A 309 3373 9977 6106 1643 1211 1540 N ATOM 1027 CD2 HIS A 309 96.481 31.232 19.538 1.00 53.10 C ANISOU 1027 CD2 HIS A 309 3310 10376 6490 1600 985 1617 C ATOM 1028 CE1 HIS A 309 94.708 30.772 18.337 1.00 50.08 C ANISOU 1028 CE1 HIS A 309 3308 9786 5934 1743 1062 1578 C ATOM 1029 NE2 HIS A 309 95.343 30.474 19.455 1.00 51.20 N ANISOU 1029 NE2 HIS A 309 3277 10018 6157 1715 929 1632 N ATOM 1030 N ARG A 310 97.718 32.827 14.970 1.00 57.14 N ANISOU 1030 N ARG A 310 3992 10775 6943 1674 1873 1478 N ATOM 1031 CA ARG A 310 97.236 32.575 13.608 1.00 57.19 C ANISOU 1031 CA ARG A 310 4262 10665 6804 1816 2082 1450 C ATOM 1032 C ARG A 310 95.814 32.018 13.517 1.00 68.57 C ANISOU 1032 C ARG A 310 5974 11987 8094 1924 1971 1440 C ATOM 1033 O ARG A 310 95.326 31.758 12.424 1.00 69.09 O ANISOU 1033 O ARG A 310 6294 11944 8011 2052 2122 1401 O ATOM 1034 CB ARG A 310 98.183 31.631 12.874 1.00 60.41 C ANISOU 1034 CB ARG A 310 4628 11066 7260 2061 2305 1448 C ATOM 1035 CG ARG A 310 99.612 32.126 12.814 1.00 63.54 C ANISOU 1035 CG ARG A 310 4746 11586 7811 1974 2452 1444 C ATOM 1036 CD ARG A 310 100.307 31.626 11.561 1.00 72.83 C ANISOU 1036 CD ARG A 310 5980 12727 8964 2156 2766 1406 C ATOM 1037 NE ARG A 310 100.289 30.170 11.453 1.00 71.90 N ANISOU 1037 NE ARG A 310 5928 12534 8856 2470 2783 1407 N ATOM 1038 CZ ARG A 310 100.758 29.496 10.409 1.00 70.30 C ANISOU 1038 CZ ARG A 310 5817 12270 8622 2675 3040 1353 C ATOM 1039 NH1 ARG A 310 101.280 30.147 9.380 1.00 72.29 N1+ ANISOU 1039 NH1 ARG A 310 6105 12546 8814 2591 3303 1302 N1+ ATOM 1040 NH2 ARG A 310 100.702 28.174 10.393 1.00 71.27 N ANISOU 1040 NH2 ARG A 310 6008 12299 8773 2958 3041 1344 N ATOM 1041 N ASN A 311 95.146 31.827 14.645 1.00 52.38 N ANISOU 1041 N ASN A 311 3884 9950 6067 1869 1713 1463 N ATOM 1042 CA ASN A 311 93.785 31.354 14.594 1.00 50.00 C ANISOU 1042 CA ASN A 311 3811 9544 5641 1951 1611 1443 C ATOM 1043 C ASN A 311 92.944 31.962 15.734 1.00 53.05 C ANISOU 1043 C ASN A 311 4153 9969 6035 1729 1349 1440 C ATOM 1044 O ASN A 311 92.103 31.299 16.360 1.00 45.79 O ANISOU 1044 O ASN A 311 3294 9008 5096 1781 1185 1448 O ATOM 1045 CB ASN A 311 93.764 29.827 14.611 1.00 50.91 C ANISOU 1045 CB ASN A 311 3985 9580 5778 2241 1616 1465 C ATOM 1046 CG ASN A 311 92.572 29.246 13.850 1.00 59.06 C ANISOU 1046 CG ASN A 311 5329 10456 6653 2406 1651 1401 C ATOM 1047 OD1 ASN A 311 91.777 29.975 13.228 1.00 59.82 O ANISOU 1047 OD1 ASN A 311 5607 10520 6602 2314 1682 1344 O ATOM 1048 ND2 ASN A 311 92.444 27.927 13.894 1.00 54.06 N ANISOU 1048 ND2 ASN A 311 4776 9713 6051 2653 1645 1404 N ATOM 1049 N ILE A 312 93.194 33.246 15.975 1.00 47.03 N ANISOU 1049 N ILE A 312 3295 9269 5306 1474 1327 1418 N ATOM 1050 CA ILE A 312 92.377 34.040 16.863 1.00 44.73 C ANISOU 1050 CA ILE A 312 3002 8986 5007 1245 1121 1381 C ATOM 1051 C ILE A 312 90.977 34.193 16.280 1.00 50.56 C ANISOU 1051 C ILE A 312 3965 9633 5611 1260 1104 1341 C ATOM 1052 O ILE A 312 90.769 34.840 15.234 1.00 42.73 O ANISOU 1052 O ILE A 312 3108 8598 4530 1242 1254 1324 O ATOM 1053 CB ILE A 312 92.984 35.424 17.098 1.00 45.30 C ANISOU 1053 CB ILE A 312 2949 9110 5152 988 1137 1347 C ATOM 1054 CG1 ILE A 312 94.325 35.306 17.821 1.00 47.52 C ANISOU 1054 CG1 ILE A 312 2987 9499 5568 961 1123 1370 C ATOM 1055 CG2 ILE A 312 92.042 36.279 17.893 1.00 43.04 C ANISOU 1055 CG2 ILE A 312 2706 8798 4851 768 950 1284 C ATOM 1056 CD1 ILE A 312 94.241 34.754 19.229 1.00 46.97 C ANISOU 1056 CD1 ILE A 312 2839 9481 5525 942 896 1385 C ATOM 1057 N LYS A 313 90.027 33.572 16.972 1.00 48.25 N ANISOU 1057 N LYS A 313 3722 9313 5299 1291 924 1330 N ATOM 1058 CA LYS A 313 88.627 33.599 16.616 1.00 38.93 C ANISOU 1058 CA LYS A 313 2715 8063 4015 1311 868 1280 C ATOM 1059 C LYS A 313 87.822 33.260 17.869 1.00 50.96 C ANISOU 1059 C LYS A 313 4206 9575 5583 1219 618 1259 C ATOM 1060 O LYS A 313 88.361 32.644 18.793 1.00 37.90 O ANISOU 1060 O LYS A 313 2459 7947 3994 1223 537 1305 O ATOM 1061 CB LYS A 313 88.345 32.621 15.490 1.00 39.63 C ANISOU 1061 CB LYS A 313 3102 7954 4001 1539 955 1246 C ATOM 1062 CG LYS A 313 88.531 31.160 15.843 1.00 40.41 C ANISOU 1062 CG LYS A 313 3183 8020 4152 1756 927 1283 C ATOM 1063 CD LYS A 313 88.449 30.325 14.575 1.00 41.67 C ANISOU 1063 CD LYS A 313 3643 7981 4209 1973 1060 1224 C ATOM 1064 CE LYS A 313 88.216 28.875 14.859 1.00 42.13 C ANISOU 1064 CE LYS A 313 3785 7908 4314 2162 990 1225 C ATOM 1065 NZ LYS A 313 88.304 28.111 13.606 1.00 43.82 N1+ ANISOU 1065 NZ LYS A 313 4274 7943 4432 2374 1149 1149 N1+ ATOM 1066 N SER A 314 86.544 33.655 17.900 1.00 35.37 N ANISOU 1066 N SER A 314 2393 7485 3563 1106 483 1173 N ATOM 1067 CA SER A 314 85.717 33.511 19.101 1.00 33.88 C ANISOU 1067 CA SER A 314 2145 7318 3412 990 277 1146 C ATOM 1068 C SER A 314 85.515 32.059 19.538 1.00 34.12 C ANISOU 1068 C SER A 314 2218 7292 3455 1148 201 1196 C ATOM 1069 O SER A 314 85.271 31.792 20.698 1.00 33.64 O ANISOU 1069 O SER A 314 2152 7210 3422 1026 81 1193 O ATOM 1070 CB SER A 314 84.350 34.180 18.894 1.00 36.67 C ANISOU 1070 CB SER A 314 2698 7506 3728 851 158 1025 C ATOM 1071 OG SER A 314 83.569 33.535 17.891 1.00 37.45 O ANISOU 1071 OG SER A 314 3101 7375 3754 979 141 969 O ATOM 1072 N ALA A 315 85.619 31.120 18.612 1.00 35.80 N ANISOU 1072 N ALA A 315 2620 7350 3634 1359 289 1200 N ATOM 1073 CA ALA A 315 85.476 29.722 18.968 1.00 37.15 C ANISOU 1073 CA ALA A 315 2848 7430 3835 1516 233 1250 C ATOM 1074 C ALA A 315 86.711 29.217 19.725 1.00 54.60 C ANISOU 1074 C ALA A 315 4805 9814 6126 1612 279 1390 C ATOM 1075 O ALA A 315 86.655 28.159 20.370 1.00 52.71 O ANISOU 1075 O ALA A 315 4590 9509 5928 1691 207 1455 O ATOM 1076 CB ALA A 315 85.222 28.871 17.722 1.00 36.49 C ANISOU 1076 CB ALA A 315 3066 7103 3694 1708 317 1186 C ATOM 1077 N ASN A 316 87.813 29.966 19.635 1.00 38.35 N ANISOU 1077 N ASN A 316 2607 7876 4086 1544 388 1406 N ATOM 1078 CA ASN A 316 89.057 29.596 20.307 1.00 40.26 C ANISOU 1078 CA ASN A 316 2696 8200 4402 1569 407 1493 C ATOM 1079 C ASN A 316 89.333 30.453 21.529 1.00 45.76 C ANISOU 1079 C ASN A 316 3280 8997 5108 1299 290 1476 C ATOM 1080 O ASN A 316 90.447 30.466 22.068 1.00 41.62 O ANISOU 1080 O ASN A 316 2604 8574 4637 1286 296 1528 O ATOM 1081 CB ASN A 316 90.258 29.685 19.368 1.00 42.35 C ANISOU 1081 CB ASN A 316 2877 8514 4701 1706 610 1517 C ATOM 1082 CG ASN A 316 90.262 28.598 18.335 1.00 43.54 C ANISOU 1082 CG ASN A 316 3149 8550 4845 2019 757 1531 C ATOM 1083 OD1 ASN A 316 89.599 27.579 18.492 1.00 58.40 O ANISOU 1083 OD1 ASN A 316 5147 10311 6731 2161 685 1548 O ATOM 1084 ND2 ASN A 316 90.997 28.812 17.252 1.00 62.78 N ANISOU 1084 ND2 ASN A 316 5588 10997 7269 2124 974 1509 N ATOM 1085 N ILE A 317 88.325 31.180 21.968 1.00 37.86 N ANISOU 1085 N ILE A 317 2360 7965 4060 1094 186 1388 N ATOM 1086 CA ILE A 317 88.435 31.846 23.244 1.00 37.60 C ANISOU 1086 CA ILE A 317 2270 7995 4023 868 79 1353 C ATOM 1087 C ILE A 317 87.531 31.111 24.211 1.00 36.77 C ANISOU 1087 C ILE A 317 2250 7834 3889 835 -40 1365 C ATOM 1088 O ILE A 317 86.312 31.084 24.047 1.00 35.41 O ANISOU 1088 O ILE A 317 2208 7555 3691 794 -84 1300 O ATOM 1089 CB ILE A 317 88.076 33.342 23.144 1.00 47.74 C ANISOU 1089 CB ILE A 317 3578 9268 5292 651 74 1231 C ATOM 1090 CG1 ILE A 317 89.022 34.017 22.157 1.00 37.54 C ANISOU 1090 CG1 ILE A 317 2196 8028 4041 679 212 1238 C ATOM 1091 CG2 ILE A 317 88.121 34.014 24.537 1.00 36.26 C ANISOU 1091 CG2 ILE A 317 2092 7857 3827 438 -27 1171 C ATOM 1092 CD1 ILE A 317 88.724 35.435 21.934 1.00 36.69 C ANISOU 1092 CD1 ILE A 317 2111 7891 3939 490 223 1139 C ATOM 1093 N LEU A 318 88.137 30.484 25.204 1.00 38.19 N ANISOU 1093 N LEU A 318 2347 8088 4077 858 -90 1454 N ATOM 1094 CA LEU A 318 87.394 29.679 26.155 1.00 37.91 C ANISOU 1094 CA LEU A 318 2377 8011 4014 839 -185 1497 C ATOM 1095 C LEU A 318 87.055 30.511 27.375 1.00 37.26 C ANISOU 1095 C LEU A 318 2296 7992 3870 598 -260 1421 C ATOM 1096 O LEU A 318 87.660 31.553 27.600 1.00 37.88 O ANISOU 1096 O LEU A 318 2301 8153 3939 478 -251 1358 O ATOM 1097 CB LEU A 318 88.190 28.436 26.536 1.00 40.15 C ANISOU 1097 CB LEU A 318 2581 8335 4338 1028 -198 1658 C ATOM 1098 CG LEU A 318 88.214 27.504 25.340 1.00 40.66 C ANISOU 1098 CG LEU A 318 2703 8281 4466 1289 -116 1710 C ATOM 1099 CD1 LEU A 318 88.636 26.117 25.731 1.00 42.73 C ANISOU 1099 CD1 LEU A 318 2946 8505 4785 1493 -142 1864 C ATOM 1100 CD2 LEU A 318 86.823 27.519 24.736 1.00 38.54 C ANISOU 1100 CD2 LEU A 318 2608 7865 4171 1261 -133 1620 C ATOM 1101 N LEU A 319 86.074 30.064 28.146 1.00 36.57 N ANISOU 1101 N LEU A 319 2291 7858 3744 532 -326 1423 N ATOM 1102 CA LEU A 319 85.674 30.783 29.351 1.00 39.25 C ANISOU 1102 CA LEU A 319 2639 8262 4012 323 -376 1349 C ATOM 1103 C LEU A 319 85.622 29.845 30.570 1.00 37.49 C ANISOU 1103 C LEU A 319 2387 8122 3737 329 -444 1475 C ATOM 1104 O LEU A 319 84.893 28.855 30.555 1.00 37.32 O ANISOU 1104 O LEU A 319 2434 8016 3730 400 -469 1545 O ATOM 1105 CB LEU A 319 84.321 31.452 29.118 1.00 33.99 C ANISOU 1105 CB LEU A 319 2106 7466 3343 195 -373 1197 C ATOM 1106 CG LEU A 319 84.242 32.444 27.956 1.00 36.90 C ANISOU 1106 CG LEU A 319 2511 7750 3757 179 -321 1082 C ATOM 1107 CD1 LEU A 319 82.791 32.750 27.649 1.00 32.09 C ANISOU 1107 CD1 LEU A 319 2031 6995 3168 106 -337 961 C ATOM 1108 CD2 LEU A 319 84.980 33.726 28.268 1.00 33.26 C ANISOU 1108 CD2 LEU A 319 1983 7366 3287 56 -305 1007 C ATOM 1109 N ASP A 320 86.408 30.134 31.612 1.00 40.84 N ANISOU 1109 N ASP A 320 2705 8714 4099 259 -483 1513 N ATOM 1110 CA ASP A 320 86.388 29.284 32.814 1.00 46.36 C ANISOU 1110 CA ASP A 320 3368 9517 4730 262 -556 1649 C ATOM 1111 C ASP A 320 85.213 29.645 33.728 1.00 51.46 C ANISOU 1111 C ASP A 320 4094 10178 5279 73 -573 1572 C ATOM 1112 O ASP A 320 84.283 30.337 33.318 1.00 37.66 O ANISOU 1112 O ASP A 320 2444 8319 3545 -23 -531 1420 O ATOM 1113 CB ASP A 320 87.709 29.355 33.599 1.00 44.13 C ANISOU 1113 CB ASP A 320 2925 9432 4410 275 -610 1734 C ATOM 1114 CG ASP A 320 87.969 30.717 34.234 1.00 51.14 C ANISOU 1114 CG ASP A 320 3768 10440 5225 78 -618 1594 C ATOM 1115 OD1 ASP A 320 87.104 31.604 34.152 1.00 49.73 O1+ ANISOU 1115 OD1 ASP A 320 3691 10183 5023 -63 -578 1436 O1+ ATOM 1116 OD2 ASP A 320 89.067 30.909 34.810 1.00 48.37 O ANISOU 1116 OD2 ASP A 320 3275 10254 4850 73 -672 1639 O ATOM 1117 N GLU A 321 85.266 29.168 34.967 1.00 48.45 N ANISOU 1117 N GLU A 321 3664 9941 4802 29 -635 1682 N ATOM 1118 CA GLU A 321 84.127 29.286 35.875 1.00 40.86 C ANISOU 1118 CA GLU A 321 2765 9019 3739 -135 -642 1642 C ATOM 1119 C GLU A 321 83.783 30.738 36.213 1.00 51.64 C ANISOU 1119 C GLU A 321 4154 10423 5043 -325 -599 1434 C ATOM 1120 O GLU A 321 82.681 31.030 36.683 1.00 38.95 O ANISOU 1120 O GLU A 321 2613 8808 3377 -455 -575 1348 O ATOM 1121 CB GLU A 321 84.406 28.515 37.165 1.00 43.36 C ANISOU 1121 CB GLU A 321 3013 9516 3946 -143 -722 1820 C ATOM 1122 CG GLU A 321 84.491 26.995 36.993 1.00 59.91 C ANISOU 1122 CG GLU A 321 5128 11535 6100 45 -776 2040 C ATOM 1123 CD GLU A 321 85.900 26.484 36.693 1.00 57.48 C ANISOU 1123 CD GLU A 321 4723 11253 5864 246 -817 2167 C ATOM 1124 OE1 GLU A 321 86.715 27.228 36.083 1.00 59.41 O ANISOU 1124 OE1 GLU A 321 4897 11513 6162 269 -780 2069 O ATOM 1125 OE2 GLU A 321 86.184 25.325 37.071 1.00 55.59 O1+ ANISOU 1125 OE2 GLU A 321 4482 11012 5630 385 -888 2371 O1+ ATOM 1126 N ALA A 322 84.733 31.640 35.982 1.00 40.09 N ANISOU 1126 N ALA A 322 2633 9000 3601 -335 -592 1354 N ATOM 1127 CA ALA A 322 84.558 33.030 36.336 1.00 39.55 C ANISOU 1127 CA ALA A 322 2584 8956 3486 -496 -564 1165 C ATOM 1128 C ALA A 322 84.414 33.858 35.090 1.00 37.63 C ANISOU 1128 C ALA A 322 2412 8519 3367 -476 -509 1024 C ATOM 1129 O ALA A 322 84.351 35.084 35.156 1.00 43.89 O ANISOU 1129 O ALA A 322 3226 9288 4163 -583 -488 866 O ATOM 1130 CB ALA A 322 85.706 33.509 37.139 1.00 41.74 C ANISOU 1130 CB ALA A 322 2733 9434 3692 -550 -616 1178 C ATOM 1131 N PHE A 323 84.374 33.178 33.949 1.00 36.73 N ANISOU 1131 N PHE A 323 2331 8271 3355 -333 -490 1088 N ATOM 1132 CA PHE A 323 84.227 33.831 32.654 1.00 35.99 C ANISOU 1132 CA PHE A 323 2299 8007 3369 -300 -442 982 C ATOM 1133 C PHE A 323 85.489 34.640 32.340 1.00 38.98 C ANISOU 1133 C PHE A 323 2579 8449 3783 -303 -434 957 C ATOM 1134 O PHE A 323 85.466 35.681 31.677 1.00 38.45 O ANISOU 1134 O PHE A 323 2540 8291 3778 -353 -399 839 O ATOM 1135 CB PHE A 323 82.970 34.702 32.622 1.00 33.41 C ANISOU 1135 CB PHE A 323 2089 7547 3057 -414 -416 809 C ATOM 1136 CG PHE A 323 81.692 33.914 32.521 1.00 32.33 C ANISOU 1136 CG PHE A 323 2042 7310 2932 -394 -419 820 C ATOM 1137 CD1 PHE A 323 81.057 33.440 33.664 1.00 32.92 C ANISOU 1137 CD1 PHE A 323 2116 7479 2913 -472 -437 855 C ATOM 1138 CD2 PHE A 323 81.119 33.642 31.270 1.00 30.97 C ANISOU 1138 CD2 PHE A 323 1940 6968 2861 -306 -407 799 C ATOM 1139 CE1 PHE A 323 79.874 32.714 33.580 1.00 32.17 C ANISOU 1139 CE1 PHE A 323 2085 7301 2839 -470 -443 867 C ATOM 1140 CE2 PHE A 323 79.923 32.910 31.172 1.00 30.22 C ANISOU 1140 CE2 PHE A 323 1913 6780 2789 -298 -425 800 C ATOM 1141 CZ PHE A 323 79.295 32.450 32.329 1.00 30.81 C ANISOU 1141 CZ PHE A 323 1981 6939 2785 -384 -443 833 C ATOM 1142 N THR A 324 86.606 34.137 32.835 1.00 47.80 N ANISOU 1142 N THR A 324 3564 9729 4870 -250 -472 1079 N ATOM 1143 CA THR A 324 87.895 34.663 32.437 1.00 45.88 C ANISOU 1143 CA THR A 324 3194 9555 4682 -229 -466 1082 C ATOM 1144 C THR A 324 88.189 34.155 31.034 1.00 51.55 C ANISOU 1144 C THR A 324 3909 10177 5501 -66 -407 1146 C ATOM 1145 O THR A 324 87.954 32.979 30.737 1.00 51.58 O ANISOU 1145 O THR A 324 3938 10144 5514 78 -405 1259 O ATOM 1146 CB THR A 324 88.984 34.221 33.409 1.00 59.57 C ANISOU 1146 CB THR A 324 4769 11500 6365 -210 -537 1196 C ATOM 1147 OG1 THR A 324 88.618 34.628 34.741 1.00 60.90 O ANISOU 1147 OG1 THR A 324 4946 11780 6412 -363 -589 1142 O ATOM 1148 CG2 THR A 324 90.346 34.797 33.001 1.00 43.77 C ANISOU 1148 CG2 THR A 324 2609 9578 4445 -198 -533 1188 C ATOM 1149 N ALA A 325 88.677 35.026 30.164 1.00 38.87 N ANISOU 1149 N ALA A 325 2268 8531 3969 -85 -354 1075 N ATOM 1150 CA ALA A 325 88.970 34.601 28.806 1.00 38.68 C ANISOU 1150 CA ALA A 325 2232 8442 4023 69 -281 1135 C ATOM 1151 C ALA A 325 90.253 33.766 28.788 1.00 41.04 C ANISOU 1151 C ALA A 325 2366 8868 4360 220 -277 1278 C ATOM 1152 O ALA A 325 91.247 34.144 29.400 1.00 42.92 O ANISOU 1152 O ALA A 325 2457 9241 4610 165 -311 1285 O ATOM 1153 CB ALA A 325 89.079 35.801 27.891 1.00 38.08 C ANISOU 1153 CB ALA A 325 2160 8298 4011 -6 -214 1030 C ATOM 1154 N LYS A 326 90.208 32.620 28.115 1.00 41.16 N ANISOU 1154 N LYS A 326 2399 8835 4404 418 -239 1386 N ATOM 1155 CA LYS A 326 91.373 31.754 27.980 1.00 43.56 C ANISOU 1155 CA LYS A 326 2550 9230 4769 601 -220 1522 C ATOM 1156 C LYS A 326 91.569 31.324 26.538 1.00 54.47 C ANISOU 1156 C LYS A 326 3941 10531 6224 790 -97 1555 C ATOM 1157 O LYS A 326 90.752 30.596 25.985 1.00 42.46 O ANISOU 1157 O LYS A 326 2549 8891 4692 906 -71 1579 O ATOM 1158 CB LYS A 326 91.247 30.532 28.868 1.00 44.54 C ANISOU 1158 CB LYS A 326 2675 9388 4862 699 -301 1651 C ATOM 1159 CG LYS A 326 90.928 30.898 30.274 1.00 45.30 C ANISOU 1159 CG LYS A 326 2777 9573 4860 520 -406 1624 C ATOM 1160 CD LYS A 326 92.044 30.546 31.214 1.00 47.49 C ANISOU 1160 CD LYS A 326 2877 10032 5134 558 -488 1732 C ATOM 1161 CE LYS A 326 91.767 31.077 32.593 1.00 47.75 C ANISOU 1161 CE LYS A 326 2912 10181 5049 366 -583 1688 C ATOM 1162 NZ LYS A 326 93.012 31.053 33.399 1.00 58.69 N1+ ANISOU 1162 NZ LYS A 326 4096 11770 6434 377 -671 1762 N1+ ATOM 1163 N ILE A 327 92.673 31.766 25.935 1.00 57.00 N ANISOU 1163 N ILE A 327 4117 10919 6621 824 -12 1554 N ATOM 1164 CA ILE A 327 92.907 31.504 24.526 1.00 45.43 C ANISOU 1164 CA ILE A 327 2659 9391 5213 994 139 1572 C ATOM 1165 C ILE A 327 93.338 30.074 24.360 1.00 47.15 C ANISOU 1165 C ILE A 327 2838 9597 5482 1261 171 1699 C ATOM 1166 O ILE A 327 94.089 29.556 25.160 1.00 54.23 O ANISOU 1166 O ILE A 327 3603 10586 6418 1315 104 1783 O ATOM 1167 CB ILE A 327 93.932 32.450 23.943 1.00 46.80 C ANISOU 1167 CB ILE A 327 2687 9634 5462 931 244 1526 C ATOM 1168 CG1 ILE A 327 93.462 33.883 24.186 1.00 45.27 C ANISOU 1168 CG1 ILE A 327 2544 9422 5234 667 204 1398 C ATOM 1169 CG2 ILE A 327 94.107 32.172 22.455 1.00 47.23 C ANISOU 1169 CG2 ILE A 327 2770 9623 5552 1109 433 1542 C ATOM 1170 CD1 ILE A 327 94.206 34.922 23.403 1.00 52.71 C ANISOU 1170 CD1 ILE A 327 3388 10385 6257 585 332 1344 C ATOM 1171 N SER A 328 92.830 29.439 23.318 1.00 52.37 N ANISOU 1171 N SER A 328 3622 10133 6142 1440 271 1710 N ATOM 1172 CA SER A 328 92.911 27.999 23.167 1.00 53.81 C ANISOU 1172 CA SER A 328 3836 10239 6372 1706 295 1813 C ATOM 1173 C SER A 328 93.362 27.626 21.752 1.00 49.07 C ANISOU 1173 C SER A 328 3252 9569 5823 1938 498 1807 C ATOM 1174 O SER A 328 93.634 28.504 20.941 1.00 48.92 O ANISOU 1174 O SER A 328 3211 9584 5795 1874 618 1736 O ATOM 1175 CB SER A 328 91.543 27.385 23.491 1.00 45.93 C ANISOU 1175 CB SER A 328 3032 9109 5310 1705 198 1816 C ATOM 1176 OG SER A 328 91.570 25.965 23.488 1.00 49.78 O ANISOU 1176 OG SER A 328 3569 9488 5857 1951 201 1919 O ATOM 1177 N ASP A 329 93.423 26.321 21.481 1.00 67.96 N ANISOU 1177 N ASP A 329 5703 11850 8270 2206 543 1877 N ATOM 1178 CA ASP A 329 93.769 25.740 20.175 1.00 51.91 C ANISOU 1178 CA ASP A 329 3735 9712 6278 2468 752 1857 C ATOM 1179 C ASP A 329 94.953 26.411 19.535 1.00 53.75 C ANISOU 1179 C ASP A 329 3801 10058 6562 2460 916 1826 C ATOM 1180 O ASP A 329 94.826 27.033 18.489 1.00 53.21 O ANISOU 1180 O ASP A 329 3811 9970 6436 2439 1069 1744 O ATOM 1181 CB ASP A 329 92.584 25.799 19.203 1.00 66.55 C ANISOU 1181 CB ASP A 329 5836 11421 8029 2509 819 1765 C ATOM 1182 CG ASP A 329 92.820 24.964 17.933 1.00 68.21 C ANISOU 1182 CG ASP A 329 6182 11479 8255 2814 1035 1727 C ATOM 1183 OD1 ASP A 329 93.922 24.384 17.775 1.00 62.07 O ANISOU 1183 OD1 ASP A 329 5293 10707 7582 2983 1146 1769 O ATOM 1184 OD2 ASP A 329 91.896 24.895 17.088 1.00 68.92 O1+ ANISOU 1184 OD2 ASP A 329 6501 11437 8249 2888 1097 1638 O1+ ATOM 1185 N PHE A 330 96.112 26.268 20.158 1.00 63.92 N ANISOU 1185 N PHE A 330 4860 11466 7961 2478 887 1892 N ATOM 1186 CA PHE A 330 97.343 26.805 19.601 1.00 68.83 C ANISOU 1186 CA PHE A 330 5289 12196 8667 2479 1045 1863 C ATOM 1187 C PHE A 330 97.862 25.953 18.441 1.00 71.53 C ANISOU 1187 C PHE A 330 5672 12432 9072 2773 1281 1849 C ATOM 1188 O PHE A 330 99.066 25.891 18.201 1.00 73.54 O ANISOU 1188 O PHE A 330 5726 12766 9448 2856 1400 1856 O ATOM 1189 CB PHE A 330 98.398 26.921 20.699 1.00 67.52 C ANISOU 1189 CB PHE A 330 4848 12200 8608 2407 919 1928 C ATOM 1190 CG PHE A 330 98.028 27.904 21.762 1.00 64.71 C ANISOU 1190 CG PHE A 330 4458 11949 8178 2105 724 1907 C ATOM 1191 CD1 PHE A 330 97.117 27.565 22.746 1.00 62.74 C ANISOU 1191 CD1 PHE A 330 4328 11665 7844 2041 533 1950 C ATOM 1192 CD2 PHE A 330 98.556 29.182 21.758 1.00 69.83 C ANISOU 1192 CD2 PHE A 330 4974 12712 8844 1880 748 1832 C ATOM 1193 CE1 PHE A 330 96.759 28.469 23.723 1.00 55.40 C ANISOU 1193 CE1 PHE A 330 3390 10823 6838 1768 376 1909 C ATOM 1194 CE2 PHE A 330 98.198 30.094 22.736 1.00 68.04 C ANISOU 1194 CE2 PHE A 330 4743 12557 8554 1612 579 1791 C ATOM 1195 CZ PHE A 330 97.294 29.732 23.720 1.00 55.59 C ANISOU 1195 CZ PHE A 330 3292 10951 6879 1561 396 1825 C ATOM 1196 N GLY A 331 96.938 25.323 17.718 1.00 59.73 N ANISOU 1196 N GLY A 331 4444 10753 7496 2926 1353 1812 N ATOM 1197 CA GLY A 331 97.273 24.404 16.648 1.00 67.95 C ANISOU 1197 CA GLY A 331 5592 11650 8574 3217 1575 1772 C ATOM 1198 C GLY A 331 98.059 24.997 15.491 1.00 70.59 C ANISOU 1198 C GLY A 331 5881 12036 8903 3223 1839 1688 C ATOM 1199 O GLY A 331 98.670 24.267 14.707 1.00 75.80 O ANISOU 1199 O GLY A 331 6567 12614 9621 3454 2041 1649 O ATOM 1200 N LEU A 332 98.059 26.318 15.370 1.00 69.20 N ANISOU 1200 N LEU A 332 5647 11983 8662 2963 1849 1653 N ATOM 1201 CA LEU A 332 98.730 26.938 14.232 1.00 64.14 C ANISOU 1201 CA LEU A 332 4992 11376 8002 2940 2113 1579 C ATOM 1202 C LEU A 332 99.881 27.848 14.676 1.00 71.39 C ANISOU 1202 C LEU A 332 5586 12490 9049 2747 2115 1600 C ATOM 1203 O LEU A 332 100.502 28.518 13.855 1.00 67.31 O ANISOU 1203 O LEU A 332 5020 12020 8534 2676 2326 1545 O ATOM 1204 CB LEU A 332 97.715 27.717 13.377 1.00 71.17 C ANISOU 1204 CB LEU A 332 6155 12194 8691 2819 2184 1504 C ATOM 1205 CG LEU A 332 96.634 26.916 12.618 1.00 67.92 C ANISOU 1205 CG LEU A 332 6099 11580 8126 3015 2238 1440 C ATOM 1206 CD1 LEU A 332 95.770 27.830 11.764 1.00 65.08 C ANISOU 1206 CD1 LEU A 332 5988 11180 7561 2878 2305 1368 C ATOM 1207 CD2 LEU A 332 97.244 25.813 11.750 1.00 63.91 C ANISOU 1207 CD2 LEU A 332 5682 10954 7648 3308 2463 1384 C ATOM 1208 N ALA A 333 100.168 27.848 15.977 1.00 73.84 N ANISOU 1208 N ALA A 333 5688 12908 9461 2662 1884 1672 N ATOM 1209 CA ALA A 333 101.195 28.713 16.558 1.00 74.27 C ANISOU 1209 CA ALA A 333 5439 13143 9636 2468 1845 1677 C ATOM 1210 C ALA A 333 102.609 28.141 16.408 1.00 71.49 C ANISOU 1210 C ALA A 333 4821 12873 9470 2643 1980 1691 C ATOM 1211 O ALA A 333 102.869 27.313 15.541 1.00 73.41 O ANISOU 1211 O ALA A 333 5131 13027 9736 2889 2179 1669 O ATOM 1212 CB ALA A 333 100.885 28.965 18.027 1.00 65.57 C ANISOU 1212 CB ALA A 333 4254 12123 8536 2300 1538 1731 C ATOM 1213 N THR A 342 110.276 40.040 6.890 1.00 98.70 N ANISOU 1213 N THR A 342 7539 16873 13091 270 5200 1065 N ATOM 1214 CA THR A 342 109.042 39.482 6.337 1.00103.16 C ANISOU 1214 CA THR A 342 8536 17291 13367 458 5127 1121 C ATOM 1215 C THR A 342 109.141 37.969 6.144 1.00102.11 C ANISOU 1215 C THR A 342 8400 17183 13214 830 5131 1097 C ATOM 1216 O THR A 342 110.079 37.461 5.519 1.00 99.99 O ANISOU 1216 O THR A 342 7980 17020 12992 943 5392 1040 O ATOM 1217 CB THR A 342 108.667 40.143 4.984 1.00101.65 C ANISOU 1217 CB THR A 342 8705 17028 12890 332 5397 1156 C ATOM 1218 OG1 THR A 342 107.825 41.278 5.226 1.00 99.41 O ANISOU 1218 OG1 THR A 342 8616 16621 12532 86 5263 1218 O ATOM 1219 CG2 THR A 342 107.919 39.157 4.089 1.00 95.37 C ANISOU 1219 CG2 THR A 342 8275 16142 11820 616 5443 1171 C ATOM 1220 N VAL A 343 108.155 37.260 6.685 1.00 92.24 N ANISOU 1220 N VAL A 343 7319 15832 11898 1016 4847 1136 N ATOM 1221 CA VAL A 343 108.138 35.803 6.663 1.00 92.47 C ANISOU 1221 CA VAL A 343 7357 15852 11925 1368 4809 1119 C ATOM 1222 C VAL A 343 106.939 35.268 5.872 1.00 93.67 C ANISOU 1222 C VAL A 343 7974 15836 11779 1536 4809 1136 C ATOM 1223 O VAL A 343 105.783 35.566 6.189 1.00 86.14 O ANISOU 1223 O VAL A 343 7258 14770 10702 1477 4587 1186 O ATOM 1224 CB VAL A 343 108.109 35.225 8.103 1.00 90.99 C ANISOU 1224 CB VAL A 343 6933 15702 11939 1471 4459 1149 C ATOM 1225 CG1 VAL A 343 108.148 33.701 8.079 1.00 91.31 C ANISOU 1225 CG1 VAL A 343 6979 15720 11994 1838 4435 1142 C ATOM 1226 CG2 VAL A 343 109.254 35.792 8.934 1.00 93.09 C ANISOU 1226 CG2 VAL A 343 6750 16130 12489 1297 4426 1126 C ATOM 1227 N MET A 344 107.231 34.471 4.844 1.00 94.12 N ANISOU 1227 N MET A 344 8154 15880 11726 1746 5060 1080 N ATOM 1228 CA MET A 344 106.200 33.864 4.005 1.00 92.51 C ANISOU 1228 CA MET A 344 8396 15516 11237 1923 5084 1068 C ATOM 1229 C MET A 344 106.010 32.379 4.310 1.00 93.75 C ANISOU 1229 C MET A 344 8566 15609 11447 2266 4972 1035 C ATOM 1230 O MET A 344 106.829 31.772 4.996 1.00 96.00 O ANISOU 1230 O MET A 344 8511 15985 11980 2389 4931 1026 O ATOM 1231 CB MET A 344 106.546 34.054 2.527 1.00 94.64 C ANISOU 1231 CB MET A 344 8874 15792 11294 1903 5450 1016 C ATOM 1232 CG MET A 344 106.458 35.500 2.077 1.00100.37 C ANISOU 1232 CG MET A 344 9705 16536 11896 1572 5551 1071 C ATOM 1233 SD MET A 344 104.768 36.136 2.180 1.00 98.83 S ANISOU 1233 SD MET A 344 9929 16155 11468 1463 5274 1157 S ATOM 1234 CE MET A 344 104.032 35.296 0.770 1.00107.77 C ANISOU 1234 CE MET A 344 11566 17151 12231 1697 5413 1102 C ATOM 1235 N THR A 345 104.917 31.805 3.809 1.00 92.04 N ANISOU 1235 N THR A 345 8746 15226 10997 2417 4916 1017 N ATOM 1236 CA THR A 345 104.667 30.369 3.941 1.00 93.03 C ANISOU 1236 CA THR A 345 8947 15255 11147 2742 4845 972 C ATOM 1237 C THR A 345 103.965 29.798 2.713 1.00 93.45 C ANISOU 1237 C THR A 345 9455 15148 10904 2896 4991 883 C ATOM 1238 O THR A 345 103.066 30.426 2.156 1.00 93.46 O ANISOU 1238 O THR A 345 9787 15069 10654 2766 4965 895 O ATOM 1239 CB THR A 345 103.811 30.031 5.188 1.00 90.27 C ANISOU 1239 CB THR A 345 8572 14845 10880 2785 4468 1045 C ATOM 1240 OG1 THR A 345 103.603 28.614 5.249 1.00 89.46 O ANISOU 1240 OG1 THR A 345 8559 14630 10801 3100 4427 1002 O ATOM 1241 CG2 THR A 345 102.448 30.725 5.140 1.00 80.59 C ANISOU 1241 CG2 THR A 345 7670 13516 9434 2630 4297 1082 C ATOM 1242 N SER A 346 104.386 28.606 2.293 1.00100.88 N ANISOU 1242 N SER A 346 10417 16039 11876 3174 5138 787 N ATOM 1243 CA SER A 346 103.686 27.869 1.244 1.00103.40 C ANISOU 1243 CA SER A 346 11175 16183 11927 3348 5239 675 C ATOM 1244 C SER A 346 102.411 27.218 1.800 1.00101.13 C ANISOU 1244 C SER A 346 11125 15719 11581 3467 4940 684 C ATOM 1245 O SER A 346 101.536 26.796 1.041 1.00101.82 O ANISOU 1245 O SER A 346 11625 15644 11417 3553 4946 594 O ATOM 1246 CB SER A 346 104.602 26.811 0.629 1.00107.63 C ANISOU 1246 CB SER A 346 11646 16714 12535 3602 5507 548 C ATOM 1247 OG SER A 346 105.694 27.413 -0.049 1.00114.50 O ANISOU 1247 OG SER A 346 12341 17749 13414 3488 5815 520 O ATOM 1248 N ARG A 347 102.314 27.149 3.126 1.00 86.20 N ANISOU 1248 N ARG A 347 8971 13866 9914 3458 4675 786 N ATOM 1249 CA ARG A 347 101.174 26.533 3.803 1.00 91.24 C ANISOU 1249 CA ARG A 347 9777 14361 10528 3559 4390 807 C ATOM 1250 C ARG A 347 100.250 27.597 4.423 1.00 94.93 C ANISOU 1250 C ARG A 347 10282 14862 10924 3308 4142 906 C ATOM 1251 O ARG A 347 100.338 27.897 5.619 1.00 85.97 O ANISOU 1251 O ARG A 347 8860 13824 9979 3212 3931 1009 O ATOM 1252 CB ARG A 347 101.670 25.547 4.872 1.00 89.92 C ANISOU 1252 CB ARG A 347 9314 14201 10649 3752 4261 852 C ATOM 1253 CG ARG A 347 100.643 25.130 5.933 1.00 79.54 C ANISOU 1253 CG ARG A 347 8055 12797 9372 3790 3930 922 C ATOM 1254 CD ARG A 347 101.330 25.045 7.293 1.00 86.57 C ANISOU 1254 CD ARG A 347 8518 13823 10551 3778 3748 1047 C ATOM 1255 NE ARG A 347 100.485 24.570 8.396 1.00 82.43 N ANISOU 1255 NE ARG A 347 8011 13231 10079 3815 3440 1127 N ATOM 1256 CZ ARG A 347 99.793 23.432 8.389 1.00 81.51 C ANISOU 1256 CZ ARG A 347 8128 12912 9932 4034 3376 1085 C ATOM 1257 NH1 ARG A 347 99.804 22.643 7.318 1.00 84.28 N ANISOU 1257 NH1 ARG A 347 8736 13094 10191 4237 3590 947 N ATOM 1258 NH2 ARG A 347 99.075 23.091 9.450 1.00 73.59 N ANISOU 1258 NH2 ARG A 347 7111 11864 8984 4035 3101 1169 N ATOM 1259 N ILE A 348 99.373 28.167 3.594 1.00 94.82 N ANISOU 1259 N ILE A 348 10631 14768 10631 3200 4163 868 N ATOM 1260 CA ILE A 348 98.478 29.239 4.023 1.00 73.65 C ANISOU 1260 CA ILE A 348 8012 12105 7867 2965 3956 949 C ATOM 1261 C ILE A 348 97.333 28.674 4.831 1.00 74.15 C ANISOU 1261 C ILE A 348 8176 12067 7929 3050 3666 958 C ATOM 1262 O ILE A 348 96.619 27.794 4.349 1.00 76.16 O ANISOU 1262 O ILE A 348 8742 12158 8037 3229 3651 860 O ATOM 1263 CB ILE A 348 97.910 30.012 2.828 1.00 73.87 C ANISOU 1263 CB ILE A 348 8410 12070 7588 2836 4063 914 C ATOM 1264 CG1 ILE A 348 99.046 30.495 1.918 1.00 77.76 C ANISOU 1264 CG1 ILE A 348 8833 12658 8055 2757 4383 900 C ATOM 1265 CG2 ILE A 348 97.051 31.170 3.315 1.00 70.46 C ANISOU 1265 CG2 ILE A 348 8014 11654 7105 2596 3851 1004 C ATOM 1266 CD1 ILE A 348 98.584 31.281 0.710 1.00 78.53 C ANISOU 1266 CD1 ILE A 348 9296 12704 7839 2620 4496 886 C ATOM 1267 N VAL A 349 97.145 29.171 6.053 1.00 70.44 N ANISOU 1267 N VAL A 349 7455 11693 7618 2911 3436 1060 N ATOM 1268 CA VAL A 349 96.134 28.586 6.925 1.00 64.65 C ANISOU 1268 CA VAL A 349 6772 10887 6905 2989 3170 1073 C ATOM 1269 C VAL A 349 95.630 29.510 8.061 1.00 68.11 C ANISOU 1269 C VAL A 349 7024 11429 7424 2755 2916 1169 C ATOM 1270 O VAL A 349 96.337 30.392 8.560 1.00 64.75 O ANISOU 1270 O VAL A 349 6319 11148 7136 2559 2907 1236 O ATOM 1271 CB VAL A 349 96.675 27.255 7.514 1.00 73.34 C ANISOU 1271 CB VAL A 349 7706 11957 8202 3234 3148 1075 C ATOM 1272 CG1 VAL A 349 98.178 27.324 7.697 1.00 69.11 C ANISOU 1272 CG1 VAL A 349 6811 11567 7879 3231 3290 1120 C ATOM 1273 CG2 VAL A 349 95.971 26.898 8.818 1.00 73.27 C ANISOU 1273 CG2 VAL A 349 7592 11945 8301 3238 2851 1145 C ATOM 1274 N GLY A 350 94.379 29.282 8.452 1.00 67.86 N ANISOU 1274 N GLY A 350 7162 11316 7304 2775 2711 1154 N ATOM 1275 CA GLY A 350 93.662 30.111 9.400 1.00 55.48 C ANISOU 1275 CA GLY A 350 5486 9824 5769 2562 2475 1214 C ATOM 1276 C GLY A 350 92.185 29.935 9.098 1.00 57.82 C ANISOU 1276 C GLY A 350 6121 9990 5857 2607 2362 1144 C ATOM 1277 O GLY A 350 91.831 29.134 8.232 1.00 54.31 O ANISOU 1277 O GLY A 350 5981 9395 5257 2798 2451 1046 O ATOM 1278 N THR A 351 91.322 30.647 9.815 1.00 44.50 N ANISOU 1278 N THR A 351 3634 7969 5306 2068 1550 665 N ATOM 1279 CA THR A 351 89.898 30.651 9.487 1.00 43.86 C ANISOU 1279 CA THR A 351 3620 7884 5160 2073 1495 485 C ATOM 1280 C THR A 351 89.618 31.881 8.621 1.00 51.05 C ANISOU 1280 C THR A 351 4597 8998 5801 2037 1464 509 C ATOM 1281 O THR A 351 89.770 33.008 9.093 1.00 48.01 O ANISOU 1281 O THR A 351 4209 8655 5378 1901 1408 707 O ATOM 1282 CB THR A 351 89.032 30.665 10.756 1.00 49.04 C ANISOU 1282 CB THR A 351 4262 8402 5968 1957 1393 551 C ATOM 1283 OG1 THR A 351 89.380 29.545 11.576 1.00 48.11 O ANISOU 1283 OG1 THR A 351 4080 8099 6100 2001 1431 586 O ATOM 1284 CG2 THR A 351 87.570 30.604 10.425 1.00 41.41 C ANISOU 1284 CG2 THR A 351 3351 7418 4965 1969 1336 345 C ATOM 1285 N THR A 352 89.216 31.676 7.365 1.00 54.16 N ANISOU 1285 N THR A 352 5048 9517 6015 2157 1499 304 N ATOM 1286 CA THR A 352 89.252 32.774 6.387 1.00 59.00 C ANISOU 1286 CA THR A 352 5714 10349 6355 2160 1499 379 C ATOM 1287 C THR A 352 88.359 33.962 6.760 1.00 43.60 C ANISOU 1287 C THR A 352 3789 8435 4343 2031 1391 507 C ATOM 1288 O THR A 352 88.663 35.092 6.394 1.00 43.58 O ANISOU 1288 O THR A 352 3800 8539 4220 1985 1398 690 O ATOM 1289 CB THR A 352 88.886 32.309 4.929 1.00 55.82 C ANISOU 1289 CB THR A 352 5371 10118 5720 2319 1535 118 C ATOM 1290 OG1 THR A 352 87.618 31.634 4.902 1.00 57.17 O ANISOU 1290 OG1 THR A 352 5568 10240 5914 2354 1456 -165 O ATOM 1291 CG2 THR A 352 89.973 31.413 4.347 1.00 50.31 C ANISOU 1291 CG2 THR A 352 4644 9416 5053 2434 1669 20 C ATOM 1292 N ALA A 353 87.284 33.728 7.500 1.00 42.12 N ANISOU 1292 N ALA A 353 3598 8135 4269 1970 1301 418 N ATOM 1293 CA ALA A 353 86.431 34.844 7.900 1.00 40.34 C ANISOU 1293 CA ALA A 353 3383 7927 4016 1838 1208 533 C ATOM 1294 C ALA A 353 87.152 35.762 8.874 1.00 38.88 C ANISOU 1294 C ALA A 353 3158 7657 3958 1663 1198 796 C ATOM 1295 O ALA A 353 86.749 36.896 9.067 1.00 42.62 O ANISOU 1295 O ALA A 353 3637 8139 4417 1543 1150 917 O ATOM 1296 CB ALA A 353 85.123 34.346 8.516 1.00 40.43 C ANISOU 1296 CB ALA A 353 3421 7781 4158 1777 1093 361 C ATOM 1297 N TYR A 354 88.220 35.273 9.485 1.00 39.07 N ANISOU 1297 N TYR A 354 3135 7594 4116 1650 1240 863 N ATOM 1298 CA TYR A 354 88.973 36.063 10.451 1.00 41.14 C ANISOU 1298 CA TYR A 354 3352 7791 4490 1489 1213 1055 C ATOM 1299 C TYR A 354 90.345 36.558 9.947 1.00 47.10 C ANISOU 1299 C TYR A 354 4079 8616 5202 1514 1295 1177 C ATOM 1300 O TYR A 354 91.033 37.316 10.641 1.00 38.78 O ANISOU 1300 O TYR A 354 2979 7517 4238 1387 1274 1300 O ATOM 1301 CB TYR A 354 89.196 35.242 11.716 1.00 37.40 C ANISOU 1301 CB TYR A 354 2826 7185 4198 1443 1177 1062 C ATOM 1302 CG TYR A 354 87.983 34.992 12.555 1.00 35.94 C ANISOU 1302 CG TYR A 354 2652 6896 4108 1365 1091 998 C ATOM 1303 CD1 TYR A 354 87.634 35.856 13.575 1.00 34.33 C ANISOU 1303 CD1 TYR A 354 2442 6641 3961 1173 1003 1080 C ATOM 1304 CD2 TYR A 354 87.210 33.868 12.360 1.00 36.84 C ANISOU 1304 CD2 TYR A 354 2775 6945 4278 1481 1105 835 C ATOM 1305 CE1 TYR A 354 86.537 35.615 14.359 1.00 33.13 C ANISOU 1305 CE1 TYR A 354 2297 6393 3898 1096 932 1025 C ATOM 1306 CE2 TYR A 354 86.113 33.615 13.134 1.00 35.21 C ANISOU 1306 CE2 TYR A 354 2568 6625 4187 1413 1035 781 C ATOM 1307 CZ TYR A 354 85.776 34.489 14.130 1.00 33.55 C ANISOU 1307 CZ TYR A 354 2354 6383 4012 1218 951 890 C ATOM 1308 OH TYR A 354 84.665 34.226 14.895 1.00 32.51 O ANISOU 1308 OH TYR A 354 2220 6138 3996 1146 890 837 O ATOM 1309 N MET A 355 90.757 36.112 8.763 1.00 41.20 N ANISOU 1309 N MET A 355 3353 7976 4326 1677 1390 1118 N ATOM 1310 CA MET A 355 92.138 36.311 8.351 1.00 42.65 C ANISOU 1310 CA MET A 355 3496 8206 4503 1716 1484 1217 C ATOM 1311 C MET A 355 92.397 37.661 7.694 1.00 53.06 C ANISOU 1311 C MET A 355 4826 9601 5735 1676 1518 1358 C ATOM 1312 O MET A 355 91.597 38.148 6.887 1.00 43.43 O ANISOU 1312 O MET A 355 3665 8473 4364 1719 1513 1355 O ATOM 1313 CB MET A 355 92.570 35.195 7.410 1.00 47.67 C ANISOU 1313 CB MET A 355 4142 8910 5062 1903 1587 1083 C ATOM 1314 CG MET A 355 92.552 33.829 8.052 1.00 46.41 C ANISOU 1314 CG MET A 355 3946 8630 5060 1956 1587 960 C ATOM 1315 SD MET A 355 93.016 32.565 6.872 1.00 48.20 S ANISOU 1315 SD MET A 355 4178 8904 5232 2167 1725 753 S ATOM 1316 CE MET A 355 94.746 32.946 6.573 1.00 49.05 C ANISOU 1316 CE MET A 355 4217 9070 5352 2180 1835 921 C ATOM 1317 N ALA A 356 93.528 38.259 8.053 1.00 43.41 N ANISOU 1317 N ALA A 356 3535 8336 4621 1601 1554 1481 N ATOM 1318 CA ALA A 356 93.936 39.525 7.466 1.00 44.20 C ANISOU 1318 CA ALA A 356 3626 8469 4700 1566 1614 1617 C ATOM 1319 C ALA A 356 94.306 39.321 6.005 1.00 60.58 C ANISOU 1319 C ALA A 356 5735 10694 6590 1743 1733 1627 C ATOM 1320 O ALA A 356 94.547 38.189 5.566 1.00 47.64 O ANISOU 1320 O ALA A 356 4110 9118 4873 1873 1780 1509 O ATOM 1321 CB ALA A 356 95.099 40.118 8.229 1.00 44.22 C ANISOU 1321 CB ALA A 356 3532 8385 4883 1447 1632 1698 C ATOM 1322 N PRO A 357 94.341 40.416 5.234 1.00 58.93 N ANISOU 1322 N PRO A 357 5535 10540 6315 1752 1792 1763 N ATOM 1323 CA PRO A 357 94.669 40.199 3.824 1.00 57.83 C ANISOU 1323 CA PRO A 357 5431 10572 5969 1930 1904 1776 C ATOM 1324 C PRO A 357 96.110 39.697 3.635 1.00 57.05 C ANISOU 1324 C PRO A 357 5273 10478 5925 1983 2022 1774 C ATOM 1325 O PRO A 357 96.307 38.799 2.817 1.00 56.00 O ANISOU 1325 O PRO A 357 5172 10464 5643 2131 2089 1666 O ATOM 1326 CB PRO A 357 94.439 41.574 3.186 1.00 50.95 C ANISOU 1326 CB PRO A 357 4564 9738 5056 1923 1946 1968 C ATOM 1327 CG PRO A 357 94.396 42.537 4.307 1.00 49.10 C ANISOU 1327 CG PRO A 357 4275 9312 5070 1725 1891 2045 C ATOM 1328 CD PRO A 357 93.944 41.807 5.518 1.00 46.77 C ANISOU 1328 CD PRO A 357 3980 8918 4874 1624 1765 1896 C ATOM 1329 N GLU A 358 97.086 40.213 4.378 1.00 51.33 N ANISOU 1329 N GLU A 358 4458 9633 5412 1866 2046 1861 N ATOM 1330 CA GLU A 358 98.456 39.721 4.203 1.00 52.96 C ANISOU 1330 CA GLU A 358 4593 9851 5677 1920 2158 1857 C ATOM 1331 C GLU A 358 98.578 38.254 4.636 1.00 57.51 C ANISOU 1331 C GLU A 358 5160 10413 6279 1981 2128 1697 C ATOM 1332 O GLU A 358 99.372 37.498 4.073 1.00 54.50 O ANISOU 1332 O GLU A 358 4753 10084 5868 2094 2234 1642 O ATOM 1333 CB GLU A 358 99.464 40.590 4.962 1.00 52.80 C ANISOU 1333 CB GLU A 358 4462 9717 5884 1777 2180 1956 C ATOM 1334 CG GLU A 358 99.440 40.436 6.477 1.00 59.80 C ANISOU 1334 CG GLU A 358 5288 10483 6950 1630 2049 1897 C ATOM 1335 CD GLU A 358 98.272 41.167 7.101 1.00 59.65 C ANISOU 1335 CD GLU A 358 5314 10391 6960 1502 1929 1898 C ATOM 1336 OE1 GLU A 358 97.533 41.842 6.342 1.00 61.12 O ANISOU 1336 OE1 GLU A 358 5566 10610 7045 1530 1952 1963 O ATOM 1337 OE2 GLU A 358 98.096 41.069 8.334 1.00 47.04 O1+ ANISOU 1337 OE2 GLU A 358 3681 8713 5481 1381 1815 1840 O1+ ATOM 1338 N ALA A 359 97.784 37.846 5.621 1.00 50.59 N ANISOU 1338 N ALA A 359 4297 9454 5470 1910 1996 1624 N ATOM 1339 CA ALA A 359 97.766 36.447 6.025 1.00 50.50 C ANISOU 1339 CA ALA A 359 4274 9406 5507 1980 1977 1485 C ATOM 1340 C ALA A 359 97.186 35.560 4.929 1.00 51.88 C ANISOU 1340 C ALA A 359 4528 9680 5502 2144 2035 1320 C ATOM 1341 O ALA A 359 97.685 34.464 4.680 1.00 65.90 O ANISOU 1341 O ALA A 359 6276 11450 7312 2252 2112 1201 O ATOM 1342 CB ALA A 359 96.981 36.270 7.313 1.00 48.17 C ANISOU 1342 CB ALA A 359 3975 9001 5325 1869 1831 1461 C ATOM 1343 N LEU A 360 96.136 36.045 4.273 1.00 61.11 N ANISOU 1343 N LEU A 360 5786 10943 6488 2164 1999 1298 N ATOM 1344 CA LEU A 360 95.472 35.306 3.206 1.00 53.23 C ANISOU 1344 CA LEU A 360 4865 10076 5284 2314 2031 1105 C ATOM 1345 C LEU A 360 96.462 35.035 2.086 1.00 57.83 C ANISOU 1345 C LEU A 360 5437 10778 5757 2441 2186 1079 C ATOM 1346 O LEU A 360 96.408 34.000 1.419 1.00 57.83 O ANISOU 1346 O LEU A 360 5459 10841 5673 2564 2247 862 O ATOM 1347 CB LEU A 360 94.262 36.085 2.675 1.00 52.83 C ANISOU 1347 CB LEU A 360 4896 10142 5035 2313 1954 1125 C ATOM 1348 CG LEU A 360 93.004 36.214 3.540 1.00 50.83 C ANISOU 1348 CG LEU A 360 4668 9802 4843 2215 1808 1089 C ATOM 1349 CD1 LEU A 360 92.027 37.213 2.951 1.00 50.30 C ANISOU 1349 CD1 LEU A 360 4658 9859 4597 2215 1750 1167 C ATOM 1350 CD2 LEU A 360 92.333 34.864 3.684 1.00 54.65 C ANISOU 1350 CD2 LEU A 360 5173 10247 5346 2286 1775 818 C ATOM 1351 N ARG A 361 97.370 35.982 1.888 1.00 56.76 N ANISOU 1351 N ARG A 361 5260 10663 5643 2403 2257 1283 N ATOM 1352 CA ARG A 361 98.379 35.863 0.850 1.00 59.57 C ANISOU 1352 CA ARG A 361 5596 11131 5905 2511 2417 1290 C ATOM 1353 C ARG A 361 99.535 34.994 1.326 1.00 72.24 C ANISOU 1353 C ARG A 361 7106 12627 7716 2522 2497 1235 C ATOM 1354 O ARG A 361 100.350 34.545 0.518 1.00 75.07 O ANISOU 1354 O ARG A 361 7440 13060 8022 2624 2639 1175 O ATOM 1355 CB ARG A 361 98.887 37.239 0.431 1.00 60.31 C ANISOU 1355 CB ARG A 361 5673 11273 5970 2473 2478 1535 C ATOM 1356 CG ARG A 361 97.892 38.067 -0.328 1.00 60.71 C ANISOU 1356 CG ARG A 361 5804 11462 5801 2510 2437 1615 C ATOM 1357 CD ARG A 361 98.368 39.494 -0.363 1.00 60.96 C ANISOU 1357 CD ARG A 361 5790 11452 5919 2438 2490 1881 C ATOM 1358 NE ARG A 361 97.264 40.433 -0.520 1.00 70.48 N ANISOU 1358 NE ARG A 361 7044 12696 7039 2417 2408 1996 N ATOM 1359 CZ ARG A 361 96.393 40.387 -1.527 1.00 76.29 C ANISOU 1359 CZ ARG A 361 7855 13637 7496 2548 2387 1966 C ATOM 1360 NH1 ARG A 361 96.490 39.432 -2.454 1.00 63.89 N1+ ANISOU 1360 NH1 ARG A 361 6327 12250 5697 2697 2439 1793 N1+ ATOM 1361 NH2 ARG A 361 95.418 41.289 -1.603 1.00 61.13 N ANISOU 1361 NH2 ARG A 361 5957 11741 5528 2531 2312 2093 N ATOM 1362 N GLY A 362 99.619 34.763 2.635 1.00 58.10 N ANISOU 1362 N GLY A 362 5252 10670 6155 2421 2406 1261 N ATOM 1363 CA GLY A 362 100.598 33.821 3.154 1.00 58.76 C ANISOU 1363 CA GLY A 362 5233 10654 6439 2450 2462 1213 C ATOM 1364 C GLY A 362 101.687 34.369 4.063 1.00 64.60 C ANISOU 1364 C GLY A 362 5856 11310 7380 2344 2450 1387 C ATOM 1365 O GLY A 362 102.563 33.628 4.499 1.00 58.98 O ANISOU 1365 O GLY A 362 5045 10534 6832 2376 2489 1370 O ATOM 1366 N GLU A 363 101.639 35.660 4.365 1.00 67.33 N ANISOU 1366 N GLU A 363 6200 11653 7729 2218 2395 1541 N ATOM 1367 CA GLU A 363 102.616 36.248 5.270 1.00 56.72 C ANISOU 1367 CA GLU A 363 4736 10238 6578 2102 2373 1662 C ATOM 1368 C GLU A 363 102.342 35.814 6.701 1.00 63.69 C ANISOU 1368 C GLU A 363 5572 11022 7606 2019 2223 1648 C ATOM 1369 O GLU A 363 101.201 35.492 7.063 1.00 59.14 O ANISOU 1369 O GLU A 363 5071 10413 6985 2004 2122 1587 O ATOM 1370 CB GLU A 363 102.612 37.774 5.170 1.00 56.38 C ANISOU 1370 CB GLU A 363 4694 10197 6530 1987 2374 1794 C ATOM 1371 CG GLU A 363 103.395 38.455 6.280 1.00 64.20 C ANISOU 1371 CG GLU A 363 5558 11105 7730 1836 2323 1862 C ATOM 1372 CD GLU A 363 103.557 39.949 6.057 1.00 70.85 C ANISOU 1372 CD GLU A 363 6379 11925 8614 1730 2370 1964 C ATOM 1373 OE1 GLU A 363 102.978 40.471 5.069 1.00 68.67 O ANISOU 1373 OE1 GLU A 363 6196 11699 8198 1781 2431 2020 O ATOM 1374 OE2 GLU A 363 104.268 40.594 6.870 1.00 73.51 O1+ ANISOU 1374 OE2 GLU A 363 6599 12201 9131 1601 2351 1981 O1+ ATOM 1375 N ILE A 364 103.398 35.800 7.508 1.00 67.20 N ANISOU 1375 N ILE A 364 5885 11431 8217 1969 2211 1705 N ATOM 1376 CA ILE A 364 103.297 35.409 8.909 1.00 67.15 C ANISOU 1376 CA ILE A 364 5816 11365 8331 1900 2071 1718 C ATOM 1377 C ILE A 364 103.820 36.506 9.833 1.00 65.97 C ANISOU 1377 C ILE A 364 5571 11212 8282 1734 1997 1791 C ATOM 1378 O ILE A 364 105.037 36.694 9.946 1.00 67.91 O ANISOU 1378 O ILE A 364 5690 11483 8632 1726 2053 1826 O ATOM 1379 CB ILE A 364 104.070 34.112 9.175 1.00 65.38 C ANISOU 1379 CB ILE A 364 5501 11120 8221 2020 2109 1701 C ATOM 1380 CG1 ILE A 364 103.632 33.030 8.180 1.00 65.67 C ANISOU 1380 CG1 ILE A 364 5617 11143 8193 2182 2211 1577 C ATOM 1381 CG2 ILE A 364 103.865 33.659 10.609 1.00 54.16 C ANISOU 1381 CG2 ILE A 364 4024 9655 6899 1968 1963 1745 C ATOM 1382 CD1 ILE A 364 103.809 31.608 8.686 1.00 63.63 C ANISOU 1382 CD1 ILE A 364 5296 10801 8080 2288 2213 1536 C ATOM 1383 N THR A 365 102.898 37.215 10.485 1.00 51.32 N ANISOU 1383 N THR A 365 3767 9325 6406 1600 1878 1787 N ATOM 1384 CA THR A 365 103.228 38.375 11.302 1.00 50.84 C ANISOU 1384 CA THR A 365 3624 9253 6442 1427 1818 1804 C ATOM 1385 C THR A 365 102.207 38.627 12.400 1.00 65.95 C ANISOU 1385 C THR A 365 5577 11130 8352 1302 1660 1770 C ATOM 1386 O THR A 365 101.008 38.384 12.209 1.00 64.16 O ANISOU 1386 O THR A 365 5473 10872 8031 1320 1617 1747 O ATOM 1387 CB THR A 365 103.311 39.645 10.457 1.00 63.69 C ANISOU 1387 CB THR A 365 5272 10863 8066 1367 1918 1826 C ATOM 1388 OG1 THR A 365 103.078 40.782 11.296 1.00 66.25 O ANISOU 1388 OG1 THR A 365 5554 11135 8483 1182 1843 1796 O ATOM 1389 CG2 THR A 365 102.243 39.629 9.364 1.00 60.61 C ANISOU 1389 CG2 THR A 365 5039 10477 7513 1449 1959 1837 C ATOM 1390 N PRO A 366 102.667 39.145 13.551 1.00 68.22 N ANISOU 1390 N PRO A 366 5751 11431 8738 1171 1578 1751 N ATOM 1391 CA PRO A 366 101.754 39.455 14.664 1.00 47.86 C ANISOU 1391 CA PRO A 366 3202 8831 6152 1041 1436 1704 C ATOM 1392 C PRO A 366 100.654 40.439 14.279 1.00 45.47 C ANISOU 1392 C PRO A 366 3011 8446 5820 943 1435 1663 C ATOM 1393 O PRO A 366 99.615 40.464 14.927 1.00 52.90 O ANISOU 1393 O PRO A 366 4019 9354 6729 872 1333 1624 O ATOM 1394 CB PRO A 366 102.676 40.064 15.730 1.00 47.77 C ANISOU 1394 CB PRO A 366 3025 8871 6254 919 1388 1661 C ATOM 1395 CG PRO A 366 103.950 40.430 15.000 1.00 49.75 C ANISOU 1395 CG PRO A 366 3170 9139 6596 953 1522 1673 C ATOM 1396 CD PRO A 366 104.071 39.441 13.879 1.00 50.42 C ANISOU 1396 CD PRO A 366 3326 9227 6604 1142 1618 1753 C ATOM 1397 N LYS A 367 100.870 41.232 13.236 1.00 54.21 N ANISOU 1397 N LYS A 367 4136 9522 6942 947 1555 1683 N ATOM 1398 CA LYS A 367 99.853 42.184 12.807 1.00 49.60 C ANISOU 1398 CA LYS A 367 3647 8862 6338 872 1564 1673 C ATOM 1399 C LYS A 367 98.549 41.482 12.379 1.00 53.61 C ANISOU 1399 C LYS A 367 4301 9370 6699 960 1515 1685 C ATOM 1400 O LYS A 367 97.465 42.067 12.486 1.00 57.12 O ANISOU 1400 O LYS A 367 4818 9755 7131 880 1464 1660 O ATOM 1401 CB LYS A 367 100.403 43.068 11.674 1.00 59.32 C ANISOU 1401 CB LYS A 367 4862 10077 7602 894 1719 1736 C ATOM 1402 CG LYS A 367 101.664 43.859 12.075 1.00 58.86 C ANISOU 1402 CG LYS A 367 4641 10003 7720 791 1786 1697 C ATOM 1403 CD LYS A 367 102.348 44.518 10.887 1.00 64.13 C ANISOU 1403 CD LYS A 367 5284 10664 8419 843 1962 1784 C ATOM 1404 CE LYS A 367 103.685 45.164 11.283 1.00 67.85 C ANISOU 1404 CE LYS A 367 5572 11127 9081 747 2038 1725 C ATOM 1405 NZ LYS A 367 104.689 45.159 10.152 1.00 67.19 N1+ ANISOU 1405 NZ LYS A 367 5447 11082 9000 860 2210 1826 N1+ ATOM 1406 N SER A 368 98.639 40.234 11.918 1.00 50.14 N ANISOU 1406 N SER A 368 3894 8991 6167 1122 1537 1703 N ATOM 1407 CA SER A 368 97.441 39.510 11.464 1.00 55.24 C ANISOU 1407 CA SER A 368 4660 9642 6688 1213 1507 1674 C ATOM 1408 C SER A 368 96.552 39.069 12.629 1.00 46.16 C ANISOU 1408 C SER A 368 3532 8446 5562 1138 1370 1621 C ATOM 1409 O SER A 368 95.320 39.145 12.542 1.00 47.34 O ANISOU 1409 O SER A 368 3769 8562 5657 1115 1321 1583 O ATOM 1410 CB SER A 368 97.820 38.294 10.621 1.00 54.46 C ANISOU 1410 CB SER A 368 4576 9604 6511 1406 1594 1662 C ATOM 1411 OG SER A 368 98.489 38.684 9.437 1.00 57.00 O ANISOU 1411 OG SER A 368 4897 9984 6778 1485 1728 1707 O ATOM 1412 N ASP A 369 97.175 38.603 13.709 1.00 45.87 N ANISOU 1412 N ASP A 369 3409 8419 5602 1106 1312 1628 N ATOM 1413 CA ASP A 369 96.443 38.331 14.940 1.00 40.46 C ANISOU 1413 CA ASP A 369 2731 7705 4937 1022 1187 1600 C ATOM 1414 C ASP A 369 95.599 39.538 15.343 1.00 39.03 C ANISOU 1414 C ASP A 369 2591 7463 4776 848 1125 1546 C ATOM 1415 O ASP A 369 94.418 39.386 15.640 1.00 53.81 O ANISOU 1415 O ASP A 369 4538 9288 6620 811 1059 1507 O ATOM 1416 CB ASP A 369 97.401 37.945 16.069 1.00 41.25 C ANISOU 1416 CB ASP A 369 2712 7864 5098 1003 1135 1640 C ATOM 1417 CG ASP A 369 97.920 36.531 15.929 1.00 49.24 C ANISOU 1417 CG ASP A 369 3691 8904 6116 1178 1178 1700 C ATOM 1418 OD1 ASP A 369 97.519 35.847 14.970 1.00 54.36 O ANISOU 1418 OD1 ASP A 369 4410 9512 6732 1306 1252 1676 O ATOM 1419 OD2 ASP A 369 98.706 36.085 16.782 1.00 47.60 O1+ ANISOU 1419 OD2 ASP A 369 3378 8756 5951 1195 1141 1763 O1+ ATOM 1420 N ILE A 370 96.181 40.734 15.331 1.00 39.52 N ANISOU 1420 N ILE A 370 2596 7508 4910 742 1160 1532 N ATOM 1421 CA ILE A 370 95.417 41.946 15.638 1.00 38.46 C ANISOU 1421 CA ILE A 370 2494 7286 4835 581 1129 1464 C ATOM 1422 C ILE A 370 94.131 42.047 14.787 1.00 49.93 C ANISOU 1422 C ILE A 370 4069 8688 6213 618 1138 1475 C ATOM 1423 O ILE A 370 93.048 42.325 15.305 1.00 48.13 O ANISOU 1423 O ILE A 370 3894 8394 5998 524 1064 1417 O ATOM 1424 CB ILE A 370 96.270 43.226 15.428 1.00 39.62 C ANISOU 1424 CB ILE A 370 2555 7396 5102 489 1216 1442 C ATOM 1425 CG1 ILE A 370 97.512 43.194 16.315 1.00 40.77 C ANISOU 1425 CG1 ILE A 370 2556 7605 5330 442 1203 1402 C ATOM 1426 CG2 ILE A 370 95.454 44.477 15.705 1.00 38.77 C ANISOU 1426 CG2 ILE A 370 2473 7169 5088 331 1209 1358 C ATOM 1427 CD1 ILE A 370 97.246 42.804 17.731 1.00 40.16 C ANISOU 1427 CD1 ILE A 370 2449 7570 5242 371 1073 1340 C ATOM 1428 N TYR A 371 94.261 41.805 13.486 1.00 38.40 N ANISOU 1428 N TYR A 371 2646 7276 4668 762 1229 1545 N ATOM 1429 CA TYR A 371 93.129 41.814 12.570 1.00 37.94 C ANISOU 1429 CA TYR A 371 2687 7222 4508 830 1241 1561 C ATOM 1430 C TYR A 371 92.053 40.835 13.007 1.00 45.82 C ANISOU 1430 C TYR A 371 3743 8214 5452 855 1152 1493 C ATOM 1431 O TYR A 371 90.882 41.198 13.153 1.00 40.16 O ANISOU 1431 O TYR A 371 3079 7444 4735 786 1097 1455 O ATOM 1432 CB TYR A 371 93.596 41.465 11.159 1.00 53.94 C ANISOU 1432 CB TYR A 371 4734 9348 6413 1011 1356 1628 C ATOM 1433 CG TYR A 371 92.569 41.682 10.083 1.00 39.73 C ANISOU 1433 CG TYR A 371 3018 7599 4479 1095 1379 1654 C ATOM 1434 CD1 TYR A 371 92.478 42.910 9.432 1.00 45.89 C ANISOU 1434 CD1 TYR A 371 3801 8368 5268 1070 1440 1754 C ATOM 1435 CD2 TYR A 371 91.709 40.664 9.700 1.00 39.47 C ANISOU 1435 CD2 TYR A 371 3050 7634 4314 1211 1349 1576 C ATOM 1436 CE1 TYR A 371 91.547 43.136 8.443 1.00 40.85 C ANISOU 1436 CE1 TYR A 371 3225 7807 4487 1166 1456 1804 C ATOM 1437 CE2 TYR A 371 90.762 40.874 8.703 1.00 48.03 C ANISOU 1437 CE2 TYR A 371 4198 8804 5246 1299 1362 1582 C ATOM 1438 CZ TYR A 371 90.689 42.119 8.075 1.00 50.67 C ANISOU 1438 CZ TYR A 371 4532 9151 5568 1281 1410 1712 C ATOM 1439 OH TYR A 371 89.764 42.361 7.078 1.00 50.66 O ANISOU 1439 OH TYR A 371 4584 9267 5399 1385 1416 1747 O ATOM 1440 N SER A 372 92.442 39.584 13.207 1.00 37.06 N ANISOU 1440 N SER A 372 2615 7145 4319 957 1151 1476 N ATOM 1441 CA SER A 372 91.481 38.601 13.640 1.00 36.13 C ANISOU 1441 CA SER A 372 2538 7000 4189 988 1089 1410 C ATOM 1442 C SER A 372 90.798 39.060 14.926 1.00 40.92 C ANISOU 1442 C SER A 372 3145 7527 4876 812 980 1379 C ATOM 1443 O SER A 372 89.582 38.916 15.085 1.00 39.79 O ANISOU 1443 O SER A 372 3055 7335 4729 780 930 1322 O ATOM 1444 CB SER A 372 92.156 37.254 13.834 1.00 38.81 C ANISOU 1444 CB SER A 372 2835 7362 4550 1116 1118 1413 C ATOM 1445 OG SER A 372 92.610 36.778 12.584 1.00 39.10 O ANISOU 1445 OG SER A 372 2884 7461 4510 1282 1227 1398 O ATOM 1446 N PHE A 373 91.569 39.649 15.831 1.00 40.66 N ANISOU 1446 N PHE A 373 3046 7488 4914 697 947 1397 N ATOM 1447 CA PHE A 373 90.983 40.084 17.090 1.00 41.42 C ANISOU 1447 CA PHE A 373 3143 7528 5068 535 851 1341 C ATOM 1448 C PHE A 373 89.931 41.172 16.869 1.00 46.04 C ANISOU 1448 C PHE A 373 3790 8020 5685 421 839 1281 C ATOM 1449 O PHE A 373 88.938 41.269 17.620 1.00 37.50 O ANISOU 1449 O PHE A 373 2746 6870 4634 321 768 1214 O ATOM 1450 CB PHE A 373 92.063 40.576 18.039 1.00 40.44 C ANISOU 1450 CB PHE A 373 2923 7445 4999 444 829 1337 C ATOM 1451 CG PHE A 373 91.550 40.906 19.403 1.00 38.09 C ANISOU 1451 CG PHE A 373 2618 7123 4732 297 736 1263 C ATOM 1452 CD1 PHE A 373 91.025 39.914 20.211 1.00 32.91 C ANISOU 1452 CD1 PHE A 373 1977 6497 4031 323 670 1289 C ATOM 1453 CD2 PHE A 373 91.579 42.210 19.872 1.00 33.29 C ANISOU 1453 CD2 PHE A 373 1983 6456 4210 138 734 1160 C ATOM 1454 CE1 PHE A 373 90.557 40.213 21.474 1.00 32.39 C ANISOU 1454 CE1 PHE A 373 1906 6433 3968 196 592 1229 C ATOM 1455 CE2 PHE A 373 91.103 42.515 21.130 1.00 32.68 C ANISOU 1455 CE2 PHE A 373 1899 6363 4154 12 660 1069 C ATOM 1456 CZ PHE A 373 90.591 41.514 21.932 1.00 32.26 C ANISOU 1456 CZ PHE A 373 1868 6371 4018 41 585 1110 C ATOM 1457 N GLY A 374 90.141 41.976 15.834 1.00 33.00 N ANISOU 1457 N GLY A 374 2143 6363 4032 444 916 1316 N ATOM 1458 CA GLY A 374 89.148 42.958 15.429 1.00 33.10 C ANISOU 1458 CA GLY A 374 2206 6295 4077 372 921 1297 C ATOM 1459 C GLY A 374 87.802 42.340 15.113 1.00 31.41 C ANISOU 1459 C GLY A 374 2063 6080 3793 424 878 1275 C ATOM 1460 O GLY A 374 86.775 42.890 15.465 1.00 42.74 O ANISOU 1460 O GLY A 374 3530 7425 5285 318 832 1222 O ATOM 1461 N VAL A 375 87.810 41.194 14.446 1.00 31.95 N ANISOU 1461 N VAL A 375 2145 6243 3752 590 902 1293 N ATOM 1462 CA VAL A 375 86.586 40.491 14.087 1.00 31.42 C ANISOU 1462 CA VAL A 375 2122 6189 3625 660 875 1233 C ATOM 1463 C VAL A 375 85.951 39.951 15.371 1.00 30.17 C ANISOU 1463 C VAL A 375 1966 5940 3557 558 790 1159 C ATOM 1464 O VAL A 375 84.721 39.963 15.529 1.00 30.30 O ANISOU 1464 O VAL A 375 2012 5898 3603 506 742 1093 O ATOM 1465 CB VAL A 375 86.867 39.342 13.062 1.00 32.72 C ANISOU 1465 CB VAL A 375 2293 6472 3667 879 942 1213 C ATOM 1466 CG1 VAL A 375 85.618 38.564 12.744 1.00 32.43 C ANISOU 1466 CG1 VAL A 375 2284 6448 3589 960 915 1091 C ATOM 1467 CG2 VAL A 375 87.476 39.889 11.788 1.00 34.18 C ANISOU 1467 CG2 VAL A 375 2486 6767 3735 983 1030 1291 C ATOM 1468 N VAL A 376 86.783 39.511 16.308 1.00 30.34 N ANISOU 1468 N VAL A 376 1950 5958 3621 532 772 1180 N ATOM 1469 CA VAL A 376 86.263 39.028 17.578 1.00 29.50 C ANISOU 1469 CA VAL A 376 1842 5788 3578 447 700 1143 C ATOM 1470 C VAL A 376 85.543 40.148 18.362 1.00 47.76 C ANISOU 1470 C VAL A 376 4185 8006 5956 251 638 1077 C ATOM 1471 O VAL A 376 84.508 39.913 19.008 1.00 41.30 O ANISOU 1471 O VAL A 376 3397 7113 5181 181 588 1018 O ATOM 1472 CB VAL A 376 87.366 38.433 18.447 1.00 30.28 C ANISOU 1472 CB VAL A 376 1880 5944 3682 472 692 1209 C ATOM 1473 CG1 VAL A 376 86.821 38.103 19.817 1.00 29.66 C ANISOU 1473 CG1 VAL A 376 1798 5829 3641 380 620 1197 C ATOM 1474 CG2 VAL A 376 87.977 37.189 17.785 1.00 31.53 C ANISOU 1474 CG2 VAL A 376 2009 6153 3819 672 762 1260 C ATOM 1475 N LEU A 377 86.074 41.367 18.289 1.00 28.53 N ANISOU 1475 N LEU A 377 1737 5552 3550 168 658 1072 N ATOM 1476 CA LEU A 377 85.428 42.494 18.941 1.00 27.70 C ANISOU 1476 CA LEU A 377 1657 5329 3539 -2 627 978 C ATOM 1477 C LEU A 377 84.075 42.768 18.289 1.00 44.07 C ANISOU 1477 C LEU A 377 3787 7325 5634 -13 622 951 C ATOM 1478 O LEU A 377 83.066 43.001 18.977 1.00 35.15 O ANISOU 1478 O LEU A 377 2695 6087 4573 -121 575 861 O ATOM 1479 CB LEU A 377 86.311 43.739 18.876 1.00 28.45 C ANISOU 1479 CB LEU A 377 1705 5398 3706 -70 682 961 C ATOM 1480 CG LEU A 377 87.702 43.630 19.526 1.00 35.60 C ANISOU 1480 CG LEU A 377 2527 6390 4608 -72 688 970 C ATOM 1481 CD1 LEU A 377 88.459 44.897 19.216 1.00 41.52 C ANISOU 1481 CD1 LEU A 377 3219 7093 5465 -135 770 936 C ATOM 1482 CD2 LEU A 377 87.615 43.413 21.028 1.00 29.20 C ANISOU 1482 CD2 LEU A 377 1698 5594 3804 -162 615 895 C ATOM 1483 N LEU A 378 84.041 42.729 16.963 1.00 27.51 N ANISOU 1483 N LEU A 378 1688 5297 3469 109 672 1029 N ATOM 1484 CA LEU A 378 82.792 42.921 16.285 1.00 27.10 C ANISOU 1484 CA LEU A 378 1663 5220 3412 123 660 1020 C ATOM 1485 C LEU A 378 81.776 41.873 16.753 1.00 33.52 C ANISOU 1485 C LEU A 378 2493 6007 4235 125 598 937 C ATOM 1486 O LEU A 378 80.588 42.185 16.903 1.00 32.33 O ANISOU 1486 O LEU A 378 2363 5768 4154 44 555 873 O ATOM 1487 CB LEU A 378 82.979 42.861 14.783 1.00 28.29 C ANISOU 1487 CB LEU A 378 1799 5512 3436 296 726 1121 C ATOM 1488 CG LEU A 378 83.717 44.029 14.122 1.00 29.33 C ANISOU 1488 CG LEU A 378 1913 5653 3577 301 804 1231 C ATOM 1489 CD1 LEU A 378 83.668 43.909 12.599 1.00 30.70 C ANISOU 1489 CD1 LEU A 378 2085 5997 3584 495 867 1342 C ATOM 1490 CD2 LEU A 378 83.203 45.387 14.594 1.00 28.83 C ANISOU 1490 CD2 LEU A 378 1852 5425 3676 137 800 1206 C ATOM 1491 N GLU A 379 82.216 40.644 17.011 1.00 26.58 N ANISOU 1491 N GLU A 379 1595 5187 3317 215 599 937 N ATOM 1492 CA GLU A 379 81.250 39.632 17.457 1.00 34.00 C ANISOU 1492 CA GLU A 379 2534 6076 4310 223 559 860 C ATOM 1493 C GLU A 379 80.698 40.028 18.821 1.00 30.02 C ANISOU 1493 C GLU A 379 2063 5437 3905 36 501 806 C ATOM 1494 O GLU A 379 79.496 39.930 19.061 1.00 34.05 O ANISOU 1494 O GLU A 379 2591 5852 4494 -29 463 728 O ATOM 1495 CB GLU A 379 81.874 38.230 17.510 1.00 26.92 C ANISOU 1495 CB GLU A 379 1600 5233 3395 373 596 882 C ATOM 1496 CG GLU A 379 82.246 37.646 16.144 1.00 28.18 C ANISOU 1496 CG GLU A 379 1740 5508 3459 587 663 869 C ATOM 1497 CD GLU A 379 82.958 36.308 16.255 1.00 33.00 C ANISOU 1497 CD GLU A 379 2320 6123 4097 737 716 877 C ATOM 1498 OE1 GLU A 379 84.207 36.297 16.187 1.00 30.70 O ANISOU 1498 OE1 GLU A 379 2015 5895 3755 783 759 966 O ATOM 1499 OE2 GLU A 379 82.277 35.265 16.417 1.00 31.81 O1+ ANISOU 1499 OE2 GLU A 379 2206 5838 4044 791 698 773 O1+ ATOM 1500 N ILE A 380 81.586 40.497 19.699 1.00 34.76 N ANISOU 1500 N ILE A 380 2667 6039 4500 -41 497 829 N ATOM 1501 CA ILE A 380 81.218 40.920 21.041 1.00 24.42 C ANISOU 1501 CA ILE A 380 1388 4640 3250 -191 455 755 C ATOM 1502 C ILE A 380 80.259 42.115 21.047 1.00 40.60 C ANISOU 1502 C ILE A 380 3489 6543 5396 -314 446 647 C ATOM 1503 O ILE A 380 79.302 42.144 21.810 1.00 35.48 O ANISOU 1503 O ILE A 380 2881 5783 4816 -403 418 558 O ATOM 1504 CB ILE A 380 82.473 41.280 21.860 1.00 32.80 C ANISOU 1504 CB ILE A 380 2412 5778 4273 -223 456 779 C ATOM 1505 CG1 ILE A 380 83.354 40.033 22.057 1.00 27.75 C ANISOU 1505 CG1 ILE A 380 1714 5276 3553 -99 460 899 C ATOM 1506 CG2 ILE A 380 82.087 41.907 23.197 1.00 25.10 C ANISOU 1506 CG2 ILE A 380 1458 4733 3347 -364 424 675 C ATOM 1507 CD1 ILE A 380 84.656 40.310 22.709 1.00 27.00 C ANISOU 1507 CD1 ILE A 380 1555 5296 3407 -110 453 938 C ATOM 1508 N ILE A 381 80.510 43.106 20.205 1.00 23.87 N ANISOU 1508 N ILE A 381 1362 4414 3293 -311 483 663 N ATOM 1509 CA ILE A 381 79.601 44.237 20.111 1.00 23.36 C ANISOU 1509 CA ILE A 381 1332 4204 3341 -404 492 579 C ATOM 1510 C ILE A 381 78.218 43.834 19.579 1.00 28.25 C ANISOU 1510 C ILE A 381 1970 4779 3983 -390 452 562 C ATOM 1511 O ILE A 381 77.206 44.312 20.072 1.00 35.44 O ANISOU 1511 O ILE A 381 2923 5542 5002 -485 435 453 O ATOM 1512 CB ILE A 381 80.167 45.316 19.206 1.00 24.14 C ANISOU 1512 CB ILE A 381 1398 4317 3457 -385 556 639 C ATOM 1513 CG1 ILE A 381 81.457 45.883 19.801 1.00 25.98 C ANISOU 1513 CG1 ILE A 381 1592 4560 3721 -427 603 610 C ATOM 1514 CG2 ILE A 381 79.165 46.416 18.997 1.00 25.41 C ANISOU 1514 CG2 ILE A 381 1580 4340 3736 -461 575 576 C ATOM 1515 CD1 ILE A 381 82.201 46.813 18.886 1.00 25.91 C ANISOU 1515 CD1 ILE A 381 1536 4573 3736 -400 685 682 C ATOM 1516 N THR A 382 78.173 42.930 18.602 1.00 24.04 N ANISOU 1516 N THR A 382 1395 4377 3360 -259 444 645 N ATOM 1517 CA THR A 382 76.955 42.671 17.842 1.00 23.14 C ANISOU 1517 CA THR A 382 1258 4267 3270 -222 405 622 C ATOM 1518 C THR A 382 76.272 41.365 18.177 1.00 22.88 C ANISOU 1518 C THR A 382 1205 4220 3269 -198 359 543 C ATOM 1519 O THR A 382 75.063 41.218 17.999 1.00 26.42 O ANISOU 1519 O THR A 382 1636 4605 3800 -227 302 459 O ATOM 1520 CB THR A 382 77.241 42.664 16.331 1.00 31.03 C ANISOU 1520 CB THR A 382 2193 5458 4139 -50 436 729 C ATOM 1521 OG1 THR A 382 78.004 41.494 15.967 1.00 26.56 O ANISOU 1521 OG1 THR A 382 1595 5040 3455 109 464 743 O ATOM 1522 CG2 THR A 382 77.993 43.899 15.936 1.00 24.86 C ANISOU 1522 CG2 THR A 382 1419 4683 3344 -61 503 841 C ATOM 1523 N GLY A 383 77.038 40.399 18.646 1.00 23.18 N ANISOU 1523 N GLY A 383 1230 4311 3265 -139 384 571 N ATOM 1524 CA GLY A 383 76.486 39.085 18.888 1.00 23.31 C ANISOU 1524 CA GLY A 383 1235 4277 3343 -85 364 504 C ATOM 1525 C GLY A 383 76.289 38.343 17.588 1.00 24.29 C ANISOU 1525 C GLY A 383 1444 4383 3401 100 333 399 C ATOM 1526 O GLY A 383 75.655 37.295 17.573 1.00 25.83 O ANISOU 1526 O GLY A 383 1703 4435 3677 152 302 264 O ATOM 1527 N LEU A 384 76.814 38.875 16.484 1.00 25.49 N ANISOU 1527 N LEU A 384 1588 4684 3413 202 351 449 N ATOM 1528 CA LEU A 384 76.653 38.205 15.195 1.00 26.25 C ANISOU 1528 CA LEU A 384 1755 4816 3402 384 320 327 C ATOM 1529 C LEU A 384 77.857 37.308 14.888 1.00 28.09 C ANISOU 1529 C LEU A 384 1978 5141 3556 540 399 356 C ATOM 1530 O LEU A 384 78.983 37.615 15.245 1.00 29.37 O ANISOU 1530 O LEU A 384 2067 5412 3680 535 478 521 O ATOM 1531 CB LEU A 384 76.461 39.218 14.075 1.00 26.80 C ANISOU 1531 CB LEU A 384 1824 5022 3336 434 300 372 C ATOM 1532 CG LEU A 384 75.330 40.248 14.171 1.00 35.47 C ANISOU 1532 CG LEU A 384 2913 6046 4518 308 233 374 C ATOM 1533 CD1 LEU A 384 75.540 41.355 13.127 1.00 26.95 C ANISOU 1533 CD1 LEU A 384 1800 5135 3303 381 262 522 C ATOM 1534 CD2 LEU A 384 73.945 39.594 14.036 1.00 26.13 C ANISOU 1534 CD2 LEU A 384 1797 4717 3415 306 113 147 C ATOM 1535 N PRO A 385 77.612 36.172 14.239 1.00 30.88 N ANISOU 1535 N PRO A 385 2388 5439 3904 676 383 176 N ATOM 1536 CA PRO A 385 78.716 35.317 13.796 1.00 29.86 C ANISOU 1536 CA PRO A 385 2244 5388 3713 839 470 180 C ATOM 1537 C PRO A 385 79.563 36.010 12.744 1.00 30.73 C ANISOU 1537 C PRO A 385 2332 5741 3603 943 522 276 C ATOM 1538 O PRO A 385 79.036 36.869 12.056 1.00 34.50 O ANISOU 1538 O PRO A 385 2831 6311 3966 935 474 280 O ATOM 1539 CB PRO A 385 78.000 34.100 13.211 1.00 31.13 C ANISOU 1539 CB PRO A 385 2462 5422 3944 940 437 -95 C ATOM 1540 CG PRO A 385 76.632 34.598 12.853 1.00 34.19 C ANISOU 1540 CG PRO A 385 2895 5769 4325 869 315 -238 C ATOM 1541 CD PRO A 385 76.294 35.615 13.896 1.00 28.87 C ANISOU 1541 CD PRO A 385 2197 5040 3730 680 290 -66 C ATOM 1542 N ALA A 386 80.838 35.637 12.622 1.00 31.57 N ANISOU 1542 N ALA A 386 2390 5945 3661 1046 628 368 N ATOM 1543 CA ALA A 386 81.766 36.256 11.670 1.00 32.58 C ANISOU 1543 CA ALA A 386 2486 6301 3593 1149 709 481 C ATOM 1544 C ALA A 386 81.373 36.048 10.192 1.00 41.49 C ANISOU 1544 C ALA A 386 3681 7559 4522 1306 689 315 C ATOM 1545 O ALA A 386 81.715 36.847 9.322 1.00 35.12 O ANISOU 1545 O ALA A 386 2865 6954 3523 1373 733 422 O ATOM 1546 CB ALA A 386 83.151 35.735 11.906 1.00 33.26 C ANISOU 1546 CB ALA A 386 2497 6441 3701 1230 824 585 C ATOM 1547 N VAL A 387 80.671 34.962 9.904 1.00 43.13 N ANISOU 1547 N VAL A 387 3945 7665 4778 1368 631 49 N ATOM 1548 CA VAL A 387 80.139 34.762 8.570 1.00 36.94 C ANISOU 1548 CA VAL A 387 3211 7029 3795 1501 584 -160 C ATOM 1549 C VAL A 387 78.737 34.198 8.675 1.00 44.91 C ANISOU 1549 C VAL A 387 4264 7870 4928 1448 452 -428 C ATOM 1550 O VAL A 387 78.457 33.388 9.561 1.00 51.40 O ANISOU 1550 O VAL A 387 5083 8442 6006 1378 451 -514 O ATOM 1551 CB VAL A 387 81.022 33.819 7.717 1.00 53.14 C ANISOU 1551 CB VAL A 387 5252 9197 5743 1688 690 -297 C ATOM 1552 CG1 VAL A 387 81.039 32.404 8.281 1.00 39.51 C ANISOU 1552 CG1 VAL A 387 3513 7225 4276 1702 723 -487 C ATOM 1553 CG2 VAL A 387 80.536 33.807 6.269 1.00 41.34 C ANISOU 1553 CG2 VAL A 387 3796 7941 3972 1827 640 -503 C ATOM 1554 N ASP A 388 77.851 34.643 7.788 1.00 39.86 N ANISOU 1554 N ASP A 388 3655 7374 4117 1485 344 -542 N ATOM 1555 CA ASP A 388 76.492 34.114 7.712 1.00 38.07 C ANISOU 1555 CA ASP A 388 3452 7021 3992 1449 209 -835 C ATOM 1556 C ASP A 388 76.088 34.034 6.249 1.00 40.58 C ANISOU 1556 C ASP A 388 3779 7615 4026 1605 134 -1056 C ATOM 1557 O ASP A 388 75.737 35.046 5.635 1.00 41.92 O ANISOU 1557 O ASP A 388 3951 8000 3975 1634 65 -931 O ATOM 1558 CB ASP A 388 75.503 34.987 8.501 1.00 36.07 C ANISOU 1558 CB ASP A 388 3203 6630 3872 1273 110 -720 C ATOM 1559 CG ASP A 388 74.114 34.345 8.646 1.00 44.05 C ANISOU 1559 CG ASP A 388 4223 7452 5062 1212 -15 -1020 C ATOM 1560 OD1 ASP A 388 73.735 33.469 7.827 1.00 38.31 O ANISOU 1560 OD1 ASP A 388 3493 6775 4291 1319 -61 -1341 O ATOM 1561 OD2 ASP A 388 73.397 34.725 9.602 1.00 38.68 O1+ ANISOU 1561 OD2 ASP A 388 3542 6572 4582 1050 -59 -951 O1+ ATOM 1562 N GLU A 389 76.138 32.830 5.696 1.00 42.60 N ANISOU 1562 N GLU A 389 4024 7870 4291 1711 153 -1384 N ATOM 1563 CA GLU A 389 75.746 32.619 4.306 1.00 54.17 C ANISOU 1563 CA GLU A 389 5481 9631 5469 1863 76 -1662 C ATOM 1564 C GLU A 389 74.460 33.360 3.936 1.00 49.23 C ANISOU 1564 C GLU A 389 4856 9123 4726 1831 -112 -1705 C ATOM 1565 O GLU A 389 74.366 33.944 2.859 1.00 47.62 O ANISOU 1565 O GLU A 389 4647 9274 4172 1957 -171 -1679 O ATOM 1566 CB GLU A 389 75.581 31.125 4.024 1.00 61.96 C ANISOU 1566 CB GLU A 389 6434 10498 6608 1921 98 -2106 C ATOM 1567 CG GLU A 389 74.700 30.819 2.828 1.00 76.66 C ANISOU 1567 CG GLU A 389 8266 12607 8256 2021 -40 -2503 C ATOM 1568 CD GLU A 389 74.809 29.372 2.393 1.00 86.83 C ANISOU 1568 CD GLU A 389 9499 13819 9675 2098 25 -2962 C ATOM 1569 OE1 GLU A 389 75.302 28.559 3.209 1.00 89.89 O ANISOU 1569 OE1 GLU A 389 9873 13869 10413 2047 163 -2962 O ATOM 1570 OE2 GLU A 389 74.417 29.056 1.241 1.00 89.14 O1+ ANISOU 1570 OE2 GLU A 389 9748 14396 9725 2213 -54 -3320 O1+ ATOM 1571 N HIS A 390 73.486 33.361 4.841 1.00 43.85 N ANISOU 1571 N HIS A 390 4172 8155 4334 1670 -199 -1746 N ATOM 1572 CA HIS A 390 72.169 33.916 4.525 1.00 51.18 C ANISOU 1572 CA HIS A 390 5082 9160 5205 1638 -384 -1835 C ATOM 1573 C HIS A 390 72.004 35.347 4.992 1.00 45.45 C ANISOU 1573 C HIS A 390 4368 8438 4462 1546 -405 -1438 C ATOM 1574 O HIS A 390 70.872 35.791 5.209 1.00 44.69 O ANISOU 1574 O HIS A 390 4251 8264 4464 1460 -536 -1466 O ATOM 1575 CB HIS A 390 71.054 33.044 5.131 1.00 53.58 C ANISOU 1575 CB HIS A 390 5358 9145 5855 1520 -467 -2164 C ATOM 1576 CG HIS A 390 71.207 31.586 4.822 1.00 61.91 C ANISOU 1576 CG HIS A 390 6380 10112 7031 1587 -413 -2565 C ATOM 1577 ND1 HIS A 390 71.056 31.075 3.548 1.00 64.35 N ANISOU 1577 ND1 HIS A 390 6644 10706 7098 1739 -479 -2918 N ATOM 1578 CD2 HIS A 390 71.540 30.536 5.609 1.00 63.51 C ANISOU 1578 CD2 HIS A 390 6576 9979 7577 1530 -284 -2662 C ATOM 1579 CE1 HIS A 390 71.271 29.772 3.569 1.00 67.43 C ANISOU 1579 CE1 HIS A 390 6996 10914 7710 1760 -387 -3247 C ATOM 1580 NE2 HIS A 390 71.567 29.419 4.809 1.00 66.67 N ANISOU 1580 NE2 HIS A 390 6922 10428 7981 1640 -263 -3079 N ATOM 1581 N ARG A 391 73.120 36.069 5.127 1.00 43.68 N ANISOU 1581 N ARG A 391 4161 8298 4139 1562 -269 -1084 N ATOM 1582 CA ARG A 391 73.086 37.450 5.607 1.00 39.57 C ANISOU 1582 CA ARG A 391 3630 7755 3651 1465 -252 -712 C ATOM 1583 C ARG A 391 73.774 38.429 4.653 1.00 40.96 C ANISOU 1583 C ARG A 391 3792 8263 3507 1608 -184 -425 C ATOM 1584 O ARG A 391 74.679 38.072 3.931 1.00 43.83 O ANISOU 1584 O ARG A 391 4165 8835 3652 1753 -94 -434 O ATOM 1585 CB ARG A 391 73.734 37.534 6.989 1.00 38.12 C ANISOU 1585 CB ARG A 391 3449 7288 3747 1298 -131 -528 C ATOM 1586 CG ARG A 391 73.961 38.949 7.498 1.00 35.43 C ANISOU 1586 CG ARG A 391 3077 6930 3455 1194 -72 -166 C ATOM 1587 CD ARG A 391 74.707 38.950 8.806 1.00 33.32 C ANISOU 1587 CD ARG A 391 2794 6448 3417 1042 42 -30 C ATOM 1588 NE ARG A 391 76.115 38.586 8.647 1.00 42.79 N ANISOU 1588 NE ARG A 391 3986 7753 4518 1134 180 59 N ATOM 1589 CZ ARG A 391 76.891 38.141 9.632 1.00 32.71 C ANISOU 1589 CZ ARG A 391 2692 6336 3401 1058 267 107 C ATOM 1590 NH1 ARG A 391 76.407 37.996 10.855 1.00 38.93 N1+ ANISOU 1590 NH1 ARG A 391 3474 6886 4431 892 236 82 N1+ ATOM 1591 NH2 ARG A 391 78.152 37.846 9.399 1.00 33.44 N ANISOU 1591 NH2 ARG A 391 2763 6540 3404 1154 386 191 N ATOM 1592 N GLU A 392 73.338 39.676 4.659 1.00 53.26 N ANISOU 1592 N GLU A 392 5320 9857 5059 1568 -210 -159 N ATOM 1593 CA GLU A 392 73.998 40.715 3.886 1.00 52.91 C ANISOU 1593 CA GLU A 392 5249 10078 4777 1690 -110 180 C ATOM 1594 C GLU A 392 74.532 41.734 4.883 1.00 39.59 C ANISOU 1594 C GLU A 392 3524 8178 3340 1527 26 508 C ATOM 1595 O GLU A 392 73.758 42.345 5.596 1.00 38.20 O ANISOU 1595 O GLU A 392 3319 7801 3393 1378 -28 566 O ATOM 1596 CB GLU A 392 73.008 41.351 2.888 1.00 54.91 C ANISOU 1596 CB GLU A 392 5471 10586 4806 1815 -245 229 C ATOM 1597 CG GLU A 392 73.609 42.344 1.896 1.00 59.80 C ANISOU 1597 CG GLU A 392 6059 11528 5136 1988 -136 593 C ATOM 1598 CD GLU A 392 74.742 41.738 1.068 1.00 71.14 C ANISOU 1598 CD GLU A 392 7525 13234 6271 2160 -19 550 C ATOM 1599 OE1 GLU A 392 74.592 40.592 0.583 1.00 73.96 O ANISOU 1599 OE1 GLU A 392 7914 13716 6471 2245 -106 179 O ATOM 1600 OE2 GLU A 392 75.793 42.401 0.915 1.00 72.36 O1+ ANISOU 1600 OE2 GLU A 392 7660 13463 6371 2205 174 874 O1+ ATOM 1601 N PRO A 393 75.859 41.883 4.994 1.00 43.91 N ANISOU 1601 N PRO A 393 4057 8758 3869 1542 205 690 N ATOM 1602 CA PRO A 393 76.961 41.200 4.307 1.00 41.33 C ANISOU 1602 CA PRO A 393 3753 8633 3320 1699 309 647 C ATOM 1603 C PRO A 393 77.272 39.847 4.933 1.00 40.69 C ANISOU 1603 C PRO A 393 3708 8380 3373 1651 301 358 C ATOM 1604 O PRO A 393 77.037 39.650 6.116 1.00 44.23 O ANISOU 1604 O PRO A 393 4152 8543 4108 1477 275 309 O ATOM 1605 CB PRO A 393 78.133 42.157 4.510 1.00 40.60 C ANISOU 1605 CB PRO A 393 3598 8550 3278 1672 512 1004 C ATOM 1606 CG PRO A 393 77.860 42.741 5.866 1.00 37.97 C ANISOU 1606 CG PRO A 393 3220 7905 3301 1433 509 1084 C ATOM 1607 CD PRO A 393 76.360 42.858 5.984 1.00 37.52 C ANISOU 1607 CD PRO A 393 3185 7752 3319 1371 330 957 C ATOM 1608 N GLN A 394 77.820 38.925 4.161 1.00 41.88 N ANISOU 1608 N GLN A 394 3884 8702 3327 1809 337 180 N ATOM 1609 CA GLN A 394 78.093 37.605 4.708 1.00 47.17 C ANISOU 1609 CA GLN A 394 4573 9187 4162 1779 346 -85 C ATOM 1610 C GLN A 394 79.250 37.621 5.714 1.00 40.55 C ANISOU 1610 C GLN A 394 3700 8182 3526 1686 492 105 C ATOM 1611 O GLN A 394 79.215 36.907 6.709 1.00 38.31 O ANISOU 1611 O GLN A 394 3416 7649 3491 1582 480 1 O ATOM 1612 CB GLN A 394 78.359 36.632 3.574 1.00 44.11 C ANISOU 1612 CB GLN A 394 4204 9024 3531 1974 360 -354 C ATOM 1613 CG GLN A 394 77.200 36.594 2.632 1.00 46.01 C ANISOU 1613 CG GLN A 394 4457 9464 3559 2061 196 -573 C ATOM 1614 CD GLN A 394 77.528 35.889 1.356 1.00 63.19 C ANISOU 1614 CD GLN A 394 6635 11957 5417 2267 219 -814 C ATOM 1615 OE1 GLN A 394 78.156 36.464 0.454 1.00 66.95 O ANISOU 1615 OE1 GLN A 394 7106 12756 5578 2413 306 -624 O ATOM 1616 NE2 GLN A 394 77.112 34.628 1.257 1.00 62.28 N ANISOU 1616 NE2 GLN A 394 6516 11755 5392 2283 157 -1245 N ATOM 1617 N LEU A 395 80.256 38.450 5.472 1.00 40.00 N ANISOU 1617 N LEU A 395 3587 8256 3357 1725 631 393 N ATOM 1618 CA LEU A 395 81.331 38.598 6.435 1.00 38.58 C ANISOU 1618 CA LEU A 395 3346 7945 3368 1628 754 573 C ATOM 1619 C LEU A 395 81.066 39.772 7.362 1.00 47.79 C ANISOU 1619 C LEU A 395 4461 8974 4724 1437 747 792 C ATOM 1620 O LEU A 395 80.901 40.917 6.915 1.00 45.24 O ANISOU 1620 O LEU A 395 4108 8750 4329 1439 777 992 O ATOM 1621 CB LEU A 395 82.677 38.779 5.735 1.00 40.14 C ANISOU 1621 CB LEU A 395 3499 8351 3402 1763 931 735 C ATOM 1622 CG LEU A 395 83.055 37.609 4.828 1.00 43.70 C ANISOU 1622 CG LEU A 395 3987 8944 3673 1951 966 500 C ATOM 1623 CD1 LEU A 395 84.234 37.951 3.967 1.00 44.14 C ANISOU 1623 CD1 LEU A 395 4023 9200 3549 2072 1116 671 C ATOM 1624 CD2 LEU A 395 83.309 36.370 5.640 1.00 41.55 C ANISOU 1624 CD2 LEU A 395 3710 8449 3628 1913 961 310 C ATOM 1625 N LEU A 396 81.030 39.468 8.655 1.00 35.20 N ANISOU 1625 N LEU A 396 2896 7660 2817 1755 -385 49 N ATOM 1626 CA LEU A 396 80.902 40.461 9.694 1.00 33.50 C ANISOU 1626 CA LEU A 396 2502 7489 2737 1504 -254 149 C ATOM 1627 C LEU A 396 81.883 41.603 9.520 1.00 35.11 C ANISOU 1627 C LEU A 396 2643 7801 2894 1426 162 280 C ATOM 1628 O LEU A 396 81.556 42.757 9.799 1.00 35.53 O ANISOU 1628 O LEU A 396 2761 7688 3050 1271 398 362 O ATOM 1629 CB LEU A 396 81.115 39.818 11.064 1.00 31.71 C ANISOU 1629 CB LEU A 396 2208 7103 2738 1123 -332 53 C ATOM 1630 CG LEU A 396 80.819 40.740 12.242 1.00 32.29 C ANISOU 1630 CG LEU A 396 2148 7206 2916 838 -222 71 C ATOM 1631 CD1 LEU A 396 79.431 41.332 12.087 1.00 30.90 C ANISOU 1631 CD1 LEU A 396 2024 6920 2797 961 -244 112 C ATOM 1632 CD2 LEU A 396 80.903 39.972 13.520 1.00 31.26 C ANISOU 1632 CD2 LEU A 396 2044 6922 2912 564 -328 15 C ATOM 1633 N LEU A 397 83.096 41.294 9.063 1.00 41.21 N ANISOU 1633 N LEU A 397 3340 8740 3578 1483 309 290 N ATOM 1634 CA LEU A 397 84.112 42.336 8.980 1.00 44.69 C ANISOU 1634 CA LEU A 397 3726 9180 4076 1298 754 417 C ATOM 1635 C LEU A 397 83.686 43.386 7.960 1.00 40.75 C ANISOU 1635 C LEU A 397 3513 8532 3438 1493 1039 635 C ATOM 1636 O LEU A 397 84.202 44.492 7.946 1.00 57.47 O ANISOU 1636 O LEU A 397 5623 10528 5683 1309 1432 784 O ATOM 1637 CB LEU A 397 85.484 41.753 8.646 1.00 40.21 C ANISOU 1637 CB LEU A 397 3021 8754 3502 1320 839 409 C ATOM 1638 CG LEU A 397 85.696 40.995 7.341 1.00 60.07 C ANISOU 1638 CG LEU A 397 5688 11404 5732 1762 834 418 C ATOM 1639 CD1 LEU A 397 85.771 41.954 6.161 1.00 45.22 C ANISOU 1639 CD1 LEU A 397 4079 9445 3658 1934 1193 644 C ATOM 1640 CD2 LEU A 397 86.967 40.122 7.421 1.00 43.24 C ANISOU 1640 CD2 LEU A 397 3348 9370 3711 1736 820 340 C ATOM 1641 N ASP A 398 82.695 43.064 7.147 1.00 40.89 N ANISOU 1641 N ASP A 398 3772 8540 3223 1852 816 665 N ATOM 1642 CA ASP A 398 82.248 44.000 6.136 1.00 43.58 C ANISOU 1642 CA ASP A 398 4394 8779 3384 2092 1033 926 C ATOM 1643 C ASP A 398 81.325 45.102 6.643 1.00 53.38 C ANISOU 1643 C ASP A 398 5693 9718 4872 1950 1114 1036 C ATOM 1644 O ASP A 398 81.098 46.077 5.928 1.00 55.31 O ANISOU 1644 O ASP A 398 6138 9819 5057 2104 1370 1318 O ATOM 1645 CB ASP A 398 81.563 43.245 5.013 1.00 44.77 C ANISOU 1645 CB ASP A 398 4781 9081 3146 2552 715 902 C ATOM 1646 CG ASP A 398 82.529 42.844 3.937 1.00 47.77 C ANISOU 1646 CG ASP A 398 5274 9715 3159 2821 909 942 C ATOM 1647 OD1 ASP A 398 83.376 43.685 3.594 1.00 52.48 O ANISOU 1647 OD1 ASP A 398 5893 10214 3831 2713 1334 1174 O ATOM 1648 OD2 ASP A 398 82.463 41.699 3.449 1.00 48.06 O1+ ANISOU 1648 OD2 ASP A 398 5361 9883 3017 3054 585 709 O1+ ATOM 1649 N ILE A 399 80.779 44.973 7.852 1.00 47.45 N ANISOU 1649 N ILE A 399 4774 8860 4393 1685 927 839 N ATOM 1650 CA ILE A 399 79.911 46.039 8.357 1.00 49.13 C ANISOU 1650 CA ILE A 399 5034 8770 4862 1575 1059 906 C ATOM 1651 C ILE A 399 80.750 47.258 8.708 1.00 52.00 C ANISOU 1651 C ILE A 399 5371 8926 5460 1266 1541 981 C ATOM 1652 O ILE A 399 80.204 48.343 8.944 1.00 44.29 O ANISOU 1652 O ILE A 399 4475 7627 4726 1200 1759 1061 O ATOM 1653 CB ILE A 399 79.073 45.638 9.599 1.00 38.13 C ANISOU 1653 CB ILE A 399 3477 7332 3680 1378 804 672 C ATOM 1654 CG1 ILE A 399 79.949 45.384 10.819 1.00 42.03 C ANISOU 1654 CG1 ILE A 399 3751 7932 4286 963 850 451 C ATOM 1655 CG2 ILE A 399 78.186 44.441 9.319 1.00 40.31 C ANISOU 1655 CG2 ILE A 399 3729 7749 3838 1631 329 602 C ATOM 1656 CD1 ILE A 399 79.098 45.222 12.096 1.00 39.19 C ANISOU 1656 CD1 ILE A 399 3274 7529 4087 763 706 270 C ATOM 1657 N LYS A 400 82.072 47.089 8.729 1.00 43.47 N ANISOU 1657 N LYS A 400 4155 8001 4361 1080 1710 949 N ATOM 1658 CA LYS A 400 82.938 48.230 8.944 1.00 46.18 C ANISOU 1658 CA LYS A 400 4438 8135 4974 767 2159 1024 C ATOM 1659 C LYS A 400 82.753 49.245 7.823 1.00 54.84 C ANISOU 1659 C LYS A 400 5784 8990 6061 1010 2514 1416 C ATOM 1660 O LYS A 400 82.663 50.443 8.080 1.00 56.89 O ANISOU 1660 O LYS A 400 6091 8872 6654 826 2832 1503 O ATOM 1661 CB LYS A 400 84.398 47.823 9.035 1.00 46.89 C ANISOU 1661 CB LYS A 400 4280 8463 5074 557 2266 963 C ATOM 1662 CG LYS A 400 85.303 49.023 9.242 1.00 50.39 C ANISOU 1662 CG LYS A 400 4610 8664 5871 189 2718 1032 C ATOM 1663 CD LYS A 400 86.761 48.659 9.121 1.00 52.01 C ANISOU 1663 CD LYS A 400 4576 9050 6136 16 2799 999 C ATOM 1664 CE LYS A 400 87.624 49.911 9.106 1.00 57.59 C ANISOU 1664 CE LYS A 400 5180 9476 7227 -339 3243 1097 C ATOM 1665 NZ LYS A 400 89.023 49.644 8.699 1.00 59.12 N1+ ANISOU 1665 NZ LYS A 400 5169 9807 7485 -443 3351 1114 N1+ ATOM 1666 N GLU A 401 82.684 48.773 6.580 1.00 51.00 N ANISOU 1666 N GLU A 401 5476 8715 5188 1436 2462 1653 N ATOM 1667 CA GLU A 401 82.517 49.691 5.457 1.00 61.36 C ANISOU 1667 CA GLU A 401 7051 9858 6404 1712 2790 2098 C ATOM 1668 C GLU A 401 81.149 50.356 5.529 1.00 55.50 C ANISOU 1668 C GLU A 401 6473 8810 5803 1873 2679 2207 C ATOM 1669 O GLU A 401 81.012 51.549 5.268 1.00 58.97 O ANISOU 1669 O GLU A 401 7038 8890 6478 1884 3035 2516 O ATOM 1670 CB GLU A 401 82.687 48.982 4.106 1.00 65.25 C ANISOU 1670 CB GLU A 401 7738 10717 6338 2170 2722 2296 C ATOM 1671 CG GLU A 401 82.786 49.973 2.948 1.00 77.75 C ANISOU 1671 CG GLU A 401 9588 12134 7820 2398 3079 2783 C ATOM 1672 CD GLU A 401 82.799 49.324 1.576 1.00 86.58 C ANISOU 1672 CD GLU A 401 10945 13559 8393 2842 2889 2884 C ATOM 1673 OE1 GLU A 401 81.738 48.818 1.141 1.00 86.44 O ANISOU 1673 OE1 GLU A 401 11099 13716 8028 3209 2489 2856 O ATOM 1674 OE2 GLU A 401 83.868 49.339 0.921 1.00 90.74 O1+ ANISOU 1674 OE2 GLU A 401 11472 14144 8861 2813 3131 2964 O1+ ATOM 1675 N GLU A 402 80.142 49.573 5.897 1.00 52.28 N ANISOU 1675 N GLU A 402 6035 8522 5308 1997 2200 1970 N ATOM 1676 CA GLU A 402 78.776 50.058 5.983 1.00 52.65 C ANISOU 1676 CA GLU A 402 6167 8326 5513 2181 2052 2055 C ATOM 1677 C GLU A 402 78.658 51.243 6.948 1.00 65.58 C ANISOU 1677 C GLU A 402 7734 9498 7685 1858 2396 1999 C ATOM 1678 O GLU A 402 77.894 52.191 6.714 1.00 56.32 O ANISOU 1678 O GLU A 402 6683 7982 6734 2034 2547 2246 O ATOM 1679 CB GLU A 402 77.858 48.933 6.429 1.00 49.08 C ANISOU 1679 CB GLU A 402 5592 8078 4977 2261 1513 1757 C ATOM 1680 CG GLU A 402 77.371 47.983 5.353 1.00 49.50 C ANISOU 1680 CG GLU A 402 5768 8453 4589 2685 1085 1818 C ATOM 1681 CD GLU A 402 76.272 47.074 5.895 1.00 68.56 C ANISOU 1681 CD GLU A 402 8014 10937 7098 2714 581 1551 C ATOM 1682 OE1 GLU A 402 75.271 46.806 5.190 1.00 75.44 O ANISOU 1682 OE1 GLU A 402 8953 11883 7828 3057 219 1641 O ATOM 1683 OE2 GLU A 402 76.395 46.650 7.059 1.00 60.68 O1+ ANISOU 1683 OE2 GLU A 402 6800 9922 6333 2380 547 1268 O1+ ATOM 1684 N ILE A 403 79.425 51.176 8.033 1.00 60.99 N ANISOU 1684 N ILE A 403 6957 8908 7308 1398 2502 1658 N ATOM 1685 CA ILE A 403 79.442 52.230 9.039 1.00 61.55 C ANISOU 1685 CA ILE A 403 6969 8567 7850 1038 2810 1484 C ATOM 1686 C ILE A 403 80.313 53.434 8.607 1.00 57.67 C ANISOU 1686 C ILE A 403 6554 7721 7635 886 3333 1742 C ATOM 1687 O ILE A 403 80.004 54.577 8.924 1.00 60.59 O ANISOU 1687 O ILE A 403 6989 7602 8431 780 3637 1769 O ATOM 1688 CB ILE A 403 79.918 51.656 10.396 1.00 50.15 C ANISOU 1688 CB ILE A 403 5294 7310 6451 601 2662 998 C ATOM 1689 CG1 ILE A 403 78.859 50.721 10.967 1.00 46.68 C ANISOU 1689 CG1 ILE A 403 4784 7081 5870 725 2247 798 C ATOM 1690 CG2 ILE A 403 80.218 52.753 11.397 1.00 52.48 C ANISOU 1690 CG2 ILE A 403 5545 7229 7166 177 2992 743 C ATOM 1691 CD1 ILE A 403 79.398 49.820 12.069 1.00 46.15 C ANISOU 1691 CD1 ILE A 403 4508 7334 5693 394 2024 440 C ATOM 1692 N GLU A 404 81.386 53.189 7.871 1.00 58.83 N ANISOU 1692 N GLU A 404 6684 8085 7584 883 3471 1942 N ATOM 1693 CA GLU A 404 82.207 54.297 7.386 1.00 69.91 C ANISOU 1693 CA GLU A 404 8132 9150 9281 741 4002 2258 C ATOM 1694 C GLU A 404 81.438 55.080 6.331 1.00 71.93 C ANISOU 1694 C GLU A 404 8675 9120 9533 1175 4194 2796 C ATOM 1695 O GLU A 404 81.341 56.308 6.404 1.00 78.37 O ANISOU 1695 O GLU A 404 9565 9389 10823 1073 4576 2978 O ATOM 1696 CB GLU A 404 83.542 53.804 6.823 1.00 64.64 C ANISOU 1696 CB GLU A 404 7336 8821 8405 659 4147 2377 C ATOM 1697 CG GLU A 404 84.423 53.146 7.865 1.00 70.65 C ANISOU 1697 CG GLU A 404 7766 9834 9244 222 3975 1905 C ATOM 1698 CD GLU A 404 85.766 52.658 7.331 1.00 78.13 C ANISOU 1698 CD GLU A 404 8550 11085 10049 148 4035 1969 C ATOM 1699 OE1 GLU A 404 86.060 52.796 6.106 1.00 78.52 O ANISOU 1699 OE1 GLU A 404 8773 11160 9900 429 4202 2340 O ATOM 1700 OE2 GLU A 404 86.536 52.131 8.168 1.00 73.10 O1+ ANISOU 1700 OE2 GLU A 404 7613 10666 9497 -192 3867 1620 O1+ ATOM 1701 N ASP A 405 80.861 54.367 5.368 1.00 72.99 N ANISOU 1701 N ASP A 405 8974 9613 9147 1669 3904 3041 N ATOM 1702 CA ASP A 405 80.037 55.011 4.348 1.00 76.81 C ANISOU 1702 CA ASP A 405 9730 9916 9539 2138 3981 3574 C ATOM 1703 C ASP A 405 78.702 55.511 4.923 1.00 75.36 C ANISOU 1703 C ASP A 405 9559 9374 9702 2247 3822 3487 C ATOM 1704 O ASP A 405 77.818 55.946 4.183 1.00 78.07 O ANISOU 1704 O ASP A 405 10080 9591 9994 2678 3772 3900 O ATOM 1705 CB ASP A 405 79.787 54.054 3.182 1.00 70.53 C ANISOU 1705 CB ASP A 405 9106 9663 8031 2628 3642 3784 C ATOM 1706 CG ASP A 405 81.070 53.577 2.541 1.00 75.01 C ANISOU 1706 CG ASP A 405 9674 10586 8241 2590 3863 3879 C ATOM 1707 OD1 ASP A 405 81.999 54.399 2.360 1.00 79.87 O1+ ANISOU 1707 OD1 ASP A 405 10265 10943 9139 2368 4340 4099 O1+ ATOM 1708 OD2 ASP A 405 81.146 52.375 2.220 1.00 72.05 O ANISOU 1708 OD2 ASP A 405 9297 10705 7372 2767 3506 3666 O ATOM 1709 N GLU A 406 78.566 55.443 6.243 1.00 71.51 N ANISOU 1709 N GLU A 406 8871 8749 9551 1874 3749 2962 N ATOM 1710 CA GLU A 406 77.384 55.949 6.937 1.00 71.20 C ANISOU 1710 CA GLU A 406 8806 8354 9891 1935 3691 2816 C ATOM 1711 C GLU A 406 76.083 55.329 6.428 1.00 66.20 C ANISOU 1711 C GLU A 406 8203 7969 8980 2427 3223 2958 C ATOM 1712 O GLU A 406 75.016 55.863 6.662 1.00 67.70 O ANISOU 1712 O GLU A 406 8377 7856 9491 2614 3212 3011 O ATOM 1713 CB GLU A 406 77.316 57.475 6.816 1.00 77.64 C ANISOU 1713 CB GLU A 406 9747 8489 11264 1934 4200 3126 C ATOM 1714 CG GLU A 406 78.594 58.193 7.241 1.00 82.04 C ANISOU 1714 CG GLU A 406 10254 8726 12190 1421 4671 3001 C ATOM 1715 CD GLU A 406 78.432 59.704 7.287 1.00 93.30 C ANISOU 1715 CD GLU A 406 11789 9371 14292 1376 5170 3222 C ATOM 1716 OE1 GLU A 406 79.457 60.411 7.398 1.00 95.73 O ANISOU 1716 OE1 GLU A 406 12068 9341 14965 990 5585 3231 O ATOM 1717 OE2 GLU A 406 77.280 60.185 7.216 1.00 98.14 O1+ ANISOU 1717 OE2 GLU A 406 12487 9677 15123 1724 5147 3386 O1+ ATOM 1718 N GLU A 407 76.178 54.207 5.723 1.00 71.65 N ANISOU 1718 N GLU A 407 8918 9198 9108 2638 2836 2999 N ATOM 1719 CA GLU A 407 74.991 53.458 5.323 1.00 70.23 C ANISOU 1719 CA GLU A 407 8716 9292 8677 3032 2305 3026 C ATOM 1720 C GLU A 407 74.322 52.863 6.570 1.00 65.02 C ANISOU 1720 C GLU A 407 7795 8660 8250 2810 2057 2534 C ATOM 1721 O GLU A 407 73.116 52.622 6.585 1.00 64.13 O ANISOU 1721 O GLU A 407 7579 8568 8220 3059 1740 2540 O ATOM 1722 CB GLU A 407 75.354 52.352 4.325 1.00 71.25 C ANISOU 1722 CB GLU A 407 8947 9969 8157 3262 1955 3085 C ATOM 1723 CG GLU A 407 76.475 52.729 3.360 1.00 82.54 C ANISOU 1723 CG GLU A 407 10598 11473 9288 3327 2320 3448 C ATOM 1724 CD GLU A 407 77.005 51.538 2.559 1.00 89.68 C ANISOU 1724 CD GLU A 407 11589 12938 9549 3498 2040 3366 C ATOM 1725 OE1 GLU A 407 76.361 50.465 2.599 1.00 91.70 O ANISOU 1725 OE1 GLU A 407 11766 13483 9594 3622 1504 3073 O ATOM 1726 OE2 GLU A 407 78.065 51.673 1.897 1.00 92.53 O1+ ANISOU 1726 OE2 GLU A 407 12083 13426 9647 3505 2380 3585 O1+ ATOM 1727 N LYS A 408 75.122 52.628 7.609 1.00 61.76 N ANISOU 1727 N LYS A 408 7258 8269 7938 2343 2205 2135 N ATOM 1728 CA LYS A 408 74.630 52.126 8.895 1.00 59.61 C ANISOU 1728 CA LYS A 408 6765 8040 7843 2093 2054 1695 C ATOM 1729 C LYS A 408 75.337 52.818 10.049 1.00 52.95 C ANISOU 1729 C LYS A 408 5876 6937 7305 1619 2452 1383 C ATOM 1730 O LYS A 408 76.254 53.610 9.846 1.00 60.57 O ANISOU 1730 O LYS A 408 6943 7680 8391 1449 2812 1483 O ATOM 1731 CB LYS A 408 74.835 50.616 9.014 1.00 56.50 C ANISOU 1731 CB LYS A 408 6245 8135 7087 2033 1615 1466 C ATOM 1732 CG LYS A 408 74.108 49.812 7.960 1.00 64.23 C ANISOU 1732 CG LYS A 408 7256 9377 7772 2458 1153 1653 C ATOM 1733 CD LYS A 408 72.630 50.194 7.914 1.00 67.92 C ANISOU 1733 CD LYS A 408 7642 9653 8513 2742 1010 1788 C ATOM 1734 CE LYS A 408 71.811 49.100 7.265 1.00 73.96 C ANISOU 1734 CE LYS A 408 8320 10729 9054 3035 423 1799 C ATOM 1735 NZ LYS A 408 71.945 47.821 8.032 1.00 72.15 N1+ ANISOU 1735 NZ LYS A 408 7895 10746 8774 2771 158 1433 N1+ ATOM 1736 N THR A 409 74.901 52.516 11.262 1.00 50.96 N ANISOU 1736 N THR A 409 5468 6724 7173 1398 2386 1002 N ATOM 1737 CA THR A 409 75.532 53.046 12.461 1.00 51.44 C ANISOU 1737 CA THR A 409 5492 6626 7427 936 2683 617 C ATOM 1738 C THR A 409 75.850 51.896 13.390 1.00 47.73 C ANISOU 1738 C THR A 409 4856 6598 6682 665 2401 283 C ATOM 1739 O THR A 409 75.199 50.857 13.324 1.00 46.94 O ANISOU 1739 O THR A 409 4652 6785 6397 848 2043 322 O ATOM 1740 CB THR A 409 74.621 54.034 13.219 1.00 60.49 C ANISOU 1740 CB THR A 409 6651 7337 8997 936 2982 448 C ATOM 1741 OG1 THR A 409 73.566 53.302 13.870 1.00 56.23 O ANISOU 1741 OG1 THR A 409 5952 7012 8401 1035 2750 292 O ATOM 1742 CG2 THR A 409 74.028 55.072 12.276 1.00 58.20 C ANISOU 1742 CG2 THR A 409 6495 6589 9030 1310 3204 856 C ATOM 1743 N ILE A 410 76.825 52.088 14.269 1.00 48.01 N ANISOU 1743 N ILE A 410 4853 6672 6715 228 2544 -34 N ATOM 1744 CA ILE A 410 77.078 51.142 15.345 1.00 45.46 C ANISOU 1744 CA ILE A 410 4381 6747 6146 -40 2305 -340 C ATOM 1745 C ILE A 410 75.782 50.767 16.091 1.00 53.68 C ANISOU 1745 C ILE A 410 5352 7843 7200 75 2211 -454 C ATOM 1746 O ILE A 410 75.499 49.590 16.297 1.00 41.89 O ANISOU 1746 O ILE A 410 3729 6697 5490 128 1884 -426 O ATOM 1747 CB ILE A 410 78.079 51.713 16.337 1.00 47.41 C ANISOU 1747 CB ILE A 410 4609 6964 6441 -523 2498 -710 C ATOM 1748 CG1 ILE A 410 79.235 52.377 15.578 1.00 62.71 C ANISOU 1748 CG1 ILE A 410 6580 8716 8530 -649 2701 -573 C ATOM 1749 CG2 ILE A 410 78.571 50.618 17.247 1.00 45.10 C ANISOU 1749 CG2 ILE A 410 4157 7169 5812 -762 2184 -915 C ATOM 1750 CD1 ILE A 410 80.141 53.266 16.444 1.00 63.72 C ANISOU 1750 CD1 ILE A 410 6683 8665 8863 -1146 2937 -955 C ATOM 1751 N GLU A 411 75.001 51.778 16.473 1.00 57.01 N ANISOU 1751 N GLU A 411 5845 7892 7924 122 2532 -566 N ATOM 1752 CA GLU A 411 73.703 51.573 17.118 1.00 61.63 C ANISOU 1752 CA GLU A 411 6337 8487 8593 268 2540 -644 C ATOM 1753 C GLU A 411 72.862 50.508 16.435 1.00 45.11 C ANISOU 1753 C GLU A 411 4096 6612 6431 607 2160 -332 C ATOM 1754 O GLU A 411 72.198 49.719 17.103 1.00 48.29 O ANISOU 1754 O GLU A 411 4338 7243 6766 596 2019 -396 O ATOM 1755 CB GLU A 411 72.902 52.880 17.156 1.00 75.09 C ANISOU 1755 CB GLU A 411 8131 9672 10729 429 2950 -686 C ATOM 1756 CG GLU A 411 73.220 53.791 18.329 1.00 83.72 C ANISOU 1756 CG GLU A 411 9331 10554 11926 88 3339 -1168 C ATOM 1757 CD GLU A 411 72.781 53.203 19.657 1.00 92.48 C ANISOU 1757 CD GLU A 411 10350 12002 12786 -78 3331 -1494 C ATOM 1758 OE1 GLU A 411 71.815 52.399 19.663 1.00 89.59 O ANISOU 1758 OE1 GLU A 411 9813 11846 12379 156 3163 -1303 O ATOM 1759 OE2 GLU A 411 73.408 53.543 20.689 1.00 97.14 O1+ ANISOU 1759 OE2 GLU A 411 11036 12658 13216 -450 3487 -1933 O1+ ATOM 1760 N ASP A 412 72.882 50.494 15.107 1.00 44.89 N ANISOU 1760 N ASP A 412 4124 6513 6419 900 1999 3 N ATOM 1761 CA ASP A 412 72.106 49.526 14.351 1.00 43.31 C ANISOU 1761 CA ASP A 412 3797 6505 6152 1220 1587 249 C ATOM 1762 C ASP A 412 72.557 48.103 14.622 1.00 39.98 C ANISOU 1762 C ASP A 412 3260 6500 5432 1066 1224 169 C ATOM 1763 O ASP A 412 71.763 47.178 14.576 1.00 55.65 O ANISOU 1763 O ASP A 412 5074 8633 7438 1199 917 235 O ATOM 1764 CB ASP A 412 72.206 49.814 12.857 1.00 52.42 C ANISOU 1764 CB ASP A 412 5091 7561 7266 1554 1477 592 C ATOM 1765 CG ASP A 412 71.606 51.153 12.487 1.00 62.22 C ANISOU 1765 CG ASP A 412 6428 8363 8852 1785 1792 778 C ATOM 1766 OD1 ASP A 412 70.562 51.535 13.092 1.00 63.53 O ANISOU 1766 OD1 ASP A 412 6463 8336 9339 1867 1928 707 O ATOM 1767 OD2 ASP A 412 72.186 51.822 11.598 1.00 61.76 O1+ ANISOU 1767 OD2 ASP A 412 6563 8141 8762 1897 1932 1019 O1+ ATOM 1768 N TYR A 413 73.831 47.932 14.924 1.00 38.84 N ANISOU 1768 N TYR A 413 3178 6517 5061 780 1260 33 N ATOM 1769 CA TYR A 413 74.397 46.608 15.019 1.00 36.19 C ANISOU 1769 CA TYR A 413 2741 6538 4472 686 918 11 C ATOM 1770 C TYR A 413 74.614 46.104 16.454 1.00 54.69 C ANISOU 1770 C TYR A 413 4964 9104 6713 350 924 -207 C ATOM 1771 O TYR A 413 74.937 44.925 16.639 1.00 50.77 O ANISOU 1771 O TYR A 413 4355 8877 6060 296 629 -179 O ATOM 1772 CB TYR A 413 75.723 46.582 14.255 1.00 39.05 C ANISOU 1772 CB TYR A 413 3206 6989 4644 656 904 71 C ATOM 1773 CG TYR A 413 75.551 46.331 12.768 1.00 46.05 C ANISOU 1773 CG TYR A 413 4187 7867 5442 1039 714 319 C ATOM 1774 CD1 TYR A 413 75.235 45.053 12.297 1.00 45.17 C ANISOU 1774 CD1 TYR A 413 3997 7963 5202 1227 291 355 C ATOM 1775 CD2 TYR A 413 75.711 47.355 11.836 1.00 38.46 C ANISOU 1775 CD2 TYR A 413 3410 6691 4513 1213 952 515 C ATOM 1776 CE1 TYR A 413 75.080 44.805 10.958 1.00 46.15 C ANISOU 1776 CE1 TYR A 413 4239 8121 5177 1575 86 514 C ATOM 1777 CE2 TYR A 413 75.543 47.118 10.483 1.00 39.38 C ANISOU 1777 CE2 TYR A 413 3647 6867 4450 1584 768 752 C ATOM 1778 CZ TYR A 413 75.234 45.835 10.052 1.00 50.43 C ANISOU 1778 CZ TYR A 413 4981 8516 5663 1763 321 718 C ATOM 1779 OH TYR A 413 75.065 45.558 8.713 1.00 52.11 O ANISOU 1779 OH TYR A 413 5341 8830 5631 2134 100 885 O ATOM 1780 N ILE A 414 74.446 46.968 17.460 1.00 30.60 N ANISOU 1780 N ILE A 414 3143 5078 3408 1453 1293 399 N ATOM 1781 CA ILE A 414 74.707 46.569 18.837 1.00 31.33 C ANISOU 1781 CA ILE A 414 3068 5405 3431 1214 1249 214 C ATOM 1782 C ILE A 414 73.800 45.422 19.228 1.00 36.84 C ANISOU 1782 C ILE A 414 3656 6301 4040 1309 1053 215 C ATOM 1783 O ILE A 414 72.595 45.514 19.036 1.00 38.71 O ANISOU 1783 O ILE A 414 3966 6407 4337 1474 1003 197 O ATOM 1784 CB ILE A 414 74.495 47.718 19.832 1.00 40.26 C ANISOU 1784 CB ILE A 414 4223 6409 4667 1039 1398 -43 C ATOM 1785 CG1 ILE A 414 75.363 48.918 19.447 1.00 46.13 C ANISOU 1785 CG1 ILE A 414 5082 6881 5565 918 1584 -49 C ATOM 1786 CG2 ILE A 414 74.829 47.266 21.261 1.00 32.20 C ANISOU 1786 CG2 ILE A 414 3022 5710 3504 763 1343 -227 C ATOM 1787 CD1 ILE A 414 75.277 50.093 20.446 1.00 51.34 C ANISOU 1787 CD1 ILE A 414 5745 7388 6373 714 1746 -357 C ATOM 1788 N ASP A 415 74.384 44.348 19.746 1.00 27.10 N ANISOU 1788 N ASP A 415 2297 5280 2720 1143 882 251 N ATOM 1789 CA ASP A 415 73.639 43.204 20.234 1.00 25.65 C ANISOU 1789 CA ASP A 415 2060 5196 2490 1138 655 275 C ATOM 1790 C ASP A 415 72.490 43.712 21.112 1.00 41.89 C ANISOU 1790 C ASP A 415 4105 7257 4554 1133 713 106 C ATOM 1791 O ASP A 415 72.700 44.535 22.003 1.00 46.17 O ANISOU 1791 O ASP A 415 4592 7882 5069 977 872 -80 O ATOM 1792 CB ASP A 415 74.569 42.264 21.019 1.00 25.15 C ANISOU 1792 CB ASP A 415 1846 5362 2347 924 521 326 C ATOM 1793 CG ASP A 415 73.905 40.940 21.407 1.00 34.40 C ANISOU 1793 CG ASP A 415 3009 6590 3470 919 313 404 C ATOM 1794 OD1 ASP A 415 72.659 40.822 21.303 1.00 23.36 O1+ ANISOU 1794 OD1 ASP A 415 1692 5096 2088 1030 285 375 O1+ ATOM 1795 OD2 ASP A 415 74.650 40.019 21.823 1.00 23.45 O ANISOU 1795 OD2 ASP A 415 1562 5305 2044 782 211 492 O ATOM 1796 N LYS A 416 71.266 43.272 20.857 1.00 36.33 N ANISOU 1796 N LYS A 416 3462 6456 3887 1274 600 136 N ATOM 1797 CA LYS A 416 70.173 43.830 21.637 1.00 39.30 C ANISOU 1797 CA LYS A 416 3815 6815 4300 1276 680 -38 C ATOM 1798 C LYS A 416 69.990 43.013 22.904 1.00 39.09 C ANISOU 1798 C LYS A 416 3651 7056 4145 1093 574 -71 C ATOM 1799 O LYS A 416 69.318 43.438 23.847 1.00 27.86 O ANISOU 1799 O LYS A 416 2174 5712 2701 1015 659 -246 O ATOM 1800 CB LYS A 416 68.892 43.891 20.814 1.00 26.50 C ANISOU 1800 CB LYS A 416 2313 4958 2797 1484 624 4 C ATOM 1801 CG LYS A 416 68.900 45.062 19.850 1.00 57.12 C ANISOU 1801 CG LYS A 416 6313 8582 6807 1655 765 11 C ATOM 1802 CD LYS A 416 67.830 44.909 18.769 1.00 58.84 C ANISOU 1802 CD LYS A 416 6653 8606 7097 1817 639 125 C ATOM 1803 CE LYS A 416 67.978 45.969 17.682 1.00 57.38 C ANISOU 1803 CE LYS A 416 6596 8194 7010 1988 741 217 C ATOM 1804 NZ LYS A 416 67.070 45.634 16.549 1.00 59.44 N1+ ANISOU 1804 NZ LYS A 416 6960 8356 7267 2077 586 342 N1+ ATOM 1805 N LYS A 417 70.620 41.847 22.934 1.00 25.90 N ANISOU 1805 N LYS A 417 1934 5520 2387 1015 400 97 N ATOM 1806 CA LYS A 417 70.514 40.999 24.099 1.00 25.28 C ANISOU 1806 CA LYS A 417 1739 5694 2172 846 290 125 C ATOM 1807 C LYS A 417 71.375 41.485 25.285 1.00 39.39 C ANISOU 1807 C LYS A 417 3387 7759 3821 584 351 11 C ATOM 1808 O LYS A 417 72.014 40.664 25.963 1.00 38.76 O ANISOU 1808 O LYS A 417 3222 7900 3606 419 218 132 O ATOM 1809 CB LYS A 417 70.888 39.560 23.718 1.00 23.97 C ANISOU 1809 CB LYS A 417 1635 5481 1991 831 144 334 C ATOM 1810 CG LYS A 417 69.969 38.871 22.704 1.00 22.21 C ANISOU 1810 CG LYS A 417 1574 4971 1895 966 112 378 C ATOM 1811 CD LYS A 417 70.685 37.664 22.064 1.00 20.99 C ANISOU 1811 CD LYS A 417 1488 4653 1834 904 67 477 C ATOM 1812 CE LYS A 417 71.661 38.193 21.037 1.00 31.46 C ANISOU 1812 CE LYS A 417 2858 5915 3181 969 99 488 C ATOM 1813 NZ LYS A 417 72.344 37.143 20.267 1.00 40.92 N1+ ANISOU 1813 NZ LYS A 417 4092 6994 4461 941 70 542 N1+ ATOM 1814 N MET A 418 71.401 42.795 25.552 1.00 28.76 N ANISOU 1814 N MET A 418 2060 6373 2496 518 562 -227 N ATOM 1815 CA MET A 418 71.938 43.276 26.842 1.00 30.92 C ANISOU 1815 CA MET A 418 2238 6907 2602 212 623 -408 C ATOM 1816 C MET A 418 71.305 44.577 27.343 1.00 39.43 C ANISOU 1816 C MET A 418 3371 7900 3711 158 859 -743 C ATOM 1817 O MET A 418 70.653 45.283 26.591 1.00 43.61 O ANISOU 1817 O MET A 418 4010 8134 4425 370 1004 -822 O ATOM 1818 CB MET A 418 73.460 43.426 26.770 1.00 37.30 C ANISOU 1818 CB MET A 418 3009 7795 3370 45 621 -366 C ATOM 1819 CG MET A 418 73.982 44.220 25.622 1.00 31.52 C ANISOU 1819 CG MET A 418 2384 6790 2800 173 785 -380 C ATOM 1820 SD MET A 418 75.766 44.019 25.320 1.00 33.78 S ANISOU 1820 SD MET A 418 2602 7155 3077 14 737 -240 S ATOM 1821 CE MET A 418 75.874 45.043 23.869 1.00 30.94 C ANISOU 1821 CE MET A 418 2396 6450 2909 230 977 -255 C ATOM 1822 N ASN A 419 71.454 44.882 28.630 1.00 47.51 N ANISOU 1822 N ASN A 419 4313 9179 4561 -123 886 -945 N ATOM 1823 CA ASN A 419 70.758 46.045 29.192 1.00 48.75 C ANISOU 1823 CA ASN A 419 4513 9246 4764 -181 1101 -1303 C ATOM 1824 C ASN A 419 71.676 47.043 29.905 1.00 48.93 C ANISOU 1824 C ASN A 419 4516 9366 4710 -478 1234 -1603 C ATOM 1825 O ASN A 419 71.204 47.902 30.647 1.00 57.70 O ANISOU 1825 O ASN A 419 5625 10469 5828 -598 1382 -1939 O ATOM 1826 CB ASN A 419 69.662 45.589 30.165 1.00 49.19 C ANISOU 1826 CB ASN A 419 4489 9499 4703 -234 1040 -1357 C ATOM 1827 CG ASN A 419 70.226 45.115 31.499 1.00 59.44 C ANISOU 1827 CG ASN A 419 5636 11244 5703 -570 907 -1376 C ATOM 1828 OD1 ASN A 419 71.316 44.549 31.561 1.00 64.48 O ANISOU 1828 OD1 ASN A 419 6205 12072 6222 -698 754 -1195 O ATOM 1829 ND2 ASN A 419 69.493 45.354 32.569 1.00 57.01 N ANISOU 1829 ND2 ASN A 419 5262 11117 5282 -715 961 -1590 N ATOM 1830 N ASP A 420 72.981 46.936 29.679 1.00 47.66 N ANISOU 1830 N ASP A 420 4325 9288 4494 -606 1181 -1500 N ATOM 1831 CA ASP A 420 73.951 47.767 30.392 1.00 43.08 C ANISOU 1831 CA ASP A 420 3701 8843 3826 -930 1278 -1780 C ATOM 1832 C ASP A 420 75.028 48.339 29.462 1.00 48.90 C ANISOU 1832 C ASP A 420 4493 9363 4723 -921 1399 -1759 C ATOM 1833 O ASP A 420 76.086 48.758 29.914 1.00 50.81 O ANISOU 1833 O ASP A 420 4670 9747 4889 -1203 1433 -1904 O ATOM 1834 CB ASP A 420 74.622 46.956 31.507 1.00 43.89 C ANISOU 1834 CB ASP A 420 3634 9424 3617 -1224 1051 -1690 C ATOM 1835 CG ASP A 420 75.414 45.769 30.967 1.00 52.67 C ANISOU 1835 CG ASP A 420 4686 10633 4694 -1153 820 -1269 C ATOM 1836 OD1 ASP A 420 74.974 45.175 29.944 1.00 44.43 O ANISOU 1836 OD1 ASP A 420 3711 9359 3812 -849 776 -1015 O ATOM 1837 OD2 ASP A 420 76.467 45.432 31.554 1.00 42.26 O1+ ANISOU 1837 OD2 ASP A 420 3245 9615 3197 -1399 678 -1202 O1+ ATOM 1838 N ALA A 421 74.750 48.369 28.169 1.00 40.79 N ANISOU 1838 N ALA A 421 3572 8010 3915 -612 1469 -1582 N ATOM 1839 CA ALA A 421 75.742 48.774 27.195 1.00 40.42 C ANISOU 1839 CA ALA A 421 3590 7730 4036 -583 1545 -1474 C ATOM 1840 C ALA A 421 75.599 50.236 26.792 1.00 56.47 C ANISOU 1840 C ALA A 421 5780 9302 6375 -544 1783 -1709 C ATOM 1841 O ALA A 421 75.018 50.536 25.747 1.00 59.02 O ANISOU 1841 O ALA A 421 6245 9253 6928 -250 1840 -1571 O ATOM 1842 CB ALA A 421 75.646 47.879 25.956 1.00 37.32 C ANISOU 1842 CB ALA A 421 3251 7215 3715 -271 1413 -1073 C ATOM 1843 N ASP A 422 76.149 51.141 27.591 1.00 45.60 N ANISOU 1843 N ASP A 422 4367 7942 5016 -844 1912 -2052 N ATOM 1844 CA ASP A 422 76.160 52.569 27.250 1.00 55.09 C ANISOU 1844 CA ASP A 422 5693 8667 6571 -843 2143 -2282 C ATOM 1845 C ASP A 422 76.927 52.888 25.955 1.00 55.54 C ANISOU 1845 C ASP A 422 5877 8355 6871 -722 2173 -1985 C ATOM 1846 O ASP A 422 77.971 52.311 25.690 1.00 53.72 O ANISOU 1846 O ASP A 422 5597 8291 6523 -815 2062 -1763 O ATOM 1847 CB ASP A 422 76.777 53.369 28.383 1.00 59.17 C ANISOU 1847 CB ASP A 422 6117 9314 7051 -1232 2257 -2724 C ATOM 1848 CG ASP A 422 78.263 53.151 28.484 1.00 63.58 C ANISOU 1848 CG ASP A 422 6594 10068 7495 -1497 2162 -2623 C ATOM 1849 OD1 ASP A 422 78.651 52.036 28.898 1.00 62.59 O1+ ANISOU 1849 OD1 ASP A 422 6338 10399 7045 -1588 1953 -2435 O1+ ATOM 1850 OD2 ASP A 422 79.034 54.073 28.120 1.00 67.14 O ANISOU 1850 OD2 ASP A 422 7099 10202 8209 -1606 2291 -2706 O ATOM 1851 N SER A 423 76.406 53.835 25.179 1.00 59.68 N ANISOU 1851 N SER A 423 6550 8383 7743 -523 2329 -1981 N ATOM 1852 CA SER A 423 76.946 54.214 23.878 1.00 48.55 C ANISOU 1852 CA SER A 423 5275 6611 6561 -383 2378 -1666 C ATOM 1853 C SER A 423 78.404 54.641 23.901 1.00 60.18 C ANISOU 1853 C SER A 423 6714 8062 8090 -670 2438 -1686 C ATOM 1854 O SER A 423 79.143 54.398 22.938 1.00 57.57 O ANISOU 1854 O SER A 423 6434 7664 7777 -607 2411 -1357 O ATOM 1855 CB SER A 423 76.121 55.357 23.282 1.00 67.23 C ANISOU 1855 CB SER A 423 7778 8441 9325 -177 2549 -1699 C ATOM 1856 OG SER A 423 74.929 54.868 22.690 1.00 67.60 O ANISOU 1856 OG SER A 423 7884 8446 9355 172 2461 -1496 O ATOM 1857 N THR A 424 78.833 55.301 24.972 1.00 60.74 N ANISOU 1857 N THR A 424 6690 8193 8195 -994 2530 -2087 N ATOM 1858 CA THR A 424 80.203 55.794 24.975 1.00 54.55 C ANISOU 1858 CA THR A 424 5862 7355 7510 -1275 2593 -2123 C ATOM 1859 C THR A 424 81.185 54.638 24.932 1.00 52.14 C ANISOU 1859 C THR A 424 5442 7470 6900 -1367 2399 -1869 C ATOM 1860 O THR A 424 82.059 54.614 24.077 1.00 57.42 O ANISOU 1860 O THR A 424 6137 8019 7660 -1357 2414 -1604 O ATOM 1861 CB THR A 424 80.513 56.670 26.195 1.00 66.97 C ANISOU 1861 CB THR A 424 7330 8961 9155 -1634 2709 -2645 C ATOM 1862 OG1 THR A 424 79.908 57.956 26.020 1.00 66.64 O ANISOU 1862 OG1 THR A 424 7387 8391 9543 -1567 2934 -2867 O ATOM 1863 CG2 THR A 424 82.030 56.847 26.338 1.00 59.60 C ANISOU 1863 CG2 THR A 424 6296 8123 8228 -1958 2703 -2664 C ATOM 1864 N SER A 425 81.045 53.674 25.837 1.00 50.79 N ANISOU 1864 N SER A 425 5129 7786 6383 -1456 2220 -1935 N ATOM 1865 CA SER A 425 82.016 52.583 25.893 1.00 56.59 C ANISOU 1865 CA SER A 425 5717 8905 6879 -1558 2023 -1699 C ATOM 1866 C SER A 425 81.856 51.639 24.701 1.00 58.29 C ANISOU 1866 C SER A 425 5996 9078 7074 -1229 1925 -1262 C ATOM 1867 O SER A 425 82.833 51.022 24.258 1.00 44.67 O ANISOU 1867 O SER A 425 4188 7474 5310 -1261 1840 -1029 O ATOM 1868 CB SER A 425 81.897 51.801 27.202 1.00 48.90 C ANISOU 1868 CB SER A 425 4559 8466 5553 -1749 1844 -1840 C ATOM 1869 OG SER A 425 80.697 51.072 27.248 1.00 46.81 O ANISOU 1869 OG SER A 425 4322 8319 5145 -1510 1760 -1745 O ATOM 1870 N VAL A 426 80.634 51.532 24.173 1.00 44.30 N ANISOU 1870 N VAL A 426 4356 7137 5339 -917 1939 -1172 N ATOM 1871 CA VAL A 426 80.423 50.693 22.999 1.00 43.57 C ANISOU 1871 CA VAL A 426 4329 7004 5224 -608 1852 -800 C ATOM 1872 C VAL A 426 81.162 51.303 21.817 1.00 42.36 C ANISOU 1872 C VAL A 426 4288 6528 5277 -558 1990 -611 C ATOM 1873 O VAL A 426 81.893 50.617 21.107 1.00 49.06 O ANISOU 1873 O VAL A 426 5095 7477 6069 -508 1929 -363 O ATOM 1874 CB VAL A 426 78.918 50.500 22.677 1.00 55.97 C ANISOU 1874 CB VAL A 426 6005 8465 6796 -291 1828 -756 C ATOM 1875 CG1 VAL A 426 78.738 49.793 21.341 1.00 37.97 C ANISOU 1875 CG1 VAL A 426 3806 6113 4509 16 1754 -404 C ATOM 1876 CG2 VAL A 426 78.232 49.700 23.787 1.00 39.28 C ANISOU 1876 CG2 VAL A 426 3755 6720 4450 -341 1684 -886 C ATOM 1877 N GLU A 427 81.013 52.601 21.625 1.00 44.86 N ANISOU 1877 N GLU A 427 4732 6462 5852 -586 2187 -730 N ATOM 1878 CA GLU A 427 81.728 53.273 20.551 1.00 46.19 C ANISOU 1878 CA GLU A 427 5003 6320 6228 -571 2335 -527 C ATOM 1879 C GLU A 427 83.236 53.223 20.769 1.00 57.04 C ANISOU 1879 C GLU A 427 6237 7845 7592 -868 2350 -540 C ATOM 1880 O GLU A 427 84.010 53.164 19.806 1.00 58.94 O ANISOU 1880 O GLU A 427 6500 8014 7882 -839 2409 -287 O ATOM 1881 CB GLU A 427 81.238 54.710 20.417 1.00 49.19 C ANISOU 1881 CB GLU A 427 5521 6226 6942 -559 2538 -648 C ATOM 1882 CG GLU A 427 79.845 54.759 19.825 1.00 78.00 C ANISOU 1882 CG GLU A 427 9311 9678 10647 -210 2523 -521 C ATOM 1883 CD GLU A 427 79.158 56.081 20.031 1.00 86.52 C ANISOU 1883 CD GLU A 427 10473 10319 12083 -197 2692 -716 C ATOM 1884 OE1 GLU A 427 79.865 57.076 20.315 1.00 90.71 O ANISOU 1884 OE1 GLU A 427 10988 10611 12868 -438 2853 -882 O ATOM 1885 OE2 GLU A 427 77.909 56.122 19.914 1.00 84.47 O1+ ANISOU 1885 OE2 GLU A 427 10276 9939 11881 54 2664 -714 O1+ ATOM 1886 N ALA A 428 83.656 53.227 22.026 1.00 48.05 N ANISOU 1886 N ALA A 428 4940 6943 6375 -1159 2294 -833 N ATOM 1887 CA ALA A 428 85.066 53.072 22.335 1.00 48.93 C ANISOU 1887 CA ALA A 428 4880 7250 6462 -1447 2265 -849 C ATOM 1888 C ALA A 428 85.584 51.724 21.848 1.00 46.26 C ANISOU 1888 C ALA A 428 4428 7211 5937 -1336 2099 -554 C ATOM 1889 O ALA A 428 86.644 51.652 21.222 1.00 50.33 O ANISOU 1889 O ALA A 428 4884 7710 6529 -1400 2149 -392 O ATOM 1890 CB ALA A 428 85.303 53.225 23.811 1.00 50.57 C ANISOU 1890 CB ALA A 428 4927 7724 6564 -1770 2196 -1211 C ATOM 1891 N MET A 429 84.845 50.654 22.120 1.00 43.77 N ANISOU 1891 N MET A 429 4068 7157 5405 -1171 1912 -490 N ATOM 1892 CA MET A 429 85.290 49.339 21.680 1.00 48.12 C ANISOU 1892 CA MET A 429 4490 7958 5834 -1056 1752 -233 C ATOM 1893 C MET A 429 85.197 49.183 20.159 1.00 51.54 C ANISOU 1893 C MET A 429 5064 8181 6340 -773 1843 36 C ATOM 1894 O MET A 429 86.070 48.551 19.546 1.00 39.90 O ANISOU 1894 O MET A 429 3485 6807 4868 -758 1823 207 O ATOM 1895 CB MET A 429 84.508 48.220 22.358 1.00 39.42 C ANISOU 1895 CB MET A 429 3292 7165 4522 -960 1529 -218 C ATOM 1896 CG MET A 429 84.996 46.844 21.945 1.00 37.46 C ANISOU 1896 CG MET A 429 2881 7137 4217 -849 1360 32 C ATOM 1897 SD MET A 429 84.054 45.459 22.592 1.00 35.20 S ANISOU 1897 SD MET A 429 2508 7108 3760 -700 1079 113 S ATOM 1898 CE MET A 429 84.479 45.519 24.334 1.00 37.09 C ANISOU 1898 CE MET A 429 2600 7641 3851 -1053 920 -64 C ATOM 1899 N TYR A 430 84.159 49.756 19.544 1.00 51.32 N ANISOU 1899 N TYR A 430 5255 7878 6367 -553 1942 69 N ATOM 1900 CA TYR A 430 84.056 49.660 18.094 1.00 39.82 C ANISOU 1900 CA TYR A 430 3933 6264 4933 -303 2020 332 C ATOM 1901 C TYR A 430 85.237 50.368 17.447 1.00 41.98 C ANISOU 1901 C TYR A 430 4218 6382 5352 -455 2210 427 C ATOM 1902 O TYR A 430 85.714 49.959 16.387 1.00 45.30 O ANISOU 1902 O TYR A 430 4645 6835 5734 -346 2257 640 O ATOM 1903 CB TYR A 430 82.746 50.241 17.554 1.00 39.91 C ANISOU 1903 CB TYR A 430 4167 6007 4991 -51 2077 380 C ATOM 1904 CG TYR A 430 82.785 50.287 16.058 1.00 40.11 C ANISOU 1904 CG TYR A 430 4328 5900 5013 156 2165 665 C ATOM 1905 CD1 TYR A 430 82.527 49.155 15.301 1.00 39.03 C ANISOU 1905 CD1 TYR A 430 4171 5961 4697 384 2045 821 C ATOM 1906 CD2 TYR A 430 83.173 51.441 15.397 1.00 44.72 C ANISOU 1906 CD2 TYR A 430 5041 6181 5769 99 2373 780 C ATOM 1907 CE1 TYR A 430 82.612 49.185 13.909 1.00 38.63 C ANISOU 1907 CE1 TYR A 430 4237 5850 4592 551 2131 1063 C ATOM 1908 CE2 TYR A 430 83.266 51.486 14.026 1.00 43.36 C ANISOU 1908 CE2 TYR A 430 4987 5941 5548 262 2458 1069 C ATOM 1909 CZ TYR A 430 82.987 50.363 13.286 1.00 50.94 C ANISOU 1909 CZ TYR A 430 5932 7142 6281 484 2338 1199 C ATOM 1910 OH TYR A 430 83.091 50.440 11.917 1.00 54.25 O ANISOU 1910 OH TYR A 430 6466 7538 6607 625 2431 1466 O ATOM 1911 N SER A 431 85.719 51.428 18.081 1.00 44.44 N ANISOU 1911 N SER A 431 4519 6533 5834 -719 2330 251 N ATOM 1912 CA SER A 431 86.830 52.177 17.513 1.00 46.84 C ANISOU 1912 CA SER A 431 4822 6662 6314 -889 2523 340 C ATOM 1913 C SER A 431 88.061 51.293 17.504 1.00 46.25 C ANISOU 1913 C SER A 431 4521 6887 6165 -1016 2456 398 C ATOM 1914 O SER A 431 88.854 51.328 16.572 1.00 49.82 O ANISOU 1914 O SER A 431 4963 7298 6668 -1019 2587 582 O ATOM 1915 CB SER A 431 87.098 53.470 18.289 1.00 49.85 C ANISOU 1915 CB SER A 431 5209 6800 6933 -1168 2655 94 C ATOM 1916 OG SER A 431 88.177 54.193 17.719 1.00 52.37 O ANISOU 1916 OG SER A 431 5514 6931 7451 -1342 2847 198 O ATOM 1917 N VAL A 432 88.215 50.491 18.544 1.00 45.02 N ANISOU 1917 N VAL A 432 4171 7041 5894 -1122 2254 254 N ATOM 1918 CA VAL A 432 89.369 49.625 18.625 1.00 48.77 C ANISOU 1918 CA VAL A 432 4396 7790 6344 -1238 2164 315 C ATOM 1919 C VAL A 432 89.299 48.588 17.522 1.00 42.81 C ANISOU 1919 C VAL A 432 3637 7128 5501 -959 2136 546 C ATOM 1920 O VAL A 432 90.289 48.313 16.860 1.00 43.49 O ANISOU 1920 O VAL A 432 3611 7266 5648 -992 2218 658 O ATOM 1921 CB VAL A 432 89.458 48.922 19.986 1.00 44.04 C ANISOU 1921 CB VAL A 432 3579 7521 5633 -1395 1920 164 C ATOM 1922 CG1 VAL A 432 90.601 47.921 19.976 1.00 43.80 C ANISOU 1922 CG1 VAL A 432 3328 7678 5636 -1421 1764 279 C ATOM 1923 CG2 VAL A 432 89.624 49.933 21.095 1.00 46.40 C ANISOU 1923 CG2 VAL A 432 3858 7786 5986 -1705 1952 -112 C ATOM 1924 N ALA A 433 88.107 48.021 17.346 1.00 40.65 N ANISOU 1924 N ALA A 433 3475 6879 5092 -693 2025 589 N ATOM 1925 CA ALA A 433 87.853 46.975 16.361 1.00 39.76 C ANISOU 1925 CA ALA A 433 3358 6864 4883 -416 1974 755 C ATOM 1926 C ALA A 433 88.200 47.473 14.980 1.00 41.58 C ANISOU 1926 C ALA A 433 3730 6932 5139 -330 2197 914 C ATOM 1927 O ALA A 433 88.817 46.768 14.185 1.00 44.37 O ANISOU 1927 O ALA A 433 4053 7332 5475 -265 2156 944 O ATOM 1928 CB ALA A 433 86.385 46.538 16.404 1.00 37.42 C ANISOU 1928 CB ALA A 433 3189 6569 4461 -161 1838 752 C ATOM 1929 N SER A 434 87.767 48.702 14.720 1.00 48.03 N ANISOU 1929 N SER A 434 4765 7472 6012 -341 2357 945 N ATOM 1930 CA SER A 434 87.960 49.397 13.460 1.00 43.63 C ANISOU 1930 CA SER A 434 4371 6735 5473 -278 2579 1146 C ATOM 1931 C SER A 434 89.425 49.520 13.131 1.00 55.44 C ANISOU 1931 C SER A 434 5723 8279 7062 -490 2723 1186 C ATOM 1932 O SER A 434 89.845 49.241 12.008 1.00 56.01 O ANISOU 1932 O SER A 434 5843 8395 7043 -409 2753 1286 O ATOM 1933 CB SER A 434 87.319 50.781 13.538 1.00 45.46 C ANISOU 1933 CB SER A 434 4818 6616 5837 -307 2698 1159 C ATOM 1934 OG SER A 434 87.172 51.347 12.251 1.00 62.07 O ANISOU 1934 OG SER A 434 7107 8555 7922 -178 2867 1423 O ATOM 1935 N GLN A 435 90.209 49.945 14.120 1.00 56.64 N ANISOU 1935 N GLN A 435 5719 8418 7382 -781 2742 1040 N ATOM 1936 CA GLN A 435 91.651 50.118 13.937 1.00 49.80 C ANISOU 1936 CA GLN A 435 4699 7594 6627 -1011 2832 1040 C ATOM 1937 C GLN A 435 92.352 48.774 13.751 1.00 47.46 C ANISOU 1937 C GLN A 435 4222 7568 6242 -962 2655 973 C ATOM 1938 O GLN A 435 93.326 48.695 13.014 1.00 55.71 O ANISOU 1938 O GLN A 435 5214 8645 7307 -1020 2737 1004 O ATOM 1939 CB GLN A 435 92.259 50.882 15.117 1.00 50.40 C ANISOU 1939 CB GLN A 435 4640 7596 6914 -1346 2869 863 C ATOM 1940 CG GLN A 435 91.794 52.325 15.209 1.00 52.54 C ANISOU 1940 CG GLN A 435 5119 7495 7347 -1440 3033 830 C ATOM 1941 CD GLN A 435 92.115 52.974 16.550 1.00 65.79 C ANISOU 1941 CD GLN A 435 6687 9126 9184 -1749 2983 539 C ATOM 1942 OE1 GLN A 435 93.264 53.320 16.826 1.00 64.68 O ANISOU 1942 OE1 GLN A 435 6374 9000 9202 -2030 3057 468 O ATOM 1943 NE2 GLN A 435 91.090 53.138 17.397 1.00 69.08 N ANISOU 1943 NE2 GLN A 435 7191 9507 9551 -1708 2860 347 N ATOM 1944 N CYS A 436 91.868 47.722 14.406 1.00 45.00 N ANISOU 1944 N CYS A 436 3826 7389 5881 -844 2426 873 N ATOM 1945 CA CYS A 436 92.436 46.400 14.198 1.00 43.99 C ANISOU 1945 CA CYS A 436 3559 7382 5772 -742 2263 824 C ATOM 1946 C CYS A 436 92.177 45.928 12.789 1.00 46.29 C ANISOU 1946 C CYS A 436 3980 7677 5933 -516 2315 902 C ATOM 1947 O CYS A 436 92.966 45.180 12.211 1.00 44.21 O ANISOU 1947 O CYS A 436 3606 7476 5715 -487 2312 864 O ATOM 1948 CB CYS A 436 91.855 45.389 15.163 1.00 41.67 C ANISOU 1948 CB CYS A 436 3173 7202 5458 -647 1969 761 C ATOM 1949 SG CYS A 436 92.257 45.722 16.853 1.00 42.37 S ANISOU 1949 SG CYS A 436 3089 7368 5641 -915 1829 665 S ATOM 1950 N LEU A 437 91.047 46.367 12.250 1.00 43.16 N ANISOU 1950 N LEU A 437 3807 7208 5384 -349 2361 1006 N ATOM 1951 CA LEU A 437 90.568 45.890 10.964 1.00 46.39 C ANISOU 1951 CA LEU A 437 4352 7640 5636 -114 2367 1079 C ATOM 1952 C LEU A 437 91.123 46.694 9.775 1.00 47.34 C ANISOU 1952 C LEU A 437 4587 7705 5696 -169 2608 1211 C ATOM 1953 O LEU A 437 90.649 46.555 8.641 1.00 47.65 O ANISOU 1953 O LEU A 437 4769 7769 5565 4 2640 1300 O ATOM 1954 CB LEU A 437 89.044 45.896 10.969 1.00 41.13 C ANISOU 1954 CB LEU A 437 3859 6930 4837 108 2264 1136 C ATOM 1955 CG LEU A 437 88.589 44.649 11.718 1.00 40.32 C ANISOU 1955 CG LEU A 437 3626 6937 4758 208 1996 1011 C ATOM 1956 CD1 LEU A 437 87.080 44.634 12.048 1.00 36.68 C ANISOU 1956 CD1 LEU A 437 3293 6446 4199 390 1869 1030 C ATOM 1957 CD2 LEU A 437 89.021 43.421 10.902 1.00 38.28 C ANISOU 1957 CD2 LEU A 437 3274 6777 4493 320 1919 953 C ATOM 1958 N HIS A 438 92.135 47.516 10.028 1.00 47.84 N ANISOU 1958 N HIS A 438 4575 7709 5893 -422 2765 1227 N ATOM 1959 CA HIS A 438 92.745 48.248 8.948 1.00 50.78 C ANISOU 1959 CA HIS A 438 5035 8038 6222 -498 2982 1368 C ATOM 1960 C HIS A 438 93.359 47.259 7.975 1.00 54.51 C ANISOU 1960 C HIS A 438 5423 8690 6600 -426 2993 1293 C ATOM 1961 O HIS A 438 93.940 46.249 8.380 1.00 56.88 O ANISOU 1961 O HIS A 438 5514 9095 7004 -439 2890 1114 O ATOM 1962 CB HIS A 438 93.794 49.226 9.456 1.00 53.17 C ANISOU 1962 CB HIS A 438 5235 8249 6718 -799 3124 1383 C ATOM 1963 CG HIS A 438 94.088 50.322 8.486 1.00 56.43 C ANISOU 1963 CG HIS A 438 5795 8528 7117 -873 3351 1600 C ATOM 1964 ND1 HIS A 438 94.597 50.082 7.230 1.00 63.56 N ANISOU 1964 ND1 HIS A 438 6722 9558 7871 -841 3458 1671 N ATOM 1965 CD2 HIS A 438 93.902 51.659 8.570 1.00 62.34 C ANISOU 1965 CD2 HIS A 438 6678 9007 8000 -978 3497 1765 C ATOM 1966 CE1 HIS A 438 94.734 51.226 6.584 1.00 66.54 C ANISOU 1966 CE1 HIS A 438 7239 9782 8262 -930 3644 1899 C ATOM 1967 NE2 HIS A 438 94.323 52.200 7.377 1.00 66.24 N ANISOU 1967 NE2 HIS A 438 7271 9476 8422 -1008 3670 1966 N ATOM 1968 N GLU A 439 93.201 47.542 6.687 1.00 56.11 N ANISOU 1968 N GLU A 439 5783 8916 6621 -345 3122 1433 N ATOM 1969 CA GLU A 439 93.686 46.660 5.635 1.00 54.30 C ANISOU 1969 CA GLU A 439 5489 8869 6273 -278 3170 1346 C ATOM 1970 C GLU A 439 95.195 46.727 5.519 1.00 56.46 C ANISOU 1970 C GLU A 439 5569 9210 6672 -507 3332 1268 C ATOM 1971 O GLU A 439 95.839 45.756 5.125 1.00 71.26 O ANISOU 1971 O GLU A 439 7283 11220 8572 -485 3351 1098 O ATOM 1972 CB GLU A 439 93.036 47.011 4.297 1.00 55.77 C ANISOU 1972 CB GLU A 439 5903 9100 6188 -149 3258 1525 C ATOM 1973 CG GLU A 439 91.556 46.695 4.247 1.00 59.49 C ANISOU 1973 CG GLU A 439 6529 9555 6520 109 3073 1568 C ATOM 1974 CD GLU A 439 91.267 45.211 4.457 1.00 62.95 C ANISOU 1974 CD GLU A 439 6830 10115 6974 268 2878 1333 C ATOM 1975 OE1 GLU A 439 92.025 44.381 3.903 1.00 70.35 O ANISOU 1975 OE1 GLU A 439 7626 11190 7914 249 2936 1179 O ATOM 1976 OE2 GLU A 439 90.291 44.869 5.170 1.00 53.85 O1+ ANISOU 1976 OE2 GLU A 439 5701 8909 5853 407 2678 1303 O1+ ATOM 1977 N LYS A 440 95.767 47.872 5.863 1.00 58.36 N ANISOU 1977 N LYS A 440 5810 9345 7019 -727 3453 1386 N ATOM 1978 CA LYS A 440 97.217 48.020 5.806 1.00 60.87 C ANISOU 1978 CA LYS A 440 5925 9742 7461 -960 3591 1325 C ATOM 1979 C LYS A 440 97.832 47.628 7.145 1.00 67.68 C ANISOU 1979 C LYS A 440 6537 10610 8568 -1083 3447 1145 C ATOM 1980 O LYS A 440 97.689 48.349 8.130 1.00 67.12 O ANISOU 1980 O LYS A 440 6467 10421 8614 -1202 3386 1191 O ATOM 1981 CB LYS A 440 97.588 49.454 5.431 1.00 64.17 C ANISOU 1981 CB LYS A 440 6449 10045 7889 -1145 3784 1566 C ATOM 1982 CG LYS A 440 97.085 49.871 4.061 1.00 66.28 C ANISOU 1982 CG LYS A 440 6952 10324 7908 -1049 3927 1778 C ATOM 1983 CD LYS A 440 97.625 51.236 3.669 1.00 84.27 C ANISOU 1983 CD LYS A 440 9303 12469 10246 -1254 4130 2032 C ATOM 1984 CE LYS A 440 97.607 51.457 2.144 1.00 87.92 C ANISOU 1984 CE LYS A 440 9919 13052 10436 -1227 4303 2220 C ATOM 1985 NZ LYS A 440 96.285 51.904 1.611 1.00 88.59 N1+ ANISOU 1985 NZ LYS A 440 10289 13026 10347 -1037 4257 2457 N1+ ATOM 1986 N LYS A 441 98.507 46.482 7.181 1.00 59.03 N ANISOU 1986 N LYS A 441 5221 9642 7566 -1056 3394 937 N ATOM 1987 CA LYS A 441 99.025 45.936 8.438 1.00 57.75 C ANISOU 1987 CA LYS A 441 4821 9476 7644 -1139 3224 774 C ATOM 1988 C LYS A 441 99.822 46.943 9.282 1.00 67.23 C ANISOU 1988 C LYS A 441 5915 10668 8961 -1413 3212 832 C ATOM 1989 O LYS A 441 99.678 46.975 10.503 1.00 66.93 O ANISOU 1989 O LYS A 441 5819 10565 9046 -1476 3040 769 O ATOM 1990 CB LYS A 441 99.894 44.707 8.162 1.00 66.60 C ANISOU 1990 CB LYS A 441 5713 10680 8912 -1073 3197 589 C ATOM 1991 CG LYS A 441 101.164 44.993 7.374 1.00 68.11 C ANISOU 1991 CG LYS A 441 5779 11016 9084 -1221 3369 585 C ATOM 1992 CD LYS A 441 102.056 43.765 7.367 1.00 69.78 C ANISOU 1992 CD LYS A 441 5727 11298 9488 -1163 3294 380 C ATOM 1993 CE LYS A 441 103.241 43.907 6.433 1.00 66.07 C ANISOU 1993 CE LYS A 441 5102 11074 8928 -1268 3452 390 C ATOM 1994 NZ LYS A 441 102.810 43.922 5.017 1.00 67.30 N1+ ANISOU 1994 NZ LYS A 441 5437 11258 8877 -1178 3690 391 N1+ ATOM 1995 N ASN A 442 100.660 47.758 8.645 1.00 71.93 N ANISOU 1995 N ASN A 442 6475 11327 9529 -1570 3389 972 N ATOM 1996 CA ASN A 442 101.440 48.761 9.372 1.00 64.70 C ANISOU 1996 CA ASN A 442 5432 10378 8773 -1808 3385 1098 C ATOM 1997 C ASN A 442 100.588 49.884 9.966 1.00 75.27 C ANISOU 1997 C ASN A 442 6957 11481 10159 -1871 3399 1219 C ATOM 1998 O ASN A 442 101.026 50.594 10.873 1.00 74.48 O ANISOU 1998 O ASN A 442 6755 11279 10264 -2052 3358 1249 O ATOM 1999 CB ASN A 442 102.496 49.358 8.461 1.00 68.50 C ANISOU 1999 CB ASN A 442 5841 10911 9274 -1948 3616 1229 C ATOM 2000 CG ASN A 442 103.363 48.305 7.835 1.00 81.65 C ANISOU 2000 CG ASN A 442 7318 12792 10915 -1869 3618 1106 C ATOM 2001 OD1 ASN A 442 103.431 47.177 8.331 1.00 77.49 O ANISOU 2001 OD1 ASN A 442 6655 12347 10441 -1756 3418 923 O ATOM 2002 ND2 ASN A 442 104.035 48.656 6.733 1.00 72.60 N ANISOU 2002 ND2 ASN A 442 6154 11730 9699 -1937 3854 1201 N ATOM 2003 N LYS A 443 99.370 50.047 9.461 1.00 62.93 N ANISOU 2003 N LYS A 443 5674 9789 8448 -1702 3453 1278 N ATOM 2004 CA LYS A 443 98.498 51.092 9.977 1.00 65.47 C ANISOU 2004 CA LYS A 443 6185 9842 8847 -1728 3477 1374 C ATOM 2005 C LYS A 443 97.733 50.605 11.193 1.00 59.65 C ANISOU 2005 C LYS A 443 5405 9130 8130 -1670 3259 1233 C ATOM 2006 O LYS A 443 97.043 51.388 11.831 1.00 59.48 O ANISOU 2006 O LYS A 443 5497 8899 8205 -1712 3272 1245 O ATOM 2007 CB LYS A 443 97.527 51.578 8.896 1.00 64.91 C ANISOU 2007 CB LYS A 443 6424 9618 8621 -1560 3621 1562 C ATOM 2008 CG LYS A 443 98.205 52.317 7.737 1.00 67.14 C ANISOU 2008 CG LYS A 443 6774 9856 8882 -1657 3852 1755 C ATOM 2009 CD LYS A 443 98.507 53.772 8.096 1.00 74.53 C ANISOU 2009 CD LYS A 443 7755 10481 10083 -1880 3990 1878 C ATOM 2010 CE LYS A 443 99.439 54.431 7.071 1.00 81.80 C ANISOU 2010 CE LYS A 443 8674 11392 11014 -2025 4206 2062 C ATOM 2011 NZ LYS A 443 98.958 54.341 5.658 1.00 75.00 N1+ ANISOU 2011 NZ LYS A 443 8012 10615 9871 -1864 4315 2263 N1+ ATOM 2012 N ARG A 444 97.870 49.316 11.513 1.00 61.88 N ANISOU 2012 N ARG A 444 5523 9644 8346 -1591 3078 1069 N ATOM 2013 CA ARG A 444 97.189 48.700 12.661 1.00 54.78 C ANISOU 2013 CA ARG A 444 4579 8778 7459 -1541 2857 917 C ATOM 2014 C ARG A 444 97.906 48.956 13.978 1.00 62.83 C ANISOU 2014 C ARG A 444 5349 9836 8687 -1672 2673 1000 C ATOM 2015 O ARG A 444 99.130 48.998 14.014 1.00 65.59 O ANISOU 2015 O ARG A 444 5506 10196 9220 -1771 2689 1058 O ATOM 2016 CB ARG A 444 97.062 47.188 12.473 1.00 52.58 C ANISOU 2016 CB ARG A 444 4256 8505 7215 -1320 2771 759 C ATOM 2017 CG ARG A 444 96.100 46.765 11.405 1.00 51.24 C ANISOU 2017 CG ARG A 444 4279 8349 6840 -1044 2791 855 C ATOM 2018 CD ARG A 444 96.026 45.263 11.290 1.00 49.40 C ANISOU 2018 CD ARG A 444 3939 8189 6642 -829 2624 764 C ATOM 2019 NE ARG A 444 95.830 44.894 9.896 1.00 52.91 N ANISOU 2019 NE ARG A 444 4490 8689 6924 -659 2726 802 N ATOM 2020 CZ ARG A 444 96.276 43.774 9.340 1.00 50.14 C ANISOU 2020 CZ ARG A 444 4006 8418 6626 -549 2700 699 C ATOM 2021 NH1 ARG A 444 96.933 42.884 10.067 1.00 49.53 N1+ ANISOU 2021 NH1 ARG A 444 3686 8352 6783 -571 2555 584 N1+ ATOM 2022 NH2 ARG A 444 96.061 43.548 8.052 1.00 50.81 N ANISOU 2022 NH2 ARG A 444 4197 8566 6542 -421 2818 715 N ATOM 2023 N PRO A 445 97.141 49.095 15.071 1.00 63.19 N ANISOU 2023 N PRO A 445 5414 9715 8880 -1644 2615 961 N ATOM 2024 CA PRO A 445 97.720 49.188 16.415 1.00 55.12 C ANISOU 2024 CA PRO A 445 4214 8693 8038 -1866 2474 794 C ATOM 2025 C PRO A 445 98.484 47.917 16.768 1.00 54.52 C ANISOU 2025 C PRO A 445 3932 8698 8086 -1796 2293 725 C ATOM 2026 O PRO A 445 98.068 46.836 16.355 1.00 52.44 O ANISOU 2026 O PRO A 445 3707 8465 7752 -1586 2235 685 O ATOM 2027 CB PRO A 445 96.490 49.336 17.332 1.00 53.40 C ANISOU 2027 CB PRO A 445 4122 8493 7677 -1884 2354 638 C ATOM 2028 CG PRO A 445 95.315 49.609 16.419 1.00 56.22 C ANISOU 2028 CG PRO A 445 4721 8760 7881 -1698 2521 743 C ATOM 2029 CD PRO A 445 95.669 48.998 15.101 1.00 58.36 C ANISOU 2029 CD PRO A 445 5007 9069 8098 -1482 2596 930 C ATOM 2030 N ASP A 446 99.570 48.033 17.521 1.00 56.55 N ANISOU 2030 N ASP A 446 3981 9007 8497 -1995 2179 672 N ATOM 2031 CA ASP A 446 100.176 46.849 18.111 1.00 59.94 C ANISOU 2031 CA ASP A 446 4218 9541 9017 -1951 1941 600 C ATOM 2032 C ASP A 446 99.323 46.404 19.310 1.00 57.88 C ANISOU 2032 C ASP A 446 3995 9431 8565 -1951 1650 509 C ATOM 2033 O ASP A 446 98.507 47.181 19.817 1.00 56.76 O ANISOU 2033 O ASP A 446 3985 9312 8270 -2051 1655 445 O ATOM 2034 CB ASP A 446 101.629 47.113 18.521 1.00 59.23 C ANISOU 2034 CB ASP A 446 3887 9460 9157 -2150 1908 596 C ATOM 2035 CG ASP A 446 101.773 48.271 19.496 1.00 74.85 C ANISOU 2035 CG ASP A 446 5857 11477 11105 -2443 1851 504 C ATOM 2036 OD1 ASP A 446 101.033 48.307 20.495 1.00 76.45 O ANISOU 2036 OD1 ASP A 446 6129 11787 11130 -2506 1674 378 O ATOM 2037 OD2 ASP A 446 102.636 49.149 19.276 1.00 80.03 O1+ ANISOU 2037 OD2 ASP A 446 6438 12068 11904 -2627 1984 533 O1+ ATOM 2038 N ILE A 447 99.512 45.172 19.772 1.00 53.52 N ANISOU 2038 N ILE A 447 3328 8984 8024 -1847 1405 503 N ATOM 2039 CA ILE A 447 98.645 44.630 20.815 1.00 57.88 C ANISOU 2039 CA ILE A 447 3931 9690 8369 -1812 1133 482 C ATOM 2040 C ILE A 447 98.666 45.455 22.104 1.00 60.99 C ANISOU 2040 C ILE A 447 4306 10219 8650 -2074 1017 381 C ATOM 2041 O ILE A 447 97.711 45.416 22.885 1.00 61.45 O ANISOU 2041 O ILE A 447 4462 10408 8479 -2085 881 336 O ATOM 2042 CB ILE A 447 99.012 43.178 21.158 1.00 51.44 C ANISOU 2042 CB ILE A 447 2984 8941 7618 -1677 885 531 C ATOM 2043 CG1 ILE A 447 97.922 42.561 22.026 1.00 60.99 C ANISOU 2043 CG1 ILE A 447 4296 10283 8596 -1598 647 566 C ATOM 2044 CG2 ILE A 447 100.324 43.124 21.883 1.00 54.23 C ANISOU 2044 CG2 ILE A 447 3115 9354 8137 -1842 765 511 C ATOM 2045 CD1 ILE A 447 96.496 42.714 21.467 1.00 46.93 C ANISOU 2045 CD1 ILE A 447 2731 8461 6638 -1448 744 574 C ATOM 2046 N LYS A 448 99.733 46.218 22.316 1.00 56.42 N ANISOU 2046 N LYS A 448 3600 9618 8220 -2295 1080 324 N ATOM 2047 CA LYS A 448 99.881 46.970 23.550 1.00 58.55 C ANISOU 2047 CA LYS A 448 3833 10033 8379 -2568 961 176 C ATOM 2048 C LYS A 448 99.005 48.220 23.554 1.00 60.71 C ANISOU 2048 C LYS A 448 4290 10243 8535 -2705 1142 25 C ATOM 2049 O LYS A 448 98.472 48.591 24.602 1.00 59.23 O ANISOU 2049 O LYS A 448 4148 10207 8148 -2858 1032 -146 O ATOM 2050 CB LYS A 448 101.350 47.356 23.794 1.00 69.92 C ANISOU 2050 CB LYS A 448 5063 11466 10038 -2768 951 146 C ATOM 2051 CG LYS A 448 102.348 46.185 23.703 1.00 74.93 C ANISOU 2051 CG LYS A 448 5489 12115 10865 -2641 812 269 C ATOM 2052 CD LYS A 448 102.670 45.820 22.232 1.00 74.01 C ANISOU 2052 CD LYS A 448 5354 11787 10978 -2445 1045 373 C ATOM 2053 CE LYS A 448 103.347 44.444 22.090 1.00 76.16 C ANISOU 2053 CE LYS A 448 5453 12062 11421 -2275 915 425 C ATOM 2054 NZ LYS A 448 103.672 44.082 20.662 1.00 72.51 N1+ ANISOU 2054 NZ LYS A 448 4969 11427 11154 -2110 1162 452 N1+ ATOM 2055 N LYS A 449 98.843 48.885 22.411 1.00 58.40 N ANISOU 2055 N LYS A 449 4105 9723 8362 -2658 1433 72 N ATOM 2056 CA LYS A 449 97.949 50.041 22.415 1.00 61.23 C ANISOU 2056 CA LYS A 449 4649 9966 8648 -2776 1616 -81 C ATOM 2057 C LYS A 449 96.491 49.556 22.299 1.00 58.43 C ANISOU 2057 C LYS A 449 4462 9651 8088 -2560 1594 -53 C ATOM 2058 O LYS A 449 95.551 50.281 22.629 1.00 55.54 O ANISOU 2058 O LYS A 449 4234 9242 7629 -2641 1680 -220 O ATOM 2059 CB LYS A 449 98.305 51.038 21.310 1.00 60.22 C ANISOU 2059 CB LYS A 449 4598 9561 8722 -2826 1937 -21 C ATOM 2060 CG LYS A 449 97.808 50.664 19.953 1.00 71.78 C ANISOU 2060 CG LYS A 449 6189 10908 10176 -2547 2111 209 C ATOM 2061 CD LYS A 449 98.500 51.488 18.858 1.00 79.23 C ANISOU 2061 CD LYS A 449 7168 11643 11294 -2604 2386 336 C ATOM 2062 CE LYS A 449 100.036 51.370 18.931 1.00 78.97 C ANISOU 2062 CE LYS A 449 6894 11669 11442 -2733 2333 380 C ATOM 2063 NZ LYS A 449 100.670 51.486 17.604 1.00 63.81 N1+ ANISOU 2063 NZ LYS A 449 4972 9673 9600 -2657 2543 601 N1+ ATOM 2064 N VAL A 450 96.318 48.316 21.849 1.00 55.56 N ANISOU 2064 N VAL A 450 4076 9350 7683 -2289 1481 131 N ATOM 2065 CA VAL A 450 95.029 47.651 21.931 1.00 50.30 C ANISOU 2065 CA VAL A 450 3529 8764 6821 -2086 1383 162 C ATOM 2066 C VAL A 450 94.655 47.494 23.403 1.00 57.11 C ANISOU 2066 C VAL A 450 4352 9865 7482 -2223 1137 21 C ATOM 2067 O VAL A 450 93.538 47.811 23.816 1.00 57.24 O ANISOU 2067 O VAL A 450 4485 9932 7331 -2233 1150 -94 O ATOM 2068 CB VAL A 450 95.048 46.268 21.248 1.00 61.50 C ANISOU 2068 CB VAL A 450 4915 10187 8266 -1794 1280 345 C ATOM 2069 CG1 VAL A 450 93.733 45.513 21.502 1.00 45.45 C ANISOU 2069 CG1 VAL A 450 2988 8247 6036 -1601 1128 373 C ATOM 2070 CG2 VAL A 450 95.327 46.402 19.761 1.00 48.03 C ANISOU 2070 CG2 VAL A 450 3265 8287 6696 -1655 1541 452 C ATOM 2071 N GLN A 451 95.604 47.004 24.195 1.00 61.11 N ANISOU 2071 N GLN A 451 4694 10527 7997 -2328 923 33 N ATOM 2072 CA GLN A 451 95.412 46.905 25.639 1.00 59.95 C ANISOU 2072 CA GLN A 451 4510 10648 7621 -2486 698 -82 C ATOM 2073 C GLN A 451 95.089 48.246 26.266 1.00 55.25 C ANISOU 2073 C GLN A 451 3975 10081 6935 -2765 822 -379 C ATOM 2074 O GLN A 451 94.184 48.345 27.081 1.00 65.11 O ANISOU 2074 O GLN A 451 5293 11499 7948 -2825 758 -521 O ATOM 2075 CB GLN A 451 96.652 46.347 26.306 1.00 55.21 C ANISOU 2075 CB GLN A 451 3722 10182 7072 -2574 491 -11 C ATOM 2076 CG GLN A 451 96.595 44.895 26.644 1.00 57.34 C ANISOU 2076 CG GLN A 451 3948 10564 7277 -2381 247 196 C ATOM 2077 CD GLN A 451 97.919 44.426 27.189 1.00 60.84 C ANISOU 2077 CD GLN A 451 4194 11090 7833 -2466 82 271 C ATOM 2078 OE1 GLN A 451 98.971 44.739 26.631 1.00 64.10 O ANISOU 2078 OE1 GLN A 451 4486 11367 8503 -2517 180 259 O ATOM 2079 NE2 GLN A 451 97.883 43.696 28.298 1.00 64.42 N ANISOU 2079 NE2 GLN A 451 4610 11770 8098 -2488 -158 358 N ATOM 2080 N GLN A 452 95.845 49.271 25.891 1.00 57.45 N ANISOU 2080 N GLN A 452 4225 10181 7421 -2942 1012 -491 N ATOM 2081 CA GLN A 452 95.655 50.598 26.460 1.00 68.16 C ANISOU 2081 CA GLN A 452 5635 11496 8766 -3227 1152 -824 C ATOM 2082 C GLN A 452 94.268 51.146 26.133 1.00 66.60 C ANISOU 2082 C GLN A 452 5627 11147 8532 -3161 1355 -951 C ATOM 2083 O GLN A 452 93.621 51.754 26.986 1.00 66.45 O ANISOU 2083 O GLN A 452 5655 11210 8385 -3330 1377 -1251 O ATOM 2084 CB GLN A 452 96.738 51.569 25.967 1.00 62.70 C ANISOU 2084 CB GLN A 452 4888 10567 8368 -3406 1339 -887 C ATOM 2085 CG GLN A 452 98.123 51.250 26.487 1.00 77.66 C ANISOU 2085 CG GLN A 452 6573 12618 10315 -3528 1150 -837 C ATOM 2086 CD GLN A 452 99.189 52.189 25.943 1.00 82.54 C ANISOU 2086 CD GLN A 452 7125 12997 11241 -3695 1337 -878 C ATOM 2087 OE1 GLN A 452 99.639 52.051 24.797 1.00 79.16 O ANISOU 2087 OE1 GLN A 452 6684 12373 11020 -3556 1481 -652 O ATOM 2088 NE2 GLN A 452 99.606 53.147 26.767 1.00 82.91 N ANISOU 2088 NE2 GLN A 452 7126 13066 11309 -3998 1342 -1174 N ATOM 2089 N LEU A 453 93.804 50.921 24.907 1.00 56.18 N ANISOU 2089 N LEU A 453 4410 9613 7321 -2910 1511 -737 N ATOM 2090 CA LEU A 453 92.529 51.477 24.490 1.00 55.10 C ANISOU 2090 CA LEU A 453 4455 9289 7190 -2824 1729 -826 C ATOM 2091 C LEU A 453 91.357 50.777 25.190 1.00 55.69 C ANISOU 2091 C LEU A 453 4561 9611 6989 -2705 1559 -865 C ATOM 2092 O LEU A 453 90.374 51.427 25.562 1.00 57.36 O ANISOU 2092 O LEU A 453 4862 9771 7160 -2767 1687 -1106 O ATOM 2093 CB LEU A 453 92.394 51.402 22.971 1.00 53.47 C ANISOU 2093 CB LEU A 453 4363 8820 7134 -2575 1936 -556 C ATOM 2094 CG LEU A 453 93.332 52.349 22.212 1.00 55.91 C ANISOU 2094 CG LEU A 453 4688 8830 7725 -2705 2177 -525 C ATOM 2095 CD1 LEU A 453 93.359 52.033 20.725 1.00 54.50 C ANISOU 2095 CD1 LEU A 453 4603 8490 7612 -2444 2333 -205 C ATOM 2096 CD2 LEU A 453 92.928 53.799 22.437 1.00 58.47 C ANISOU 2096 CD2 LEU A 453 5133 8843 8240 -2913 2427 -800 C ATOM 2097 N LEU A 454 91.465 49.465 25.392 1.00 51.21 N ANISOU 2097 N LEU A 454 3913 9280 6264 -2536 1285 -639 N ATOM 2098 CA LEU A 454 90.416 48.724 26.101 1.00 55.70 C ANISOU 2098 CA LEU A 454 4506 10082 6574 -2428 1104 -637 C ATOM 2099 C LEU A 454 90.462 48.993 27.615 1.00 61.32 C ANISOU 2099 C LEU A 454 5149 11090 7059 -2707 964 -894 C ATOM 2100 O LEU A 454 89.438 48.905 28.296 1.00 59.83 O ANISOU 2100 O LEU A 454 5005 11071 6657 -2708 922 -1017 O ATOM 2101 CB LEU A 454 90.517 47.216 25.835 1.00 47.16 C ANISOU 2101 CB LEU A 454 3378 9095 5446 -2163 867 -311 C ATOM 2102 CG LEU A 454 90.425 46.680 24.401 1.00 44.81 C ANISOU 2102 CG LEU A 454 3139 8571 5314 -1861 960 -74 C ATOM 2103 CD1 LEU A 454 90.735 45.206 24.402 1.00 43.35 C ANISOU 2103 CD1 LEU A 454 2879 8469 5122 -1676 709 153 C ATOM 2104 CD2 LEU A 454 89.065 46.920 23.778 1.00 42.98 C ANISOU 2104 CD2 LEU A 454 3070 8216 5044 -1667 1118 -83 C ATOM 2105 N GLN A 455 91.637 49.324 28.151 1.00 66.08 N ANISOU 2105 N GLN A 455 5643 11774 7690 -2940 899 -981 N ATOM 2106 CA GLN A 455 91.706 49.722 29.556 1.00 69.53 C ANISOU 2106 CA GLN A 455 6029 12505 7884 -3220 802 -1261 C ATOM 2107 C GLN A 455 91.035 51.096 29.718 1.00 71.29 C ANISOU 2107 C GLN A 455 6336 12578 8174 -3416 1069 -1689 C ATOM 2108 O GLN A 455 90.165 51.271 30.587 1.00 60.21 O ANISOU 2108 O GLN A 455 4962 11376 6540 -3507 1065 -1936 O ATOM 2109 CB GLN A 455 93.154 49.718 30.072 1.00 60.32 C ANISOU 2109 CB GLN A 455 4720 11462 6737 -3402 663 -1239 C ATOM 2110 CG GLN A 455 93.632 48.314 30.532 1.00 71.31 C ANISOU 2110 CG GLN A 455 6018 13101 7976 -3267 363 -900 C ATOM 2111 CD GLN A 455 95.137 48.237 30.880 1.00 84.25 C ANISOU 2111 CD GLN A 455 7493 14812 9707 -3405 237 -832 C ATOM 2112 OE1 GLN A 455 95.629 48.976 31.741 1.00 86.98 O ANISOU 2112 OE1 GLN A 455 7778 15320 9950 -3684 229 -1079 O ATOM 2113 NE2 GLN A 455 95.866 47.328 30.209 1.00 72.96 N ANISOU 2113 NE2 GLN A 455 5980 13257 8486 -3206 144 -519 N ATOM 2114 N GLU A 456 91.392 52.043 28.850 1.00 60.21 N ANISOU 2114 N GLU A 456 4975 10793 7111 -3468 1323 -1772 N ATOM 2115 CA GLU A 456 90.771 53.367 28.850 1.00 62.13 C ANISOU 2115 CA GLU A 456 5308 10761 7537 -3624 1618 -2159 C ATOM 2116 C GLU A 456 89.251 53.296 28.667 1.00 68.04 C ANISOU 2116 C GLU A 456 6180 11439 8235 -3430 1735 -2204 C ATOM 2117 O GLU A 456 88.509 54.170 29.128 1.00 61.89 O ANISOU 2117 O GLU A 456 5510 10507 7497 -3489 1877 -2559 O ATOM 2118 CB GLU A 456 91.388 54.239 27.763 1.00 63.09 C ANISOU 2118 CB GLU A 456 5480 10417 8074 -3648 1879 -2115 C ATOM 2119 CG GLU A 456 92.852 54.533 28.009 1.00 72.28 C ANISOU 2119 CG GLU A 456 6522 11609 9330 -3859 1799 -2139 C ATOM 2120 CD GLU A 456 93.508 55.308 26.874 1.00 76.66 C ANISOU 2120 CD GLU A 456 7124 11714 10288 -3867 2051 -2031 C ATOM 2121 OE1 GLU A 456 92.972 55.261 25.737 1.00 74.16 O ANISOU 2121 OE1 GLU A 456 6933 11126 10120 -3642 2235 -1796 O ATOM 2122 OE2 GLU A 456 94.552 55.962 27.131 1.00 70.00 O1+ ANISOU 2122 OE2 GLU A 456 6197 10801 9600 -4093 2065 -2166 O1+ ATOM 2123 N MET A 457 88.801 52.236 28.007 1.00 65.48 N ANISOU 2123 N MET A 457 5898 11161 7820 -3106 1632 -1825 N ATOM 2124 CA MET A 457 87.381 52.013 27.735 1.00 58.63 C ANISOU 2124 CA MET A 457 5217 10172 6888 -2790 1669 -1773 C ATOM 2125 C MET A 457 86.545 51.944 29.018 1.00 55.50 C ANISOU 2125 C MET A 457 4775 10109 6204 -2917 1586 -2060 C ATOM 2126 O MET A 457 85.351 52.251 28.999 1.00 55.66 O ANISOU 2126 O MET A 457 4950 9961 6237 -2742 1693 -2186 O ATOM 2127 CB MET A 457 87.223 50.731 26.922 1.00 55.05 C ANISOU 2127 CB MET A 457 4757 9794 6367 -2476 1528 -1336 C ATOM 2128 CG MET A 457 85.877 50.515 26.279 1.00 48.18 C ANISOU 2128 CG MET A 457 4088 8716 5502 -2109 1581 -1222 C ATOM 2129 SD MET A 457 85.795 48.817 25.624 1.00 47.66 S ANISOU 2129 SD MET A 457 3936 8857 5318 -1817 1360 -778 S ATOM 2130 CE MET A 457 86.082 47.866 27.117 1.00 52.43 C ANISOU 2130 CE MET A 457 4335 9961 5623 -2018 1033 -783 C ATOM 2131 N THR A 458 87.179 51.568 30.130 1.00 56.89 N ANISOU 2131 N THR A 458 4745 10755 6117 -3213 1392 -2155 N ATOM 2132 CA THR A 458 86.466 51.383 31.395 1.00 61.74 C ANISOU 2132 CA THR A 458 5324 11756 6379 -3334 1286 -2380 C ATOM 2133 C THR A 458 87.047 52.200 32.565 1.00 69.59 C ANISOU 2133 C THR A 458 6253 12957 7233 -3710 1295 -2806 C ATOM 2134 O THR A 458 87.823 53.157 32.380 1.00 72.18 O ANISOU 2134 O THR A 458 6571 13039 7813 -3890 1433 -3018 O ATOM 2135 CB THR A 458 86.439 49.879 31.797 1.00 67.54 C ANISOU 2135 CB THR A 458 6022 12847 6791 -3171 956 -1979 C ATOM 2136 OG1 THR A 458 87.692 49.496 32.373 1.00 70.44 O ANISOU 2136 OG1 THR A 458 6304 13435 7027 -3309 752 -1845 O ATOM 2137 CG2 THR A 458 86.177 49.000 30.595 1.00 52.19 C ANISOU 2137 CG2 THR A 458 4135 10674 5020 -2803 908 -1555 C TER 2138 THR A 458 ATOM 2139 N HIS B 166 79.238 25.463 -35.181 1.00112.12 N ANISOU 2139 N HIS B 166 7585 15731 19284 -3576 -3827 -1200 N ATOM 2140 CA HIS B 166 79.826 24.403 -35.998 1.00117.23 C ANISOU 2140 CA HIS B 166 8797 16046 19699 -3673 -4293 -1235 C ATOM 2141 C HIS B 166 80.159 23.140 -35.183 1.00117.88 C ANISOU 2141 C HIS B 166 9415 15687 19686 -4475 -3947 -1198 C ATOM 2142 O HIS B 166 80.353 23.214 -33.968 1.00117.28 O ANISOU 2142 O HIS B 166 9445 15476 19638 -4800 -3348 -1017 O ATOM 2143 CB HIS B 166 81.090 24.914 -36.696 1.00105.21 C ANISOU 2143 CB HIS B 166 7843 14234 17897 -2970 -4580 -902 C ATOM 2144 CG HIS B 166 81.573 24.018 -37.794 1.00105.35 C ANISOU 2144 CG HIS B 166 8383 14052 17594 -2839 -5170 -963 C ATOM 2145 ND1 HIS B 166 82.367 22.915 -37.561 1.00102.94 N ANISOU 2145 ND1 HIS B 166 8805 13266 17041 -3272 -5143 -859 N ATOM 2146 CD2 HIS B 166 81.356 24.050 -39.130 1.00110.03 C ANISOU 2146 CD2 HIS B 166 8889 14886 18032 -2269 -5799 -1131 C ATOM 2147 CE1 HIS B 166 82.624 22.312 -38.709 1.00104.78 C ANISOU 2147 CE1 HIS B 166 9369 13428 17016 -3014 -5742 -970 C ATOM 2148 NE2 HIS B 166 82.022 22.979 -39.677 1.00108.13 N ANISOU 2148 NE2 HIS B 166 9327 14307 17451 -2392 -6100 -1136 N ATOM 2149 N SER B 167 80.227 21.988 -35.858 1.00122.69 N ANISOU 2149 N SER B 167 10393 16072 20153 -4728 -4301 -1378 N ATOM 2150 CA SER B 167 80.544 20.706 -35.209 1.00122.47 C ANISOU 2150 CA SER B 167 10960 15535 20038 -5421 -3987 -1347 C ATOM 2151 C SER B 167 81.590 19.891 -35.985 1.00118.48 C ANISOU 2151 C SER B 167 11286 14549 19182 -5250 -4442 -1225 C ATOM 2152 O SER B 167 81.579 19.868 -37.218 1.00112.80 O ANISOU 2152 O SER B 167 10544 13977 18338 -4832 -5044 -1398 O ATOM 2153 CB SER B 167 79.280 19.863 -35.038 1.00123.37 C ANISOU 2153 CB SER B 167 10673 15829 20374 -6159 -3780 -1785 C ATOM 2154 OG SER B 167 79.238 18.837 -36.011 1.00127.17 O ANISOU 2154 OG SER B 167 11421 16128 20769 -6314 -4218 -2078 O ATOM 2155 N PHE B 168 82.470 19.202 -35.258 1.00112.19 N ANISOU 2155 N PHE B 168 11249 13222 18156 -5525 -4146 -928 N ATOM 2156 CA PHE B 168 83.596 18.493 -35.873 1.00105.47 C ANISOU 2156 CA PHE B 168 11288 11933 16851 -5297 -4543 -754 C ATOM 2157 C PHE B 168 83.582 16.980 -35.684 1.00112.78 C ANISOU 2157 C PHE B 168 12835 12328 17686 -5870 -4389 -847 C ATOM 2158 O PHE B 168 82.834 16.441 -34.864 1.00116.79 O ANISOU 2158 O PHE B 168 13179 12709 18487 -6507 -3847 -973 O ATOM 2159 CB PHE B 168 84.919 19.022 -35.324 1.00100.30 C ANISOU 2159 CB PHE B 168 11194 11171 15742 -4837 -4293 -311 C ATOM 2160 CG PHE B 168 85.173 20.462 -35.634 1.00 94.57 C ANISOU 2160 CG PHE B 168 10070 10855 15008 -4158 -4342 -211 C ATOM 2161 CD1 PHE B 168 84.679 21.461 -34.808 1.00 95.50 C ANISOU 2161 CD1 PHE B 168 9563 11275 15447 -4200 -3885 -186 C ATOM 2162 CD2 PHE B 168 85.916 20.822 -36.741 1.00 90.06 C ANISOU 2162 CD2 PHE B 168 9789 10329 14102 -3468 -4793 -132 C ATOM 2163 CE1 PHE B 168 84.915 22.803 -35.086 1.00 91.63 C ANISOU 2163 CE1 PHE B 168 8778 11069 14968 -3579 -3860 -96 C ATOM 2164 CE2 PHE B 168 86.158 22.157 -37.025 1.00 91.67 C ANISOU 2164 CE2 PHE B 168 9704 10815 14312 -2858 -4734 -13 C ATOM 2165 CZ PHE B 168 85.652 23.150 -36.197 1.00 86.80 C ANISOU 2165 CZ PHE B 168 8499 10440 14042 -2921 -4257 -1 C ATOM 2166 N SER B 169 84.437 16.310 -36.452 1.00113.66 N ANISOU 2166 N SER B 169 13698 12110 17378 -5595 -4829 -780 N ATOM 2167 CA SER B 169 84.678 14.881 -36.296 1.00121.35 C ANISOU 2167 CA SER B 169 15466 12475 18166 -6006 -4685 -789 C ATOM 2168 C SER B 169 85.799 14.647 -35.301 1.00123.00 C ANISOU 2168 C SER B 169 16550 12281 17904 -5966 -4321 -307 C ATOM 2169 O SER B 169 86.835 15.310 -35.355 1.00116.97 O ANISOU 2169 O SER B 169 16030 11735 16679 -5262 -4396 -43 O ATOM 2170 CB SER B 169 85.036 14.232 -37.630 1.00121.29 C ANISOU 2170 CB SER B 169 15864 12340 17881 -5664 -5327 -984 C ATOM 2171 OG SER B 169 85.502 12.908 -37.425 1.00123.48 O ANISOU 2171 OG SER B 169 17066 11963 17887 -5942 -5166 -909 O ATOM 2172 N PHE B 170 85.595 13.699 -34.396 1.00131.87 N ANISOU 2172 N PHE B 170 18118 12943 19045 -6508 -3736 -221 N ATOM 2173 CA PHE B 170 86.596 13.417 -33.380 1.00133.42 C ANISOU 2173 CA PHE B 170 19152 12864 18676 -6301 -3256 223 C ATOM 2174 C PHE B 170 87.890 12.915 -34.014 1.00127.78 C ANISOU 2174 C PHE B 170 19375 11935 17240 -5652 -3654 381 C ATOM 2175 O PHE B 170 88.986 13.250 -33.555 1.00123.80 O ANISOU 2175 O PHE B 170 19275 11610 16151 -5048 -3503 672 O ATOM 2176 CB PHE B 170 86.067 12.394 -32.375 1.00144.40 C ANISOU 2176 CB PHE B 170 20951 13705 20209 -7012 -2557 311 C ATOM 2177 CG PHE B 170 87.014 12.110 -31.244 1.00145.10 C ANISOU 2177 CG PHE B 170 21877 13606 19648 -6668 -1987 772 C ATOM 2178 CD1 PHE B 170 86.979 12.870 -30.086 1.00143.90 C ANISOU 2178 CD1 PHE B 170 21345 13845 19486 -6582 -1435 971 C ATOM 2179 CD2 PHE B 170 87.937 11.082 -31.339 1.00146.87 C ANISOU 2179 CD2 PHE B 170 23263 13317 19225 -6353 -2009 977 C ATOM 2180 CE1 PHE B 170 87.847 12.607 -29.043 1.00143.36 C ANISOU 2180 CE1 PHE B 170 22004 13710 18756 -6171 -931 1340 C ATOM 2181 CE2 PHE B 170 88.809 10.816 -30.301 1.00145.91 C ANISOU 2181 CE2 PHE B 170 23898 13120 18420 -5909 -1498 1374 C ATOM 2182 CZ PHE B 170 88.763 11.580 -29.151 1.00144.29 C ANISOU 2182 CZ PHE B 170 23269 13362 18194 -5809 -965 1543 C ATOM 2183 N TYR B 171 87.762 12.124 -35.075 1.00127.46 N ANISOU 2183 N TYR B 171 19632 11565 17232 -5765 -4172 136 N ATOM 2184 CA TYR B 171 88.929 11.517 -35.702 1.00122.14 C ANISOU 2184 CA TYR B 171 19889 10652 15868 -5175 -4555 264 C ATOM 2185 C TYR B 171 89.687 12.496 -36.598 1.00114.33 C ANISOU 2185 C TYR B 171 18631 10222 14587 -4373 -5116 280 C ATOM 2186 O TYR B 171 90.917 12.450 -36.666 1.00112.06 O ANISOU 2186 O TYR B 171 18973 9984 13621 -3731 -5209 505 O ATOM 2187 CB TYR B 171 88.517 10.267 -36.479 1.00128.83 C ANISOU 2187 CB TYR B 171 21126 10991 16832 -5506 -4801 -22 C ATOM 2188 CG TYR B 171 88.502 9.036 -35.595 1.00136.35 C ANISOU 2188 CG TYR B 171 22898 11268 17641 -5892 -4133 145 C ATOM 2189 CD1 TYR B 171 87.602 8.926 -34.541 1.00141.44 C ANISOU 2189 CD1 TYR B 171 23205 11782 18755 -6544 -3387 164 C ATOM 2190 CD2 TYR B 171 89.404 7.998 -35.794 1.00137.47 C ANISOU 2190 CD2 TYR B 171 24157 10934 17142 -5521 -4198 308 C ATOM 2191 CE1 TYR B 171 87.589 7.809 -33.715 1.00147.77 C ANISOU 2191 CE1 TYR B 171 24777 11957 19412 -6814 -2696 360 C ATOM 2192 CE2 TYR B 171 89.399 6.877 -34.975 1.00144.56 C ANISOU 2192 CE2 TYR B 171 25837 11224 17867 -5763 -3521 496 C ATOM 2193 CZ TYR B 171 88.489 6.787 -33.936 1.00149.98 C ANISOU 2193 CZ TYR B 171 26188 11751 19046 -6408 -2757 533 C ATOM 2194 OH TYR B 171 88.477 5.674 -33.119 1.00155.96 O ANISOU 2194 OH TYR B 171 27732 11895 19630 -6581 -2032 751 O ATOM 2195 N GLU B 172 88.970 13.393 -37.268 1.00110.16 N ANISOU 2195 N GLU B 172 17183 10134 14541 -4374 -5448 43 N ATOM 2196 CA GLU B 172 89.639 14.461 -38.003 1.00 98.77 C ANISOU 2196 CA GLU B 172 15481 9190 12856 -3614 -5819 121 C ATOM 2197 C GLU B 172 90.398 15.349 -37.026 1.00 90.72 C ANISOU 2197 C GLU B 172 14421 8465 11583 -3293 -5304 422 C ATOM 2198 O GLU B 172 91.481 15.853 -37.336 1.00 83.44 O ANISOU 2198 O GLU B 172 13734 7777 10193 -2654 -5426 566 O ATOM 2199 CB GLU B 172 88.644 15.291 -38.817 1.00101.94 C ANISOU 2199 CB GLU B 172 14930 10003 13798 -3609 -6186 -158 C ATOM 2200 CG GLU B 172 88.341 14.727 -40.202 1.00104.71 C ANISOU 2200 CG GLU B 172 15272 10379 14134 -3369 -6717 -437 C ATOM 2201 CD GLU B 172 87.720 15.759 -41.128 1.00103.30 C ANISOU 2201 CD GLU B 172 14269 10770 14209 -2922 -6974 -601 C ATOM 2202 OE1 GLU B 172 87.458 16.891 -40.672 1.00 97.72 O ANISOU 2202 OE1 GLU B 172 13005 10378 13747 -2866 -6789 -507 O ATOM 2203 OE2 GLU B 172 87.498 15.442 -42.315 1.00109.11 O1+ ANISOU 2203 OE2 GLU B 172 14942 11642 14876 -2590 -7332 -823 O1+ ATOM 2204 N LEU B 173 89.822 15.530 -35.839 1.00 90.71 N ANISOU 2204 N LEU B 173 14096 8475 11896 -3755 -4710 472 N ATOM 2205 CA LEU B 173 90.472 16.293 -34.783 1.00 86.19 C ANISOU 2205 CA LEU B 173 13460 8195 11094 -3503 -4186 683 C ATOM 2206 C LEU B 173 91.672 15.523 -34.250 1.00 85.86 C ANISOU 2206 C LEU B 173 14360 7971 10293 -3182 -4002 892 C ATOM 2207 O LEU B 173 92.745 16.098 -34.035 1.00 76.23 O ANISOU 2207 O LEU B 173 13259 7093 8612 -2638 -3912 979 O ATOM 2208 CB LEU B 173 89.496 16.604 -33.650 1.00 85.78 C ANISOU 2208 CB LEU B 173 12832 8218 11541 -4056 -3611 670 C ATOM 2209 CG LEU B 173 88.633 17.846 -33.840 1.00 85.47 C ANISOU 2209 CG LEU B 173 11772 8598 12105 -4111 -3636 513 C ATOM 2210 CD1 LEU B 173 87.814 18.129 -32.598 1.00 88.02 C ANISOU 2210 CD1 LEU B 173 11588 9033 12823 -4597 -3023 518 C ATOM 2211 CD2 LEU B 173 89.512 19.020 -34.171 1.00 79.36 C ANISOU 2211 CD2 LEU B 173 10858 8193 11103 -3441 -3717 583 C ATOM 2212 N LYS B 174 91.488 14.222 -34.038 1.00 85.97 N ANISOU 2212 N LYS B 174 15044 7454 10168 -3506 -3920 941 N ATOM 2213 CA LYS B 174 92.587 13.378 -33.602 1.00 85.40 C ANISOU 2213 CA LYS B 174 15966 7178 9304 -3108 -3772 1150 C ATOM 2214 C LYS B 174 93.711 13.421 -34.630 1.00 81.10 C ANISOU 2214 C LYS B 174 15796 6809 8210 -2415 -4336 1129 C ATOM 2215 O LYS B 174 94.880 13.594 -34.277 1.00 77.84 O ANISOU 2215 O LYS B 174 15723 6708 7145 -1830 -4232 1233 O ATOM 2216 CB LYS B 174 92.118 11.942 -33.384 1.00 96.00 C ANISOU 2216 CB LYS B 174 18046 7793 10637 -3573 -3593 1208 C ATOM 2217 CG LYS B 174 93.249 10.965 -33.103 1.00 94.66 C ANISOU 2217 CG LYS B 174 19036 7351 9580 -3046 -3506 1435 C ATOM 2218 CD LYS B 174 92.791 9.522 -33.286 1.00103.31 C ANISOU 2218 CD LYS B 174 20948 7592 10715 -3481 -3451 1448 C ATOM 2219 CE LYS B 174 93.956 8.563 -33.118 1.00102.85 C ANISOU 2219 CE LYS B 174 22115 7258 9707 -2824 -3412 1683 C ATOM 2220 NZ LYS B 174 94.809 8.986 -31.969 1.00100.99 N1+ ANISOU 2220 NZ LYS B 174 22017 7526 8829 -2223 -2955 1927 N1+ ATOM 2221 N ASN B 175 93.347 13.274 -35.901 1.00 82.14 N ANISOU 2221 N ASN B 175 15818 6801 8592 -2465 -4930 957 N ATOM 2222 CA ASN B 175 94.313 13.318 -36.995 1.00 78.61 C ANISOU 2222 CA ASN B 175 15687 6521 7662 -1817 -5488 937 C ATOM 2223 C ASN B 175 95.138 14.602 -37.038 1.00 81.82 C ANISOU 2223 C ASN B 175 15421 7545 8121 -1255 -5107 906 C ATOM 2224 O ASN B 175 96.372 14.553 -37.032 1.00 69.12 O ANISOU 2224 O ASN B 175 13778 6193 6293 -713 -4606 800 O ATOM 2225 CB ASN B 175 93.598 13.134 -38.336 1.00 86.55 C ANISOU 2225 CB ASN B 175 16446 7376 9064 -1951 -6095 709 C ATOM 2226 CG ASN B 175 93.898 11.792 -38.971 1.00 92.02 C ANISOU 2226 CG ASN B 175 17884 7583 9495 -1825 -6284 676 C ATOM 2227 OD1 ASN B 175 94.526 10.930 -38.345 1.00 95.67 O ANISOU 2227 OD1 ASN B 175 19180 7721 9451 -1749 -6067 805 O ATOM 2228 ND2 ASN B 175 93.449 11.601 -40.211 1.00 86.88 N ANISOU 2228 ND2 ASN B 175 16935 6906 9170 -1738 -6632 495 N ATOM 2229 N VAL B 176 94.451 15.745 -37.080 1.00 79.43 N ANISOU 2229 N VAL B 176 14447 7520 8214 -1454 -5266 895 N ATOM 2230 CA VAL B 176 95.110 17.043 -37.258 1.00 76.76 C ANISOU 2230 CA VAL B 176 13507 7664 7994 -995 -4875 845 C ATOM 2231 C VAL B 176 95.803 17.585 -36.014 1.00 71.75 C ANISOU 2231 C VAL B 176 12837 7359 7064 -911 -4409 885 C ATOM 2232 O VAL B 176 96.310 18.706 -36.034 1.00 70.54 O ANISOU 2232 O VAL B 176 12231 7581 6992 -654 -4143 811 O ATOM 2233 CB VAL B 176 94.118 18.120 -37.722 1.00 77.88 C ANISOU 2233 CB VAL B 176 12964 7955 8671 -1164 -5174 819 C ATOM 2234 CG1 VAL B 176 93.329 17.621 -38.915 1.00 82.80 C ANISOU 2234 CG1 VAL B 176 13501 8373 9584 -1200 -5608 705 C ATOM 2235 CG2 VAL B 176 93.196 18.528 -36.573 1.00 79.62 C ANISOU 2235 CG2 VAL B 176 12668 8220 9363 -1703 -4774 801 C ATOM 2236 N THR B 177 95.809 16.815 -34.932 1.00 73.13 N ANISOU 2236 N THR B 177 13535 7396 6855 -1124 -4294 1002 N ATOM 2237 CA THR B 177 96.566 17.203 -33.751 1.00 69.89 C ANISOU 2237 CA THR B 177 13092 7379 6083 -915 -3773 980 C ATOM 2238 C THR B 177 97.692 16.212 -33.522 1.00 68.77 C ANISOU 2238 C THR B 177 13282 7290 5560 -430 -3378 877 C ATOM 2239 O THR B 177 98.399 16.276 -32.513 1.00 70.66 O ANISOU 2239 O THR B 177 13471 7905 5473 -168 -2953 819 O ATOM 2240 CB THR B 177 95.686 17.272 -32.491 1.00 66.20 C ANISOU 2240 CB THR B 177 12321 6867 5964 -1394 -3254 1026 C ATOM 2241 OG1 THR B 177 95.288 15.949 -32.110 1.00 70.86 O ANISOU 2241 OG1 THR B 177 13559 6976 6387 -1644 -3179 1186 O ATOM 2242 CG2 THR B 177 94.464 18.140 -32.736 1.00 66.96 C ANISOU 2242 CG2 THR B 177 11573 6939 6930 -1848 -3234 956 C ATOM 2243 N ASN B 178 97.842 15.286 -34.462 1.00 70.04 N ANISOU 2243 N ASN B 178 13318 6466 6827 -2507 231 -1886 N ATOM 2244 CA ASN B 178 98.905 14.297 -34.392 1.00 76.78 C ANISOU 2244 CA ASN B 178 14695 6806 7671 -1925 560 -2066 C ATOM 2245 C ASN B 178 98.653 13.261 -33.278 1.00 81.13 C ANISOU 2245 C ASN B 178 15598 6828 8400 -1825 582 -1785 C ATOM 2246 O ASN B 178 99.530 13.018 -32.445 1.00 80.89 O ANISOU 2246 O ASN B 178 15550 6671 8514 -1158 709 -1675 O ATOM 2247 CB ASN B 178 100.250 15.011 -34.178 1.00 73.85 C ANISOU 2247 CB ASN B 178 13850 6845 7364 -1169 759 -2141 C ATOM 2248 CG ASN B 178 101.417 14.258 -34.778 1.00 84.26 C ANISOU 2248 CG ASN B 178 15606 7776 8632 -651 1107 -2562 C ATOM 2249 OD1 ASN B 178 101.278 13.597 -35.807 1.00 88.69 O ANISOU 2249 OD1 ASN B 178 16597 8058 9043 -915 1177 -2820 O ATOM 2250 ND2 ASN B 178 102.579 14.347 -34.131 1.00 83.03 N ANISOU 2250 ND2 ASN B 178 15135 7714 8700 135 1276 -2563 N ATOM 2251 N ASN B 179 97.463 12.658 -33.260 1.00 79.45 N ANISOU 2251 N ASN B 179 15715 6298 8172 -2524 424 -1652 N ATOM 2252 CA ASN B 179 97.090 11.731 -32.185 1.00 91.24 C ANISOU 2252 CA ASN B 179 17568 7322 9776 -2604 431 -1319 C ATOM 2253 C ASN B 179 96.998 12.455 -30.836 1.00 79.79 C ANISOU 2253 C ASN B 179 15474 6398 8443 -2419 428 -913 C ATOM 2254 O ASN B 179 97.195 11.858 -29.774 1.00 83.26 O ANISOU 2254 O ASN B 179 16185 6532 8916 -2206 482 -619 O ATOM 2255 CB ASN B 179 98.098 10.573 -32.101 1.00100.32 C ANISOU 2255 CB ASN B 179 19461 7699 10957 -2010 574 -1454 C ATOM 2256 CG ASN B 179 97.728 9.522 -31.051 1.00113.54 C ANISOU 2256 CG ASN B 179 21687 8756 12697 -2155 505 -1071 C ATOM 2257 OD1 ASN B 179 97.147 8.483 -31.366 1.00122.48 O ANISOU 2257 OD1 ASN B 179 23309 9437 13791 -2559 419 -1052 O ATOM 2258 ND2 ASN B 179 98.085 9.789 -29.796 1.00113.38 N ANISOU 2258 ND2 ASN B 179 21387 8940 12750 -1767 508 -700 N ATOM 2259 N PHE B 180 96.691 13.745 -30.879 1.00 75.22 N ANISOU 2259 N PHE B 180 14096 6581 7903 -2515 331 -904 N ATOM 2260 CA PHE B 180 96.714 14.555 -29.668 1.00 67.78 C ANISOU 2260 CA PHE B 180 12524 6180 7051 -2262 339 -611 C ATOM 2261 C PHE B 180 98.062 14.412 -28.987 1.00 67.46 C ANISOU 2261 C PHE B 180 12599 6006 7027 -1410 454 -532 C ATOM 2262 O PHE B 180 98.142 13.930 -27.861 1.00 71.81 O ANISOU 2262 O PHE B 180 13368 6350 7567 -1260 491 -223 O ATOM 2263 CB PHE B 180 95.592 14.149 -28.712 1.00 65.27 C ANISOU 2263 CB PHE B 180 12223 5830 6746 -2828 367 -294 C ATOM 2264 CG PHE B 180 94.217 14.478 -29.217 1.00 70.79 C ANISOU 2264 CG PHE B 180 12559 6802 7538 -3634 222 -375 C ATOM 2265 CD1 PHE B 180 93.657 15.728 -28.984 1.00 61.32 C ANISOU 2265 CD1 PHE B 180 10471 6339 6488 -3728 103 -391 C ATOM 2266 CD2 PHE B 180 93.481 13.539 -29.931 1.00 77.15 C ANISOU 2266 CD2 PHE B 180 13896 7096 8323 -4281 153 -459 C ATOM 2267 CE1 PHE B 180 92.391 16.041 -29.445 1.00 62.37 C ANISOU 2267 CE1 PHE B 180 10194 6706 6796 -4416 -97 -498 C ATOM 2268 CE2 PHE B 180 92.208 13.841 -30.398 1.00 78.43 C ANISOU 2268 CE2 PHE B 180 13606 7565 8630 -4932 -43 -527 C ATOM 2269 CZ PHE B 180 91.663 15.100 -30.153 1.00 75.77 C ANISOU 2269 CZ PHE B 180 12321 7978 8492 -4941 -171 -545 C ATOM 2270 N ASP B 181 99.118 14.811 -29.693 1.00 67.28 N ANISOU 2270 N ASP B 181 12444 6094 7024 -894 496 -813 N ATOM 2271 CA ASP B 181 100.488 14.674 -29.204 1.00 66.49 C ANISOU 2271 CA ASP B 181 12370 5869 7024 -48 579 -818 C ATOM 2272 C ASP B 181 100.670 15.506 -27.945 1.00 65.26 C ANISOU 2272 C ASP B 181 11661 6209 6925 253 481 -495 C ATOM 2273 O ASP B 181 100.752 16.735 -28.000 1.00 63.45 O ANISOU 2273 O ASP B 181 10755 6630 6724 311 405 -530 O ATOM 2274 CB ASP B 181 101.490 15.087 -30.287 1.00 69.63 C ANISOU 2274 CB ASP B 181 12585 6437 7434 327 703 -1228 C ATOM 2275 CG ASP B 181 102.935 14.788 -29.907 1.00 73.37 C ANISOU 2275 CG ASP B 181 13058 6721 8099 1211 805 -1321 C ATOM 2276 OD1 ASP B 181 103.352 15.129 -28.773 1.00 68.90 O ANISOU 2276 OD1 ASP B 181 12185 6338 7657 1626 677 -1029 O ATOM 2277 OD2 ASP B 181 103.657 14.215 -30.758 1.00 78.12 O1+ ANISOU 2277 OD2 ASP B 181 13951 6995 8734 1493 1005 -1721 O1+ ATOM 2278 N GLU B 182 100.738 14.813 -26.815 1.00 69.98 N ANISOU 2278 N GLU B 182 12625 6453 7511 422 449 -178 N ATOM 2279 CA GLU B 182 100.808 15.440 -25.508 1.00 69.76 C ANISOU 2279 CA GLU B 182 12238 6821 7446 627 355 150 C ATOM 2280 C GLU B 182 102.074 16.274 -25.325 1.00 54.55 C ANISOU 2280 C GLU B 182 9804 5257 5665 1385 261 69 C ATOM 2281 O GLU B 182 102.102 17.179 -24.513 1.00 51.12 O ANISOU 2281 O GLU B 182 8893 5329 5200 1509 155 237 O ATOM 2282 CB GLU B 182 100.727 14.366 -24.421 1.00 86.52 C ANISOU 2282 CB GLU B 182 15048 8374 9451 622 312 519 C ATOM 2283 CG GLU B 182 100.079 14.831 -23.118 1.00 93.13 C ANISOU 2283 CG GLU B 182 15687 9621 10076 343 308 884 C ATOM 2284 CD GLU B 182 98.564 14.650 -23.103 1.00101.40 C ANISOU 2284 CD GLU B 182 16768 10781 10977 -586 480 968 C ATOM 2285 OE1 GLU B 182 98.025 13.996 -24.030 1.00106.49 O ANISOU 2285 OE1 GLU B 182 17722 11058 11680 -1028 533 810 O ATOM 2286 OE2 GLU B 182 97.918 15.159 -22.158 1.00 99.83 O1+ ANISOU 2286 OE2 GLU B 182 16271 11050 10610 -881 569 1162 O1+ ATOM 2287 N ARG B 183 103.126 15.966 -26.072 1.00 64.02 N ANISOU 2287 N ARG B 183 11089 6205 7033 1879 314 -219 N ATOM 2288 CA ARG B 183 104.378 16.706 -25.941 1.00 60.65 C ANISOU 2288 CA ARG B 183 10128 6125 6793 2565 243 -317 C ATOM 2289 C ARG B 183 104.152 18.190 -26.203 1.00 54.68 C ANISOU 2289 C ARG B 183 8618 6161 5996 2348 199 -372 C ATOM 2290 O ARG B 183 103.272 18.562 -26.984 1.00 58.46 O ANISOU 2290 O ARG B 183 9002 6847 6361 1763 249 -492 O ATOM 2291 CB ARG B 183 105.430 16.147 -26.892 1.00 57.70 C ANISOU 2291 CB ARG B 183 9883 5421 6620 3027 407 -721 C ATOM 2292 CG ARG B 183 105.841 14.728 -26.584 1.00 64.80 C ANISOU 2292 CG ARG B 183 11492 5471 7659 3413 362 -711 C ATOM 2293 CD ARG B 183 106.860 14.265 -27.588 1.00 68.89 C ANISOU 2293 CD ARG B 183 12028 5732 8414 3900 577 -1223 C ATOM 2294 NE ARG B 183 106.280 14.218 -28.922 1.00 68.66 N ANISOU 2294 NE ARG B 183 12162 5746 8181 3340 864 -1573 N ATOM 2295 CZ ARG B 183 106.965 13.988 -30.037 1.00 71.87 C ANISOU 2295 CZ ARG B 183 12505 6131 8670 3491 1147 -2069 C ATOM 2296 NH1 ARG B 183 108.279 13.784 -29.995 1.00 75.69 N1+ ANISOU 2296 NH1 ARG B 183 12487 6713 9561 3976 1169 -2216 N1+ ATOM 2297 NH2 ARG B 183 106.328 13.965 -31.200 1.00 71.88 N ANISOU 2297 NH2 ARG B 183 12817 6120 8373 2948 1376 -2371 N ATOM 2298 N PRO B 184 104.920 19.052 -25.528 1.00 53.94 N ANISOU 2298 N PRO B 184 8010 6475 6009 2806 33 -273 N ATOM 2299 CA PRO B 184 104.701 20.492 -25.711 1.00 42.22 C ANISOU 2299 CA PRO B 184 5856 5682 4502 2603 -80 -308 C ATOM 2300 C PRO B 184 105.196 20.945 -27.074 1.00 45.44 C ANISOU 2300 C PRO B 184 6019 6290 4958 2534 46 -643 C ATOM 2301 O PRO B 184 106.034 20.249 -27.672 1.00 50.55 O ANISOU 2301 O PRO B 184 6871 6638 5698 2839 256 -877 O ATOM 2302 CB PRO B 184 105.517 21.125 -24.579 1.00 41.93 C ANISOU 2302 CB PRO B 184 5455 5910 4567 3091 -309 -116 C ATOM 2303 CG PRO B 184 106.554 20.093 -24.246 1.00 46.31 C ANISOU 2303 CG PRO B 184 6336 5974 5285 3437 -285 -97 C ATOM 2304 CD PRO B 184 105.922 18.761 -24.491 1.00 49.77 C ANISOU 2304 CD PRO B 184 7528 5757 5625 3486 -142 -93 C ATOM 2305 N ILE B 185 104.692 22.086 -27.544 1.00 51.75 N ANISOU 2305 N ILE B 185 6442 6815 6407 380 -417 1105 N ATOM 2306 CA ILE B 185 105.023 22.588 -28.867 1.00 44.92 C ANISOU 2306 CA ILE B 185 5354 5820 5892 243 -535 904 C ATOM 2307 C ILE B 185 106.517 22.712 -29.043 1.00 52.58 C ANISOU 2307 C ILE B 185 6307 6634 7037 615 -719 805 C ATOM 2308 O ILE B 185 107.070 22.277 -30.048 1.00 51.48 O ANISOU 2308 O ILE B 185 6297 6158 7105 555 -683 819 O ATOM 2309 CB ILE B 185 104.398 23.960 -29.135 1.00 45.98 C ANISOU 2309 CB ILE B 185 5048 6274 6148 152 -640 664 C ATOM 2310 CG1 ILE B 185 102.882 23.843 -29.227 1.00 46.30 C ANISOU 2310 CG1 ILE B 185 5038 6499 6056 -235 -486 663 C ATOM 2311 CG2 ILE B 185 104.921 24.528 -30.447 1.00 39.91 C ANISOU 2311 CG2 ILE B 185 4148 5318 5699 188 -670 512 C ATOM 2312 CD1 ILE B 185 102.392 23.237 -30.515 1.00 43.16 C ANISOU 2312 CD1 ILE B 185 4704 5923 5772 -529 -365 588 C ATOM 2313 N SER B 186 107.163 23.286 -28.034 1.00 56.79 N ANISOU 2313 N SER B 186 6646 7441 7490 1016 -918 642 N ATOM 2314 CA SER B 186 108.580 23.625 -28.093 1.00 56.23 C ANISOU 2314 CA SER B 186 6384 7321 7659 1383 -1109 351 C ATOM 2315 C SER B 186 109.522 22.426 -28.241 1.00 59.68 C ANISOU 2315 C SER B 186 7205 7464 8005 1612 -1114 509 C ATOM 2316 O SER B 186 110.727 22.620 -28.357 1.00 60.73 O ANISOU 2316 O SER B 186 7161 7552 8360 1910 -1274 215 O ATOM 2317 CB SER B 186 108.970 24.416 -26.845 1.00 55.54 C ANISOU 2317 CB SER B 186 5934 7701 7470 1798 -1341 17 C ATOM 2318 OG SER B 186 109.244 23.548 -25.761 1.00 61.55 O ANISOU 2318 OG SER B 186 6999 8653 7734 2249 -1433 181 O ATOM 2319 N VAL B 187 108.993 21.202 -28.227 1.00 60.07 N ANISOU 2319 N VAL B 187 7758 7295 7770 1476 -892 924 N ATOM 2320 CA VAL B 187 109.813 20.040 -28.584 1.00 59.14 C ANISOU 2320 CA VAL B 187 8050 6809 7611 1635 -819 1114 C ATOM 2321 C VAL B 187 109.160 19.209 -29.696 1.00 57.45 C ANISOU 2321 C VAL B 187 8123 6158 7548 1107 -518 1351 C ATOM 2322 O VAL B 187 109.530 18.053 -29.920 1.00 57.18 O ANISOU 2322 O VAL B 187 8513 5769 7443 1143 -338 1587 O ATOM 2323 CB VAL B 187 110.106 19.134 -27.355 1.00 55.15 C ANISOU 2323 CB VAL B 187 7977 6404 6573 2179 -756 1374 C ATOM 2324 CG1 VAL B 187 110.324 19.987 -26.123 1.00 59.50 C ANISOU 2324 CG1 VAL B 187 8205 7535 6867 2692 -1047 1103 C ATOM 2325 CG2 VAL B 187 108.987 18.102 -27.117 1.00 57.74 C ANISOU 2325 CG2 VAL B 187 8824 6467 6648 1900 -265 1839 C ATOM 2326 N GLY B 188 108.191 19.799 -30.393 1.00 52.40 N ANISOU 2326 N GLY B 188 7231 5577 7100 663 -461 1241 N ATOM 2327 CA GLY B 188 107.636 19.168 -31.579 1.00 52.06 C ANISOU 2327 CA GLY B 188 7316 5236 7228 230 -261 1286 C ATOM 2328 C GLY B 188 106.311 18.444 -31.411 1.00 58.55 C ANISOU 2328 C GLY B 188 8286 6027 7934 -182 75 1382 C ATOM 2329 O GLY B 188 105.862 17.743 -32.330 1.00 57.91 O ANISOU 2329 O GLY B 188 8281 5712 8012 -538 267 1320 O ATOM 2330 N GLY B 189 105.681 18.597 -30.247 1.00 53.95 N ANISOU 2330 N GLY B 189 7715 5677 7106 -137 179 1471 N ATOM 2331 CA GLY B 189 104.345 18.055 -30.032 1.00 56.21 C ANISOU 2331 CA GLY B 189 8066 5929 7361 -569 571 1480 C ATOM 2332 C GLY B 189 103.256 19.058 -30.392 1.00 53.29 C ANISOU 2332 C GLY B 189 7205 5969 7073 -857 427 1158 C ATOM 2333 O GLY B 189 103.512 20.035 -31.089 1.00 51.27 O ANISOU 2333 O GLY B 189 6634 5926 6919 -746 97 969 O ATOM 2334 N ASN B 190 102.038 18.831 -29.915 1.00 60.90 N ANISOU 2334 N ASN B 190 8118 7027 7994 -1189 729 1088 N ATOM 2335 CA ASN B 190 100.939 19.752 -30.210 1.00 58.82 C ANISOU 2335 CA ASN B 190 7375 7211 7762 -1421 584 746 C ATOM 2336 C ASN B 190 100.270 20.334 -28.974 1.00 57.79 C ANISOU 2336 C ASN B 190 7148 7387 7422 -1383 633 814 C ATOM 2337 O ASN B 190 99.239 20.995 -29.087 1.00 55.53 O ANISOU 2337 O ASN B 190 6488 7469 7142 -1595 571 536 O ATOM 2338 CB ASN B 190 99.878 19.051 -31.055 1.00 65.70 C ANISOU 2338 CB ASN B 190 8084 8027 8851 -1930 855 372 C ATOM 2339 CG ASN B 190 100.406 18.623 -32.397 1.00 66.82 C ANISOU 2339 CG ASN B 190 8235 7981 9174 -1941 743 220 C ATOM 2340 OD1 ASN B 190 101.341 17.827 -32.480 1.00 65.29 O ANISOU 2340 OD1 ASN B 190 8415 7346 9045 -1846 859 475 O ATOM 2341 ND2 ASN B 190 99.808 19.143 -33.464 1.00 67.91 N ANISOU 2341 ND2 ASN B 190 7976 8479 9346 -1989 515 -201 N ATOM 2342 N LYS B 191 100.839 20.077 -27.796 1.00 62.90 N ANISOU 2342 N LYS B 191 8137 7923 7840 -1052 740 1164 N ATOM 2343 CA LYS B 191 100.278 20.609 -26.553 1.00 61.99 C ANISOU 2343 CA LYS B 191 7970 8111 7474 -930 785 1253 C ATOM 2344 C LYS B 191 100.633 22.070 -26.369 1.00 52.60 C ANISOU 2344 C LYS B 191 6379 7395 6212 -624 272 1112 C ATOM 2345 O LYS B 191 101.813 22.428 -26.321 1.00 50.96 O ANISOU 2345 O LYS B 191 6171 7202 5989 -210 -21 1141 O ATOM 2346 CB LYS B 191 100.770 19.825 -25.346 1.00 60.59 C ANISOU 2346 CB LYS B 191 8335 7702 6984 -531 1092 1671 C ATOM 2347 CG LYS B 191 100.317 20.414 -24.030 1.00 62.08 C ANISOU 2347 CG LYS B 191 8497 8245 6846 -275 1100 1777 C ATOM 2348 CD LYS B 191 100.850 19.606 -22.864 1.00 67.04 C ANISOU 2348 CD LYS B 191 9739 8678 7054 300 1423 2216 C ATOM 2349 CE LYS B 191 100.571 20.306 -21.547 1.00 77.71 C ANISOU 2349 CE LYS B 191 11043 10476 8006 712 1327 2297 C ATOM 2350 NZ LYS B 191 101.106 19.536 -20.393 1.00 83.18 N1+ ANISOU 2350 NZ LYS B 191 12385 11051 8168 1457 1640 2735 N1+ ATOM 2351 N MET B 192 99.619 22.918 -26.264 1.00 51.60 N ANISOU 2351 N MET B 192 5884 7641 6080 -831 204 907 N ATOM 2352 CA MET B 192 99.868 24.332 -26.055 1.00 48.44 C ANISOU 2352 CA MET B 192 5109 7644 5652 -568 -179 763 C ATOM 2353 C MET B 192 99.718 24.704 -24.572 1.00 50.09 C ANISOU 2353 C MET B 192 5325 8136 5571 -312 -192 879 C ATOM 2354 O MET B 192 100.383 25.612 -24.077 1.00 48.69 O ANISOU 2354 O MET B 192 4930 8218 5353 57 -489 779 O ATOM 2355 CB MET B 192 98.936 25.174 -26.918 1.00 46.33 C ANISOU 2355 CB MET B 192 4440 7653 5510 -826 -274 468 C ATOM 2356 CG MET B 192 98.562 24.545 -28.247 1.00 54.80 C ANISOU 2356 CG MET B 192 5517 8555 6749 -1112 -173 299 C ATOM 2357 SD MET B 192 97.651 25.714 -29.297 1.00 57.01 S ANISOU 2357 SD MET B 192 5342 9289 7031 -1117 -365 -67 S ATOM 2358 CE MET B 192 98.987 26.926 -29.354 1.00 41.20 C ANISOU 2358 CE MET B 192 3305 7220 5128 -619 -577 60 C ATOM 2359 N GLY B 193 98.858 23.990 -23.859 1.00 53.64 N ANISOU 2359 N GLY B 193 6016 8518 5845 -490 178 1049 N ATOM 2360 CA GLY B 193 98.601 24.321 -22.474 1.00 55.66 C ANISOU 2360 CA GLY B 193 6318 9052 5777 -212 208 1182 C ATOM 2361 C GLY B 193 97.567 23.422 -21.841 1.00 60.24 C ANISOU 2361 C GLY B 193 7230 9424 6234 -467 784 1387 C ATOM 2362 O GLY B 193 96.999 22.569 -22.504 1.00 61.97 O ANISOU 2362 O GLY B 193 7568 9285 6693 -931 1174 1339 O ATOM 2363 N GLU B 194 97.349 23.616 -20.546 1.00 62.76 N ANISOU 2363 N GLU B 194 7688 9955 6203 -139 881 1573 N ATOM 2364 CA GLU B 194 96.334 22.899 -19.782 1.00 67.73 C ANISOU 2364 CA GLU B 194 8655 10368 6711 -324 1526 1788 C ATOM 2365 C GLU B 194 95.474 23.936 -19.080 1.00 75.85 C ANISOU 2365 C GLU B 194 9316 11886 7616 -380 1376 1646 C ATOM 2366 O GLU B 194 95.994 24.787 -18.352 1.00 72.06 O ANISOU 2366 O GLU B 194 8689 11838 6851 127 953 1650 O ATOM 2367 CB GLU B 194 96.961 21.942 -18.759 1.00 73.19 C ANISOU 2367 CB GLU B 194 10064 10768 6978 305 1930 2280 C ATOM 2368 CG GLU B 194 97.985 20.986 -19.359 1.00 84.11 C ANISOU 2368 CG GLU B 194 11832 11714 8414 493 2017 2448 C ATOM 2369 CD GLU B 194 98.522 19.963 -18.364 1.00 91.76 C ANISOU 2369 CD GLU B 194 13596 12374 8896 1203 2514 2973 C ATOM 2370 OE1 GLU B 194 97.885 19.746 -17.300 1.00 94.62 O ANISOU 2370 OE1 GLU B 194 14315 12693 8943 1431 3017 3256 O ATOM 2371 OE2 GLU B 194 99.590 19.371 -18.660 1.00 88.36 O1+ ANISOU 2371 OE2 GLU B 194 13464 11738 8373 1588 2430 3116 O1+ ATOM 2372 N GLY B 195 94.165 23.878 -19.315 1.00 67.81 N ANISOU 2372 N GLY B 195 8097 10828 6840 -995 1713 1444 N ATOM 2373 CA GLY B 195 93.247 24.841 -18.741 1.00 66.93 C ANISOU 2373 CA GLY B 195 7615 11173 6642 -1109 1589 1281 C ATOM 2374 C GLY B 195 91.810 24.549 -19.119 1.00 69.05 C ANISOU 2374 C GLY B 195 7657 11346 7235 -1820 2029 971 C ATOM 2375 O GLY B 195 91.547 23.713 -19.973 1.00 70.78 O ANISOU 2375 O GLY B 195 7894 11202 7796 -2252 2351 775 O ATOM 2376 N GLY B 196 90.876 25.239 -18.477 1.00 69.34 N ANISOU 2376 N GLY B 196 7430 11734 7183 -1939 2041 854 N ATOM 2377 CA GLY B 196 89.464 25.025 -18.737 1.00 84.42 C ANISOU 2377 CA GLY B 196 9044 13625 9407 -2594 2453 458 C ATOM 2378 C GLY B 196 89.001 23.580 -18.596 1.00 88.80 C ANISOU 2378 C GLY B 196 10007 13495 10238 -2966 3386 506 C ATOM 2379 O GLY B 196 88.102 23.144 -19.315 1.00 88.29 O ANISOU 2379 O GLY B 196 9612 13315 10620 -3592 3709 -17 O ATOM 2380 N PHE B 197 89.617 22.842 -17.673 1.00 89.35 N ANISOU 2380 N PHE B 197 10785 13118 10044 -2533 3861 1084 N ATOM 2381 CA PHE B 197 89.252 21.451 -17.405 1.00 94.93 C ANISOU 2381 CA PHE B 197 12022 13047 11000 -2790 4930 1238 C ATOM 2382 C PHE B 197 89.680 20.508 -18.524 1.00 97.26 C ANISOU 2382 C PHE B 197 12386 12882 11688 -3089 5112 1061 C ATOM 2383 O PHE B 197 89.049 19.472 -18.738 1.00 97.51 O ANISOU 2383 O PHE B 197 12539 12322 12190 -3617 5981 847 O ATOM 2384 CB PHE B 197 87.739 21.316 -17.189 1.00104.32 C ANISOU 2384 CB PHE B 197 12918 14133 12586 -3465 5591 815 C ATOM 2385 CG PHE B 197 87.184 22.247 -16.146 1.00105.41 C ANISOU 2385 CG PHE B 197 12942 14727 12384 -3249 5436 938 C ATOM 2386 CD1 PHE B 197 87.225 21.907 -14.806 1.00110.35 C ANISOU 2386 CD1 PHE B 197 14239 15049 12639 -2775 6058 1531 C ATOM 2387 CD2 PHE B 197 86.619 23.458 -16.510 1.00101.56 C ANISOU 2387 CD2 PHE B 197 11707 14971 11909 -3455 4701 475 C ATOM 2388 CE1 PHE B 197 86.720 22.760 -13.844 1.00111.50 C ANISOU 2388 CE1 PHE B 197 14275 15634 12456 -2554 5903 1632 C ATOM 2389 CE2 PHE B 197 86.113 24.318 -15.554 1.00101.56 C ANISOU 2389 CE2 PHE B 197 11593 15384 11610 -3270 4562 580 C ATOM 2390 CZ PHE B 197 86.162 23.968 -14.218 1.00107.27 C ANISOU 2390 CZ PHE B 197 12951 15818 11990 -2843 5145 1143 C ATOM 2391 N GLY B 198 90.743 20.863 -19.241 1.00 60.52 N ANISOU 2391 N GLY B 198 5635 9483 7879 -1156 2258 1090 N ATOM 2392 CA GLY B 198 91.220 20.021 -20.323 1.00 63.03 C ANISOU 2392 CA GLY B 198 6683 9376 7889 -1448 1963 1102 C ATOM 2393 C GLY B 198 92.610 20.378 -20.801 1.00 62.39 C ANISOU 2393 C GLY B 198 6910 9225 7570 -1031 1915 668 C ATOM 2394 O GLY B 198 93.235 21.310 -20.291 1.00 65.40 O ANISOU 2394 O GLY B 198 6915 9876 8059 -527 2098 338 O ATOM 2395 N VAL B 199 93.104 19.628 -21.779 1.00 60.28 N ANISOU 2395 N VAL B 199 7324 8592 6989 -1240 1678 651 N ATOM 2396 CA VAL B 199 94.369 19.956 -22.415 1.00 44.85 C ANISOU 2396 CA VAL B 199 5655 6552 4832 -903 1616 290 C ATOM 2397 C VAL B 199 94.121 20.559 -23.793 1.00 44.42 C ANISOU 2397 C VAL B 199 5467 6393 5018 -1251 1263 378 C ATOM 2398 O VAL B 199 93.295 20.061 -24.548 1.00 63.68 O ANISOU 2398 O VAL B 199 8067 8646 7482 -1809 972 671 O ATOM 2399 CB VAL B 199 95.265 18.722 -22.538 1.00 52.29 C ANISOU 2399 CB VAL B 199 7486 7182 5200 -779 1646 170 C ATOM 2400 CG1 VAL B 199 96.546 19.059 -23.291 1.00 42.04 C ANISOU 2400 CG1 VAL B 199 6462 5803 3709 -452 1583 -177 C ATOM 2401 CG2 VAL B 199 95.570 18.178 -21.152 1.00 52.15 C ANISOU 2401 CG2 VAL B 199 7582 7309 4922 -362 2008 113 C ATOM 2402 N VAL B 200 94.854 21.623 -24.114 1.00 50.14 N ANISOU 2402 N VAL B 200 5893 7240 5917 -914 1289 126 N ATOM 2403 CA VAL B 200 94.671 22.375 -25.357 1.00 50.66 C ANISOU 2403 CA VAL B 200 5748 7261 6240 -1151 1008 240 C ATOM 2404 C VAL B 200 95.747 22.077 -26.382 1.00 51.52 C ANISOU 2404 C VAL B 200 6468 7142 5966 -1051 887 62 C ATOM 2405 O VAL B 200 96.921 22.253 -26.101 1.00 52.70 O ANISOU 2405 O VAL B 200 6748 7311 5964 -566 1100 -275 O ATOM 2406 CB VAL B 200 94.676 23.889 -25.099 1.00 39.18 C ANISOU 2406 CB VAL B 200 3474 6067 5344 -865 1143 140 C ATOM 2407 CG1 VAL B 200 94.664 24.637 -26.418 1.00 38.98 C ANISOU 2407 CG1 VAL B 200 3299 5972 5539 -1036 890 283 C ATOM 2408 CG2 VAL B 200 93.481 24.286 -24.221 1.00 43.29 C ANISOU 2408 CG2 VAL B 200 3334 6828 6288 -988 1246 345 C ATOM 2409 N TYR B 201 95.348 21.651 -27.574 1.00 41.84 N ANISOU 2409 N TYR B 201 5588 5728 4582 -1498 544 277 N ATOM 2410 CA TYR B 201 96.308 21.241 -28.592 1.00 41.34 C ANISOU 2410 CA TYR B 201 6174 5448 4083 -1420 433 121 C ATOM 2411 C TYR B 201 96.224 22.132 -29.818 1.00 53.19 C ANISOU 2411 C TYR B 201 7428 7015 5768 -1543 204 268 C ATOM 2412 O TYR B 201 95.147 22.622 -30.156 1.00 59.38 O ANISOU 2412 O TYR B 201 7751 7920 6890 -1897 -18 579 O ATOM 2413 CB TYR B 201 96.064 19.787 -29.018 1.00 54.35 C ANISOU 2413 CB TYR B 201 8614 6784 5253 -1801 226 188 C ATOM 2414 CG TYR B 201 96.036 18.775 -27.888 1.00 52.86 C ANISOU 2414 CG TYR B 201 8729 6475 4879 -1735 445 138 C ATOM 2415 CD1 TYR B 201 95.005 18.770 -26.950 1.00 57.37 C ANISOU 2415 CD1 TYR B 201 8852 7183 5763 -1928 527 361 C ATOM 2416 CD2 TYR B 201 97.034 17.813 -27.768 1.00 56.29 C ANISOU 2416 CD2 TYR B 201 9898 6663 4825 -1460 591 -97 C ATOM 2417 CE1 TYR B 201 94.981 17.849 -25.914 1.00 60.03 C ANISOU 2417 CE1 TYR B 201 9467 7424 5919 -1845 761 370 C ATOM 2418 CE2 TYR B 201 97.013 16.877 -26.736 1.00 57.97 C ANISOU 2418 CE2 TYR B 201 10400 6760 4867 -1369 808 -89 C ATOM 2419 CZ TYR B 201 95.986 16.905 -25.817 1.00 61.62 C ANISOU 2419 CZ TYR B 201 10410 7370 5633 -1564 896 156 C ATOM 2420 OH TYR B 201 95.960 15.988 -24.797 1.00 71.28 O ANISOU 2420 OH TYR B 201 11915 8493 6677 -1455 1141 218 O ATOM 2421 N LYS B 202 97.354 22.338 -30.490 1.00 51.87 N ANISOU 2421 N LYS B 202 7553 6779 5376 -1237 267 75 N ATOM 2422 CA LYS B 202 97.354 23.017 -31.782 1.00 40.53 C ANISOU 2422 CA LYS B 202 6020 5384 3997 -1346 58 256 C ATOM 2423 C LYS B 202 96.973 22.038 -32.878 1.00 50.30 C ANISOU 2423 C LYS B 202 7919 6456 4736 -1782 -317 387 C ATOM 2424 O LYS B 202 97.479 20.909 -32.908 1.00 51.99 O ANISOU 2424 O LYS B 202 8866 6438 4449 -1772 -306 182 O ATOM 2425 CB LYS B 202 98.711 23.623 -32.081 1.00 42.06 C ANISOU 2425 CB LYS B 202 6247 5576 4160 -849 306 23 C ATOM 2426 CG LYS B 202 98.797 24.314 -33.423 1.00 43.49 C ANISOU 2426 CG LYS B 202 6356 5802 4366 -913 145 249 C ATOM 2427 CD LYS B 202 100.012 25.244 -33.473 1.00 44.46 C ANISOU 2427 CD LYS B 202 6225 5954 4713 -407 475 70 C ATOM 2428 CE LYS B 202 100.179 25.859 -34.852 1.00 51.51 C ANISOU 2428 CE LYS B 202 7113 6881 5576 -437 362 341 C ATOM 2429 NZ LYS B 202 101.256 26.899 -34.872 1.00 56.61 N1+ ANISOU 2429 NZ LYS B 202 7383 7539 6585 16 711 228 N1+ ATOM 2430 N GLY B 203 96.068 22.462 -33.759 1.00 50.14 N ANISOU 2430 N GLY B 203 7636 6558 4857 -2155 -656 716 N ATOM 2431 CA GLY B 203 95.595 21.619 -34.844 1.00 50.64 C ANISOU 2431 CA GLY B 203 8259 6519 4464 -2604 -1074 822 C ATOM 2432 C GLY B 203 95.388 22.422 -36.111 1.00 52.42 C ANISOU 2432 C GLY B 203 8275 6941 4703 -2688 -1333 1092 C ATOM 2433 O GLY B 203 95.404 23.647 -36.088 1.00 50.81 O ANISOU 2433 O GLY B 203 7417 6928 4962 -2463 -1196 1269 O ATOM 2434 N TYR B 204 95.213 21.746 -37.234 1.00 56.15 N ANISOU 2434 N TYR B 204 9310 7364 4660 -2991 -1701 1121 N ATOM 2435 CA TYR B 204 94.969 22.472 -38.469 1.00 58.53 C ANISOU 2435 CA TYR B 204 9430 7905 4903 -3059 -1970 1414 C ATOM 2436 C TYR B 204 94.020 21.722 -39.369 1.00 64.03 C ANISOU 2436 C TYR B 204 10460 8643 5224 -3622 -2528 1527 C ATOM 2437 O TYR B 204 94.147 20.519 -39.574 1.00 74.52 O ANISOU 2437 O TYR B 204 12521 9735 6056 -3833 -2677 1257 O ATOM 2438 CB TYR B 204 96.272 22.752 -39.222 1.00 57.25 C ANISOU 2438 CB TYR B 204 9640 7728 4383 -2608 -1752 1290 C ATOM 2439 CG TYR B 204 96.040 23.310 -40.619 1.00 60.70 C ANISOU 2439 CG TYR B 204 10037 8418 4607 -2683 -2047 1613 C ATOM 2440 CD1 TYR B 204 95.916 24.680 -40.837 1.00 60.02 C ANISOU 2440 CD1 TYR B 204 9228 8566 5013 -2484 -1946 1983 C ATOM 2441 CD2 TYR B 204 95.927 22.463 -41.715 1.00 70.08 C ANISOU 2441 CD2 TYR B 204 11916 9614 5098 -2942 -2426 1549 C ATOM 2442 CE1 TYR B 204 95.701 25.190 -42.112 1.00 63.63 C ANISOU 2442 CE1 TYR B 204 9649 9276 5250 -2518 -2201 2335 C ATOM 2443 CE2 TYR B 204 95.706 22.957 -42.992 1.00 74.22 C ANISOU 2443 CE2 TYR B 204 12369 10403 5428 -2949 -2665 1823 C ATOM 2444 CZ TYR B 204 95.597 24.319 -43.189 1.00 75.69 C ANISOU 2444 CZ TYR B 204 11876 10864 6017 -2761 -2590 2272 C ATOM 2445 OH TYR B 204 95.381 24.797 -44.468 1.00 77.09 O ANISOU 2445 OH TYR B 204 12023 11335 5933 -2751 -2835 2602 O ATOM 2446 N VAL B 205 93.067 22.444 -39.927 1.00 66.72 N ANISOU 2446 N VAL B 205 10252 9284 5816 -3859 -2848 1918 N ATOM 2447 CA VAL B 205 92.142 21.819 -40.840 1.00 86.54 C ANISOU 2447 CA VAL B 205 13008 11899 7976 -4395 -3431 2022 C ATOM 2448 C VAL B 205 91.373 22.867 -41.639 1.00 89.99 C ANISOU 2448 C VAL B 205 12814 12745 8633 -4479 -3737 2500 C ATOM 2449 O VAL B 205 91.038 23.935 -41.119 1.00 88.17 O ANISOU 2449 O VAL B 205 11790 12666 9045 -4312 -3548 2794 O ATOM 2450 CB VAL B 205 91.167 20.903 -40.082 1.00 84.07 C ANISOU 2450 CB VAL B 205 12681 11419 7842 -4909 -3617 1947 C ATOM 2451 CG1 VAL B 205 90.435 21.688 -39.012 1.00 72.32 C ANISOU 2451 CG1 VAL B 205 10287 10064 7128 -4904 -3425 2216 C ATOM 2452 CG2 VAL B 205 90.191 20.243 -41.061 1.00 89.43 C ANISOU 2452 CG2 VAL B 205 13553 12151 8274 -5405 -4136 2010 C ATOM 2453 N ASN B 206 91.124 22.567 -42.908 1.00 88.84 N ANISOU 2453 N ASN B 206 13011 12739 8006 -4656 -4124 2543 N ATOM 2454 CA ASN B 206 90.263 23.403 -43.719 1.00 84.16 C ANISOU 2454 CA ASN B 206 11854 12522 7600 -4743 -4421 2986 C ATOM 2455 C ASN B 206 90.752 24.844 -43.781 1.00 84.75 C ANISOU 2455 C ASN B 206 11385 12851 7967 -4302 -4203 3393 C ATOM 2456 O ASN B 206 89.985 25.776 -43.537 1.00 84.40 O ANISOU 2456 O ASN B 206 10528 13016 8523 -4318 -4242 3799 O ATOM 2457 CB ASN B 206 88.836 23.346 -43.172 1.00 95.19 C ANISOU 2457 CB ASN B 206 12664 13998 9507 -5191 -4668 3195 C ATOM 2458 CG ASN B 206 88.290 21.918 -43.112 1.00100.99 C ANISOU 2458 CG ASN B 206 13906 14454 10014 -5623 -4855 2862 C ATOM 2459 OD1 ASN B 206 88.716 21.052 -43.880 1.00103.84 O ANISOU 2459 OD1 ASN B 206 14980 14647 9826 -5644 -4943 2538 O ATOM 2460 ND2 ASN B 206 87.346 21.670 -42.201 1.00 96.91 N ANISOU 2460 ND2 ASN B 206 12996 13864 9961 -5901 -4851 2946 N ATOM 2461 N ASN B 207 92.037 25.008 -44.097 1.00 83.87 N ANISOU 2461 N ASN B 207 11691 12633 7542 -3843 -3847 3244 N ATOM 2462 CA ASN B 207 92.652 26.324 -44.275 1.00 82.70 C ANISOU 2462 CA ASN B 207 11081 12593 7750 -3336 -3469 3558 C ATOM 2463 C ASN B 207 92.490 27.210 -43.046 1.00 72.07 C ANISOU 2463 C ASN B 207 8928 11139 7315 -3156 -3080 3653 C ATOM 2464 O ASN B 207 92.313 28.429 -43.148 1.00 72.02 O ANISOU 2464 O ASN B 207 8249 11278 7837 -2932 -2947 4056 O ATOM 2465 CB ASN B 207 92.074 27.017 -45.507 1.00 89.24 C ANISOU 2465 CB ASN B 207 11637 13807 8464 -3351 -3796 4047 C ATOM 2466 CG ASN B 207 92.457 26.320 -46.794 1.00 97.16 C ANISOU 2466 CG ASN B 207 13365 14822 8728 -3284 -3900 3769 C ATOM 2467 OD1 ASN B 207 93.612 26.364 -47.213 1.00 98.27 O ANISOU 2467 OD1 ASN B 207 13913 14872 8553 -2874 -3565 3620 O ATOM 2468 ND2 ASN B 207 91.489 25.669 -47.428 1.00104.59 N ANISOU 2468 ND2 ASN B 207 14439 15883 9419 -3663 -4348 3695 N ATOM 2469 N THR B 208 92.582 26.574 -41.886 1.00 71.20 N ANISOU 2469 N THR B 208 8920 10764 7367 -3231 -2884 3269 N ATOM 2470 CA THR B 208 92.333 27.207 -40.603 1.00 66.60 C ANISOU 2470 CA THR B 208 7643 10097 7563 -3107 -2552 3270 C ATOM 2471 C THR B 208 93.225 26.573 -39.556 1.00 60.77 C ANISOU 2471 C THR B 208 7277 9051 6762 -2905 -2156 2762 C ATOM 2472 O THR B 208 93.127 25.373 -39.301 1.00 63.55 O ANISOU 2472 O THR B 208 8175 9254 6718 -3172 -2295 2484 O ATOM 2473 CB THR B 208 90.850 27.035 -40.166 1.00 67.85 C ANISOU 2473 CB THR B 208 7326 10394 8059 -3580 -2891 3474 C ATOM 2474 OG1 THR B 208 89.984 27.272 -41.281 1.00 73.10 O ANISOU 2474 OG1 THR B 208 7819 11372 8584 -3850 -3390 3896 O ATOM 2475 CG2 THR B 208 90.495 27.975 -39.027 1.00 65.08 C ANISOU 2475 CG2 THR B 208 6133 10042 8552 -3391 -2551 3579 C ATOM 2476 N THR B 209 94.097 27.349 -38.939 1.00 56.68 N ANISOU 2476 N THR B 209 6464 8432 6641 -2436 -1669 2636 N ATOM 2477 CA THR B 209 94.802 26.818 -37.781 1.00 54.99 C ANISOU 2477 CA THR B 209 6471 7990 6433 -2237 -1317 2174 C ATOM 2478 C THR B 209 93.886 26.986 -36.566 1.00 55.78 C ANISOU 2478 C THR B 209 5977 8126 7090 -2381 -1258 2196 C ATOM 2479 O THR B 209 93.212 28.011 -36.422 1.00 57.53 O ANISOU 2479 O THR B 209 5447 8499 7912 -2367 -1245 2491 O ATOM 2480 CB THR B 209 96.148 27.502 -37.555 1.00 49.13 C ANISOU 2480 CB THR B 209 5659 7141 5867 -1685 -839 1961 C ATOM 2481 OG1 THR B 209 97.039 27.151 -38.613 1.00 50.10 O ANISOU 2481 OG1 THR B 209 6413 7223 5400 -1552 -858 1912 O ATOM 2482 CG2 THR B 209 96.757 27.038 -36.265 1.00 45.52 C ANISOU 2482 CG2 THR B 209 5316 6520 5460 -1469 -512 1506 C ATOM 2483 N VAL B 210 93.831 25.971 -35.712 1.00 51.09 N ANISOU 2483 N VAL B 210 5720 7396 6296 -2509 -1211 1911 N ATOM 2484 CA VAL B 210 92.888 25.980 -34.600 1.00 51.08 C ANISOU 2484 CA VAL B 210 5219 7456 6734 -2679 -1163 1963 C ATOM 2485 C VAL B 210 93.501 25.495 -33.306 1.00 47.91 C ANISOU 2485 C VAL B 210 4984 6916 6306 -2418 -787 1570 C ATOM 2486 O VAL B 210 94.516 24.796 -33.297 1.00 46.37 O ANISOU 2486 O VAL B 210 5429 6543 5648 -2219 -654 1256 O ATOM 2487 CB VAL B 210 91.645 25.090 -34.880 1.00 60.20 C ANISOU 2487 CB VAL B 210 6515 8649 7707 -3291 -1608 2175 C ATOM 2488 CG1 VAL B 210 91.035 25.429 -36.233 1.00 61.70 C ANISOU 2488 CG1 VAL B 210 6613 9025 7807 -3566 -2056 2542 C ATOM 2489 CG2 VAL B 210 92.016 23.619 -34.807 1.00 56.03 C ANISOU 2489 CG2 VAL B 210 6848 7866 6573 -3468 -1670 1877 C ATOM 2490 N ALA B 211 92.844 25.868 -32.214 1.00 59.75 N ANISOU 2490 N ALA B 211 5891 8524 8289 -2403 -620 1608 N ATOM 2491 CA ALA B 211 93.193 25.422 -30.875 1.00 45.20 C ANISOU 2491 CA ALA B 211 4119 6628 6428 -2175 -285 1294 C ATOM 2492 C ALA B 211 92.152 24.421 -30.417 1.00 48.02 C ANISOU 2492 C ALA B 211 4600 6967 6679 -2622 -443 1442 C ATOM 2493 O ALA B 211 90.957 24.721 -30.447 1.00 50.62 O ANISOU 2493 O ALA B 211 4424 7443 7365 -2942 -624 1764 O ATOM 2494 CB ALA B 211 93.261 26.604 -29.929 1.00 43.00 C ANISOU 2494 CB ALA B 211 3076 6505 6756 -1787 60 1195 C ATOM 2495 N VAL B 212 92.586 23.234 -30.007 1.00 47.93 N ANISOU 2495 N VAL B 212 5247 6760 6204 -2634 -364 1226 N ATOM 2496 CA VAL B 212 91.633 22.214 -29.572 1.00 51.10 C ANISOU 2496 CA VAL B 212 5800 7086 6529 -3076 -482 1385 C ATOM 2497 C VAL B 212 91.774 21.864 -28.098 1.00 58.76 C ANISOU 2497 C VAL B 212 6718 8076 7531 -2812 -84 1234 C ATOM 2498 O VAL B 212 92.842 21.448 -27.639 1.00 55.32 O ANISOU 2498 O VAL B 212 6730 7530 6761 -2422 166 923 O ATOM 2499 CB VAL B 212 91.771 20.913 -30.372 1.00 57.86 C ANISOU 2499 CB VAL B 212 7519 7642 6823 -3428 -766 1337 C ATOM 2500 CG1 VAL B 212 90.609 20.002 -30.045 1.00 57.81 C ANISOU 2500 CG1 VAL B 212 7540 7545 6881 -3977 -930 1560 C ATOM 2501 CG2 VAL B 212 91.821 21.196 -31.873 1.00 55.07 C ANISOU 2501 CG2 VAL B 212 7329 7300 6294 -3610 -1149 1425 C ATOM 2502 N LYS B 213 90.690 22.039 -27.355 1.00 51.69 N ANISOU 2502 N LYS B 213 5259 7355 7026 -3002 -21 1472 N ATOM 2503 CA LYS B 213 90.665 21.654 -25.957 1.00 51.45 C ANISOU 2503 CA LYS B 213 5167 7388 6992 -2784 351 1395 C ATOM 2504 C LYS B 213 89.889 20.355 -25.811 1.00 57.67 C ANISOU 2504 C LYS B 213 6327 7979 7606 -3283 242 1627 C ATOM 2505 O LYS B 213 88.675 20.308 -26.043 1.00 59.00 O ANISOU 2505 O LYS B 213 6141 8202 8075 -3785 20 1966 O ATOM 2506 CB LYS B 213 90.046 22.754 -25.095 1.00 51.04 C ANISOU 2506 CB LYS B 213 4219 7680 7494 -2583 583 1478 C ATOM 2507 CG LYS B 213 89.864 22.350 -23.638 1.00 51.67 C ANISOU 2507 CG LYS B 213 4198 7892 7541 -2376 966 1446 C ATOM 2508 CD LYS B 213 89.352 23.503 -22.782 1.00 51.36 C ANISOU 2508 CD LYS B 213 3518 8061 7935 -1971 1176 1283 C ATOM 2509 CE LYS B 213 87.895 23.828 -23.049 1.00 62.47 C ANISOU 2509 CE LYS B 213 4701 9405 9628 -2199 958 1438 C ATOM 2510 NZ LYS B 213 87.391 24.874 -22.119 1.00 60.48 N1+ ANISOU 2510 NZ LYS B 213 4089 9307 9582 -1828 1147 1161 N1+ ATOM 2511 N LYS B 214 90.607 19.294 -25.458 1.00 59.65 N ANISOU 2511 N LYS B 214 7287 7981 7396 -3148 394 1452 N ATOM 2512 CA LYS B 214 89.996 17.999 -25.201 1.00 65.14 C ANISOU 2512 CA LYS B 214 8387 8418 7945 -3571 365 1657 C ATOM 2513 C LYS B 214 89.729 17.885 -23.710 1.00 69.88 C ANISOU 2513 C LYS B 214 8693 9201 8655 -3320 801 1754 C ATOM 2514 O LYS B 214 90.662 17.860 -22.902 1.00 57.37 O ANISOU 2514 O LYS B 214 7295 7690 6812 -2754 1139 1508 O ATOM 2515 CB LYS B 214 90.895 16.852 -25.676 1.00 67.25 C ANISOU 2515 CB LYS B 214 9624 8266 7661 -3559 302 1445 C ATOM 2516 CG LYS B 214 90.236 15.477 -25.637 1.00 75.83 C ANISOU 2516 CG LYS B 214 11182 8981 8648 -4084 214 1653 C ATOM 2517 CD LYS B 214 91.257 14.351 -25.809 1.00 83.21 C ANISOU 2517 CD LYS B 214 13076 9488 9052 -3918 282 1412 C ATOM 2518 CE LYS B 214 92.256 14.309 -24.647 1.00 85.10 C ANISOU 2518 CE LYS B 214 13447 9832 9056 -3209 763 1243 C ATOM 2519 NZ LYS B 214 93.008 13.018 -24.588 1.00 89.61 N1+ ANISOU 2519 NZ LYS B 214 14916 9958 9174 -3090 881 1126 N1+ ATOM 2520 N LEU B 215 88.448 17.832 -23.352 1.00 80.74 N ANISOU 2520 N LEU B 215 9585 10687 10405 -3728 792 2121 N ATOM 2521 CA LEU B 215 88.047 17.720 -21.952 1.00 78.95 C ANISOU 2521 CA LEU B 215 9038 10671 10287 -3522 1222 2278 C ATOM 2522 C LEU B 215 88.518 16.395 -21.357 1.00 84.56 C ANISOU 2522 C LEU B 215 10477 11084 10567 -3442 1457 2287 C ATOM 2523 O LEU B 215 88.483 15.358 -22.023 1.00 82.93 O ANISOU 2523 O LEU B 215 10883 10444 10180 -3860 1233 2354 O ATOM 2524 CB LEU B 215 86.527 17.868 -21.813 1.00 68.95 C ANISOU 2524 CB LEU B 215 7168 9509 9521 -3885 1139 2603 C ATOM 2525 CG LEU B 215 86.010 19.311 -21.762 1.00 67.54 C ANISOU 2525 CG LEU B 215 6245 9653 9764 -3555 1114 2465 C ATOM 2526 CD1 LEU B 215 86.557 20.131 -22.904 1.00 69.31 C ANISOU 2526 CD1 LEU B 215 6459 9869 10007 -3482 799 2265 C ATOM 2527 CD2 LEU B 215 84.503 19.360 -21.794 1.00 72.91 C ANISOU 2527 CD2 LEU B 215 6570 10333 10801 -3777 977 2623 C ATOM 2528 N ALA B 216 88.978 16.446 -20.107 1.00 82.85 N ANISOU 2528 N ALA B 216 10198 11104 10180 -2879 1904 2207 N ATOM 2529 CA ALA B 216 89.385 15.248 -19.373 1.00 91.42 C ANISOU 2529 CA ALA B 216 11902 11967 10868 -2717 2191 2285 C ATOM 2530 C ALA B 216 88.837 15.282 -17.946 1.00 96.01 C ANISOU 2530 C ALA B 216 12050 12899 11531 -2474 2646 2536 C ATOM 2531 O ALA B 216 88.543 16.357 -17.422 1.00 95.80 O ANISOU 2531 O ALA B 216 11313 13333 11753 -2214 2785 2477 O ATOM 2532 CB ALA B 216 90.898 15.123 -19.358 1.00 86.43 C ANISOU 2532 CB ALA B 216 11837 11264 9738 -2121 2277 1867 C ATOM 2533 N ALA B 217 88.707 14.115 -17.318 1.00100.85 N ANISOU 2533 N ALA B 217 13095 13289 11934 -2537 2898 2820 N ATOM 2534 CA ALA B 217 88.173 14.044 -15.960 1.00107.26 C ANISOU 2534 CA ALA B 217 13546 14440 12768 -2300 3366 3119 C ATOM 2535 C ALA B 217 89.188 14.525 -14.923 1.00105.70 C ANISOU 2535 C ALA B 217 13318 14680 12162 -1424 3708 2795 C ATOM 2536 O ALA B 217 88.853 14.704 -13.748 1.00110.03 O ANISOU 2536 O ALA B 217 13496 15642 12670 -1095 4101 2952 O ATOM 2537 CB ALA B 217 87.727 12.627 -15.641 1.00112.29 C ANISOU 2537 CB ALA B 217 14666 14672 13329 -2644 3548 3572 C ATOM 2538 N LEU B 226 78.955 15.258 -16.396 1.00126.33 N ANISOU 2538 N LEU B 226 15052 18252 14696 -5954 3649 1437 N ATOM 2539 CA LEU B 226 79.968 16.188 -16.907 1.00123.86 C ANISOU 2539 CA LEU B 226 14676 18162 14225 -5273 3163 1424 C ATOM 2540 C LEU B 226 79.515 16.969 -18.139 1.00122.88 C ANISOU 2540 C LEU B 226 13568 18539 14580 -5143 2739 1365 C ATOM 2541 O LEU B 226 79.766 18.175 -18.252 1.00120.33 O ANISOU 2541 O LEU B 226 12865 18510 14346 -4663 2658 1380 O ATOM 2542 CB LEU B 226 81.266 15.440 -17.255 1.00119.26 C ANISOU 2542 CB LEU B 226 14943 17274 13097 -5043 2654 1378 C ATOM 2543 CG LEU B 226 82.304 16.168 -18.137 1.00112.87 C ANISOU 2543 CG LEU B 226 14010 16703 12174 -4448 2053 1323 C ATOM 2544 CD1 LEU B 226 83.688 15.551 -17.991 1.00109.48 C ANISOU 2544 CD1 LEU B 226 14519 15924 11153 -4141 1750 1275 C ATOM 2545 CD2 LEU B 226 81.913 16.185 -19.613 1.00112.22 C ANISOU 2545 CD2 LEU B 226 13272 16931 12436 -4551 1538 1253 C ATOM 2546 N LYS B 227 78.885 16.260 -19.073 1.00128.47 N ANISOU 2546 N LYS B 227 13936 19313 15563 -5563 2439 1292 N ATOM 2547 CA LYS B 227 78.583 16.791 -20.403 1.00120.67 C ANISOU 2547 CA LYS B 227 12185 18725 14941 -5432 1893 1216 C ATOM 2548 C LYS B 227 77.731 18.052 -20.344 1.00123.60 C ANISOU 2548 C LYS B 227 11625 19528 15808 -5264 2113 1222 C ATOM 2549 O LYS B 227 77.670 18.810 -21.311 1.00116.32 O ANISOU 2549 O LYS B 227 10153 18938 15105 -4968 1672 1174 O ATOM 2550 CB LYS B 227 77.880 15.726 -21.257 1.00126.23 C ANISOU 2550 CB LYS B 227 12697 19383 15881 -5993 1598 1128 C ATOM 2551 CG LYS B 227 77.713 16.107 -22.726 1.00121.29 C ANISOU 2551 CG LYS B 227 11469 19087 15529 -5836 922 1038 C ATOM 2552 CD LYS B 227 77.124 14.963 -23.545 1.00124.68 C ANISOU 2552 CD LYS B 227 11834 19410 16127 -6388 584 943 C ATOM 2553 CE LYS B 227 77.301 15.194 -25.044 1.00122.46 C ANISOU 2553 CE LYS B 227 11270 19339 15921 -6148 -180 858 C ATOM 2554 NZ LYS B 227 76.629 16.435 -25.524 1.00122.80 N1+ ANISOU 2554 NZ LYS B 227 10382 19845 16432 -5873 -309 820 N1+ ATOM 2555 N GLN B 228 77.068 18.269 -19.212 1.00124.79 N ANISOU 2555 N GLN B 228 11639 19658 16119 -5441 2800 1278 N ATOM 2556 CA GLN B 228 76.327 19.505 -19.009 1.00126.44 C ANISOU 2556 CA GLN B 228 11034 20252 16754 -5219 3067 1285 C ATOM 2557 C GLN B 228 77.300 20.680 -19.088 1.00121.26 C ANISOU 2557 C GLN B 228 10517 19727 15831 -4506 2841 1334 C ATOM 2558 O GLN B 228 76.996 21.706 -19.692 1.00115.53 O ANISOU 2558 O GLN B 228 9133 19368 15397 -4190 2617 1304 O ATOM 2559 CB GLN B 228 75.578 19.489 -17.668 1.00128.11 C ANISOU 2559 CB GLN B 228 11215 20360 17102 -5508 3915 1341 C ATOM 2560 CG GLN B 228 74.385 18.528 -17.635 1.00136.28 C ANISOU 2560 CG GLN B 228 11879 21352 18549 -6253 4214 1269 C ATOM 2561 CD GLN B 228 73.529 18.656 -16.374 1.00142.21 C ANISOU 2561 CD GLN B 228 12466 22055 19511 -6535 5112 1309 C ATOM 2562 OE1 GLN B 228 74.044 18.686 -15.256 1.00140.23 O ANISOU 2562 OE1 GLN B 228 12943 21498 18838 -6408 5588 1418 O ATOM 2563 NE2 GLN B 228 72.213 18.727 -16.558 1.00147.85 N ANISOU 2563 NE2 GLN B 228 12224 23068 20885 -6914 5345 1205 N ATOM 2564 N GLN B 229 78.483 20.507 -18.506 1.00118.40 N ANISOU 2564 N GLN B 229 11030 19050 14909 -4257 2870 1394 N ATOM 2565 CA GLN B 229 79.497 21.560 -18.486 1.00113.33 C ANISOU 2565 CA GLN B 229 10580 18489 13990 -3624 2687 1425 C ATOM 2566 C GLN B 229 80.097 21.829 -19.871 1.00111.35 C ANISOU 2566 C GLN B 229 10177 18421 13709 -3339 1971 1355 C ATOM 2567 O GLN B 229 80.400 22.974 -20.226 1.00105.48 O ANISOU 2567 O GLN B 229 9161 17918 13001 -2887 1798 1357 O ATOM 2568 CB GLN B 229 80.603 21.195 -17.502 1.00114.13 C ANISOU 2568 CB GLN B 229 11654 18189 13521 -3461 2867 1474 C ATOM 2569 CG GLN B 229 81.677 22.250 -17.376 1.00112.61 C ANISOU 2569 CG GLN B 229 11673 18059 13055 -2847 2707 1486 C ATOM 2570 CD GLN B 229 82.423 22.146 -16.068 1.00116.98 C ANISOU 2570 CD GLN B 229 13027 18259 13160 -2685 3049 1534 C ATOM 2571 OE1 GLN B 229 82.153 21.262 -15.251 1.00119.67 O ANISOU 2571 OE1 GLN B 229 13832 18281 13355 -3020 3415 1567 O ATOM 2572 NE2 GLN B 229 83.365 23.053 -15.855 1.00114.55 N ANISOU 2572 NE2 GLN B 229 12917 17986 12622 -2175 2928 1529 N ATOM 2573 N PHE B 230 80.281 20.761 -20.639 1.00112.13 N ANISOU 2573 N PHE B 230 10513 18377 13715 -3608 1578 1293 N ATOM 2574 CA PHE B 230 80.717 20.863 -22.026 1.00 99.58 C ANISOU 2574 CA PHE B 230 8793 16933 12110 -3413 919 1219 C ATOM 2575 C PHE B 230 79.692 21.669 -22.824 1.00105.12 C ANISOU 2575 C PHE B 230 8583 18036 13322 -3381 743 1182 C ATOM 2576 O PHE B 230 80.054 22.527 -23.629 1.00 98.62 O ANISOU 2576 O PHE B 230 7565 17414 12493 -2981 377 1158 O ATOM 2577 CB PHE B 230 80.918 19.456 -22.610 1.00101.38 C ANISOU 2577 CB PHE B 230 9449 16903 12167 -3774 591 1161 C ATOM 2578 CG PHE B 230 80.929 19.396 -24.115 1.00100.89 C ANISOU 2578 CG PHE B 230 9127 16998 12207 -3727 -50 1077 C ATOM 2579 CD1 PHE B 230 82.103 19.598 -24.821 1.00 96.54 C ANISOU 2579 CD1 PHE B 230 8955 16415 11311 -3323 -463 1042 C ATOM 2580 CD2 PHE B 230 79.771 19.093 -24.820 1.00104.72 C ANISOU 2580 CD2 PHE B 230 9014 17644 13129 -4100 -235 1020 C ATOM 2581 CE1 PHE B 230 82.119 19.524 -26.204 1.00 96.78 C ANISOU 2581 CE1 PHE B 230 8824 16553 11396 -3278 -1024 968 C ATOM 2582 CE2 PHE B 230 79.779 19.019 -26.201 1.00104.26 C ANISOU 2582 CE2 PHE B 230 8788 17694 13130 -4043 -851 939 C ATOM 2583 CZ PHE B 230 80.953 19.233 -26.894 1.00102.53 C ANISOU 2583 CZ PHE B 230 9008 17421 12529 -3629 -1234 922 C ATOM 2584 N ASP B 231 78.411 21.400 -22.571 1.00111.24 N ANISOU 2584 N ASP B 231 8813 18915 14539 -3800 1020 1166 N ATOM 2585 CA ASP B 231 77.315 22.114 -23.228 1.00110.93 C ANISOU 2585 CA ASP B 231 7850 19261 15036 -3780 866 1103 C ATOM 2586 C ASP B 231 77.024 23.468 -22.578 1.00111.40 C ANISOU 2586 C ASP B 231 7504 19561 15263 -3395 1239 1156 C ATOM 2587 O ASP B 231 76.300 24.287 -23.148 1.00114.09 O ANISOU 2587 O ASP B 231 7135 20230 15982 -3215 1058 1102 O ATOM 2588 CB ASP B 231 76.037 21.264 -23.223 1.00121.57 C ANISOU 2588 CB ASP B 231 8706 20643 16844 -4402 1012 1029 C ATOM 2589 CG ASP B 231 76.095 20.107 -24.204 1.00123.23 C ANISOU 2589 CG ASP B 231 9122 20699 17000 -4755 493 947 C ATOM 2590 OD1 ASP B 231 76.742 20.259 -25.262 1.00119.63 O ANISOU 2590 OD1 ASP B 231 8836 20272 16346 -4459 -101 915 O ATOM 2591 OD2 ASP B 231 75.490 19.049 -23.918 1.00124.07 O1+ ANISOU 2591 OD2 ASP B 231 9248 20640 17252 -5338 695 913 O1+ ATOM 2592 N GLN B 232 77.575 23.700 -21.388 1.00108.46 N ANISOU 2592 N GLN B 232 7608 19008 14595 -3252 1735 1254 N ATOM 2593 CA GLN B 232 77.314 24.940 -20.664 1.00108.28 C ANISOU 2593 CA GLN B 232 7282 19169 14691 -2900 2133 1311 C ATOM 2594 C GLN B 232 78.219 26.058 -21.145 1.00107.77 C ANISOU 2594 C GLN B 232 7356 19211 14381 -2301 1796 1330 C ATOM 2595 O GLN B 232 77.814 27.221 -21.181 1.00107.87 O ANISOU 2595 O GLN B 232 6902 19481 14601 -1968 1852 1337 O ATOM 2596 CB GLN B 232 77.476 24.739 -19.155 1.00123.93 C ANISOU 2596 CB GLN B 232 9753 20887 16449 -3002 2817 1404 C ATOM 2597 CG GLN B 232 76.152 24.459 -18.441 1.00132.88 C ANISOU 2597 CG GLN B 232 10393 22084 18013 -3433 3406 1396 C ATOM 2598 CD GLN B 232 76.330 24.015 -16.998 1.00136.63 C ANISOU 2598 CD GLN B 232 11503 22211 18200 -3614 4082 1488 C ATOM 2599 OE1 GLN B 232 77.456 23.871 -16.516 1.00135.57 O ANISOU 2599 OE1 GLN B 232 12196 21778 17537 -3407 4062 1549 O ATOM 2600 NE2 GLN B 232 75.216 23.792 -16.301 1.00141.39 N ANISOU 2600 NE2 GLN B 232 11730 22842 19151 -3999 4685 1483 N ATOM 2601 N GLU B 233 79.445 25.706 -21.518 1.00102.44 N ANISOU 2601 N GLU B 233 7328 18330 13265 -2166 1458 1328 N ATOM 2602 CA GLU B 233 80.359 26.688 -22.083 1.00 97.11 C ANISOU 2602 CA GLU B 233 6798 17739 12359 -1655 1130 1326 C ATOM 2603 C GLU B 233 79.858 27.099 -23.471 1.00 97.00 C ANISOU 2603 C GLU B 233 6246 17992 12615 -1553 611 1253 C ATOM 2604 O GLU B 233 79.886 28.279 -23.824 1.00 91.83 O ANISOU 2604 O GLU B 233 5357 17530 12006 -1151 495 1257 O ATOM 2605 CB GLU B 233 81.793 26.136 -22.149 1.00 90.64 C ANISOU 2605 CB GLU B 233 6764 16639 11035 -1561 916 1312 C ATOM 2606 CG GLU B 233 82.826 27.131 -22.670 1.00 86.52 C ANISOU 2606 CG GLU B 233 6417 16184 10271 -1072 641 1293 C ATOM 2607 CD GLU B 233 84.261 26.608 -22.618 1.00 83.92 C ANISOU 2607 CD GLU B 233 6808 15595 9482 -966 482 1251 C ATOM 2608 OE1 GLU B 233 84.596 25.857 -21.673 1.00 82.52 O ANISOU 2608 OE1 GLU B 233 7092 15163 9098 -1116 732 1266 O ATOM 2609 OE2 GLU B 233 85.054 26.961 -23.526 1.00 75.27 O1+ ANISOU 2609 OE2 GLU B 233 5825 14543 8229 -721 112 1191 O1+ ATOM 2610 N ILE B 234 79.373 26.128 -24.242 1.00 96.20 N ANISOU 2610 N ILE B 234 5988 17881 12681 -1916 293 1183 N ATOM 2611 CA ILE B 234 78.889 26.396 -25.593 1.00 97.49 C ANISOU 2611 CA ILE B 234 5707 18258 13077 -1834 -259 1099 C ATOM 2612 C ILE B 234 77.697 27.356 -25.561 1.00104.92 C ANISOU 2612 C ILE B 234 5852 19523 14489 -1695 -153 1077 C ATOM 2613 O ILE B 234 77.408 28.044 -26.544 1.00104.69 O ANISOU 2613 O ILE B 234 5490 19689 14598 -1426 -579 1019 O ATOM 2614 CB ILE B 234 78.490 25.097 -26.323 1.00100.58 C ANISOU 2614 CB ILE B 234 6076 18557 13583 -2298 -603 1019 C ATOM 2615 CG1 ILE B 234 79.573 24.033 -26.145 1.00 97.55 C ANISOU 2615 CG1 ILE B 234 6495 17826 12742 -2462 -620 1039 C ATOM 2616 CG2 ILE B 234 78.252 25.363 -27.803 1.00101.12 C ANISOU 2616 CG2 ILE B 234 5872 18780 13769 -2145 -1258 929 C ATOM 2617 CD1 ILE B 234 79.346 22.783 -26.965 1.00100.01 C ANISOU 2617 CD1 ILE B 234 6907 18008 13083 -2867 -1014 962 C ATOM 2618 N LYS B 235 77.008 27.396 -24.425 1.00109.80 N ANISOU 2618 N LYS B 235 6194 20184 15340 -1861 423 1115 N ATOM 2619 CA LYS B 235 75.971 28.394 -24.192 1.00114.48 C ANISOU 2619 CA LYS B 235 6168 20979 16350 -1642 618 1072 C ATOM 2620 C LYS B 235 76.633 29.754 -23.993 1.00114.52 C ANISOU 2620 C LYS B 235 6463 20954 16097 -1056 677 1127 C ATOM 2621 O LYS B 235 76.349 30.713 -24.713 1.00116.67 O ANISOU 2621 O LYS B 235 6613 21227 16488 -678 362 1044 O ATOM 2622 CB LYS B 235 75.117 28.019 -22.974 1.00119.59 C ANISOU 2622 CB LYS B 235 6568 21584 17288 -1983 1282 1081 C ATOM 2623 CG LYS B 235 74.378 29.185 -22.313 1.00120.34 C ANISOU 2623 CG LYS B 235 6400 21657 17666 -1633 1651 1033 C ATOM 2624 CD LYS B 235 73.837 28.785 -20.939 1.00122.86 C ANISOU 2624 CD LYS B 235 6678 21872 18131 -1950 2405 1072 C ATOM 2625 CE LYS B 235 73.054 29.917 -20.278 1.00125.44 C ANISOU 2625 CE LYS B 235 6736 22166 18759 -1618 2778 1001 C ATOM 2626 NZ LYS B 235 72.296 29.460 -19.071 1.00127.45 N1+ ANISOU 2626 NZ LYS B 235 6869 22294 19261 -1966 3510 996 N1+ ATOM 2627 N VAL B 236 77.530 29.817 -23.016 1.00108.54 N ANISOU 2627 N VAL B 236 6133 20141 14965 -998 1076 1263 N ATOM 2628 CA VAL B 236 78.278 31.032 -22.718 1.00108.75 C ANISOU 2628 CA VAL B 236 6509 20101 14710 -491 1158 1313 C ATOM 2629 C VAL B 236 78.983 31.611 -23.950 1.00103.52 C ANISOU 2629 C VAL B 236 6050 19445 13837 -158 584 1270 C ATOM 2630 O VAL B 236 79.046 32.831 -24.123 1.00101.15 O ANISOU 2630 O VAL B 236 5844 19090 13500 251 523 1249 O ATOM 2631 CB VAL B 236 79.326 30.770 -21.614 1.00106.38 C ANISOU 2631 CB VAL B 236 6850 19586 13983 -507 1546 1415 C ATOM 2632 CG1 VAL B 236 80.328 31.917 -21.530 1.00102.03 C ANISOU 2632 CG1 VAL B 236 6667 19002 13099 -19 1504 1453 C ATOM 2633 CG2 VAL B 236 78.638 30.538 -20.273 1.00111.32 C ANISOU 2633 CG2 VAL B 236 7381 20157 14760 -725 2201 1470 C ATOM 2634 N MET B 237 79.501 30.739 -24.809 1.00 90.75 N ANISOU 2634 N MET B 237 4594 17819 12065 -351 176 1245 N ATOM 2635 CA MET B 237 80.243 31.192 -25.985 1.00 87.38 C ANISOU 2635 CA MET B 237 4419 17381 11401 -65 -326 1205 C ATOM 2636 C MET B 237 79.332 31.724 -27.083 1.00 93.31 C ANISOU 2636 C MET B 237 4909 18100 12445 84 -724 1086 C ATOM 2637 O MET B 237 79.687 32.671 -27.789 1.00 88.60 O ANISOU 2637 O MET B 237 4554 17412 11699 442 -959 1055 O ATOM 2638 CB MET B 237 81.109 30.063 -26.540 1.00 85.04 C ANISOU 2638 CB MET B 237 4620 16871 10820 -298 -614 1167 C ATOM 2639 CG MET B 237 82.240 29.661 -25.618 1.00 82.29 C ANISOU 2639 CG MET B 237 4889 16276 10103 -330 -310 1209 C ATOM 2640 SD MET B 237 83.024 31.093 -24.860 1.00 77.54 S ANISOU 2640 SD MET B 237 4514 15679 9271 137 2 1268 S ATOM 2641 CE MET B 237 84.728 30.885 -25.397 1.00 72.54 C ANISOU 2641 CE MET B 237 4562 14839 8161 277 -267 1205 C ATOM 2642 N ALA B 238 78.158 31.112 -27.221 1.00 98.76 N ANISOU 2642 N ALA B 238 5117 18851 13556 -203 -790 1010 N ATOM 2643 CA ALA B 238 77.204 31.511 -28.245 1.00 99.67 C ANISOU 2643 CA ALA B 238 4931 18941 14000 -71 -1202 872 C ATOM 2644 C ALA B 238 76.775 32.959 -28.030 1.00100.50 C ANISOU 2644 C ALA B 238 4930 19031 14224 358 -1065 855 C ATOM 2645 O ALA B 238 76.633 33.723 -28.986 1.00100.90 O ANISOU 2645 O ALA B 238 5050 19010 14279 660 -1444 788 O ATOM 2646 CB ALA B 238 76.011 30.590 -28.237 1.00110.30 C ANISOU 2646 CB ALA B 238 5728 20359 15823 -478 -1231 776 C ATOM 2647 N LYS B 239 76.587 33.326 -26.764 1.00103.55 N ANISOU 2647 N LYS B 239 5203 19462 14680 379 -518 918 N ATOM 2648 CA LYS B 239 76.238 34.695 -26.395 1.00105.29 C ANISOU 2648 CA LYS B 239 5376 19657 14972 773 -336 911 C ATOM 2649 C LYS B 239 77.426 35.630 -26.555 1.00101.73 C ANISOU 2649 C LYS B 239 5509 19107 14035 1125 -384 994 C ATOM 2650 O LYS B 239 77.361 36.616 -27.296 1.00 95.93 O ANISOU 2650 O LYS B 239 4876 18318 13256 1452 -657 953 O ATOM 2651 CB LYS B 239 75.725 34.759 -24.950 1.00109.20 C ANISOU 2651 CB LYS B 239 5654 20182 15657 675 291 948 C ATOM 2652 CG LYS B 239 74.327 34.164 -24.758 1.00117.67 C ANISOU 2652 CG LYS B 239 6067 21337 17307 382 412 828 C ATOM 2653 CD LYS B 239 73.590 34.745 -23.541 1.00119.49 C ANISOU 2653 CD LYS B 239 6053 21559 17789 453 990 812 C ATOM 2654 CE LYS B 239 74.239 34.344 -22.219 1.00115.98 C ANISOU 2654 CE LYS B 239 5970 21035 17061 270 1579 949 C ATOM 2655 NZ LYS B 239 73.339 34.635 -21.062 1.00118.19 N1+ ANISOU 2655 NZ LYS B 239 5977 21280 17648 232 2168 899 N1+ ATOM 2656 N CYS B 240 78.515 35.299 -25.868 1.00 97.35 N ANISOU 2656 N CYS B 240 5343 18522 13122 1042 -119 1103 N ATOM 2657 CA CYS B 240 79.673 36.178 -25.771 1.00 94.68 C ANISOU 2657 CA CYS B 240 5533 18084 12357 1339 -66 1170 C ATOM 2658 C CYS B 240 80.626 36.112 -26.969 1.00 93.72 C ANISOU 2658 C CYS B 240 5792 17893 11926 1410 -494 1145 C ATOM 2659 O CYS B 240 81.692 35.499 -26.887 1.00 93.05 O ANISOU 2659 O CYS B 240 6025 17784 11547 1296 -481 1181 O ATOM 2660 CB CYS B 240 80.452 35.859 -24.490 1.00 91.01 C ANISOU 2660 CB CYS B 240 5327 17591 11662 1243 385 1271 C ATOM 2661 SG CYS B 240 79.532 36.135 -22.951 1.00127.09 S ANISOU 2661 SG CYS B 240 9653 22142 16492 1210 985 1307 S ATOM 2662 N GLN B 241 80.247 36.754 -28.072 1.00 84.57 N ANISOU 2662 N GLN B 241 4623 16683 10828 1609 -861 1072 N ATOM 2663 CA GLN B 241 81.174 36.988 -29.174 1.00 81.50 C ANISOU 2663 CA GLN B 241 4689 16169 10110 1734 -1184 1047 C ATOM 2664 C GLN B 241 81.496 38.479 -29.251 1.00 80.08 C ANISOU 2664 C GLN B 241 4782 15914 9733 2103 -1110 1066 C ATOM 2665 O GLN B 241 80.596 39.315 -29.347 1.00 83.27 O ANISOU 2665 O GLN B 241 4968 16336 10335 2311 -1156 1041 O ATOM 2666 CB GLN B 241 80.602 36.479 -30.497 1.00 84.36 C ANISOU 2666 CB GLN B 241 4942 16481 10631 1653 -1690 952 C ATOM 2667 CG GLN B 241 80.467 34.955 -30.566 1.00 93.09 C ANISOU 2667 CG GLN B 241 5877 17637 11858 1262 -1814 929 C ATOM 2668 CD GLN B 241 79.757 34.462 -31.830 1.00 99.80 C ANISOU 2668 CD GLN B 241 6597 18413 12909 1179 -2338 823 C ATOM 2669 OE1 GLN B 241 79.425 35.246 -32.728 1.00100.44 O ANISOU 2669 OE1 GLN B 241 6753 18392 13018 1431 -2638 771 O ATOM 2670 NE2 GLN B 241 79.519 33.154 -31.898 1.00 99.51 N ANISOU 2670 NE2 GLN B 241 6390 18418 13003 818 -2464 792 N ATOM 2671 N HIS B 242 82.789 38.795 -29.194 1.00 76.98 N ANISOU 2671 N HIS B 242 4855 15438 8954 2178 -995 1099 N ATOM 2672 CA HIS B 242 83.274 40.168 -29.092 1.00 73.88 C ANISOU 2672 CA HIS B 242 4758 14982 8330 2482 -854 1126 C ATOM 2673 C HIS B 242 84.722 40.238 -29.604 1.00 69.67 C ANISOU 2673 C HIS B 242 4723 14340 7408 2493 -888 1106 C ATOM 2674 O HIS B 242 85.448 39.247 -29.560 1.00 67.52 O ANISOU 2674 O HIS B 242 4560 14055 7039 2279 -892 1088 O ATOM 2675 CB HIS B 242 83.162 40.652 -27.642 1.00 73.59 C ANISOU 2675 CB HIS B 242 4636 14994 8331 2548 -419 1201 C ATOM 2676 CG HIS B 242 83.524 42.090 -27.437 1.00 72.42 C ANISOU 2676 CG HIS B 242 4767 14780 7968 2855 -272 1231 C ATOM 2677 ND1 HIS B 242 84.826 42.513 -27.258 1.00 68.42 N ANISOU 2677 ND1 HIS B 242 4688 14197 7112 2915 -137 1248 N ATOM 2678 CD2 HIS B 242 82.755 43.200 -27.341 1.00 74.99 C ANISOU 2678 CD2 HIS B 242 4999 15110 8383 3118 -235 1242 C ATOM 2679 CE1 HIS B 242 84.839 43.825 -27.080 1.00 68.55 C ANISOU 2679 CE1 HIS B 242 4874 14171 7001 3187 -23 1277 C ATOM 2680 NE2 HIS B 242 83.597 44.263 -27.125 1.00 72.43 N ANISOU 2680 NE2 HIS B 242 5073 14708 7738 3324 -81 1279 N ATOM 2681 N GLU B 243 85.128 41.401 -30.104 1.00 68.87 N ANISOU 2681 N GLU B 243 4919 14159 7089 2745 -908 1097 N ATOM 2682 CA GLU B 243 86.448 41.579 -30.710 1.00 65.62 C ANISOU 2682 CA GLU B 243 4957 13636 6340 2760 -925 1055 C ATOM 2683 C GLU B 243 87.598 41.198 -29.770 1.00 67.59 C ANISOU 2683 C GLU B 243 5348 13903 6430 2640 -638 1059 C ATOM 2684 O GLU B 243 88.675 40.799 -30.214 1.00 59.60 O ANISOU 2684 O GLU B 243 4604 12813 5227 2543 -674 990 O ATOM 2685 CB GLU B 243 86.616 43.031 -31.170 1.00 65.86 C ANISOU 2685 CB GLU B 243 5260 13598 6168 3067 -916 1059 C ATOM 2686 CG GLU B 243 88.058 43.494 -31.283 1.00 73.49 C ANISOU 2686 CG GLU B 243 6646 14482 6795 3103 -754 1028 C ATOM 2687 CD GLU B 243 88.438 43.938 -32.689 1.00 75.21 C ANISOU 2687 CD GLU B 243 7239 14534 6801 3193 -972 968 C ATOM 2688 OE1 GLU B 243 87.601 44.610 -33.328 1.00 83.98 O ANISOU 2688 OE1 GLU B 243 8376 15595 7938 3395 -1173 982 O ATOM 2689 OE2 GLU B 243 89.565 43.621 -33.158 1.00 71.44 O1+ ANISOU 2689 OE2 GLU B 243 7055 13954 6136 3065 -940 898 O1+ ATOM 2690 N ASN B 244 87.359 41.317 -28.471 1.00 65.41 N ANISOU 2690 N ASN B 244 4906 13703 6242 2653 -359 1127 N ATOM 2691 CA ASN B 244 88.395 41.065 -27.493 1.00 58.89 C ANISOU 2691 CA ASN B 244 4240 12867 5267 2584 -113 1125 C ATOM 2692 C ASN B 244 88.133 39.819 -26.678 1.00 59.22 C ANISOU 2692 C ASN B 244 4067 12970 5464 2362 -40 1150 C ATOM 2693 O ASN B 244 88.672 39.672 -25.590 1.00 57.70 O ANISOU 2693 O ASN B 244 3967 12756 5198 2342 194 1165 O ATOM 2694 CB ASN B 244 88.553 42.273 -26.580 1.00 58.32 C ANISOU 2694 CB ASN B 244 4298 12759 5100 2790 163 1177 C ATOM 2695 CG ASN B 244 89.123 43.467 -27.311 1.00 57.54 C ANISOU 2695 CG ASN B 244 4474 12615 4774 3008 129 1149 C ATOM 2696 OD1 ASN B 244 88.423 44.435 -27.597 1.00 64.31 O ANISOU 2696 OD1 ASN B 244 5316 13471 5649 3218 102 1191 O ATOM 2697 ND2 ASN B 244 90.397 43.396 -27.640 1.00 54.97 N ANISOU 2697 ND2 ASN B 244 4400 12253 4233 2971 129 1065 N ATOM 2698 N LEU B 245 87.312 38.914 -27.203 1.00 61.49 N ANISOU 2698 N LEU B 245 4089 13318 5957 2196 -248 1150 N ATOM 2699 CA LEU B 245 87.140 37.613 -26.572 1.00 61.99 C ANISOU 2699 CA LEU B 245 3958 13461 6133 1956 -197 1172 C ATOM 2700 C LEU B 245 87.493 36.521 -27.561 1.00 61.57 C ANISOU 2700 C LEU B 245 3981 13388 6026 1763 -520 1101 C ATOM 2701 O LEU B 245 87.215 36.643 -28.747 1.00 62.65 O ANISOU 2701 O LEU B 245 4159 13455 6191 1775 -797 1053 O ATOM 2702 CB LEU B 245 85.714 37.415 -26.050 1.00 65.84 C ANISOU 2702 CB LEU B 245 4011 14046 6959 1873 -89 1237 C ATOM 2703 CG LEU B 245 85.189 38.329 -24.933 1.00 67.01 C ANISOU 2703 CG LEU B 245 4091 14170 7200 2027 266 1302 C ATOM 2704 CD1 LEU B 245 83.741 37.946 -24.538 1.00 74.77 C ANISOU 2704 CD1 LEU B 245 4599 15243 8566 1895 375 1329 C ATOM 2705 CD2 LEU B 245 86.086 38.349 -23.716 1.00 64.42 C ANISOU 2705 CD2 LEU B 245 4055 13755 6667 2048 584 1331 C ATOM 2706 N VAL B 246 88.121 35.458 -27.077 1.00 60.20 N ANISOU 2706 N VAL B 246 3873 13247 5754 1601 -494 1088 N ATOM 2707 CA VAL B 246 88.477 34.362 -27.950 1.00 59.94 C ANISOU 2707 CA VAL B 246 3980 13152 5642 1409 -799 1014 C ATOM 2708 C VAL B 246 87.231 33.695 -28.464 1.00 63.53 C ANISOU 2708 C VAL B 246 4096 13677 6364 1214 -1013 1043 C ATOM 2709 O VAL B 246 86.358 33.313 -27.685 1.00 68.64 O ANISOU 2709 O VAL B 246 4404 14438 7237 1071 -853 1110 O ATOM 2710 CB VAL B 246 89.340 33.318 -27.260 1.00 58.22 C ANISOU 2710 CB VAL B 246 4048 12803 5271 1245 -706 960 C ATOM 2711 CG1 VAL B 246 89.412 32.083 -28.129 1.00 58.86 C ANISOU 2711 CG1 VAL B 246 4236 12816 5314 1025 -1023 898 C ATOM 2712 CG2 VAL B 246 90.744 33.870 -27.009 1.00 54.85 C ANISOU 2712 CG2 VAL B 246 3980 12277 4585 1427 -591 870 C ATOM 2713 N GLU B 247 87.162 33.553 -29.782 1.00 64.22 N ANISOU 2713 N GLU B 247 4332 13624 6445 1185 -1338 969 N ATOM 2714 CA GLU B 247 85.973 33.052 -30.453 1.00 68.01 C ANISOU 2714 CA GLU B 247 4515 14133 7191 1033 -1615 965 C ATOM 2715 C GLU B 247 85.949 31.532 -30.553 1.00 75.92 C ANISOU 2715 C GLU B 247 5498 15153 8195 708 -1801 947 C ATOM 2716 O GLU B 247 86.956 30.908 -30.890 1.00 66.60 O ANISOU 2716 O GLU B 247 4721 13828 6757 654 -1893 886 O ATOM 2717 CB GLU B 247 85.874 33.649 -31.848 1.00 68.76 C ANISOU 2717 CB GLU B 247 4815 14047 7264 1182 -1910 894 C ATOM 2718 CG GLU B 247 84.726 33.094 -32.651 1.00 81.03 C ANISOU 2718 CG GLU B 247 6110 15593 9084 1047 -2276 860 C ATOM 2719 CD GLU B 247 84.704 33.606 -34.079 1.00 83.46 C ANISOU 2719 CD GLU B 247 6695 15692 9325 1208 -2615 793 C ATOM 2720 OE1 GLU B 247 83.629 33.545 -34.713 1.00 77.71 O ANISOU 2720 OE1 GLU B 247 5725 14956 8845 1197 -2932 760 O ATOM 2721 OE2 GLU B 247 85.764 34.060 -34.566 1.00 82.16 O1+ ANISOU 2721 OE2 GLU B 247 6984 15367 8864 1337 -2563 767 O1+ ATOM 2722 N LEU B 248 84.786 30.945 -30.266 1.00 65.79 N ANISOU 2722 N LEU B 248 4146 13389 7463 -861 -337 1013 N ATOM 2723 CA LEU B 248 84.611 29.499 -30.359 1.00 66.47 C ANISOU 2723 CA LEU B 248 4153 13436 7667 -1215 -376 899 C ATOM 2724 C LEU B 248 84.188 29.120 -31.786 1.00 63.48 C ANISOU 2724 C LEU B 248 3666 13273 7181 -1419 -601 775 C ATOM 2725 O LEU B 248 83.284 29.716 -32.359 1.00 65.77 O ANISOU 2725 O LEU B 248 3801 13801 7389 -1339 -726 828 O ATOM 2726 CB LEU B 248 83.590 29.015 -29.322 1.00 62.72 C ANISOU 2726 CB LEU B 248 3505 12946 7381 -1299 -288 981 C ATOM 2727 CG LEU B 248 83.271 27.513 -29.291 1.00 69.60 C ANISOU 2727 CG LEU B 248 4279 13747 8419 -1674 -299 882 C ATOM 2728 CD1 LEU B 248 84.535 26.706 -29.077 1.00 67.77 C ANISOU 2728 CD1 LEU B 248 4268 13246 8236 -1798 -199 791 C ATOM 2729 CD2 LEU B 248 82.259 27.175 -28.222 1.00 66.98 C ANISOU 2729 CD2 LEU B 248 3768 13406 8274 -1718 -186 989 C ATOM 2730 N LEU B 249 84.865 28.139 -32.366 1.00 63.41 N ANISOU 2730 N LEU B 249 3754 13174 7164 -1679 -652 603 N ATOM 2731 CA LEU B 249 84.619 27.784 -33.752 1.00 65.93 C ANISOU 2731 CA LEU B 249 4030 13676 7346 -1873 -873 449 C ATOM 2732 C LEU B 249 83.667 26.602 -33.871 1.00 72.67 C ANISOU 2732 C LEU B 249 4710 14561 8341 -2226 -964 344 C ATOM 2733 O LEU B 249 83.079 26.378 -34.929 1.00 78.26 O ANISOU 2733 O LEU B 249 5325 15460 8949 -2379 -1170 230 O ATOM 2734 CB LEU B 249 85.938 27.468 -34.465 1.00 64.00 C ANISOU 2734 CB LEU B 249 4019 13320 6979 -1955 -889 286 C ATOM 2735 CG LEU B 249 86.760 28.654 -34.972 1.00 61.57 C ANISOU 2735 CG LEU B 249 3852 13075 6466 -1649 -890 342 C ATOM 2736 CD1 LEU B 249 88.129 28.204 -35.446 1.00 59.58 C ANISOU 2736 CD1 LEU B 249 3822 12677 6139 -1750 -865 178 C ATOM 2737 CD2 LEU B 249 86.034 29.371 -36.079 1.00 64.03 C ANISOU 2737 CD2 LEU B 249 4070 13681 6576 -1547 -1085 366 C ATOM 2738 N GLY B 250 83.517 25.844 -32.790 1.00 69.68 N ANISOU 2738 N GLY B 250 4294 13986 8196 -2354 -808 381 N ATOM 2739 CA GLY B 250 82.704 24.645 -32.838 1.00 79.02 C ANISOU 2739 CA GLY B 250 5326 15146 9551 -2708 -863 279 C ATOM 2740 C GLY B 250 83.030 23.628 -31.764 1.00 82.34 C ANISOU 2740 C GLY B 250 5810 15260 10216 -2875 -655 290 C ATOM 2741 O GLY B 250 83.619 23.966 -30.739 1.00 84.20 O ANISOU 2741 O GLY B 250 6151 15341 10501 -2671 -460 425 O ATOM 2742 N PHE B 251 82.648 22.374 -31.995 1.00 85.50 N ANISOU 2742 N PHE B 251 6157 15559 10771 -3243 -693 148 N ATOM 2743 CA PHE B 251 82.784 21.342 -30.972 1.00 86.06 C ANISOU 2743 CA PHE B 251 6264 15333 11103 -3415 -485 183 C ATOM 2744 C PHE B 251 82.702 19.927 -31.537 1.00 88.71 C ANISOU 2744 C PHE B 251 6635 15493 11577 -3841 -539 -32 C ATOM 2745 O PHE B 251 82.225 19.715 -32.656 1.00 91.34 O ANISOU 2745 O PHE B 251 6904 15977 11823 -4026 -759 -210 O ATOM 2746 CB PHE B 251 81.703 21.522 -29.905 1.00 83.13 C ANISOU 2746 CB PHE B 251 5654 15029 10901 -3327 -375 381 C ATOM 2747 CG PHE B 251 80.303 21.457 -30.449 1.00 88.87 C ANISOU 2747 CG PHE B 251 6085 16006 11676 -3471 -551 346 C ATOM 2748 CD1 PHE B 251 79.634 20.242 -30.538 1.00 96.26 C ANISOU 2748 CD1 PHE B 251 6892 16848 12836 -3842 -570 242 C ATOM 2749 CD2 PHE B 251 79.658 22.606 -30.877 1.00 88.10 C ANISOU 2749 CD2 PHE B 251 5836 16226 11411 -3237 -693 419 C ATOM 2750 CE1 PHE B 251 78.334 20.171 -31.046 1.00100.98 C ANISOU 2750 CE1 PHE B 251 7195 17684 13490 -3983 -742 202 C ATOM 2751 CE2 PHE B 251 78.364 22.549 -31.384 1.00 96.53 C ANISOU 2751 CE2 PHE B 251 6614 17536 12526 -3363 -861 393 C ATOM 2752 CZ PHE B 251 77.698 21.327 -31.468 1.00100.96 C ANISOU 2752 CZ PHE B 251 7030 18020 13312 -3741 -893 279 C ATOM 2753 N SER B 252 83.158 18.965 -30.740 1.00 90.20 N ANISOU 2753 N SER B 252 6940 15350 11981 -3987 -331 -11 N ATOM 2754 CA SER B 252 83.037 17.555 -31.083 1.00 96.25 C ANISOU 2754 CA SER B 252 7755 15880 12934 -4390 -333 -191 C ATOM 2755 C SER B 252 82.512 16.758 -29.892 1.00 99.69 C ANISOU 2755 C SER B 252 8084 16107 13687 -4504 -116 -38 C ATOM 2756 O SER B 252 82.912 16.999 -28.750 1.00 97.24 O ANISOU 2756 O SER B 252 7826 15685 13435 -4293 101 168 O ATOM 2757 CB SER B 252 84.383 16.996 -31.546 1.00 99.85 C ANISOU 2757 CB SER B 252 8551 16057 13332 -4492 -283 -366 C ATOM 2758 OG SER B 252 84.243 15.670 -32.028 1.00106.56 O ANISOU 2758 OG SER B 252 9480 16663 14343 -4877 -302 -576 O ATOM 2759 N SER B 253 81.610 15.816 -30.160 1.00102.35 N ANISOU 2759 N SER B 253 8272 16393 14224 -4834 -174 -138 N ATOM 2760 CA SER B 253 81.048 14.978 -29.107 1.00103.45 C ANISOU 2760 CA SER B 253 8295 16324 14686 -4976 37 4 C ATOM 2761 C SER B 253 81.048 13.499 -29.498 1.00109.03 C ANISOU 2761 C SER B 253 9100 16706 15621 -5389 53 -176 C ATOM 2762 O SER B 253 79.991 12.901 -29.709 1.00112.20 O ANISOU 2762 O SER B 253 9284 17138 16209 -5650 -22 -238 O ATOM 2763 CB SER B 253 79.629 15.437 -28.762 1.00105.55 C ANISOU 2763 CB SER B 253 8192 16878 15034 -4930 -7 129 C ATOM 2764 OG SER B 253 78.841 15.584 -29.932 1.00108.05 O ANISOU 2764 OG SER B 253 8333 17461 15259 -5074 -298 -48 O ATOM 2765 N ASP B 254 82.240 12.914 -29.586 1.00108.93 N ANISOU 2765 N ASP B 254 9419 16366 15603 -5442 156 -261 N ATOM 2766 CA ASP B 254 82.382 11.491 -29.898 1.00112.08 C ANISOU 2766 CA ASP B 254 9976 16389 16221 -5804 204 -428 C ATOM 2767 C ASP B 254 83.224 10.755 -28.858 1.00110.93 C ANISOU 2767 C ASP B 254 10053 15824 16270 -5777 514 -258 C ATOM 2768 O ASP B 254 83.027 9.563 -28.618 1.00114.05 O ANISOU 2768 O ASP B 254 10497 15896 16942 -6038 631 -261 O ATOM 2769 CB ASP B 254 83.001 11.309 -31.282 1.00111.37 C ANISOU 2769 CB ASP B 254 10121 16264 15929 -5939 10 -763 C ATOM 2770 CG ASP B 254 82.108 11.828 -32.384 1.00113.41 C ANISOU 2770 CG ASP B 254 10171 16913 16007 -6009 -307 -938 C ATOM 2771 OD1 ASP B 254 80.877 11.628 -32.288 1.00113.82 O ANISOU 2771 OD1 ASP B 254 9921 17105 16220 -6157 -383 -901 O ATOM 2772 OD2 ASP B 254 82.635 12.443 -33.338 1.00113.38 O ANISOU 2772 OD2 ASP B 254 10298 17080 15702 -5908 -475 -1102 O ATOM 2773 N LEU B 258 85.420 14.407 -26.026 1.00 78.22 N ANISOU 2773 N LEU B 258 6052 12113 11554 -4405 897 470 N ATOM 2774 CA LEU B 258 84.812 15.739 -25.999 1.00 84.96 C ANISOU 2774 CA LEU B 258 6703 13362 12217 -4140 773 538 C ATOM 2775 C LEU B 258 85.810 16.879 -26.259 1.00 83.53 C ANISOU 2775 C LEU B 258 6670 13312 11754 -3827 703 527 C ATOM 2776 O LEU B 258 86.821 17.020 -25.557 1.00 82.51 O ANISOU 2776 O LEU B 258 6729 13028 11591 -3633 859 635 O ATOM 2777 CB LEU B 258 84.115 15.962 -24.667 1.00 77.39 C ANISOU 2777 CB LEU B 258 5585 12457 11362 -3980 959 781 C ATOM 2778 CG LEU B 258 82.762 15.262 -24.609 1.00 89.34 C ANISOU 2778 CG LEU B 258 6838 13996 13112 -4250 966 783 C ATOM 2779 CD1 LEU B 258 82.897 13.766 -24.891 1.00 91.29 C ANISOU 2779 CD1 LEU B 258 7182 13891 13613 -4627 1031 686 C ATOM 2780 CD2 LEU B 258 82.109 15.517 -23.263 1.00 90.31 C ANISOU 2780 CD2 LEU B 258 6822 14177 13314 -4083 1179 1011 C ATOM 2781 N CYS B 259 85.506 17.702 -27.262 1.00 83.54 N ANISOU 2781 N CYS B 259 6580 13605 11557 -3773 468 406 N ATOM 2782 CA CYS B 259 86.423 18.749 -27.713 1.00 75.24 C ANISOU 2782 CA CYS B 259 5665 12674 10249 -3512 388 372 C ATOM 2783 C CYS B 259 85.731 20.073 -28.005 1.00 76.71 C ANISOU 2783 C CYS B 259 5672 13226 10249 -3266 230 425 C ATOM 2784 O CYS B 259 84.651 20.098 -28.600 1.00 80.10 O ANISOU 2784 O CYS B 259 5895 13862 10677 -3390 70 367 O ATOM 2785 CB CYS B 259 87.155 18.298 -28.974 1.00 68.69 C ANISOU 2785 CB CYS B 259 5014 11758 9329 -3720 266 115 C ATOM 2786 SG CYS B 259 88.260 16.916 -28.746 1.00 98.66 S ANISOU 2786 SG CYS B 259 9104 15076 13306 -3946 467 32 S ATOM 2787 N LEU B 260 86.368 21.170 -27.602 1.00 71.65 N ANISOU 2787 N LEU B 260 5120 12648 9457 -2915 275 533 N ATOM 2788 CA LEU B 260 85.960 22.500 -28.043 1.00 63.87 C ANISOU 2788 CA LEU B 260 4034 11960 8273 -2661 130 568 C ATOM 2789 C LEU B 260 87.036 23.088 -28.955 1.00 65.72 C ANISOU 2789 C LEU B 260 4443 12226 8300 -2552 39 458 C ATOM 2790 O LEU B 260 88.227 22.973 -28.676 1.00 63.98 O ANISOU 2790 O LEU B 260 4427 11805 8076 -2487 156 448 O ATOM 2791 CB LEU B 260 85.703 23.415 -26.853 1.00 62.37 C ANISOU 2791 CB LEU B 260 3807 11813 8076 -2332 256 772 C ATOM 2792 CG LEU B 260 84.463 23.065 -26.029 1.00 68.55 C ANISOU 2792 CG LEU B 260 4379 12640 9028 -2404 336 885 C ATOM 2793 CD1 LEU B 260 84.383 23.929 -24.775 1.00 71.52 C ANISOU 2793 CD1 LEU B 260 4778 13023 9374 -2081 484 1060 C ATOM 2794 CD2 LEU B 260 83.210 23.226 -26.863 1.00 70.71 C ANISOU 2794 CD2 LEU B 260 4397 13182 9288 -2519 148 836 C ATOM 2795 N VAL B 261 86.613 23.702 -30.056 1.00 66.88 N ANISOU 2795 N VAL B 261 4504 12630 8277 -2531 -165 380 N ATOM 2796 CA VAL B 261 87.552 24.235 -31.031 1.00 64.93 C ANISOU 2796 CA VAL B 261 4407 12439 7824 -2446 -255 271 C ATOM 2797 C VAL B 261 87.510 25.753 -31.067 1.00 58.68 C ANISOU 2797 C VAL B 261 3592 11839 6865 -2070 -292 401 C ATOM 2798 O VAL B 261 86.438 26.335 -31.213 1.00 60.51 O ANISOU 2798 O VAL B 261 3648 12290 7055 -1983 -389 479 O ATOM 2799 CB VAL B 261 87.259 23.710 -32.448 1.00 68.72 C ANISOU 2799 CB VAL B 261 4863 13048 8198 -2724 -469 50 C ATOM 2800 CG1 VAL B 261 88.383 24.126 -33.397 1.00 61.23 C ANISOU 2800 CG1 VAL B 261 4104 12122 7038 -2655 -529 -78 C ATOM 2801 CG2 VAL B 261 87.068 22.195 -32.442 1.00 65.76 C ANISOU 2801 CG2 VAL B 261 4507 12464 8013 -3121 -441 -96 C ATOM 2802 N TYR B 262 88.674 26.389 -30.952 1.00 55.39 N ANISOU 2802 N TYR B 262 3356 11323 6365 -1852 -206 423 N ATOM 2803 CA TYR B 262 88.741 27.847 -30.971 1.00 53.74 C ANISOU 2803 CA TYR B 262 3164 11238 6017 -1494 -218 540 C ATOM 2804 C TYR B 262 89.586 28.392 -32.104 1.00 52.57 C ANISOU 2804 C TYR B 262 3125 11175 5676 -1417 -305 450 C ATOM 2805 O TYR B 262 90.373 27.673 -32.713 1.00 52.33 O ANISOU 2805 O TYR B 262 3195 11070 5620 -1614 -322 290 O ATOM 2806 CB TYR B 262 89.314 28.393 -29.672 1.00 50.96 C ANISOU 2806 CB TYR B 262 2935 10687 5742 -1236 -27 670 C ATOM 2807 CG TYR B 262 88.715 27.836 -28.412 1.00 57.62 C ANISOU 2807 CG TYR B 262 3714 11418 6762 -1287 92 762 C ATOM 2808 CD1 TYR B 262 89.119 26.600 -27.917 1.00 55.51 C ANISOU 2808 CD1 TYR B 262 3502 10945 6645 -1506 195 720 C ATOM 2809 CD2 TYR B 262 87.785 28.561 -27.686 1.00 52.50 C ANISOU 2809 CD2 TYR B 262 2961 10858 6128 -1108 121 896 C ATOM 2810 CE1 TYR B 262 88.594 26.096 -26.752 1.00 52.80 C ANISOU 2810 CE1 TYR B 262 3103 10503 6455 -1540 319 821 C ATOM 2811 CE2 TYR B 262 87.264 28.066 -26.524 1.00 53.36 C ANISOU 2811 CE2 TYR B 262 3011 10880 6383 -1148 241 979 C ATOM 2812 CZ TYR B 262 87.670 26.833 -26.064 1.00 53.51 C ANISOU 2812 CZ TYR B 262 3081 10709 6543 -1361 339 946 C ATOM 2813 OH TYR B 262 87.142 26.338 -24.903 1.00 62.52 O ANISOU 2813 OH TYR B 262 4163 11771 7821 -1395 474 1044 O ATOM 2814 N VAL B 263 89.423 29.685 -32.356 1.00 52.01 N ANISOU 2814 N VAL B 263 3043 11244 5473 -1126 -342 556 N ATOM 2815 CA VAL B 263 90.338 30.424 -33.202 1.00 53.33 C ANISOU 2815 CA VAL B 263 3332 11458 5472 -969 -374 522 C ATOM 2816 C VAL B 263 91.730 30.430 -32.572 1.00 49.19 C ANISOU 2816 C VAL B 263 2997 10668 5025 -875 -191 506 C ATOM 2817 O VAL B 263 91.877 30.620 -31.369 1.00 46.89 O ANISOU 2817 O VAL B 263 2768 10185 4862 -744 -46 599 O ATOM 2818 CB VAL B 263 89.872 31.865 -33.411 1.00 51.40 C ANISOU 2818 CB VAL B 263 3058 11360 5112 -651 -404 673 C ATOM 2819 CG1 VAL B 263 90.915 32.649 -34.177 1.00 48.95 C ANISOU 2819 CG1 VAL B 263 2889 11058 4651 -467 -401 662 C ATOM 2820 CG2 VAL B 263 88.549 31.885 -34.134 1.00 54.07 C ANISOU 2820 CG2 VAL B 263 3208 11969 5366 -728 -582 693 C ATOM 2821 N TYR B 264 92.745 30.212 -33.392 1.00 46.41 N ANISOU 2821 N TYR B 264 2859 10188 4587 -915 -194 371 N ATOM 2822 CA TYR B 264 94.123 30.201 -32.930 1.00 43.62 C ANISOU 2822 CA TYR B 264 2774 9492 4309 -806 -16 338 C ATOM 2823 C TYR B 264 94.687 31.613 -32.808 1.00 41.62 C ANISOU 2823 C TYR B 264 2583 9231 3998 -469 55 449 C ATOM 2824 O TYR B 264 94.494 32.424 -33.696 1.00 48.14 O ANISOU 2824 O TYR B 264 3405 10219 4668 -343 -33 480 O ATOM 2825 CB TYR B 264 94.965 29.370 -33.889 1.00 43.90 C ANISOU 2825 CB TYR B 264 3072 9320 4288 -970 -25 139 C ATOM 2826 CG TYR B 264 96.439 29.381 -33.608 1.00 46.91 C ANISOU 2826 CG TYR B 264 3719 9368 4738 -849 146 99 C ATOM 2827 CD1 TYR B 264 96.959 28.797 -32.454 1.00 39.99 C ANISOU 2827 CD1 TYR B 264 2883 8259 4052 -870 288 124 C ATOM 2828 CD2 TYR B 264 97.320 29.965 -34.505 1.00 40.56 C ANISOU 2828 CD2 TYR B 264 3116 8490 3806 -712 166 46 C ATOM 2829 CE1 TYR B 264 98.335 28.806 -32.203 1.00 37.90 C ANISOU 2829 CE1 TYR B 264 2836 7709 3853 -752 429 90 C ATOM 2830 CE2 TYR B 264 98.674 29.972 -34.274 1.00 38.49 C ANISOU 2830 CE2 TYR B 264 3067 7936 3623 -610 322 9 C ATOM 2831 CZ TYR B 264 99.184 29.394 -33.127 1.00 41.63 C ANISOU 2831 CZ TYR B 264 3485 8117 4214 -629 444 27 C ATOM 2832 OH TYR B 264 100.546 29.422 -32.917 1.00 39.71 O ANISOU 2832 OH TYR B 264 3430 7607 4052 -519 584 -7 O ATOM 2833 N MET B 265 95.355 31.921 -31.700 1.00 39.39 N ANISOU 2833 N MET B 265 2360 8767 3841 -322 213 511 N ATOM 2834 CA MET B 265 95.958 33.241 -31.530 1.00 37.64 C ANISOU 2834 CA MET B 265 2211 8500 3592 -25 292 591 C ATOM 2835 C MET B 265 97.483 33.141 -31.677 1.00 46.30 C ANISOU 2835 C MET B 265 3586 9284 4723 13 402 492 C ATOM 2836 O MET B 265 98.178 32.710 -30.762 1.00 41.32 O ANISOU 2836 O MET B 265 3026 8450 4223 3 510 472 O ATOM 2837 CB MET B 265 95.595 33.846 -30.182 1.00 36.85 C ANISOU 2837 CB MET B 265 2163 8245 3596 132 336 692 C ATOM 2838 CG MET B 265 94.096 33.954 -29.925 1.00 38.89 C ANISOU 2838 CG MET B 265 2244 8693 3837 111 252 784 C ATOM 2839 SD MET B 265 93.172 34.725 -31.274 1.00 41.11 S ANISOU 2839 SD MET B 265 2371 9311 3936 180 108 846 S ATOM 2840 CE MET B 265 91.478 34.545 -30.722 1.00 43.63 C ANISOU 2840 CE MET B 265 2489 9790 4298 113 43 935 C ATOM 2841 N PRO B 266 98.004 33.552 -32.835 1.00 35.82 N ANISOU 2841 N PRO B 266 2407 7930 3273 67 378 440 N ATOM 2842 CA PRO B 266 99.397 33.208 -33.137 1.00 39.14 C ANISOU 2842 CA PRO B 266 3076 8065 3731 51 482 327 C ATOM 2843 C PRO B 266 100.449 33.927 -32.307 1.00 32.28 C ANISOU 2843 C PRO B 266 2287 6996 2982 243 626 365 C ATOM 2844 O PRO B 266 101.611 33.542 -32.367 1.00 39.11 O ANISOU 2844 O PRO B 266 3320 7626 3915 223 718 278 O ATOM 2845 CB PRO B 266 99.540 33.573 -34.627 1.00 35.63 C ANISOU 2845 CB PRO B 266 2751 7688 3097 74 425 285 C ATOM 2846 CG PRO B 266 98.348 34.377 -34.969 1.00 37.14 C ANISOU 2846 CG PRO B 266 2761 8190 3162 167 300 408 C ATOM 2847 CD PRO B 266 97.268 34.029 -34.016 1.00 37.73 C ANISOU 2847 CD PRO B 266 2593 8416 3327 90 242 470 C ATOM 2848 N ASN B 267 100.104 34.940 -31.538 1.00 31.69 N ANISOU 2848 N ASN B 267 2120 6973 2948 420 638 476 N ATOM 2849 CA ASN B 267 101.170 35.539 -30.745 1.00 29.83 C ANISOU 2849 CA ASN B 267 2066 6412 2857 544 705 460 C ATOM 2850 C ASN B 267 101.095 35.107 -29.292 1.00 29.12 C ANISOU 2850 C ASN B 267 1976 6191 2899 509 703 465 C ATOM 2851 O ASN B 267 101.700 35.735 -28.434 1.00 29.98 O ANISOU 2851 O ASN B 267 2192 6098 3102 606 726 459 O ATOM 2852 CB ASN B 267 101.140 37.055 -30.855 1.00 37.24 C ANISOU 2852 CB ASN B 267 3060 7308 3781 739 696 532 C ATOM 2853 CG ASN B 267 101.770 37.550 -32.138 1.00 43.09 C ANISOU 2853 CG ASN B 267 3885 8053 4434 806 750 524 C ATOM 2854 OD1 ASN B 267 102.896 37.162 -32.475 1.00 36.68 O ANISOU 2854 OD1 ASN B 267 3202 7069 3664 759 834 436 O ATOM 2855 ND2 ASN B 267 101.049 38.400 -32.871 1.00 31.18 N ANISOU 2855 ND2 ASN B 267 2312 6741 2795 925 713 627 N ATOM 2856 N GLY B 268 100.364 34.022 -29.039 1.00 30.09 N ANISOU 2856 N GLY B 268 1974 6441 3017 355 678 473 N ATOM 2857 CA GLY B 268 100.262 33.430 -27.721 1.00 29.78 C ANISOU 2857 CA GLY B 268 1933 6299 3084 313 697 495 C ATOM 2858 C GLY B 268 99.788 34.384 -26.644 1.00 29.49 C ANISOU 2858 C GLY B 268 1913 6225 3066 453 670 561 C ATOM 2859 O GLY B 268 99.015 35.290 -26.926 1.00 30.16 O ANISOU 2859 O GLY B 268 1946 6432 3081 541 622 616 O ATOM 2860 N SER B 269 100.241 34.193 -25.407 1.00 28.71 N ANISOU 2860 N SER B 269 1885 5977 3047 478 708 557 N ATOM 2861 CA SER B 269 99.698 34.987 -24.308 1.00 28.80 C ANISOU 2861 CA SER B 269 1902 5989 3051 585 694 607 C ATOM 2862 C SER B 269 100.465 36.283 -24.060 1.00 39.94 C ANISOU 2862 C SER B 269 3441 7255 4478 727 700 563 C ATOM 2863 O SER B 269 101.629 36.428 -24.441 1.00 41.02 O ANISOU 2863 O SER B 269 3677 7247 4664 737 722 492 O ATOM 2864 CB SER B 269 99.667 34.169 -23.022 1.00 28.95 C ANISOU 2864 CB SER B 269 1912 5974 3114 542 731 636 C ATOM 2865 OG SER B 269 100.971 33.824 -22.624 1.00 36.40 O ANISOU 2865 OG SER B 269 2963 6748 4118 550 769 579 O ATOM 2866 N LEU B 270 99.799 37.216 -23.402 1.00 28.18 N ANISOU 2866 N LEU B 270 1943 5805 2958 826 691 602 N ATOM 2867 CA LEU B 270 100.442 38.426 -22.948 1.00 27.49 C ANISOU 2867 CA LEU B 270 1964 5583 2900 937 709 553 C ATOM 2868 C LEU B 270 101.615 38.111 -22.048 1.00 26.49 C ANISOU 2868 C LEU B 270 1923 5308 2834 919 731 479 C ATOM 2869 O LEU B 270 102.638 38.797 -22.084 1.00 35.06 O ANISOU 2869 O LEU B 270 3096 6251 3975 956 745 403 O ATOM 2870 CB LEU B 270 99.448 39.300 -22.209 1.00 28.50 C ANISOU 2870 CB LEU B 270 2054 5791 2984 1035 715 603 C ATOM 2871 CG LEU B 270 99.973 40.582 -21.582 1.00 37.10 C ANISOU 2871 CG LEU B 270 3236 6754 4104 1141 747 543 C ATOM 2872 CD1 LEU B 270 100.613 41.451 -22.648 1.00 27.78 C ANISOU 2872 CD1 LEU B 270 2119 5472 2966 1180 758 509 C ATOM 2873 CD2 LEU B 270 98.813 41.303 -20.859 1.00 29.60 C ANISOU 2873 CD2 LEU B 270 2231 5909 3106 1239 769 600 C ATOM 2874 N LEU B 271 101.483 37.070 -21.236 1.00 28.89 N ANISOU 2874 N LEU B 271 2190 5657 3131 865 738 509 N ATOM 2875 CA LEU B 271 102.561 36.720 -20.323 1.00 27.99 C ANISOU 2875 CA LEU B 271 2140 5443 3052 869 753 461 C ATOM 2876 C LEU B 271 103.813 36.373 -21.120 1.00 34.42 C ANISOU 2876 C LEU B 271 3011 6121 3945 822 763 391 C ATOM 2877 O LEU B 271 104.907 36.870 -20.825 1.00 33.22 O ANISOU 2877 O LEU B 271 2927 5851 3845 860 766 317 O ATOM 2878 CB LEU B 271 102.155 35.561 -19.416 1.00 36.60 C ANISOU 2878 CB LEU B 271 3172 6621 4113 827 774 536 C ATOM 2879 CG LEU B 271 103.293 35.017 -18.533 1.00 32.75 C ANISOU 2879 CG LEU B 271 2734 6064 3645 845 788 515 C ATOM 2880 CD1 LEU B 271 103.884 36.118 -17.662 1.00 29.49 C ANISOU 2880 CD1 LEU B 271 2383 5618 3204 952 770 449 C ATOM 2881 CD2 LEU B 271 102.840 33.844 -17.700 1.00 27.37 C ANISOU 2881 CD2 LEU B 271 1992 5477 2931 812 826 621 C ATOM 2882 N ASP B 272 103.647 35.541 -22.144 1.00 25.20 N ANISOU 2882 N ASP B 272 1805 4981 2790 737 774 409 N ATOM 2883 CA ASP B 272 104.771 35.151 -22.981 1.00 24.51 C ANISOU 2883 CA ASP B 272 1768 4774 2772 697 804 344 C ATOM 2884 C ASP B 272 105.428 36.336 -23.651 1.00 35.41 C ANISOU 2884 C ASP B 272 3219 6050 4185 752 806 279 C ATOM 2885 O ASP B 272 106.660 36.417 -23.774 1.00 28.55 O ANISOU 2885 O ASP B 272 2409 5040 3398 753 833 208 O ATOM 2886 CB ASP B 272 104.328 34.176 -24.066 1.00 36.85 C ANISOU 2886 CB ASP B 272 3270 6416 4317 595 829 365 C ATOM 2887 CG ASP B 272 103.787 32.882 -23.509 1.00 36.63 C ANISOU 2887 CG ASP B 272 3164 6465 4289 505 853 427 C ATOM 2888 OD1 ASP B 272 104.123 32.525 -22.343 1.00 31.19 O ANISOU 2888 OD1 ASP B 272 2489 5735 3626 533 868 455 O ATOM 2889 OD2 ASP B 272 103.035 32.229 -24.271 1.00 41.86 O1+ ANISOU 2889 OD2 ASP B 272 3741 7242 4922 397 862 451 O1+ ATOM 2890 N ARG B 273 104.602 37.247 -24.127 1.00 24.34 N ANISOU 2890 N ARG B 273 1799 4722 2726 799 786 312 N ATOM 2891 CA ARG B 273 105.127 38.385 -24.828 1.00 24.07 C ANISOU 2891 CA ARG B 273 1826 4596 2724 855 806 274 C ATOM 2892 C ARG B 273 105.795 39.365 -23.860 1.00 31.40 C ANISOU 2892 C ARG B 273 2806 5405 3719 910 814 212 C ATOM 2893 O ARG B 273 106.799 39.972 -24.203 1.00 34.84 O ANISOU 2893 O ARG B 273 3293 5706 4238 916 849 143 O ATOM 2894 CB ARG B 273 104.018 39.060 -25.637 1.00 24.93 C ANISOU 2894 CB ARG B 273 1890 4840 2744 910 789 350 C ATOM 2895 CG ARG B 273 103.713 38.358 -26.985 1.00 25.45 C ANISOU 2895 CG ARG B 273 1907 5024 2738 859 791 383 C ATOM 2896 CD ARG B 273 104.955 37.647 -27.609 1.00 24.81 C ANISOU 2896 CD ARG B 273 1892 4818 2717 790 849 305 C ATOM 2897 NE ARG B 273 104.716 36.211 -27.553 1.00 30.73 N ANISOU 2897 NE ARG B 273 2582 5647 3448 683 850 302 N ATOM 2898 CZ ARG B 273 105.627 35.287 -27.315 1.00 32.11 C ANISOU 2898 CZ ARG B 273 2794 5707 3701 621 898 245 C ATOM 2899 NH1 ARG B 273 106.899 35.604 -27.155 1.00 34.28 N1+ ANISOU 2899 NH1 ARG B 273 3156 5792 4078 651 938 180 N1+ ATOM 2900 NH2 ARG B 273 105.251 34.025 -27.257 1.00 46.03 N ANISOU 2900 NH2 ARG B 273 4491 7551 5446 521 913 258 N ATOM 2901 N LEU B 274 105.255 39.527 -22.654 1.00 34.30 N ANISOU 2901 N LEU B 274 3150 5832 4050 947 790 229 N ATOM 2902 CA LEU B 274 105.904 40.404 -21.678 1.00 24.04 C ANISOU 2902 CA LEU B 274 1888 4448 2800 998 800 154 C ATOM 2903 C LEU B 274 107.257 39.834 -21.292 1.00 29.92 C ANISOU 2903 C LEU B 274 2652 5094 3621 956 803 83 C ATOM 2904 O LEU B 274 108.199 40.567 -20.958 1.00 29.44 O ANISOU 2904 O LEU B 274 2613 4934 3641 976 820 -4 O ATOM 2905 CB LEU B 274 105.045 40.583 -20.437 1.00 24.78 C ANISOU 2905 CB LEU B 274 1951 4652 2812 1055 785 188 C ATOM 2906 CG LEU B 274 103.904 41.586 -20.610 1.00 27.76 C ANISOU 2906 CG LEU B 274 2309 5095 3145 1131 799 234 C ATOM 2907 CD1 LEU B 274 103.047 41.655 -19.352 1.00 26.56 C ANISOU 2907 CD1 LEU B 274 2122 5059 2912 1189 800 266 C ATOM 2908 CD2 LEU B 274 104.485 42.944 -20.988 1.00 25.74 C ANISOU 2908 CD2 LEU B 274 2102 4707 2971 1182 843 161 C ATOM 2909 N SER B 275 107.359 38.513 -21.349 1.00 34.08 N ANISOU 2909 N SER B 275 3158 5657 4133 901 792 120 N ATOM 2910 CA SER B 275 108.546 37.883 -20.833 1.00 35.40 C ANISOU 2910 CA SER B 275 3328 5759 4363 886 792 75 C ATOM 2911 C SER B 275 109.472 37.535 -21.989 1.00 27.84 C ANISOU 2911 C SER B 275 2391 4682 3504 832 831 31 C ATOM 2912 O SER B 275 110.521 36.918 -21.797 1.00 39.61 O ANISOU 2912 O SER B 275 3873 6108 5067 819 840 -4 O ATOM 2913 CB SER B 275 108.172 36.657 -20.001 1.00 23.32 C ANISOU 2913 CB SER B 275 1758 4338 2763 882 776 152 C ATOM 2914 OG SER B 275 107.822 35.592 -20.833 1.00 25.96 O ANISOU 2914 OG SER B 275 2072 4690 3103 813 803 202 O ATOM 2915 N CYS B 276 109.062 37.956 -23.183 1.00 33.75 N ANISOU 2915 N CYS B 276 3160 5418 4245 815 858 39 N ATOM 2916 CA CYS B 276 109.817 37.773 -24.420 1.00 22.17 C ANISOU 2916 CA CYS B 276 1722 3860 2843 774 912 -1 C ATOM 2917 C CYS B 276 110.247 36.321 -24.552 1.00 24.22 C ANISOU 2917 C CYS B 276 1966 4113 3122 725 935 4 C ATOM 2918 O CYS B 276 111.379 36.006 -24.917 1.00 23.12 O ANISOU 2918 O CYS B 276 1840 3871 3074 706 977 -58 O ATOM 2919 CB CYS B 276 110.990 38.721 -24.443 1.00 22.05 C ANISOU 2919 CB CYS B 276 1724 3710 2944 785 940 -95 C ATOM 2920 SG CYS B 276 110.512 40.454 -24.416 1.00 32.31 S ANISOU 2920 SG CYS B 276 3039 4998 4239 845 947 -107 S ATOM 2921 N LEU B 277 109.318 35.430 -24.218 1.00 27.97 N ANISOU 2921 N LEU B 277 2403 4705 3519 706 917 78 N ATOM 2922 CA LEU B 277 109.548 33.995 -24.337 1.00 26.95 C ANISOU 2922 CA LEU B 277 2251 4579 3410 658 962 95 C ATOM 2923 C LEU B 277 109.956 33.647 -25.761 1.00 40.77 C ANISOU 2923 C LEU B 277 4035 6276 5181 613 1040 51 C ATOM 2924 O LEU B 277 109.462 34.243 -26.728 1.00 31.50 O ANISOU 2924 O LEU B 277 2881 5144 3944 607 1049 51 O ATOM 2925 CB LEU B 277 108.290 33.236 -23.923 1.00 38.82 C ANISOU 2925 CB LEU B 277 3691 6230 4827 621 948 187 C ATOM 2926 CG LEU B 277 108.272 31.711 -23.880 1.00 42.85 C ANISOU 2926 CG LEU B 277 4161 6761 5360 557 1013 231 C ATOM 2927 CD1 LEU B 277 109.340 31.168 -22.925 1.00 44.89 C ANISOU 2927 CD1 LEU B 277 4426 6934 5695 614 1027 241 C ATOM 2928 CD2 LEU B 277 106.879 31.264 -23.449 1.00 40.54 C ANISOU 2928 CD2 LEU B 277 3789 6624 4989 500 995 325 C ATOM 2929 N ASP B 278 110.894 32.714 -25.879 1.00 36.85 N ANISOU 2929 N ASP B 278 3546 5693 4761 599 1104 16 N ATOM 2930 CA ASP B 278 111.428 32.275 -27.171 1.00 34.71 C ANISOU 2930 CA ASP B 278 3322 5362 4506 565 1202 -40 C ATOM 2931 C ASP B 278 112.133 33.341 -27.994 1.00 28.48 C ANISOU 2931 C ASP B 278 2587 4496 3737 586 1213 -110 C ATOM 2932 O ASP B 278 112.350 33.156 -29.185 1.00 32.73 O ANISOU 2932 O ASP B 278 3179 5020 4239 565 1294 -145 O ATOM 2933 CB ASP B 278 110.307 31.658 -28.007 1.00 38.00 C ANISOU 2933 CB ASP B 278 3726 5906 4805 495 1252 -4 C ATOM 2934 CG ASP B 278 109.859 30.321 -27.457 1.00 48.54 C ANISOU 2934 CG ASP B 278 5001 7295 6147 437 1291 54 C ATOM 2935 OD1 ASP B 278 110.740 29.516 -27.078 1.00 50.70 O ANISOU 2935 OD1 ASP B 278 5293 7437 6533 463 1360 55 O ATOM 2936 OD2 ASP B 278 108.634 30.088 -27.376 1.00 47.94 O1+ ANISOU 2936 OD2 ASP B 278 4852 7384 5979 363 1254 109 O1+ ATOM 2937 N GLY B 279 112.525 34.445 -27.381 1.00 24.92 N ANISOU 2937 N GLY B 279 2126 4004 3337 624 1147 -132 N ATOM 2938 CA GLY B 279 113.343 35.417 -28.095 1.00 22.50 C ANISOU 2938 CA GLY B 279 1852 3631 3066 637 1167 -195 C ATOM 2939 C GLY B 279 112.556 36.493 -28.820 1.00 32.02 C ANISOU 2939 C GLY B 279 3095 4876 4197 652 1178 -155 C ATOM 2940 O GLY B 279 113.118 37.316 -29.533 1.00 33.90 O ANISOU 2940 O GLY B 279 3364 5068 4447 669 1213 -181 O ATOM 2941 N THR B 280 111.243 36.517 -28.631 1.00 31.26 N ANISOU 2941 N THR B 280 2982 4890 4005 664 1140 -74 N ATOM 2942 CA THR B 280 110.424 37.506 -29.335 1.00 29.30 C ANISOU 2942 CA THR B 280 2753 4717 3663 708 1137 -14 C ATOM 2943 C THR B 280 110.722 38.930 -28.834 1.00 27.82 C ANISOU 2943 C THR B 280 2569 4457 3545 760 1115 -31 C ATOM 2944 O THR B 280 111.077 39.125 -27.688 1.00 22.50 O ANISOU 2944 O THR B 280 1865 3733 2950 760 1072 -75 O ATOM 2945 CB THR B 280 108.942 37.183 -29.168 1.00 33.46 C ANISOU 2945 CB THR B 280 3223 5428 4063 715 1074 73 C ATOM 2946 OG1 THR B 280 108.592 37.278 -27.780 1.00 28.06 O ANISOU 2946 OG1 THR B 280 2494 4754 3412 729 1001 87 O ATOM 2947 CG2 THR B 280 108.666 35.777 -29.634 1.00 23.92 C ANISOU 2947 CG2 THR B 280 1992 4307 2790 642 1106 71 C ATOM 2948 N PRO B 281 110.587 39.937 -29.698 1.00 36.80 N ANISOU 2948 N PRO B 281 3743 5594 4645 812 1156 7 N ATOM 2949 CA PRO B 281 111.065 41.232 -29.182 1.00 33.41 C ANISOU 2949 CA PRO B 281 3313 5073 4307 852 1158 -31 C ATOM 2950 C PRO B 281 110.146 41.799 -28.146 1.00 29.88 C ANISOU 2950 C PRO B 281 2832 4681 3841 899 1095 -1 C ATOM 2951 O PRO B 281 108.990 41.391 -28.102 1.00 33.57 O ANISOU 2951 O PRO B 281 3275 5281 4200 920 1049 81 O ATOM 2952 CB PRO B 281 111.105 42.137 -30.419 1.00 24.27 C ANISOU 2952 CB PRO B 281 2212 3898 3112 912 1240 33 C ATOM 2953 CG PRO B 281 110.434 41.383 -31.490 1.00 32.11 C ANISOU 2953 CG PRO B 281 3231 5007 3962 917 1262 110 C ATOM 2954 CD PRO B 281 110.447 39.920 -31.159 1.00 27.06 C ANISOU 2954 CD PRO B 281 2561 4407 3312 832 1228 59 C ATOM 2955 N PRO B 282 110.653 42.706 -27.302 1.00 37.90 N ANISOU 2955 N PRO B 282 3832 5614 4953 916 1093 -77 N ATOM 2956 CA PRO B 282 109.766 43.316 -26.302 1.00 31.24 C ANISOU 2956 CA PRO B 282 2967 4820 4084 972 1052 -56 C ATOM 2957 C PRO B 282 108.656 44.096 -26.971 1.00 24.52 C ANISOU 2957 C PRO B 282 2132 4045 3141 1065 1070 57 C ATOM 2958 O PRO B 282 108.863 44.622 -28.058 1.00 53.45 O ANISOU 2958 O PRO B 282 5834 7675 6799 1102 1133 103 O ATOM 2959 CB PRO B 282 110.707 44.230 -25.504 1.00 27.68 C ANISOU 2959 CB PRO B 282 2496 4259 3762 976 1074 -184 C ATOM 2960 CG PRO B 282 112.086 43.553 -25.674 1.00 30.17 C ANISOU 2960 CG PRO B 282 2790 4511 4162 901 1078 -275 C ATOM 2961 CD PRO B 282 112.067 43.052 -27.087 1.00 23.47 C ANISOU 2961 CD PRO B 282 1987 3677 3252 884 1117 -199 C ATOM 2962 N LEU B 283 107.484 44.121 -26.357 1.00 24.81 N ANISOU 2962 N LEU B 283 2136 4194 3095 1112 1020 118 N ATOM 2963 CA LEU B 283 106.407 44.968 -26.820 1.00 25.83 C ANISOU 2963 CA LEU B 283 2261 4407 3148 1223 1033 228 C ATOM 2964 C LEU B 283 106.689 46.414 -26.441 1.00 26.58 C ANISOU 2964 C LEU B 283 2384 4381 3334 1297 1097 180 C ATOM 2965 O LEU B 283 107.028 46.696 -25.296 1.00 28.75 O ANISOU 2965 O LEU B 283 2648 4595 3682 1278 1092 72 O ATOM 2966 CB LEU B 283 105.078 44.541 -26.197 1.00 37.42 C ANISOU 2966 CB LEU B 283 3664 6043 4509 1250 963 299 C ATOM 2967 CG LEU B 283 104.475 43.146 -26.294 1.00 33.88 C ANISOU 2967 CG LEU B 283 3158 5749 3967 1182 896 347 C ATOM 2968 CD1 LEU B 283 103.410 43.075 -25.231 1.00 26.30 C ANISOU 2968 CD1 LEU B 283 2138 4902 2953 1209 852 381 C ATOM 2969 CD2 LEU B 283 103.874 42.941 -27.676 1.00 26.53 C ANISOU 2969 CD2 LEU B 283 2192 4959 2929 1215 890 451 C ATOM 2970 N SER B 284 106.513 47.336 -27.372 1.00 27.57 N ANISOU 2970 N SER B 284 2544 4480 3450 1394 1165 267 N ATOM 2971 CA SER B 284 106.643 48.756 -27.045 1.00 28.64 C ANISOU 2971 CA SER B 284 2710 4497 3675 1481 1240 237 C ATOM 2972 C SER B 284 105.602 49.199 -26.031 1.00 35.87 C ANISOU 2972 C SER B 284 3589 5480 4560 1554 1215 240 C ATOM 2973 O SER B 284 104.626 48.485 -25.758 1.00 33.95 O ANISOU 2973 O SER B 284 3296 5395 4208 1554 1143 305 O ATOM 2974 CB SER B 284 106.481 49.610 -28.284 1.00 29.87 C ANISOU 2974 CB SER B 284 2921 4618 3811 1599 1333 382 C ATOM 2975 OG SER B 284 105.104 49.774 -28.560 1.00 30.82 O ANISOU 2975 OG SER B 284 3011 4895 3805 1721 1309 537 O ATOM 2976 N TRP B 285 105.776 50.408 -25.516 1.00 30.38 N ANISOU 2976 N TRP B 285 2919 4666 3959 1624 1285 172 N ATOM 2977 CA TRP B 285 104.826 50.966 -24.579 1.00 31.37 C ANISOU 2977 CA TRP B 285 3019 4839 4063 1711 1287 165 C ATOM 2978 C TRP B 285 103.485 51.210 -25.258 1.00 47.19 C ANISOU 2978 C TRP B 285 5006 6971 5953 1842 1292 362 C ATOM 2979 O TRP B 285 102.409 50.974 -24.688 1.00 48.61 O ANISOU 2979 O TRP B 285 5129 7290 6050 1882 1248 409 O ATOM 2980 CB TRP B 285 105.368 52.267 -23.999 1.00 32.61 C ANISOU 2980 CB TRP B 285 3211 4825 4353 1769 1377 36 C ATOM 2981 CG TRP B 285 104.392 52.971 -23.104 1.00 50.82 C ANISOU 2981 CG TRP B 285 5504 7163 6642 1880 1405 23 C ATOM 2982 CD1 TRP B 285 103.826 54.196 -23.300 1.00 35.90 C ANISOU 2982 CD1 TRP B 285 3651 5202 4787 2032 1498 83 C ATOM 2983 CD2 TRP B 285 103.849 52.470 -21.873 1.00 46.90 C ANISOU 2983 CD2 TRP B 285 4960 6774 6085 1858 1355 -38 C ATOM 2984 NE1 TRP B 285 102.967 54.494 -22.266 1.00 36.91 N ANISOU 2984 NE1 TRP B 285 3750 5390 4885 2104 1506 43 N ATOM 2985 CE2 TRP B 285 102.959 53.456 -21.384 1.00 50.10 C ANISOU 2985 CE2 TRP B 285 5370 7175 6490 2000 1423 -26 C ATOM 2986 CE3 TRP B 285 104.041 51.291 -21.143 1.00 32.48 C ANISOU 2986 CE3 TRP B 285 3098 5041 4201 1746 1274 -84 C ATOM 2987 CZ2 TRP B 285 102.267 53.296 -20.183 1.00 36.20 C ANISOU 2987 CZ2 TRP B 285 3575 5510 4668 2027 1414 -71 C ATOM 2988 CZ3 TRP B 285 103.346 51.134 -19.960 1.00 33.01 C ANISOU 2988 CZ3 TRP B 285 3139 5205 4199 1779 1264 -107 C ATOM 2989 CH2 TRP B 285 102.470 52.133 -19.489 1.00 52.71 C ANISOU 2989 CH2 TRP B 285 5636 7703 6690 1916 1335 -105 C ATOM 2990 N HIS B 286 103.551 51.711 -26.481 1.00 46.50 N ANISOU 2990 N HIS B 286 4962 6847 5859 1921 1353 489 N ATOM 2991 CA HIS B 286 102.343 52.093 -27.190 1.00 34.64 C ANISOU 2991 CA HIS B 286 3437 5475 4250 2077 1367 690 C ATOM 2992 C HIS B 286 101.494 50.857 -27.435 1.00 50.25 C ANISOU 2992 C HIS B 286 5321 7699 6072 2034 1251 774 C ATOM 2993 O HIS B 286 100.251 50.916 -27.366 1.00 45.31 O ANISOU 2993 O HIS B 286 4621 7242 5354 2128 1221 884 O ATOM 2994 CB HIS B 286 102.675 52.796 -28.506 1.00 35.69 C ANISOU 2994 CB HIS B 286 3643 5528 4390 2181 1467 832 C ATOM 2995 CG HIS B 286 101.469 53.129 -29.325 1.00 65.96 C ANISOU 2995 CG HIS B 286 7441 9529 8092 2360 1477 1062 C ATOM 2996 ND1 HIS B 286 101.230 52.567 -30.562 1.00 67.60 N ANISOU 2996 ND1 HIS B 286 7624 9905 8156 2402 1447 1220 N ATOM 2997 CD2 HIS B 286 100.425 53.958 -29.076 1.00 68.81 C ANISOU 2997 CD2 HIS B 286 7774 9937 8434 2519 1512 1159 C ATOM 2998 CE1 HIS B 286 100.094 53.042 -31.044 1.00 69.25 C ANISOU 2998 CE1 HIS B 286 7780 10276 8255 2580 1454 1410 C ATOM 2999 NE2 HIS B 286 99.584 53.886 -30.163 1.00 67.11 N ANISOU 2999 NE2 HIS B 286 7508 9925 8065 2652 1497 1380 N ATOM 3000 N MET B 287 102.165 49.737 -27.708 1.00 32.44 N ANISOU 3000 N MET B 287 3062 5466 3798 1892 1192 717 N ATOM 3001 CA MET B 287 101.458 48.494 -27.945 1.00 32.11 C ANISOU 3001 CA MET B 287 2932 5644 3624 1834 1088 775 C ATOM 3002 C MET B 287 100.852 48.011 -26.629 1.00 46.78 C ANISOU 3002 C MET B 287 4729 7567 5478 1777 1030 707 C ATOM 3003 O MET B 287 99.695 47.585 -26.594 1.00 44.70 O ANISOU 3003 O MET B 287 4369 7504 5113 1804 974 798 O ATOM 3004 CB MET B 287 102.392 47.451 -28.547 1.00 38.43 C ANISOU 3004 CB MET B 287 3756 6424 4423 1702 1061 720 C ATOM 3005 CG MET B 287 101.707 46.242 -29.161 1.00 30.59 C ANISOU 3005 CG MET B 287 2670 5665 3288 1656 973 790 C ATOM 3006 SD MET B 287 100.774 46.610 -30.659 1.00 45.48 S ANISOU 3006 SD MET B 287 4490 7788 5002 1819 971 998 S ATOM 3007 CE MET B 287 99.142 46.634 -29.984 1.00 33.78 C ANISOU 3007 CE MET B 287 2867 6527 3442 1875 898 1080 C ATOM 3008 N ARG B 288 101.609 48.109 -25.540 1.00 30.85 N ANISOU 3008 N ARG B 288 2758 5398 3564 1707 1049 555 N ATOM 3009 CA ARG B 288 101.101 47.634 -24.270 1.00 30.71 C ANISOU 3009 CA ARG B 288 2694 5448 3525 1668 1009 505 C ATOM 3010 C ARG B 288 99.809 48.364 -23.907 1.00 40.91 C ANISOU 3010 C ARG B 288 3932 6842 4768 1803 1034 591 C ATOM 3011 O ARG B 288 98.864 47.748 -23.378 1.00 36.88 O ANISOU 3011 O ARG B 288 3340 6489 4181 1794 991 638 O ATOM 3012 CB ARG B 288 102.144 47.795 -23.168 1.00 29.99 C ANISOU 3012 CB ARG B 288 2658 5200 3538 1606 1034 337 C ATOM 3013 CG ARG B 288 103.347 46.925 -23.370 1.00 28.48 C ANISOU 3013 CG ARG B 288 2497 4931 3394 1474 1005 260 C ATOM 3014 CD ARG B 288 104.415 47.165 -22.357 1.00 28.11 C ANISOU 3014 CD ARG B 288 2481 4752 3446 1429 1029 103 C ATOM 3015 NE ARG B 288 105.689 46.626 -22.832 1.00 37.02 N ANISOU 3015 NE ARG B 288 3634 5782 4649 1328 1024 38 N ATOM 3016 CZ ARG B 288 106.634 46.082 -22.066 1.00 34.65 C ANISOU 3016 CZ ARG B 288 3333 5432 4402 1254 1005 -62 C ATOM 3017 NH1 ARG B 288 106.445 45.981 -20.750 1.00 36.48 N1+ ANISOU 3017 NH1 ARG B 288 3549 5715 4597 1275 986 -102 N1+ ATOM 3018 NH2 ARG B 288 107.759 45.643 -22.624 1.00 25.57 N ANISOU 3018 NH2 ARG B 288 2193 4193 3329 1176 1010 -112 N ATOM 3019 N CYS B 289 99.753 49.663 -24.218 1.00 40.16 N ANISOU 3019 N CYS B 289 3877 6658 4725 1934 1114 619 N ATOM 3020 CA CYS B 289 98.550 50.448 -23.936 1.00 43.59 C ANISOU 3020 CA CYS B 289 4262 7176 5126 2084 1155 706 C ATOM 3021 C CYS B 289 97.351 49.924 -24.725 1.00 38.68 C ANISOU 3021 C CYS B 289 3528 6795 4373 2130 1096 884 C ATOM 3022 O CYS B 289 96.262 49.777 -24.161 1.00 39.44 O ANISOU 3022 O CYS B 289 3533 7036 4416 2170 1082 934 O ATOM 3023 CB CYS B 289 98.769 51.929 -24.235 1.00 36.96 C ANISOU 3023 CB CYS B 289 3494 6175 4375 2225 1265 715 C ATOM 3024 SG CYS B 289 99.825 52.809 -23.048 1.00 38.90 S ANISOU 3024 SG CYS B 289 3829 6173 4779 2203 1349 486 S ATOM 3025 N LYS B 290 97.549 49.625 -26.011 1.00 36.20 N ANISOU 3025 N LYS B 290 3210 6541 4003 2125 1065 975 N ATOM 3026 CA LYS B 290 96.471 49.065 -26.820 1.00 37.21 C ANISOU 3026 CA LYS B 290 3210 6935 3994 2157 997 1128 C ATOM 3027 C LYS B 290 95.935 47.773 -26.215 1.00 41.98 C ANISOU 3027 C LYS B 290 3711 7692 4546 2019 911 1094 C ATOM 3028 O LYS B 290 94.728 47.574 -26.108 1.00 42.34 O ANISOU 3028 O LYS B 290 3627 7936 4523 2054 881 1183 O ATOM 3029 CB LYS B 290 96.933 48.801 -28.251 1.00 37.02 C ANISOU 3029 CB LYS B 290 3199 6967 3901 2157 974 1205 C ATOM 3030 CG LYS B 290 97.355 50.046 -28.998 1.00 44.30 C ANISOU 3030 CG LYS B 290 4217 7759 4858 2313 1074 1285 C ATOM 3031 CD LYS B 290 96.348 51.155 -28.815 1.00 49.11 C ANISOU 3031 CD LYS B 290 4790 8405 5464 2498 1134 1399 C ATOM 3032 CE LYS B 290 95.458 51.360 -30.030 1.00 58.62 C ANISOU 3032 CE LYS B 290 5902 9847 6523 2647 1117 1615 C ATOM 3033 NZ LYS B 290 94.412 52.399 -29.733 1.00 64.32 N1+ ANISOU 3033 NZ LYS B 290 6577 10605 7258 2829 1179 1723 N1+ ATOM 3034 N ILE B 291 96.847 46.898 -25.820 1.00 42.70 N ANISOU 3034 N ILE B 291 3857 7686 4680 1864 881 970 N ATOM 3035 CA ILE B 291 96.479 45.627 -25.237 1.00 34.23 C ANISOU 3035 CA ILE B 291 2706 6726 3573 1731 818 942 C ATOM 3036 C ILE B 291 95.675 45.830 -23.955 1.00 42.31 C ANISOU 3036 C ILE B 291 3684 7783 4608 1771 847 938 C ATOM 3037 O ILE B 291 94.608 45.212 -23.783 1.00 42.20 O ANISOU 3037 O ILE B 291 3540 7959 4536 1746 814 1010 O ATOM 3038 CB ILE B 291 97.727 44.795 -24.963 1.00 40.90 C ANISOU 3038 CB ILE B 291 3637 7425 4477 1587 802 816 C ATOM 3039 CG1 ILE B 291 98.405 44.444 -26.298 1.00 31.64 C ANISOU 3039 CG1 ILE B 291 2489 6252 3282 1547 781 827 C ATOM 3040 CG2 ILE B 291 97.373 43.560 -24.138 1.00 31.92 C ANISOU 3040 CG2 ILE B 291 2433 6372 3321 1468 761 794 C ATOM 3041 CD1 ILE B 291 99.792 43.873 -26.173 1.00 29.89 C ANISOU 3041 CD1 ILE B 291 2365 5850 3142 1433 791 703 C ATOM 3042 N ALA B 292 96.172 46.699 -23.067 1.00 40.31 N ANISOU 3042 N ALA B 292 3527 7359 4432 1831 916 850 N ATOM 3043 CA ALA B 292 95.459 47.024 -21.836 1.00 36.06 C ANISOU 3043 CA ALA B 292 2953 6853 3893 1894 963 839 C ATOM 3044 C ALA B 292 94.029 47.448 -22.159 1.00 57.05 C ANISOU 3044 C ALA B 292 5486 9692 6497 2014 977 980 C ATOM 3045 O ALA B 292 93.086 46.972 -21.537 1.00 39.21 O ANISOU 3045 O ALA B 292 3121 7578 4199 2006 974 1026 O ATOM 3046 CB ALA B 292 96.170 48.114 -21.065 1.00 36.08 C ANISOU 3046 CB ALA B 292 3068 6662 3980 1965 1043 721 C ATOM 3047 N GLN B 293 93.881 48.329 -23.144 1.00 39.15 N ANISOU 3047 N GLN B 293 3224 7422 4229 2131 998 1060 N ATOM 3048 CA GLN B 293 92.576 48.776 -23.560 1.00 41.44 C ANISOU 3048 CA GLN B 293 3387 7892 4466 2261 1009 1209 C ATOM 3049 C GLN B 293 91.726 47.613 -24.068 1.00 45.70 C ANISOU 3049 C GLN B 293 3762 8687 4916 2164 917 1299 C ATOM 3050 O GLN B 293 90.573 47.434 -23.649 1.00 46.68 O ANISOU 3050 O GLN B 293 3745 8976 5016 2191 920 1368 O ATOM 3051 CB GLN B 293 92.707 49.848 -24.637 1.00 43.17 C ANISOU 3051 CB GLN B 293 3651 8064 4689 2406 1047 1296 C ATOM 3052 CG GLN B 293 92.894 51.266 -24.112 1.00 48.30 C ANISOU 3052 CG GLN B 293 4399 8520 5433 2561 1167 1258 C ATOM 3053 CD GLN B 293 93.620 52.176 -25.103 1.00 56.90 C ANISOU 3053 CD GLN B 293 5595 9462 6561 2652 1218 1299 C ATOM 3054 OE1 GLN B 293 94.210 53.184 -24.709 1.00 57.89 O ANISOU 3054 OE1 GLN B 293 5834 9367 6794 2721 1314 1221 O ATOM 3055 NE2 GLN B 293 93.584 51.821 -26.394 1.00 57.54 N ANISOU 3055 NE2 GLN B 293 5637 9670 6553 2653 1161 1422 N ATOM 3056 N GLY B 294 92.293 46.820 -24.962 1.00 40.70 N ANISOU 3056 N GLY B 294 3135 8087 4242 2048 841 1291 N ATOM 3057 CA GLY B 294 91.586 45.687 -25.514 1.00 41.30 C ANISOU 3057 CA GLY B 294 3051 8399 4241 1934 751 1352 C ATOM 3058 C GLY B 294 91.097 44.735 -24.446 1.00 48.94 C ANISOU 3058 C GLY B 294 3941 9422 5233 1815 744 1314 C ATOM 3059 O GLY B 294 89.942 44.315 -24.470 1.00 53.34 O ANISOU 3059 O GLY B 294 4322 10187 5759 1792 716 1396 O ATOM 3060 N ALA B 295 91.965 44.391 -23.496 1.00 41.28 N ANISOU 3060 N ALA B 295 3091 8272 4320 1742 774 1198 N ATOM 3061 CA ALA B 295 91.544 43.536 -22.391 1.00 39.71 C ANISOU 3061 CA ALA B 295 2832 8119 4137 1652 786 1179 C ATOM 3062 C ALA B 295 90.399 44.166 -21.549 1.00 47.40 C ANISOU 3062 C ALA B 295 3715 9183 5113 1776 855 1245 C ATOM 3063 O ALA B 295 89.459 43.475 -21.171 1.00 43.11 O ANISOU 3063 O ALA B 295 3024 8796 4561 1719 854 1304 O ATOM 3064 CB ALA B 295 92.724 43.210 -21.516 1.00 37.74 C ANISOU 3064 CB ALA B 295 2734 7673 3934 1587 810 1057 C ATOM 3065 N ALA B 296 90.482 45.463 -21.254 1.00 42.29 N ANISOU 3065 N ALA B 296 3147 8433 4488 1940 926 1232 N ATOM 3066 CA ALA B 296 89.449 46.122 -20.464 1.00 44.43 C ANISOU 3066 CA ALA B 296 3337 8778 4766 2074 1007 1285 C ATOM 3067 C ALA B 296 88.110 46.069 -21.209 1.00 46.75 C ANISOU 3067 C ALA B 296 3425 9312 5027 2115 977 1433 C ATOM 3068 O ALA B 296 87.076 45.829 -20.606 1.00 48.55 O ANISOU 3068 O ALA B 296 3510 9679 5256 2130 1012 1492 O ATOM 3069 CB ALA B 296 89.839 47.554 -20.145 1.00 44.74 C ANISOU 3069 CB ALA B 296 3502 8650 4848 2242 1093 1233 C ATOM 3070 N ASN B 297 88.148 46.260 -22.526 1.00 48.61 N ANISOU 3070 N ASN B 297 3635 9607 5228 2132 912 1493 N ATOM 3071 CA ASN B 297 86.966 46.106 -23.374 1.00 49.19 C ANISOU 3071 CA ASN B 297 3498 9936 5256 2151 857 1628 C ATOM 3072 C ASN B 297 86.357 44.717 -23.277 1.00 49.67 C ANISOU 3072 C ASN B 297 3391 10172 5311 1961 791 1641 C ATOM 3073 O ASN B 297 85.156 44.580 -23.149 1.00 52.05 O ANISOU 3073 O ASN B 297 3495 10663 5620 1976 793 1729 O ATOM 3074 CB ASN B 297 87.299 46.405 -24.849 1.00 49.12 C ANISOU 3074 CB ASN B 297 3504 9974 5187 2184 788 1681 C ATOM 3075 CG ASN B 297 87.485 47.886 -25.121 1.00 62.83 C ANISOU 3075 CG ASN B 297 5342 11595 6935 2404 864 1729 C ATOM 3076 OD1 ASN B 297 87.154 48.724 -24.281 1.00 64.18 O ANISOU 3076 OD1 ASN B 297 5538 11685 7163 2539 962 1730 O ATOM 3077 ND2 ASN B 297 88.001 48.217 -26.303 1.00 49.54 N ANISOU 3077 ND2 ASN B 297 3715 9908 5201 2447 830 1772 N ATOM 3078 N GLY B 298 87.184 43.684 -23.362 1.00 47.64 N ANISOU 3078 N GLY B 298 3203 9845 5052 1781 739 1555 N ATOM 3079 CA GLY B 298 86.682 42.326 -23.291 1.00 48.20 C ANISOU 3079 CA GLY B 298 3123 10054 5136 1585 686 1560 C ATOM 3080 C GLY B 298 86.121 42.014 -21.922 1.00 49.01 C ANISOU 3080 C GLY B 298 3172 10158 5293 1574 772 1567 C ATOM 3081 O GLY B 298 85.159 41.266 -21.793 1.00 60.57 O ANISOU 3081 O GLY B 298 4441 11790 6785 1476 760 1624 O ATOM 3082 N ILE B 299 86.725 42.586 -20.887 1.00 47.88 N ANISOU 3082 N ILE B 299 3193 9834 5164 1671 861 1506 N ATOM 3083 CA ILE B 299 86.229 42.391 -19.538 1.00 48.84 C ANISOU 3083 CA ILE B 299 3275 9968 5314 1687 955 1515 C ATOM 3084 C ILE B 299 84.896 43.121 -19.377 1.00 59.55 C ANISOU 3084 C ILE B 299 4462 11484 6679 1832 1012 1620 C ATOM 3085 O ILE B 299 83.983 42.625 -18.719 1.00 53.62 O ANISOU 3085 O ILE B 299 3556 10860 5956 1799 1064 1679 O ATOM 3086 CB ILE B 299 87.235 42.881 -18.482 1.00 53.96 C ANISOU 3086 CB ILE B 299 4137 10407 5959 1761 1027 1412 C ATOM 3087 CG1 ILE B 299 88.548 42.089 -18.590 1.00 52.73 C ANISOU 3087 CG1 ILE B 299 4127 10104 5805 1619 972 1316 C ATOM 3088 CG2 ILE B 299 86.648 42.754 -17.086 1.00 48.59 C ANISOU 3088 CG2 ILE B 299 3407 9773 5280 1802 1134 1433 C ATOM 3089 CD1 ILE B 299 89.616 42.496 -17.580 1.00 43.03 C ANISOU 3089 CD1 ILE B 299 3091 8686 4572 1674 1024 1209 C ATOM 3090 N ASN B 300 84.788 44.291 -19.998 1.00 52.39 N ANISOU 3090 N ASN B 300 3579 10570 5757 1996 1013 1652 N ATOM 3091 CA ASN B 300 83.565 45.061 -19.944 1.00 55.34 C ANISOU 3091 CA ASN B 300 3792 11089 6145 2156 1069 1759 C ATOM 3092 C ASN B 300 82.400 44.322 -20.591 1.00 57.63 C ANISOU 3092 C ASN B 300 3810 11641 6447 2061 997 1866 C ATOM 3093 O ASN B 300 81.272 44.372 -20.106 1.00 60.26 O ANISOU 3093 O ASN B 300 3958 12121 6817 2115 1056 1946 O ATOM 3094 CB ASN B 300 83.746 46.416 -20.617 1.00 55.66 C ANISOU 3094 CB ASN B 300 3914 11061 6171 2350 1081 1784 C ATOM 3095 CG ASN B 300 82.442 47.196 -20.697 1.00 66.39 C ANISOU 3095 CG ASN B 300 5090 12585 7550 2529 1134 1913 C ATOM 3096 OD1 ASN B 300 82.011 47.811 -19.719 1.00 60.40 O ANISOU 3096 OD1 ASN B 300 4328 11796 6825 2664 1255 1914 O ATOM 3097 ND2 ASN B 300 81.810 47.171 -21.863 1.00 60.59 N ANISOU 3097 ND2 ASN B 300 4194 12036 6790 2536 1043 2020 N ATOM 3098 N PHE B 301 82.677 43.638 -21.690 1.00 56.86 N ANISOU 3098 N PHE B 301 3678 11606 6320 1915 870 1860 N ATOM 3099 CA PHE B 301 81.651 42.883 -22.373 1.00 59.16 C ANISOU 3099 CA PHE B 301 3705 12147 6625 1793 781 1937 C ATOM 3100 C PHE B 301 81.173 41.744 -21.485 1.00 69.56 C ANISOU 3100 C PHE B 301 4901 13516 8013 1625 820 1930 C ATOM 3101 O PHE B 301 79.989 41.419 -21.459 1.00 76.69 O ANISOU 3101 O PHE B 301 5551 14618 8968 1585 817 2010 O ATOM 3102 CB PHE B 301 82.166 42.341 -23.708 1.00 58.17 C ANISOU 3102 CB PHE B 301 3586 12072 6445 1657 636 1907 C ATOM 3103 CG PHE B 301 81.140 41.553 -24.477 1.00 72.12 C ANISOU 3103 CG PHE B 301 5074 14105 8224 1509 521 1963 C ATOM 3104 CD1 PHE B 301 80.922 40.208 -24.200 1.00 73.77 C ANISOU 3104 CD1 PHE B 301 5169 14361 8498 1265 491 1921 C ATOM 3105 CD2 PHE B 301 80.382 42.154 -25.462 1.00 63.24 C ANISOU 3105 CD2 PHE B 301 3791 13183 7053 1609 440 2058 C ATOM 3106 CE1 PHE B 301 79.968 39.481 -24.900 1.00 74.47 C ANISOU 3106 CE1 PHE B 301 4990 14689 8617 1106 377 1955 C ATOM 3107 CE2 PHE B 301 79.441 41.432 -26.169 1.00 65.94 C ANISOU 3107 CE2 PHE B 301 3865 13781 7409 1462 313 2095 C ATOM 3108 CZ PHE B 301 79.234 40.097 -25.888 1.00 66.28 C ANISOU 3108 CZ PHE B 301 3794 13862 7528 1201 278 2036 C ATOM 3109 N LEU B 302 82.090 41.132 -20.753 1.00 64.66 N ANISOU 3109 N LEU B 302 4450 12719 7401 1528 863 1839 N ATOM 3110 CA LEU B 302 81.716 40.023 -19.891 1.00 58.28 C ANISOU 3110 CA LEU B 302 3542 11943 6658 1372 917 1844 C ATOM 3111 C LEU B 302 80.779 40.462 -18.751 1.00 71.25 C ANISOU 3111 C LEU B 302 5082 13655 8337 1502 1056 1916 C ATOM 3112 O LEU B 302 79.737 39.838 -18.505 1.00 63.12 O ANISOU 3112 O LEU B 302 3820 12786 7376 1413 1085 1987 O ATOM 3113 CB LEU B 302 82.970 39.355 -19.328 1.00 55.38 C ANISOU 3113 CB LEU B 302 3393 11367 6282 1272 939 1745 C ATOM 3114 CG LEU B 302 83.784 38.581 -20.364 1.00 58.74 C ANISOU 3114 CG LEU B 302 3876 11744 6697 1099 820 1677 C ATOM 3115 CD1 LEU B 302 84.966 37.886 -19.729 1.00 51.10 C ANISOU 3115 CD1 LEU B 302 3102 10578 5737 1011 855 1592 C ATOM 3116 CD2 LEU B 302 82.882 37.569 -21.042 1.00 64.81 C ANISOU 3116 CD2 LEU B 302 4394 12707 7524 897 744 1718 C ATOM 3117 N HIS B 303 81.162 41.536 -18.066 1.00 68.96 N ANISOU 3117 N HIS B 303 4958 13240 8005 1705 1146 1890 N ATOM 3118 CA HIS B 303 80.407 42.065 -16.935 1.00 61.93 C ANISOU 3118 CA HIS B 303 4002 12396 7131 1852 1293 1939 C ATOM 3119 C HIS B 303 79.029 42.626 -17.329 1.00 78.66 C ANISOU 3119 C HIS B 303 5867 14727 9293 1963 1306 2057 C ATOM 3120 O HIS B 303 78.083 42.624 -16.523 1.00 67.94 O ANISOU 3120 O HIS B 303 4355 13481 7980 2017 1421 2124 O ATOM 3121 CB HIS B 303 81.222 43.149 -16.237 1.00 60.45 C ANISOU 3121 CB HIS B 303 4060 12018 6890 2037 1372 1859 C ATOM 3122 CG HIS B 303 82.406 42.623 -15.499 1.00 57.85 C ANISOU 3122 CG HIS B 303 3943 11512 6524 1953 1386 1755 C ATOM 3123 ND1 HIS B 303 83.129 43.390 -14.617 1.00 56.86 N ANISOU 3123 ND1 HIS B 303 4018 11233 6355 2083 1464 1668 N ATOM 3124 CD2 HIS B 303 82.990 41.403 -15.512 1.00 56.28 C ANISOU 3124 CD2 HIS B 303 3778 11274 6332 1753 1333 1724 C ATOM 3125 CE1 HIS B 303 84.121 42.664 -14.125 1.00 54.77 C ANISOU 3125 CE1 HIS B 303 3895 10855 6062 1972 1447 1593 C ATOM 3126 NE2 HIS B 303 84.052 41.454 -14.647 1.00 54.38 N ANISOU 3126 NE2 HIS B 303 3751 10866 6043 1778 1374 1632 N ATOM 3127 N GLU B 304 78.928 43.119 -18.559 1.00 65.62 N ANISOU 3127 N GLU B 304 4171 13138 7624 2008 1196 2088 N ATOM 3128 CA GLU B 304 77.660 43.620 -19.059 1.00 69.04 C ANISOU 3128 CA GLU B 304 4350 13788 8094 2115 1186 2208 C ATOM 3129 C GLU B 304 76.706 42.473 -19.345 1.00 71.32 C ANISOU 3129 C GLU B 304 4347 14295 8456 1912 1123 2267 C ATOM 3130 O GLU B 304 75.505 42.592 -19.133 1.00 82.22 O ANISOU 3130 O GLU B 304 5478 15859 9903 1968 1172 2363 O ATOM 3131 CB GLU B 304 77.871 44.470 -20.305 1.00 68.83 C ANISOU 3131 CB GLU B 304 4365 13774 8015 2228 1084 2235 C ATOM 3132 CG GLU B 304 78.258 45.890 -19.969 1.00 75.30 C ANISOU 3132 CG GLU B 304 5370 14435 8807 2486 1186 2225 C ATOM 3133 CD GLU B 304 78.381 46.766 -21.195 1.00 79.97 C ANISOU 3133 CD GLU B 304 5988 15044 9355 2615 1108 2279 C ATOM 3134 OE1 GLU B 304 78.500 46.219 -22.322 1.00 78.06 O ANISOU 3134 OE1 GLU B 304 5684 14902 9072 2488 962 2294 O ATOM 3135 OE2 GLU B 304 78.355 48.006 -21.020 1.00 82.70 O1+ ANISOU 3135 OE2 GLU B 304 6415 15303 9705 2847 1200 2307 O1+ ATOM 3136 N ASN B 305 77.249 41.361 -19.818 1.00 69.70 N ANISOU 3136 N ASN B 305 4166 14064 8251 1672 1020 2204 N ATOM 3137 CA ASN B 305 76.486 40.134 -19.977 1.00 71.73 C ANISOU 3137 CA ASN B 305 4170 14486 8600 1436 970 2231 C ATOM 3138 C ASN B 305 76.473 39.308 -18.702 1.00 71.72 C ANISOU 3138 C ASN B 305 4176 14413 8662 1329 1108 2218 C ATOM 3139 O ASN B 305 76.339 38.087 -18.750 1.00 72.23 O ANISOU 3139 O ASN B 305 4132 14513 8801 1086 1079 2203 O ATOM 3140 CB ASN B 305 77.057 39.306 -21.121 1.00 70.35 C ANISOU 3140 CB ASN B 305 4014 14315 8402 1220 799 2162 C ATOM 3141 CG ASN B 305 76.725 39.885 -22.469 1.00 71.59 C ANISOU 3141 CG ASN B 305 4068 14629 8503 1286 650 2201 C ATOM 3142 OD1 ASN B 305 75.899 39.338 -23.197 1.00 87.97 O ANISOU 3142 OD1 ASN B 305 5886 16916 10624 1148 534 2232 O ATOM 3143 ND2 ASN B 305 77.346 41.009 -22.805 1.00 70.00 N ANISOU 3143 ND2 ASN B 305 4061 14330 8206 1496 653 2202 N ATOM 3144 N HIS B 306 76.629 39.994 -17.572 1.00 71.33 N ANISOU 3144 N HIS B 306 4260 14262 8580 1512 1262 2223 N ATOM 3145 CA HIS B 306 76.653 39.385 -16.243 1.00 71.48 C ANISOU 3145 CA HIS B 306 4313 14219 8628 1460 1415 2222 C ATOM 3146 C HIS B 306 77.434 38.072 -16.219 1.00 76.56 C ANISOU 3146 C HIS B 306 5046 14753 9290 1212 1376 2159 C ATOM 3147 O HIS B 306 76.875 36.986 -16.069 1.00 76.80 O ANISOU 3147 O HIS B 306 4898 14864 9419 1013 1402 2197 O ATOM 3148 CB HIS B 306 75.225 39.192 -15.737 1.00 75.56 C ANISOU 3148 CB HIS B 306 4525 14939 9245 1459 1521 2331 C ATOM 3149 CG HIS B 306 74.420 40.454 -15.768 1.00 84.78 C ANISOU 3149 CG HIS B 306 5587 16220 10407 1712 1568 2401 C ATOM 3150 ND1 HIS B 306 74.503 41.411 -14.779 1.00 85.09 N ANISOU 3150 ND1 HIS B 306 5759 16181 10390 1945 1720 2399 N ATOM 3151 CD2 HIS B 306 73.553 40.938 -16.690 1.00 80.22 C ANISOU 3151 CD2 HIS B 306 4788 15823 9868 1776 1481 2472 C ATOM 3152 CE1 HIS B 306 73.704 42.420 -15.081 1.00 88.92 C ANISOU 3152 CE1 HIS B 306 6110 16783 10894 2142 1738 2469 C ATOM 3153 NE2 HIS B 306 73.118 42.157 -16.236 1.00 91.06 N ANISOU 3153 NE2 HIS B 306 6162 17215 11220 2050 1592 2522 N ATOM 3154 N HIS B 307 78.744 38.208 -16.381 1.00 76.01 N ANISOU 3154 N HIS B 307 5252 14491 9138 1227 1320 2064 N ATOM 3155 CA HIS B 307 79.671 37.093 -16.407 1.00 63.88 C ANISOU 3155 CA HIS B 307 3837 12823 7610 1026 1282 1997 C ATOM 3156 C HIS B 307 80.856 37.398 -15.510 1.00 61.17 C ANISOU 3156 C HIS B 307 3786 12275 7181 1131 1348 1928 C ATOM 3157 O HIS B 307 81.488 38.438 -15.662 1.00 65.04 O ANISOU 3157 O HIS B 307 4446 12669 7595 1296 1319 1872 O ATOM 3158 CB HIS B 307 80.152 36.848 -17.827 1.00 83.06 C ANISOU 3158 CB HIS B 307 6282 15244 10031 909 1108 1938 C ATOM 3159 CG HIS B 307 79.675 35.563 -18.421 1.00 91.26 C ANISOU 3159 CG HIS B 307 7122 16382 11172 635 1041 1946 C ATOM 3160 ND1 HIS B 307 80.208 34.340 -18.068 1.00 89.43 N ANISOU 3160 ND1 HIS B 307 6946 16038 10997 433 1077 1911 N ATOM 3161 CD2 HIS B 307 78.735 35.312 -19.363 1.00 91.37 C ANISOU 3161 CD2 HIS B 307 6880 16590 11247 523 938 1977 C ATOM 3162 CE1 HIS B 307 79.602 33.389 -18.758 1.00 95.67 C ANISOU 3162 CE1 HIS B 307 7526 16935 11891 197 1007 1913 C ATOM 3163 NE2 HIS B 307 78.706 33.951 -19.551 1.00 96.59 N ANISOU 3163 NE2 HIS B 307 7447 17245 12008 242 913 1947 N ATOM 3164 N ILE B 308 81.159 36.519 -14.567 1.00 60.98 N ANISOU 3164 N ILE B 308 3813 12186 7171 1037 1440 1935 N ATOM 3165 CA ILE B 308 82.381 36.683 -13.797 1.00 58.48 C ANISOU 3165 CA ILE B 308 3764 11688 6767 1115 1475 1865 C ATOM 3166 C ILE B 308 83.415 35.767 -14.405 1.00 66.82 C ANISOU 3166 C ILE B 308 4928 12618 7841 941 1380 1800 C ATOM 3167 O ILE B 308 83.163 34.571 -14.554 1.00 67.58 O ANISOU 3167 O ILE B 308 4913 12743 8021 737 1388 1836 O ATOM 3168 CB ILE B 308 82.215 36.346 -12.311 1.00 63.82 C ANISOU 3168 CB ILE B 308 4459 12374 7417 1152 1638 1919 C ATOM 3169 CG1 ILE B 308 81.080 37.165 -11.683 1.00 62.54 C ANISOU 3169 CG1 ILE B 308 4163 12354 7247 1317 1755 1987 C ATOM 3170 CG2 ILE B 308 83.520 36.592 -11.570 1.00 57.32 C ANISOU 3170 CG2 ILE B 308 3904 11386 6488 1243 1649 1838 C ATOM 3171 CD1 ILE B 308 80.868 36.868 -10.224 1.00 64.12 C ANISOU 3171 CD1 ILE B 308 4378 12583 7404 1363 1930 2045 C ATOM 3172 N HIS B 309 84.563 36.333 -14.773 1.00 53.38 N ANISOU 3172 N HIS B 309 3436 10771 6075 1015 1301 1703 N ATOM 3173 CA HIS B 309 85.630 35.565 -15.382 1.00 51.14 C ANISOU 3173 CA HIS B 309 3264 10360 5807 874 1218 1634 C ATOM 3174 C HIS B 309 86.313 34.652 -14.373 1.00 52.22 C ANISOU 3174 C HIS B 309 3503 10398 5940 808 1297 1641 C ATOM 3175 O HIS B 309 86.501 33.463 -14.643 1.00 50.53 O ANISOU 3175 O HIS B 309 3252 10152 5795 619 1291 1654 O ATOM 3176 CB HIS B 309 86.666 36.490 -16.012 1.00 48.62 C ANISOU 3176 CB HIS B 309 3131 9914 5427 982 1129 1533 C ATOM 3177 CG HIS B 309 87.682 35.763 -16.828 1.00 46.59 C ANISOU 3177 CG HIS B 309 2963 9546 5192 843 1043 1463 C ATOM 3178 ND1 HIS B 309 88.638 34.946 -16.266 1.00 45.27 N ANISOU 3178 ND1 HIS B 309 2916 9251 5032 770 1073 1433 N ATOM 3179 CD2 HIS B 309 87.865 35.693 -18.166 1.00 46.81 C ANISOU 3179 CD2 HIS B 309 2968 9585 5234 765 937 1425 C ATOM 3180 CE1 HIS B 309 89.375 34.415 -17.221 1.00 43.84 C ANISOU 3180 CE1 HIS B 309 2782 8992 4881 654 995 1373 C ATOM 3181 NE2 HIS B 309 88.932 34.858 -18.385 1.00 44.19 N ANISOU 3181 NE2 HIS B 309 2744 9121 4924 647 912 1362 N ATOM 3182 N ARG B 310 86.705 35.226 -13.233 1.00 50.20 N ANISOU 3182 N ARG B 310 3376 10096 5600 967 1371 1632 N ATOM 3183 CA ARG B 310 87.297 34.485 -12.117 1.00 50.05 C ANISOU 3183 CA ARG B 310 3452 10019 5547 947 1454 1660 C ATOM 3184 C ARG B 310 88.801 34.239 -12.267 1.00 47.48 C ANISOU 3184 C ARG B 310 3320 9526 5193 928 1383 1574 C ATOM 3185 O ARG B 310 89.460 33.842 -11.315 1.00 51.61 O ANISOU 3185 O ARG B 310 3946 10003 5662 957 1437 1591 O ATOM 3186 CB ARG B 310 86.596 33.130 -11.924 1.00 52.07 C ANISOU 3186 CB ARG B 310 3553 10341 5892 759 1536 1769 C ATOM 3187 CG ARG B 310 85.076 33.189 -11.828 1.00 60.23 C ANISOU 3187 CG ARG B 310 4357 11546 6981 740 1612 1860 C ATOM 3188 CD ARG B 310 84.610 33.383 -10.408 1.00 68.13 C ANISOU 3188 CD ARG B 310 5352 12620 7913 863 1767 1940 C ATOM 3189 NE ARG B 310 85.008 32.270 -9.550 1.00 75.01 N ANISOU 3189 NE ARG B 310 6279 13442 8778 774 1866 2012 N ATOM 3190 CZ ARG B 310 84.353 31.115 -9.473 1.00 75.16 C ANISOU 3190 CZ ARG B 310 6155 13499 8905 586 1956 2114 C ATOM 3191 NH1 ARG B 310 83.268 30.917 -10.211 1.00 78.70 N1+ ANISOU 3191 NH1 ARG B 310 6378 14046 9477 459 1946 2140 N1+ ATOM 3192 NH2 ARG B 310 84.786 30.156 -8.665 1.00 75.22 N ANISOU 3192 NH2 ARG B 310 6238 13445 8897 523 2058 2192 N ATOM 3193 N ASN B 311 89.346 34.458 -13.450 1.00 45.56 N ANISOU 3193 N ASN B 311 3122 9207 4983 886 1269 1490 N ATOM 3194 CA ASN B 311 90.723 34.090 -13.684 1.00 43.28 C ANISOU 3194 CA ASN B 311 2989 8765 4691 848 1212 1415 C ATOM 3195 C ASN B 311 91.488 35.052 -14.558 1.00 41.25 C ANISOU 3195 C ASN B 311 2843 8413 4418 919 1112 1300 C ATOM 3196 O ASN B 311 92.360 34.629 -15.310 1.00 47.46 O ANISOU 3196 O ASN B 311 3695 9096 5240 837 1051 1242 O ATOM 3197 CB ASN B 311 90.806 32.711 -14.314 1.00 43.39 C ANISOU 3197 CB ASN B 311 2937 8750 4799 636 1206 1445 C ATOM 3198 CG ASN B 311 91.394 31.695 -13.383 1.00 61.26 C ANISOU 3198 CG ASN B 311 5263 10952 7062 590 1287 1504 C ATOM 3199 OD1 ASN B 311 92.597 31.712 -13.101 1.00 62.86 O ANISOU 3199 OD1 ASN B 311 5617 11046 7221 650 1264 1455 O ATOM 3200 ND2 ASN B 311 90.553 30.791 -12.893 1.00 61.35 N ANISOU 3200 ND2 ASN B 311 5153 11035 7123 482 1388 1618 N ATOM 3201 N ILE B 312 91.167 36.336 -14.470 1.00 41.49 N ANISOU 3201 N ILE B 312 2892 8469 4402 1071 1109 1272 N ATOM 3202 CA ILE B 312 91.953 37.327 -15.161 1.00 39.77 C ANISOU 3202 CA ILE B 312 2795 8140 4175 1147 1039 1170 C ATOM 3203 C ILE B 312 93.388 37.201 -14.717 1.00 37.96 C ANISOU 3203 C ILE B 312 2730 7765 3927 1157 1023 1087 C ATOM 3204 O ILE B 312 93.692 37.371 -13.538 1.00 38.26 O ANISOU 3204 O ILE B 312 2831 7802 3905 1240 1073 1078 O ATOM 3205 CB ILE B 312 91.483 38.746 -14.889 1.00 40.56 C ANISOU 3205 CB ILE B 312 2908 8265 4237 1318 1069 1152 C ATOM 3206 CG1 ILE B 312 90.031 38.942 -15.352 1.00 54.69 C ANISOU 3206 CG1 ILE B 312 4517 10217 6046 1330 1085 1246 C ATOM 3207 CG2 ILE B 312 92.406 39.738 -15.573 1.00 44.58 C ANISOU 3207 CG2 ILE B 312 3551 8632 4754 1382 1014 1049 C ATOM 3208 CD1 ILE B 312 89.767 38.650 -16.803 1.00 42.47 C ANISOU 3208 CD1 ILE B 312 2880 8716 4540 1230 998 1266 C ATOM 3209 N LYS B 313 94.260 36.866 -15.666 1.00 36.31 N ANISOU 3209 N LYS B 313 2580 7451 3764 1074 956 1028 N ATOM 3210 CA LYS B 313 95.697 36.876 -15.459 1.00 34.59 C ANISOU 3210 CA LYS B 313 2509 7089 3546 1088 931 940 C ATOM 3211 C LYS B 313 96.321 36.996 -16.841 1.00 36.40 C ANISOU 3211 C LYS B 313 2778 7220 3833 1030 865 874 C ATOM 3212 O LYS B 313 95.659 36.710 -17.848 1.00 33.62 O ANISOU 3212 O LYS B 313 2332 6934 3506 956 838 911 O ATOM 3213 CB LYS B 313 96.167 35.627 -14.714 1.00 34.67 C ANISOU 3213 CB LYS B 313 2524 7097 3551 1020 965 987 C ATOM 3214 CG LYS B 313 95.812 34.323 -15.393 1.00 37.68 C ANISOU 3214 CG LYS B 313 2810 7502 4003 854 972 1052 C ATOM 3215 CD LYS B 313 96.252 33.112 -14.597 1.00 35.44 C ANISOU 3215 CD LYS B 313 2537 7205 3725 796 1030 1120 C ATOM 3216 CE LYS B 313 96.052 31.851 -15.450 1.00 59.04 C ANISOU 3216 CE LYS B 313 5444 10176 6811 608 1044 1159 C ATOM 3217 NZ LYS B 313 96.572 30.566 -14.858 1.00 57.27 N1+ ANISOU 3217 NZ LYS B 313 5238 9903 6618 534 1117 1237 N1+ ATOM 3218 N SER B 314 97.574 37.441 -16.902 1.00 31.69 N ANISOU 3218 N SER B 314 2308 6480 3251 1065 841 777 N ATOM 3219 CA SER B 314 98.188 37.759 -18.192 1.00 30.51 C ANISOU 3219 CA SER B 314 2205 6233 3154 1034 795 714 C ATOM 3220 C SER B 314 98.384 36.534 -19.113 1.00 30.13 C ANISOU 3220 C SER B 314 2113 6183 3150 894 775 730 C ATOM 3221 O SER B 314 98.393 36.697 -20.322 1.00 35.69 O ANISOU 3221 O SER B 314 2806 6884 3871 863 743 712 O ATOM 3222 CB SER B 314 99.525 38.498 -17.987 1.00 29.26 C ANISOU 3222 CB SER B 314 2178 5917 3024 1091 789 604 C ATOM 3223 OG SER B 314 100.481 37.719 -17.295 1.00 28.70 O ANISOU 3223 OG SER B 314 2150 5796 2958 1060 792 579 O ATOM 3224 N ALA B 315 98.506 35.324 -18.559 1.00 34.95 N ANISOU 3224 N ALA B 315 2696 6809 3775 813 804 770 N ATOM 3225 CA ALA B 315 98.518 34.088 -19.370 1.00 30.52 C ANISOU 3225 CA ALA B 315 2073 6255 3266 664 807 789 C ATOM 3226 C ALA B 315 97.158 33.697 -19.988 1.00 51.32 C ANISOU 3226 C ALA B 315 4553 9050 5898 569 798 857 C ATOM 3227 O ALA B 315 97.111 32.798 -20.836 1.00 32.39 O ANISOU 3227 O ALA B 315 2093 6675 3541 428 792 854 O ATOM 3228 CB ALA B 315 99.019 32.945 -18.554 1.00 30.67 C ANISOU 3228 CB ALA B 315 2104 6235 3313 610 861 828 C ATOM 3229 N ASN B 316 96.065 34.336 -19.553 1.00 33.23 N ANISOU 3229 N ASN B 316 2188 6877 3562 638 800 916 N ATOM 3230 CA ASN B 316 94.747 34.074 -20.125 1.00 34.97 C ANISOU 3230 CA ASN B 316 2238 7269 3781 556 781 982 C ATOM 3231 C ASN B 316 94.353 35.172 -21.104 1.00 36.39 C ANISOU 3231 C ASN B 316 2394 7521 3912 640 719 970 C ATOM 3232 O ASN B 316 93.249 35.163 -21.654 1.00 36.68 O ANISOU 3232 O ASN B 316 2279 7727 3931 600 687 1027 O ATOM 3233 CB ASN B 316 93.652 33.958 -19.042 1.00 36.73 C ANISOU 3233 CB ASN B 316 2359 7602 3995 574 840 1077 C ATOM 3234 CG ASN B 316 93.550 32.567 -18.428 1.00 43.37 C ANISOU 3234 CG ASN B 316 3145 8441 4894 432 907 1134 C ATOM 3235 OD1 ASN B 316 94.005 31.561 -18.996 1.00 39.43 O ANISOU 3235 OD1 ASN B 316 2640 7886 4456 282 907 1113 O ATOM 3236 ND2 ASN B 316 92.937 32.506 -17.248 1.00 53.19 N ANISOU 3236 ND2 ASN B 316 4347 9744 6120 478 982 1215 N ATOM 3237 N ILE B 317 95.241 36.139 -21.298 1.00 33.61 N ANISOU 3237 N ILE B 317 2182 7045 3542 757 707 905 N ATOM 3238 CA ILE B 317 95.027 37.167 -22.295 1.00 33.73 C ANISOU 3238 CA ILE B 317 2193 7108 3515 842 664 906 C ATOM 3239 C ILE B 317 95.837 36.827 -23.553 1.00 38.76 C ANISOU 3239 C ILE B 317 2866 7707 4154 771 625 849 C ATOM 3240 O ILE B 317 97.052 37.001 -23.575 1.00 39.78 O ANISOU 3240 O ILE B 317 3135 7662 4317 796 643 773 O ATOM 3241 CB ILE B 317 95.411 38.555 -21.759 1.00 33.12 C ANISOU 3241 CB ILE B 317 2236 6918 3431 1012 695 876 C ATOM 3242 CG1 ILE B 317 94.585 38.878 -20.506 1.00 34.30 C ANISOU 3242 CG1 ILE B 317 2342 7127 3564 1086 745 924 C ATOM 3243 CG2 ILE B 317 95.251 39.615 -22.852 1.00 33.41 C ANISOU 3243 CG2 ILE B 317 2274 6989 3433 1108 668 895 C ATOM 3244 CD1 ILE B 317 94.931 40.169 -19.790 1.00 34.05 C ANISOU 3244 CD1 ILE B 317 2418 6990 3528 1237 788 879 C ATOM 3245 N LEU B 318 95.175 36.316 -24.588 1.00 34.00 N ANISOU 3245 N LEU B 318 2127 7279 3511 675 572 881 N ATOM 3246 CA LEU B 318 95.864 35.932 -25.806 1.00 33.49 C ANISOU 3246 CA LEU B 318 2079 7220 3424 601 541 825 C ATOM 3247 C LEU B 318 96.007 37.114 -26.753 1.00 33.42 C ANISOU 3247 C LEU B 318 2110 7247 3343 741 516 840 C ATOM 3248 O LEU B 318 95.289 38.108 -26.636 1.00 42.66 O ANISOU 3248 O LEU B 318 3249 8484 4475 872 509 912 O ATOM 3249 CB LEU B 318 95.130 34.777 -26.490 1.00 35.09 C ANISOU 3249 CB LEU B 318 2107 7620 3607 403 490 834 C ATOM 3250 CG LEU B 318 95.042 33.519 -25.623 1.00 35.39 C ANISOU 3250 CG LEU B 318 2109 7599 3739 246 537 829 C ATOM 3251 CD1 LEU B 318 94.339 32.381 -26.333 1.00 37.25 C ANISOU 3251 CD1 LEU B 318 2171 8004 3979 8 487 820 C ATOM 3252 CD2 LEU B 318 96.446 33.122 -25.266 1.00 36.48 C ANISOU 3252 CD2 LEU B 318 2413 7506 3941 245 605 757 C ATOM 3253 N LEU B 319 96.928 36.992 -27.699 1.00 32.65 N ANISOU 3253 N LEU B 319 2076 7104 3225 719 517 781 N ATOM 3254 CA LEU B 319 97.196 38.040 -28.681 1.00 37.23 C ANISOU 3254 CA LEU B 319 2701 7711 3734 854 512 806 C ATOM 3255 C LEU B 319 97.084 37.482 -30.103 1.00 33.76 C ANISOU 3255 C LEU B 319 2156 7494 3177 768 460 799 C ATOM 3256 O LEU B 319 97.713 36.469 -30.430 1.00 36.11 O ANISOU 3256 O LEU B 319 2466 7767 3488 621 479 710 O ATOM 3257 CB LEU B 319 98.592 38.638 -28.450 1.00 30.86 C ANISOU 3257 CB LEU B 319 2094 6619 3014 932 585 735 C ATOM 3258 CG LEU B 319 98.815 39.245 -27.069 1.00 30.71 C ANISOU 3258 CG LEU B 319 2170 6409 3091 998 624 715 C ATOM 3259 CD1 LEU B 319 100.284 39.580 -26.822 1.00 28.41 C ANISOU 3259 CD1 LEU B 319 2042 5854 2898 1015 681 619 C ATOM 3260 CD2 LEU B 319 97.943 40.498 -26.914 1.00 31.09 C ANISOU 3260 CD2 LEU B 319 2188 6524 3099 1148 624 801 C ATOM 3261 N ASP B 320 96.309 38.120 -30.965 1.00 35.35 N ANISOU 3261 N ASP B 320 2252 7928 3253 857 399 889 N ATOM 3262 CA ASP B 320 96.244 37.604 -32.323 1.00 36.60 C ANISOU 3262 CA ASP B 320 2296 8341 3268 772 335 870 C ATOM 3263 C ASP B 320 97.369 38.184 -33.189 1.00 43.21 C ANISOU 3263 C ASP B 320 3276 9091 4049 890 416 851 C ATOM 3264 O ASP B 320 98.290 38.833 -32.699 1.00 34.15 O ANISOU 3264 O ASP B 320 2322 7641 3013 994 512 833 O ATOM 3265 CB ASP B 320 94.860 37.849 -32.957 1.00 39.17 C ANISOU 3265 CB ASP B 320 2417 9002 3462 791 203 973 C ATOM 3266 CG ASP B 320 94.575 39.312 -33.272 1.00 47.80 C ANISOU 3266 CG ASP B 320 3549 10122 4490 1053 222 1111 C ATOM 3267 OD1 ASP B 320 95.457 40.174 -33.090 1.00 38.38 O ANISOU 3267 OD1 ASP B 320 2534 8695 3352 1210 331 1123 O ATOM 3268 OD2 ASP B 320 93.433 39.595 -33.730 1.00 42.23 O1+ ANISOU 3268 OD2 ASP B 320 2697 9661 3689 1090 127 1207 O1+ ATOM 3269 N GLU B 321 97.284 37.943 -34.486 1.00 39.31 N ANISOU 3269 N GLU B 321 2780 8769 3387 836 344 833 N ATOM 3270 CA GLU B 321 98.347 38.321 -35.392 1.00 36.74 C ANISOU 3270 CA GLU B 321 2692 8276 2991 900 417 798 C ATOM 3271 C GLU B 321 98.576 39.828 -35.396 1.00 36.47 C ANISOU 3271 C GLU B 321 2694 8191 2971 1183 518 938 C ATOM 3272 O GLU B 321 99.612 40.303 -35.838 1.00 35.75 O ANISOU 3272 O GLU B 321 2795 7901 2887 1258 634 924 O ATOM 3273 CB GLU B 321 98.006 37.825 -36.783 1.00 38.83 C ANISOU 3273 CB GLU B 321 3008 8711 3035 783 280 754 C ATOM 3274 CG GLU B 321 99.165 37.411 -37.648 1.00 49.31 C ANISOU 3274 CG GLU B 321 4597 9842 4295 707 354 630 C ATOM 3275 CD GLU B 321 98.664 36.878 -38.983 1.00 55.27 C ANISOU 3275 CD GLU B 321 5394 10809 4798 583 199 570 C ATOM 3276 OE1 GLU B 321 97.627 36.157 -38.954 1.00 42.51 O ANISOU 3276 OE1 GLU B 321 3608 9407 3137 417 32 529 O ATOM 3277 OE2 GLU B 321 99.282 37.198 -40.038 1.00 41.65 O1+ ANISOU 3277 OE2 GLU B 321 3863 9045 2917 649 245 566 O1+ ATOM 3278 N ALA B 322 97.611 40.583 -34.889 1.00 38.74 N ANISOU 3278 N ALA B 322 2811 8627 3281 1334 482 1072 N ATOM 3279 CA ALA B 322 97.705 42.041 -34.930 1.00 44.46 C ANISOU 3279 CA ALA B 322 3641 9219 4031 1574 547 1200 C ATOM 3280 C ALA B 322 97.979 42.577 -33.537 1.00 47.86 C ANISOU 3280 C ALA B 322 4201 9311 4674 1585 604 1158 C ATOM 3281 O ALA B 322 97.976 43.788 -33.320 1.00 47.04 O ANISOU 3281 O ALA B 322 4179 9070 4622 1746 665 1238 O ATOM 3282 CB ALA B 322 96.432 42.647 -35.496 1.00 39.93 C ANISOU 3282 CB ALA B 322 2900 8960 3311 1720 449 1372 C ATOM 3283 N PHE B 323 98.210 41.653 -32.607 1.00 34.50 N ANISOU 3283 N PHE B 323 2518 7500 3090 1409 589 1032 N ATOM 3284 CA PHE B 323 98.371 41.945 -31.178 1.00 33.25 C ANISOU 3284 CA PHE B 323 2446 7092 3095 1396 623 978 C ATOM 3285 C PHE B 323 97.125 42.572 -30.610 1.00 34.56 C ANISOU 3285 C PHE B 323 2521 7370 3240 1485 595 1076 C ATOM 3286 O PHE B 323 97.174 43.417 -29.713 1.00 35.84 O ANISOU 3286 O PHE B 323 2765 7355 3496 1564 650 1069 O ATOM 3287 CB PHE B 323 99.586 42.830 -30.904 1.00 31.95 C ANISOU 3287 CB PHE B 323 2474 6606 3061 1463 723 924 C ATOM 3288 CG PHE B 323 100.880 42.143 -31.164 1.00 30.57 C ANISOU 3288 CG PHE B 323 2400 6267 2949 1351 768 806 C ATOM 3289 CD1 PHE B 323 101.472 41.362 -30.203 1.00 36.77 C ANISOU 3289 CD1 PHE B 323 3226 6898 3846 1219 769 687 C ATOM 3290 CD2 PHE B 323 101.493 42.247 -32.390 1.00 31.19 C ANISOU 3290 CD2 PHE B 323 2535 6354 2963 1386 821 822 C ATOM 3291 CE1 PHE B 323 102.689 40.707 -30.456 1.00 30.70 C ANISOU 3291 CE1 PHE B 323 2548 5975 3143 1124 820 585 C ATOM 3292 CE2 PHE B 323 102.684 41.591 -32.645 1.00 32.99 C ANISOU 3292 CE2 PHE B 323 2865 6418 3250 1277 881 708 C ATOM 3293 CZ PHE B 323 103.279 40.826 -31.667 1.00 28.43 C ANISOU 3293 CZ PHE B 323 2319 5681 2803 1148 878 589 C ATOM 3294 N THR B 324 95.990 42.127 -31.119 1.00 36.30 N ANISOU 3294 N THR B 324 2560 7894 3339 1458 511 1153 N ATOM 3295 CA THR B 324 94.735 42.453 -30.484 1.00 37.70 C ANISOU 3295 CA THR B 324 2630 8181 3514 1503 489 1229 C ATOM 3296 C THR B 324 94.570 41.552 -29.279 1.00 41.81 C ANISOU 3296 C THR B 324 3129 8628 4128 1351 484 1146 C ATOM 3297 O THR B 324 94.826 40.348 -29.353 1.00 39.33 O ANISOU 3297 O THR B 324 2776 8348 3821 1178 447 1073 O ATOM 3298 CB THR B 324 93.592 42.291 -31.448 1.00 40.13 C ANISOU 3298 CB THR B 324 2739 8832 3676 1510 396 1335 C ATOM 3299 OG1 THR B 324 93.633 43.385 -32.363 1.00 41.18 O ANISOU 3299 OG1 THR B 324 2906 9017 3723 1708 422 1448 O ATOM 3300 CG2 THR B 324 92.264 42.276 -30.723 1.00 41.69 C ANISOU 3300 CG2 THR B 324 2797 9146 3899 1499 372 1390 C ATOM 3301 N ALA B 325 94.194 42.143 -28.151 1.00 47.64 N ANISOU 3301 N ALA B 325 3766 8917 5419 1291 990 -1382 N ATOM 3302 CA ALA B 325 94.020 41.381 -26.920 1.00 46.92 C ANISOU 3302 CA ALA B 325 3438 8929 5462 1201 957 -1241 C ATOM 3303 C ALA B 325 92.754 40.513 -26.991 1.00 47.80 C ANISOU 3303 C ALA B 325 3174 9318 5671 1151 826 -1119 C ATOM 3304 O ALA B 325 91.670 41.019 -27.245 1.00 47.01 O ANISOU 3304 O ALA B 325 3035 9390 5436 1242 841 -1001 O ATOM 3305 CB ALA B 325 93.972 42.322 -25.734 1.00 43.26 C ANISOU 3305 CB ALA B 325 3147 8404 4887 1248 1098 -1040 C ATOM 3306 N LYS B 326 92.913 39.202 -26.807 1.00 49.31 N ANISOU 3306 N LYS B 326 3105 9507 6124 982 675 -1146 N ATOM 3307 CA LYS B 326 91.769 38.288 -26.758 1.00 48.73 C ANISOU 3307 CA LYS B 326 2705 9598 6214 862 527 -990 C ATOM 3308 C LYS B 326 91.673 37.620 -25.402 1.00 49.34 C ANISOU 3308 C LYS B 326 2641 9665 6440 734 526 -769 C ATOM 3309 O LYS B 326 92.485 36.761 -25.074 1.00 49.01 O ANISOU 3309 O LYS B 326 2550 9478 6593 603 442 -835 O ATOM 3310 CB LYS B 326 91.876 37.204 -27.828 1.00 51.29 C ANISOU 3310 CB LYS B 326 2867 9858 6764 719 303 -1183 C ATOM 3311 CG LYS B 326 92.046 37.716 -29.227 1.00 53.48 C ANISOU 3311 CG LYS B 326 3270 10141 6911 846 287 -1430 C ATOM 3312 CD LYS B 326 90.782 38.361 -29.726 1.00 50.39 C ANISOU 3312 CD LYS B 326 2831 9984 6331 993 307 -1334 C ATOM 3313 CE LYS B 326 90.855 38.573 -31.227 1.00 50.49 C ANISOU 3313 CE LYS B 326 2916 10015 6254 1107 237 -1588 C ATOM 3314 NZ LYS B 326 89.573 39.066 -31.791 1.00 52.15 N1+ ANISOU 3314 NZ LYS B 326 3052 10469 6295 1257 213 -1516 N1+ ATOM 3315 N ILE B 327 90.674 37.995 -24.613 1.00 50.58 N ANISOU 3315 N ILE B 327 2743 9968 6508 774 614 -514 N ATOM 3316 CA ILE B 327 90.500 37.355 -23.318 1.00 51.80 C ANISOU 3316 CA ILE B 327 2768 10122 6791 661 628 -292 C ATOM 3317 C ILE B 327 90.008 35.935 -23.526 1.00 53.11 C ANISOU 3317 C ILE B 327 2648 10272 7258 438 441 -250 C ATOM 3318 O ILE B 327 89.163 35.697 -24.384 1.00 54.44 O ANISOU 3318 O ILE B 327 2685 10513 7487 396 340 -285 O ATOM 3319 CB ILE B 327 89.535 38.127 -22.434 1.00 51.87 C ANISOU 3319 CB ILE B 327 2809 10271 6628 752 772 -52 C ATOM 3320 CG1 ILE B 327 90.214 39.405 -21.953 1.00 49.92 C ANISOU 3320 CG1 ILE B 327 2882 9953 6131 924 939 -81 C ATOM 3321 CG2 ILE B 327 89.106 37.274 -21.260 1.00 53.37 C ANISOU 3321 CG2 ILE B 327 2818 10484 6976 615 771 184 C ATOM 3322 CD1 ILE B 327 89.328 40.314 -21.169 1.00 50.38 C ANISOU 3322 CD1 ILE B 327 3021 10116 6004 1016 1056 117 C ATOM 3323 N SER B 328 90.562 34.986 -22.777 1.00 53.35 N ANISOU 3323 N SER B 328 2597 10192 7482 293 388 -188 N ATOM 3324 CA SER B 328 90.100 33.611 -22.897 1.00 55.33 C ANISOU 3324 CA SER B 328 2607 10381 8035 56 221 -132 C ATOM 3325 C SER B 328 89.911 32.889 -21.558 1.00 70.14 C ANISOU 3325 C SER B 328 4362 12253 10034 -61 269 133 C ATOM 3326 O SER B 328 90.057 33.480 -20.480 1.00 56.07 O ANISOU 3326 O SER B 328 2678 10539 8088 57 431 291 O ATOM 3327 CB SER B 328 91.056 32.803 -23.755 1.00 54.68 C ANISOU 3327 CB SER B 328 2543 10092 8143 -66 32 -390 C ATOM 3328 OG SER B 328 92.086 32.282 -22.944 1.00 68.52 O ANISOU 3328 OG SER B 328 4432 11620 9983 -124 19 -376 O ATOM 3329 N ASP B 329 89.577 31.601 -21.677 1.00 58.49 N ANISOU 3329 N ASP B 329 2702 10671 8849 -292 130 176 N ATOM 3330 CA ASP B 329 89.258 30.692 -20.576 1.00 62.22 C ANISOU 3330 CA ASP B 329 3090 11062 9487 -442 163 431 C ATOM 3331 C ASP B 329 88.287 31.245 -19.542 1.00 61.42 C ANISOU 3331 C ASP B 329 2899 11190 9245 -369 365 719 C ATOM 3332 O ASP B 329 88.624 31.369 -18.369 1.00 61.21 O ANISOU 3332 O ASP B 329 2993 11136 9129 -307 484 897 O ATOM 3333 CB ASP B 329 90.533 30.239 -19.864 1.00 59.31 C ANISOU 3333 CB ASP B 329 2952 10429 9156 -447 134 420 C ATOM 3334 CG ASP B 329 90.283 29.057 -18.952 1.00 61.49 C ANISOU 3334 CG ASP B 329 3161 10558 9643 -623 129 650 C ATOM 3335 OD1 ASP B 329 89.138 28.546 -18.954 1.00 79.20 O ANISOU 3335 OD1 ASP B 329 5169 12888 12033 -769 152 798 O ATOM 3336 OD2 ASP B 329 91.215 28.629 -18.245 1.00 61.08 O ANISOU 3336 OD2 ASP B 329 3292 10301 9614 -612 108 675 O ATOM 3337 N PHE B 330 87.071 31.543 -19.966 1.00 62.73 N ANISOU 3337 N PHE B 330 2970 11476 9389 -363 390 724 N ATOM 3338 CA PHE B 330 86.070 32.018 -19.022 1.00 70.90 C ANISOU 3338 CA PHE B 330 3976 12662 10301 -307 568 958 C ATOM 3339 C PHE B 330 84.853 31.095 -19.002 1.00 75.11 C ANISOU 3339 C PHE B 330 4260 13203 11076 -512 550 1055 C ATOM 3340 O PHE B 330 84.961 29.899 -19.280 1.00 75.91 O ANISOU 3340 O PHE B 330 4229 13152 11460 -724 434 1022 O ATOM 3341 CB PHE B 330 85.650 33.447 -19.359 1.00 62.83 C ANISOU 3341 CB PHE B 330 3089 11801 8984 -79 650 887 C ATOM 3342 CG PHE B 330 85.028 33.585 -20.713 1.00 63.33 C ANISOU 3342 CG PHE B 330 3067 11915 9080 -71 530 689 C ATOM 3343 CD1 PHE B 330 83.677 33.382 -20.891 1.00 81.73 C ANISOU 3343 CD1 PHE B 330 5201 14352 11501 -138 523 735 C ATOM 3344 CD2 PHE B 330 85.796 33.918 -21.809 1.00 72.31 C ANISOU 3344 CD2 PHE B 330 4321 12998 10156 14 427 450 C ATOM 3345 CE1 PHE B 330 83.109 33.515 -22.137 1.00 83.64 C ANISOU 3345 CE1 PHE B 330 5360 14652 11765 -107 401 550 C ATOM 3346 CE2 PHE B 330 85.229 34.050 -23.057 1.00 69.75 C ANISOU 3346 CE2 PHE B 330 3930 12732 9841 43 314 283 C ATOM 3347 CZ PHE B 330 83.892 33.851 -23.220 1.00 64.52 C ANISOU 3347 CZ PHE B 330 3069 12183 9262 -10 295 335 C ATOM 3348 N VAL B 343 84.476 28.031 5.620 1.00 93.73 N ANISOU 3348 N VAL B 343 9196 14984 11431 807 3627 6216 N ATOM 3349 CA VAL B 343 85.146 28.883 6.598 1.00102.14 C ANISOU 3349 CA VAL B 343 10501 16162 12145 1162 3580 6174 C ATOM 3350 C VAL B 343 85.001 28.349 8.036 1.00107.32 C ANISOU 3350 C VAL B 343 11453 16660 12664 1290 3731 6436 C ATOM 3351 O VAL B 343 84.385 28.981 8.902 1.00108.74 O ANISOU 3351 O VAL B 343 11675 16934 12708 1389 3803 6434 O ATOM 3352 CB VAL B 343 84.624 30.343 6.552 1.00 90.45 C ANISOU 3352 CB VAL B 343 8880 14944 10544 1251 3511 5921 C ATOM 3353 CG1 VAL B 343 85.501 31.244 7.419 1.00 88.87 C ANISOU 3353 CG1 VAL B 343 8895 14848 10023 1607 3430 5823 C ATOM 3354 CG2 VAL B 343 84.552 30.865 5.107 1.00 87.64 C ANISOU 3354 CG2 VAL B 343 8247 14720 10333 1110 3369 5649 C ATOM 3355 N MET B 344 85.540 27.156 8.263 1.00108.31 N ANISOU 3355 N MET B 344 11790 16521 12840 1279 3774 6659 N ATOM 3356 CA MET B 344 86.044 26.765 9.575 1.00109.25 C ANISOU 3356 CA MET B 344 12291 16493 12728 1539 3823 6841 C ATOM 3357 C MET B 344 87.557 26.900 9.405 1.00107.65 C ANISOU 3357 C MET B 344 12268 16280 12355 1804 3580 6684 C ATOM 3358 O MET B 344 87.997 27.750 8.614 1.00105.77 O ANISOU 3358 O MET B 344 11854 16222 12113 1833 3395 6363 O ATOM 3359 CB MET B 344 85.618 25.358 9.954 1.00104.16 C ANISOU 3359 CB MET B 344 11804 15515 12255 1370 3997 7134 C ATOM 3360 CG MET B 344 86.168 24.282 9.048 1.00104.21 C ANISOU 3360 CG MET B 344 11818 15249 12527 1197 3866 7102 C ATOM 3361 SD MET B 344 85.527 22.660 9.494 1.00154.27 S ANISOU 3361 SD MET B 344 18331 21182 19102 969 4117 7454 S ATOM 3362 CE MET B 344 86.896 21.611 9.003 1.00128.27 C ANISOU 3362 CE MET B 344 15280 17530 15928 1030 3781 7250 C ATOM 3363 N THR B 345 88.370 26.090 10.081 1.00 99.44 N ANISOU 3363 N THR B 345 11577 14988 11219 1991 3502 6764 N ATOM 3364 CA THR B 345 89.812 26.155 9.790 1.00103.07 C ANISOU 3364 CA THR B 345 12178 15381 11604 2209 3168 6435 C ATOM 3365 C THR B 345 90.119 25.431 8.476 1.00101.80 C ANISOU 3365 C THR B 345 11876 15008 11794 1944 2958 6197 C ATOM 3366 O THR B 345 89.582 24.359 8.195 1.00106.51 O ANISOU 3366 O THR B 345 12456 15361 12652 1684 3041 6353 O ATOM 3367 CB THR B 345 90.697 25.561 10.908 1.00 99.33 C ANISOU 3367 CB THR B 345 12127 14719 10894 2539 3108 6551 C ATOM 3368 OG1 THR B 345 90.438 26.237 12.142 1.00100.39 O ANISOU 3368 OG1 THR B 345 12402 15055 10686 2804 3296 6764 O ATOM 3369 CG2 THR B 345 92.172 25.730 10.560 1.00 96.86 C ANISOU 3369 CG2 THR B 345 11914 14372 10515 2763 2755 6163 C ATOM 3370 N SER B 346 90.984 26.021 7.668 1.00 92.68 N ANISOU 3370 N SER B 346 10621 13943 10652 2005 2696 5812 N ATOM 3371 CA SER B 346 91.254 25.465 6.359 1.00 91.39 C ANISOU 3371 CA SER B 346 10302 13614 10810 1756 2498 5564 C ATOM 3372 C SER B 346 92.565 25.994 5.805 1.00 88.12 C ANISOU 3372 C SER B 346 9910 13239 10334 1931 2197 5146 C ATOM 3373 O SER B 346 93.162 26.912 6.364 1.00 86.67 O ANISOU 3373 O SER B 346 9813 13244 9873 2221 2158 5031 O ATOM 3374 CB SER B 346 90.104 25.792 5.409 1.00 90.60 C ANISOU 3374 CB SER B 346 9828 13661 10935 1428 2616 5557 C ATOM 3375 OG SER B 346 89.844 27.189 5.397 1.00 93.00 O ANISOU 3375 OG SER B 346 9967 14318 11050 1533 2677 5465 O ATOM 3376 N ARG B 347 93.027 25.412 4.709 1.00 87.05 N ANISOU 3376 N ARG B 347 9693 12921 10463 1752 1990 4905 N ATOM 3377 CA ARG B 347 94.127 26.035 3.992 1.00 93.83 C ANISOU 3377 CA ARG B 347 10509 13841 11300 1862 1736 4481 C ATOM 3378 C ARG B 347 93.675 26.413 2.592 1.00 94.22 C ANISOU 3378 C ARG B 347 10235 13984 11579 1584 1697 4276 C ATOM 3379 O ARG B 347 92.844 25.734 1.984 1.00 91.74 O ANISOU 3379 O ARG B 347 9764 13568 11525 1285 1760 4392 O ATOM 3380 CB ARG B 347 95.353 25.124 3.942 1.00 93.83 C ANISOU 3380 CB ARG B 347 10735 13550 11364 1966 1481 4305 C ATOM 3381 CG ARG B 347 95.180 23.826 3.179 1.00 96.21 C ANISOU 3381 CG ARG B 347 11003 13547 12006 1676 1407 4335 C ATOM 3382 CD ARG B 347 96.556 23.261 2.861 1.00 97.09 C ANISOU 3382 CD ARG B 347 11278 13435 12176 1791 1107 4038 C ATOM 3383 NE ARG B 347 97.349 24.262 2.155 1.00 97.57 N ANISOU 3383 NE ARG B 347 11216 13665 12192 1875 938 3624 N ATOM 3384 CZ ARG B 347 98.676 24.320 2.154 1.00 97.59 C ANISOU 3384 CZ ARG B 347 11357 13597 12123 2091 703 3308 C ATOM 3385 NH1 ARG B 347 99.389 23.428 2.830 1.00 97.23 N ANISOU 3385 NH1 ARG B 347 11587 13326 12032 2267 584 3355 N ATOM 3386 NH2 ARG B 347 99.287 25.283 1.471 1.00 96.56 N ANISOU 3386 NH2 ARG B 347 11094 13623 11970 2135 595 2936 N ATOM 3387 N ILE B 348 94.204 27.527 2.102 1.00 97.00 N ANISOU 3387 N ILE B 348 10491 14536 11829 1692 1606 3968 N ATOM 3388 CA ILE B 348 93.924 27.969 0.748 1.00 99.77 C ANISOU 3388 CA ILE B 348 10572 14976 12360 1478 1551 3739 C ATOM 3389 C ILE B 348 94.953 27.366 -0.209 1.00107.90 C ANISOU 3389 C ILE B 348 11632 15776 13590 1407 1279 3411 C ATOM 3390 O ILE B 348 96.091 27.080 0.183 1.00106.76 O ANISOU 3390 O ILE B 348 11702 15491 13373 1600 1120 3265 O ATOM 3391 CB ILE B 348 93.936 29.510 0.632 1.00 98.57 C ANISOU 3391 CB ILE B 348 10308 15144 12002 1622 1616 3572 C ATOM 3392 CG1 ILE B 348 93.215 30.158 1.823 1.00 96.36 C ANISOU 3392 CG1 ILE B 348 10061 15087 11465 1776 1859 3869 C ATOM 3393 CG2 ILE B 348 93.297 29.949 -0.690 1.00 99.07 C ANISOU 3393 CG2 ILE B 348 10089 15320 12234 1390 1620 3429 C ATOM 3394 CD1 ILE B 348 94.057 30.303 3.071 1.00 93.27 C ANISOU 3394 CD1 ILE B 348 9940 14693 10806 2106 1841 3896 C ATOM 3395 N VAL B 349 94.541 27.161 -1.459 1.00112.62 N ANISOU 3395 N VAL B 349 12012 16339 14438 1138 1224 3288 N ATOM 3396 CA VAL B 349 95.420 26.605 -2.489 1.00115.48 C ANISOU 3396 CA VAL B 349 12376 16492 15009 1040 976 2973 C ATOM 3397 C VAL B 349 95.408 27.477 -3.752 1.00110.25 C ANISOU 3397 C VAL B 349 11503 15984 14403 949 924 2674 C ATOM 3398 O VAL B 349 96.325 27.403 -4.578 1.00112.94 O ANISOU 3398 O VAL B 349 11860 16209 14844 936 729 2346 O ATOM 3399 CB VAL B 349 95.015 25.153 -2.861 1.00119.04 C ANISOU 3399 CB VAL B 349 12802 16665 15762 775 929 3111 C ATOM 3400 CG1 VAL B 349 96.096 24.494 -3.713 1.00117.18 C ANISOU 3400 CG1 VAL B 349 12622 16186 15713 722 659 2794 C ATOM 3401 CG2 VAL B 349 94.747 24.330 -1.605 1.00122.00 C ANISOU 3401 CG2 VAL B 349 13378 16898 16078 842 1051 3471 C ATOM 3402 N GLY B 350 94.371 28.305 -3.886 1.00107.15 N ANISOU 3402 N GLY B 350 10924 15848 13939 897 1103 2789 N ATOM 3403 CA GLY B 350 94.199 29.159 -5.050 1.00100.50 C ANISOU 3403 CA GLY B 350 9893 15166 13127 825 1082 2549 C ATOM 3404 C GLY B 350 95.387 30.064 -5.312 1.00 93.20 C ANISOU 3404 C GLY B 350 9067 14288 12058 1024 985 2197 C ATOM 3405 O GLY B 350 96.043 30.523 -4.376 1.00 93.27 O ANISOU 3405 O GLY B 350 9240 14343 11855 1267 1011 2181 O ATOM 3406 N THR B 351 95.662 30.319 -6.589 1.00 88.35 N ANISOU 3406 N THR B 351 8351 13657 11560 924 879 1904 N ATOM 3407 CA THR B 351 96.817 31.123 -6.988 1.00 84.69 C ANISOU 3407 CA THR B 351 7976 13203 10999 1080 797 1534 C ATOM 3408 C THR B 351 96.709 32.564 -6.494 1.00 77.23 C ANISOU 3408 C THR B 351 7035 12532 9775 1289 978 1525 C ATOM 3409 O THR B 351 96.158 33.443 -7.174 1.00 56.93 O ANISOU 3409 O THR B 351 4334 10141 7155 1259 1078 1469 O ATOM 3410 CB THR B 351 97.000 31.116 -8.511 1.00 81.50 C ANISOU 3410 CB THR B 351 7464 12730 10775 917 678 1247 C ATOM 3411 OG1 THR B 351 97.390 29.796 -8.928 1.00 85.41 O ANISOU 3411 OG1 THR B 351 7984 12944 11522 754 484 1192 O ATOM 3412 CG2 THR B 351 98.074 32.135 -8.924 1.00 76.74 C ANISOU 3412 CG2 THR B 351 6943 12162 10052 1077 656 873 C ATOM 3413 N THR B 352 97.264 32.777 -5.303 1.00 74.48 N ANISOU 3413 N THR B 352 6847 12209 9244 1512 1014 1574 N ATOM 3414 CA THR B 352 97.171 34.039 -4.572 1.00 70.17 C ANISOU 3414 CA THR B 352 6323 11914 8424 1729 1192 1602 C ATOM 3415 C THR B 352 97.563 35.270 -5.387 1.00 68.09 C ANISOU 3415 C THR B 352 6013 11772 8087 1791 1240 1283 C ATOM 3416 O THR B 352 97.034 36.356 -5.141 1.00 67.44 O ANISOU 3416 O THR B 352 5876 11928 7821 1890 1425 1353 O ATOM 3417 CB THR B 352 98.064 34.009 -3.290 1.00 67.88 C ANISOU 3417 CB THR B 352 6235 11588 7966 1985 1162 1590 C ATOM 3418 OG1 THR B 352 99.345 33.422 -3.596 1.00 65.39 O ANISOU 3418 OG1 THR B 352 6039 11039 7769 2015 943 1283 O ATOM 3419 CG2 THR B 352 97.387 33.214 -2.173 1.00 61.20 C ANISOU 3419 CG2 THR B 352 5453 10720 7078 1995 1224 1997 C ATOM 3420 N ALA B 353 98.477 35.085 -6.345 1.00 53.62 N ANISOU 3420 N ALA B 353 4210 9767 6396 1732 1086 940 N ATOM 3421 CA ALA B 353 99.142 36.174 -7.054 1.00 51.18 C ANISOU 3421 CA ALA B 353 3910 9513 6021 1812 1129 586 C ATOM 3422 C ALA B 353 98.190 37.123 -7.760 1.00 50.24 C ANISOU 3422 C ALA B 353 3657 9600 5832 1762 1297 639 C ATOM 3423 O ALA B 353 98.435 38.322 -7.847 1.00 48.66 O ANISOU 3423 O ALA B 353 3566 9435 5489 1842 1386 464 O ATOM 3424 CB ALA B 353 100.116 35.604 -8.048 1.00 53.21 C ANISOU 3424 CB ALA B 353 4208 9527 6483 1710 935 250 C ATOM 3425 N TYR B 354 97.097 36.593 -8.272 1.00 51.33 N ANISOU 3425 N TYR B 354 3653 9763 6087 1572 1290 859 N ATOM 3426 CA TYR B 354 96.142 37.434 -8.964 1.00 50.69 C ANISOU 3426 CA TYR B 354 3442 9881 5938 1536 1426 908 C ATOM 3427 C TYR B 354 94.867 37.670 -8.161 1.00 52.19 C ANISOU 3427 C TYR B 354 3612 10205 6015 1517 1542 1257 C ATOM 3428 O TYR B 354 94.139 38.630 -8.401 1.00 51.64 O ANISOU 3428 O TYR B 354 3644 10138 5837 1483 1576 1249 O ATOM 3429 CB TYR B 354 95.784 36.818 -10.304 1.00 50.75 C ANISOU 3429 CB TYR B 354 3335 9789 6159 1320 1303 829 C ATOM 3430 CG TYR B 354 96.851 36.923 -11.356 1.00 48.95 C ANISOU 3430 CG TYR B 354 3190 9393 6015 1306 1194 439 C ATOM 3431 CD1 TYR B 354 96.914 38.028 -12.202 1.00 47.21 C ANISOU 3431 CD1 TYR B 354 3079 9160 5701 1329 1257 224 C ATOM 3432 CD2 TYR B 354 97.778 35.907 -11.532 1.00 49.10 C ANISOU 3432 CD2 TYR B 354 3286 9148 6221 1222 994 276 C ATOM 3433 CE1 TYR B 354 97.885 38.115 -13.187 1.00 52.48 C ANISOU 3433 CE1 TYR B 354 3830 9660 6449 1308 1182 -123 C ATOM 3434 CE2 TYR B 354 98.749 35.989 -12.505 1.00 47.52 C ANISOU 3434 CE2 TYR B 354 3157 8792 6108 1200 901 -89 C ATOM 3435 CZ TYR B 354 98.803 37.089 -13.327 1.00 45.85 C ANISOU 3435 CZ TYR B 354 2956 8673 5790 1261 1020 -289 C ATOM 3436 OH TYR B 354 99.763 37.155 -14.301 1.00 44.43 O ANISOU 3436 OH TYR B 354 2858 8324 5698 1233 947 -651 O ATOM 3437 N MET B 355 94.591 36.802 -7.200 1.00 40.83 N ANISOU 3437 N MET B 355 3117 8054 4345 1123 1405 893 N ATOM 3438 CA MET B 355 93.312 36.865 -6.508 1.00 47.35 C ANISOU 3438 CA MET B 355 3891 8998 5102 1219 1483 926 C ATOM 3439 C MET B 355 93.194 37.968 -5.450 1.00 48.54 C ANISOU 3439 C MET B 355 4124 9263 5057 1326 1541 881 C ATOM 3440 O MET B 355 94.098 38.193 -4.633 1.00 43.84 O ANISOU 3440 O MET B 355 3578 8723 4356 1301 1541 884 O ATOM 3441 CB MET B 355 93.006 35.511 -5.867 1.00 43.90 C ANISOU 3441 CB MET B 355 3329 8606 4744 1172 1528 1074 C ATOM 3442 CG MET B 355 92.698 34.431 -6.879 1.00 43.64 C ANISOU 3442 CG MET B 355 3202 8454 4926 1073 1529 1074 C ATOM 3443 SD MET B 355 92.380 32.887 -6.035 1.00 75.33 S ANISOU 3443 SD MET B 355 7071 12490 9061 1019 1622 1248 S ATOM 3444 CE MET B 355 90.582 32.848 -6.041 1.00 47.48 C ANISOU 3444 CE MET B 355 3429 9056 5557 1072 1711 1227 C ATOM 3445 N ALA B 356 92.043 38.636 -5.466 1.00 50.27 N ANISOU 3445 N ALA B 356 4352 9526 5224 1445 1604 833 N ATOM 3446 CA ALA B 356 91.721 39.628 -4.449 1.00 55.15 C ANISOU 3446 CA ALA B 356 5051 10237 5667 1560 1702 772 C ATOM 3447 C ALA B 356 91.503 38.953 -3.096 1.00 48.40 C ANISOU 3447 C ALA B 356 4127 9543 4721 1569 1762 887 C ATOM 3448 O ALA B 356 91.306 37.742 -3.013 1.00 48.59 O ANISOU 3448 O ALA B 356 4024 9597 4841 1513 1744 1029 O ATOM 3449 CB ALA B 356 90.507 40.429 -4.854 1.00 47.82 C ANISOU 3449 CB ALA B 356 4136 9308 4725 1701 1766 717 C ATOM 3450 N PRO B 357 91.563 39.740 -2.024 1.00 49.97 N ANISOU 3450 N PRO B 357 4416 9840 4729 1636 1851 818 N ATOM 3451 CA PRO B 357 91.395 39.174 -0.685 1.00 51.98 C ANISOU 3451 CA PRO B 357 4609 10283 4857 1657 1913 932 C ATOM 3452 C PRO B 357 90.003 38.586 -0.477 1.00 59.11 C ANISOU 3452 C PRO B 357 5386 11261 5811 1742 1984 1048 C ATOM 3453 O PRO B 357 89.889 37.494 0.084 1.00 61.73 O ANISOU 3453 O PRO B 357 5597 11685 6173 1709 1992 1220 O ATOM 3454 CB PRO B 357 91.641 40.369 0.237 1.00 54.17 C ANISOU 3454 CB PRO B 357 5020 10708 4854 1755 2006 807 C ATOM 3455 CG PRO B 357 91.509 41.575 -0.625 1.00 61.27 C ANISOU 3455 CG PRO B 357 6056 11440 5786 1806 2037 622 C ATOM 3456 CD PRO B 357 91.905 41.169 -1.997 1.00 50.51 C ANISOU 3456 CD PRO B 357 4650 9885 4657 1703 1909 642 C ATOM 3457 N GLU B 358 88.965 39.279 -0.935 1.00 54.39 N ANISOU 3457 N GLU B 358 4804 10629 5230 1852 2042 973 N ATOM 3458 CA GLU B 358 87.608 38.761 -0.789 1.00 57.18 C ANISOU 3458 CA GLU B 358 5021 11073 5633 1928 2113 1084 C ATOM 3459 C GLU B 358 87.431 37.477 -1.596 1.00 55.16 C ANISOU 3459 C GLU B 358 4613 10757 5590 1811 2040 1201 C ATOM 3460 O GLU B 358 86.697 36.583 -1.190 1.00 56.72 O ANISOU 3460 O GLU B 358 4672 11034 5844 1804 2101 1335 O ATOM 3461 CB GLU B 358 86.565 39.802 -1.210 1.00 57.35 C ANISOU 3461 CB GLU B 358 5078 11081 5633 2079 2185 991 C ATOM 3462 CG GLU B 358 86.430 40.008 -2.694 1.00 55.67 C ANISOU 3462 CG GLU B 358 4850 10738 5563 2060 2093 944 C ATOM 3463 CD GLU B 358 87.382 41.064 -3.222 1.00 57.62 C ANISOU 3463 CD GLU B 358 5272 10842 5779 2056 2052 792 C ATOM 3464 OE1 GLU B 358 88.079 41.700 -2.402 1.00 58.55 O ANISOU 3464 OE1 GLU B 358 5527 10957 5763 2061 2112 698 O ATOM 3465 OE2 GLU B 358 87.428 41.266 -4.454 1.00 52.66 O1+ ANISOU 3465 OE2 GLU B 358 4643 10112 5252 2039 1973 761 O1+ ATOM 3466 N ALA B 359 88.121 37.366 -2.724 1.00 52.80 N ANISOU 3466 N ALA B 359 4341 10306 5413 1709 1929 1141 N ATOM 3467 CA ALA B 359 88.019 36.151 -3.517 1.00 52.08 C ANISOU 3467 CA ALA B 359 4125 10136 5526 1579 1884 1209 C ATOM 3468 C ALA B 359 88.711 34.987 -2.808 1.00 59.37 C ANISOU 3468 C ALA B 359 4993 11065 6499 1482 1892 1350 C ATOM 3469 O ALA B 359 88.267 33.843 -2.898 1.00 62.55 O ANISOU 3469 O ALA B 359 5263 11444 7059 1407 1936 1447 O ATOM 3470 CB ALA B 359 88.602 36.362 -4.894 1.00 49.79 C ANISOU 3470 CB ALA B 359 3889 9694 5336 1504 1778 1098 C ATOM 3471 N LEU B 360 89.792 35.279 -2.091 1.00 56.07 N ANISOU 3471 N LEU B 360 4667 10685 5955 1484 1861 1365 N ATOM 3472 CA LEU B 360 90.468 34.241 -1.326 1.00 56.32 C ANISOU 3472 CA LEU B 360 4636 10756 6006 1423 1868 1536 C ATOM 3473 C LEU B 360 89.577 33.800 -0.184 1.00 60.53 C ANISOU 3473 C LEU B 360 5072 11455 6470 1500 1986 1685 C ATOM 3474 O LEU B 360 89.635 32.648 0.237 1.00 64.15 O ANISOU 3474 O LEU B 360 5427 11924 7026 1454 2028 1867 O ATOM 3475 CB LEU B 360 91.827 34.717 -0.800 1.00 51.43 C ANISOU 3475 CB LEU B 360 4114 10187 5240 1408 1802 1521 C ATOM 3476 CG LEU B 360 92.891 34.894 -1.886 1.00 48.84 C ANISOU 3476 CG LEU B 360 3857 9691 5009 1311 1691 1421 C ATOM 3477 CD1 LEU B 360 94.175 35.423 -1.293 1.00 48.39 C ANISOU 3477 CD1 LEU B 360 3874 9715 4798 1289 1636 1402 C ATOM 3478 CD2 LEU B 360 93.120 33.595 -2.624 1.00 48.16 C ANISOU 3478 CD2 LEU B 360 3684 9454 5162 1204 1670 1518 C ATOM 3479 N ARG B 361 88.751 34.714 0.313 1.00 56.45 N ANISOU 3479 N ARG B 361 4591 11060 5797 1625 2056 1615 N ATOM 3480 CA ARG B 361 87.781 34.364 1.341 1.00 59.31 C ANISOU 3480 CA ARG B 361 4858 11587 6091 1711 2183 1749 C ATOM 3481 C ARG B 361 86.660 33.518 0.763 1.00 67.49 C ANISOU 3481 C ARG B 361 5740 12564 7339 1671 2242 1817 C ATOM 3482 O ARG B 361 85.958 32.837 1.494 1.00 69.94 O ANISOU 3482 O ARG B 361 5931 12975 7666 1698 2350 1973 O ATOM 3483 CB ARG B 361 87.186 35.609 1.991 1.00 60.87 C ANISOU 3483 CB ARG B 361 5143 11917 6068 1863 2264 1637 C ATOM 3484 CG ARG B 361 88.120 36.335 2.904 1.00 61.21 C ANISOU 3484 CG ARG B 361 5318 12067 5873 1891 2262 1566 C ATOM 3485 CD ARG B 361 87.428 37.510 3.513 1.00 63.25 C ANISOU 3485 CD ARG B 361 5677 12422 5934 2032 2383 1428 C ATOM 3486 NE ARG B 361 88.325 38.641 3.662 1.00 62.92 N ANISOU 3486 NE ARG B 361 5815 12382 5709 2039 2367 1237 N ATOM 3487 CZ ARG B 361 89.238 38.744 4.617 1.00 64.26 C ANISOU 3487 CZ ARG B 361 6028 12746 5641 2034 2362 1253 C ATOM 3488 NH1 ARG B 361 89.375 37.773 5.503 1.00 65.74 N1+ ANISOU 3488 NH1 ARG B 361 6092 13122 5765 2025 2366 1468 N1+ ATOM 3489 NH2 ARG B 361 90.017 39.811 4.686 1.00 64.41 N ANISOU 3489 NH2 ARG B 361 6213 12778 5481 2029 2359 1056 N ATOM 3490 N GLY B 362 86.466 33.575 -0.548 1.00 66.31 N ANISOU 3490 N GLY B 362 5582 12266 7346 1602 2180 1694 N ATOM 3491 CA GLY B 362 85.422 32.768 -1.154 1.00 67.32 C ANISOU 3491 CA GLY B 362 5546 12355 7678 1536 2238 1722 C ATOM 3492 C GLY B 362 84.290 33.507 -1.848 1.00 60.19 C ANISOU 3492 C GLY B 362 4604 11493 6772 1608 2249 1608 C ATOM 3493 O GLY B 362 83.569 32.902 -2.635 1.00 69.75 O ANISOU 3493 O GLY B 362 5673 12665 8163 1522 2267 1583 O ATOM 3494 N GLU B 363 84.119 34.795 -1.567 1.00 60.37 N ANISOU 3494 N GLU B 363 4740 11598 6601 1764 2251 1536 N ATOM 3495 CA GLU B 363 83.187 35.616 -2.335 1.00 60.82 C ANISOU 3495 CA GLU B 363 4776 11682 6650 1857 2249 1441 C ATOM 3496 C GLU B 363 83.409 35.466 -3.847 1.00 68.88 C ANISOU 3496 C GLU B 363 5778 12572 7821 1744 2136 1336 C ATOM 3497 O GLU B 363 84.543 35.278 -4.317 1.00 67.56 O ANISOU 3497 O GLU B 363 5700 12269 7701 1639 2043 1283 O ATOM 3498 CB GLU B 363 83.306 37.084 -1.929 1.00 60.99 C ANISOU 3498 CB GLU B 363 4964 11743 6465 2032 2269 1353 C ATOM 3499 CG GLU B 363 83.364 37.294 -0.427 1.00 62.82 C ANISOU 3499 CG GLU B 363 5250 12099 6521 2126 2378 1411 C ATOM 3500 CD GLU B 363 82.980 38.709 -0.020 1.00 83.06 C ANISOU 3500 CD GLU B 363 7939 14712 8908 2317 2466 1303 C ATOM 3501 OE1 GLU B 363 82.854 39.569 -0.921 1.00 85.23 O ANISOU 3501 OE1 GLU B 363 8277 14900 9206 2377 2428 1196 O ATOM 3502 OE2 GLU B 363 82.790 38.957 1.195 1.00 82.02 O1+ ANISOU 3502 OE2 GLU B 363 7844 14704 8617 2411 2587 1326 O1+ ATOM 3503 N ILE B 364 82.319 35.521 -4.607 1.00 71.85 N ANISOU 3503 N ILE B 364 6023 13009 8266 1767 2147 1310 N ATOM 3504 CA ILE B 364 82.396 35.482 -6.071 1.00 70.62 C ANISOU 3504 CA ILE B 364 5835 12777 8219 1681 2045 1203 C ATOM 3505 C ILE B 364 81.761 36.740 -6.662 1.00 65.79 C ANISOU 3505 C ILE B 364 5256 12248 7491 1852 2020 1158 C ATOM 3506 O ILE B 364 80.555 36.933 -6.539 1.00 64.54 O ANISOU 3506 O ILE B 364 4970 12241 7312 1955 2091 1210 O ATOM 3507 CB ILE B 364 81.700 34.221 -6.645 1.00 68.21 C ANISOU 3507 CB ILE B 364 5301 12481 8134 1516 2077 1200 C ATOM 3508 CG1 ILE B 364 82.546 32.969 -6.364 1.00 65.85 C ANISOU 3508 CG1 ILE B 364 4989 12036 7994 1335 2098 1223 C ATOM 3509 CG2 ILE B 364 81.449 34.383 -8.143 1.00 59.26 C ANISOU 3509 CG2 ILE B 364 4104 11347 7066 1470 1985 1082 C ATOM 3510 CD1 ILE B 364 81.729 31.728 -6.021 1.00 61.48 C ANISOU 3510 CD1 ILE B 364 4214 11515 7633 1219 2223 1284 C ATOM 3511 N THR B 365 82.570 37.589 -7.296 1.00 57.14 N ANISOU 3511 N THR B 365 4323 11057 6330 1889 1931 1075 N ATOM 3512 CA THR B 365 82.098 38.901 -7.746 1.00 57.80 C ANISOU 3512 CA THR B 365 4468 11194 6300 2079 1929 1052 C ATOM 3513 C THR B 365 83.002 39.588 -8.775 1.00 73.14 C ANISOU 3513 C THR B 365 6551 13014 8225 2073 1823 965 C ATOM 3514 O THR B 365 84.215 39.467 -8.717 1.00 53.43 O ANISOU 3514 O THR B 365 4179 10378 5746 1973 1771 915 O ATOM 3515 CB THR B 365 81.950 39.854 -6.569 1.00 59.16 C ANISOU 3515 CB THR B 365 4756 11395 6327 2263 2041 1074 C ATOM 3516 OG1 THR B 365 82.034 41.199 -7.049 1.00 59.10 O ANISOU 3516 OG1 THR B 365 4880 11338 6237 2422 2041 1019 O ATOM 3517 CG2 THR B 365 83.068 39.636 -5.593 1.00 57.89 C ANISOU 3517 CG2 THR B 365 4724 11143 6127 2185 2052 1053 C ATOM 3518 N PRO B 366 82.402 40.357 -9.699 1.00 75.54 N ANISOU 3518 N PRO B 366 6829 13386 8487 2196 1798 965 N ATOM 3519 CA PRO B 366 83.142 41.063 -10.756 1.00 64.46 C ANISOU 3519 CA PRO B 366 5544 11886 7062 2212 1711 907 C ATOM 3520 C PRO B 366 84.182 42.043 -10.215 1.00 53.48 C ANISOU 3520 C PRO B 366 4382 10330 5608 2276 1743 852 C ATOM 3521 O PRO B 366 85.130 42.362 -10.924 1.00 64.07 O ANISOU 3521 O PRO B 366 5829 11550 6965 2226 1672 796 O ATOM 3522 CB PRO B 366 82.033 41.813 -11.508 1.00 65.46 C ANISOU 3522 CB PRO B 366 5582 12165 7125 2394 1724 965 C ATOM 3523 CG PRO B 366 80.928 41.950 -10.492 1.00 59.50 C ANISOU 3523 CG PRO B 366 4743 11534 6330 2530 1851 1043 C ATOM 3524 CD PRO B 366 80.963 40.674 -9.736 1.00 59.27 C ANISOU 3524 CD PRO B 366 4620 11514 6386 2352 1866 1043 C ATOM 3525 N LYS B 367 84.017 42.510 -8.981 1.00 54.75 N ANISOU 3525 N LYS B 367 4613 10489 5700 2378 1860 855 N ATOM 3526 CA LYS B 367 84.999 43.415 -8.393 1.00 54.01 C ANISOU 3526 CA LYS B 367 4727 10245 5548 2414 1912 765 C ATOM 3527 C LYS B 367 86.356 42.708 -8.184 1.00 52.59 C ANISOU 3527 C LYS B 367 4605 9963 5412 2207 1832 715 C ATOM 3528 O LYS B 367 87.388 43.352 -8.012 1.00 50.45 O ANISOU 3528 O LYS B 367 4490 9565 5113 2185 1843 626 O ATOM 3529 CB LYS B 367 84.471 43.980 -7.075 1.00 56.36 C ANISOU 3529 CB LYS B 367 5078 10587 5748 2555 2072 754 C ATOM 3530 CG LYS B 367 83.184 44.768 -7.218 1.00 59.13 C ANISOU 3530 CG LYS B 367 5383 11024 6059 2784 2174 809 C ATOM 3531 CD LYS B 367 82.276 44.572 -5.994 1.00 66.98 C ANISOU 3531 CD LYS B 367 6308 12154 6987 2873 2306 857 C ATOM 3532 CE LYS B 367 80.853 45.107 -6.210 1.00 64.70 C ANISOU 3532 CE LYS B 367 5914 11991 6677 3095 2399 951 C ATOM 3533 NZ LYS B 367 79.960 44.748 -5.058 1.00 67.22 N1+ ANISOU 3533 NZ LYS B 367 6138 12460 6944 3164 2524 1013 N1+ ATOM 3534 N SER B 368 86.323 41.378 -8.186 1.00 50.89 N ANISOU 3534 N SER B 368 4258 9805 5275 2058 1771 774 N ATOM 3535 CA SER B 368 87.513 40.553 -8.105 1.00 48.83 C ANISOU 3535 CA SER B 368 4021 9457 5076 1874 1698 760 C ATOM 3536 C SER B 368 88.227 40.549 -9.442 1.00 52.62 C ANISOU 3536 C SER B 368 4530 9830 5632 1789 1590 711 C ATOM 3537 O SER B 368 89.455 40.645 -9.495 1.00 45.10 O ANISOU 3537 O SER B 368 3679 8764 4693 1705 1547 664 O ATOM 3538 CB SER B 368 87.160 39.120 -7.705 1.00 49.33 C ANISOU 3538 CB SER B 368 3931 9588 5223 1758 1703 846 C ATOM 3539 OG SER B 368 86.733 39.038 -6.358 1.00 56.42 O ANISOU 3539 OG SER B 368 4810 10586 6041 1822 1803 907 O ATOM 3540 N ASP B 369 87.451 40.424 -10.521 1.00 51.24 N ANISOU 3540 N ASP B 369 4257 9715 5499 1809 1551 723 N ATOM 3541 CA ASP B 369 88.004 40.509 -11.870 1.00 52.77 C ANISOU 3541 CA ASP B 369 4474 9841 5737 1752 1458 677 C ATOM 3542 C ASP B 369 88.808 41.797 -12.033 1.00 44.98 C ANISOU 3542 C ASP B 369 3662 8740 4689 1838 1465 631 C ATOM 3543 O ASP B 369 89.850 41.797 -12.663 1.00 45.76 O ANISOU 3543 O ASP B 369 3827 8730 4829 1749 1403 589 O ATOM 3544 CB ASP B 369 86.899 40.436 -12.932 1.00 47.11 C ANISOU 3544 CB ASP B 369 3620 9260 5021 1802 1429 697 C ATOM 3545 CG ASP B 369 86.463 39.009 -13.232 1.00 47.49 C ANISOU 3545 CG ASP B 369 3490 9370 5185 1641 1408 687 C ATOM 3546 OD1 ASP B 369 87.083 38.053 -12.727 1.00 46.62 O ANISOU 3546 OD1 ASP B 369 3374 9165 5175 1495 1419 676 O ATOM 3547 OD2 ASP B 369 85.488 38.838 -13.985 1.00 48.94 O1+ ANISOU 3547 OD2 ASP B 369 3527 9697 5369 1662 1392 689 O1+ ATOM 3548 N ILE B 370 88.323 42.884 -11.443 1.00 46.49 N ANISOU 3548 N ILE B 370 3926 8943 4796 2010 1561 631 N ATOM 3549 CA ILE B 370 89.003 44.173 -11.495 1.00 46.25 C ANISOU 3549 CA ILE B 370 4067 8777 4730 2095 1615 566 C ATOM 3550 C ILE B 370 90.351 44.146 -10.771 1.00 44.77 C ANISOU 3550 C ILE B 370 3992 8469 4550 1965 1623 484 C ATOM 3551 O ILE B 370 91.353 44.687 -11.233 1.00 43.56 O ANISOU 3551 O ILE B 370 3943 8187 4422 1920 1612 422 O ATOM 3552 CB ILE B 370 88.111 45.263 -10.889 1.00 48.74 C ANISOU 3552 CB ILE B 370 4438 9113 4967 2307 1756 565 C ATOM 3553 CG1 ILE B 370 86.857 45.443 -11.752 1.00 50.38 C ANISOU 3553 CG1 ILE B 370 4530 9453 5159 2457 1746 667 C ATOM 3554 CG2 ILE B 370 88.874 46.567 -10.688 1.00 48.91 C ANISOU 3554 CG2 ILE B 370 4660 8955 4967 2370 1861 456 C ATOM 3555 CD1 ILE B 370 87.118 45.699 -13.217 1.00 49.53 C ANISOU 3555 CD1 ILE B 370 4418 9327 5073 2465 1660 697 C ATOM 3556 N TYR B 371 90.365 43.508 -9.619 1.00 45.11 N ANISOU 3556 N TYR B 371 4003 8575 4564 1906 1650 493 N ATOM 3557 CA TYR B 371 91.568 43.435 -8.835 1.00 44.15 C ANISOU 3557 CA TYR B 371 3963 8393 4418 1789 1659 433 C ATOM 3558 C TYR B 371 92.642 42.668 -9.611 1.00 41.84 C ANISOU 3558 C TYR B 371 3640 8033 4225 1625 1537 453 C ATOM 3559 O TYR B 371 93.788 43.097 -9.703 1.00 40.74 O ANISOU 3559 O TYR B 371 3593 7794 4091 1555 1532 388 O ATOM 3560 CB TYR B 371 91.258 42.776 -7.502 1.00 45.29 C ANISOU 3560 CB TYR B 371 4051 8661 4494 1773 1705 478 C ATOM 3561 CG TYR B 371 92.413 42.725 -6.540 1.00 58.38 C ANISOU 3561 CG TYR B 371 5783 10316 6083 1669 1722 431 C ATOM 3562 CD1 TYR B 371 93.367 41.712 -6.621 1.00 43.24 C ANISOU 3562 CD1 TYR B 371 3801 8396 4230 1517 1620 499 C ATOM 3563 CD2 TYR B 371 92.541 43.680 -5.535 1.00 56.40 C ANISOU 3563 CD2 TYR B 371 5656 10113 5660 1746 1848 333 C ATOM 3564 CE1 TYR B 371 94.411 41.662 -5.734 1.00 43.30 C ANISOU 3564 CE1 TYR B 371 3846 8464 4141 1443 1626 491 C ATOM 3565 CE2 TYR B 371 93.585 43.636 -4.642 1.00 47.16 C ANISOU 3565 CE2 TYR B 371 4529 9042 4348 1675 1855 309 C ATOM 3566 CZ TYR B 371 94.517 42.630 -4.747 1.00 51.64 C ANISOU 3566 CZ TYR B 371 5004 9636 4982 1529 1734 404 C ATOM 3567 OH TYR B 371 95.562 42.593 -3.853 1.00 51.61 O ANISOU 3567 OH TYR B 371 5015 9782 4814 1465 1728 404 O ATOM 3568 N SER B 372 92.255 41.541 -10.188 1.00 41.39 N ANISOU 3568 N SER B 372 3452 8022 4250 1560 1459 530 N ATOM 3569 CA SER B 372 93.174 40.751 -10.985 1.00 39.58 C ANISOU 3569 CA SER B 372 3197 7717 4125 1414 1367 538 C ATOM 3570 C SER B 372 93.728 41.567 -12.149 1.00 42.96 C ANISOU 3570 C SER B 372 3705 8046 4573 1430 1333 482 C ATOM 3571 O SER B 372 94.916 41.481 -12.484 1.00 37.12 O ANISOU 3571 O SER B 372 3010 7213 3881 1330 1293 459 O ATOM 3572 CB SER B 372 92.485 39.491 -11.501 1.00 39.84 C ANISOU 3572 CB SER B 372 3087 7799 4252 1346 1331 589 C ATOM 3573 OG SER B 372 92.203 38.598 -10.448 1.00 40.70 O ANISOU 3573 OG SER B 372 3120 7969 4376 1306 1372 657 O ATOM 3574 N PHE B 373 92.862 42.369 -12.761 1.00 44.11 N ANISOU 3574 N PHE B 373 3861 8221 4677 1566 1358 478 N ATOM 3575 CA PHE B 373 93.278 43.195 -13.887 1.00 40.37 C ANISOU 3575 CA PHE B 373 3457 7668 4213 1608 1341 452 C ATOM 3576 C PHE B 373 94.341 44.205 -13.455 1.00 38.52 C ANISOU 3576 C PHE B 373 3370 7299 3967 1603 1410 377 C ATOM 3577 O PHE B 373 95.240 44.544 -14.237 1.00 55.24 O ANISOU 3577 O PHE B 373 5541 9318 6128 1556 1390 353 O ATOM 3578 CB PHE B 373 92.086 43.906 -14.510 1.00 40.60 C ANISOU 3578 CB PHE B 373 3462 7777 4186 1785 1368 491 C ATOM 3579 CG PHE B 373 92.403 44.597 -15.792 1.00 41.24 C ANISOU 3579 CG PHE B 373 3589 7810 4269 1838 1344 502 C ATOM 3580 CD1 PHE B 373 92.853 43.871 -16.890 1.00 41.45 C ANISOU 3580 CD1 PHE B 373 3557 7856 4338 1729 1246 507 C ATOM 3581 CD2 PHE B 373 92.279 45.973 -15.901 1.00 41.40 C ANISOU 3581 CD2 PHE B 373 3718 7760 4253 2003 1440 505 C ATOM 3582 CE1 PHE B 373 93.155 44.507 -18.085 1.00 38.96 C ANISOU 3582 CE1 PHE B 373 3279 7519 4005 1787 1229 530 C ATOM 3583 CE2 PHE B 373 92.578 46.613 -17.079 1.00 41.32 C ANISOU 3583 CE2 PHE B 373 3748 7708 4245 2066 1430 541 C ATOM 3584 CZ PHE B 373 93.013 45.886 -18.175 1.00 40.07 C ANISOU 3584 CZ PHE B 373 3520 7598 4106 1960 1319 562 C ATOM 3585 N GLY B 374 94.255 44.657 -12.209 1.00 39.54 N ANISOU 3585 N GLY B 374 3562 7431 4032 1638 1507 326 N ATOM 3586 CA GLY B 374 95.246 45.552 -11.650 1.00 39.80 C ANISOU 3586 CA GLY B 374 3727 7384 4010 1624 1598 232 C ATOM 3587 C GLY B 374 96.628 44.921 -11.657 1.00 39.09 C ANISOU 3587 C GLY B 374 3618 7275 3960 1450 1527 235 C ATOM 3588 O GLY B 374 97.628 45.561 -11.996 1.00 41.12 O ANISOU 3588 O GLY B 374 3947 7472 4206 1428 1558 193 O ATOM 3589 N VAL B 375 96.680 43.646 -11.293 1.00 38.25 N ANISOU 3589 N VAL B 375 3410 7216 3907 1333 1443 295 N ATOM 3590 CA VAL B 375 97.918 42.908 -11.283 1.00 35.77 C ANISOU 3590 CA VAL B 375 3059 6887 3646 1182 1372 327 C ATOM 3591 C VAL B 375 98.450 42.847 -12.693 1.00 39.75 C ANISOU 3591 C VAL B 375 3561 7284 4259 1136 1310 332 C ATOM 3592 O VAL B 375 99.660 43.018 -12.933 1.00 43.67 O ANISOU 3592 O VAL B 375 4083 7727 4784 1053 1301 319 O ATOM 3593 CB VAL B 375 97.729 41.491 -10.730 1.00 35.68 C ANISOU 3593 CB VAL B 375 2929 6961 3666 1117 1310 427 C ATOM 3594 CG1 VAL B 375 99.041 40.736 -10.785 1.00 46.28 C ANISOU 3594 CG1 VAL B 375 4235 8272 5078 979 1246 476 C ATOM 3595 CG2 VAL B 375 97.212 41.549 -9.299 1.00 37.19 C ANISOU 3595 CG2 VAL B 375 3120 7274 3738 1165 1378 434 C ATOM 3596 N VAL B 376 97.548 42.620 -13.641 1.00 42.48 N ANISOU 3596 N VAL B 376 3858 7648 4633 1204 1270 365 N ATOM 3597 CA VAL B 376 97.931 42.583 -15.054 1.00 33.64 C ANISOU 3597 CA VAL B 376 2734 6467 3579 1180 1217 371 C ATOM 3598 C VAL B 376 98.498 43.924 -15.524 1.00 33.61 C ANISOU 3598 C VAL B 376 2841 6363 3565 1229 1282 321 C ATOM 3599 O VAL B 376 99.441 43.947 -16.284 1.00 32.66 O ANISOU 3599 O VAL B 376 2735 6170 3503 1160 1259 320 O ATOM 3600 CB VAL B 376 96.747 42.196 -15.953 1.00 34.28 C ANISOU 3600 CB VAL B 376 2739 6632 3652 1249 1176 404 C ATOM 3601 CG1 VAL B 376 97.163 42.244 -17.413 1.00 33.63 C ANISOU 3601 CG1 VAL B 376 2659 6517 3604 1231 1132 402 C ATOM 3602 CG2 VAL B 376 96.238 40.806 -15.584 1.00 34.49 C ANISOU 3602 CG2 VAL B 376 2653 6729 3722 1171 1144 432 C ATOM 3603 N LEU B 377 97.932 45.043 -15.077 1.00 37.01 N ANISOU 3603 N LEU B 377 3351 6787 3923 1357 1383 281 N ATOM 3604 CA LEU B 377 98.497 46.339 -15.443 1.00 35.86 C ANISOU 3604 CA LEU B 377 3310 6579 3735 1450 1481 257 C ATOM 3605 C LEU B 377 99.909 46.489 -14.877 1.00 35.63 C ANISOU 3605 C LEU B 377 3317 6534 3685 1339 1525 214 C ATOM 3606 O LEU B 377 100.807 46.984 -15.555 1.00 38.78 O ANISOU 3606 O LEU B 377 3754 6869 4113 1318 1558 217 O ATOM 3607 CB LEU B 377 97.608 47.471 -14.969 1.00 38.11 C ANISOU 3607 CB LEU B 377 3688 6866 3928 1646 1613 229 C ATOM 3608 CG LEU B 377 96.244 47.518 -15.667 1.00 56.02 C ANISOU 3608 CG LEU B 377 5904 9178 6201 1785 1580 303 C ATOM 3609 CD1 LEU B 377 95.408 48.645 -15.098 1.00 41.34 C ANISOU 3609 CD1 LEU B 377 4141 7305 4262 1996 1728 287 C ATOM 3610 CD2 LEU B 377 96.362 47.645 -17.203 1.00 38.25 C ANISOU 3610 CD2 LEU B 377 3632 6911 3991 1817 1521 381 C ATOM 3611 N LEU B 378 100.129 46.019 -13.657 1.00 35.83 N ANISOU 3611 N LEU B 378 3317 6648 3650 1265 1524 191 N ATOM 3612 CA LEU B 378 101.475 46.069 -13.083 1.00 42.37 C ANISOU 3612 CA LEU B 378 4146 7528 4423 1146 1548 168 C ATOM 3613 C LEU B 378 102.451 45.198 -13.884 1.00 38.21 C ANISOU 3613 C LEU B 378 3523 6959 4036 1002 1433 246 C ATOM 3614 O LEU B 378 103.628 45.557 -14.051 1.00 40.28 O ANISOU 3614 O LEU B 378 3785 7225 4296 922 1464 247 O ATOM 3615 CB LEU B 378 101.462 45.645 -11.612 1.00 39.33 C ANISOU 3615 CB LEU B 378 3729 7303 3909 1103 1549 156 C ATOM 3616 CG LEU B 378 100.764 46.620 -10.669 1.00 39.18 C ANISOU 3616 CG LEU B 378 3842 7330 3713 1226 1694 39 C ATOM 3617 CD1 LEU B 378 101.000 46.211 -9.247 1.00 40.28 C ANISOU 3617 CD1 LEU B 378 3951 7672 3683 1159 1687 25 C ATOM 3618 CD2 LEU B 378 101.277 48.014 -10.896 1.00 40.72 C ANISOU 3618 CD2 LEU B 378 4211 7438 3824 1276 1854 -92 C ATOM 3619 N GLU B 379 101.966 44.075 -14.407 1.00 44.05 N ANISOU 3619 N GLU B 379 4193 7650 4894 962 1321 298 N ATOM 3620 CA GLU B 379 102.802 43.238 -15.280 1.00 41.65 C ANISOU 3620 CA GLU B 379 3837 7259 4727 841 1237 339 C ATOM 3621 C GLU B 379 103.198 43.991 -16.547 1.00 40.01 C ANISOU 3621 C GLU B 379 3675 6971 4556 872 1266 329 C ATOM 3622 O GLU B 379 104.349 43.953 -16.989 1.00 30.35 O ANISOU 3622 O GLU B 379 2432 5708 3390 785 1260 353 O ATOM 3623 CB GLU B 379 102.072 41.954 -15.654 1.00 30.46 C ANISOU 3623 CB GLU B 379 2354 5841 3380 827 1155 377 C ATOM 3624 CG GLU B 379 102.062 40.911 -14.571 1.00 30.69 C ANISOU 3624 CG GLU B 379 2313 5942 3406 774 1125 433 C ATOM 3625 CD GLU B 379 101.345 39.661 -15.006 1.00 30.80 C ANISOU 3625 CD GLU B 379 2251 5970 3482 769 1086 473 C ATOM 3626 OE1 GLU B 379 100.125 39.590 -14.830 1.00 41.18 O ANISOU 3626 OE1 GLU B 379 3543 7350 4753 840 1099 467 O ATOM 3627 OE2 GLU B 379 101.991 38.740 -15.540 1.00 42.76 O1+ ANISOU 3627 OE2 GLU B 379 3723 7424 5099 690 1061 499 O1+ ATOM 3628 N ILE B 380 102.219 44.689 -17.112 1.00 37.20 N ANISOU 3628 N ILE B 380 3371 6605 4160 1007 1303 313 N ATOM 3629 CA ILE B 380 102.417 45.430 -18.352 1.00 31.68 C ANISOU 3629 CA ILE B 380 2712 5852 3473 1075 1335 334 C ATOM 3630 C ILE B 380 103.431 46.553 -18.142 1.00 38.88 C ANISOU 3630 C ILE B 380 3688 6739 4347 1090 1463 332 C ATOM 3631 O ILE B 380 104.223 46.826 -19.031 1.00 36.51 O ANISOU 3631 O ILE B 380 3390 6387 4094 1065 1483 374 O ATOM 3632 CB ILE B 380 101.071 46.002 -18.881 1.00 32.70 C ANISOU 3632 CB ILE B 380 2872 6008 3542 1250 1353 353 C ATOM 3633 CG1 ILE B 380 100.240 44.900 -19.565 1.00 32.08 C ANISOU 3633 CG1 ILE B 380 2706 5998 3484 1228 1236 375 C ATOM 3634 CG2 ILE B 380 101.295 47.226 -19.785 1.00 33.83 C ANISOU 3634 CG2 ILE B 380 3091 6108 3654 1388 1445 408 C ATOM 3635 CD1 ILE B 380 98.864 45.324 -19.916 1.00 33.43 C ANISOU 3635 CD1 ILE B 380 2866 6266 3570 1396 1241 417 C ATOM 3636 N ILE B 381 103.419 47.186 -16.967 1.00 34.06 N ANISOU 3636 N ILE B 381 3132 6170 3637 1123 1567 275 N ATOM 3637 CA ILE B 381 104.319 48.304 -16.682 1.00 35.58 C ANISOU 3637 CA ILE B 381 3412 6340 3765 1125 1735 238 C ATOM 3638 C ILE B 381 105.748 47.850 -16.385 1.00 35.25 C ANISOU 3638 C ILE B 381 3273 6373 3748 919 1705 264 C ATOM 3639 O ILE B 381 106.721 48.520 -16.735 1.00 35.77 O ANISOU 3639 O ILE B 381 3358 6409 3825 864 1811 288 O ATOM 3640 CB ILE B 381 103.837 49.117 -15.467 1.00 39.77 C ANISOU 3640 CB ILE B 381 4072 6901 4139 1215 1879 118 C ATOM 3641 CG1 ILE B 381 102.546 49.871 -15.776 1.00 38.91 C ANISOU 3641 CG1 ILE B 381 4075 6688 4019 1444 1950 108 C ATOM 3642 CG2 ILE B 381 104.924 50.084 -14.992 1.00 39.50 C ANISOU 3642 CG2 ILE B 381 4153 6863 3994 1158 2068 34 C ATOM 3643 CD1 ILE B 381 101.895 50.411 -14.547 1.00 40.88 C ANISOU 3643 CD1 ILE B 381 4448 6954 4132 1529 2064 -21 C ATOM 3644 N THR B 382 105.864 46.704 -15.726 1.00 36.50 N ANISOU 3644 N THR B 382 3319 6625 3923 805 1568 287 N ATOM 3645 CA THR B 382 107.119 46.325 -15.098 1.00 34.10 C ANISOU 3645 CA THR B 382 2906 6446 3605 620 1528 328 C ATOM 3646 C THR B 382 107.841 45.258 -15.881 1.00 32.38 C ANISOU 3646 C THR B 382 2589 6144 3569 517 1393 425 C ATOM 3647 O THR B 382 109.051 45.145 -15.786 1.00 32.61 O ANISOU 3647 O THR B 382 2529 6224 3636 372 1368 486 O ATOM 3648 CB THR B 382 106.887 45.824 -13.627 1.00 34.78 C ANISOU 3648 CB THR B 382 2944 6722 3551 579 1477 308 C ATOM 3649 OG1 THR B 382 105.960 44.730 -13.603 1.00 33.48 O ANISOU 3649 OG1 THR B 382 2754 6498 3471 640 1368 351 O ATOM 3650 CG2 THR B 382 106.345 46.939 -12.775 1.00 36.95 C ANISOU 3650 CG2 THR B 382 3355 7085 3600 662 1630 162 C ATOM 3651 N GLY B 383 107.088 44.484 -16.654 1.00 30.95 N ANISOU 3651 N GLY B 383 2431 5841 3488 580 1313 424 N ATOM 3652 CA GLY B 383 107.598 43.280 -17.288 1.00 29.54 C ANISOU 3652 CA GLY B 383 2203 5567 3455 495 1210 463 C ATOM 3653 C GLY B 383 107.834 42.140 -16.310 1.00 29.32 C ANISOU 3653 C GLY B 383 2106 5585 3449 421 1132 509 C ATOM 3654 O GLY B 383 108.291 41.050 -16.689 1.00 28.48 O ANISOU 3654 O GLY B 383 1974 5381 3466 361 1076 531 O ATOM 3655 N LEU B 384 107.523 42.392 -15.041 1.00 30.37 N ANISOU 3655 N LEU B 384 2214 5876 3449 438 1146 521 N ATOM 3656 CA LEU B 384 107.749 41.414 -13.983 1.00 30.63 C ANISOU 3656 CA LEU B 384 2170 6004 3465 386 1078 599 C ATOM 3657 C LEU B 384 106.601 40.413 -13.887 1.00 29.96 C ANISOU 3657 C LEU B 384 2111 5840 3433 443 1055 585 C ATOM 3658 O LEU B 384 105.464 40.747 -14.188 1.00 46.80 O ANISOU 3658 O LEU B 384 4303 7935 5544 526 1088 512 O ATOM 3659 CB LEU B 384 107.955 42.140 -12.654 1.00 41.99 C ANISOU 3659 CB LEU B 384 3555 7707 4692 362 1105 612 C ATOM 3660 CG LEU B 384 109.266 42.947 -12.543 1.00 38.19 C ANISOU 3660 CG LEU B 384 3003 7364 4145 226 1120 630 C ATOM 3661 CD1 LEU B 384 109.382 43.623 -11.202 1.00 35.89 C ANISOU 3661 CD1 LEU B 384 2662 7393 3581 154 1150 586 C ATOM 3662 CD2 LEU B 384 110.479 42.074 -12.808 1.00 33.20 C ANISOU 3662 CD2 LEU B 384 2276 6680 3658 120 1020 758 C ATOM 3663 N PRO B 385 106.896 39.160 -13.524 1.00 35.70 N ANISOU 3663 N PRO B 385 2772 6568 4224 405 1007 679 N ATOM 3664 CA PRO B 385 105.814 38.184 -13.273 1.00 35.88 C ANISOU 3664 CA PRO B 385 2768 6610 4253 465 1006 718 C ATOM 3665 C PRO B 385 105.065 38.467 -11.956 1.00 40.55 C ANISOU 3665 C PRO B 385 3356 7343 4709 509 1025 725 C ATOM 3666 O PRO B 385 105.651 39.050 -11.030 1.00 32.05 O ANISOU 3666 O PRO B 385 2254 6419 3505 484 1022 754 O ATOM 3667 CB PRO B 385 106.560 36.842 -13.209 1.00 30.75 C ANISOU 3667 CB PRO B 385 2041 5934 3709 420 983 846 C ATOM 3668 CG PRO B 385 107.919 37.203 -12.767 1.00 30.97 C ANISOU 3668 CG PRO B 385 2035 6020 3711 352 946 910 C ATOM 3669 CD PRO B 385 108.226 38.551 -13.398 1.00 30.25 C ANISOU 3669 CD PRO B 385 2010 5886 3597 325 963 786 C ATOM 3670 N ALA B 386 103.792 38.061 -11.881 1.00 32.00 N ANISOU 3670 N ALA B 386 2269 6272 3616 579 1047 719 N ATOM 3671 CA ALA B 386 102.959 38.389 -10.735 1.00 32.58 C ANISOU 3671 CA ALA B 386 2345 6475 3558 639 1080 717 C ATOM 3672 C ALA B 386 103.554 37.838 -9.456 1.00 33.52 C ANISOU 3672 C ALA B 386 2394 6734 3611 602 1062 840 C ATOM 3673 O ALA B 386 103.533 38.503 -8.438 1.00 34.86 O ANISOU 3673 O ALA B 386 2546 7117 3584 637 1078 851 O ATOM 3674 CB ALA B 386 101.546 37.879 -10.932 1.00 33.03 C ANISOU 3674 CB ALA B 386 2382 6526 3642 709 1105 714 C ATOM 3675 N VAL B 387 104.100 36.627 -9.503 1.00 46.07 N ANISOU 3675 N VAL B 387 3907 8293 5304 564 1032 976 N ATOM 3676 CA VAL B 387 104.792 36.093 -8.333 1.00 44.74 C ANISOU 3676 CA VAL B 387 3656 8276 5067 541 1006 1136 C ATOM 3677 C VAL B 387 106.178 35.576 -8.704 1.00 34.69 C ANISOU 3677 C VAL B 387 2335 6953 3891 474 958 1239 C ATOM 3678 O VAL B 387 106.376 35.035 -9.767 1.00 43.37 O ANISOU 3678 O VAL B 387 3447 7879 5152 461 968 1229 O ATOM 3679 CB VAL B 387 103.986 34.956 -7.643 1.00 40.04 C ANISOU 3679 CB VAL B 387 2991 7728 4493 597 1043 1278 C ATOM 3680 CG1 VAL B 387 103.865 33.747 -8.559 1.00 35.91 C ANISOU 3680 CG1 VAL B 387 2440 7013 4192 585 1076 1326 C ATOM 3681 CG2 VAL B 387 104.654 34.558 -6.333 1.00 37.61 C ANISOU 3681 CG2 VAL B 387 2594 7623 4074 595 1014 1466 C ATOM 3682 N ASP B 388 107.139 35.769 -7.816 1.00 37.48 N ANISOU 3682 N ASP B 388 2612 7514 4116 438 905 1357 N ATOM 3683 CA ASP B 388 108.495 35.273 -8.016 1.00 41.89 C ANISOU 3683 CA ASP B 388 3107 8052 4757 381 855 1485 C ATOM 3684 C ASP B 388 109.012 34.838 -6.667 1.00 38.35 C ANISOU 3684 C ASP B 388 2513 7913 4143 397 801 1738 C ATOM 3685 O ASP B 388 109.256 35.670 -5.801 1.00 39.89 O ANISOU 3685 O ASP B 388 2626 8456 4075 367 746 1768 O ATOM 3686 CB ASP B 388 109.410 36.334 -8.629 1.00 35.59 C ANISOU 3686 CB ASP B 388 2318 7279 3926 303 816 1399 C ATOM 3687 CG ASP B 388 110.802 35.797 -8.950 1.00 46.99 C ANISOU 3687 CG ASP B 388 3697 8674 5482 247 770 1528 C ATOM 3688 OD1 ASP B 388 111.181 34.715 -8.419 1.00 46.40 O ANISOU 3688 OD1 ASP B 388 3548 8630 5451 278 757 1725 O ATOM 3689 OD2 ASP B 388 111.530 36.466 -9.739 1.00 42.20 O1+ ANISOU 3689 OD2 ASP B 388 3110 7999 4924 180 756 1447 O1+ ATOM 3690 N GLU B 389 109.186 33.533 -6.499 1.00 38.90 N ANISOU 3690 N GLU B 389 2540 7886 4354 438 823 1916 N ATOM 3691 CA GLU B 389 109.449 32.992 -5.180 1.00 48.86 C ANISOU 3691 CA GLU B 389 3656 9447 5462 488 786 2200 C ATOM 3692 C GLU B 389 110.825 33.422 -4.713 1.00 43.00 C ANISOU 3692 C GLU B 389 2780 9009 4549 423 674 2359 C ATOM 3693 O GLU B 389 111.093 33.418 -3.517 1.00 67.71 O ANISOU 3693 O GLU B 389 5759 12534 7435 436 606 2566 O ATOM 3694 CB GLU B 389 109.315 31.463 -5.168 1.00 55.12 C ANISOU 3694 CB GLU B 389 4425 10044 6473 560 859 2380 C ATOM 3695 CG GLU B 389 109.297 30.880 -3.754 1.00 71.94 C ANISOU 3695 CG GLU B 389 6406 12480 8449 647 842 2698 C ATOM 3696 CD GLU B 389 109.023 29.380 -3.712 1.00 82.06 C ANISOU 3696 CD GLU B 389 7652 13562 9964 734 945 2902 C ATOM 3697 OE1 GLU B 389 107.842 28.987 -3.913 1.00 86.30 O ANISOU 3697 OE1 GLU B 389 8236 13948 10606 768 1040 2828 O ATOM 3698 OE2 GLU B 389 109.986 28.606 -3.468 1.00 81.82 O1+ ANISOU 3698 OE2 GLU B 389 7519 13564 10004 781 936 3181 O1+ ATOM 3699 N HIS B 390 111.677 33.824 -5.650 1.00 41.86 N ANISOU 3699 N HIS B 390 2675 8718 4513 343 650 2259 N ATOM 3700 CA HIS B 390 113.036 34.253 -5.320 1.00 54.90 C ANISOU 3700 CA HIS B 390 4191 10644 6023 248 543 2396 C ATOM 3701 C HIS B 390 113.206 35.767 -5.450 1.00 56.25 C ANISOU 3701 C HIS B 390 4363 10994 6014 111 494 2179 C ATOM 3702 O HIS B 390 114.322 36.269 -5.679 1.00 56.35 O ANISOU 3702 O HIS B 390 4305 11105 5999 -13 425 2195 O ATOM 3703 CB HIS B 390 114.066 33.543 -6.212 1.00 53.38 C ANISOU 3703 CB HIS B 390 4009 10181 6091 249 559 2479 C ATOM 3704 CG HIS B 390 113.914 32.058 -6.239 1.00 54.99 C ANISOU 3704 CG HIS B 390 4216 10174 6505 370 639 2654 C ATOM 3705 ND1 HIS B 390 113.849 31.296 -5.092 1.00 63.44 N ANISOU 3705 ND1 HIS B 390 5160 11471 7473 455 628 2956 N ATOM 3706 CD2 HIS B 390 113.807 31.192 -7.275 1.00 56.33 C ANISOU 3706 CD2 HIS B 390 4460 9991 6950 426 737 2622 C ATOM 3707 CE1 HIS B 390 113.701 30.025 -5.418 1.00 60.66 C ANISOU 3707 CE1 HIS B 390 4834 10839 7376 550 730 3060 C ATOM 3708 NE2 HIS B 390 113.676 29.934 -6.736 1.00 63.28 N ANISOU 3708 NE2 HIS B 390 5265 10860 7920 537 795 2893 N ATOM 3709 N ARG B 391 112.100 36.487 -5.297 1.00 42.81 N ANISOU 3709 N ARG B 391 2735 9332 4198 129 543 1979 N ATOM 3710 CA ARG B 391 112.119 37.936 -5.406 1.00 42.98 C ANISOU 3710 CA ARG B 391 2768 9511 4051 7 539 1752 C ATOM 3711 C ARG B 391 111.580 38.574 -4.134 1.00 45.23 C ANISOU 3711 C ARG B 391 2975 10238 3971 -26 528 1694 C ATOM 3712 O ARG B 391 110.736 37.993 -3.460 1.00 45.69 O ANISOU 3712 O ARG B 391 3035 10348 3976 102 557 1771 O ATOM 3713 CB ARG B 391 111.296 38.383 -6.626 1.00 40.33 C ANISOU 3713 CB ARG B 391 2623 8779 3921 68 648 1515 C ATOM 3714 CG ARG B 391 111.158 39.877 -6.806 1.00 40.61 C ANISOU 3714 CG ARG B 391 2700 8923 3808 -23 697 1282 C ATOM 3715 CD ARG B 391 110.324 40.156 -8.024 1.00 38.24 C ANISOU 3715 CD ARG B 391 2575 8237 3716 79 801 1118 C ATOM 3716 NE ARG B 391 108.945 39.727 -7.813 1.00 41.36 N ANISOU 3716 NE ARG B 391 3058 8530 4126 230 859 1083 N ATOM 3717 CZ ARG B 391 108.034 39.614 -8.773 1.00 35.72 C ANISOU 3717 CZ ARG B 391 2474 7505 3594 323 922 982 C ATOM 3718 NH1 ARG B 391 108.344 39.883 -10.028 1.00 41.50 N1+ ANISOU 3718 NH1 ARG B 391 3272 8002 4494 301 940 907 N1+ ATOM 3719 NH2 ARG B 391 106.811 39.211 -8.480 1.00 37.69 N ANISOU 3719 NH2 ARG B 391 2773 7703 3846 424 961 962 N ATOM 3720 N GLU B 392 112.081 39.761 -3.802 1.00 49.47 N ANISOU 3720 N GLU B 392 3451 11096 4249 -220 501 1536 N ATOM 3721 CA GLU B 392 111.497 40.583 -2.740 1.00 49.17 C ANISOU 3721 CA GLU B 392 3426 11428 3827 -278 545 1355 C ATOM 3722 C GLU B 392 110.888 41.848 -3.338 1.00 61.29 C ANISOU 3722 C GLU B 392 5188 12775 5325 -303 696 1012 C ATOM 3723 O GLU B 392 111.613 42.704 -3.839 1.00 63.81 O ANISOU 3723 O GLU B 392 5527 13108 5611 -497 711 873 O ATOM 3724 CB GLU B 392 112.554 40.952 -1.692 1.00 67.85 C ANISOU 3724 CB GLU B 392 5603 14366 5811 -533 417 1392 C ATOM 3725 CG GLU B 392 112.017 41.702 -0.470 1.00 76.03 C ANISOU 3725 CG GLU B 392 6763 15750 6375 -601 443 1162 C ATOM 3726 CD GLU B 392 110.949 40.911 0.282 1.00 87.92 C ANISOU 3726 CD GLU B 392 8263 17247 7895 -346 482 1289 C ATOM 3727 OE1 GLU B 392 111.264 39.797 0.764 1.00 91.81 O ANISOU 3727 OE1 GLU B 392 8522 17909 8453 -267 386 1627 O ATOM 3728 OE2 GLU B 392 109.795 41.397 0.386 1.00 86.72 O1+ ANISOU 3728 OE2 GLU B 392 8343 16907 7698 -217 616 1066 O1+ ATOM 3729 N PRO B 393 109.556 41.979 -3.298 1.00 47.61 N ANISOU 3729 N PRO B 393 3633 10850 3605 -107 817 886 N ATOM 3730 CA PRO B 393 108.564 41.062 -2.735 1.00 47.41 C ANISOU 3730 CA PRO B 393 3595 10785 3634 94 826 1023 C ATOM 3731 C PRO B 393 108.229 39.912 -3.670 1.00 44.57 C ANISOU 3731 C PRO B 393 3231 10023 3680 235 816 1201 C ATOM 3732 O PRO B 393 108.391 40.026 -4.879 1.00 42.43 O ANISOU 3732 O PRO B 393 3037 9433 3652 230 837 1143 O ATOM 3733 CB PRO B 393 107.346 41.958 -2.550 1.00 47.84 C ANISOU 3733 CB PRO B 393 3880 10737 3561 203 975 759 C ATOM 3734 CG PRO B 393 107.461 42.925 -3.689 1.00 46.47 C ANISOU 3734 CG PRO B 393 3856 10303 3498 167 1059 559 C ATOM 3735 CD PRO B 393 108.925 43.183 -3.861 1.00 47.17 C ANISOU 3735 CD PRO B 393 3827 10581 3516 -78 971 582 C ATOM 3736 N GLN B 394 107.746 38.813 -3.117 1.00 44.82 N ANISOU 3736 N GLN B 394 3204 10060 3766 345 797 1394 N ATOM 3737 CA GLN B 394 107.370 37.694 -3.959 1.00 49.45 C ANISOU 3737 CA GLN B 394 3845 10246 4696 433 815 1501 C ATOM 3738 C GLN B 394 106.184 38.060 -4.841 1.00 40.65 C ANISOU 3738 C GLN B 394 2901 8806 3737 511 915 1298 C ATOM 3739 O GLN B 394 106.195 37.822 -6.043 1.00 47.45 O ANISOU 3739 O GLN B 394 3843 9340 4847 501 927 1242 O ATOM 3740 CB GLN B 394 107.054 36.466 -3.119 1.00 43.74 C ANISOU 3740 CB GLN B 394 3035 9601 3985 518 806 1742 C ATOM 3741 CG GLN B 394 108.232 35.932 -2.353 1.00 45.78 C ANISOU 3741 CG GLN B 394 3110 10161 4123 470 700 2006 C ATOM 3742 CD GLN B 394 107.868 34.678 -1.614 1.00 60.25 C ANISOU 3742 CD GLN B 394 4863 12027 6000 581 718 2272 C ATOM 3743 OE1 GLN B 394 106.932 33.976 -1.996 1.00 67.05 O ANISOU 3743 OE1 GLN B 394 5820 12576 7079 658 812 2255 O ATOM 3744 NE2 GLN B 394 108.582 34.390 -0.544 1.00 61.35 N ANISOU 3744 NE2 GLN B 394 4812 12571 5927 580 630 2521 N ATOM 3745 N LEU B 395 105.163 38.661 -4.261 1.00 41.60 N ANISOU 3745 N LEU B 395 3078 9031 3698 588 987 1182 N ATOM 3746 CA LEU B 395 104.018 39.042 -5.074 1.00 42.72 C ANISOU 3746 CA LEU B 395 3363 8895 3975 668 1072 1018 C ATOM 3747 C LEU B 395 104.228 40.430 -5.660 1.00 39.93 C ANISOU 3747 C LEU B 395 3114 8506 3551 648 1122 812 C ATOM 3748 O LEU B 395 104.670 41.350 -4.963 1.00 44.40 O ANISOU 3748 O LEU B 395 3696 9317 3858 601 1151 714 O ATOM 3749 CB LEU B 395 102.728 38.985 -4.251 1.00 46.13 C ANISOU 3749 CB LEU B 395 3817 9404 4306 781 1144 1007 C ATOM 3750 CG LEU B 395 102.571 37.628 -3.559 1.00 42.08 C ANISOU 3750 CG LEU B 395 3190 8952 3844 799 1117 1232 C ATOM 3751 CD1 LEU B 395 101.392 37.597 -2.604 1.00 43.77 C ANISOU 3751 CD1 LEU B 395 3403 9295 3933 903 1193 1244 C ATOM 3752 CD2 LEU B 395 102.471 36.536 -4.607 1.00 40.03 C ANISOU 3752 CD2 LEU B 395 2947 8358 3907 763 1106 1284 C ATOM 3753 N LEU B 396 103.910 40.566 -6.945 1.00 37.96 N ANISOU 3753 N LEU B 396 2950 7957 3516 671 1143 736 N ATOM 3754 CA LEU B 396 104.038 41.830 -7.660 1.00 37.78 C ANISOU 3754 CA LEU B 396 3035 7853 3467 678 1210 571 C ATOM 3755 C LEU B 396 103.123 42.917 -7.096 1.00 44.92 C ANISOU 3755 C LEU B 396 4070 8818 4181 788 1335 412 C ATOM 3756 O LEU B 396 103.503 44.089 -7.049 1.00 48.14 O ANISOU 3756 O LEU B 396 4588 9268 4436 773 1422 260 O ATOM 3757 CB LEU B 396 103.749 41.612 -9.145 1.00 35.58 C ANISOU 3757 CB LEU B 396 2807 7266 3446 698 1197 554 C ATOM 3758 CG LEU B 396 103.790 42.808 -10.095 1.00 35.33 C ANISOU 3758 CG LEU B 396 2882 7112 3430 734 1272 428 C ATOM 3759 CD1 LEU B 396 105.064 43.594 -9.938 1.00 36.29 C ANISOU 3759 CD1 LEU B 396 2993 7361 3435 633 1301 391 C ATOM 3760 CD2 LEU B 396 103.671 42.277 -11.487 1.00 33.34 C ANISOU 3760 CD2 LEU B 396 2638 6624 3407 724 1220 449 C ATOM 3761 N LEU B 397 101.935 42.531 -6.640 1.00 43.63 N ANISOU 3761 N LEU B 397 3914 8643 4020 891 1360 436 N ATOM 3762 CA LEU B 397 100.963 43.507 -6.143 1.00 44.60 C ANISOU 3762 CA LEU B 397 4175 8779 3993 1016 1490 293 C ATOM 3763 C LEU B 397 101.467 44.262 -4.905 1.00 45.00 C ANISOU 3763 C LEU B 397 4306 9073 3717 979 1557 171 C ATOM 3764 O LEU B 397 100.902 45.285 -4.518 1.00 46.58 O ANISOU 3764 O LEU B 397 4690 9244 3765 1064 1691 -5 O ATOM 3765 CB LEU B 397 99.626 42.815 -5.841 1.00 41.67 C ANISOU 3765 CB LEU B 397 3758 8382 3693 1112 1496 369 C ATOM 3766 CG LEU B 397 99.559 41.759 -4.725 1.00 51.24 C ANISOU 3766 CG LEU B 397 4846 9792 4833 1088 1450 516 C ATOM 3767 CD1 LEU B 397 99.326 42.375 -3.342 1.00 45.47 C ANISOU 3767 CD1 LEU B 397 4177 9294 3806 1144 1541 440 C ATOM 3768 CD2 LEU B 397 98.491 40.738 -5.029 1.00 41.64 C ANISOU 3768 CD2 LEU B 397 3557 8456 3807 1123 1429 622 C ATOM 3769 N ASP B 398 102.536 43.766 -4.294 1.00 44.87 N ANISOU 3769 N ASP B 398 4168 9299 3581 840 1460 255 N ATOM 3770 CA ASP B 398 103.079 44.392 -3.093 1.00 47.83 C ANISOU 3770 CA ASP B 398 4613 9965 3595 751 1482 124 C ATOM 3771 C ASP B 398 103.920 45.649 -3.376 1.00 57.47 C ANISOU 3771 C ASP B 398 6003 11178 4654 631 1537 -117 C ATOM 3772 O ASP B 398 104.223 46.402 -2.455 1.00 51.86 O ANISOU 3772 O ASP B 398 5442 10649 3614 535 1566 -326 O ATOM 3773 CB ASP B 398 103.927 43.384 -2.303 1.00 55.08 C ANISOU 3773 CB ASP B 398 5308 11203 4418 628 1334 326 C ATOM 3774 CG ASP B 398 103.103 42.556 -1.303 1.00 57.30 C ANISOU 3774 CG ASP B 398 5506 11618 4648 733 1331 471 C ATOM 3775 OD1 ASP B 398 102.055 43.036 -0.811 1.00 57.70 O ANISOU 3775 OD1 ASP B 398 5698 11628 4599 853 1447 350 O ATOM 3776 OD2 ASP B 398 103.516 41.417 -1.002 1.00 49.26 O1+ ANISOU 3776 OD2 ASP B 398 4282 10739 3697 703 1223 720 O1+ ATOM 3777 N ILE B 399 104.301 45.891 -4.631 1.00 53.45 N ANISOU 3777 N ILE B 399 5494 10455 4361 617 1550 -112 N ATOM 3778 CA ILE B 399 105.083 47.098 -4.915 1.00 52.75 C ANISOU 3778 CA ILE B 399 5571 10348 4123 491 1625 -348 C ATOM 3779 C ILE B 399 104.188 48.323 -4.743 1.00 50.26 C ANISOU 3779 C ILE B 399 5570 9833 3695 641 1817 -615 C ATOM 3780 O ILE B 399 104.669 49.416 -4.457 1.00 52.73 O ANISOU 3780 O ILE B 399 6099 10149 3784 525 1897 -909 O ATOM 3781 CB ILE B 399 105.730 47.093 -6.337 1.00 45.93 C ANISOU 3781 CB ILE B 399 4622 9301 3527 450 1615 -257 C ATOM 3782 CG1 ILE B 399 104.667 47.078 -7.429 1.00 51.10 C ANISOU 3782 CG1 ILE B 399 5329 9608 4479 685 1687 -186 C ATOM 3783 CG2 ILE B 399 106.655 45.904 -6.506 1.00 44.31 C ANISOU 3783 CG2 ILE B 399 4130 9241 3465 309 1439 2 C ATOM 3784 CD1 ILE B 399 105.176 47.557 -8.750 1.00 42.67 C ANISOU 3784 CD1 ILE B 399 4280 8343 3589 676 1735 -181 C ATOM 3785 N LYS B 400 102.880 48.128 -4.884 1.00 49.53 N ANISOU 3785 N LYS B 400 5501 9554 3762 871 1888 -531 N ATOM 3786 CA LYS B 400 101.932 49.196 -4.615 1.00 51.72 C ANISOU 3786 CA LYS B 400 6049 9644 3958 1034 2081 -737 C ATOM 3787 C LYS B 400 102.118 49.744 -3.204 1.00 55.35 C ANISOU 3787 C LYS B 400 6694 10290 4045 941 2124 -981 C ATOM 3788 O LYS B 400 102.042 50.955 -2.994 1.00 60.00 O ANISOU 3788 O LYS B 400 7580 10724 4492 964 2286 -1277 O ATOM 3789 CB LYS B 400 100.497 48.714 -4.805 1.00 50.67 C ANISOU 3789 CB LYS B 400 5836 9385 4030 1232 2107 -581 C ATOM 3790 CG LYS B 400 99.455 49.691 -4.276 1.00 53.42 C ANISOU 3790 CG LYS B 400 6414 9604 4280 1389 2303 -762 C ATOM 3791 CD LYS B 400 98.053 49.198 -4.546 1.00 52.46 C ANISOU 3791 CD LYS B 400 6158 9415 4361 1552 2298 -597 C ATOM 3792 CE LYS B 400 97.010 49.935 -3.707 1.00 67.36 C ANISOU 3792 CE LYS B 400 8206 11267 6120 1690 2477 -742 C ATOM 3793 NZ LYS B 400 96.816 49.368 -2.335 1.00 70.34 N1+ ANISOU 3793 NZ LYS B 400 8553 11892 6283 1649 2462 -733 N1+ ATOM 3794 N GLU B 401 102.369 48.855 -2.244 1.00 60.64 N ANISOU 3794 N GLU B 401 7198 11278 4564 836 1980 -866 N ATOM 3795 CA GLU B 401 102.589 49.262 -0.852 1.00 67.75 C ANISOU 3795 CA GLU B 401 8248 12408 5085 721 1977 -1079 C ATOM 3796 C GLU B 401 103.961 49.925 -0.727 1.00 61.26 C ANISOU 3796 C GLU B 401 7520 11719 4035 420 1890 -1332 C ATOM 3797 O GLU B 401 104.101 50.955 -0.070 1.00 64.80 O ANISOU 3797 O GLU B 401 8253 12136 4232 313 1959 -1689 O ATOM 3798 CB GLU B 401 102.477 48.066 0.113 1.00 69.66 C ANISOU 3798 CB GLU B 401 8252 12978 5239 705 1841 -840 C ATOM 3799 CG GLU B 401 102.411 48.458 1.608 1.00 83.45 C ANISOU 3799 CG GLU B 401 10157 14956 6594 640 1856 -1034 C ATOM 3800 CD GLU B 401 103.053 47.430 2.556 1.00 85.57 C ANISOU 3800 CD GLU B 401 10170 15660 6683 504 1657 -830 C ATOM 3801 OE1 GLU B 401 103.131 46.236 2.197 1.00 87.49 O ANISOU 3801 OE1 GLU B 401 10108 15981 7152 544 1557 -489 O ATOM 3802 OE2 GLU B 401 103.485 47.823 3.665 1.00 90.48 O1+ ANISOU 3802 OE2 GLU B 401 10899 16536 6945 357 1600 -1013 O1+ ATOM 3803 N GLU B 402 104.963 49.333 -1.378 1.00 62.23 N ANISOU 3803 N GLU B 402 7406 11970 4269 254 1739 -1162 N ATOM 3804 CA GLU B 402 106.311 49.907 -1.450 1.00 60.46 C ANISOU 3804 CA GLU B 402 7239 11766 3968 -91 1606 -1344 C ATOM 3805 C GLU B 402 106.318 51.329 -1.982 1.00 62.01 C ANISOU 3805 C GLU B 402 7785 11483 4293 -130 1738 -1663 C ATOM 3806 O GLU B 402 107.066 52.175 -1.507 1.00 65.21 O ANISOU 3806 O GLU B 402 8386 11824 4566 -414 1676 -1960 O ATOM 3807 CB GLU B 402 107.212 49.054 -2.340 1.00 60.07 C ANISOU 3807 CB GLU B 402 6888 11733 4202 -197 1439 -1027 C ATOM 3808 CG GLU B 402 107.625 47.718 -1.752 1.00 63.22 C ANISOU 3808 CG GLU B 402 6940 12585 4493 -247 1280 -714 C ATOM 3809 CD GLU B 402 108.773 47.092 -2.512 1.00 63.17 C ANISOU 3809 CD GLU B 402 6680 12576 4747 -407 1115 -466 C ATOM 3810 OE1 GLU B 402 109.447 46.203 -1.961 1.00 72.13 O ANISOU 3810 OE1 GLU B 402 7550 14069 5786 -513 961 -235 O ATOM 3811 OE2 GLU B 402 109.014 47.498 -3.664 1.00 65.53 O1+ ANISOU 3811 OE2 GLU B 402 7037 12520 5340 -414 1152 -485 O1+ ATOM 3812 N ILE B 403 105.493 51.581 -2.991 1.00 63.92 N ANISOU 3812 N ILE B 403 8093 11392 4801 151 1923 -1590 N ATOM 3813 CA ILE B 403 105.400 52.910 -3.576 1.00 61.53 C ANISOU 3813 CA ILE B 403 8116 10605 4659 174 2089 -1829 C ATOM 3814 C ILE B 403 104.641 53.879 -2.678 1.00 68.58 C ANISOU 3814 C ILE B 403 9344 11394 5317 273 2297 -2178 C ATOM 3815 O ILE B 403 105.117 54.988 -2.438 1.00 74.41 O ANISOU 3815 O ILE B 403 10380 11866 6027 75 2351 -2508 O ATOM 3816 CB ILE B 403 104.730 52.869 -4.954 1.00 61.02 C ANISOU 3816 CB ILE B 403 7994 10263 4927 473 2223 -1606 C ATOM 3817 CG1 ILE B 403 105.655 52.183 -5.971 1.00 56.01 C ANISOU 3817 CG1 ILE B 403 7102 9634 4544 333 2046 -1339 C ATOM 3818 CG2 ILE B 403 104.386 54.273 -5.406 1.00 60.73 C ANISOU 3818 CG2 ILE B 403 8309 9743 5024 581 2451 -1822 C ATOM 3819 CD1 ILE B 403 104.939 51.625 -7.194 1.00 52.01 C ANISOU 3819 CD1 ILE B 403 6420 9056 4285 626 2121 -1058 C ATOM 3820 N GLU B 404 103.471 53.474 -2.183 1.00 65.20 N ANISOU 3820 N GLU B 404 8873 11165 4736 570 2431 -2114 N ATOM 3821 CA GLU B 404 102.685 54.345 -1.302 1.00 74.14 C ANISOU 3821 CA GLU B 404 10322 12184 5663 701 2643 -2412 C ATOM 3822 C GLU B 404 103.516 54.819 -0.130 1.00 77.50 C ANISOU 3822 C GLU B 404 10926 12771 5750 347 2543 -2775 C ATOM 3823 O GLU B 404 103.529 56.005 0.198 1.00 76.87 O ANISOU 3823 O GLU B 404 11204 12396 5608 274 2698 -3159 O ATOM 3824 CB GLU B 404 101.437 53.634 -0.783 1.00 73.29 C ANISOU 3824 CB GLU B 404 10110 12169 5570 970 2685 -2142 C ATOM 3825 CG GLU B 404 100.205 53.833 -1.644 1.00 74.78 C ANISOU 3825 CG GLU B 404 10291 12038 6084 1273 2884 -1981 C ATOM 3826 CD GLU B 404 99.195 52.707 -1.487 1.00 77.06 C ANISOU 3826 CD GLU B 404 10284 12489 6506 1392 2803 -1648 C ATOM 3827 OE1 GLU B 404 99.082 52.153 -0.365 1.00 78.07 O ANISOU 3827 OE1 GLU B 404 10364 12880 6418 1335 2734 -1622 O ATOM 3828 OE2 GLU B 404 98.526 52.372 -2.494 1.00 74.68 O1+ ANISOU 3828 OE2 GLU B 404 9794 12062 6520 1536 2789 -1421 O1+ ATOM 3829 N ASP B 405 104.221 53.873 0.482 1.00 78.41 N ANISOU 3829 N ASP B 405 10782 13335 5677 126 2275 -2627 N ATOM 3830 CA ASP B 405 105.073 54.141 1.632 1.00 76.41 C ANISOU 3830 CA ASP B 405 10619 13334 5079 -227 2111 -2903 C ATOM 3831 C ASP B 405 106.352 54.873 1.236 1.00 82.17 C ANISOU 3831 C ASP B 405 11455 13873 5892 -634 1997 -3149 C ATOM 3832 O ASP B 405 107.220 55.109 2.071 1.00 87.43 O ANISOU 3832 O ASP B 405 12164 14773 6283 -995 1826 -3393 O ATOM 3833 CB ASP B 405 105.413 52.832 2.348 1.00 75.42 C ANISOU 3833 CB ASP B 405 10138 13734 4783 -295 1853 -2573 C ATOM 3834 CG ASP B 405 104.220 52.242 3.087 1.00 91.97 C ANISOU 3834 CG ASP B 405 12192 15928 6825 21 1939 -2361 C ATOM 3835 OD1 ASP B 405 103.092 52.762 2.924 1.00 90.55 O1+ ANISOU 3835 OD1 ASP B 405 12222 15429 6756 307 2189 -2421 O1+ ATOM 3836 OD2 ASP B 405 104.410 51.264 3.844 1.00 95.06 O ANISOU 3836 OD2 ASP B 405 12335 16711 7072 -26 1768 -2123 O ATOM 3837 N GLU B 406 106.466 55.222 -0.042 1.00 78.25 N ANISOU 3837 N GLU B 406 10987 12924 5821 -569 2066 -3034 N ATOM 3838 CA GLU B 406 107.568 56.048 -0.532 1.00 79.87 C ANISOU 3838 CA GLU B 406 11323 12802 6222 -913 1993 -3218 C ATOM 3839 C GLU B 406 108.938 55.403 -0.311 1.00 76.83 C ANISOU 3839 C GLU B 406 10647 12789 5756 -1303 1649 -3102 C ATOM 3840 O GLU B 406 109.954 56.087 -0.255 1.00 79.54 O ANISOU 3840 O GLU B 406 11087 13011 6122 -1684 1546 -3338 O ATOM 3841 CB GLU B 406 107.516 57.435 0.127 1.00 84.93 C ANISOU 3841 CB GLU B 406 12406 13140 6724 -1070 2171 -3754 C ATOM 3842 CG GLU B 406 106.356 58.303 -0.366 1.00 88.42 C ANISOU 3842 CG GLU B 406 13160 13066 7369 -693 2547 -3853 C ATOM 3843 CD GLU B 406 106.172 59.584 0.435 1.00 99.83 C ANISOU 3843 CD GLU B 406 15055 14224 8652 -805 2769 -4396 C ATOM 3844 OE1 GLU B 406 106.680 59.671 1.580 1.00105.81 O ANISOU 3844 OE1 GLU B 406 15878 15292 9032 -1125 2637 -4721 O ATOM 3845 OE2 GLU B 406 105.506 60.508 -0.083 1.00103.39 O1+ ANISOU 3845 OE2 GLU B 406 15795 14142 9348 -564 3087 -4499 O1+ ATOM 3846 N GLU B 407 108.958 54.082 -0.186 1.00 79.55 N ANISOU 3846 N GLU B 407 10623 13582 6020 -1206 1484 -2726 N ATOM 3847 CA GLU B 407 110.213 53.343 -0.170 1.00 73.21 C ANISOU 3847 CA GLU B 407 9491 13114 5213 -1498 1181 -2512 C ATOM 3848 C GLU B 407 110.712 53.187 -1.605 1.00 73.17 C ANISOU 3848 C GLU B 407 9345 12791 5665 -1481 1167 -2247 C ATOM 3849 O GLU B 407 111.880 52.881 -1.833 1.00 74.23 O ANISOU 3849 O GLU B 407 9259 13056 5887 -1749 958 -2115 O ATOM 3850 CB GLU B 407 110.041 51.969 0.484 1.00 85.67 C ANISOU 3850 CB GLU B 407 10729 15256 6566 -1372 1048 -2177 C ATOM 3851 CG GLU B 407 109.369 51.987 1.852 1.00 91.16 C ANISOU 3851 CG GLU B 407 11538 16302 6795 -1310 1097 -2368 C ATOM 3852 CD GLU B 407 108.808 50.624 2.258 1.00 93.82 C ANISOU 3852 CD GLU B 407 11568 17071 7010 -1054 1073 -1967 C ATOM 3853 OE1 GLU B 407 108.261 50.515 3.380 1.00 97.57 O ANISOU 3853 OE1 GLU B 407 12094 17746 7232 -961 1085 -2007 O ATOM 3854 OE2 GLU B 407 108.908 49.665 1.457 1.00 93.46 O1+ ANISOU 3854 OE2 GLU B 407 11234 17015 7261 -926 1029 -1564 O1+ ATOM 3855 N LYS B 408 109.813 53.395 -2.565 1.00 67.19 N ANISOU 3855 N LYS B 408 8703 11645 5182 -1156 1394 -2160 N ATOM 3856 CA LYS B 408 110.143 53.298 -3.990 1.00 71.88 C ANISOU 3856 CA LYS B 408 9191 11936 6183 -1096 1414 -1917 C ATOM 3857 C LYS B 408 109.246 54.206 -4.833 1.00 66.52 C ANISOU 3857 C LYS B 408 8796 10747 5730 -828 1695 -2005 C ATOM 3858 O LYS B 408 108.318 54.843 -4.316 1.00 69.45 O ANISOU 3858 O LYS B 408 9430 10995 5965 -659 1886 -2234 O ATOM 3859 CB LYS B 408 110.011 51.853 -4.490 1.00 69.27 C ANISOU 3859 CB LYS B 408 8483 11871 5965 -901 1329 -1481 C ATOM 3860 CG LYS B 408 110.958 50.847 -3.844 1.00 72.57 C ANISOU 3860 CG LYS B 408 8574 12765 6233 -1117 1071 -1293 C ATOM 3861 CD LYS B 408 112.411 51.146 -4.177 1.00 77.54 C ANISOU 3861 CD LYS B 408 9115 13354 6992 -1477 900 -1301 C ATOM 3862 CE LYS B 408 113.372 50.240 -3.409 1.00 80.62 C ANISOU 3862 CE LYS B 408 9173 14260 7200 -1690 641 -1116 C ATOM 3863 NZ LYS B 408 114.796 50.515 -3.772 1.00 82.14 N1+ ANISOU 3863 NZ LYS B 408 9239 14436 7535 -2037 475 -1100 N1+ ATOM 3864 N THR B 409 109.536 54.266 -6.132 1.00 65.38 N ANISOU 3864 N THR B 409 8591 10325 5926 -775 1730 -1808 N ATOM 3865 CA THR B 409 108.690 54.974 -7.091 1.00 60.84 C ANISOU 3865 CA THR B 409 8218 9320 5578 -475 1985 -1789 C ATOM 3866 C THR B 409 108.356 54.018 -8.219 1.00 62.01 C ANISOU 3866 C THR B 409 8092 9544 5927 -221 1971 -1406 C ATOM 3867 O THR B 409 109.045 53.013 -8.411 1.00 58.50 O ANISOU 3867 O THR B 409 7347 9363 5519 -341 1783 -1189 O ATOM 3868 CB THR B 409 109.368 56.245 -7.673 1.00 63.29 C ANISOU 3868 CB THR B 409 8785 9149 6115 -667 2086 -1954 C ATOM 3869 OG1 THR B 409 110.408 55.872 -8.588 1.00 62.35 O ANISOU 3869 OG1 THR B 409 8446 9023 6220 -838 1950 -1721 O ATOM 3870 CG2 THR B 409 109.955 57.101 -6.573 1.00 67.94 C ANISOU 3870 CG2 THR B 409 9609 9683 6521 -1025 2058 -2363 C ATOM 3871 N ILE B 410 107.304 54.321 -8.971 1.00 60.98 N ANISOU 3871 N ILE B 410 8054 9194 5922 130 2175 -1324 N ATOM 3872 CA ILE B 410 106.927 53.467 -10.094 1.00 51.80 C ANISOU 3872 CA ILE B 410 6639 8114 4928 361 2165 -998 C ATOM 3873 C ILE B 410 108.016 53.450 -11.185 1.00 50.58 C ANISOU 3873 C ILE B 410 6384 7820 5015 192 2086 -841 C ATOM 3874 O ILE B 410 108.154 52.471 -11.923 1.00 50.91 O ANISOU 3874 O ILE B 410 6156 8030 5157 251 2002 -593 O ATOM 3875 CB ILE B 410 105.578 53.898 -10.691 1.00 60.07 C ANISOU 3875 CB ILE B 410 7796 8988 6039 767 2392 -944 C ATOM 3876 CG1 ILE B 410 105.186 52.960 -11.827 1.00 54.37 C ANISOU 3876 CG1 ILE B 410 6793 8413 5454 970 2357 -639 C ATOM 3877 CG2 ILE B 410 105.626 55.337 -11.157 1.00 66.98 C ANISOU 3877 CG2 ILE B 410 8995 9394 7060 806 2588 -1067 C ATOM 3878 CD1 ILE B 410 105.238 51.488 -11.432 1.00 45.91 C ANISOU 3878 CD1 ILE B 410 5399 7748 4295 908 2185 -506 C ATOM 3879 N GLU B 411 108.807 54.515 -11.268 1.00 53.13 N ANISOU 3879 N GLU B 411 6920 7832 5433 -30 2126 -994 N ATOM 3880 CA GLU B 411 109.942 54.548 -12.184 1.00 63.25 C ANISOU 3880 CA GLU B 411 8103 8995 6933 -228 2057 -852 C ATOM 3881 C GLU B 411 110.917 53.404 -11.914 1.00 59.92 C ANISOU 3881 C GLU B 411 7357 8940 6471 -465 1810 -722 C ATOM 3882 O GLU B 411 111.350 52.723 -12.843 1.00 62.10 O ANISOU 3882 O GLU B 411 7411 9282 6903 -439 1759 -477 O ATOM 3883 CB GLU B 411 110.683 55.881 -12.088 1.00 74.63 C ANISOU 3883 CB GLU B 411 9821 10057 8477 -489 2137 -1069 C ATOM 3884 CG GLU B 411 109.874 57.078 -12.554 1.00 86.74 C ANISOU 3884 CG GLU B 411 11679 11149 10130 -245 2420 -1142 C ATOM 3885 CD GLU B 411 109.749 57.153 -14.064 1.00 90.88 C ANISOU 3885 CD GLU B 411 12145 11495 10889 -16 2533 -843 C ATOM 3886 OE1 GLU B 411 110.677 56.686 -14.768 1.00 90.60 O ANISOU 3886 OE1 GLU B 411 11906 11539 10977 -173 2417 -659 O ATOM 3887 OE2 GLU B 411 108.720 57.680 -14.541 1.00 93.60 O1+ ANISOU 3887 OE2 GLU B 411 12638 11644 11281 333 2743 -781 O1+ ATOM 3888 N ASP B 412 111.262 53.191 -10.648 1.00 52.38 N ANISOU 3888 N ASP B 412 6371 8235 5298 -682 1670 -878 N ATOM 3889 CA ASP B 412 112.182 52.116 -10.275 1.00 51.35 C ANISOU 3889 CA ASP B 412 5919 8478 5113 -886 1442 -726 C ATOM 3890 C ASP B 412 111.761 50.751 -10.818 1.00 47.62 C ANISOU 3890 C ASP B 412 5154 8233 4706 -646 1417 -424 C ATOM 3891 O ASP B 412 112.552 49.817 -10.851 1.00 47.82 O ANISOU 3891 O ASP B 412 4899 8492 4778 -762 1275 -232 O ATOM 3892 CB ASP B 412 112.304 52.013 -8.745 1.00 63.03 C ANISOU 3892 CB ASP B 412 7402 10266 6281 -1070 1309 -913 C ATOM 3893 CG ASP B 412 112.892 53.254 -8.111 1.00 68.26 C ANISOU 3893 CG ASP B 412 8322 10756 6857 -1388 1300 -1254 C ATOM 3894 OD1 ASP B 412 113.863 53.814 -8.673 1.00 70.47 O ANISOU 3894 OD1 ASP B 412 8617 10829 7330 -1628 1275 -1267 O ATOM 3895 OD2 ASP B 412 112.387 53.658 -7.037 1.00 72.07 O1+ ANISOU 3895 OD2 ASP B 412 8990 11317 7078 -1408 1326 -1518 O1+ ATOM 3896 N TYR B 413 110.502 50.614 -11.201 1.00 46.61 N ANISOU 3896 N TYR B 413 5083 8045 4583 -314 1561 -385 N ATOM 3897 CA TYR B 413 109.998 49.307 -11.581 1.00 43.03 C ANISOU 3897 CA TYR B 413 4362 7814 4175 -115 1544 -150 C ATOM 3898 C TYR B 413 109.661 49.225 -13.065 1.00 47.91 C ANISOU 3898 C TYR B 413 4941 8255 5007 87 1651 -2 C ATOM 3899 O TYR B 413 109.323 48.151 -13.557 1.00 44.19 O ANISOU 3899 O TYR B 413 4249 7939 4604 222 1643 170 O ATOM 3900 CB TYR B 413 108.762 48.953 -10.753 1.00 43.01 C ANISOU 3900 CB TYR B 413 4374 7989 3979 90 1600 -202 C ATOM 3901 CG TYR B 413 109.056 48.391 -9.380 1.00 44.21 C ANISOU 3901 CG TYR B 413 4422 8471 3907 -61 1470 -223 C ATOM 3902 CD1 TYR B 413 109.615 47.133 -9.235 1.00 42.85 C ANISOU 3902 CD1 TYR B 413 3939 8571 3770 -132 1346 9 C ATOM 3903 CD2 TYR B 413 108.745 49.105 -8.226 1.00 57.94 C ANISOU 3903 CD2 TYR B 413 6370 10255 5388 -114 1490 -466 C ATOM 3904 CE1 TYR B 413 109.882 46.602 -7.986 1.00 44.23 C ANISOU 3904 CE1 TYR B 413 4000 9078 3729 -245 1232 39 C ATOM 3905 CE2 TYR B 413 108.999 48.575 -6.960 1.00 58.54 C ANISOU 3905 CE2 TYR B 413 6340 10688 5215 -242 1367 -470 C ATOM 3906 CZ TYR B 413 109.572 47.322 -6.854 1.00 61.25 C ANISOU 3906 CZ TYR B 413 6356 11318 5596 -302 1233 -197 C ATOM 3907 OH TYR B 413 109.839 46.775 -5.619 1.00 68.46 O ANISOU 3907 OH TYR B 413 7143 12612 6258 -407 1115 -149 O ATOM 3908 N ILE B 414 109.741 50.356 -13.768 1.00 51.49 N ANISOU 3908 N ILE B 414 5612 8389 5561 106 1760 -70 N ATOM 3909 CA ILE B 414 109.377 50.403 -15.177 1.00 40.57 C ANISOU 3909 CA ILE B 414 4210 6866 4338 317 1869 77 C ATOM 3910 C ILE B 414 110.221 49.435 -15.962 1.00 45.85 C ANISOU 3910 C ILE B 414 4614 7658 5147 228 1782 274 C ATOM 3911 O ILE B 414 111.442 49.460 -15.839 1.00 46.22 O ANISOU 3911 O ILE B 414 4601 7697 5262 -33 1691 297 O ATOM 3912 CB ILE B 414 109.554 51.805 -15.790 1.00 46.92 C ANISOU 3912 CB ILE B 414 5282 7297 5247 322 2007 17 C ATOM 3913 CG1 ILE B 414 108.630 52.807 -15.105 1.00 51.56 C ANISOU 3913 CG1 ILE B 414 6154 7711 5725 458 2143 -180 C ATOM 3914 CG2 ILE B 414 109.226 51.777 -17.271 1.00 41.24 C ANISOU 3914 CG2 ILE B 414 4510 6500 4658 549 2107 210 C ATOM 3915 CD1 ILE B 414 108.081 53.883 -16.050 1.00 53.10 C ANISOU 3915 CD1 ILE B 414 6560 7578 6038 693 2353 -132 C ATOM 3916 N ASP B 415 109.564 48.587 -16.753 1.00 36.39 N ANISOU 3916 N ASP B 415 3253 6581 3993 438 1816 405 N ATOM 3917 CA ASP B 415 110.232 47.646 -17.642 1.00 34.64 C ANISOU 3917 CA ASP B 415 2892 6321 3950 361 1688 525 C ATOM 3918 C ASP B 415 111.275 48.367 -18.469 1.00 40.14 C ANISOU 3918 C ASP B 415 3574 6933 4745 266 1798 624 C ATOM 3919 O ASP B 415 110.960 49.297 -19.211 1.00 42.66 O ANISOU 3919 O ASP B 415 4058 7064 5088 390 1923 630 O ATOM 3920 CB ASP B 415 109.218 46.970 -18.559 1.00 32.93 C ANISOU 3920 CB ASP B 415 2732 5978 3801 524 1588 509 C ATOM 3921 CG ASP B 415 109.798 45.788 -19.328 1.00 34.39 C ANISOU 3921 CG ASP B 415 2845 6096 4128 438 1441 553 C ATOM 3922 OD1 ASP B 415 111.054 45.630 -19.433 1.00 31.45 O1+ ANISOU 3922 OD1 ASP B 415 2392 5719 3837 295 1425 617 O1+ ATOM 3923 OD2 ASP B 415 108.968 45.016 -19.847 1.00 31.74 O ANISOU 3923 OD2 ASP B 415 2539 5705 3815 511 1355 513 O ATOM 3924 N LYS B 416 112.520 47.943 -18.347 1.00 35.55 N ANISOU 3924 N LYS B 416 2846 6408 4253 36 1705 698 N ATOM 3925 CA LYS B 416 113.595 48.621 -19.036 1.00 36.66 C ANISOU 3925 CA LYS B 416 3015 6387 4527 -114 1746 769 C ATOM 3926 C LYS B 416 113.633 48.203 -20.496 1.00 35.28 C ANISOU 3926 C LYS B 416 2828 6112 4465 21 1756 857 C ATOM 3927 O LYS B 416 114.366 48.773 -21.308 1.00 36.17 O ANISOU 3927 O LYS B 416 2950 6114 4680 -38 1845 959 O ATOM 3928 CB LYS B 416 114.931 48.330 -18.348 1.00 54.14 C ANISOU 3928 CB LYS B 416 5072 8706 6792 -420 1610 805 C ATOM 3929 CG LYS B 416 115.010 48.872 -16.923 1.00 54.89 C ANISOU 3929 CG LYS B 416 5279 8834 6743 -610 1507 626 C ATOM 3930 CD LYS B 416 116.304 48.454 -16.243 1.00 61.34 C ANISOU 3930 CD LYS B 416 5882 9843 7581 -904 1345 690 C ATOM 3931 CE LYS B 416 116.765 47.089 -16.755 1.00 61.50 C ANISOU 3931 CE LYS B 416 5627 10013 7728 -819 1304 910 C ATOM 3932 NZ LYS B 416 117.822 46.510 -15.886 1.00 62.86 N1+ ANISOU 3932 NZ LYS B 416 5642 10346 7895 -1001 1110 970 N1+ ATOM 3933 N LYS B 417 112.817 47.222 -20.840 1.00 33.41 N ANISOU 3933 N LYS B 417 2627 5864 4204 171 1625 778 N ATOM 3934 CA LYS B 417 112.809 46.716 -22.198 1.00 32.35 C ANISOU 3934 CA LYS B 417 2527 5638 4125 253 1570 790 C ATOM 3935 C LYS B 417 111.850 47.478 -23.128 1.00 32.74 C ANISOU 3935 C LYS B 417 2692 5640 4106 454 1661 808 C ATOM 3936 O LYS B 417 111.223 46.879 -23.990 1.00 45.01 O ANISOU 3936 O LYS B 417 4275 7192 5636 552 1577 772 O ATOM 3937 CB LYS B 417 112.486 45.217 -22.161 1.00 30.59 C ANISOU 3937 CB LYS B 417 2285 5413 3925 260 1407 704 C ATOM 3938 CG LYS B 417 113.578 44.404 -21.440 1.00 30.50 C ANISOU 3938 CG LYS B 417 2176 5418 3997 109 1325 730 C ATOM 3939 CD LYS B 417 113.456 42.902 -21.632 1.00 29.16 C ANISOU 3939 CD LYS B 417 2011 5187 3881 126 1224 670 C ATOM 3940 CE LYS B 417 112.117 42.360 -21.141 1.00 28.34 C ANISOU 3940 CE LYS B 417 1954 5091 3724 206 1184 590 C ATOM 3941 NZ LYS B 417 111.915 42.555 -19.672 1.00 28.92 N1+ ANISOU 3941 NZ LYS B 417 1987 5271 3732 182 1168 621 N1+ ATOM 3942 N MET B 418 111.750 48.795 -22.941 1.00 38.76 N ANISOU 3942 N MET B 418 3532 6354 4843 514 1851 875 N ATOM 3943 CA MET B 418 110.910 49.693 -23.756 1.00 35.49 C ANISOU 3943 CA MET B 418 3253 5856 4376 746 1971 937 C ATOM 3944 C MET B 418 111.712 50.946 -24.015 1.00 47.05 C ANISOU 3944 C MET B 418 4797 7146 5933 715 2220 1085 C ATOM 3945 O MET B 418 112.565 51.289 -23.207 1.00 53.86 O ANISOU 3945 O MET B 418 5657 7932 6874 492 2276 1068 O ATOM 3946 CB MET B 418 109.603 50.082 -23.053 1.00 35.93 C ANISOU 3946 CB MET B 418 3405 5925 4320 920 2010 853 C ATOM 3947 CG MET B 418 108.768 48.950 -22.543 1.00 38.18 C ANISOU 3947 CG MET B 418 3624 6336 4548 908 1805 721 C ATOM 3948 SD MET B 418 107.172 49.509 -21.859 1.00 48.69 S ANISOU 3948 SD MET B 418 5066 7676 5759 1123 1851 647 S ATOM 3949 CE MET B 418 107.636 50.309 -20.342 1.00 38.52 C ANISOU 3949 CE MET B 418 3854 6363 4419 1064 2045 570 C ATOM 3950 N ASN B 419 111.445 51.656 -25.110 1.00 51.71 N ANISOU 3950 N ASN B 419 5491 7626 6528 894 2332 1215 N ATOM 3951 CA ASN B 419 112.118 52.945 -25.304 1.00 41.31 C ANISOU 3951 CA ASN B 419 4319 6037 5341 849 2590 1352 C ATOM 3952 C ASN B 419 111.155 54.108 -25.565 1.00 43.36 C ANISOU 3952 C ASN B 419 4816 6089 5572 1117 2755 1404 C ATOM 3953 O ASN B 419 111.579 55.219 -25.850 1.00 45.81 O ANISOU 3953 O ASN B 419 5312 6085 6010 1085 2902 1490 O ATOM 3954 CB ASN B 419 113.149 52.848 -26.432 1.00 53.58 C ANISOU 3954 CB ASN B 419 5787 7579 6991 764 2602 1520 C ATOM 3955 CG ASN B 419 112.528 52.479 -27.772 1.00 56.05 C ANISOU 3955 CG ASN B 419 6089 8020 7188 997 2485 1583 C ATOM 3956 OD1 ASN B 419 111.311 52.535 -27.955 1.00 56.67 O ANISOU 3956 OD1 ASN B 419 6223 8168 7139 1230 2449 1562 O ATOM 3957 ND2 ASN B 419 113.372 52.113 -28.722 1.00 60.68 N ANISOU 3957 ND2 ASN B 419 6598 8644 7813 923 2427 1660 N ATOM 3958 N ASP B 420 109.862 53.846 -25.414 1.00 54.01 N ANISOU 3958 N ASP B 420 6151 7600 6772 1373 2734 1355 N ATOM 3959 CA ASP B 420 108.815 54.813 -25.740 1.00 56.42 C ANISOU 3959 CA ASP B 420 6630 7771 7035 1690 2889 1444 C ATOM 3960 C ASP B 420 107.865 55.041 -24.564 1.00 45.02 C ANISOU 3960 C ASP B 420 5296 6285 5523 1782 2903 1261 C ATOM 3961 O ASP B 420 106.800 55.629 -24.727 1.00 53.31 O ANISOU 3961 O ASP B 420 6451 7282 6521 2063 2978 1317 O ATOM 3962 CB ASP B 420 108.016 54.331 -26.947 1.00 43.85 C ANISOU 3962 CB ASP B 420 4941 6400 5321 1880 2681 1551 C ATOM 3963 CG ASP B 420 107.311 53.017 -26.670 1.00 46.81 C ANISOU 3963 CG ASP B 420 5158 7053 5577 1805 2364 1370 C ATOM 3964 OD1 ASP B 420 107.903 52.163 -25.958 1.00 44.67 O ANISOU 3964 OD1 ASP B 420 4786 6848 5340 1564 2248 1216 O ATOM 3965 OD2 ASP B 420 106.162 52.842 -27.131 1.00 45.93 O1+ ANISOU 3965 OD2 ASP B 420 5023 7079 5350 1975 2251 1397 O1+ ATOM 3966 N ALA B 421 108.226 54.570 -23.379 1.00 55.38 N ANISOU 3966 N ALA B 421 6587 7627 6828 1528 2774 1043 N ATOM 3967 CA ALA B 421 107.361 54.822 -22.222 1.00 58.19 C ANISOU 3967 CA ALA B 421 7063 7945 7100 1604 2789 858 C ATOM 3968 C ALA B 421 107.570 56.240 -21.681 1.00 64.92 C ANISOU 3968 C ALA B 421 8248 8358 8062 1546 2955 756 C ATOM 3969 O ALA B 421 108.591 56.517 -21.051 1.00 72.46 O ANISOU 3969 O ALA B 421 9293 9138 9101 1211 2911 614 O ATOM 3970 CB ALA B 421 107.611 53.788 -21.121 1.00 42.90 C ANISOU 3970 CB ALA B 421 4981 6235 5084 1373 2599 678 C ATOM 3971 N ASP B 422 106.621 57.140 -21.925 1.00 59.92 N ANISOU 3971 N ASP B 422 7787 7543 7435 1864 3153 828 N ATOM 3972 CA ASP B 422 106.703 58.475 -21.329 1.00 66.45 C ANISOU 3972 CA ASP B 422 8953 7912 8383 1828 3347 699 C ATOM 3973 C ASP B 422 106.111 58.435 -19.924 1.00 68.63 C ANISOU 3973 C ASP B 422 9324 8216 8535 1802 3324 414 C ATOM 3974 O ASP B 422 105.029 57.885 -19.714 1.00 72.43 O ANISOU 3974 O ASP B 422 9685 8971 8865 2048 3296 424 O ATOM 3975 CB ASP B 422 105.988 59.524 -22.187 1.00 65.38 C ANISOU 3975 CB ASP B 422 8977 7526 8337 2205 3610 927 C ATOM 3976 CG ASP B 422 104.514 59.223 -22.370 1.00 72.32 C ANISOU 3976 CG ASP B 422 9738 8681 9058 2629 3642 1036 C ATOM 3977 OD1 ASP B 422 104.194 58.357 -23.218 1.00 73.15 O1+ ANISOU 3977 OD1 ASP B 422 9572 9169 9054 2737 3484 1215 O1+ ATOM 3978 OD2 ASP B 422 103.677 59.838 -21.667 1.00 69.61 O ANISOU 3978 OD2 ASP B 422 9568 8178 8701 2820 3792 931 O ATOM 3979 N SER B 423 106.822 59.014 -18.964 1.00 68.43 N ANISOU 3979 N SER B 423 9508 7930 8564 1491 3338 154 N ATOM 3980 CA SER B 423 106.448 58.885 -17.555 1.00 67.35 C ANISOU 3980 CA SER B 423 9449 7873 8267 1404 3289 -144 C ATOM 3981 C SER B 423 105.031 59.362 -17.265 1.00 58.42 C ANISOU 3981 C SER B 423 8455 6679 7063 1800 3487 -168 C ATOM 3982 O SER B 423 104.363 58.820 -16.385 1.00 63.08 O ANISOU 3982 O SER B 423 8980 7521 7468 1860 3422 -304 O ATOM 3983 CB SER B 423 107.433 59.641 -16.665 1.00 59.79 C ANISOU 3983 CB SER B 423 8730 6615 7374 1006 3301 -438 C ATOM 3984 OG SER B 423 107.578 60.975 -17.108 1.00 82.48 O ANISOU 3984 OG SER B 423 11895 8976 10468 1046 3559 -427 O ATOM 3985 N THR B 424 104.564 60.367 -17.993 1.00 60.81 N ANISOU 3985 N THR B 424 8935 6658 7514 2086 3740 -13 N ATOM 3986 CA THR B 424 103.206 60.834 -17.768 1.00 62.56 C ANISOU 3986 CA THR B 424 9262 6827 7682 2499 3947 2 C ATOM 3987 C THR B 424 102.191 59.718 -18.013 1.00 68.90 C ANISOU 3987 C THR B 424 9729 8147 8305 2747 3787 167 C ATOM 3988 O THR B 424 101.334 59.458 -17.165 1.00 59.56 O ANISOU 3988 O THR B 424 8503 7136 6991 2789 3687 47 O ATOM 3989 CB THR B 424 102.856 62.044 -18.644 1.00 65.78 C ANISOU 3989 CB THR B 424 9873 6827 8294 2813 4252 222 C ATOM 3990 OG1 THR B 424 103.388 63.230 -18.042 1.00 82.47 O ANISOU 3990 OG1 THR B 424 12364 8396 10575 2630 4460 -16 O ATOM 3991 CG2 THR B 424 101.345 62.201 -18.744 1.00 66.73 C ANISOU 3991 CG2 THR B 424 9929 7089 8337 3216 4284 387 C ATOM 3992 N SER B 425 102.296 59.038 -19.153 1.00 69.36 N ANISOU 3992 N SER B 425 9519 8461 8373 2767 3607 435 N ATOM 3993 CA SER B 425 101.293 58.030 -19.489 1.00 66.96 C ANISOU 3993 CA SER B 425 8901 8596 7946 2833 3290 570 C ATOM 3994 C SER B 425 101.472 56.779 -18.617 1.00 61.43 C ANISOU 3994 C SER B 425 8004 8217 7118 2581 3055 385 C ATOM 3995 O SER B 425 100.485 56.156 -18.227 1.00 50.84 O ANISOU 3995 O SER B 425 6514 7113 5691 2608 2881 365 O ATOM 3996 CB SER B 425 101.337 57.684 -20.984 1.00 53.25 C ANISOU 3996 CB SER B 425 6979 7017 6236 2898 3163 861 C ATOM 3997 OG SER B 425 102.400 56.810 -21.285 1.00 50.56 O ANISOU 3997 OG SER B 425 6482 6830 5900 2647 3030 842 O ATOM 3998 N VAL B 426 102.720 56.441 -18.289 1.00 50.62 N ANISOU 3998 N VAL B 426 6641 6843 5750 2332 3079 268 N ATOM 3999 CA VAL B 426 103.004 55.339 -17.376 1.00 48.47 C ANISOU 3999 CA VAL B 426 6202 6859 5355 2101 2896 121 C ATOM 4000 C VAL B 426 102.419 55.585 -15.993 1.00 50.10 C ANISOU 4000 C VAL B 426 6546 7060 5431 2120 2959 -107 C ATOM 4001 O VAL B 426 101.733 54.725 -15.446 1.00 52.86 O ANISOU 4001 O VAL B 426 6711 7680 5692 2086 2768 -130 O ATOM 4002 CB VAL B 426 104.502 55.093 -17.225 1.00 53.58 C ANISOU 4002 CB VAL B 426 6843 7470 6046 1752 2832 55 C ATOM 4003 CG1 VAL B 426 104.752 54.152 -16.057 1.00 46.46 C ANISOU 4003 CG1 VAL B 426 5811 6840 5003 1525 2655 -94 C ATOM 4004 CG2 VAL B 426 105.089 54.531 -18.519 1.00 45.66 C ANISOU 4004 CG2 VAL B 426 5635 6568 5145 1719 2746 281 C ATOM 4005 N GLU B 427 102.689 56.758 -15.425 1.00 59.96 N ANISOU 4005 N GLU B 427 8133 7957 6692 2121 3202 -292 N ATOM 4006 CA GLU B 427 102.040 57.177 -14.175 1.00 62.30 C ANISOU 4006 CA GLU B 427 8615 8207 6849 2188 3319 -533 C ATOM 4007 C GLU B 427 100.511 57.151 -14.265 1.00 55.90 C ANISOU 4007 C GLU B 427 7677 7514 6049 2443 3229 -404 C ATOM 4008 O GLU B 427 99.835 56.872 -13.280 1.00 56.36 O ANISOU 4008 O GLU B 427 7699 7732 5982 2442 3178 -527 O ATOM 4009 CB GLU B 427 102.507 58.573 -13.771 1.00 59.57 C ANISOU 4009 CB GLU B 427 8662 7374 6596 2077 3510 -758 C ATOM 4010 CG GLU B 427 103.651 58.560 -12.767 1.00 74.56 C ANISOU 4010 CG GLU B 427 10659 9255 8414 1613 3364 -1046 C ATOM 4011 CD GLU B 427 104.653 59.680 -13.001 1.00 83.02 C ANISOU 4011 CD GLU B 427 12001 9860 9682 1366 3461 -1168 C ATOM 4012 OE1 GLU B 427 104.223 60.844 -13.186 1.00 84.28 O ANISOU 4012 OE1 GLU B 427 12449 9596 9977 1556 3742 -1216 O ATOM 4013 OE2 GLU B 427 105.874 59.392 -13.008 1.00 82.68 O1+ ANISOU 4013 OE2 GLU B 427 11872 9869 9675 983 3268 -1201 O1+ ATOM 4014 N ALA B 428 99.967 57.432 -15.442 1.00 55.88 N ANISOU 4014 N ALA B 428 7606 7445 6182 2645 3221 -146 N ATOM 4015 CA ALA B 428 98.533 57.302 -15.652 1.00 56.13 C ANISOU 4015 CA ALA B 428 7494 7626 6208 2851 3126 5 C ATOM 4016 C ALA B 428 98.076 55.852 -15.510 1.00 53.84 C ANISOU 4016 C ALA B 428 6882 7731 5843 2709 2834 46 C ATOM 4017 O ALA B 428 97.133 55.567 -14.764 1.00 53.40 O ANISOU 4017 O ALA B 428 6763 7806 5720 2746 2791 -4 O ATOM 4018 CB ALA B 428 98.143 57.842 -17.009 1.00 56.93 C ANISOU 4018 CB ALA B 428 7585 7625 6421 3073 3168 291 C ATOM 4019 N MET B 429 98.728 54.931 -16.214 1.00 50.01 N ANISOU 4019 N MET B 429 6210 7402 5388 2541 2652 137 N ATOM 4020 CA MET B 429 98.324 53.539 -16.100 1.00 47.32 C ANISOU 4020 CA MET B 429 5612 7348 5019 2388 2400 165 C ATOM 4021 C MET B 429 98.566 53.013 -14.685 1.00 61.23 C ANISOU 4021 C MET B 429 7368 9212 6683 2221 2388 -21 C ATOM 4022 O MET B 429 97.774 52.218 -14.164 1.00 57.57 O ANISOU 4022 O MET B 429 6773 8910 6191 2185 2275 -11 O ATOM 4023 CB MET B 429 99.046 52.650 -17.105 1.00 44.58 C ANISOU 4023 CB MET B 429 5100 7100 4736 2228 2225 271 C ATOM 4024 CG MET B 429 98.471 51.247 -17.149 1.00 42.30 C ANISOU 4024 CG MET B 429 4594 7024 4454 2096 1994 306 C ATOM 4025 SD MET B 429 99.403 50.121 -18.175 1.00 52.32 S ANISOU 4025 SD MET B 429 5714 8363 5804 1883 1810 370 S ATOM 4026 CE MET B 429 98.613 50.347 -19.768 1.00 43.90 C ANISOU 4026 CE MET B 429 4605 7337 4737 2053 1756 542 C ATOM 4027 N TYR B 430 99.646 53.455 -14.052 1.00 47.88 N ANISOU 4027 N TYR B 430 5831 7436 4925 2118 2517 -181 N ATOM 4028 CA TYR B 430 99.888 53.016 -12.694 1.00 48.08 C ANISOU 4028 CA TYR B 430 5863 7605 4801 1968 2510 -349 C ATOM 4029 C TYR B 430 98.733 53.421 -11.769 1.00 50.34 C ANISOU 4029 C TYR B 430 6236 7886 5004 2107 2598 -445 C ATOM 4030 O TYR B 430 98.342 52.649 -10.894 1.00 49.85 O ANISOU 4030 O TYR B 430 6070 8013 4860 2025 2515 -467 O ATOM 4031 CB TYR B 430 101.207 53.558 -12.151 1.00 49.34 C ANISOU 4031 CB TYR B 430 6215 7695 4837 1835 2653 -532 C ATOM 4032 CG TYR B 430 101.383 53.164 -10.706 1.00 50.12 C ANISOU 4032 CG TYR B 430 6332 8001 4709 1691 2634 -706 C ATOM 4033 CD1 TYR B 430 101.923 51.933 -10.366 1.00 47.94 C ANISOU 4033 CD1 TYR B 430 5825 8006 4384 1491 2443 -619 C ATOM 4034 CD2 TYR B 430 100.959 54.004 -9.681 1.00 53.32 C ANISOU 4034 CD2 TYR B 430 6987 8317 4955 1758 2798 -942 C ATOM 4035 CE1 TYR B 430 102.061 51.562 -9.044 1.00 48.94 C ANISOU 4035 CE1 TYR B 430 5954 8356 4286 1371 2405 -732 C ATOM 4036 CE2 TYR B 430 101.091 53.645 -8.367 1.00 54.33 C ANISOU 4036 CE2 TYR B 430 7134 8671 4837 1623 2767 -1097 C ATOM 4037 CZ TYR B 430 101.641 52.426 -8.050 1.00 52.13 C ANISOU 4037 CZ TYR B 430 6610 8707 4492 1434 2563 -975 C ATOM 4038 OH TYR B 430 101.772 52.065 -6.735 1.00 60.03 O ANISOU 4038 OH TYR B 430 7615 9955 5238 1304 2506 -1085 O ATOM 4039 N SER B 431 98.190 54.622 -11.976 1.00 63.14 N ANISOU 4039 N SER B 431 8050 9277 6662 2327 2779 -475 N ATOM 4040 CA SER B 431 97.072 55.122 -11.171 1.00 55.60 C ANISOU 4040 CA SER B 431 7182 8296 5648 2485 2888 -557 C ATOM 4041 C SER B 431 95.835 54.259 -11.351 1.00 54.24 C ANISOU 4041 C SER B 431 6758 8328 5522 2548 2730 -368 C ATOM 4042 O SER B 431 95.149 53.960 -10.385 1.00 55.07 O ANISOU 4042 O SER B 431 6829 8554 5542 2550 2738 -428 O ATOM 4043 CB SER B 431 96.748 56.580 -11.522 1.00 61.71 C ANISOU 4043 CB SER B 431 8211 8737 6498 2729 3121 -578 C ATOM 4044 OG SER B 431 95.591 57.045 -10.828 1.00 61.61 O ANISOU 4044 OG SER B 431 8257 8705 6447 2905 3230 -629 O ATOM 4045 N VAL B 432 95.551 53.858 -12.584 1.00 52.41 N ANISOU 4045 N VAL B 432 6367 8137 5410 2593 2593 -149 N ATOM 4046 CA VAL B 432 94.505 52.872 -12.824 1.00 59.93 C ANISOU 4046 CA VAL B 432 7089 9291 6392 2595 2421 4 C ATOM 4047 C VAL B 432 94.764 51.548 -12.093 1.00 58.80 C ANISOU 4047 C VAL B 432 6800 9329 6212 2363 2273 -33 C ATOM 4048 O VAL B 432 93.843 50.969 -11.490 1.00 55.14 O ANISOU 4048 O VAL B 432 6238 8994 5720 2376 2234 -3 O ATOM 4049 CB VAL B 432 94.346 52.566 -14.308 1.00 49.46 C ANISOU 4049 CB VAL B 432 5634 8001 5156 2628 2285 201 C ATOM 4050 CG1 VAL B 432 93.468 51.330 -14.490 1.00 47.85 C ANISOU 4050 CG1 VAL B 432 5207 8010 4963 2553 2096 300 C ATOM 4051 CG2 VAL B 432 93.755 53.772 -15.015 1.00 60.67 C ANISOU 4051 CG2 VAL B 432 7163 9289 6598 2908 2427 315 C ATOM 4052 N ALA B 433 96.009 51.076 -12.146 1.00 46.95 N ANISOU 4052 N ALA B 433 5287 7836 4718 2166 2205 -74 N ATOM 4053 CA ALA B 433 96.379 49.850 -11.449 1.00 45.21 C ANISOU 4053 CA ALA B 433 4941 7767 4469 1966 2080 -75 C ATOM 4054 C ALA B 433 96.179 49.959 -9.934 1.00 47.08 C ANISOU 4054 C ALA B 433 5255 8084 4548 1962 2182 -198 C ATOM 4055 O ALA B 433 95.729 49.015 -9.284 1.00 46.54 O ANISOU 4055 O ALA B 433 5066 8158 4459 1905 2101 -140 O ATOM 4056 CB ALA B 433 97.837 49.479 -11.758 1.00 43.43 C ANISOU 4056 CB ALA B 433 4697 7537 4267 1782 2014 -84 C ATOM 4057 N SER B 434 96.548 51.104 -9.375 1.00 49.53 N ANISOU 4057 N SER B 434 5784 8299 4738 2017 2369 -380 N ATOM 4058 CA SER B 434 96.492 51.306 -7.940 1.00 51.76 C ANISOU 4058 CA SER B 434 6181 8664 4821 1991 2478 -543 C ATOM 4059 C SER B 434 95.033 51.265 -7.491 1.00 55.97 C ANISOU 4059 C SER B 434 6663 9244 5358 2148 2520 -493 C ATOM 4060 O SER B 434 94.694 50.652 -6.480 1.00 59.81 O ANISOU 4060 O SER B 434 7094 9890 5740 2103 2504 -491 O ATOM 4061 CB SER B 434 97.165 52.633 -7.567 1.00 60.77 C ANISOU 4061 CB SER B 434 7613 9651 5825 2007 2682 -801 C ATOM 4062 OG SER B 434 97.480 52.712 -6.185 1.00 60.75 O ANISOU 4062 OG SER B 434 7744 9770 5569 1900 2755 -1001 O ATOM 4063 N GLN B 435 94.160 51.892 -8.267 1.00 53.98 N ANISOU 4063 N GLN B 435 6417 8872 5221 2345 2571 -424 N ATOM 4064 CA GLN B 435 92.746 51.895 -7.938 1.00 55.53 C ANISOU 4064 CA GLN B 435 6548 9130 5422 2510 2615 -355 C ATOM 4065 C GLN B 435 92.110 50.523 -8.081 1.00 53.35 C ANISOU 4065 C GLN B 435 6020 9035 5215 2438 2428 -168 C ATOM 4066 O GLN B 435 91.235 50.178 -7.301 1.00 76.75 O ANISOU 4066 O GLN B 435 8921 12115 8124 2487 2458 -143 O ATOM 4067 CB GLN B 435 92.002 52.895 -8.802 1.00 57.19 C ANISOU 4067 CB GLN B 435 6815 9190 5725 2753 2709 -287 C ATOM 4068 CG GLN B 435 92.566 54.279 -8.701 1.00 59.78 C ANISOU 4068 CG GLN B 435 7415 9280 6018 2849 2917 -466 C ATOM 4069 CD GLN B 435 91.963 55.211 -9.715 1.00 61.32 C ANISOU 4069 CD GLN B 435 7664 9304 6332 3104 3004 -332 C ATOM 4070 OE1 GLN B 435 90.742 55.290 -9.849 1.00 76.39 O ANISOU 4070 OE1 GLN B 435 9484 11273 8269 3289 3024 -195 O ATOM 4071 NE2 GLN B 435 92.812 55.918 -10.448 1.00 61.43 N ANISOU 4071 NE2 GLN B 435 7823 9108 6410 3123 3064 -347 N ATOM 4072 N CYS B 436 92.514 49.735 -9.070 1.00 50.48 N ANISOU 4072 N CYS B 436 5523 8688 4970 2323 2249 -47 N ATOM 4073 CA CYS B 436 91.941 48.401 -9.191 1.00 48.77 C ANISOU 4073 CA CYS B 436 5099 8610 4821 2234 2089 90 C ATOM 4074 C CYS B 436 92.337 47.539 -8.000 1.00 48.44 C ANISOU 4074 C CYS B 436 5019 8687 4699 2095 2065 68 C ATOM 4075 O CYS B 436 91.617 46.625 -7.608 1.00 48.32 O ANISOU 4075 O CYS B 436 4871 8786 4701 2073 2012 157 O ATOM 4076 CB CYS B 436 92.383 47.720 -10.481 1.00 46.08 C ANISOU 4076 CB CYS B 436 4655 8242 4611 2119 1919 182 C ATOM 4077 SG CYS B 436 91.871 48.528 -11.986 1.00 46.52 S ANISOU 4077 SG CYS B 436 4719 8227 4731 2282 1917 260 S ATOM 4078 N LEU B 437 93.495 47.843 -7.427 1.00 53.67 N ANISOU 4078 N LEU B 437 5798 9335 5260 2006 2111 -43 N ATOM 4079 CA LEU B 437 94.102 46.994 -6.410 1.00 48.25 C ANISOU 4079 CA LEU B 437 5063 8795 4477 1868 2063 -31 C ATOM 4080 C LEU B 437 93.714 47.437 -5.018 1.00 59.50 C ANISOU 4080 C LEU B 437 6588 10322 5696 1937 2210 -132 C ATOM 4081 O LEU B 437 94.358 47.068 -4.029 1.00 60.62 O ANISOU 4081 O LEU B 437 6742 10610 5680 1840 2203 -157 O ATOM 4082 CB LEU B 437 95.619 47.000 -6.553 1.00 47.07 C ANISOU 4082 CB LEU B 437 4959 8633 4294 1719 2014 -78 C ATOM 4083 CG LEU B 437 96.126 46.266 -7.791 1.00 45.38 C ANISOU 4083 CG LEU B 437 4620 8345 4275 1619 1855 37 C ATOM 4084 CD1 LEU B 437 97.631 46.422 -7.924 1.00 43.38 C ANISOU 4084 CD1 LEU B 437 4411 8089 3984 1490 1831 -9 C ATOM 4085 CD2 LEU B 437 95.730 44.808 -7.690 1.00 42.77 C ANISOU 4085 CD2 LEU B 437 4111 8098 4042 1542 1724 185 C ATOM 4086 N HIS B 438 92.664 48.244 -4.946 1.00 58.55 N ANISOU 4086 N HIS B 438 6540 10143 5563 2111 2345 -187 N ATOM 4087 CA HIS B 438 92.117 48.643 -3.665 1.00 56.35 C ANISOU 4087 CA HIS B 438 6357 9955 5098 2191 2502 -287 C ATOM 4088 C HIS B 438 91.717 47.418 -2.837 1.00 56.14 C ANISOU 4088 C HIS B 438 6162 10138 5032 2141 2427 -145 C ATOM 4089 O HIS B 438 90.988 46.538 -3.298 1.00 54.76 O ANISOU 4089 O HIS B 438 5799 9996 5010 2150 2325 26 O ATOM 4090 CB HIS B 438 90.922 49.562 -3.866 1.00 58.59 C ANISOU 4090 CB HIS B 438 6698 10142 5422 2409 2648 -323 C ATOM 4091 CG HIS B 438 90.650 50.443 -2.689 1.00 73.05 C ANISOU 4091 CG HIS B 438 8722 11984 7051 2495 2866 -518 C ATOM 4092 ND1 HIS B 438 90.371 49.946 -1.433 1.00 63.90 N ANISOU 4092 ND1 HIS B 438 7543 11015 5722 2468 2909 -525 N ATOM 4093 CD2 HIS B 438 90.628 51.793 -2.575 1.00 73.12 C ANISOU 4093 CD2 HIS B 438 8958 11830 6995 2607 3063 -728 C ATOM 4094 CE1 HIS B 438 90.185 50.951 -0.598 1.00 71.97 C ANISOU 4094 CE1 HIS B 438 8776 12001 6567 2547 3122 -744 C ATOM 4095 NE2 HIS B 438 90.331 52.082 -1.267 1.00 73.75 N ANISOU 4095 NE2 HIS B 438 9158 12002 6862 2629 3222 -883 N ATOM 4096 N GLU B 439 92.209 47.376 -1.608 1.00 57.85 N ANISOU 4096 N GLU B 439 6456 10502 5022 2081 2483 -222 N ATOM 4097 CA GLU B 439 91.990 46.254 -0.703 1.00 60.37 C ANISOU 4097 CA GLU B 439 6624 11041 5273 2039 2424 -76 C ATOM 4098 C GLU B 439 90.507 45.976 -0.381 1.00 59.50 C ANISOU 4098 C GLU B 439 6410 10988 5209 2180 2497 22 C ATOM 4099 O GLU B 439 90.122 44.826 -0.152 1.00 58.81 O ANISOU 4099 O GLU B 439 6137 11021 5187 2148 2416 203 O ATOM 4100 CB GLU B 439 92.779 46.493 0.591 1.00 65.64 C ANISOU 4100 CB GLU B 439 7424 11885 5630 1967 2485 -197 C ATOM 4101 CG GLU B 439 92.926 47.974 0.984 1.00 74.93 C ANISOU 4101 CG GLU B 439 8901 12964 6606 2008 2678 -494 C ATOM 4102 CD GLU B 439 93.995 48.703 0.179 1.00 81.01 C ANISOU 4102 CD GLU B 439 9815 13562 7403 1917 2658 -639 C ATOM 4103 OE1 GLU B 439 93.630 49.550 -0.672 1.00 81.75 O ANISOU 4103 OE1 GLU B 439 9996 13421 7643 2014 2746 -722 O ATOM 4104 OE2 GLU B 439 95.201 48.429 0.391 1.00 85.30 O1+ ANISOU 4104 OE2 GLU B 439 10368 14222 7820 1754 2551 -656 O1+ ATOM 4105 N LYS B 440 89.674 47.011 -0.358 1.00 61.73 N ANISOU 4105 N LYS B 440 6806 11185 5462 2339 2659 -94 N ATOM 4106 CA LYS B 440 88.240 46.783 -0.173 1.00 66.91 C ANISOU 4106 CA LYS B 440 7342 11906 6175 2482 2724 13 C ATOM 4107 C LYS B 440 87.517 46.892 -1.503 1.00 61.73 C ANISOU 4107 C LYS B 440 6588 11119 5747 2560 2662 98 C ATOM 4108 O LYS B 440 87.575 47.922 -2.171 1.00 62.08 O ANISOU 4108 O LYS B 440 6751 11005 5830 2645 2719 -1 O ATOM 4109 CB LYS B 440 87.646 47.753 0.851 1.00 67.17 C ANISOU 4109 CB LYS B 440 7535 11976 6009 2629 2957 -143 C ATOM 4110 CG LYS B 440 88.107 47.486 2.280 1.00 69.19 C ANISOU 4110 CG LYS B 440 7862 12429 5996 2558 3018 -201 C ATOM 4111 CD LYS B 440 87.766 46.066 2.745 1.00 68.43 C ANISOU 4111 CD LYS B 440 7530 12541 5929 2514 2914 44 C ATOM 4112 CE LYS B 440 86.276 45.927 3.064 1.00 76.46 C ANISOU 4112 CE LYS B 440 8433 13634 6986 2676 3026 144 C ATOM 4113 NZ LYS B 440 85.892 44.579 3.577 1.00 73.30 N1+ ANISOU 4113 NZ LYS B 440 7817 13424 6612 2634 2959 374 N1+ ATOM 4114 N LYS B 441 86.823 45.817 -1.860 1.00 60.49 N ANISOU 4114 N LYS B 441 6219 11039 5727 2527 2553 280 N ATOM 4115 CA LYS B 441 86.250 45.637 -3.195 1.00 65.30 C ANISOU 4115 CA LYS B 441 6704 11594 6512 2565 2449 385 C ATOM 4116 C LYS B 441 85.340 46.769 -3.701 1.00 61.13 C ANISOU 4116 C LYS B 441 6224 11003 5999 2781 2559 359 C ATOM 4117 O LYS B 441 85.187 46.941 -4.907 1.00 60.13 O ANISOU 4117 O LYS B 441 6052 10819 5976 2820 2476 417 O ATOM 4118 CB LYS B 441 85.469 44.318 -3.237 1.00 64.53 C ANISOU 4118 CB LYS B 441 6374 11663 6480 2537 2365 578 C ATOM 4119 CG LYS B 441 84.315 44.262 -2.251 1.00 67.76 C ANISOU 4119 CG LYS B 441 6713 12231 6803 2673 2505 640 C ATOM 4120 CD LYS B 441 83.557 42.941 -2.318 1.00 66.36 C ANISOU 4120 CD LYS B 441 6302 12204 6708 2620 2442 824 C ATOM 4121 CE LYS B 441 82.630 42.782 -1.095 1.00 68.42 C ANISOU 4121 CE LYS B 441 6497 12634 6866 2729 2594 892 C ATOM 4122 NZ LYS B 441 81.599 41.732 -1.337 1.00 66.11 N1+ ANISOU 4122 NZ LYS B 441 5966 12474 6677 2710 2571 1064 N1+ ATOM 4123 N ASN B 442 84.736 47.527 -2.790 1.00 74.24 N ANISOU 4123 N ASN B 442 7974 12685 7548 2928 2751 279 N ATOM 4124 CA ASN B 442 83.780 48.567 -3.170 1.00 66.63 C ANISOU 4124 CA ASN B 442 7042 11670 6603 3164 2878 280 C ATOM 4125 C ASN B 442 84.413 49.935 -3.443 1.00 67.53 C ANISOU 4125 C ASN B 442 7390 11578 6692 3251 2989 115 C ATOM 4126 O ASN B 442 83.734 50.857 -3.890 1.00 69.58 O ANISOU 4126 O ASN B 442 7688 11762 6986 3463 3096 132 O ATOM 4127 CB ASN B 442 82.703 48.708 -2.090 1.00 74.79 C ANISOU 4127 CB ASN B 442 8047 12838 7532 3324 3055 296 C ATOM 4128 CG ASN B 442 81.726 47.545 -2.084 1.00 74.17 C ANISOU 4128 CG ASN B 442 7707 12982 7490 3336 2977 516 C ATOM 4129 OD1 ASN B 442 81.639 46.791 -3.060 1.00 69.01 O ANISOU 4129 OD1 ASN B 442 6896 12374 6950 3257 2805 648 O ATOM 4130 ND2 ASN B 442 80.980 47.397 -0.987 1.00 73.02 N ANISOU 4130 ND2 ASN B 442 7520 12981 7245 3424 3116 543 N ATOM 4131 N LYS B 443 85.709 50.074 -3.187 1.00 69.86 N ANISOU 4131 N LYS B 443 7837 11787 6921 3101 2975 -33 N ATOM 4132 CA LYS B 443 86.403 51.319 -3.516 1.00 73.94 C ANISOU 4132 CA LYS B 443 8578 12094 7422 3160 3081 -200 C ATOM 4133 C LYS B 443 87.063 51.212 -4.893 1.00 73.29 C ANISOU 4133 C LYS B 443 8454 11906 7487 3082 2915 -121 C ATOM 4134 O LYS B 443 87.622 52.178 -5.411 1.00 75.59 O ANISOU 4134 O LYS B 443 8905 12013 7802 3138 2984 -213 O ATOM 4135 CB LYS B 443 87.441 51.666 -2.448 1.00 68.40 C ANISOU 4135 CB LYS B 443 8087 11368 6532 3035 3185 -441 C ATOM 4136 CG LYS B 443 86.868 51.778 -1.024 1.00 78.99 C ANISOU 4136 CG LYS B 443 9492 12835 7683 3095 3358 -544 C ATOM 4137 CD LYS B 443 85.783 52.848 -0.916 1.00 80.36 C ANISOU 4137 CD LYS B 443 9747 12921 7867 3364 3575 -598 C ATOM 4138 CE LYS B 443 84.980 52.713 0.379 1.00 82.41 C ANISOU 4138 CE LYS B 443 9999 13349 7965 3438 3726 -636 C ATOM 4139 NZ LYS B 443 83.742 53.539 0.366 1.00 82.05 N1+ ANISOU 4139 NZ LYS B 443 9963 13248 7965 3724 3916 -616 N1+ ATOM 4140 N ARG B 444 86.988 50.030 -5.489 1.00 73.87 N ANISOU 4140 N ARG B 444 8320 12088 7658 2954 2709 44 N ATOM 4141 CA ARG B 444 87.545 49.819 -6.812 1.00 58.64 C ANISOU 4141 CA ARG B 444 6340 10085 5855 2872 2550 119 C ATOM 4142 C ARG B 444 86.557 50.286 -7.851 1.00 59.60 C ANISOU 4142 C ARG B 444 6390 10198 6057 3063 2551 251 C ATOM 4143 O ARG B 444 85.355 50.174 -7.640 1.00 61.35 O ANISOU 4143 O ARG B 444 6502 10538 6269 3189 2594 342 O ATOM 4144 CB ARG B 444 87.869 48.350 -7.039 1.00 55.59 C ANISOU 4144 CB ARG B 444 5780 9804 5536 2651 2347 214 C ATOM 4145 CG ARG B 444 88.755 47.752 -6.005 1.00 54.87 C ANISOU 4145 CG ARG B 444 5724 9766 5360 2486 2335 144 C ATOM 4146 CD ARG B 444 88.781 46.276 -6.192 1.00 52.60 C ANISOU 4146 CD ARG B 444 5253 9575 5160 2321 2166 271 C ATOM 4147 NE ARG B 444 89.225 45.629 -4.976 1.00 52.84 N ANISOU 4147 NE ARG B 444 5277 9710 5091 2223 2180 263 N ATOM 4148 CZ ARG B 444 89.004 44.353 -4.695 1.00 59.49 C ANISOU 4148 CZ ARG B 444 5960 10675 5969 2140 2095 393 C ATOM 4149 NH1 ARG B 444 88.351 43.584 -5.566 1.00 51.51 N1+ ANISOU 4149 NH1 ARG B 444 4789 9710 5073 2140 1996 520 N1+ ATOM 4150 NH2 ARG B 444 89.432 43.847 -3.540 1.00 57.38 N ANISOU 4150 NH2 ARG B 444 5694 10503 5602 2063 2120 398 N ATOM 4151 N PRO B 445 87.063 50.790 -8.984 1.00 60.19 N ANISOU 4151 N PRO B 445 6515 10156 6198 3088 2506 279 N ATOM 4152 CA PRO B 445 86.206 51.178 -10.105 1.00 59.58 C ANISOU 4152 CA PRO B 445 6358 10107 6172 3268 2487 440 C ATOM 4153 C PRO B 445 85.502 49.968 -10.699 1.00 58.29 C ANISOU 4153 C PRO B 445 5952 10162 6032 3189 2308 591 C ATOM 4154 O PRO B 445 85.928 48.836 -10.483 1.00 58.46 O ANISOU 4154 O PRO B 445 5890 10260 6063 2985 2184 577 O ATOM 4155 CB PRO B 445 87.186 51.780 -11.118 1.00 58.48 C ANISOU 4155 CB PRO B 445 6330 9809 6079 3262 2462 436 C ATOM 4156 CG PRO B 445 88.509 51.906 -10.389 1.00 57.52 C ANISOU 4156 CG PRO B 445 6371 9552 5930 3103 2508 244 C ATOM 4157 CD PRO B 445 88.494 50.879 -9.326 1.00 56.60 C ANISOU 4157 CD PRO B 445 6170 9571 5764 2934 2454 188 C ATOM 4158 N ASP B 446 84.425 50.203 -11.433 1.00 60.07 N ANISOU 4158 N ASP B 446 6069 10513 6244 3377 2309 750 N ATOM 4159 CA ASP B 446 83.791 49.130 -12.181 1.00 64.59 C ANISOU 4159 CA ASP B 446 6413 11321 6806 3313 2147 883 C ATOM 4160 C ASP B 446 84.518 49.078 -13.519 1.00 62.54 C ANISOU 4160 C ASP B 446 6159 11027 6576 3232 2018 910 C ATOM 4161 O ASP B 446 85.336 49.953 -13.806 1.00 63.66 O ANISOU 4161 O ASP B 446 6467 10970 6749 3265 2072 859 O ATOM 4162 CB ASP B 446 82.282 49.363 -12.336 1.00 62.57 C ANISOU 4162 CB ASP B 446 6012 11263 6498 3538 2210 1036 C ATOM 4163 CG ASP B 446 81.954 50.493 -13.285 1.00 81.38 C ANISOU 4163 CG ASP B 446 8439 13618 8864 3772 2274 1151 C ATOM 4164 OD1 ASP B 446 82.027 51.671 -12.873 1.00 82.95 O ANISOU 4164 OD1 ASP B 446 8813 13627 9078 3949 2452 1118 O ATOM 4165 OD2 ASP B 446 81.606 50.197 -14.449 1.00 81.70 O1+ ANISOU 4165 OD2 ASP B 446 8338 13832 8871 3782 2157 1273 O1+ ATOM 4166 N ILE B 447 84.262 48.064 -14.333 1.00 56.48 N ANISOU 4166 N ILE B 447 5216 10445 5800 3117 1861 972 N ATOM 4167 CA ILE B 447 85.081 47.928 -15.520 1.00 54.55 C ANISOU 4167 CA ILE B 447 4988 10167 5573 3015 1744 970 C ATOM 4168 C ILE B 447 84.845 49.092 -16.488 1.00 59.68 C ANISOU 4168 C ILE B 447 5688 10807 6180 3238 1799 1084 C ATOM 4169 O ILE B 447 85.721 49.410 -17.287 1.00 54.88 O ANISOU 4169 O ILE B 447 5167 10094 5592 3202 1762 1077 O ATOM 4170 CB ILE B 447 84.853 46.573 -16.227 1.00 53.53 C ANISOU 4170 CB ILE B 447 4664 10236 5439 2835 1583 977 C ATOM 4171 CG1 ILE B 447 85.757 46.456 -17.460 1.00 61.83 C ANISOU 4171 CG1 ILE B 447 5745 11252 6497 2735 1476 959 C ATOM 4172 CG2 ILE B 447 83.408 46.380 -16.602 1.00 56.10 C ANISOU 4172 CG2 ILE B 447 4788 10836 5692 2952 1576 1088 C ATOM 4173 CD1 ILE B 447 87.273 46.481 -17.148 1.00 49.10 C ANISOU 4173 CD1 ILE B 447 4300 9386 4968 2585 1471 848 C ATOM 4174 N LYS B 448 83.690 49.755 -16.398 1.00 59.23 N ANISOU 4174 N LYS B 448 5582 10855 6068 3481 1903 1203 N ATOM 4175 CA LYS B 448 83.420 50.877 -17.287 1.00 61.21 C ANISOU 4175 CA LYS B 448 5879 11101 6279 3721 1976 1348 C ATOM 4176 C LYS B 448 84.389 52.018 -16.992 1.00 61.04 C ANISOU 4176 C LYS B 448 6112 10746 6333 3788 2119 1278 C ATOM 4177 O LYS B 448 84.886 52.669 -17.907 1.00 61.32 O ANISOU 4177 O LYS B 448 6228 10719 6352 3886 2138 1371 O ATOM 4178 CB LYS B 448 81.968 51.367 -17.166 1.00 72.60 C ANISOU 4178 CB LYS B 448 7211 12721 7653 3987 2081 1507 C ATOM 4179 CG LYS B 448 81.764 52.410 -16.059 1.00 80.90 C ANISOU 4179 CG LYS B 448 8427 13556 8754 4175 2304 1475 C ATOM 4180 CD LYS B 448 80.343 52.965 -15.984 1.00 79.99 C ANISOU 4180 CD LYS B 448 8206 13606 8581 4467 2430 1654 C ATOM 4181 CE LYS B 448 79.469 52.197 -15.002 1.00 81.01 C ANISOU 4181 CE LYS B 448 8186 13904 8689 4426 2434 1624 C ATOM 4182 NZ LYS B 448 78.112 52.816 -14.953 1.00 87.06 N1+ ANISOU 4182 NZ LYS B 448 8846 14829 9405 4728 2572 1809 N1+ ATOM 4183 N LYS B 449 84.672 52.253 -15.716 1.00 61.15 N ANISOU 4183 N LYS B 449 6254 10584 6394 3762 2235 1135 N ATOM 4184 CA LYS B 449 85.551 53.356 -15.353 1.00 61.88 C ANISOU 4184 CA LYS B 449 6595 10391 6525 3853 2403 1060 C ATOM 4185 C LYS B 449 86.994 53.056 -15.738 1.00 67.65 C ANISOU 4185 C LYS B 449 7404 10997 7304 3631 2307 958 C ATOM 4186 O LYS B 449 87.759 53.959 -16.083 1.00 59.39 O ANISOU 4186 O LYS B 449 6528 9751 6287 3715 2411 962 O ATOM 4187 CB LYS B 449 85.468 53.659 -13.860 1.00 63.19 C ANISOU 4187 CB LYS B 449 6875 10437 6695 3873 2560 901 C ATOM 4188 CG LYS B 449 86.224 54.928 -13.471 1.00 74.91 C ANISOU 4188 CG LYS B 449 8635 11618 8208 3992 2774 796 C ATOM 4189 CD LYS B 449 86.195 55.142 -11.973 1.00 80.87 C ANISOU 4189 CD LYS B 449 9508 12288 8932 3979 2925 593 C ATOM 4190 CE LYS B 449 86.745 56.501 -11.550 1.00 83.81 C ANISOU 4190 CE LYS B 449 10175 12347 9322 4120 3178 458 C ATOM 4191 NZ LYS B 449 86.470 56.714 -10.086 1.00 85.82 N1+ ANISOU 4191 NZ LYS B 449 10531 12569 9508 4132 3336 253 N1+ ATOM 4192 N VAL B 450 87.366 51.784 -15.666 1.00 55.85 N ANISOU 4192 N VAL B 450 5788 9604 5828 3353 2127 873 N ATOM 4193 CA VAL B 450 88.695 51.379 -16.086 1.00 58.13 C ANISOU 4193 CA VAL B 450 6121 9800 6164 3141 2028 794 C ATOM 4194 C VAL B 450 88.874 51.653 -17.589 1.00 57.55 C ANISOU 4194 C VAL B 450 6024 9769 6075 3217 1969 939 C ATOM 4195 O VAL B 450 89.949 52.069 -18.027 1.00 56.33 O ANISOU 4195 O VAL B 450 5983 9465 5954 3185 1993 922 O ATOM 4196 CB VAL B 450 88.958 49.883 -15.753 1.00 51.81 C ANISOU 4196 CB VAL B 450 5190 9096 5398 2848 1861 702 C ATOM 4197 CG1 VAL B 450 90.148 49.358 -16.505 1.00 47.60 C ANISOU 4197 CG1 VAL B 450 4662 8510 4914 2655 1743 668 C ATOM 4198 CG2 VAL B 450 89.165 49.706 -14.267 1.00 50.22 C ANISOU 4198 CG2 VAL B 450 5049 8835 5198 2767 1935 570 C ATOM 4199 N GLN B 451 87.819 51.451 -18.374 1.00 54.14 N ANISOU 4199 N GLN B 451 5441 9558 5573 3325 1904 1087 N ATOM 4200 CA GLN B 451 87.888 51.733 -19.806 1.00 54.61 C ANISOU 4200 CA GLN B 451 5465 9714 5571 3424 1856 1243 C ATOM 4201 C GLN B 451 88.141 53.203 -20.085 1.00 56.97 C ANISOU 4201 C GLN B 451 5943 9833 5869 3692 2048 1371 C ATOM 4202 O GLN B 451 88.942 53.559 -20.948 1.00 56.55 O ANISOU 4202 O GLN B 451 5960 9710 5817 3708 2053 1440 O ATOM 4203 CB GLN B 451 86.608 51.308 -20.502 1.00 56.14 C ANISOU 4203 CB GLN B 451 5452 10225 5654 3511 1771 1376 C ATOM 4204 CG GLN B 451 86.473 49.818 -20.672 1.00 54.61 C ANISOU 4204 CG GLN B 451 5080 10228 5441 3263 1586 1282 C ATOM 4205 CD GLN B 451 85.217 49.454 -21.432 1.00 66.14 C ANISOU 4205 CD GLN B 451 6324 12041 6763 3360 1517 1407 C ATOM 4206 OE1 GLN B 451 84.107 49.544 -20.893 1.00 66.85 O ANISOU 4206 OE1 GLN B 451 6325 12256 6819 3485 1574 1469 O ATOM 4207 NE2 GLN B 451 85.378 49.063 -22.701 1.00 61.89 N ANISOU 4207 NE2 GLN B 451 5694 11687 6136 3306 1401 1441 N ATOM 4208 N GLN B 452 87.447 54.053 -19.341 1.00 64.15 N ANISOU 4208 N GLN B 452 6936 10655 6785 3908 2226 1408 N ATOM 4209 CA GLN B 452 87.549 55.495 -19.513 1.00 64.85 C ANISOU 4209 CA GLN B 452 7218 10526 6896 4189 2456 1535 C ATOM 4210 C GLN B 452 88.947 55.991 -19.184 1.00 61.60 C ANISOU 4210 C GLN B 452 7027 9790 6587 4091 2556 1391 C ATOM 4211 O GLN B 452 89.613 56.598 -20.030 1.00 62.04 O ANISOU 4211 O GLN B 452 7182 9724 6665 4169 2623 1505 O ATOM 4212 CB GLN B 452 86.522 56.208 -18.636 1.00 67.07 C ANISOU 4212 CB GLN B 452 7552 10753 7180 4420 2642 1562 C ATOM 4213 CG GLN B 452 86.682 57.713 -18.624 1.00 82.84 C ANISOU 4213 CG GLN B 452 9793 12443 9238 4698 2924 1655 C ATOM 4214 CD GLN B 452 86.028 58.362 -17.416 1.00 90.35 C ANISOU 4214 CD GLN B 452 10859 13243 10225 4852 3132 1565 C ATOM 4215 OE1 GLN B 452 85.078 57.821 -16.834 1.00 87.81 O ANISOU 4215 OE1 GLN B 452 10386 13124 9852 4849 3077 1542 O ATOM 4216 NE2 GLN B 452 86.543 59.527 -17.024 1.00 90.88 N ANISOU 4216 NE2 GLN B 452 11205 12940 10385 4983 3389 1502 N ATOM 4217 N LEU B 453 89.378 55.726 -17.955 1.00 60.48 N ANISOU 4217 N LEU B 453 6955 9530 6493 3922 2578 1148 N ATOM 4218 CA LEU B 453 90.700 56.122 -17.491 1.00 59.70 C ANISOU 4218 CA LEU B 453 7054 9160 6468 3801 2674 973 C ATOM 4219 C LEU B 453 91.794 55.647 -18.450 1.00 63.82 C ANISOU 4219 C LEU B 453 7534 9700 7015 3629 2541 1002 C ATOM 4220 O LEU B 453 92.720 56.406 -18.764 1.00 61.33 O ANISOU 4220 O LEU B 453 7390 9153 6761 3665 2672 1010 O ATOM 4221 CB LEU B 453 90.946 55.581 -16.085 1.00 58.59 C ANISOU 4221 CB LEU B 453 6928 9013 6319 3602 2660 717 C ATOM 4222 CG LEU B 453 90.099 56.240 -14.991 1.00 61.68 C ANISOU 4222 CG LEU B 453 7421 9330 6686 3773 2846 640 C ATOM 4223 CD1 LEU B 453 90.272 55.530 -13.672 1.00 60.53 C ANISOU 4223 CD1 LEU B 453 7251 9258 6492 3566 2805 417 C ATOM 4224 CD2 LEU B 453 90.470 57.702 -14.854 1.00 64.92 C ANISOU 4224 CD2 LEU B 453 8121 9396 7150 3965 3124 597 C ATOM 4225 N LEU B 454 91.665 54.408 -18.934 1.00 54.39 N ANISOU 4225 N LEU B 454 6123 8762 5781 3446 2300 1019 N ATOM 4226 CA LEU B 454 92.605 53.863 -19.905 1.00 52.04 C ANISOU 4226 CA LEU B 454 5768 8507 5499 3286 2168 1046 C ATOM 4227 C LEU B 454 92.510 54.583 -21.252 1.00 61.93 C ANISOU 4227 C LEU B 454 7043 9776 6712 3501 2222 1287 C ATOM 4228 O LEU B 454 93.505 54.672 -21.971 1.00 60.90 O ANISOU 4228 O LEU B 454 6957 9571 6612 3442 2220 1324 O ATOM 4229 CB LEU B 454 92.390 52.355 -20.090 1.00 49.37 C ANISOU 4229 CB LEU B 454 5217 8408 5134 3048 1926 989 C ATOM 4230 CG LEU B 454 93.001 51.470 -18.987 1.00 47.09 C ANISOU 4230 CG LEU B 454 4912 8077 4903 2781 1862 783 C ATOM 4231 CD1 LEU B 454 92.785 49.991 -19.231 1.00 44.86 C ANISOU 4231 CD1 LEU B 454 4448 7970 4626 2564 1660 748 C ATOM 4232 CD2 LEU B 454 94.477 51.770 -18.785 1.00 46.05 C ANISOU 4232 CD2 LEU B 454 4908 7755 4833 2664 1926 686 C ATOM 4233 N GLN B 455 91.330 55.100 -21.594 1.00 56.40 N ANISOU 4233 N GLN B 455 6306 9187 5935 3758 2284 1470 N ATOM 4234 CA GLN B 455 91.153 55.839 -22.852 1.00 65.73 C ANISOU 4234 CA GLN B 455 7505 10418 7052 3999 2358 1744 C ATOM 4235 C GLN B 455 91.778 57.238 -22.766 1.00 67.79 C ANISOU 4235 C GLN B 455 8027 10313 7417 4189 2639 1823 C ATOM 4236 O GLN B 455 92.601 57.614 -23.604 1.00 60.99 O ANISOU 4236 O GLN B 455 7238 9353 6581 4216 2697 1940 O ATOM 4237 CB GLN B 455 89.664 55.941 -23.226 1.00 69.06 C ANISOU 4237 CB GLN B 455 7787 11109 7342 4225 2348 1937 C ATOM 4238 CG GLN B 455 89.118 54.783 -24.089 1.00 71.49 C ANISOU 4238 CG GLN B 455 7840 11820 7504 4108 2101 1970 C ATOM 4239 CD GLN B 455 90.103 53.601 -24.250 1.00 79.48 C ANISOU 4239 CD GLN B 455 8788 12855 8556 3763 1905 1768 C ATOM 4240 OE1 GLN B 455 90.388 52.865 -23.286 1.00 77.47 O ANISOU 4240 OE1 GLN B 455 8526 12513 8397 3528 1836 1543 O ATOM 4241 NE2 GLN B 455 90.611 53.410 -25.482 1.00 70.09 N ANISOU 4241 NE2 GLN B 455 7549 11795 7286 3744 1827 1863 N ATOM 4242 N GLU B 456 91.387 57.995 -21.741 1.00 71.95 N ANISOU 4242 N GLU B 456 8705 10622 8012 4314 2831 1750 N ATOM 4243 CA GLU B 456 91.991 59.297 -21.457 1.00 78.23 C ANISOU 4243 CA GLU B 456 9789 10998 8936 4458 3129 1756 C ATOM 4244 C GLU B 456 93.520 59.239 -21.505 1.00 75.59 C ANISOU 4244 C GLU B 456 9570 10453 8698 4244 3145 1620 C ATOM 4245 O GLU B 456 94.184 60.217 -21.845 1.00 83.17 O ANISOU 4245 O GLU B 456 10739 11097 9765 4350 3371 1709 O ATOM 4246 CB GLU B 456 91.535 59.808 -20.087 1.00 67.64 C ANISOU 4246 CB GLU B 456 8592 9458 7649 4516 3293 1567 C ATOM 4247 CG GLU B 456 90.117 60.368 -20.060 1.00 81.42 C ANISOU 4247 CG GLU B 456 10308 11281 9348 4817 3405 1751 C ATOM 4248 CD GLU B 456 89.478 60.266 -18.682 1.00 84.87 C ANISOU 4248 CD GLU B 456 10761 11704 9780 4796 3444 1532 C ATOM 4249 OE1 GLU B 456 88.228 60.279 -18.606 1.00 84.68 O ANISOU 4249 OE1 GLU B 456 10618 11865 9691 4976 3451 1659 O ATOM 4250 OE2 GLU B 456 90.223 60.166 -17.678 1.00 83.79 O1+ ANISOU 4250 OE2 GLU B 456 10752 11396 9690 4602 3474 1238 O1+ ATOM 4251 N MET B 457 94.069 58.076 -21.183 1.00 73.31 N ANISOU 4251 N MET B 457 9141 10332 8381 3943 2920 1422 N ATOM 4252 CA MET B 457 95.506 57.918 -21.044 1.00 66.41 C ANISOU 4252 CA MET B 457 8351 9294 7587 3719 2931 1268 C ATOM 4253 C MET B 457 96.275 58.070 -22.360 1.00 72.49 C ANISOU 4253 C MET B 457 9115 10041 8385 3740 2940 1470 C ATOM 4254 O MET B 457 97.488 58.288 -22.343 1.00 75.64 O ANISOU 4254 O MET B 457 9632 10227 8881 3618 3038 1397 O ATOM 4255 CB MET B 457 95.801 56.557 -20.421 1.00 54.52 C ANISOU 4255 CB MET B 457 6667 8012 6037 3407 2686 1052 C ATOM 4256 CG MET B 457 97.268 56.289 -20.165 1.00 67.65 C ANISOU 4256 CG MET B 457 8385 9558 7760 3164 2690 893 C ATOM 4257 SD MET B 457 97.542 54.563 -19.711 1.00 63.83 S ANISOU 4257 SD MET B 457 7654 9371 7229 2822 2392 731 S ATOM 4258 CE MET B 457 97.032 53.707 -21.203 1.00 60.82 C ANISOU 4258 CE MET B 457 7051 9255 6803 2822 2165 927 C ATOM 4259 N THR B 458 95.585 57.967 -23.496 1.00 67.16 N ANISOU 4259 N THR B 458 8305 9601 7613 3896 2854 1726 N ATOM 4260 CA THR B 458 96.265 58.004 -24.797 1.00 76.14 C ANISOU 4260 CA THR B 458 9411 10783 8737 3916 2845 1926 C ATOM 4261 C THR B 458 95.847 59.181 -25.686 1.00 71.14 C ANISOU 4261 C THR B 458 8886 10052 8093 4256 3069 2266 C ATOM 4262 O THR B 458 94.775 59.775 -25.506 1.00 80.44 O ANISOU 4262 O THR B 458 10098 11234 9233 4488 3173 2382 O ATOM 4263 CB THR B 458 96.033 56.693 -25.583 1.00 74.23 C ANISOU 4263 CB THR B 458 8900 10955 8349 3765 2533 1931 C ATOM 4264 OG1 THR B 458 94.627 56.460 -25.738 1.00 82.64 O ANISOU 4264 OG1 THR B 458 9830 12298 9274 3902 2436 2021 O ATOM 4265 CG2 THR B 458 96.645 55.527 -24.854 1.00 51.93 C ANISOU 4265 CG2 THR B 458 5982 8179 5569 3421 2346 1638 C TER 4266 THR B 458 HETATM 4267 O4 STU A 501 86.670 21.369 21.331 1.00 53.00 O HETATM 4268 C25 STU A 501 85.639 22.210 22.062 1.00 51.14 C HETATM 4269 C24 STU A 501 85.291 23.404 21.255 1.00 54.15 C HETATM 4270 C23 STU A 501 86.118 23.505 20.045 1.00 51.53 C HETATM 4271 C22 STU A 501 87.570 23.427 20.424 1.00 45.52 C HETATM 4272 C21 STU A 501 87.936 22.047 20.881 1.00 54.37 C HETATM 4273 C26 STU A 501 88.446 21.199 19.705 1.00 44.78 C HETATM 4274 N2 STU A 501 88.876 22.214 21.940 1.00 52.93 N HETATM 4275 C18 STU A 501 88.553 22.457 23.220 1.00 55.63 C HETATM 4276 C19 STU A 501 87.342 22.579 23.825 1.00 55.72 C HETATM 4277 C6 STU A 501 87.280 22.851 25.232 1.00 53.12 C HETATM 4278 C7 STU A 501 88.469 22.993 25.987 1.00 50.13 C HETATM 4279 C10 STU A 501 89.679 22.878 25.345 1.00 51.65 C HETATM 4280 C11 STU A 501 89.738 22.618 23.985 1.00 56.01 C HETATM 4281 C12 STU A 501 90.805 22.453 23.096 1.00 53.71 C HETATM 4282 C17 STU A 501 90.255 22.209 21.824 1.00 55.19 C HETATM 4283 C16 STU A 501 91.140 22.014 20.749 1.00 54.93 C HETATM 4284 C15 STU A 501 92.512 22.079 21.010 1.00 55.61 C HETATM 4285 C14 STU A 501 93.028 22.323 22.263 1.00 56.08 C HETATM 4286 C13 STU A 501 92.191 22.517 23.349 1.00 57.44 C HETATM 4287 C9 STU A 501 90.799 23.080 26.383 1.00 46.58 C HETATM 4288 N1 STU A 501 90.165 23.327 27.643 1.00 44.44 N HETATM 4289 C8 STU A 501 88.759 23.272 27.454 1.00 48.69 C HETATM 4290 O5 STU A 501 87.941 23.431 28.337 1.00 49.00 O HETATM 4291 C5 STU A 501 85.913 22.905 25.541 1.00 52.02 C HETATM 4292 C20 STU A 501 85.198 22.671 24.348 1.00 49.62 C HETATM 4293 C1 STU A 501 83.793 22.659 24.348 1.00 47.75 C HETATM 4294 C2 STU A 501 83.151 22.883 25.559 1.00 45.07 C HETATM 4295 C3 STU A 501 83.848 23.117 26.723 1.00 50.60 C HETATM 4296 C4 STU A 501 85.242 23.131 26.753 1.00 50.85 C HETATM 4297 N3 STU A 501 86.129 22.493 23.343 1.00 53.14 N HETATM 4298 O6 STU A 501 87.744 24.378 21.486 1.00 33.88 O HETATM 4299 C27 STU A 501 88.771 25.352 21.319 1.00 30.57 C HETATM 4300 N4 STU A 501 85.816 24.790 19.432 1.00 61.03 N HETATM 4301 C28 STU A 501 86.315 24.829 18.066 1.00 64.25 C HETATM 4302 O4 STU B 501 96.965 27.240 -23.220 1.00 35.21 O HETATM 4303 C25 STU B 501 97.870 28.314 -23.811 1.00 38.12 C HETATM 4304 C24 STU B 501 98.117 29.385 -22.811 1.00 30.19 C HETATM 4305 C23 STU B 501 97.436 29.046 -21.535 1.00 31.64 C HETATM 4306 C22 STU B 501 95.965 28.941 -21.823 1.00 37.83 C HETATM 4307 C21 STU B 501 95.700 27.684 -22.539 1.00 36.70 C HETATM 4308 C26 STU B 501 95.374 26.579 -21.526 1.00 36.14 C HETATM 4309 N2 STU B 501 94.702 27.941 -23.522 1.00 47.59 N HETATM 4310 C18 STU B 501 94.918 28.403 -24.771 1.00 48.37 C HETATM 4311 C19 STU B 501 96.061 28.748 -25.415 1.00 44.22 C HETATM 4312 C6 STU B 501 96.008 29.224 -26.769 1.00 48.62 C HETATM 4313 C7 STU B 501 94.762 29.358 -27.441 1.00 46.42 C HETATM 4314 C10 STU B 501 93.624 29.013 -26.759 1.00 46.45 C HETATM 4315 C11 STU B 501 93.678 28.549 -25.449 1.00 52.98 C HETATM 4316 C12 STU B 501 92.691 28.136 -24.537 1.00 55.64 C HETATM 4317 C17 STU B 501 93.343 27.768 -23.341 1.00 52.51 C HETATM 4318 C16 STU B 501 92.554 27.319 -22.260 1.00 53.16 C HETATM 4319 C15 STU B 501 91.166 27.255 -22.426 1.00 50.85 C HETATM 4320 C14 STU B 501 90.549 27.614 -23.598 1.00 54.23 C HETATM 4321 C13 STU B 501 91.287 28.065 -24.688 1.00 56.40 C HETATM 4322 C9 STU B 501 92.426 29.231 -27.696 1.00 43.01 C HETATM 4323 N1 STU B 501 92.942 29.729 -28.932 1.00 44.13 N HETATM 4324 C8 STU B 501 94.342 29.822 -28.838 1.00 43.01 C HETATM 4325 O5 STU B 501 95.044 30.210 -29.753 1.00 44.86 O HETATM 4326 C5 STU B 501 97.350 29.470 -27.134 1.00 37.36 C HETATM 4327 C20 STU B 501 98.157 29.148 -26.015 1.00 40.11 C HETATM 4328 C1 STU B 501 99.559 29.299 -26.073 1.00 37.94 C HETATM 4329 C2 STU B 501 100.099 29.772 -27.270 1.00 29.18 C HETATM 4330 C3 STU B 501 99.312 30.100 -28.357 1.00 35.15 C HETATM 4331 C4 STU B 501 97.920 29.954 -28.329 1.00 33.60 C HETATM 4332 N3 STU B 501 97.299 28.733 -25.010 1.00 38.88 N HETATM 4333 O6 STU B 501 95.566 29.985 -22.729 1.00 20.40 O HETATM 4334 C27 STU B 501 94.737 31.022 -22.199 1.00 30.06 C HETATM 4335 N4 STU B 501 97.738 30.095 -20.572 1.00 34.35 N HETATM 4336 C28 STU B 501 97.217 29.813 -19.251 1.00 20.62 C HETATM 4337 S SO4 B 502 88.036 24.140 13.704 1.00 71.51 S HETATM 4338 O1 SO4 B 502 89.031 24.163 12.644 1.00 80.54 O HETATM 4339 O2 SO4 B 502 87.350 25.426 13.786 1.00 81.11 O HETATM 4340 O3 SO4 B 502 87.066 23.075 13.449 1.00 79.62 O HETATM 4341 O4 SO4 B 502 88.734 23.886 14.965 1.00 86.42 O HETATM 4342 S SO4 B 503 101.040 29.243 -19.590 1.00 86.87 S HETATM 4343 O1 SO4 B 503 100.533 29.572 -18.252 1.00 81.65 O HETATM 4344 O2 SO4 B 503 102.454 28.890 -19.487 1.00 85.79 O HETATM 4345 O3 SO4 B 503 100.904 30.411 -20.479 1.00 81.14 O HETATM 4346 O4 SO4 B 503 100.318 28.084 -20.128 1.00 80.78 O HETATM 4347 S SO4 B 504 78.856 41.499 -5.144 1.00112.36 S HETATM 4348 O1 SO4 B 504 77.804 40.509 -4.935 1.00112.61 O HETATM 4349 O2 SO4 B 504 78.478 42.807 -4.610 1.00113.06 O HETATM 4350 O3 SO4 B 504 80.050 41.049 -4.432 1.00112.11 O HETATM 4351 O4 SO4 B 504 79.087 41.627 -6.582 1.00107.46 O HETATM 4352 O HOH A 601 87.467 54.946 33.614 1.00 39.19 O HETATM 4353 O HOH A 602 72.614 43.100 29.903 1.00 41.89 O HETATM 4354 O HOH A 603 70.642 41.768 18.752 1.00 54.45 O HETATM 4355 O HOH A 604 77.995 41.558 34.702 1.00 36.48 O HETATM 4356 O HOH A 605 70.541 35.430 8.956 1.00 51.96 O HETATM 4357 O HOH A 606 71.284 46.406 10.617 1.00 58.45 O HETATM 4358 O HOH A 607 80.374 29.156 36.066 1.00 31.18 O HETATM 4359 O HOH A 608 94.247 48.585 34.438 1.00 53.48 O HETATM 4360 O HOH A 609 104.176 9.582 35.132 0.50 62.08 O HETATM 4361 O HOH A 610 69.573 37.245 18.583 1.00 28.96 O HETATM 4362 O HOH A 611 71.361 32.586 18.216 1.00 34.14 O HETATM 4363 O HOH A 612 104.474 12.205 36.724 1.00 61.86 O HETATM 4364 O HOH A 613 71.647 37.508 11.410 1.00 33.58 O HETATM 4365 O HOH A 614 84.012 38.596 9.282 1.00 31.34 O HETATM 4366 O HOH A 615 75.896 36.666 25.172 1.00 25.90 O HETATM 4367 O HOH A 616 73.256 43.135 15.827 1.00 52.77 O HETATM 4368 O HOH A 617 76.242 34.560 17.630 1.00 31.94 O HETATM 4369 O HOH A 618 77.079 38.123 31.969 1.00 47.49 O HETATM 4370 O HOH A 619 89.154 26.415 34.815 1.00 34.55 O HETATM 4371 O HOH A 620 77.715 55.083 13.922 1.00 56.28 O HETATM 4372 O HOH A 621 71.361 38.059 16.571 1.00 34.20 O HETATM 4373 O HOH A 622 77.716 28.480 30.242 1.00 25.50 O HETATM 4374 O HOH A 623 76.303 33.099 30.387 1.00 33.93 O HETATM 4375 O HOH A 624 92.775 32.680 11.179 1.00 57.30 O HETATM 4376 O HOH A 625 72.566 39.399 17.770 1.00 39.04 O HETATM 4377 O HOH A 626 76.227 30.900 30.578 1.00 41.11 O HETATM 4378 O HOH A 627 90.758 28.579 35.126 1.00 42.22 O HETATM 4379 O HOH A 628 74.886 37.197 22.577 1.00 34.83 O HETATM 4380 O HOH A 629 94.853 37.167 10.531 1.00 42.00 O HETATM 4381 O HOH A 630 98.800 29.851 30.778 1.00 47.02 O HETATM 4382 O HOH A 631 84.010 41.245 1.419 1.00 47.10 O HETATM 4383 O HOH A 632 80.899 40.054 2.843 1.00 55.75 O HETATM 4384 O HOH A 633 102.790 39.924 2.357 1.00 33.93 O HETATM 4385 O HOH A 634 75.399 33.089 27.114 1.00 30.96 O HETATM 4386 O HOH A 635 73.276 36.966 11.237 1.00 27.52 O HETATM 4387 O HOH A 636 89.749 23.987 17.099 1.00 56.78 O HETATM 4388 O HOH A 637 98.317 40.861 31.931 1.00 52.18 O HETATM 4389 O HOH A 638 92.439 32.552 36.076 1.00 51.04 O HETATM 4390 O HOH A 639 97.673 21.232 6.538 1.00 47.10 O HETATM 4391 O HOH A 640 70.893 46.017 17.424 1.00 56.02 O HETATM 4392 O HOH A 641 72.520 30.782 8.690 1.00 55.02 O HETATM 4393 O HOH A 642 88.874 37.709 30.806 1.00 36.67 O HETATM 4394 O HOH A 643 101.097 43.049 18.196 1.00 51.90 O HETATM 4395 O HOH A 644 100.481 23.300 12.264 1.00 59.26 O HETATM 4396 O HOH A 645 72.735 35.711 15.275 1.00 40.58 O HETATM 4397 O HOH A 646 104.609 28.382 -2.605 1.00 59.65 O HETATM 4398 O HOH A 647 74.085 36.111 19.413 1.00 39.24 O HETATM 4399 O HOH A 648 89.066 46.105 7.080 1.00 53.91 O HETATM 4400 O HOH A 649 75.174 54.159 16.663 1.00 52.19 O HETATM 4401 O HOH A 650 93.426 44.823 28.185 1.00 56.05 O HETATM 4402 O HOH A 651 81.832 33.042 14.011 1.00 53.48 O HETATM 4403 O HOH A 652 95.934 30.752 32.875 1.00 61.61 O HETATM 4404 O HOH A 653 105.915 42.448 9.863 1.00 54.86 O HETATM 4405 O HOH A 654 100.995 47.721 12.573 1.00 72.68 O HETATM 4406 O HOH B 601 112.004 51.669 -19.861 1.00 33.82 O HETATM 4407 O HOH B 602 93.946 34.878 -35.060 1.00 53.48 O HETATM 4408 O HOH B 603 114.373 36.618 -9.447 1.00 41.11 O HETATM 4409 O HOH B 604 113.854 41.013 -18.216 1.00 37.13 O HETATM 4410 O HOH B 605 113.557 47.804 -8.694 1.00 53.48 O HETATM 4411 O HOH B 606 107.621 19.660 -34.780 1.00 28.69 O HETATM 4412 O HOH B 607 104.375 39.564 -35.141 1.00 43.18 O HETATM 4413 O HOH B 608 109.877 40.831 -18.948 1.00 28.33 O HETATM 4414 O HOH B 609 107.670 39.539 -27.054 1.00 22.08 O HETATM 4415 O HOH B 610 107.597 38.341 -17.314 1.00 32.50 O HETATM 4416 O HOH B 611 102.161 38.786 -36.074 1.00 23.11 O HETATM 4417 O HOH B 612 108.537 32.183 -7.951 1.00 38.53 O HETATM 4418 O HOH B 613 104.970 39.422 -1.256 1.00 52.58 O HETATM 4419 O HOH B 614 84.696 46.706 -9.577 1.00 40.96 O HETATM 4420 O HOH B 615 100.998 39.621 -7.579 1.00 32.11 O HETATM 4421 O HOH B 616 101.951 36.237 -36.564 1.00 40.73 O HETATM 4422 O HOH B 617 107.172 42.588 -23.882 1.00 29.86 O HETATM 4423 O HOH B 618 105.061 36.019 -31.263 1.00 36.46 O HETATM 4424 O HOH B 619 102.871 36.414 -14.072 1.00 25.29 O HETATM 4425 O HOH B 620 103.098 34.650 -13.048 1.00 56.22 O HETATM 4426 O HOH B 621 90.260 26.205 14.985 1.00 36.02 O HETATM 4427 O HOH B 622 111.009 46.116 -13.599 1.00 36.85 O HETATM 4428 O HOH B 623 108.851 42.947 -21.677 1.00 22.21 O HETATM 4429 O HOH B 624 99.664 34.577 -15.850 1.00 35.65 O HETATM 4430 O HOH B 625 92.176 29.648 -36.112 1.00 62.35 O HETATM 4431 O HOH B 626 83.240 45.246 -10.505 1.00 41.82 O HETATM 4432 O HOH B 627 101.663 32.322 -5.296 1.00 51.50 O HETATM 4433 O HOH B 628 100.165 32.933 -15.283 1.00 44.09 O HETATM 4434 O HOH B 629 87.342 37.710 -31.570 1.00 37.65 O HETATM 4435 O HOH B 630 83.953 30.808 10.781 1.00 50.01 O HETATM 4436 O HOH B 631 84.211 36.639 -29.552 1.00 57.53 O HETATM 4437 O HOH B 632 95.763 62.317 -25.627 1.00 72.25 O HETATM 4438 O HOH B 633 106.886 40.537 -30.301 1.00 39.53 O HETATM 4439 O HOH B 634 106.735 38.583 -31.781 1.00 49.55 O HETATM 4440 O HOH B 635 107.645 39.241 0.270 1.00 54.77 O HETATM 4441 O HOH B 636 111.745 40.051 -15.566 1.00 53.48 O HETATM 4442 O HOH B 637 110.935 38.204 -15.614 1.00 65.54 O HETATM 4443 O HOH B 638 105.983 31.549 -27.478 1.00 53.48 O HETATM 4444 O HOH B 639 104.927 33.600 -2.305 1.00 58.87 O HETATM 4445 O HOH B 640 92.372 42.026 -34.381 1.00 57.45 O HETATM 4446 O HOH B 641 83.248 43.776 -30.804 1.00 53.48 O HETATM 4447 O HOH B 642 98.609 25.844 -19.518 1.00 69.10 O HETATM 4448 O HOH B 643 83.480 42.094 -33.428 1.00 61.53 O CONECT 4267 4268 4272 CONECT 4268 4267 4269 4297 CONECT 4269 4268 4270 CONECT 4270 4269 4271 4300 CONECT 4271 4270 4272 4298 CONECT 4272 4267 4271 4273 4274 CONECT 4273 4272 CONECT 4274 4272 4275 4282 CONECT 4275 4274 4276 4280 CONECT 4276 4275 4277 4297 CONECT 4277 4276 4278 4291 CONECT 4278 4277 4279 4289 CONECT 4279 4278 4280 4287 CONECT 4280 4275 4279 4281 CONECT 4281 4280 4282 4286 CONECT 4282 4274 4281 4283 CONECT 4283 4282 4284 CONECT 4284 4283 4285 CONECT 4285 4284 4286 CONECT 4286 4281 4285 CONECT 4287 4279 4288 CONECT 4288 4287 4289 CONECT 4289 4278 4288 4290 CONECT 4290 4289 CONECT 4291 4277 4292 4296 CONECT 4292 4291 4293 4297 CONECT 4293 4292 4294 CONECT 4294 4293 4295 CONECT 4295 4294 4296 CONECT 4296 4291 4295 CONECT 4297 4268 4276 4292 CONECT 4298 4271 4299 CONECT 4299 4298 CONECT 4300 4270 4301 CONECT 4301 4300 CONECT 4302 4303 4307 CONECT 4303 4302 4304 4332 CONECT 4304 4303 4305 CONECT 4305 4304 4306 4335 CONECT 4306 4305 4307 4333 CONECT 4307 4302 4306 4308 4309 CONECT 4308 4307 CONECT 4309 4307 4310 4317 CONECT 4310 4309 4311 4315 CONECT 4311 4310 4312 4332 CONECT 4312 4311 4313 4326 CONECT 4313 4312 4314 4324 CONECT 4314 4313 4315 4322 CONECT 4315 4310 4314 4316 CONECT 4316 4315 4317 4321 CONECT 4317 4309 4316 4318 CONECT 4318 4317 4319 CONECT 4319 4318 4320 CONECT 4320 4319 4321 CONECT 4321 4316 4320 CONECT 4322 4314 4323 CONECT 4323 4322 4324 CONECT 4324 4313 4323 4325 CONECT 4325 4324 CONECT 4326 4312 4327 4331 CONECT 4327 4326 4328 4332 CONECT 4328 4327 4329 CONECT 4329 4328 4330 CONECT 4330 4329 4331 CONECT 4331 4326 4330 CONECT 4332 4303 4311 4327 CONECT 4333 4306 4334 CONECT 4334 4333 CONECT 4335 4305 4336 CONECT 4336 4335 CONECT 4337 4338 4339 4340 4341 CONECT 4338 4337 CONECT 4339 4337 CONECT 4340 4337 CONECT 4341 4337 CONECT 4342 4343 4344 4345 4346 CONECT 4343 4342 CONECT 4344 4342 CONECT 4345 4342 CONECT 4346 4342 CONECT 4347 4348 4349 4350 4351 CONECT 4348 4347 CONECT 4349 4347 CONECT 4350 4347 CONECT 4351 4347 MASTER 650 0 5 30 16 0 11 6 4446 2 85 48 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4u97
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Interleukin-1 receptor-associated kinase 4 IRAK4 KD-D311N
Ligand Name
Interleukin-1 receptor-associated kinase 4 IRAK4 KD-D311N
EC.Number
E.C.2.7.11.1
Resolution
2.65(Å)
Affinity (Kd/Ki/IC50)
Kd=2.5uM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) Mol.Cell Vol. 55: pp. 891-903
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q9NWZ3
Entrez Gene ID
NCBI Entrez Gene ID:
51135
ASD
Information of known allosteric effects of PDB entries
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times since Nov 2007.
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