Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE 22-SEP-16 5LXM TITLE CRYSTAL STRUCTURE OF AURORA-A BOUND TO A HYDROCARBON-STAPLED TITLE 2 PROTEOMIMETIC OF TPX2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AURORA KINASE A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: AURORA 2,AURORA/IPL1-RELATED KINASE 1,HARK1,BREAST TUMOR- COMPND 5 AMPLIFIED KINASE,SERINE/THREONINE-PROTEIN KINASE 15,SERINE/THREONINE- COMPND 6 PROTEIN KINASE 6,SERINE/THREONINE-PROTEIN KINASE AURORA-A; COMPND 7 EC: 2.7.11.1; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: TARGETING PROTEIN FOR XKLP2; COMPND 12 CHAIN: D; COMPND 13 SYNONYM: DIFFERENTIALLY EXPRESSED IN CANCEROUS AND NON-CANCEROUS LUNG COMPND 14 CELLS 2,DIL-2,HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN 519, COMPND 15 HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN 90,PROTEIN FLS353, COMPND 16 RESTRICTED EXPRESSION PROLIFERATION-ASSOCIATED PROTEIN 100,P100; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606 KEYWDS PROTEIN KINASE, PROTEOMIMETIC, STAPLED HELIX PEPTIDE, MITOSIS, KEYWDS 2 TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR P.J.MCINTYRE,R.BAYLISS REVDAT 4 16-OCT-19 5LXM 1 REMARK REVDAT 3 13-SEP-17 5LXM 1 REMARK REVDAT 2 28-DEC-16 5LXM 1 JRNL REVDAT 1 02-NOV-16 5LXM 0 JRNL AUTH Y.K.RENNIE,P.J.MCINTYRE,T.AKINDELE,R.BAYLISS,A.G.JAMIESON JRNL TITL A TPX2 PROTEOMIMETIC HAS ENHANCED AFFINITY FOR AURORA-A DUE JRNL TITL 2 TO HYDROCARBON STAPLING OF A HELIX. JRNL REF ACS CHEM. BIOL. V. 11 3383 2016 JRNL REFN ESSN 1554-8937 JRNL PMID 27775325 JRNL DOI 10.1021/ACSCHEMBIO.6B00727 REMARK 2 REMARK 2 RESOLUTION. 2.08 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.98 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 31526 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 1602 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.130 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.38 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 126 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.3288 -0.4605 4.9321 REMARK 3 T TENSOR REMARK 3 T11: 1.2402 T22: 1.0177 REMARK 3 T33: 0.4606 T12: 0.4579 REMARK 3 T13: 0.0547 T23: 0.0368 REMARK 3 L TENSOR REMARK 3 L11: 2.5061 L22: 1.4398 REMARK 3 L33: 9.2684 L12: 1.6527 REMARK 3 L13: 0.9430 L23: 0.1678 REMARK 3 S TENSOR REMARK 3 S11: 0.6606 S12: 1.4377 S13: 0.1701 REMARK 3 S21: -1.0330 S22: -0.4275 S23: 0.0909 REMARK 3 S31: -1.5824 S32: 0.2503 S33: -0.1914 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 171 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.4526 -1.9274 6.1031 REMARK 3 T TENSOR REMARK 3 T11: 0.9790 T22: 0.6515 REMARK 3 T33: 0.3662 T12: 0.2053 REMARK 3 T13: 0.1308 T23: 0.0424 REMARK 3 L TENSOR REMARK 3 L11: 7.4140 L22: 4.6060 REMARK 3 L33: 7.2480 L12: -2.2399 REMARK 3 L13: 2.4045 L23: -0.1056 REMARK 3 S TENSOR REMARK 3 S11: 0.1488 S12: 0.7824 S13: 0.3781 REMARK 3 S21: -0.3136 S22: -0.1934 S23: 0.0927 REMARK 3 S31: -1.6278 S32: -0.7413 S33: 0.1519 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.7404 -14.5040 2.2049 REMARK 3 T TENSOR REMARK 3 T11: 0.6390 T22: 0.8040 REMARK 3 T33: 0.3466 T12: 0.1894 REMARK 3 T13: 0.0527 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 4.0051 L22: 4.8779 REMARK 3 L33: 5.6751 L12: -1.0571 REMARK 3 L13: -3.6942 L23: -0.5861 REMARK 3 S TENSOR REMARK 3 S11: 0.4328 S12: 0.8040 S13: 0.0535 REMARK 3 S21: -0.7920 S22: -0.5265 S23: -0.2232 REMARK 3 S31: -0.8537 S32: -0.4889 S33: 0.0919 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.2690 -9.7729 17.1404 REMARK 3 T TENSOR REMARK 3 T11: 0.7123 T22: 0.6470 REMARK 3 T33: 0.3808 T12: 0.1113 REMARK 3 T13: 0.0485 T23: -0.0577 REMARK 3 L TENSOR REMARK 3 L11: 3.0054 L22: 4.1290 REMARK 3 L33: 8.0559 L12: -1.9471 REMARK 3 L13: -2.7790 L23: -2.1541 REMARK 3 S TENSOR REMARK 3 S11: 0.0769 S12: 0.0012 S13: 0.1690 REMARK 3 S21: 0.6573 S22: -0.0872 S23: 0.1588 REMARK 3 S31: -0.8531 S32: 0.1678 S33: 0.0029 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 250 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.1669 -26.6159 16.4901 REMARK 3 T TENSOR REMARK 3 T11: 0.3625 T22: 0.4838 REMARK 3 T33: 0.5146 T12: 0.0189 REMARK 3 T13: 0.0728 T23: -0.1451 REMARK 3 L TENSOR REMARK 3 L11: 6.9728 L22: 4.6476 REMARK 3 L33: 8.8121 L12: 0.1430 REMARK 3 L13: 1.3372 L23: -3.2212 REMARK 3 S TENSOR REMARK 3 S11: -0.0385 S12: 0.8399 S13: -0.8983 REMARK 3 S21: 0.3546 S22: -0.1145 S23: 0.5168 REMARK 3 S31: 0.0636 S32: -1.4266 S33: 0.1226 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 269 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.3099 -19.1357 14.3136 REMARK 3 T TENSOR REMARK 3 T11: 0.5541 T22: 0.5171 REMARK 3 T33: 0.3559 T12: 0.0565 REMARK 3 T13: 0.0611 T23: -0.0425 REMARK 3 L TENSOR REMARK 3 L11: 7.3088 L22: 5.9213 REMARK 3 L33: 8.2372 L12: -6.5604 REMARK 3 L13: -6.3273 L23: 6.5726 REMARK 3 S TENSOR REMARK 3 S11: -0.2356 S12: 0.0219 S13: -0.0580 REMARK 3 S21: 0.4981 S22: 0.1933 S23: -0.0384 REMARK 3 S31: 0.0304 S32: 0.0752 S33: -0.0530 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 270 THROUGH 292 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.8994 -23.3001 6.6908 REMARK 3 T TENSOR REMARK 3 T11: 0.3944 T22: 0.8374 REMARK 3 T33: 0.3070 T12: 0.0421 REMARK 3 T13: -0.0440 T23: -0.1225 REMARK 3 L TENSOR REMARK 3 L11: 5.7880 L22: 3.4650 REMARK 3 L33: 5.0774 L12: -3.2392 REMARK 3 L13: -2.4357 L23: -0.2685 REMARK 3 S TENSOR REMARK 3 S11: 0.3587 S12: 1.1181 S13: -0.1583 REMARK 3 S21: -0.0895 S22: -0.4680 S23: -0.0572 REMARK 3 S31: -0.3247 S32: 0.3108 S33: 0.1401 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 324 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.3319 -26.8770 18.7879 REMARK 3 T TENSOR REMARK 3 T11: 0.5148 T22: 0.5528 REMARK 3 T33: 0.3585 T12: 0.0388 REMARK 3 T13: 0.0385 T23: -0.0334 REMARK 3 L TENSOR REMARK 3 L11: 7.0177 L22: 3.7890 REMARK 3 L33: 2.8578 L12: -1.5462 REMARK 3 L13: -1.3636 L23: -1.6163 REMARK 3 S TENSOR REMARK 3 S11: -0.4241 S12: 0.0854 S13: -0.3772 REMARK 3 S21: 0.4294 S22: -0.0489 S23: 0.0865 REMARK 3 S31: -0.2026 S32: 0.0712 S33: 0.4253 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 343 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.8247 -22.7575 27.3874 REMARK 3 T TENSOR REMARK 3 T11: 0.8344 T22: 0.6983 REMARK 3 T33: 0.4445 T12: 0.0766 REMARK 3 T13: -0.1420 T23: -0.0097 REMARK 3 L TENSOR REMARK 3 L11: 9.6347 L22: 8.2205 REMARK 3 L33: 3.3593 L12: -4.3188 REMARK 3 L13: -3.1339 L23: 0.5506 REMARK 3 S TENSOR REMARK 3 S11: -0.4598 S12: -0.3734 S13: 1.0283 REMARK 3 S21: 1.3912 S22: 0.2501 S23: -1.0344 REMARK 3 S31: -0.1340 S32: 0.8045 S33: 0.2256 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 344 THROUGH 363 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.1755 -32.4961 31.0889 REMARK 3 T TENSOR REMARK 3 T11: 0.9624 T22: 0.6216 REMARK 3 T33: 0.4940 T12: 0.2751 REMARK 3 T13: 0.1735 T23: 0.0748 REMARK 3 L TENSOR REMARK 3 L11: 8.0290 L22: 4.1471 REMARK 3 L33: 6.3059 L12: 2.8623 REMARK 3 L13: -3.6624 L23: -3.1142 REMARK 3 S TENSOR REMARK 3 S11: -0.5826 S12: -1.2020 S13: -0.4722 REMARK 3 S21: 1.0263 S22: 0.2523 S23: 0.2063 REMARK 3 S31: 0.1075 S32: 0.1610 S33: 0.2915 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 392 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.8878 -34.8757 19.7330 REMARK 3 T TENSOR REMARK 3 T11: 0.6314 T22: 0.4023 REMARK 3 T33: 0.6239 T12: -0.0737 REMARK 3 T13: 0.2150 T23: -0.1316 REMARK 3 L TENSOR REMARK 3 L11: 3.2405 L22: 4.1690 REMARK 3 L33: 9.1654 L12: -2.2350 REMARK 3 L13: -3.8145 L23: 0.3629 REMARK 3 S TENSOR REMARK 3 S11: -0.3765 S12: 0.9076 S13: -1.5239 REMARK 3 S21: 0.7212 S22: 0.0093 S23: 0.8896 REMARK 3 S31: 0.8306 S32: -0.9730 S33: 0.4601 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 6 THROUGH 10 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.0643 -8.9193 -5.8914 REMARK 3 T TENSOR REMARK 3 T11: 1.0472 T22: 1.1517 REMARK 3 T33: 0.6666 T12: -0.0178 REMARK 3 T13: 0.3465 T23: -0.0054 REMARK 3 L TENSOR REMARK 3 L11: 2.8199 L22: 6.2261 REMARK 3 L33: 6.5969 L12: -1.4471 REMARK 3 L13: -2.1307 L23: -4.0982 REMARK 3 S TENSOR REMARK 3 S11: 0.8717 S12: 2.7928 S13: -0.4633 REMARK 3 S21: -3.2333 S22: 0.3918 S23: -2.2087 REMARK 3 S31: -2.8133 S32: 0.1009 S33: -1.4791 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 11 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.1666 -11.3314 -3.6083 REMARK 3 T TENSOR REMARK 3 T11: 0.9483 T22: 1.7635 REMARK 3 T33: 0.6268 T12: 0.2431 REMARK 3 T13: -0.0275 T23: -0.2136 REMARK 3 L TENSOR REMARK 3 L11: 2.2457 L22: 6.6810 REMARK 3 L33: 3.2309 L12: -1.3224 REMARK 3 L13: 2.3754 L23: -0.7533 REMARK 3 S TENSOR REMARK 3 S11: 0.0521 S12: 0.6747 S13: -0.0416 REMARK 3 S21: -0.4256 S22: -0.6806 S23: 1.3814 REMARK 3 S31: 0.5661 S32: -0.6815 S33: 0.5041 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 31 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.0302 -26.0654 -6.7796 REMARK 3 T TENSOR REMARK 3 T11: 0.4946 T22: 1.2702 REMARK 3 T33: 0.4645 T12: 0.1410 REMARK 3 T13: -0.0294 T23: -0.2137 REMARK 3 L TENSOR REMARK 3 L11: 6.5902 L22: 8.9596 REMARK 3 L33: 6.8846 L12: -6.5617 REMARK 3 L13: -6.8137 L23: 6.0179 REMARK 3 S TENSOR REMARK 3 S11: 0.4102 S12: -0.6725 S13: -0.7575 REMARK 3 S21: -0.2491 S22: -1.0850 S23: 0.5542 REMARK 3 S31: -0.2808 S32: -1.6172 S33: 0.6534 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 5LXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-16. REMARK 100 THE DEPOSITION ID IS D_1200001525. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-MAR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31554 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080 REMARK 200 RESOLUTION RANGE LOW (A) : 61.980 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 9.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 9.9400 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
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: NULL REMARK 200 STARTING MODEL: 4CEG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS CRYSTALLIZATION SCREEN REMARK 280 CONDITION C1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 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 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 46.75333 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 93.50667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 93.50667 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 46.75333 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: 6020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 13510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 121 REMARK 465 GLU A 122 REMARK 465 SER A 123 REMARK 465 LYS A 124 REMARK 465 LYS A 125 REMARK 465 ALA A 393 REMARK 465 GLN A 394 REMARK 465 ASN A 395 REMARK 465 LYS A 396 REMARK 465 GLU A 397 REMARK 465 SER A 398 REMARK 465 ALA A 399 REMARK 465 SER A 400 REMARK 465 LYS A 401 REMARK 465 GLN A 402 REMARK 465 SER A 403 REMARK 465 ASP D 23 REMARK 465 ASP D 24 REMARK 465 GLU D 25 REMARK 465 GLY D 26 REMARK 465 ASP D 27 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 141 CG CD CE NZ REMARK 470 LYS A 143 CG CD CE NZ REMARK 470 LYS A 156 CG CD CE NZ REMARK 470 GLN A 168 CD OE1 NE2 REMARK 470 LYS A 171 CG CD CE NZ REMARK 470 ARG A 220 CD NE CZ NH1 NH2 REMARK 470 LYS A 227 CG CD CE NZ REMARK 470 LYS A 326 CD CE NZ REMARK 470 LYS A 339 NZ REMARK 470 GLU A 354 CG CD OE1 OE2 REMARK 470 ARG A 375 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 389 CE NZ REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 TYR A 334 CE1 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 OD1 ASN D 30 OG SER D 33 2.14 REMARK 500 OH TYR A 295 OE1 GLU A 321 2.17 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 ASP A 202 35.77 -146.31 REMARK 500 THR A 204 -42.42 -135.11 REMARK 500 SER A 226 -45.50 66.56 REMARK 500 ASP A 256 41.36 -142.20 REMARK 500 ASP A 274 80.97 54.70 REMARK 500 PHE A 275 30.12 -90.80 REMARK 500 SER A 283 55.87 -142.63 REMARK 500 SER A 284 143.77 -171.46 REMARK 500 LEU A 289 96.09 -68.89 REMARK 500 ASP A 307 -153.06 -133.84 REMARK 500 LEU A 364 41.54 -99.58 REMARK 500 SER D 21 -70.65 -72.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 509 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 261 OD1 REMARK 620 2 ASP A 274 OD2 75.1 REMARK 620 3 ADP A 501 O3B 164.4 90.0 REMARK 620 4 ADP A 501 O2A 87.5 82.0 85.9 REMARK 620 5 HOH A 654 O 79.9 154.1 114.3 90.6 REMARK 620 6 HOH A 651 O 93.7 83.5 89.0 164.6 104.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 510 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 274 OD1 REMARK 620 2 ADP A 501 O1B 70.7 REMARK 620 3 PEG A 505 O4 134.9 74.6 REMARK 620 4 HOH A 631 O 73.1 127.7 151.9 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P4G A 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NH3 D 101 DBREF 5LXM A 122 403 UNP O14965 AURKA_HUMAN 122 403 DBREF 5LXM D 6 43 UNP Q9ULW0 TPX2_HUMAN 6 43 SEQADV 5LXM MET A 121 UNP O14965 INITIATING METHIONINE SEQADV 5LXM ALA A 290 UNP O14965 CYS 290 ENGINEERED MUTATION SEQADV 5LXM ALA A 393 UNP O14965 CYS 393 ENGINEERED MUTATION SEQRES 1 A 283 MET GLU SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE SEQRES 2 A 283 GLU ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN SEQRES 3 A 283 VAL TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU SEQRES 4 A 283 ALA LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA SEQRES 5 A 283 GLY VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SEQRES 6 A 283 SER HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY SEQRES 7 A 283 TYR PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU SEQRES 8 A 283 TYR ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS SEQRES 9 A 283 LEU SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE SEQRES 10 A 283 THR GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS SEQRES 11 A 283 ARG VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU SEQRES 12 A 283 LEU GLY SER ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY SEQRES 13 A 283 TRP SER VAL HIS ALA PRO SER SER ARG ARG THR TPO LEU SEQRES 14 A 283 ALA GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU SEQRES 15 A 283 GLY ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU SEQRES 16 A 283 GLY VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO SEQRES 17 A 283 PHE GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE SEQRES 18 A 283 SER ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU SEQRES 19 A 283 GLY ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN SEQRES 20 A 283 PRO SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS SEQRES 21 A 283 PRO TRP ILE THR ALA ASN SER SER LYS PRO SER ASN ALA SEQRES 22 A 283 GLN ASN LYS GLU SER ALA SER LYS GLN SER SEQRES 1 D 38 SER SER TYR SER TYR ASP ALA PRO SER ASP PHE ILE ASN SEQRES 2 D 38 PHE SER SER LEU ASP ASP GLU GLY ASP THR GLN ASN ILE SEQRES 3 D 38 ASP SER TRP PHE GLU MK8 LYS ALA ASN MK8 GLU ASN MODRES 5LXM TPO A 288 THR MODIFIED RESIDUE MODRES 5LXM MK8 D 37 GLU MODIFIED RESIDUE MODRES 5LXM MK8 D 41 LEU MODIFIED RESIDUE HET TPO A 288 11 HET MK8 D 37 9 HET MK8 D 41 9 HET ADP A 501 27 HET PG4 A 502 13 HET SO4 A 503 5 HET PEG A 504 7 HET PEG A 505 7 HET MES A 506 12 HET P4G A 507 11 HET CL A 508 1 HET MG A 509 1 HET MG A 510 1 HET NH3 D 101 1 HETNAM TPO PHOSPHOTHREONINE HETNAM MK8 2-METHYL-L-NORLEUCINE HETNAM ADP ADENOSINE-5'-DIPHOSPHATE HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM SO4 SULFATE ION HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE HETNAM CL CHLORIDE ION HETNAM MG MAGNESIUM ION HETNAM NH3 AMMONIA HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 TPO C4 H10 N O6 P FORMUL 2 MK8 2(C7 H15 N O2) FORMUL 3 ADP C10 H15 N5 O10 P2 FORMUL 4 PG4 C8 H18 O5 FORMUL 5 SO4 O4 S 2- FORMUL 6 PEG 2(C4 H10 O3) FORMUL 8 MES C6 H13 N O4 S FORMUL 9 P4G C8 H18 O3 FORMUL 10 CL CL 1- FORMUL 11 MG 2(MG 2+) FORMUL 13 NH3 H3 N FORMUL 14 HOH *77(H2 O) HELIX 1 AA1 ALA A 129 GLU A 131 5 3 HELIX 2 AA2 LYS A 166 GLY A 173 1 8 HELIX 3 AA3 VAL A 174 HIS A 187 1 14 HELIX 4 AA4 THR A 217 SER A 226 1 10 HELIX 5 AA5 ASP A 229 LYS A 250 1 22 HELIX 6 AA6 LYS A 258 GLU A 260 5 3 HELIX 7 AA7 THR A 292 LEU A 296 5 5 HELIX 8 AA8 PRO A 297 GLU A 302 1 6 HELIX 9 AA9 LYS A 309 GLY A 325 1 17 HELIX 10 AB1 THR A 333 VAL A 344 1 12 HELIX 11 AB2 THR A 353 LEU A 364 1 12 HELIX 12 AB3 ASN A 367 ARG A 371 5 5 HELIX 13 AB4 MET A 373 GLU A 379 1 7 HELIX 14 AB5 HIS A 380 ALA A 385 1 6 HELIX 15 AB6 GLN D 29 ILE D 31 5 3 HELIX 16 AB7 ASP D 32 GLU D 42 1 11 SHEET 1 AA1 5 PHE A 133 LYS A 141 0 SHEET 2 AA1 5 ASN A 146 GLU A 152 -1 O VAL A 147 N LEU A 139 SHEET 3 AA1 5 PHE A 157 PHE A 165 -1 O LEU A 159 N ALA A 150 SHEET 4 AA1 5 ARG A 205 LEU A 210 -1 O VAL A 206 N LEU A 164 SHEET 5 AA1 5 LEU A 196 HIS A 201 -1 N PHE A 200 O TYR A 207 SHEET 1 AA2 2 VAL A 252 ILE A 253 0 SHEET 2 AA2 2 VAL A 279 HIS A 280 -1 O VAL A 279 N ILE A 253 SHEET 1 AA3 2 LEU A 262 LEU A 264 0 SHEET 2 AA3 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263 LINK OD1 ASN A 261 MG MG A 509 1555 1555 2.67 LINK OD1 ASP A 274 MG MG A 510 1555 1555 2.45 LINK OD2 ASP A 274 MG MG A 509 1555 1555 2.39 LINK C THR A 287 N TPO A 288 1555 1555 1.33 LINK C TPO A 288 N LEU A 289 1555 1555 1.33 LINK C GLU D 36 N MK8 D 37 1555 1555 1.33 LINK C MK8 D 37 N LYS D 38 1555 1555 1.33 LINK CE MK8 D 37 CE MK8 D 41 1555 1555 1.33 LINK C ASN D 40 N MK8 D 41 1555 1555 1.33 LINK C MK8 D 41 N GLU D 42 1555 1555 1.33 LINK C ASN D 43 N NH3 D 101 1555 1555 1.33 LINK O1B ADP A 501 MG MG A 510 1555 1555 2.30 LINK O3B ADP A 501 MG MG A 509 1555 1555 2.25 LINK O2A ADP A 501 MG MG A 509 1555 1555 2.00 LINK O4 PEG A 505 MG MG A 510 1555 1555 2.94 LINK MG MG A 509 O HOH A 654 1555 1555 2.23 LINK MG MG A 509 O HOH A 651 1555 1555 2.05 LINK MG MG A 510 O HOH A 631 1555 1555 2.48 SITE 1 AC1 22 LEU A 139 GLY A 140 GLY A 142 LYS A 143 SITE 2 AC1 22 VAL A 147 ALA A 160 LYS A 162 LEU A 194 SITE 3 AC1 22 GLU A 211 ALA A 213 THR A 217 GLU A 260 SITE 4 AC1 22 ASN A 261 LEU A 263 ASP A 274 PEG A 505 SITE 5 AC1 22 MG A 509 MG A 510 HOH A 643 HOH A 651 SITE 6 AC1 22 HOH A 652 HOH A 654 SITE 1 AC2 3 GLU A 221 LYS A 224 GLU A 302 SITE 1 AC3 5 ARG A 220 LYS A 224 ARG A 304 HIS A 366 SITE 2 AC3 5 ASN A 367 SITE 1 AC4 6 SER A 245 HIS A 248 GLU A 308 MET A 373 SITE 2 AC4 6 LEU A 374 ARG A 375 SITE 1 AC5 6 PHE A 144 GLU A 181 GLY A 276 TRP A 277 SITE 2 AC5 6 ADP A 501 MG A 510 SITE 1 AC6 10 ARG A 180 HIS A 280 PRO A 282 ARG A 286 SITE 2 AC6 10 MET A 305 HOH A 612 HOH A 626 LYS D 38 SITE 3 AC6 10 ALA D 39 GLU D 42 SITE 1 AC7 3 LEU A 289 GLY A 291 TYR A 338 SITE 1 AC8 5 ASN A 261 ASP A 274 ADP A 501 HOH A 651 SITE 2 AC8 5 HOH A 654 SITE 1 AC9 5 ASP A 274 GLY A 276 ADP A 501 PEG A 505 SITE 2 AC9 5 HOH A 631 SITE 1 AD1 4 SER A 283 ALA D 39 GLU D 42 ASN D 43 CRYST1 79.780 79.780 140.260 90.00 90.00 120.00 P 31 2 1 6 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 0.012534 0.007237 0.000000 0.00000 SCALE2 0.000000 0.014474 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007130 0.00000 ATOM 1 N ARG A 126 39.244 -0.115 -10.780 1.00115.92 N ANISOU 1 N ARG A 126 18519 18894 6630 6855 -708 905 N ATOM 2 CA ARG A 126 38.884 -1.513 -10.576 1.00114.88 C ANISOU 2 CA ARG A 126 17946 18994 6711 6891 -867 492 C ATOM 3 C ARG A 126 39.740 -2.151 -9.483 1.00108.25 C ANISOU 3 C ARG A 126 16954 18005 6173 6721 -742 257 C ATOM 4 O ARG A 126 39.334 -3.127 -8.853 1.00105.14 O ANISOU 4 O ARG A 126 16265 17626 6059 6761 -891 -39 O ATOM 5 CB ARG A 126 39.028 -2.297 -11.883 1.00115.97 C ANISOU 5 CB ARG A 126 17953 19556 6555 6791 -928 310 C ATOM 6 CG ARG A 126 38.561 -3.739 -11.795 1.00114.01 C ANISOU 6 CG ARG A 126 17330 19501 6486 6800 -1121 -109 C ATOM 7 CD ARG A 126 38.640 -4.442 -13.136 1.00148.51 C ANISOU 7 CD ARG A 126 21635 24256 10537 6703 -1177 -279 C ATOM 8 NE ARG A 126 38.212 -5.834 -13.034 1.00148.26 N ANISOU 8 NE ARG A 126 21326 24340 10667 6664 -1363 -679 N ATOM 9 CZ ARG A 126 36.945 -6.230 -13.075 1.00148.89 C ANISOU 9 CZ ARG A 126 21244 24532 10797 6728 -1621 -743 C ATOM 10 NH1 ARG A 126 35.973 -5.339 -13.218 1.00154.09 N ANISOU 10 NH1 ARG A 126 21941 25236 11372 6903 -1720 -447 N ATOM 11 NH2 ARG A 126 36.648 -7.518 -12.973 1.00143.45 N ANISOU 11 NH2 ARG A 126 20366 23909 10227 6601 -1780 -1100 N ATOM 12 N GLN A 127 40.924 -1.590 -9.263 1.00108.07 N ANISOU 12 N GLN A 127 17138 17849 6075 6489 -472 401 N ATOM 13 CA GLN A 127 41.868 -2.134 -8.294 1.00104.17 C ANISOU 13 CA GLN A 127 16491 17262 5828 6302 -326 202 C ATOM 14 C GLN A 127 41.712 -1.474 -6.927 1.00101.01 C ANISOU 14 C GLN A 127 16226 16444 5711 6319 -275 362 C ATOM 15 O GLN A 127 41.167 -0.376 -6.821 1.00102.58 O ANISOU 15 O GLN A 127 16728 16389 5857 6433 -272 673 O ATOM 16 CB GLN A 127 43.302 -1.958 -8.798 1.00106.11 C ANISOU 16 CB GLN A 127 16810 17688 5819 5978 -36 237 C ATOM 17 CG GLN A 127 44.189 -3.179 -8.614 1.00121.15 C ANISOU 17 CG GLN A 127 18365 19808 7859 5876 27 -158 C ATOM 18 CD GLN A 127 43.815 -4.322 -9.540 1.00105.85 C ANISOU 18 CD GLN A 127 16201 18171 5845 6021 -161 -484 C ATOM 19 OE1 GLN A 127 42.989 -4.165 -10.439 1.00108.61 O ANISOU 19 OE1 GLN A 127 16639 18644 5983 6138 -308 -400 O ATOM 20 NE2 GLN A 127 44.422 -5.481 -9.322 1.00104.48 N ANISOU 20 NE2 GLN A 127 15757 18101 5840 6009 -163 -857 N ATOM 21 N TRP A 128 42.189 -2.148 -5.884 1.00 96.94 N ANISOU 21 N TRP A 128 15502 15839 5490 6212 -240 140 N ATOM 22 CA TRP A 128 42.162 -1.582 -4.539 1.00 94.67 C ANISOU 22 CA TRP A 128 15339 15173 5458 6168 -168 271 C ATOM 23 C TRP A 128 43.011 -0.315 -4.470 1.00 95.70 C ANISOU 23 C TRP A 128 15867 15089 5405 5911 130 629 C ATOM 24 O TRP A 128 44.045 -0.211 -5.130 1.00110.93 O ANISOU 24 O TRP A 128 17839 17228 7083 5640 329 673 O ATOM 25 CB TRP A 128 42.663 -2.593 -3.500 1.00 89.57 C ANISOU 25 CB TRP A 128 14397 14508 5129 6041 -181 -36 C ATOM 26 CG TRP A 128 41.706 -3.707 -3.182 1.00 87.41 C ANISOU 26 CG TRP A 128 13816 14292 5102 6210 -499 -352 C ATOM 27 CD1 TRP A 128 41.896 -5.041 -3.404 1.00 89.89 C ANISOU 27 CD1 TRP A 128 13851 14796 5508 6180 -639 -716 C ATOM 28 CD2 TRP A 128 40.412 -3.583 -2.581 1.00 86.19 C ANISOU 28 CD2 TRP A 128 13615 14006 5128 6387 -712 -336 C ATOM 29 NE1 TRP A 128 40.802 -5.754 -2.978 1.00 85.13 N ANISOU 29 NE1 TRP A 128 13065 14160 5119 6262 -932 -909 N ATOM 30 CE2 TRP A 128 39.874 -4.881 -2.469 1.00 86.06 C ANISOU 30 CE2 TRP A 128 13278 14131 5291 6380 -974 -687 C ATOM 31 CE3 TRP A 128 39.653 -2.499 -2.125 1.00 86.66 C ANISOU 31 CE3 TRP A 128 13871 13841 5213 6542 -699 -70 C ATOM 32 CZ2 TRP A 128 38.617 -5.125 -1.922 1.00 86.73 C ANISOU 32 CZ2 TRP A 128 13190 14204 5561 6450 -1207 -774 C ATOM 33 CZ3 TRP A 128 38.404 -2.743 -1.584 1.00 92.43 C ANISOU 33 CZ3 TRP A 128 14394 14584 6139 6690 -925 -182 C ATOM 34 CH2 TRP A 128 37.899 -4.045 -1.487 1.00 89.82 C ANISOU 34 CH2 TRP A 128 13701 14461 5967 6608 -1169 -527 C ATOM 35 N ALA A 129 42.559 0.647 -3.675 1.00 95.19 N ANISOU 35 N ALA A 129 16099 14613 5455 5965 161 873 N ATOM 36 CA ALA A 129 43.328 1.857 -3.412 1.00100.62 C ANISOU 36 CA ALA A 129 17224 14992 6014 5649 434 1205 C ATOM 37 C ALA A 129 43.239 2.213 -1.931 1.00 93.55 C ANISOU 37 C ALA A 129 16440 13679 5426 5588 502 1253 C ATOM 38 O ALA A 129 42.280 1.842 -1.257 1.00 91.05 O ANISOU 38 O ALA A 129 15953 13273 5368 5887 306 1110 O ATOM 39 CB ALA A 129 42.831 3.006 -4.269 1.00103.33 C ANISOU 39 CB ALA A 129 18010 15167 6085 5766 412 1534 C ATOM 40 N LEU A 130 44.241 2.931 -1.431 1.00 93.86 N ANISOU 40 N LEU A 130 16750 13495 5419 5149 780 1445 N ATOM 41 CA LEU A 130 44.264 3.355 -0.034 1.00 95.46 C ANISOU 41 CA LEU A 130 17108 13276 5887 5008 882 1509 C ATOM 42 C LEU A 130 43.119 4.321 0.253 1.00 98.36 C ANISOU 42 C LEU A 130 17860 13184 6330 5349 778 1691 C ATOM 43 O LEU A 130 42.650 4.429 1.387 1.00 90.29 O ANISOU 43 O LEU A 130 16862 11869 5576 5440 759 1650 O ATOM 44 CB LEU A 130 45.607 4.005 0.309 1.00 92.11 C ANISOU 44 CB LEU A 130 16902 12739 5357 4378 1207 1693 C ATOM 45 CG LEU A 130 45.851 4.372 1.773 1.00 97.71 C ANISOU 45 CG LEU A 130 17741 13050 6334 4099 1352 1741 C ATOM 46 CD1 LEU A 130 45.762 3.138 2.659 1.00 84.21 C ANISOU 46 CD1 LEU A 130 15538 11533 4923 4218 1254 1423 C ATOM 47 CD2 LEU A 130 47.198 5.058 1.937 1.00103.22 C ANISOU 47 CD2 LEU A 130 18619 13718 6882 3393 1655 1929 C ATOM 48 N GLU A 131 42.667 5.009 -0.792 1.00 97.38 N ANISOU 48 N GLU A 131 18019 13023 5959 5552 710 1875 N ATOM 49 CA GLU A 131 41.576 5.968 -0.677 1.00104.18 C ANISOU 49 CA GLU A 131 19237 13489 6857 5944 609 2024 C ATOM 50 C GLU A 131 40.234 5.280 -0.443 1.00 98.23 C ANISOU 50 C GLU A 131 18071 12936 6315 6486 335 1782 C ATOM 51 O GLU A 131 39.252 5.930 -0.096 1.00 99.94 O ANISOU 51 O GLU A 131 18447 12907 6618 6842 260 1820 O ATOM 52 CB GLU A 131 41.492 6.843 -1.935 1.00106.09 C ANISOU 52 CB GLU A 131 19879 13682 6747 6004 590 2282 C ATOM 53 CG GLU A 131 42.668 7.792 -2.134 1.00109.22 C ANISOU 53 CG GLU A 131 20769 13826 6904 5418 840 2559 C ATOM 54 CD GLU A 131 43.891 7.113 -2.725 1.00130.68 C ANISOU 54 CD GLU A 131 23198 17035 9418 4927 973 2503 C ATOM 55 OE1 GLU A 131 43.821 5.902 -3.026 1.00123.10 O ANISOU 55 OE1 GLU A 131 21703 16562 8506 5094 868 2236 O ATOM 56 OE2 GLU A 131 44.925 7.794 -2.892 1.00136.40 O ANISOU 56 OE2 GLU A 131 24214 17689 9921 4359 1179 2704 O ATOM 57 N ASP A 132 40.194 3.966 -0.636 1.00 95.21 N ANISOU 57 N ASP A 132 17143 13029 6003 6515 187 1504 N ATOM 58 CA ASP A 132 38.962 3.208 -0.452 1.00 93.69 C ANISOU 58 CA ASP A 132 16503 13099 5995 6894 -87 1245 C ATOM 59 C ASP A 132 38.671 2.923 1.020 1.00 89.57 C ANISOU 59 C ASP A 132 15800 12418 5814 6866 -108 1090 C ATOM 60 O ASP A 132 37.581 2.467 1.366 1.00 88.68 O ANISOU 60 O ASP A 132 15333 12495 5864 7105 -313 885 O ATOM 61 CB ASP A 132 39.027 1.890 -1.226 1.00 92.54 C ANISOU 61 CB ASP A 132 15891 13477 5793 6865 -254 983 C ATOM 62 CG ASP A 132 39.132 2.097 -2.727 1.00 96.88 C ANISOU 62 CG ASP A 132 16564 14249 5998 6919 -267 1109 C ATOM 63 OD1 ASP A 132 38.636 3.129 -3.222 1.00101.02 O ANISOU 63 OD1 ASP A 132 17426 14602 6357 7125 -265 1357 O ATOM 64 OD2 ASP A 132 39.708 1.224 -3.408 1.00 96.48 O ANISOU 64 OD2 ASP A 132 16283 14540 5834 6756 -285 947 O ATOM 65 N PHE A 133 39.642 3.196 1.885 1.00 87.38 N ANISOU 65 N PHE A 133 15745 11830 5624 6509 112 1184 N ATOM 66 CA PHE A 133 39.515 2.837 3.296 1.00 91.60 C ANISOU 66 CA PHE A 133 16104 12231 6469 6411 93 1046 C ATOM 67 C PHE A 133 39.723 4.010 4.247 1.00 91.55 C ANISOU 67 C PHE A 133 16576 11662 6548 6276 327 1262 C ATOM 68 O PHE A 133 40.650 4.802 4.083 1.00102.10 O ANISOU 68 O PHE A 133 18356 12710 7727 5957 582 1494 O ATOM 69 CB PHE A 133 40.511 1.730 3.650 1.00 80.78 C ANISOU 69 CB PHE A 133 14403 11066 5225 6003 126 840 C ATOM 70 CG PHE A 133 40.362 0.488 2.820 1.00 86.57 C ANISOU 70 CG PHE A 133 14713 12299 5880 6116 -105 572 C ATOM 71 CD1 PHE A 133 39.454 -0.495 3.176 1.00 89.30 C ANISOU 71 CD1 PHE A 133 14618 12865 6449 6245 -403 277 C ATOM 72 CD2 PHE A 133 41.134 0.301 1.684 1.00 91.56 C ANISOU 72 CD2 PHE A 133 15381 13170 6237 6029 -17 594 C ATOM 73 CE1 PHE A 133 39.317 -1.641 2.415 1.00 83.10 C ANISOU 73 CE1 PHE A 133 13508 12476 5591 6289 -613 15 C ATOM 74 CE2 PHE A 133 41.002 -0.842 0.919 1.00 80.79 C ANISOU 74 CE2 PHE A 133 13647 12208 4841 6110 -213 315 C ATOM 75 CZ PHE A 133 40.092 -1.814 1.284 1.00 80.30 C ANISOU 75 CZ PHE A 133 13214 12303 4994 6237 -511 26 C ATOM 76 N GLU A 134 38.851 4.110 5.245 1.00 95.11 N ANISOU 76 N GLU A 134 16911 11976 7252 6460 245 1154 N ATOM 77 CA GLU A 134 39.092 4.984 6.385 1.00 88.83 C ANISOU 77 CA GLU A 134 16495 10654 6601 6268 463 1276 C ATOM 78 C GLU A 134 39.893 4.208 7.420 1.00 78.40 C ANISOU 78 C GLU A 134 14842 9334 5613 5709 548 1101 C ATOM 79 O GLU A 134 39.539 3.081 7.760 1.00 77.91 O ANISOU 79 O GLU A 134 14192 9599 5810 5670 346 805 O ATOM 80 CB GLU A 134 37.781 5.486 6.990 1.00 88.52 C ANISOU 80 CB GLU A 134 16391 10533 6709 6635 378 1154 C ATOM 81 CG GLU A 134 37.074 6.548 6.168 1.00 96.28 C ANISOU 81 CG GLU A 134 17722 11426 7434 7033 382 1278 C ATOM 82 CD GLU A 134 35.841 7.091 6.865 1.00112.97 C ANISOU 82 CD GLU A 134 19772 13526 9626 7365 325 1159 C ATOM 83 OE1 GLU A 134 35.390 6.466 7.848 1.00117.15 O ANISOU 83 OE1 GLU A 134 19856 14243 10411 7283 236 945 O ATOM 84 OE2 GLU A 134 35.325 8.143 6.432 1.00129.54 O ANISOU 84 OE2 GLU A 134 22259 15444 11517 7696 359 1279 O ATOM 85 N ILE A 135 40.975 4.803 7.912 1.00 85.62 N ANISOU 85 N ILE A 135 16106 9897 6530 5203 845 1260 N ATOM 86 CA ILE A 135 41.843 4.124 8.870 1.00 78.75 C ANISOU 86 CA ILE A 135 14882 9056 5984 4608 944 1094 C ATOM 87 C ILE A 135 41.466 4.477 10.304 1.00 71.34 C ANISOU 87 C ILE A 135 13981 7771 5355 4456 1010 1025 C ATOM 88 O ILE A 135 41.367 5.650 10.656 1.00 77.84 O ANISOU 88 O ILE A 135 15373 8138 6066 4481 1191 1222 O ATOM 89 CB ILE A 135 43.326 4.475 8.639 1.00 78.20 C ANISOU 89 CB ILE A 135 15067 8929 5717 4057 1230 1289 C ATOM 90 CG1 ILE A 135 43.702 4.268 7.170 1.00 80.81 C ANISOU 90 CG1 ILE A 135 15413 9620 5673 4209 1200 1370 C ATOM 91 CG2 ILE A 135 44.220 3.642 9.550 1.00 72.42 C ANISOU 91 CG2 ILE A 135 13873 8336 5306 3512 1289 1108 C ATOM 92 CD1 ILE A 135 43.450 2.867 6.670 1.00 76.22 C ANISOU 92 CD1 ILE A 135 14198 9546 5214 4429 937 1061 C ATOM 93 N GLY A 136 41.257 3.455 11.127 1.00 72.03 N ANISOU 93 N GLY A 136 13499 8060 5807 4286 857 742 N ATOM 94 CA GLY A 136 40.894 3.658 12.518 1.00 69.41 C ANISOU 94 CA GLY A 136 13126 7477 5768 4093 906 643 C ATOM 95 C GLY A 136 42.046 3.419 13.474 1.00 82.23 C ANISOU 95 C GLY A 136 14651 8982 7611 3386 1080 631 C ATOM 96 O GLY A 136 43.202 3.687 13.147 1.00 83.16 O ANISOU 96 O GLY A 136 14974 9056 7568 3034 1281 806 O ATOM 97 N ARG A 137 41.725 2.914 14.662 1.00 77.18 N ANISOU 97 N ARG A 137 13676 8341 7309 3156 997 430 N ATOM 98 CA ARG A 137 42.731 2.640 15.679 1.00 71.68 C ANISOU 98 CA ARG A 137 12844 7556 6836 2489 1126 416 C ATOM 99 C ARG A 137 43.602 1.452 15.285 1.00 62.96 C ANISOU 99 C ARG A 137 11300 6815 5808 2282 1000 322 C ATOM 100 O ARG A 137 43.160 0.570 14.548 1.00 64.97 O ANISOU 100 O ARG A 137 11252 7380 6053 2622 745 165 O ATOM 101 CB ARG A 137 42.065 2.368 17.033 1.00 72.39 C ANISOU 101 CB ARG A 137 12685 7577 7245 2310 1038 221 C ATOM 102 CG ARG A 137 41.320 1.042 17.092 1.00 69.89 C ANISOU 102 CG ARG A 137 11779 7644 7131 2452 675 -60 C ATOM 103 CD ARG A 137 40.826 0.734 18.492 1.00 68.37 C ANISOU 103 CD ARG A 137 11333 7419 7225 2134 600 -235 C ATOM 104 NE ARG A 137 40.119 -0.543 18.550 1.00 58.75 N ANISOU 104 NE ARG A 137 9606 6565 6154 2183 237 -488 N ATOM 105 CZ ARG A 137 40.690 -1.698 18.877 1.00 61.01 C ANISOU 105 CZ ARG A 137 9570 6976 6638 1808 53 -598 C ATOM 106 NH1 ARG A 137 41.979 -1.741 19.184 1.00 62.68 N ANISOU 106 NH1 ARG A 137 9837 7043 6936 1400 201 -480 N ATOM 107 NH2 ARG A 137 39.969 -2.810 18.904 1.00 59.07 N ANISOU 107 NH2 ARG A 137 8960 7009 6476 1835 -293 -821 N ATOM 108 N PRO A 138 44.852 1.429 15.771 1.00 77.50 N ANISOU 108 N PRO A 138 13113 8635 7700 1736 1176 413 N ATOM 109 CA PRO A 138 45.715 0.257 15.588 1.00 77.15 C ANISOU 109 CA PRO A 138 12614 8939 7760 1571 1050 296 C ATOM 110 C PRO A 138 45.160 -0.957 16.326 1.00 75.38 C ANISOU 110 C PRO A 138 11933 8818 7890 1554 729 23 C ATOM 111 O PRO A 138 44.818 -0.851 17.503 1.00 68.74 O ANISOU 111 O PRO A 138 11057 7790 7273 1272 721 -19 O ATOM 112 CB PRO A 138 47.052 0.701 16.193 1.00 68.12 C ANISOU 112 CB PRO A 138 11549 7750 6585 963 1327 477 C ATOM 113 CG PRO A 138 47.003 2.195 16.186 1.00 77.89 C ANISOU 113 CG PRO A 138 13404 8628 7562 850 1623 731 C ATOM 114 CD PRO A 138 45.567 2.544 16.416 1.00 73.31 C ANISOU 114 CD PRO A 138 13006 7777 7071 1262 1508 641 C ATOM 115 N LEU A 139 45.063 -2.088 15.637 1.00 73.92 N ANISOU 115 N LEU A 139 11443 8918 7725 1825 465 -165 N ATOM 116 CA LEU A 139 44.574 -3.317 16.249 1.00 68.29 C ANISOU 116 CA LEU A 139 10368 8281 7297 1770 126 -418 C ATOM 117 C LEU A 139 45.717 -4.082 16.905 1.00 76.69 C ANISOU 117 C LEU A 139 11182 9396 8560 1384 91 -450 C ATOM 118 O LEU A 139 45.504 -4.863 17.833 1.00 82.99 O ANISOU 118 O LEU A 139 11767 10140 9626 1149 -134 -586 O ATOM 119 CB LEU A 139 43.874 -4.196 15.211 1.00 75.08 C ANISOU 119 CB LEU A 139 11093 9381 8053 2223 -167 -616 C ATOM 120 CG LEU A 139 42.574 -3.639 14.626 1.00 74.03 C ANISOU 120 CG LEU A 139 11106 9287 7734 2633 -218 -613 C ATOM 121 CD1 LEU A 139 42.031 -4.559 13.543 1.00 63.44 C ANISOU 121 CD1 LEU A 139 9623 8237 6246 3006 -504 -800 C ATOM 122 CD2 LEU A 139 41.543 -3.437 15.727 1.00 65.04 C ANISOU 122 CD2 LEU A 139 9899 8037 6775 2500 -300 -680 C ATOM 123 N GLY A 140 46.932 -3.849 16.417 1.00 66.43 N ANISOU 123 N GLY A 140 9902 8237 7099 1315 305 -316 N ATOM 124 CA GLY A 140 48.109 -4.492 16.969 1.00 59.91 C ANISOU 124 CA GLY A 140 8807 7542 6415 1009 292 -324 C ATOM 125 C GLY A 140 49.376 -4.119 16.227 1.00 67.63 C ANISOU 125 C GLY A 140 9777 8803 7117 989 559 -178 C ATOM 126 O GLY A 140 49.330 -3.669 15.081 1.00 72.17 O ANISOU 126 O GLY A 140 10529 9504 7389 1277 685 -124 O ATOM 127 N LYS A 141 50.514 -4.304 16.887 1.00 68.94 N ANISOU 127 N LYS A 141 9715 9120 7357 626 642 -106 N ATOM 128 CA LYS A 141 51.806 -4.010 16.283 1.00 69.48 C ANISOU 128 CA LYS A 141 9682 9579 7137 542 897 24 C ATOM 129 C LYS A 141 52.433 -5.277 15.715 1.00 81.85 C ANISOU 129 C LYS A 141 10869 11511 8719 915 696 -195 C ATOM 130 O LYS A 141 52.287 -6.360 16.282 1.00 81.94 O ANISOU 130 O LYS A 141 10674 11435 9026 1014 384 -381 O ATOM 131 CB LYS A 141 52.746 -3.365 17.304 1.00 69.41 C ANISOU 131 CB LYS A 141 9626 9617 7131 -99 1133 250 C ATOM 132 N GLY A 142 53.126 -5.136 14.591 1.00 85.70 N ANISOU 132 N GLY A 142 11302 12400 8862 1125 873 -179 N ATOM 133 CA GLY A 142 53.770 -6.265 13.948 1.00 87.23 C ANISOU 133 CA GLY A 142 11157 12976 9013 1544 725 -411 C ATOM 134 C GLY A 142 55.259 -6.046 13.777 1.00 92.99 C ANISOU 134 C GLY A 142 11575 14280 9477 1362 993 -298 C ATOM 135 O GLY A 142 55.799 -5.024 14.202 1.00 92.54 O ANISOU 135 O GLY A 142 11578 14318 9266 828 1284 -23 O ATOM 136 N LYS A 143 55.924 -7.007 13.146 1.00 89.19 N ANISOU 136 N LYS A 143 10765 14211 8910 1801 896 -522 N ATOM 137 CA LYS A 143 57.372 -6.960 12.987 1.00 90.38 C ANISOU 137 CA LYS A 143 10506 15036 8796 1701 1123 -461 C ATOM 138 C LYS A 143 57.800 -6.012 11.871 1.00 98.99 C ANISOU 138 C LYS A 143 11688 16559 9367 1590 1489 -317 C ATOM 139 O LYS A 143 58.947 -5.568 11.833 1.00107.79 O ANISOU 139 O LYS A 143 12523 18256 10176 1272 1762 -169 O ATOM 140 CB LYS A 143 57.921 -8.363 12.716 1.00 85.60 C ANISOU 140 CB LYS A 143 9522 14728 8274 2297 880 -786 C ATOM 141 N PHE A 144 56.877 -5.704 10.965 1.00 95.83 N ANISOU 141 N PHE A 144 11671 15906 8832 1819 1483 -348 N ATOM 142 CA PHE A 144 57.197 -4.877 9.806 1.00 89.04 C ANISOU 142 CA PHE A 144 10954 15423 7455 1747 1787 -216 C ATOM 143 C PHE A 144 56.155 -3.790 9.567 1.00 87.55 C ANISOU 143 C PHE A 144 11362 14728 7175 1565 1863 5 C ATOM 144 O PHE A 144 56.151 -3.141 8.522 1.00 91.27 O ANISOU 144 O PHE A 144 12067 15380 7230 1573 2046 115 O ATOM 145 CB PHE A 144 57.334 -5.749 8.558 1.00 89.56 C ANISOU 145 CB PHE A 144 10829 15886 7315 2374 1705 -526 C ATOM 146 CG PHE A 144 58.379 -6.819 8.679 1.00 93.21 C ANISOU 146 CG PHE A 144 10730 16866 7821 2675 1635 -773 C ATOM 147 CD1 PHE A 144 59.701 -6.554 8.360 1.00 94.02 C ANISOU 147 CD1 PHE A 144 10429 17765 7527 2501 1931 -706 C ATOM 148 CD2 PHE A 144 58.041 -8.090 9.111 1.00 88.38 C ANISOU 148 CD2 PHE A 144 10005 15962 7612 3135 1263 -1070 C ATOM 149 CE1 PHE A 144 60.665 -7.537 8.470 1.00 97.96 C ANISOU 149 CE1 PHE A 144 10378 18793 8050 2863 1862 -945 C ATOM 150 CE2 PHE A 144 59.002 -9.076 9.223 1.00 91.80 C ANISOU 150 CE2 PHE A 144 9975 16827 8077 3490 1176 -1297 C ATOM 151 CZ PHE A 144 60.315 -8.799 8.902 1.00 95.85 C ANISOU 151 CZ PHE A 144 10044 18165 8211 3396 1479 -1241 C ATOM 152 N GLY A 145 55.273 -3.595 10.541 1.00 86.87 N ANISOU 152 N GLY A 145 11522 14027 7459 1419 1717 70 N ATOM 153 CA GLY A 145 54.233 -2.590 10.434 1.00 84.66 C ANISOU 153 CA GLY A 145 11796 13249 7123 1329 1766 259 C ATOM 154 C GLY A 145 53.043 -2.912 11.313 1.00 83.27 C ANISOU 154 C GLY A 145 11737 12497 7404 1449 1486 158 C ATOM 155 O GLY A 145 53.019 -3.941 11.984 1.00 83.22 O ANISOU 155 O GLY A 145 11418 12452 7748 1556 1240 -50 O ATOM 156 N ASN A 146 52.048 -2.033 11.307 1.00 74.17 N ANISOU 156 N ASN A 146 12924 7840 7419 40 1274 127 N ATOM 157 CA ASN A 146 50.887 -2.199 12.172 1.00 67.60 C ANISOU 157 CA ASN A 146 12122 7086 6479 373 1247 23 C ATOM 158 C ASN A 146 49.649 -2.688 11.430 1.00 71.96 C ANISOU 158 C ASN A 146 12463 7957 6922 672 1321 64 C ATOM 159 O ASN A 146 49.530 -2.528 10.213 1.00 64.93 O ANISOU 159 O ASN A 146 11551 7150 5968 717 1367 169 O ATOM 160 CB ASN A 146 50.571 -0.883 12.883 1.00 79.25 C ANISOU 160 CB ASN A 146 14065 8197 7848 566 1172 -17 C ATOM 161 CG ASN A 146 51.667 -0.459 13.840 1.00 99.46 C ANISOU 161 CG ASN A 146 16824 10446 10521 290 1029 -133 C ATOM 162 OD1 ASN A 146 52.802 -0.927 13.749 1.00105.26 O ANISOU 162 OD1 ASN A 146 17360 11206 11427 -88 1002 -124 O ATOM 163 ND2 ASN A 146 51.332 0.430 14.768 1.00104.78 N ANISOU 163 ND2 ASN A 146 17876 10846 11088 510 914 -278 N ATOM 164 N VAL A 147 48.736 -3.297 12.180 1.00 67.99 N ANISOU 164 N VAL A 147 11781 7666 6387 864 1326 -5 N ATOM 165 CA VAL A 147 47.433 -3.693 11.660 1.00 67.72 C ANISOU 165 CA VAL A 147 11510 7943 6277 1143 1365 21 C ATOM 166 C VAL A 147 46.377 -2.733 12.186 1.00 70.43 C ANISOU 166 C VAL A 147 12075 8265 6420 1554 1392 18 C ATOM 167 O VAL A 147 46.234 -2.557 13.396 1.00 71.28 O ANISOU 167 O VAL A 147 12279 8346 6457 1652 1406 -49 O ATOM 168 CB VAL A 147 47.065 -5.135 12.057 1.00 63.36 C ANISOU 168 CB VAL A 147 10519 7680 5876 1038 1356 -11 C ATOM 169 CG1 VAL A 147 45.618 -5.437 11.690 1.00 54.46 C ANISOU 169 CG1 VAL A 147 9118 6875 4700 1300 1374 15 C ATOM 170 CG2 VAL A 147 48.006 -6.121 11.392 1.00 69.09 C ANISOU 170 CG2 VAL A 147 11028 8421 6801 730 1294 -59 C ATOM 171 N TYR A 148 45.642 -2.110 11.274 1.00 71.07 N ANISOU 171 N TYR A 148 12240 8389 6376 1843 1391 80 N ATOM 172 CA TYR A 148 44.685 -1.079 11.649 1.00 69.57 C ANISOU 172 CA TYR A 148 12293 8147 5992 2310 1394 60 C ATOM 173 C TYR A 148 43.245 -1.527 11.441 1.00 74.25 C ANISOU 173 C TYR A 148 12497 9211 6505 2647 1431 62 C ATOM 174 O TYR A 148 42.961 -2.373 10.593 1.00 71.24 O ANISOU 174 O TYR A 148 11750 9109 6209 2537 1405 95 O ATOM 175 CB TYR A 148 44.946 0.200 10.850 1.00 75.86 C ANISOU 175 CB TYR A 148 13559 8557 6707 2441 1328 161 C ATOM 176 CG TYR A 148 46.310 0.810 11.085 1.00 74.47 C ANISOU 176 CG TYR A 148 13762 7886 6646 2082 1277 185 C ATOM 177 CD1 TYR A 148 47.405 0.432 10.317 1.00 82.11 C ANISOU 177 CD1 TYR A 148 14640 8816 7744 1642 1300 304 C ATOM 178 CD2 TYR A 148 46.500 1.771 12.069 1.00 75.10 C ANISOU 178 CD2 TYR A 148 14265 7563 6704 2195 1190 67 C ATOM 179 CE1 TYR A 148 48.653 0.991 10.528 1.00 86.08 C ANISOU 179 CE1 TYR A 148 15411 8915 8382 1275 1256 347 C ATOM 180 CE2 TYR A 148 47.742 2.335 12.286 1.00 69.99 C ANISOU 180 CE2 TYR A 148 13933 6449 6210 1819 1096 75 C ATOM 181 CZ TYR A 148 48.814 1.942 11.516 1.00 74.22 C ANISOU 181 CZ TYR A 148 14318 6979 6905 1336 1138 237 C ATOM 182 OH TYR A 148 50.051 2.505 11.734 1.00 85.74 O ANISOU 182 OH TYR A 148 16015 8019 8544 925 1047 264 O ATOM 183 N LEU A 149 42.340 -0.956 12.229 1.00 77.17 N ANISOU 183 N LEU A 149 12924 9690 6708 3070 1476 0 N ATOM 184 CA LEU A 149 40.914 -1.130 11.999 1.00 74.82 C ANISOU 184 CA LEU A 149 12251 9860 6317 3454 1510 12 C ATOM 185 C LEU A 149 40.523 -0.294 10.785 1.00 72.19 C ANISOU 185 C LEU A 149 12124 9429 5875 3776 1398 67 C ATOM 186 O LEU A 149 40.927 0.862 10.670 1.00 72.73 O ANISOU 186 O LEU A 149 12732 9049 5851 3948 1335 83 O ATOM 187 CB LEU A 149 40.107 -0.721 13.232 1.00 66.00 C ANISOU 187 CB LEU A 149 11113 8956 5007 3867 1620 -76 C ATOM 188 CG LEU A 149 38.603 -0.991 13.177 1.00 73.89 C ANISOU 188 CG LEU A 149 11598 10555 5921 4245 1695 -50 C ATOM 189 CD1 LEU A 149 38.347 -2.461 12.902 1.00 81.05 C ANISOU 189 CD1 LEU A 149 11879 11847 7071 3818 1719 63 C ATOM 190 CD2 LEU A 149 37.936 -0.567 14.471 1.00 80.27 C ANISOU 190 CD2 LEU A 149 12355 11605 6538 4618 1813 -122 C ATOM 191 N ALA A 150 39.745 -0.876 9.880 1.00 74.18 N ANISOU 191 N ALA A 150 11962 10078 6146 3851 1345 105 N ATOM 192 CA ALA A 150 39.478 -0.226 8.601 1.00 70.21 C ANISOU 192 CA ALA A 150 11639 9528 5509 4125 1215 186 C ATOM 193 C ALA A 150 37.997 -0.218 8.230 1.00 78.36 C ANISOU 193 C ALA A 150 12289 11055 6430 4609 1146 158 C ATOM 194 O ALA A 150 37.233 -1.085 8.654 1.00 76.26 O ANISOU 194 O ALA A 150 11457 11251 6268 4565 1191 95 O ATOM 195 CB ALA A 150 40.288 -0.898 7.503 1.00 61.73 C ANISOU 195 CB ALA A 150 10502 8436 4518 3714 1152 244 C ATOM 196 N ARG A 151 37.610 0.770 7.428 1.00 81.07 N ANISOU 196 N ARG A 151 12931 11298 6575 5060 1024 234 N ATOM 197 CA ARG A 151 36.238 0.909 6.954 1.00 81.98 C ANISOU 197 CA ARG A 151 12706 11881 6559 5589 912 207 C ATOM 198 C ARG A 151 36.213 1.187 5.453 1.00 87.76 C ANISOU 198 C ARG A 151 13586 12626 7132 5741 716 330 C ATOM 199 O ARG A 151 36.702 2.222 5.000 1.00 90.93 O ANISOU 199 O ARG A 151 14586 12580 7383 5915 668 496 O ATOM 200 CB ARG A 151 35.526 2.035 7.704 1.00 81.99 C ANISOU 200 CB ARG A 151 12947 11806 6400 6228 940 156 C ATOM 201 CG ARG A 151 34.014 1.908 7.763 1.00106.27 C ANISOU 201 CG ARG A 151 15444 15539 9396 6740 908 70 C ATOM 202 CD ARG A 151 33.482 2.509 9.054 1.00113.58 C ANISOU 202 CD ARG A 151 16404 16535 10215 7191 1061 -59 C ATOM 203 NE ARG A 151 32.408 1.707 9.631 1.00117.38 N ANISOU 203 NE ARG A 151 16081 17753 10765 7175 1158 -99 N ATOM 204 CZ ARG A 151 31.791 1.998 10.772 1.00123.55 C ANISOU 204 CZ ARG A 151 16702 18761 11479 7349 1250 -142 C ATOM 205 NH1 ARG A 151 30.826 1.211 11.227 1.00132.66 N ANISOU 205 NH1 ARG A 151 17094 20615 12696 7290 1371 -122 N ATOM 206 NH2 ARG A 151 32.146 3.073 11.463 1.00122.79 N ANISOU 206 NH2 ARG A 151 17202 18204 11250 7576 1217 -209 N ATOM 207 N GLU A 152 35.655 0.260 4.680 1.00 74.09 N ANISOU 207 N GLU A 152 11321 11400 5430 5664 586 259 N ATOM 208 CA GLU A 152 35.483 0.480 3.247 1.00 84.22 C ANISOU 208 CA GLU A 152 12693 12822 6485 5894 373 344 C ATOM 209 C GLU A 152 34.464 1.594 3.046 1.00 91.83 C ANISOU 209 C GLU A 152 13810 13865 7215 6642 245 420 C ATOM 210 O GLU A 152 33.296 1.442 3.395 1.00 96.62 O ANISOU 210 O GLU A 152 13930 14928 7852 6982 191 287 O ATOM 211 CB GLU A 152 35.037 -0.804 2.543 1.00 76.01 C ANISOU 211 CB GLU A 152 11022 12321 5538 5674 202 166 C ATOM 212 CG GLU A 152 35.265 -0.807 1.031 1.00 84.10 C ANISOU 212 CG GLU A 152 12189 13474 6290 5765 -3 214 C ATOM 213 CD GLU A 152 34.235 0.008 0.269 1.00 94.67 C ANISOU 213 CD GLU A 152 13567 15085 7319 6447 -227 297 C ATOM 214 OE1 GLU A 152 33.030 -0.114 0.573 1.00 97.11 O ANISOU 214 OE1 GLU A 152 13391 15802 7705 6758 -340 163 O ATOM 215 OE2 GLU A 152 34.631 0.775 -0.634 1.00107.91 O ANISOU 215 OE2 GLU A 152 15742 16591 8670 6678 -287 525 O ATOM 216 N LYS A 153 34.917 2.708 2.477 1.00 92.13 N ANISOU 216 N LYS A 153 14511 13462 7032 6895 194 656 N ATOM 217 CA LYS A 153 34.135 3.943 2.441 1.00 98.36 C ANISOU 217 CA LYS A 153 15618 14125 7628 7634 70 755 C ATOM 218 C LYS A 153 32.759 3.812 1.788 1.00102.26 C ANISOU 218 C LYS A 153 15617 15275 7961 8196 -169 669 C ATOM 219 O LYS A 153 31.810 4.477 2.203 1.00110.11 O ANISOU 219 O LYS A 153 16551 16378 8907 8735 -212 586 O ATOM 220 CB LYS A 153 34.929 5.037 1.725 1.00107.86 C ANISOU 220 CB LYS A 153 17623 14713 8646 7716 18 1100 C ATOM 221 CG LYS A 153 36.163 5.497 2.482 1.00100.06 C ANISOU 221 CG LYS A 153 17174 13001 7842 7274 206 1191 C ATOM 222 CD LYS A 153 36.810 6.693 1.805 1.00 97.16 C ANISOU 222 CD LYS A 153 17482 12014 7420 7225 174 1497 C ATOM 223 CE LYS A 153 38.025 7.175 2.579 1.00 93.95 C ANISOU 223 CE LYS A 153 17573 10887 7236 6764 306 1578 C ATOM 224 NZ LYS A 153 38.723 8.285 1.873 1.00101.12 N ANISOU 224 NZ LYS A 153 19022 11222 8176 6555 276 1897 N ATOM 225 N GLN A 154 32.645 2.961 0.774 1.00 94.03 N ANISOU 225 N GLN A 154 14198 14685 6845 8006 -325 628 N ATOM 226 CA GLN A 154 31.388 2.837 0.043 1.00100.59 C ANISOU 226 CA GLN A 154 14553 16151 7516 8513 -614 532 C ATOM 227 C GLN A 154 30.364 1.972 0.778 1.00 97.57 C ANISOU 227 C GLN A 154 13309 16364 7399 8477 -611 244 C ATOM 228 O GLN A 154 29.223 2.388 0.977 1.00102.14 O ANISOU 228 O GLN A 154 13600 17267 7941 8901 -670 150 O ATOM 229 CB GLN A 154 31.640 2.275 -1.360 1.00102.70 C ANISOU 229 CB GLN A 154 14753 16685 7584 8324 -815 541 C ATOM 230 CG GLN A 154 32.399 3.223 -2.279 1.00 99.86 C ANISOU 230 CG GLN A 154 15107 15840 6996 8322 -755 825 C ATOM 231 CD GLN A 154 32.441 2.740 -3.717 1.00116.33 C ANISOU 231 CD GLN A 154 17054 18292 8855 8251 -936 795 C ATOM 232 OE1 GLN A 154 31.857 1.711 -4.057 1.00119.99 O ANISOU 232 OE1 GLN A 154 16918 19347 9325 8219 -1155 507 O ATOM 233 NE2 GLN A 154 33.134 3.485 -4.572 1.00110.74 N ANISOU 233 NE2 GLN A 154 16879 17237 7960 8211 -858 1087 N ATOM 234 N SER A 155 30.772 0.774 1.184 1.00 95.23 N ANISOU 234 N SER A 155 12616 16165 7401 7787 -489 94 N ATOM 235 CA SER A 155 29.850 -0.169 1.813 1.00106.06 C ANISOU 235 CA SER A 155 13138 18092 9068 7624 -485 -110 C ATOM 236 C SER A 155 29.850 -0.075 3.338 1.00109.86 C ANISOU 236 C SER A 155 13553 18452 9738 7530 -143 -101 C ATOM 237 O SER A 155 29.065 -0.755 4.001 1.00110.33 O ANISOU 237 O SER A 155 12912 18989 10018 7412 -72 -191 O ATOM 238 CB SER A 155 30.187 -1.600 1.390 1.00103.38 C ANISOU 238 CB SER A 155 12380 17921 8978 6941 -596 -272 C ATOM 239 OG SER A 155 31.470 -1.979 1.857 1.00 95.42 O ANISOU 239 OG SER A 155 11735 16403 8117 6362 -362 -225 O ATOM 240 N LYS A 156 30.733 0.762 3.880 1.00102.40 N ANISOU 240 N LYS A 156 13326 16887 8696 7569 57 18 N ATOM 241 CA LYS A 156 30.882 0.933 5.327 1.00 93.46 C ANISOU 241 CA LYS A 156 12250 15595 7667 7514 360 -3 C ATOM 242 C LYS A 156 31.206 -0.391 6.019 1.00 93.94 C ANISOU 242 C LYS A 156 11841 15805 8044 6787 529 -53 C ATOM 243 O LYS A 156 30.854 -0.601 7.180 1.00 93.55 O ANISOU 243 O LYS A 156 11491 15969 8084 6759 755 -70 O ATOM 244 CB LYS A 156 29.619 1.555 5.932 1.00 96.99 C ANISOU 244 CB LYS A 156 12392 16462 7997 8165 388 -69 C ATOM 245 N PHE A 157 31.887 -1.275 5.296 1.00 81.82 N ANISOU 245 N PHE A 157 10267 14164 6658 6232 414 -65 N ATOM 246 CA PHE A 157 32.219 -2.601 5.804 1.00 80.42 C ANISOU 246 CA PHE A 157 9679 14060 6818 5548 504 -108 C ATOM 247 C PHE A 157 33.493 -2.570 6.642 1.00 81.15 C ANISOU 247 C PHE A 157 10261 13604 6967 5168 738 -42 C ATOM 248 O PHE A 157 34.528 -2.074 6.197 1.00 83.37 O ANISOU 248 O PHE A 157 11137 13407 7133 5097 723 2 O ATOM 249 CB PHE A 157 32.370 -3.589 4.644 1.00 87.02 C ANISOU 249 CB PHE A 157 10262 15010 7790 5188 227 -221 C ATOM 250 CG PHE A 157 32.443 -5.028 5.074 1.00 91.58 C ANISOU 250 CG PHE A 157 10331 15688 8776 4545 230 -285 C ATOM 251 CD1 PHE A 157 31.303 -5.698 5.488 1.00 98.34 C ANISOU 251 CD1 PHE A 157 10436 17046 9880 4461 196 -294 C ATOM 252 CD2 PHE A 157 33.646 -5.714 5.049 1.00 84.80 C ANISOU 252 CD2 PHE A 157 9728 14418 8073 4026 255 -317 C ATOM 253 CE1 PHE A 157 31.364 -7.022 5.879 1.00 97.79 C ANISOU 253 CE1 PHE A 157 9930 16995 10231 3833 175 -300 C ATOM 254 CE2 PHE A 157 33.712 -7.040 5.439 1.00 77.02 C ANISOU 254 CE2 PHE A 157 8322 13452 7489 3467 218 -364 C ATOM 255 CZ PHE A 157 32.570 -7.694 5.854 1.00 86.49 C ANISOU 255 CZ PHE A 157 8823 15081 8957 3352 172 -339 C ATOM 256 N ILE A 158 33.406 -3.107 7.856 1.00 75.79 N ANISOU 256 N ILE A 158 9301 13037 6458 4917 951 -11 N ATOM 257 CA ILE A 158 34.524 -3.092 8.794 1.00 72.02 C ANISOU 257 CA ILE A 158 9237 12113 6015 4602 1152 37 C ATOM 258 C ILE A 158 35.561 -4.159 8.471 1.00 66.33 C ANISOU 258 C ILE A 158 8522 11132 5548 3953 1086 25 C ATOM 259 O ILE A 158 35.241 -5.345 8.385 1.00 66.79 O ANISOU 259 O ILE A 158 8062 11433 5882 3591 1007 7 O ATOM 260 CB ILE A 158 34.049 -3.299 10.244 1.00 71.20 C ANISOU 260 CB ILE A 158 8836 12286 5930 4614 1408 97 C ATOM 261 CG1 ILE A 158 33.244 -2.092 10.719 1.00105.58 C ANISOU 261 CG1 ILE A 158 13311 16832 9975 5338 1507 54 C ATOM 262 CG2 ILE A 158 35.240 -3.491 11.158 1.00 67.62 C ANISOU 262 CG2 ILE A 158 8756 11414 5522 4231 1558 134 C ATOM 263 CD1 ILE A 158 34.077 -0.838 10.875 1.00110.25 C ANISOU 263 CD1 ILE A 158 14731 16817 10342 5625 1504 -11 C ATOM 264 N LEU A 159 36.808 -3.731 8.308 1.00 66.06 N ANISOU 264 N LEU A 159 9065 10592 5441 3810 1104 31 N ATOM 265 CA LEU A 159 37.894 -4.645 7.984 1.00 62.16 C ANISOU 265 CA LEU A 159 8604 9862 5151 3274 1049 -4 C ATOM 266 C LEU A 159 39.126 -4.393 8.847 1.00 57.32 C ANISOU 266 C LEU A 159 8421 8808 4550 3031 1202 42 C ATOM 267 O LEU A 159 39.159 -3.463 9.652 1.00 63.08 O ANISOU 267 O LEU A 159 9471 9377 5120 3270 1323 78 O ATOM 268 CB LEU A 159 38.265 -4.525 6.501 1.00 70.25 C ANISOU 268 CB LEU A 159 9800 10831 6062 3317 866 -59 C ATOM 269 CG LEU A 159 37.205 -4.954 5.485 1.00 77.16 C ANISOU 269 CG LEU A 159 10242 12150 6927 3505 632 -163 C ATOM 270 CD1 LEU A 159 37.461 -4.321 4.125 1.00 67.76 C ANISOU 270 CD1 LEU A 159 9376 10935 5435 3766 493 -158 C ATOM 271 CD2 LEU A 159 37.182 -6.468 5.371 1.00 86.30 C ANISOU 271 CD2 LEU A 159 10915 13448 8427 3056 490 -310 C ATOM 272 N ALA A 160 40.133 -5.242 8.677 1.00 59.87 N ANISOU 272 N ALA A 160 8737 8946 5064 2580 1162 5 N ATOM 273 CA ALA A 160 41.435 -5.024 9.289 1.00 60.64 C ANISOU 273 CA ALA A 160 9216 8644 5182 2330 1256 31 C ATOM 274 C ALA A 160 42.470 -4.836 8.188 1.00 69.08 C ANISOU 274 C ALA A 160 10547 9497 6202 2195 1190 11 C ATOM 275 O ALA A 160 42.543 -5.635 7.253 1.00 62.68 O ANISOU 275 O ALA A 160 9503 8846 5469 2072 1072 -78 O ATOM 276 CB ALA A 160 41.812 -6.186 10.196 1.00 59.47 C ANISOU 276 CB ALA A 160 8812 8495 5291 1941 1288 34 C ATOM 277 N LEU A 161 43.258 -3.771 8.290 1.00 71.61 N ANISOU 277 N LEU A 161 11345 9473 6392 2223 1258 92 N ATOM 278 CA LEU A 161 44.246 -3.462 7.264 1.00 62.36 C ANISOU 278 CA LEU A 161 10409 8141 5145 2084 1247 152 C ATOM 279 C LEU A 161 45.664 -3.653 7.790 1.00 72.93 C ANISOU 279 C LEU A 161 11873 9204 6634 1675 1309 147 C ATOM 280 O LEU A 161 46.128 -2.903 8.650 1.00 72.26 O ANISOU 280 O LEU A 161 12094 8803 6557 1623 1355 190 O ATOM 281 CB LEU A 161 44.057 -2.031 6.751 1.00 61.31 C ANISOU 281 CB LEU A 161 10714 7812 4770 2397 1253 318 C ATOM 282 CG LEU A 161 44.807 -1.664 5.470 1.00 73.39 C ANISOU 282 CG LEU A 161 12443 9294 6149 2314 1262 475 C ATOM 283 CD1 LEU A 161 44.454 -2.629 4.349 1.00 74.03 C ANISOU 283 CD1 LEU A 161 12150 9830 6148 2365 1175 368 C ATOM 284 CD2 LEU A 161 44.498 -0.232 5.056 1.00 72.03 C ANISOU 284 CD2 LEU A 161 12737 8870 5763 2636 1247 707 C ATOM 285 N LYS A 162 46.344 -4.667 7.266 1.00 71.87 N ANISOU 285 N LYS A 162 11489 9200 6619 1415 1279 57 N ATOM 286 CA LYS A 162 47.713 -4.962 7.663 1.00 61.53 C ANISOU 286 CA LYS A 162 10215 7706 5459 1057 1319 35 C ATOM 287 C LYS A 162 48.697 -4.212 6.773 1.00 67.71 C ANISOU 287 C LYS A 162 11227 8392 6108 951 1399 171 C ATOM 288 O LYS A 162 48.778 -4.458 5.568 1.00 64.38 O ANISOU 288 O LYS A 162 10698 8219 5546 1011 1407 175 O ATOM 289 CB LYS A 162 47.972 -6.468 7.608 1.00 66.96 C ANISOU 289 CB LYS A 162 10510 8571 6362 877 1234 -144 C ATOM 290 CG LYS A 162 49.336 -6.893 8.125 1.00 61.81 C ANISOU 290 CG LYS A 162 9839 7764 5882 564 1247 -189 C ATOM 291 CD LYS A 162 49.416 -8.405 8.243 1.00 65.61 C ANISOU 291 CD LYS A 162 9971 8345 6610 455 1118 -365 C ATOM 292 CE LYS A 162 50.766 -8.852 8.773 1.00 67.51 C ANISOU 292 CE LYS A 162 10176 8454 7019 209 1104 -417 C ATOM 293 NZ LYS A 162 50.816 -10.331 8.965 1.00 58.38 N ANISOU 293 NZ LYS A 162 8733 7314 6135 141 941 -572 N ATOM 294 N VAL A 163 49.437 -3.289 7.378 1.00 70.64 N ANISOU 294 N VAL A 163 11909 8418 6513 786 1451 289 N ATOM 295 CA VAL A 163 50.367 -2.442 6.644 1.00 73.85 C ANISOU 295 CA VAL A 163 12539 8687 6836 613 1540 499 C ATOM 296 C VAL A 163 51.810 -2.886 6.859 1.00 79.31 C ANISOU 296 C VAL A 163 13061 9369 7704 210 1584 459 C ATOM 297 O VAL A 163 52.272 -2.988 7.995 1.00 89.31 O ANISOU 297 O VAL A 163 14336 10434 9162 31 1519 357 O ATOM 298 CB VAL A 163 50.229 -0.968 7.063 1.00 75.21 C ANISOU 298 CB VAL A 163 13198 8408 6971 674 1524 679 C ATOM 299 CG1 VAL A 163 51.217 -0.103 6.295 1.00 75.74 C ANISOU 299 CG1 VAL A 163 13483 8293 7004 410 1614 972 C ATOM 300 CG2 VAL A 163 48.802 -0.488 6.847 1.00 79.19 C ANISOU 300 CG2 VAL A 163 13856 8945 7289 1148 1471 708 C ATOM 301 N LEU A 164 52.515 -3.146 5.763 1.00 67.27 N ANISOU 301 N LEU A 164 11363 8113 6082 104 1690 533 N ATOM 302 CA LEU A 164 53.909 -3.573 5.824 1.00 76.00 C ANISOU 302 CA LEU A 164 12235 9307 7334 -234 1751 496 C ATOM 303 C LEU A 164 54.802 -2.666 4.987 1.00 81.08 C ANISOU 303 C LEU A 164 12978 9967 7862 -462 1927 815 C ATOM 304 O LEU A 164 54.558 -2.474 3.799 1.00 81.32 O ANISOU 304 O LEU A 164 13027 10260 7611 -305 2044 984 O ATOM 305 CB LEU A 164 54.050 -5.016 5.341 1.00 75.48 C ANISOU 305 CB LEU A 164 11751 9652 7278 -134 1725 230 C ATOM 306 CG LEU A 164 53.133 -6.058 5.976 1.00 71.61 C ANISOU 306 CG LEU A 164 11116 9162 6930 49 1547 -31 C ATOM 307 CD1 LEU A 164 53.397 -7.418 5.364 1.00 66.00 C ANISOU 307 CD1 LEU A 164 10043 8769 6267 128 1479 -298 C ATOM 308 CD2 LEU A 164 53.329 -6.099 7.482 1.00 80.00 C ANISOU 308 CD2 LEU A 164 12241 9920 8237 -114 1456 -74 C ATOM 309 N PHE A 165 55.841 -2.117 5.609 1.00 90.66 N ANISOU 309 N PHE A 165 14238 10922 9285 -846 1937 915 N ATOM 310 CA PHE A 165 56.788 -1.263 4.900 1.00 88.96 C ANISOU 310 CA PHE A 165 14060 10711 9029 -1167 2112 1272 C ATOM 311 C PHE A 165 57.737 -2.100 4.048 1.00 94.02 C ANISOU 311 C PHE A 165 14217 11935 9571 -1250 2296 1243 C ATOM 312 O PHE A 165 58.352 -3.047 4.538 1.00101.98 O ANISOU 312 O PHE A 165 14878 13119 10752 -1308 2235 956 O ATOM 313 CB PHE A 165 57.579 -0.403 5.886 1.00 92.86 C ANISOU 313 CB PHE A 165 14729 10720 9835 -1591 2012 1358 C ATOM 314 CG PHE A 165 56.721 0.506 6.718 1.00105.79 C ANISOU 314 CG PHE A 165 16876 11776 11542 -1464 1819 1344 C ATOM 315 CD1 PHE A 165 56.403 1.779 6.274 1.00111.95 C ANISOU 315 CD1 PHE A 165 18100 12174 12262 -1481 1833 1682 C ATOM 316 CD2 PHE A 165 56.230 0.087 7.944 1.00101.78 C ANISOU 316 CD2 PHE A 165 16415 11117 11139 -1293 1624 1002 C ATOM 317 CE1 PHE A 165 55.614 2.618 7.038 1.00115.07 C ANISOU 317 CE1 PHE A 165 18978 12027 12715 -1287 1633 1616 C ATOM 318 CE2 PHE A 165 55.439 0.921 8.712 1.00109.64 C ANISOU 318 CE2 PHE A 165 17862 11652 12145 -1107 1464 950 C ATOM 319 CZ PHE A 165 55.130 2.188 8.258 1.00112.53 C ANISOU 319 CZ PHE A 165 18670 11622 12464 -1082 1457 1225 C ATOM 320 N LYS A 166 57.850 -1.745 2.772 1.00 96.54 N ANISOU 320 N LYS A 166 14523 12575 9582 -1212 2519 1545 N ATOM 321 CA LYS A 166 58.680 -2.495 1.836 1.00 92.78 C ANISOU 321 CA LYS A 166 13591 12751 8910 -1197 2728 1509 C ATOM 322 C LYS A 166 60.159 -2.425 2.196 1.00 95.53 C ANISOU 322 C LYS A 166 13604 13186 9508 -1658 2834 1589 C ATOM 323 O LYS A 166 60.911 -3.364 1.940 1.00 98.34 O ANISOU 323 O LYS A 166 13493 14033 9839 -1603 2915 1363 O ATOM 324 CB LYS A 166 58.468 -1.985 0.410 1.00100.03 C ANISOU 324 CB LYS A 166 14606 14031 9370 -1048 2965 1879 C ATOM 325 CG LYS A 166 57.050 -2.164 -0.099 1.00 95.85 C ANISOU 325 CG LYS A 166 14322 13546 8551 -545 2838 1763 C ATOM 326 CD LYS A 166 56.940 -1.799 -1.567 1.00 93.55 C ANISOU 326 CD LYS A 166 14083 13726 7734 -346 3057 2101 C ATOM 327 CE LYS A 166 55.539 -2.067 -2.088 1.00 90.46 C ANISOU 327 CE LYS A 166 13876 13441 7052 182 2877 1925 C ATOM 328 NZ LYS A 166 55.447 -1.859 -3.555 1.00 85.88 N ANISOU 328 NZ LYS A 166 13227 13346 6056 362 2930 2098 N ATOM 329 N ALA A 167 60.570 -1.310 2.791 1.00 95.30 N ANISOU 329 N ALA A 167 13802 12672 9734 -2094 2804 1884 N ATOM 330 CA ALA A 167 61.962 -1.118 3.179 1.00 93.70 C ANISOU 330 CA ALA A 167 13264 12521 9817 -2596 2863 1981 C ATOM 331 C ALA A 167 62.396 -2.138 4.231 1.00 88.08 C ANISOU 331 C ALA A 167 12243 11842 9383 -2560 2644 1496 C ATOM 332 O ALA A 167 63.476 -2.719 4.133 1.00 93.17 O ANISOU 332 O ALA A 167 12377 12921 10103 -2688 2736 1401 O ATOM 333 CB ALA A 167 62.177 0.297 3.692 1.00 91.23 C ANISOU 333 CB ALA A 167 13323 11562 9776 -3074 2779 2340 C ATOM 334 N GLN A 168 61.548 -2.358 5.231 1.00 83.59 N ANISOU 334 N GLN A 168 11971 10846 8944 -2358 2362 1211 N ATOM 335 CA GLN A 168 61.858 -3.302 6.301 1.00 81.26 C ANISOU 335 CA GLN A 168 11453 10536 8884 -2302 2134 810 C ATOM 336 C GLN A 168 61.836 -4.745 5.803 1.00 80.90 C ANISOU 336 C GLN A 168 11035 10994 8711 -1920 2169 502 C ATOM 337 O GLN A 168 62.668 -5.561 6.200 1.00 82.96 O ANISOU 337 O GLN A 168 10918 11465 9139 -1936 2088 270 O ATOM 338 CB GLN A 168 60.878 -3.135 7.465 1.00 78.64 C ANISOU 338 CB GLN A 168 11548 9676 8657 -2162 1864 644 C ATOM 339 CG GLN A 168 60.959 -1.783 8.157 1.00 86.14 C ANISOU 339 CG GLN A 168 12894 10066 9770 -2485 1743 822 C ATOM 340 N LEU A 169 60.880 -5.052 4.932 1.00 79.31 N ANISOU 340 N LEU A 169 10949 10962 8221 -1558 2249 479 N ATOM 341 CA LEU A 169 60.745 -6.391 4.370 1.00 83.95 C ANISOU 341 CA LEU A 169 11243 11963 8690 -1173 2231 145 C ATOM 342 C LEU A 169 61.945 -6.777 3.512 1.00 90.68 C ANISOU 342 C LEU A 169 11616 13415 9421 -1188 2448 127 C ATOM 343 O LEU A 169 62.486 -7.875 3.641 1.00 96.11 O ANISOU 343 O LEU A 169 11960 14342 10217 -1009 2354 -212 O ATOM 344 CB LEU A 169 59.467 -6.490 3.538 1.00 94.03 C ANISOU 344 CB LEU A 169 12748 13311 9669 -811 2243 128 C ATOM 345 CG LEU A 169 58.153 -6.398 4.311 1.00 90.29 C ANISOU 345 CG LEU A 169 12632 12380 9295 -685 2029 70 C ATOM 346 CD1 LEU A 169 56.983 -6.299 3.349 1.00 90.14 C ANISOU 346 CD1 LEU A 169 12786 12498 8964 -361 2055 106 C ATOM 347 CD2 LEU A 169 57.996 -7.596 5.233 1.00 91.30 C ANISOU 347 CD2 LEU A 169 12612 12382 9695 -577 1784 -279 C ATOM 348 N GLU A 170 62.354 -5.868 2.633 1.00 95.39 N ANISOU 348 N GLU A 170 12192 14268 9785 -1379 2743 512 N ATOM 349 CA GLU A 170 63.464 -6.128 1.724 1.00 93.04 C ANISOU 349 CA GLU A 170 11404 14653 9293 -1384 3023 560 C ATOM 350 C GLU A 170 64.801 -6.141 2.457 1.00 98.41 C ANISOU 350 C GLU A 170 11678 15398 10315 -1745 3012 550 C ATOM 351 O GLU A 170 65.736 -6.824 2.042 1.00112.91 O ANISOU 351 O GLU A 170 12999 17811 12091 -1623 3140 383 O ATOM 352 CB GLU A 170 63.486 -5.089 0.602 1.00 97.55 C ANISOU 352 CB GLU A 170 12077 15493 9496 -1526 3367 1075 C ATOM 353 CG GLU A 170 62.283 -5.166 -0.321 1.00102.57 C ANISOU 353 CG GLU A 170 13028 16235 9708 -1091 3382 1064 C ATOM 354 CD GLU A 170 62.190 -3.984 -1.262 1.00111.92 C ANISOU 354 CD GLU A 170 14431 17551 10544 -1247 3674 1661 C ATOM 355 OE1 GLU A 170 63.117 -3.147 -1.263 1.00127.81 O ANISOU 355 OE1 GLU A 170 16315 19589 12658 -1730 3894 2105 O ATOM 356 OE2 GLU A 170 61.185 -3.890 -1.997 1.00112.04 O ANISOU 356 OE2 GLU A 170 14741 17633 10195 -900 3664 1708 O ATOM 357 N LYS A 171 64.886 -5.385 3.546 1.00 99.13 N ANISOU 357 N LYS A 171 11990 14922 10751 -2153 2838 696 N ATOM 358 CA LYS A 171 66.100 -5.350 4.352 1.00102.54 C ANISOU 358 CA LYS A 171 12053 15373 11534 -2514 2751 661 C ATOM 359 C LYS A 171 66.302 -6.676 5.075 1.00 97.16 C ANISOU 359 C LYS A 171 11135 14751 11032 -2187 2480 160 C ATOM 360 O LYS A 171 67.410 -7.210 5.118 1.00102.96 O ANISOU 360 O LYS A 171 11342 15899 11878 -2197 2499 15 O ATOM 361 CB LYS A 171 66.048 -4.200 5.360 1.00100.53 C ANISOU 361 CB LYS A 171 12163 14451 11585 -2993 2562 878 C ATOM 362 N ALA A 172 65.220 -7.205 5.639 1.00 96.41 N ANISOU 362 N ALA A 172 10797 12865 12971 -3219 2640 1579 N ATOM 363 CA ALA A 172 65.266 -8.476 6.350 1.00 89.71 C ANISOU 363 CA ALA A 172 9480 12507 12098 -3078 2205 1609 C ATOM 364 C ALA A 172 65.233 -9.652 5.380 1.00 97.63 C ANISOU 364 C ALA A 172 10370 13626 13099 -2537 2347 1853 C ATOM 365 O ALA A 172 65.509 -10.790 5.761 1.00100.21 O ANISOU 365 O ALA A 172 10267 14324 13484 -2393 2120 1951 O ATOM 366 CB ALA A 172 64.113 -8.572 7.337 1.00 85.05 C ANISOU 366 CB ALA A 172 9156 11961 11199 -2985 1817 1384 C ATOM 367 N GLY A 173 64.889 -9.369 4.127 1.00 97.70 N ANISOU 367 N GLY A 173 10797 13307 13019 -2225 2744 1950 N ATOM 368 CA GLY A 173 64.840 -10.388 3.094 1.00 92.92 C ANISOU 368 CA GLY A 173 10174 12764 12366 -1734 2927 2140 C ATOM 369 C GLY A 173 63.770 -11.437 3.331 1.00 88.42 C ANISOU 369 C GLY A 173 9699 12364 11534 -1338 2619 2044 C ATOM 370 O GLY A 173 64.046 -12.636 3.291 1.00 89.45 O ANISOU 370 O GLY A 173 9509 12739 11738 -1135 2564 2151 O ATOM 371 N VAL A 174 62.544 -10.986 3.577 1.00 82.39 N ANISOU 371 N VAL A 174 9373 11451 10482 -1226 2457 1848 N ATOM 372 CA VAL A 174 61.430 -11.897 3.815 1.00 77.80 C ANISOU 372 CA VAL A 174 8883 11010 9669 -888 2182 1727 C ATOM 373 C VAL A 174 60.266 -11.612 2.871 1.00 69.75 C ANISOU 373 C VAL A 174 8390 9785 8327 -498 2303 1661 C ATOM 374 O VAL A 174 59.121 -11.959 3.163 1.00 71.62 O ANISOU 374 O VAL A 174 8778 10084 8350 -289 2065 1504 O ATOM 375 CB VAL A 174 60.929 -11.809 5.267 1.00 81.06 C ANISOU 375 CB VAL A 174 9225 11544 10030 -1103 1782 1541 C ATOM 376 CG1 VAL A 174 61.976 -12.355 6.225 1.00 87.39 C ANISOU 376 CG1 VAL A 174 9464 12665 11074 -1393 1584 1616 C ATOM 377 CG2 VAL A 174 60.567 -10.374 5.617 1.00 87.07 C ANISOU 377 CG2 VAL A 174 10357 12026 10698 -1351 1813 1404 C ATOM 378 N GLU A 175 60.568 -10.981 1.742 1.00 75.08 N ANISOU 378 N GLU A 175 9325 10239 8964 -391 2679 1795 N ATOM 379 CA GLU A 175 59.550 -10.650 0.753 1.00 75.76 C ANISOU 379 CA GLU A 175 9905 10179 8701 20 2803 1777 C ATOM 380 C GLU A 175 58.890 -11.918 0.221 1.00 71.04 C ANISOU 380 C GLU A 175 9277 9805 7909 397 2667 1703 C ATOM 381 O GLU A 175 57.676 -11.958 0.017 1.00 67.05 O ANISOU 381 O GLU A 175 9026 9344 7106 677 2505 1566 O ATOM 382 CB GLU A 175 60.163 -9.838 -0.394 1.00 87.18 C ANISOU 382 CB GLU A 175 11622 11362 10142 90 3282 1982 C ATOM 383 CG GLU A 175 59.152 -9.181 -1.328 1.00 96.47 C ANISOU 383 CG GLU A 175 13357 12376 10922 514 3427 2007 C ATOM 384 CD GLU A 175 58.608 -10.132 -2.378 1.00103.49 C ANISOU 384 CD GLU A 175 14349 13466 11506 976 3401 1997 C ATOM 385 OE1 GLU A 175 59.314 -11.100 -2.731 1.00101.23 O ANISOU 385 OE1 GLU A 175 13804 13310 11349 975 3483 2045 O ATOM 386 OE2 GLU A 175 57.472 -9.911 -2.849 1.00109.24 O ANISOU 386 OE2 GLU A 175 15413 14235 11858 1341 3304 1936 O ATOM 387 N HIS A 176 59.697 -12.954 0.008 1.00 69.98 N ANISOU 387 N HIS A 176 8819 9814 7958 393 2752 1789 N ATOM 388 CA HIS A 176 59.202 -14.229 -0.500 1.00 65.49 C ANISOU 388 CA HIS A 176 8231 9410 7242 696 2691 1696 C ATOM 389 C HIS A 176 58.210 -14.844 0.473 1.00 67.67 C ANISOU 389 C HIS A 176 8399 9846 7466 692 2296 1472 C ATOM 390 O HIS A 176 57.284 -15.553 0.079 1.00 62.25 O ANISOU 390 O HIS A 176 7833 9254 6566 938 2191 1303 O ATOM 391 CB HIS A 176 60.360 -15.197 -0.747 1.00 72.27 C ANISOU 391 CB HIS A 176 8753 10344 8361 672 2913 1858 C ATOM 392 CG HIS A 176 61.015 -15.684 0.509 1.00 93.02 C ANISOU 392 CG HIS A 176 10890 13133 11321 397 2730 1910 C ATOM 393 ND1 HIS A 176 61.814 -14.879 1.292 1.00 98.23 N ANISOU 393 ND1 HIS A 176 11303 13796 12223 31 2686 2013 N ATOM 394 CD2 HIS A 176 60.982 -16.891 1.121 1.00 93.85 C ANISOU 394 CD2 HIS A 176 10712 13415 11533 446 2583 1875 C ATOM 395 CE1 HIS A 176 62.249 -15.570 2.330 1.00 94.84 C ANISOU 395 CE1 HIS A 176 10441 13592 12002 -114 2478 2049 C ATOM 396 NE2 HIS A 176 61.759 -16.794 2.251 1.00 88.71 N ANISOU 396 NE2 HIS A 176 9646 12907 11153 158 2434 1991 N ATOM 397 N GLN A 177 58.408 -14.568 1.755 1.00 65.21 N ANISOU 397 N GLN A 177 7862 9571 7346 395 2088 1459 N ATOM 398 CA GLN A 177 57.532 -15.103 2.778 1.00 54.03 C ANISOU 398 CA GLN A 177 6350 8283 5896 384 1755 1277 C ATOM 399 C GLN A 177 56.197 -14.360 2.767 1.00 55.83 C ANISOU 399 C GLN A 177 6931 8434 5846 523 1610 1112 C ATOM 400 O GLN A 177 55.148 -14.950 3.029 1.00 51.49 O ANISOU 400 O GLN A 177 6392 7989 5182 667 1411 935 O ATOM 401 CB GLN A 177 58.202 -15.011 4.150 1.00 65.86 C ANISOU 401 CB GLN A 177 7523 9869 7632 45 1580 1328 C ATOM 402 CG GLN A 177 57.549 -15.863 5.213 1.00 71.14 C ANISOU 402 CG GLN A 177 8036 10690 8302 66 1304 1203 C ATOM 403 CD GLN A 177 57.605 -17.350 4.913 1.00 68.36 C ANISOU 403 CD GLN A 177 7497 10451 8027 276 1386 1224 C ATOM 404 OE1 GLN A 177 58.660 -17.890 4.582 1.00 77.64 O ANISOU 404 OE1 GLN A 177 8434 11680 9384 282 1578 1412 O ATOM 405 NE2 GLN A 177 56.464 -18.019 5.031 1.00 48.55 N ANISOU 405 NE2 GLN A 177 5090 7958 5397 445 1274 1031 N ATOM 406 N LEU A 178 56.239 -13.068 2.452 1.00 59.63 N ANISOU 406 N LEU A 178 7695 8724 6239 491 1746 1183 N ATOM 407 CA LEU A 178 55.016 -12.279 2.328 1.00 67.17 C ANISOU 407 CA LEU A 178 9003 9596 6922 695 1672 1088 C ATOM 408 C LEU A 178 54.183 -12.765 1.145 1.00 62.72 C ANISOU 408 C LEU A 178 8605 9157 6068 1103 1683 1027 C ATOM 409 O LEU A 178 52.951 -12.768 1.200 1.00 51.18 O ANISOU 409 O LEU A 178 7246 7796 4403 1310 1490 885 O ATOM 410 CB LEU A 178 55.332 -10.790 2.169 1.00 64.55 C ANISOU 410 CB LEU A 178 8980 8979 6568 601 1907 1215 C ATOM 411 CG LEU A 178 54.113 -9.899 1.903 1.00 58.31 C ANISOU 411 CG LEU A 178 8592 8080 5483 900 1911 1188 C ATOM 412 CD1 LEU A 178 53.061 -10.080 2.996 1.00 53.67 C ANISOU 412 CD1 LEU A 178 7939 7590 4863 895 1598 1002 C ATOM 413 CD2 LEU A 178 54.514 -8.439 1.774 1.00 63.03 C ANISOU 413 CD2 LEU A 178 9535 8324 6091 800 2231 1333 C ATOM 414 N ARG A 179 54.861 -13.170 0.076 1.00 60.96 N ANISOU 414 N ARG A 179 8399 8947 5817 1213 1910 1128 N ATOM 415 CA ARG A 179 54.183 -13.765 -1.069 1.00 63.17 C ANISOU 415 CA ARG A 179 8829 9386 5789 1563 1907 1033 C ATOM 416 C ARG A 179 53.417 -14.997 -0.608 1.00 64.14 C ANISOU 416 C ARG A 179 8716 9723 5931 1564 1632 779 C ATOM 417 O ARG A 179 52.236 -15.164 -0.919 1.00 53.25 O ANISOU 417 O ARG A 179 7425 8510 4298 1776 1443 596 O ATOM 418 CB ARG A 179 55.181 -14.135 -2.171 1.00 56.17 C ANISOU 418 CB ARG A 179 7991 8456 4894 1640 2233 1174 C ATOM 419 CG ARG A 179 54.575 -14.944 -3.310 1.00 58.23 C ANISOU 419 CG ARG A 179 8400 8904 4820 1952 2220 1022 C ATOM 420 CD ARG A 179 55.618 -15.301 -4.365 1.00 66.43 C ANISOU 420 CD ARG A 179 9531 9865 5845 2034 2595 1170 C ATOM 421 NE ARG A 179 56.174 -14.112 -5.005 1.00 73.58 N ANISOU 421 NE ARG A 179 10719 10573 6664 2129 2905 1439 N ATOM 422 CZ ARG A 179 55.662 -13.544 -6.093 1.00 77.41 C ANISOU 422 CZ ARG A 179 11606 11088 6719 2482 3001 1488 C ATOM 423 NH1 ARG A 179 54.584 -14.061 -6.667 1.00 76.31 N ANISOU 423 NH1 ARG A 179 11590 11221 6182 2751 2756 1262 N ATOM 424 NH2 ARG A 179 56.228 -12.462 -6.608 1.00 78.98 N ANISOU 424 NH2 ARG A 179 12076 11053 6878 2566 3350 1765 N ATOM 425 N ARG A 180 54.102 -15.842 0.155 1.00 51.48 N ANISOU 425 N ARG A 180 6796 8122 4640 1329 1627 780 N ATOM 426 CA ARG A 180 53.506 -17.050 0.708 1.00 64.53 C ANISOU 426 CA ARG A 180 8232 9912 6374 1302 1447 570 C ATOM 427 C ARG A 180 52.315 -16.735 1.613 1.00 68.22 C ANISOU 427 C ARG A 180 8691 10437 6793 1289 1160 416 C ATOM 428 O ARG A 180 51.283 -17.395 1.532 1.00 61.26 O ANISOU 428 O ARG A 180 7773 9693 5811 1393 1013 189 O ATOM 429 CB ARG A 180 54.558 -17.851 1.477 1.00 68.71 C ANISOU 429 CB ARG A 180 8440 10415 7251 1092 1532 684 C ATOM 430 CG ARG A 180 54.788 -19.243 0.920 1.00 72.46 C ANISOU 430 CG ARG A 180 8824 10929 7779 1185 1698 613 C ATOM 431 CD ARG A 180 56.262 -19.508 0.653 1.00 76.59 C ANISOU 431 CD ARG A 180 9198 11382 8520 1139 1998 875 C ATOM 432 NE ARG A 180 57.045 -19.558 1.881 1.00 77.02 N ANISOU 432 NE ARG A 180 8915 11465 8884 931 1937 1058 N ATOM 433 CZ ARG A 180 58.305 -19.975 1.947 1.00 78.46 C ANISOU 433 CZ ARG A 180 8835 11659 9319 885 2149 1303 C ATOM 434 NH1 ARG A 180 58.931 -20.384 0.853 1.00 76.44 N ANISOU 434 NH1 ARG A 180 8644 11335 9066 1033 2484 1398 N ATOM 435 NH2 ARG A 180 58.940 -19.988 3.111 1.00 72.35 N ANISOU 435 NH2 ARG A 180 7725 10986 8777 708 2028 1461 N ATOM 436 N GLU A 181 52.453 -15.723 2.466 1.00 60.21 N ANISOU 436 N GLU A 181 7714 9308 5855 1145 1106 524 N ATOM 437 CA GLU A 181 51.366 -15.338 3.366 1.00 60.17 C ANISOU 437 CA GLU A 181 7736 9321 5805 1148 887 404 C ATOM 438 C GLU A 181 50.128 -14.911 2.583 1.00 58.15 C ANISOU 438 C GLU A 181 7687 9165 5243 1458 809 301 C ATOM 439 O GLU A 181 49.014 -15.340 2.883 1.00 49.27 O ANISOU 439 O GLU A 181 6467 8182 4072 1544 626 117 O ATOM 440 CB GLU A 181 51.806 -14.209 4.308 1.00 57.50 C ANISOU 440 CB GLU A 181 7483 8805 5559 933 894 526 C ATOM 441 CG GLU A 181 50.694 -13.689 5.220 1.00 56.81 C ANISOU 441 CG GLU A 181 7493 8690 5403 963 729 419 C ATOM 442 CD GLU A 181 51.144 -12.542 6.115 1.00 55.35 C ANISOU 442 CD GLU A 181 7461 8294 5277 723 770 500 C ATOM 443 OE1 GLU A 181 52.322 -12.136 6.024 1.00 58.61 O ANISOU 443 OE1 GLU A 181 7868 8603 5800 501 906 625 O ATOM 444 OE2 GLU A 181 50.317 -12.044 6.907 1.00 56.74 O ANISOU 444 OE2 GLU A 181 7764 8404 5393 743 685 424 O ATOM 445 N VAL A 182 50.332 -14.082 1.565 1.00 54.94 N ANISOU 445 N VAL A 182 7543 8703 4627 1640 960 437 N ATOM 446 CA VAL A 182 49.219 -13.521 0.808 1.00 56.90 C ANISOU 446 CA VAL A 182 7998 9082 4541 1992 887 405 C ATOM 447 C VAL A 182 48.549 -14.565 -0.087 1.00 60.12 C ANISOU 447 C VAL A 182 8299 9793 4752 2172 751 190 C ATOM 448 O VAL A 182 47.321 -14.654 -0.136 1.00 56.10 O ANISOU 448 O VAL A 182 7724 9509 4083 2347 536 31 O ATOM 449 CB VAL A 182 49.678 -12.328 -0.049 1.00 65.66 C ANISOU 449 CB VAL A 182 9460 10029 5457 2175 1138 653 C ATOM 450 CG1 VAL A 182 48.550 -11.841 -0.946 1.00 68.95 C ANISOU 450 CG1 VAL A 182 10080 10646 5474 2622 1060 662 C ATOM 451 CG2 VAL A 182 50.169 -11.202 0.842 1.00 52.63 C ANISOU 451 CG2 VAL A 182 7950 8058 3989 1966 1283 808 C ATOM 452 N GLU A 183 49.354 -15.361 -0.781 1.00 54.82 N ANISOU 452 N GLU A 183 7598 9132 4098 2113 889 170 N ATOM 453 CA GLU A 183 48.820 -16.353 -1.710 1.00 58.97 C ANISOU 453 CA GLU A 183 8082 9914 4410 2241 801 -73 C ATOM 454 C GLU A 183 48.141 -17.518 -0.985 1.00 64.65 C ANISOU 454 C GLU A 183 8496 10744 5326 2059 621 -366 C ATOM 455 O GLU A 183 47.052 -17.942 -1.371 1.00 60.97 O ANISOU 455 O GLU A 183 7952 10540 4675 2160 420 -624 O ATOM 456 CB GLU A 183 49.929 -16.875 -2.632 1.00 57.27 C ANISOU 456 CB GLU A 183 7974 9621 4166 2231 1070 -6 C ATOM 457 CG GLU A 183 50.479 -15.820 -3.591 1.00 60.90 C ANISOU 457 CG GLU A 183 8769 9994 4377 2457 1290 261 C ATOM 458 CD GLU A 183 51.427 -16.392 -4.633 1.00 70.93 C ANISOU 458 CD GLU A 183 10168 11215 5566 2499 1577 308 C ATOM 459 OE1 GLU A 183 51.689 -17.613 -4.603 1.00 70.54 O ANISOU 459 OE1 GLU A 183 9954 11184 5663 2352 1616 132 O ATOM 460 OE2 GLU A 183 51.904 -15.619 -5.493 1.00 61.06 O ANISOU 460 OE2 GLU A 183 9211 9883 4105 2699 1807 531 O ATOM 461 N ILE A 184 48.777 -18.027 0.067 1.00 55.64 N ANISOU 461 N ILE A 184 7170 9416 4554 1794 700 -321 N ATOM 462 CA ILE A 184 48.240 -19.179 0.786 1.00 59.54 C ANISOU 462 CA ILE A 184 7409 9954 5261 1632 614 -557 C ATOM 463 C ILE A 184 46.958 -18.842 1.542 1.00 51.26 C ANISOU 463 C ILE A 184 6250 9014 4212 1661 377 -678 C ATOM 464 O ILE A 184 45.973 -19.578 1.458 1.00 49.39 O ANISOU 464 O ILE A 184 5858 8948 3959 1651 253 -959 O ATOM 465 CB ILE A 184 49.264 -19.756 1.782 1.00 62.56 C ANISOU 465 CB ILE A 184 7632 10129 6009 1405 770 -416 C ATOM 466 CG1 ILE A 184 50.438 -20.383 1.033 1.00 61.76 C ANISOU 466 CG1 ILE A 184 7567 9942 5956 1394 1039 -321 C ATOM 467 CG2 ILE A 184 48.612 -20.792 2.690 1.00 53.59 C ANISOU 467 CG2 ILE A 184 6274 8996 5090 1276 714 -610 C ATOM 468 CD1 ILE A 184 51.525 -20.907 1.943 1.00 60.54 C ANISOU 468 CD1 ILE A 184 7217 9641 6145 1230 1195 -122 C ATOM 469 N GLN A 185 46.966 -17.731 2.272 1.00 52.16 N ANISOU 469 N GLN A 185 6446 9019 4354 1682 340 -478 N ATOM 470 CA GLN A 185 45.825 -17.384 3.113 1.00 58.82 C ANISOU 470 CA GLN A 185 7201 9920 5228 1722 174 -555 C ATOM 471 C GLN A 185 44.601 -17.014 2.280 1.00 57.56 C ANISOU 471 C GLN A 185 7053 10043 4773 2001 2 -677 C ATOM 472 O GLN A 185 43.475 -17.320 2.667 1.00 51.70 O ANISOU 472 O GLN A 185 6109 9460 4076 2023 -146 -858 O ATOM 473 CB GLN A 185 46.178 -16.237 4.067 1.00 53.63 C ANISOU 473 CB GLN A 185 6691 9043 4643 1673 218 -324 C ATOM 474 CG GLN A 185 45.062 -15.897 5.051 1.00 57.99 C ANISOU 474 CG GLN A 185 7185 9606 5243 1718 104 -385 C ATOM 475 CD GLN A 185 45.477 -14.888 6.106 1.00 62.56 C ANISOU 475 CD GLN A 185 7946 9932 5892 1612 175 -206 C ATOM 476 OE1 GLN A 185 46.577 -14.338 6.062 1.00 71.19 O ANISOU 476 OE1 GLN A 185 9195 10857 6996 1488 291 -44 O ATOM 477 NE2 GLN A 185 44.588 -14.635 7.061 1.00 59.72 N ANISOU 477 NE2 GLN A 185 7569 9541 5580 1643 123 -251 N ATOM 478 N SER A 186 44.824 -16.375 1.134 1.00 59.64 N ANISOU 478 N SER A 186 7536 10393 4731 2230 31 -566 N ATOM 479 CA SER A 186 43.722 -15.920 0.287 1.00 66.11 C ANISOU 479 CA SER A 186 8375 11539 5205 2562 -149 -626 C ATOM 480 C SER A 186 42.954 -17.080 -0.339 1.00 70.21 C ANISOU 480 C SER A 186 8644 12403 5630 2526 -338 -990 C ATOM 481 O SER A 186 41.780 -16.941 -0.674 1.00 77.15 O ANISOU 481 O SER A 186 9373 13629 6312 2723 -566 -1118 O ATOM 482 CB SER A 186 44.236 -14.995 -0.820 1.00 64.39 C ANISOU 482 CB SER A 186 8495 11319 4650 2845 -31 -386 C ATOM 483 OG SER A 186 45.075 -15.695 -1.723 1.00 66.78 O ANISOU 483 OG SER A 186 8878 11630 4866 2771 81 -449 O ATOM 484 N HIS A 187 43.615 -18.223 -0.491 1.00 61.25 N ANISOU 484 N HIS A 187 7454 11178 4640 2268 -228 -1161 N ATOM 485 CA HIS A 187 42.992 -19.375 -1.136 1.00 70.87 C ANISOU 485 CA HIS A 187 8490 12664 5772 2170 -350 -1553 C ATOM 486 C HIS A 187 42.448 -20.389 -0.129 1.00 63.11 C ANISOU 486 C HIS A 187 7197 11613 5170 1874 -356 -1801 C ATOM 487 O HIS A 187 41.899 -21.421 -0.514 1.00 68.85 O ANISOU 487 O HIS A 187 7753 12506 5901 1715 -414 -2169 O ATOM 488 CB HIS A 187 43.988 -20.057 -2.079 1.00 69.32 C ANISOU 488 CB HIS A 187 8486 12387 5466 2099 -159 -1613 C ATOM 489 CG HIS A 187 44.341 -19.240 -3.284 1.00 71.44 C ANISOU 489 CG HIS A 187 9061 12785 5298 2409 -147 -1436 C ATOM 490 ND1 HIS A 187 45.395 -18.352 -3.300 1.00 57.42 N ANISOU 490 ND1 HIS A 187 7547 10740 3532 2517 80 -1051 N ATOM 491 CD2 HIS A 187 43.783 -19.182 -4.518 1.00 76.41 C ANISOU 491 CD2 HIS A 187 9783 13788 5460 2633 -319 -1587 C ATOM 492 CE1 HIS A 187 45.470 -17.782 -4.490 1.00 72.34 C ANISOU 492 CE1 HIS A 187 9702 12792 4991 2815 91 -951 C ATOM 493 NE2 HIS A 187 44.504 -18.268 -5.248 1.00 63.52 N ANISOU 493 NE2 HIS A 187 8479 12020 3635 2875 -164 -1241 N ATOM 494 N LEU A 188 42.598 -20.093 1.158 1.00 62.55 N ANISOU 494 N LEU A 188 7076 11287 5405 1790 -273 -1613 N ATOM 495 CA LEU A 188 42.064 -20.959 2.205 1.00 56.38 C ANISOU 495 CA LEU A 188 6035 10413 4975 1556 -236 -1792 C ATOM 496 C LEU A 188 40.634 -20.568 2.567 1.00 54.02 C ANISOU 496 C LEU A 188 5502 10357 4665 1660 -446 -1900 C ATOM 497 O LEU A 188 40.304 -19.385 2.635 1.00 62.09 O ANISOU 497 O LEU A 188 6608 11458 5526 1916 -549 -1684 O ATOM 498 CB LEU A 188 42.951 -20.911 3.453 1.00 61.95 C ANISOU 498 CB LEU A 188 6806 10754 5979 1427 -41 -1534 C ATOM 499 CG LEU A 188 44.333 -21.559 3.347 1.00 59.14 C ANISOU 499 CG LEU A 188 6561 10168 5742 1295 195 -1425 C ATOM 500 CD1 LEU A 188 45.177 -21.212 4.558 1.00 57.66 C ANISOU 500 CD1 LEU A 188 6412 9730 5766 1219 300 -1127 C ATOM 501 CD2 LEU A 188 44.227 -23.069 3.189 1.00 53.94 C ANISOU 501 CD2 LEU A 188 5773 9465 5259 1106 346 -1711 C ATOM 502 N ARG A 189 39.790 -21.569 2.794 1.00 61.93 N ANISOU 502 N ARG A 189 6211 11458 5861 1462 -469 -2228 N ATOM 503 CA ARG A 189 38.402 -21.337 3.184 1.00 63.90 C ANISOU 503 CA ARG A 189 6161 11952 6168 1530 -638 -2347 C ATOM 504 C ARG A 189 37.999 -22.249 4.333 1.00 71.65 C ANISOU 504 C ARG A 189 6927 12721 7578 1261 -459 -2490 C ATOM 505 O ARG A 189 37.790 -23.449 4.144 1.00 72.99 O ANISOU 505 O ARG A 189 6935 12886 7913 992 -369 -2818 O ATOM 506 CB ARG A 189 37.457 -21.553 2.002 1.00 73.15 C ANISOU 506 CB ARG A 189 7103 13620 7071 1586 -910 -2668 C ATOM 507 CG ARG A 189 37.614 -20.552 0.877 1.00 74.27 C ANISOU 507 CG ARG A 189 7446 14041 6732 1942 -1103 -2497 C ATOM 508 CD ARG A 189 37.247 -19.142 1.308 1.00 77.15 C ANISOU 508 CD ARG A 189 7880 14433 6999 2310 -1161 -2127 C ATOM 509 NE ARG A 189 37.152 -18.245 0.159 1.00 87.39 N ANISOU 509 NE ARG A 189 9329 16054 7820 2699 -1338 -1978 N ATOM 510 CZ ARG A 189 38.167 -17.536 -0.325 1.00 85.84 C ANISOU 510 CZ ARG A 189 9545 15669 7402 2875 -1210 -1689 C ATOM 511 NH1 ARG A 189 39.364 -17.611 0.244 1.00 73.72 N ANISOU 511 NH1 ARG A 189 8261 13658 6092 2670 -940 -1536 N ATOM 512 NH2 ARG A 189 37.986 -16.749 -1.377 1.00 78.35 N ANISOU 512 NH2 ARG A 189 8742 15000 6029 3256 -1331 -1536 N ATOM 513 N HIS A 190 37.887 -21.671 5.523 1.00 63.54 N ANISOU 513 N HIS A 190 5931 11494 6716 1336 -374 -2246 N ATOM 514 CA HIS A 190 37.508 -22.422 6.712 1.00 73.14 C ANISOU 514 CA HIS A 190 6990 12488 8310 1137 -171 -2318 C ATOM 515 C HIS A 190 36.966 -21.467 7.770 1.00 61.31 C ANISOU 515 C HIS A 190 5507 10922 6866 1319 -164 -2083 C ATOM 516 O HIS A 190 37.519 -20.386 7.970 1.00 66.60 O ANISOU 516 O HIS A 190 6454 11491 7361 1504 -192 -1789 O ATOM 517 CB HIS A 190 38.702 -23.209 7.258 1.00 64.34 C ANISOU 517 CB HIS A 190 6068 10996 7381 950 98 -2220 C ATOM 518 CG HIS A 190 38.324 -24.282 8.232 1.00 72.52 C ANISOU 518 CG HIS A 190 6953 11815 8788 743 356 -2341 C ATOM 519 ND1 HIS A 190 38.091 -24.029 9.567 1.00 67.79 N ANISOU 519 ND1 HIS A 190 6375 11028 8354 788 481 -2150 N ATOM 520 CD2 HIS A 190 38.143 -25.614 8.064 1.00 65.12 C ANISOU 520 CD2 HIS A 190 5878 10786 8079 495 558 -2630 C ATOM 521 CE1 HIS A 190 37.779 -25.158 10.179 1.00 63.21 C ANISOU 521 CE1 HIS A 190 5668 10259 8088 602 750 -2289 C ATOM 522 NE2 HIS A 190 37.804 -26.134 9.289 1.00 75.95 N ANISOU 522 NE2 HIS A 190 7183 11909 9764 413 816 -2583 N ATOM 523 N PRO A 191 35.872 -21.861 8.441 1.00 64.37 N ANISOU 523 N PRO A 191 5609 11344 7505 1255 -91 -2225 N ATOM 524 CA PRO A 191 35.237 -21.048 9.485 1.00 64.48 C ANISOU 524 CA PRO A 191 5632 11278 7589 1434 -30 -2024 C ATOM 525 C PRO A 191 36.199 -20.659 10.606 1.00 59.12 C ANISOU 525 C PRO A 191 5328 10209 6927 1436 147 -1727 C ATOM 526 O PRO A 191 36.035 -19.604 11.215 1.00 62.86 O ANISOU 526 O PRO A 191 5978 10601 7304 1629 157 -1511 O ATOM 527 CB PRO A 191 34.131 -21.966 10.016 1.00 59.65 C ANISOU 527 CB PRO A 191 4642 10697 7326 1264 112 -2269 C ATOM 528 CG PRO A 191 33.817 -22.865 8.880 1.00 71.13 C ANISOU 528 CG PRO A 191 5807 12428 8791 1062 -13 -2643 C ATOM 529 CD PRO A 191 35.120 -23.099 8.174 1.00 71.20 C ANISOU 529 CD PRO A 191 6119 12328 8606 993 -37 -2613 C ATOM 530 N ASN A 192 37.194 -21.502 10.862 1.00 58.44 N ANISOU 530 N ASN A 192 5361 9897 6945 1229 289 -1720 N ATOM 531 CA ASN A 192 38.163 -21.251 11.921 1.00 60.13 C ANISOU 531 CA ASN A 192 5875 9817 7155 1209 416 -1455 C ATOM 532 C ASN A 192 39.494 -20.739 11.378 1.00 68.60 C ANISOU 532 C ASN A 192 7199 10857 8008 1216 315 -1286 C ATOM 533 O ASN A 192 40.533 -20.878 12.023 1.00 63.23 O ANISOU 533 O ASN A 192 6686 9993 7347 1127 399 -1116 O ATOM 534 CB ASN A 192 38.387 -22.520 12.742 1.00 51.31 C ANISOU 534 CB ASN A 192 4703 8483 6310 1027 675 -1492 C ATOM 535 CG ASN A 192 37.118 -23.015 13.402 1.00 62.78 C ANISOU 535 CG ASN A 192 5928 9908 8017 1001 847 -1636 C ATOM 536 OD1 ASN A 192 36.632 -24.104 13.099 1.00 76.74 O ANISOU 536 OD1 ASN A 192 7452 11687 10018 838 981 -1882 O ATOM 537 ND2 ASN A 192 36.573 -22.214 14.312 1.00 56.20 N ANISOU 537 ND2 ASN A 192 5185 9016 7152 1148 880 -1493 N ATOM 538 N ILE A 193 39.457 -20.159 10.184 1.00 60.74 N ANISOU 538 N ILE A 193 6212 10065 6802 1331 140 -1323 N ATOM 539 CA ILE A 193 40.631 -19.516 9.606 1.00 58.10 C ANISOU 539 CA ILE A 193 6123 9690 6262 1358 80 -1147 C ATOM 540 C ILE A 193 40.269 -18.110 9.151 1.00 60.85 C ANISOU 540 C ILE A 193 6629 10132 6360 1601 -40 -1027 C ATOM 541 O ILE A 193 39.287 -17.919 8.433 1.00 62.68 O ANISOU 541 O ILE A 193 6709 10615 6490 1779 -156 -1138 O ATOM 542 CB ILE A 193 41.204 -20.314 8.415 1.00 55.92 C ANISOU 542 CB ILE A 193 5780 9518 5949 1279 69 -1278 C ATOM 543 CG1 ILE A 193 41.650 -21.706 8.865 1.00 50.55 C ANISOU 543 CG1 ILE A 193 4993 8685 5530 1069 262 -1360 C ATOM 544 CG2 ILE A 193 42.375 -19.569 7.781 1.00 46.64 C ANISOU 544 CG2 ILE A 193 4848 8299 4574 1329 44 -1074 C ATOM 545 CD1 ILE A 193 42.300 -22.525 7.767 1.00 54.93 C ANISOU 545 CD1 ILE A 193 5536 9276 6059 990 323 -1480 C ATOM 546 N LEU A 194 41.054 -17.127 9.583 1.00 56.41 N ANISOU 546 N LEU A 194 6365 9374 5695 1609 1 -800 N ATOM 547 CA LEU A 194 40.809 -15.738 9.214 1.00 55.54 C ANISOU 547 CA LEU A 194 6480 9262 5361 1843 -26 -654 C ATOM 548 C LEU A 194 40.908 -15.556 7.702 1.00 59.76 C ANISOU 548 C LEU A 194 7018 10007 5681 2007 -118 -661 C ATOM 549 O LEU A 194 41.808 -16.100 7.066 1.00 50.96 O ANISOU 549 O LEU A 194 5904 8902 4555 1879 -112 -684 O ATOM 550 CB LEU A 194 41.797 -14.808 9.918 1.00 54.83 C ANISOU 550 CB LEU A 194 6731 8880 5221 1731 73 -456 C ATOM 551 CG LEU A 194 41.427 -13.324 9.903 1.00 62.42 C ANISOU 551 CG LEU A 194 7995 9719 6002 1951 146 -306 C ATOM 552 CD1 LEU A 194 40.312 -13.046 10.905 1.00 56.56 C ANISOU 552 CD1 LEU A 194 7255 8917 5319 2072 210 -324 C ATOM 553 CD2 LEU A 194 42.641 -12.452 10.177 1.00 67.89 C ANISOU 553 CD2 LEU A 194 9027 10136 6631 1768 250 -160 C ATOM 554 N ARG A 195 39.979 -14.791 7.137 1.00 59.35 N ANISOU 554 N ARG A 195 6974 10132 5442 2324 -185 -620 N ATOM 555 CA ARG A 195 39.944 -14.545 5.701 1.00 66.49 C ANISOU 555 CA ARG A 195 7904 11286 6074 2551 -284 -605 C ATOM 556 C ARG A 195 40.842 -13.384 5.291 1.00 74.62 C ANISOU 556 C ARG A 195 9337 12101 6913 2664 -148 -337 C ATOM 557 O ARG A 195 40.899 -12.357 5.968 1.00 70.50 O ANISOU 557 O ARG A 195 9073 11319 6395 2721 -4 -158 O ATOM 558 CB ARG A 195 38.510 -14.263 5.244 1.00 66.11 C ANISOU 558 CB ARG A 195 7642 11595 5883 2891 -434 -652 C ATOM 559 CG ARG A 195 37.643 -15.500 5.097 1.00 71.98 C ANISOU 559 CG ARG A 195 7929 12663 6757 2767 -604 -978 C ATOM 560 CD ARG A 195 38.026 -16.296 3.860 1.00 88.20 C ANISOU 560 CD ARG A 195 9905 14957 8650 2682 -733 -1175 C ATOM 561 NE ARG A 195 38.053 -15.459 2.663 1.00 86.49 N ANISOU 561 NE ARG A 195 9869 14962 8031 3033 -825 -1021 N ATOM 562 CZ ARG A 195 36.976 -15.121 1.961 1.00 89.72 C ANISOU 562 CZ ARG A 195 10086 15812 8190 3365 -1035 -1044 C ATOM 563 NH1 ARG A 195 35.776 -15.544 2.336 1.00 89.49 N ANISOU 563 NH1 ARG A 195 9636 16058 8309 3355 -1180 -1237 N ATOM 564 NH2 ARG A 195 37.097 -14.354 0.886 1.00 83.98 N ANISOU 564 NH2 ARG A 195 9575 15272 7063 3724 -1089 -858 N ATOM 565 N LEU A 196 41.545 -13.565 4.178 1.00 68.00 N ANISOU 565 N LEU A 196 8573 11348 5914 2681 -155 -323 N ATOM 566 CA LEU A 196 42.280 -12.483 3.537 1.00 68.94 C ANISOU 566 CA LEU A 196 9061 11301 5831 2836 5 -69 C ATOM 567 C LEU A 196 41.589 -12.144 2.222 1.00 67.16 C ANISOU 567 C LEU A 196 8862 11413 5244 3260 -95 -21 C ATOM 568 O LEU A 196 41.715 -12.877 1.245 1.00 64.30 O ANISOU 568 O LEU A 196 8393 11305 4734 3271 -206 -156 O ATOM 569 CB LEU A 196 43.741 -12.876 3.305 1.00 65.09 C ANISOU 569 CB LEU A 196 8665 10629 5437 2549 129 -37 C ATOM 570 CG LEU A 196 44.597 -11.939 2.448 1.00 72.89 C ANISOU 570 CG LEU A 196 9998 11456 6238 2675 332 204 C ATOM 571 CD1 LEU A 196 44.566 -10.517 2.980 1.00 76.53 C ANISOU 571 CD1 LEU A 196 10783 11614 6680 2768 522 423 C ATOM 572 CD2 LEU A 196 46.027 -12.448 2.367 1.00 73.32 C ANISOU 572 CD2 LEU A 196 10050 11349 6461 2355 462 227 C ATOM 573 N TYR A 197 40.849 -11.039 2.206 1.00 72.99 N ANISOU 573 N TYR A 197 9754 12161 5817 3629 -43 177 N ATOM 574 CA TYR A 197 40.008 -10.698 1.062 1.00 72.84 C ANISOU 574 CA TYR A 197 9709 12543 5425 4108 -174 254 C ATOM 575 C TYR A 197 40.803 -10.212 -0.145 1.00 77.87 C ANISOU 575 C TYR A 197 10684 13150 5755 4304 -36 448 C ATOM 576 O TYR A 197 40.409 -10.452 -1.285 1.00 71.06 O ANISOU 576 O TYR A 197 9717 12631 4650 4532 -193 396 O ATOM 577 CB TYR A 197 38.980 -9.635 1.457 1.00 75.59 C ANISOU 577 CB TYR A 197 10124 12897 5701 4508 -110 465 C ATOM 578 CG TYR A 197 38.020 -10.090 2.531 1.00 79.26 C ANISOU 578 CG TYR A 197 10236 13447 6433 4396 -230 292 C ATOM 579 CD1 TYR A 197 37.021 -11.012 2.251 1.00 83.93 C ANISOU 579 CD1 TYR A 197 10335 14538 7018 4428 -539 38 C ATOM 580 CD2 TYR A 197 38.112 -9.595 3.826 1.00 76.34 C ANISOU 580 CD2 TYR A 197 10033 12656 6319 4240 -15 365 C ATOM 581 CE1 TYR A 197 36.140 -11.431 3.229 1.00 81.85 C ANISOU 581 CE1 TYR A 197 9739 14330 7031 4319 -598 -109 C ATOM 582 CE2 TYR A 197 37.235 -10.008 4.811 1.00 68.87 C ANISOU 582 CE2 TYR A 197 8794 11768 5607 4162 -80 226 C ATOM 583 CZ TYR A 197 36.252 -10.925 4.508 1.00 80.29 C ANISOU 583 CZ TYR A 197 9736 13692 7078 4208 -355 3 C ATOM 584 OH TYR A 197 35.378 -11.338 5.488 1.00 83.55 O ANISOU 584 OH TYR A 197 9849 14141 7756 4123 -370 -124 O ATOM 585 N GLY A 198 41.914 -9.525 0.104 1.00 76.37 N ANISOU 585 N GLY A 198 10858 12487 5672 4150 280 646 N ATOM 586 CA GLY A 198 42.725 -8.998 -0.979 1.00 82.73 C ANISOU 586 CA GLY A 198 12008 13192 6232 4322 493 860 C ATOM 587 C GLY A 198 43.939 -8.225 -0.504 1.00 75.74 C ANISOU 587 C GLY A 198 11470 11750 5559 4059 867 1047 C ATOM 588 O GLY A 198 44.164 -8.079 0.698 1.00 66.17 O ANISOU 588 O GLY A 198 10238 10247 4657 3731 928 994 O ATOM 589 N TYR A 199 44.722 -7.727 -1.456 1.00 70.55 N ANISOU 589 N TYR A 199 11121 10947 4738 4184 1119 1252 N ATOM 590 CA TYR A 199 45.935 -6.980 -1.145 1.00 74.08 C ANISOU 590 CA TYR A 199 11880 10884 5384 3910 1506 1422 C ATOM 591 C TYR A 199 46.232 -5.919 -2.203 1.00 76.39 C ANISOU 591 C TYR A 199 12562 10952 5511 4233 1836 1715 C ATOM 592 O TYR A 199 45.711 -5.979 -3.318 1.00 80.96 O ANISOU 592 O TYR A 199 13098 11782 5880 4605 1717 1747 O ATOM 593 CB TYR A 199 47.129 -7.929 -1.020 1.00 66.50 C ANISOU 593 CB TYR A 199 10709 9869 4690 3424 1490 1268 C ATOM 594 CG TYR A 199 47.874 -8.144 -2.320 1.00 80.61 C ANISOU 594 CG TYR A 199 12628 11714 6286 3551 1653 1376 C ATOM 595 CD1 TYR A 199 47.369 -8.984 -3.304 1.00 79.76 C ANISOU 595 CD1 TYR A 199 12377 12020 5906 3796 1420 1248 C ATOM 596 CD2 TYR A 199 49.084 -7.504 -2.563 1.00 87.64 C ANISOU 596 CD2 TYR A 199 13773 12226 7300 3387 2050 1581 C ATOM 597 CE1 TYR A 199 48.047 -9.180 -4.494 1.00 87.89 C ANISOU 597 CE1 TYR A 199 13521 13041 6834 3872 1561 1314 C ATOM 598 CE2 TYR A 199 49.768 -7.693 -3.749 1.00 81.05 C ANISOU 598 CE2 TYR A 199 13075 11423 6298 3522 2248 1699 C ATOM 599 CZ TYR A 199 49.246 -8.532 -4.710 1.00 83.14 C ANISOU 599 CZ TYR A 199 13186 12055 6347 3756 1979 1552 C ATOM 600 OH TYR A 199 49.926 -8.723 -5.890 1.00 87.39 O ANISOU 600 OH TYR A 199 13843 12567 6794 3848 2149 1629 O ATOM 601 N PHE A 200 47.078 -4.956 -1.843 1.00 69.12 N ANISOU 601 N PHE A 200 11991 9534 4738 4045 2252 1897 N ATOM 602 CA PHE A 200 47.554 -3.937 -2.779 1.00 80.83 C ANISOU 602 CA PHE A 200 13835 10691 6186 4258 2633 2152 C ATOM 603 C PHE A 200 48.786 -3.232 -2.213 1.00 82.22 C ANISOU 603 C PHE A 200 14293 10330 6618 3817 3081 2252 C ATOM 604 O PHE A 200 49.082 -3.346 -1.024 1.00 82.88 O ANISOU 604 O PHE A 200 14288 10280 6923 3375 3053 2113 O ATOM 605 CB PHE A 200 46.448 -2.922 -3.103 1.00 81.25 C ANISOU 605 CB PHE A 200 14083 10701 6088 4800 2704 2319 C ATOM 606 CG PHE A 200 45.940 -2.156 -1.908 1.00 85.88 C ANISOU 606 CG PHE A 200 14835 11003 6793 4752 2838 2346 C ATOM 607 CD1 PHE A 200 45.050 -2.738 -1.017 1.00 75.54 C ANISOU 607 CD1 PHE A 200 13244 9982 5475 4728 2502 2175 C ATOM 608 CD2 PHE A 200 46.330 -0.844 -1.694 1.00 86.85 C ANISOU 608 CD2 PHE A 200 15414 10546 7040 4734 3333 2528 C ATOM 609 CE1 PHE A 200 44.573 -2.032 0.074 1.00 74.12 C ANISOU 609 CE1 PHE A 200 13252 9521 5388 4703 2657 2203 C ATOM 610 CE2 PHE A 200 45.858 -0.133 -0.605 1.00 80.57 C ANISOU 610 CE2 PHE A 200 14820 9450 6344 4680 3492 2530 C ATOM 611 CZ PHE A 200 44.977 -0.727 0.280 1.00 78.55 C ANISOU 611 CZ PHE A 200 14298 9491 6057 4677 3153 2377 C ATOM 612 N HIS A 201 49.507 -2.517 -3.071 1.00 80.01 N ANISOU 612 N HIS A 201 14288 9738 6373 3890 3460 2444 N ATOM 613 CA HIS A 201 50.737 -1.842 -2.663 1.00 90.94 C ANISOU 613 CA HIS A 201 15900 10613 8041 3425 3914 2521 C ATOM 614 C HIS A 201 50.895 -0.490 -3.357 1.00 97.34 C ANISOU 614 C HIS A 201 17146 10959 8880 3677 4389 2743 C ATOM 615 O HIS A 201 50.168 -0.180 -4.300 1.00103.55 O ANISOU 615 O HIS A 201 18043 11863 9437 4253 4368 2869 O ATOM 616 CB HIS A 201 51.956 -2.727 -2.948 1.00 90.92 C ANISOU 616 CB HIS A 201 15656 10716 8173 3057 3941 2480 C ATOM 617 CG HIS A 201 52.074 -3.165 -4.376 1.00 99.44 C ANISOU 617 CG HIS A 201 16696 12009 9077 3413 3907 2556 C ATOM 618 ND1 HIS A 201 53.176 -2.879 -5.154 1.00 99.64 N ANISOU 618 ND1 HIS A 201 16849 11776 9235 3320 4287 2700 N ATOM 619 CD2 HIS A 201 51.236 -3.883 -5.163 1.00105.16 C ANISOU 619 CD2 HIS A 201 17271 13180 9507 3832 3545 2485 C ATOM 620 CE1 HIS A 201 53.008 -3.392 -6.359 1.00 93.17 C ANISOU 620 CE1 HIS A 201 16002 11217 8180 3697 4171 2729 C ATOM 621 NE2 HIS A 201 51.839 -4.006 -6.391 1.00 98.29 N ANISOU 621 NE2 HIS A 201 16484 12300 8561 3992 3714 2589 N ATOM 622 N ASP A 202 51.848 0.310 -2.887 1.00 86.14 N ANISOU 622 N ASP A 202 12530 11545 8653 3472 2644 2623 N ATOM 623 CA ASP A 202 52.032 1.664 -3.402 1.00 91.69 C ANISOU 623 CA ASP A 202 13567 11893 9378 3570 3082 2903 C ATOM 624 C ASP A 202 53.498 2.094 -3.408 1.00 99.70 C ANISOU 624 C ASP A 202 14493 12749 10641 3106 3300 3177 C ATOM 625 O ASP A 202 53.810 3.258 -3.154 1.00110.14 O ANISOU 625 O ASP A 202 16103 13643 12101 2793 3605 3300 O ATOM 626 CB ASP A 202 51.202 2.656 -2.582 1.00102.03 C ANISOU 626 CB ASP A 202 15263 12808 10696 3446 3203 2766 C ATOM 627 CG ASP A 202 51.620 2.703 -1.123 1.00105.60 C ANISOU 627 CG ASP A 202 15709 13051 11365 2714 3036 2549 C ATOM 628 OD1 ASP A 202 52.181 1.702 -0.631 1.00116.84 O ANISOU 628 OD1 ASP A 202 16756 14754 12882 2402 2715 2427 O ATOM 629 OD2 ASP A 202 51.387 3.741 -0.468 1.00102.21 O ANISOU 629 OD2 ASP A 202 15684 12173 10979 2477 3240 2506 O ATOM 630 N ALA A 203 54.385 1.142 -3.688 1.00104.74 N ANISOU 630 N ALA A 203 14738 13734 11325 3054 3156 3279 N ATOM 631 CA ALA A 203 55.822 1.395 -3.837 1.00120.25 C ANISOU 631 CA ALA A 203 16490 15689 13510 2684 3355 3606 C ATOM 632 C ALA A 203 56.486 1.912 -2.560 1.00117.91 C ANISOU 632 C ALA A 203 16138 15179 13485 1843 3285 3519 C ATOM 633 O ALA A 203 57.647 2.319 -2.579 1.00126.21 O ANISOU 633 O ALA A 203 17006 16204 14745 1418 3453 3787 O ATOM 634 CB ALA A 203 56.071 2.370 -4.989 1.00125.27 C ANISOU 634 CB ALA A 203 17367 16104 14126 3010 3845 3988 C ATOM 635 N THR A 204 55.749 1.895 -1.454 1.00110.91 N ANISOU 635 N THR A 204 15400 14162 12579 1596 3033 3152 N ATOM 636 CA THR A 204 56.297 2.268 -0.155 1.00108.24 C ANISOU 636 CA THR A 204 15038 13659 12427 813 2894 3003 C ATOM 637 C THR A 204 55.857 1.262 0.898 1.00 98.98 C ANISOU 637 C THR A 204 13688 12731 11189 709 2456 2657 C ATOM 638 O THR A 204 56.643 0.846 1.749 1.00 88.67 O ANISOU 638 O THR A 204 12077 11625 9987 214 2219 2607 O ATOM 639 CB THR A 204 55.855 3.681 0.279 1.00114.53 C ANISOU 639 CB THR A 204 16407 13851 13260 540 3157 2916 C ATOM 640 OG1 THR A 204 54.424 3.757 0.284 1.00116.00 O ANISOU 640 OG1 THR A 204 16945 13894 13234 1055 3164 2712 O ATOM 641 CG2 THR A 204 56.414 4.738 -0.661 1.00124.68 C ANISOU 641 CG2 THR A 204 17901 14828 14642 550 3644 3280 C ATOM 642 N ARG A 205 54.587 0.876 0.828 1.00 96.78 N ANISOU 642 N ARG A 205 13584 12463 10727 1189 2359 2438 N ATOM 643 CA ARG A 205 54.015 -0.073 1.771 1.00 88.49 C ANISOU 643 CA ARG A 205 12406 11602 9615 1144 1998 2120 C ATOM 644 C ARG A 205 53.242 -1.169 1.044 1.00 84.36 C ANISOU 644 C ARG A 205 11741 11396 8916 1748 1867 2051 C ATOM 645 O ARG A 205 52.897 -1.029 -0.130 1.00 79.15 O ANISOU 645 O ARG A 205 11167 10774 8133 2241 2040 2197 O ATOM 646 CB ARG A 205 53.094 0.644 2.763 1.00 89.23 C ANISOU 646 CB ARG A 205 12902 11327 9675 976 1995 1855 C ATOM 647 CG ARG A 205 53.761 1.761 3.551 1.00 95.42 C ANISOU 647 CG ARG A 205 13945 11724 10587 333 2113 1852 C ATOM 648 CD ARG A 205 52.739 2.568 4.337 1.00 96.42 C ANISOU 648 CD ARG A 205 14602 11413 10619 313 2206 1622 C ATOM 649 NE ARG A 205 53.343 3.712 5.014 1.00103.46 N ANISOU 649 NE ARG A 205 15864 11851 11593 -310 2355 1591 N ATOM 650 CZ ARG A 205 53.535 4.899 4.446 1.00115.53 C ANISOU 650 CZ ARG A 205 17785 12949 13163 -365 2755 1773 C ATOM 651 NH1 ARG A 205 53.174 5.100 3.186 1.00112.33 N ANISOU 651 NH1 ARG A 205 17427 12545 12708 229 3047 2025 N ATOM 652 NH2 ARG A 205 54.092 5.885 5.137 1.00121.75 N ANISOU 652 NH2 ARG A 205 18946 13293 14022 -1019 2871 1698 N ATOM 653 N VAL A 206 52.986 -2.265 1.750 1.00 76.00 N ANISOU 653 N VAL A 206 10487 10561 7828 1693 1566 1824 N ATOM 654 CA VAL A 206 52.129 -3.330 1.244 1.00 65.66 C ANISOU 654 CA VAL A 206 9094 9498 6357 2152 1416 1682 C ATOM 655 C VAL A 206 50.915 -3.444 2.157 1.00 66.80 C ANISOU 655 C VAL A 206 9364 9551 6466 2123 1259 1371 C ATOM 656 O VAL A 206 51.055 -3.477 3.377 1.00 73.33 O ANISOU 656 O VAL A 206 10190 10288 7384 1734 1142 1233 O ATOM 657 CB VAL A 206 52.865 -4.681 1.177 1.00 63.74 C ANISOU 657 CB VAL A 206 8534 9585 6100 2167 1256 1713 C ATOM 658 CG1 VAL A 206 51.950 -5.761 0.616 1.00 58.73 C ANISOU 658 CG1 VAL A 206 7895 9135 5283 2582 1116 1527 C ATOM 659 CG2 VAL A 206 54.127 -4.556 0.343 1.00 71.48 C ANISOU 659 CG2 VAL A 206 9356 10685 7117 2213 1444 2073 C ATOM 660 N TYR A 207 49.726 -3.497 1.567 1.00 66.32 N ANISOU 660 N TYR A 207 9394 9549 6257 2546 1257 1280 N ATOM 661 CA TYR A 207 48.494 -3.490 2.345 1.00 65.66 C ANISOU 661 CA TYR A 207 9399 9405 6143 2568 1161 1046 C ATOM 662 C TYR A 207 47.714 -4.790 2.187 1.00 67.58 C ANISOU 662 C TYR A 207 9428 9952 6299 2756 920 844 C ATOM 663 O TYR A 207 47.342 -5.170 1.078 1.00 60.99 O ANISOU 663 O TYR A 207 8525 9337 5312 3114 886 861 O ATOM 664 CB TYR A 207 47.614 -2.307 1.938 1.00 69.74 C ANISOU 664 CB TYR A 207 10191 9750 6558 2884 1387 1132 C ATOM 665 CG TYR A 207 48.310 -0.967 2.008 1.00 79.83 C ANISOU 665 CG TYR A 207 11777 10644 7910 2701 1687 1328 C ATOM 666 CD1 TYR A 207 48.986 -0.455 0.907 1.00 76.82 C ANISOU 666 CD1 TYR A 207 11449 10231 7508 2870 1909 1596 C ATOM 667 CD2 TYR A 207 48.286 -0.209 3.172 1.00 78.10 C ANISOU 667 CD2 TYR A 207 11836 10067 7769 2349 1768 1241 C ATOM 668 CE1 TYR A 207 49.622 0.770 0.965 1.00 83.44 C ANISOU 668 CE1 TYR A 207 12588 10679 8437 2649 2216 1778 C ATOM 669 CE2 TYR A 207 48.920 1.019 3.239 1.00 84.74 C ANISOU 669 CE2 TYR A 207 13019 10505 8672 2111 2051 1388 C ATOM 670 CZ TYR A 207 49.586 1.503 2.132 1.00 90.77 C ANISOU 670 CZ TYR A 207 13809 11232 9449 2242 2280 1659 C ATOM 671 OH TYR A 207 50.219 2.724 2.190 1.00 95.33 O ANISOU 671 OH TYR A 207 14742 11370 10108 1956 2594 1808 O ATOM 672 N LEU A 208 47.471 -5.462 3.307 1.00 66.66 N ANISOU 672 N LEU A 208 9230 9834 6265 2498 762 645 N ATOM 673 CA LEU A 208 46.671 -6.681 3.325 1.00 64.29 C ANISOU 673 CA LEU A 208 8759 9754 5916 2590 565 434 C ATOM 674 C LEU A 208 45.286 -6.404 3.899 1.00 67.25 C ANISOU 674 C LEU A 208 9160 10111 6281 2664 548 297 C ATOM 675 O LEU A 208 45.152 -5.814 4.973 1.00 70.52 O ANISOU 675 O LEU A 208 9712 10307 6775 2485 623 277 O ATOM 676 CB LEU A 208 47.367 -7.777 4.137 1.00 64.47 C ANISOU 676 CB LEU A 208 8663 9804 6030 2301 446 346 C ATOM 677 CG LEU A 208 48.290 -8.745 3.393 1.00 56.32 C ANISOU 677 CG LEU A 208 7524 8934 4940 2380 415 425 C ATOM 678 CD1 LEU A 208 49.430 -8.009 2.704 1.00 54.66 C ANISOU 678 CD1 LEU A 208 7330 8709 4728 2424 568 709 C ATOM 679 CD2 LEU A 208 48.832 -9.804 4.351 1.00 50.41 C ANISOU 679 CD2 LEU A 208 6687 8208 4258 2154 339 358 C ATOM 680 N ILE A 209 44.259 -6.839 3.178 1.00 59.99 N ANISOU 680 N ILE A 209 8102 9446 5244 2931 447 209 N ATOM 681 CA ILE A 209 42.878 -6.626 3.591 1.00 62.93 C ANISOU 681 CA ILE A 209 8408 9906 5598 3050 434 128 C ATOM 682 C ILE A 209 42.332 -7.874 4.272 1.00 69.40 C ANISOU 682 C ILE A 209 9029 10835 6507 2830 258 -99 C ATOM 683 O ILE A 209 41.913 -8.823 3.607 1.00 60.66 O ANISOU 683 O ILE A 209 7742 9975 5331 2864 88 -234 O ATOM 684 CB ILE A 209 41.987 -6.261 2.392 1.00 70.45 C ANISOU 684 CB ILE A 209 9266 11153 6347 3477 419 196 C ATOM 685 CG1 ILE A 209 42.657 -5.171 1.552 1.00 70.94 C ANISOU 685 CG1 ILE A 209 9552 11096 6308 3730 628 443 C ATOM 686 CG2 ILE A 209 40.609 -5.823 2.864 1.00 64.09 C ANISOU 686 CG2 ILE A 209 8362 10472 5515 3649 459 199 C ATOM 687 CD1 ILE A 209 41.873 -4.776 0.324 1.00 68.96 C ANISOU 687 CD1 ILE A 209 9233 11162 5808 4223 633 548 C ATOM 688 N LEU A 210 42.338 -7.860 5.602 1.00 68.43 N ANISOU 688 N LEU A 210 8975 10505 6520 2596 314 -144 N ATOM 689 CA LEU A 210 41.983 -9.034 6.391 1.00 64.89 C ANISOU 689 CA LEU A 210 8387 10091 6177 2372 211 -324 C ATOM 690 C LEU A 210 40.577 -8.953 6.975 1.00 61.70 C ANISOU 690 C LEU A 210 7850 9782 5811 2441 239 -371 C ATOM 691 O LEU A 210 40.020 -7.868 7.145 1.00 58.12 O ANISOU 691 O LEU A 210 7482 9292 5310 2650 380 -245 O ATOM 692 CB LEU A 210 42.995 -9.230 7.524 1.00 60.60 C ANISOU 692 CB LEU A 210 7988 9301 5734 2092 254 -324 C ATOM 693 CG LEU A 210 44.448 -9.464 7.108 1.00 62.74 C ANISOU 693 CG LEU A 210 8308 9544 5986 1998 231 -240 C ATOM 694 CD1 LEU A 210 45.392 -9.229 8.275 1.00 67.29 C ANISOU 694 CD1 LEU A 210 9003 9941 6624 1741 269 -190 C ATOM 695 CD2 LEU A 210 44.615 -10.873 6.561 1.00 52.43 C ANISOU 695 CD2 LEU A 210 6882 8384 4655 1995 129 -341 C ATOM 696 N GLU A 211 40.014 -10.118 7.278 1.00 49.41 N ANISOU 696 N GLU A 211 6097 8339 4338 2276 139 -533 N ATOM 697 CA GLU A 211 38.748 -10.204 7.990 1.00 53.81 C ANISOU 697 CA GLU A 211 6478 8993 4975 2283 187 -557 C ATOM 698 C GLU A 211 38.891 -9.635 9.403 1.00 58.56 C ANISOU 698 C GLU A 211 7306 9298 5647 2241 377 -482 C ATOM 699 O GLU A 211 39.895 -9.867 10.077 1.00 59.64 O ANISOU 699 O GLU A 211 7642 9197 5821 2047 394 -511 O ATOM 700 CB GLU A 211 38.269 -11.656 8.046 1.00 53.36 C ANISOU 700 CB GLU A 211 6198 9057 5019 2032 67 -751 C ATOM 701 CG GLU A 211 37.090 -11.886 8.977 1.00 68.67 C ANISOU 701 CG GLU A 211 7937 11062 7093 1970 156 -755 C ATOM 702 CD GLU A 211 36.755 -13.353 9.140 1.00 68.03 C ANISOU 702 CD GLU A 211 7700 11006 7143 1648 89 -946 C ATOM 703 OE1 GLU A 211 35.848 -13.667 9.938 1.00 61.83 O ANISOU 703 OE1 GLU A 211 6738 10256 6499 1555 190 -938 O ATOM 704 OE2 GLU A 211 37.399 -14.191 8.472 1.00 59.25 O ANISOU 704 OE2 GLU A 211 6672 9853 5987 1499 -29 -1091 O ATOM 705 N TYR A 212 37.887 -8.885 9.844 1.00 58.30 N ANISOU 705 N TYR A 212 7249 9306 5598 2450 522 -372 N ATOM 706 CA TYR A 212 37.914 -8.270 11.167 1.00 56.98 C ANISOU 706 CA TYR A 212 7366 8840 5444 2459 723 -306 C ATOM 707 C TYR A 212 37.484 -9.252 12.254 1.00 62.81 C ANISOU 707 C TYR A 212 7996 9550 6320 2280 757 -390 C ATOM 708 O TYR A 212 36.441 -9.898 12.145 1.00 54.05 O ANISOU 708 O TYR A 212 6546 8691 5300 2287 741 -407 O ATOM 709 CB TYR A 212 37.017 -7.031 11.190 1.00 59.93 C ANISOU 709 CB TYR A 212 7831 9234 5707 2836 932 -118 C ATOM 710 CG TYR A 212 36.775 -6.444 12.566 1.00 69.42 C ANISOU 710 CG TYR A 212 9354 10137 6885 2903 1173 -53 C ATOM 711 CD1 TYR A 212 37.831 -6.003 13.354 1.00 55.58 C ANISOU 711 CD1 TYR A 212 8049 7986 5081 2711 1220 -111 C ATOM 712 CD2 TYR A 212 35.486 -6.316 13.068 1.00 76.98 C ANISOU 712 CD2 TYR A 212 10164 11236 7847 3164 1353 74 C ATOM 713 CE1 TYR A 212 37.606 -5.458 14.612 1.00 74.32 C ANISOU 713 CE1 TYR A 212 10783 10075 7381 2776 1428 -81 C ATOM 714 CE2 TYR A 212 35.253 -5.771 14.315 1.00 75.79 C ANISOU 714 CE2 TYR A 212 10364 10794 7637 3281 1606 145 C ATOM 715 CZ TYR A 212 36.315 -5.344 15.083 1.00 73.30 C ANISOU 715 CZ TYR A 212 10560 10048 7243 3086 1637 49 C ATOM 716 OH TYR A 212 36.078 -4.804 16.326 1.00 84.09 O ANISOU 716 OH TYR A 212 12335 11114 8500 3204 1876 91 O ATOM 717 N ALA A 213 38.298 -9.363 13.299 1.00 57.93 N ANISOU 717 N ALA A 213 7658 8645 5709 2111 806 -432 N ATOM 718 CA ALA A 213 37.973 -10.216 14.436 1.00 63.35 C ANISOU 718 CA ALA A 213 8314 9261 6495 1994 889 -480 C ATOM 719 C ALA A 213 37.668 -9.355 15.659 1.00 55.99 C ANISOU 719 C ALA A 213 7694 8102 5478 2148 1106 -389 C ATOM 720 O ALA A 213 38.582 -8.850 16.309 1.00 56.93 O ANISOU 720 O ALA A 213 8179 7969 5482 2065 1111 -414 O ATOM 721 CB ALA A 213 39.109 -11.180 14.721 1.00 51.58 C ANISOU 721 CB ALA A 213 6897 7669 5032 1738 785 -586 C ATOM 722 N PRO A 214 36.372 -9.189 15.969 1.00 52.36 N ANISOU 722 N PRO A 214 7088 7751 5056 2372 1286 -277 N ATOM 723 CA PRO A 214 35.841 -8.230 16.948 1.00 53.87 C ANISOU 723 CA PRO A 214 7594 7747 5127 2639 1551 -146 C ATOM 724 C PRO A 214 36.311 -8.434 18.390 1.00 63.66 C ANISOU 724 C PRO A 214 9186 8695 6307 2545 1648 -200 C ATOM 725 O PRO A 214 36.387 -7.457 19.138 1.00 55.10 O ANISOU 725 O PRO A 214 8555 7344 5037 2697 1807 -157 O ATOM 726 CB PRO A 214 34.324 -8.449 16.866 1.00 56.31 C ANISOU 726 CB PRO A 214 7494 8362 5541 2872 1702 9 C ATOM 727 CG PRO A 214 34.091 -9.102 15.564 1.00 63.77 C ANISOU 727 CG PRO A 214 7954 9675 6602 2740 1469 -52 C ATOM 728 CD PRO A 214 35.294 -9.951 15.316 1.00 66.21 C ANISOU 728 CD PRO A 214 8332 9863 6961 2377 1243 -261 C ATOM 729 N LEU A 215 36.602 -9.670 18.785 1.00 53.03 N ANISOU 729 N LEU A 215 7680 7387 5082 2321 1574 -291 N ATOM 730 CA LEU A 215 36.912 -9.940 20.187 1.00 64.01 C ANISOU 730 CA LEU A 215 9372 8560 6390 2302 1688 -310 C ATOM 731 C LEU A 215 38.410 -10.082 20.446 1.00 64.48 C ANISOU 731 C LEU A 215 9674 8498 6327 2056 1483 -440 C ATOM 732 O LEU A 215 38.820 -10.528 21.517 1.00 68.47 O ANISOU 732 O LEU A 215 10367 8902 6746 2018 1520 -468 O ATOM 733 CB LEU A 215 36.178 -11.195 20.665 1.00 62.30 C ANISOU 733 CB LEU A 215 8861 8445 6364 2279 1824 -272 C ATOM 734 CG LEU A 215 34.648 -11.133 20.612 1.00 67.55 C ANISOU 734 CG LEU A 215 9215 9287 7163 2496 2047 -106 C ATOM 735 CD1 LEU A 215 34.031 -12.300 21.370 1.00 60.89 C ANISOU 735 CD1 LEU A 215 8174 8462 6501 2436 2239 -53 C ATOM 736 CD2 LEU A 215 34.130 -9.807 21.144 1.00 73.44 C ANISOU 736 CD2 LEU A 215 10282 9907 7716 2863 2267 46 C ATOM 737 N GLY A 216 39.221 -9.700 19.465 1.00 53.87 N ANISOU 737 N GLY A 216 8303 7204 4963 1913 1278 -493 N ATOM 738 CA GLY A 216 40.659 -9.637 19.652 1.00 57.63 C ANISOU 738 CA GLY A 216 8963 7621 5314 1681 1085 -573 C ATOM 739 C GLY A 216 41.354 -10.981 19.761 1.00 58.95 C ANISOU 739 C GLY A 216 8930 7925 5545 1539 982 -604 C ATOM 740 O GLY A 216 40.818 -12.009 19.350 1.00 62.97 O ANISOU 740 O GLY A 216 9154 8545 6225 1561 1033 -598 O ATOM 741 N THR A 217 42.558 -10.966 20.326 1.00 53.69 N ANISOU 741 N THR A 217 8425 7254 4720 1390 845 -632 N ATOM 742 CA THR A 217 43.392 -12.160 20.396 1.00 51.93 C ANISOU 742 CA THR A 217 8034 7189 4507 1316 764 -614 C ATOM 743 C THR A 217 43.056 -13.056 21.575 1.00 58.44 C ANISOU 743 C THR A 217 8935 7973 5297 1440 927 -588 C ATOM 744 O THR A 217 42.466 -12.618 22.564 1.00 59.73 O ANISOU 744 O THR A 217 9336 7995 5365 1553 1058 -592 O ATOM 745 CB THR A 217 44.888 -11.800 20.492 1.00 54.96 C ANISOU 745 CB THR A 217 8477 7688 4718 1126 540 -603 C ATOM 746 OG1 THR A 217 45.114 -10.960 21.632 1.00 58.68 O ANISOU 746 OG1 THR A 217 9283 8048 4965 1058 501 -656 O ATOM 747 CG2 THR A 217 45.339 -11.080 19.240 1.00 54.99 C ANISOU 747 CG2 THR A 217 8375 7736 4783 1001 416 -590 C ATOM 748 N VAL A 218 43.445 -14.320 21.460 1.00 58.42 N ANISOU 748 N VAL A 218 8770 8072 5353 1454 958 -546 N ATOM 749 CA VAL A 218 43.353 -15.246 22.576 1.00 62.38 C ANISOU 749 CA VAL A 218 9371 8535 5795 1591 1136 -490 C ATOM 750 C VAL A 218 44.413 -14.855 23.604 1.00 60.81 C ANISOU 750 C VAL A 218 9382 8435 5289 1593 995 -465 C ATOM 751 O VAL A 218 44.241 -15.061 24.807 1.00 60.12 O ANISOU 751 O VAL A 218 9497 8296 5051 1742 1118 -434 O ATOM 752 CB VAL A 218 43.538 -16.707 22.112 1.00 47.69 C ANISOU 752 CB VAL A 218 7349 6715 4058 1620 1249 -440 C ATOM 753 CG1 VAL A 218 43.473 -17.665 23.289 1.00 55.78 C ANISOU 753 CG1 VAL A 218 8518 7667 5007 1800 1490 -350 C ATOM 754 CG2 VAL A 218 42.471 -17.066 21.089 1.00 52.11 C ANISOU 754 CG2 VAL A 218 7712 7196 4892 1542 1340 -510 C ATOM 755 N TYR A 219 45.501 -14.267 23.112 1.00 63.29 N ANISOU 755 N TYR A 219 9633 8914 5500 1416 730 -475 N ATOM 756 CA TYR A 219 46.576 -13.769 23.964 1.00 61.35 C ANISOU 756 CA TYR A 219 9525 8832 4954 1321 522 -471 C ATOM 757 C TYR A 219 46.068 -12.730 24.958 1.00 64.85 C ANISOU 757 C TYR A 219 10344 9077 5220 1304 530 -584 C ATOM 758 O TYR A 219 46.396 -12.780 26.145 1.00 64.47 O ANISOU 758 O TYR A 219 10504 9092 4901 1368 493 -589 O ATOM 759 CB TYR A 219 47.698 -13.169 23.113 1.00 59.71 C ANISOU 759 CB TYR A 219 9140 8822 4725 1066 254 -456 C ATOM 760 CG TYR A 219 48.811 -12.542 23.922 1.00 75.68 C ANISOU 760 CG TYR A 219 11250 11057 6449 862 -9 -470 C ATOM 761 CD1 TYR A 219 49.786 -13.327 24.522 1.00 72.50 C ANISOU 761 CD1 TYR A 219 10693 11010 5843 943 -106 -338 C ATOM 762 CD2 TYR A 219 48.885 -11.164 24.088 1.00 80.65 C ANISOU 762 CD2 TYR A 219 12126 11541 6976 583 -156 -612 C ATOM 763 CE1 TYR A 219 50.805 -12.759 25.263 1.00 88.32 C ANISOU 763 CE1 TYR A 219 12719 13292 7548 722 -395 -354 C ATOM 764 CE2 TYR A 219 49.900 -10.587 24.829 1.00 83.30 C ANISOU 764 CE2 TYR A 219 12550 12076 7026 310 -429 -661 C ATOM 765 CZ TYR A 219 50.856 -11.389 25.413 1.00 86.97 C ANISOU 765 CZ TYR A 219 12789 12966 7291 365 -575 -536 C ATOM 766 OH TYR A 219 51.868 -10.819 26.150 1.00 98.18 O ANISOU 766 OH TYR A 219 14237 14665 8402 61 -894 -588 O ATOM 767 N ARG A 220 45.270 -11.787 24.467 1.00 58.56 N ANISOU 767 N ARG A 220 9666 8046 4540 1258 592 -662 N ATOM 768 CA ARG A 220 44.677 -10.770 25.328 1.00 59.39 C ANISOU 768 CA ARG A 220 10199 7899 4467 1302 670 -753 C ATOM 769 C ARG A 220 43.689 -11.408 26.299 1.00 65.42 C ANISOU 769 C ARG A 220 11093 8550 5215 1621 958 -695 C ATOM 770 O ARG A 220 43.589 -11.001 27.459 1.00 63.26 O ANISOU 770 O ARG A 220 11203 8161 4671 1719 1005 -740 O ATOM 771 CB ARG A 220 43.985 -9.690 24.494 1.00 63.23 C ANISOU 771 CB ARG A 220 10776 8165 5083 1272 745 -792 C ATOM 772 CG ARG A 220 43.412 -8.546 25.315 1.00 78.90 C ANISOU 772 CG ARG A 220 13286 9840 6851 1354 872 -869 C ATOM 773 N GLU A 221 42.966 -12.417 25.823 1.00 57.40 N ANISOU 773 N GLU A 221 9774 7558 4479 1767 1159 -597 N ATOM 774 CA AGLU A 221 41.997 -13.126 26.651 0.56 61.57 C ANISOU 774 CA AGLU A 221 10360 7980 5053 2038 1476 -508 C ATOM 775 CA BGLU A 221 41.997 -13.113 26.662 0.44 61.56 C ANISOU 775 CA BGLU A 221 10365 7978 5049 2039 1475 -509 C ATOM 776 C GLU A 221 42.700 -13.906 27.758 1.00 66.87 C ANISOU 776 C GLU A 221 11162 8756 5488 2154 1483 -456 C ATOM 777 O GLU A 221 42.243 -13.937 28.901 1.00 64.42 O ANISOU 777 O GLU A 221 11129 8335 5011 2384 1676 -414 O ATOM 778 CB AGLU A 221 41.150 -14.070 25.794 0.56 59.76 C ANISOU 778 CB AGLU A 221 9750 7765 5192 2063 1661 -436 C ATOM 779 CB BGLU A 221 41.119 -14.043 25.825 0.44 60.01 C ANISOU 779 CB BGLU A 221 9792 7791 5220 2069 1667 -435 C ATOM 780 CG AGLU A 221 40.013 -14.750 26.544 0.56 61.23 C ANISOU 780 CG AGLU A 221 9941 7830 5493 2287 2027 -323 C ATOM 781 CG BGLU A 221 39.985 -14.677 26.616 0.44 60.92 C ANISOU 781 CG BGLU A 221 9928 7781 5438 2300 2033 -322 C ATOM 782 CD AGLU A 221 38.855 -13.812 26.835 0.56 65.58 C ANISOU 782 CD AGLU A 221 10618 8245 6053 2456 2214 -279 C ATOM 783 CD BGLU A 221 39.163 -15.643 25.790 0.44 61.76 C ANISOU 783 CD BGLU A 221 9645 7910 5909 2225 2193 -276 C ATOM 784 OE1AGLU A 221 38.850 -12.679 26.307 0.56 62.04 O ANISOU 784 OE1AGLU A 221 10252 7774 5547 2406 2077 -343 O ATOM 785 OE1BGLU A 221 37.925 -15.656 25.951 0.44 61.65 O ANISOU 785 OE1BGLU A 221 9525 7834 6066 2328 2447 -192 O ATOM 786 OE2AGLU A 221 37.945 -14.211 27.592 0.56 82.98 O ANISOU 786 OE2AGLU A 221 12851 10361 8316 2671 2537 -153 O ATOM 787 OE2BGLU A 221 39.754 -16.394 24.986 0.44 66.52 O ANISOU 787 OE2BGLU A 221 10056 8603 6617 2058 2071 -321 O ATOM 788 N LEU A 222 43.814 -14.540 27.405 1.00 59.47 N ANISOU 788 N LEU A 222 10026 8056 4515 2043 1293 -430 N ATOM 789 CA LEU A 222 44.599 -15.301 28.366 1.00 64.21 C ANISOU 789 CA LEU A 222 10705 8836 4855 2198 1286 -342 C ATOM 790 C LEU A 222 45.201 -14.372 29.416 1.00 66.58 C ANISOU 790 C LEU A 222 11344 9215 4740 2159 1062 -434 C ATOM 791 O LEU A 222 45.262 -14.712 30.594 1.00 73.57 O ANISOU 791 O LEU A 222 12456 10143 5353 2393 1151 -381 O ATOM 792 CB LEU A 222 45.703 -16.091 27.663 1.00 60.53 C ANISOU 792 CB LEU A 222 9934 8647 4418 2126 1140 -255 C ATOM 793 CG LEU A 222 46.542 -16.982 28.582 1.00 71.00 C ANISOU 793 CG LEU A 222 11298 10221 5460 2364 1167 -104 C ATOM 794 CD1 LEU A 222 45.662 -18.011 29.277 1.00 59.30 C ANISOU 794 CD1 LEU A 222 9956 8525 4050 2690 1595 11 C ATOM 795 CD2 LEU A 222 47.663 -17.661 27.811 1.00 72.20 C ANISOU 795 CD2 LEU A 222 11144 10670 5619 2340 1045 22 C ATOM 796 N GLN A 223 45.640 -13.198 28.974 1.00 65.56 N ANISOU 796 N GLN A 223 11276 9088 4546 1853 782 -577 N ATOM 797 CA GLN A 223 46.195 -12.192 29.868 1.00 72.53 C ANISOU 797 CA GLN A 223 12530 9996 5033 1708 543 -720 C ATOM 798 C GLN A 223 45.110 -11.653 30.799 1.00 70.35 C ANISOU 798 C GLN A 223 12736 9376 4616 1939 793 -781 C ATOM 799 O GLN A 223 45.368 -11.342 31.963 1.00 78.41 O ANISOU 799 O GLN A 223 14142 10411 5238 2006 716 -857 O ATOM 800 CB GLN A 223 46.827 -11.052 29.064 1.00 82.24 C ANISOU 800 CB GLN A 223 13739 11226 6283 1281 249 -857 C ATOM 801 CG GLN A 223 48.330 -10.918 29.244 1.00 97.77 C ANISOU 801 CG GLN A 223 15564 13593 7992 973 -154 -883 C ATOM 802 CD GLN A 223 48.889 -9.682 28.566 1.00100.76 C ANISOU 802 CD GLN A 223 15986 13908 8390 504 -401 -1022 C ATOM 803 OE1 GLN A 223 48.210 -9.038 27.767 1.00 99.63 O ANISOU 803 OE1 GLN A 223 15933 13437 8484 458 -252 -1066 O ATOM 804 NE2 GLN A 223 50.132 -9.343 28.886 1.00116.87 N ANISOU 804 NE2 GLN A 223 17952 16281 10172 153 -769 -1075 N ATOM 805 N LYS A 224 43.895 -11.553 30.272 1.00 63.24 N ANISOU 805 N LYS A 224 11806 8201 4022 2081 1094 -733 N ATOM 806 CA LYS A 224 42.748 -11.084 31.037 1.00 67.78 C ANISOU 806 CA LYS A 224 12778 8467 4508 2369 1404 -723 C ATOM 807 C LYS A 224 42.309 -12.116 32.071 1.00 79.55 C ANISOU 807 C LYS A 224 14234 9968 6023 2692 1646 -549 C ATOM 808 O LYS A 224 41.912 -11.766 33.179 1.00 73.29 O ANISOU 808 O LYS A 224 13752 9004 5089 2863 1737 -519 O ATOM 809 CB LYS A 224 41.581 -10.758 30.101 1.00 84.45 C ANISOU 809 CB LYS A 224 14723 10383 6981 2439 1645 -657 C ATOM 810 CG LYS A 224 40.570 -9.774 30.668 1.00 85.55 C ANISOU 810 CG LYS A 224 15235 10202 7066 2642 1868 -625 C ATOM 811 CD LYS A 224 39.343 -9.673 29.772 1.00 99.08 C ANISOU 811 CD LYS A 224 16690 11847 9111 2802 2144 -494 C ATOM 812 CE LYS A 224 38.709 -11.041 29.563 1.00104.64 C ANISOU 812 CE LYS A 224 16923 12713 10122 2936 2365 -335 C ATOM 813 NZ LYS A 224 37.555 -11.008 28.624 1.00101.72 N ANISOU 813 NZ LYS A 224 16195 12375 10081 3025 2571 -218 N ATOM 814 N LEU A 225 42.391 -13.389 31.702 1.00 73.12 N ANISOU 814 N LEU A 225 13061 9324 5397 2775 1764 -421 N ATOM 815 CA LEU A 225 41.855 -14.467 32.527 1.00 62.91 C ANISOU 815 CA LEU A 225 11703 7977 4225 3060 2056 -220 C ATOM 816 C LEU A 225 42.923 -15.237 33.296 1.00 83.01 C ANISOU 816 C LEU A 225 14260 10767 6513 3150 1923 -160 C ATOM 817 O LEU A 225 42.595 -16.123 34.090 1.00 79.42 O ANISOU 817 O LEU A 225 13806 10249 6119 3410 2159 21 O ATOM 818 CB LEU A 225 41.061 -15.441 31.654 1.00 74.97 C ANISOU 818 CB LEU A 225 12846 9452 6186 3079 2346 -98 C ATOM 819 CG LEU A 225 39.540 -15.454 31.796 1.00 81.99 C ANISOU 819 CG LEU A 225 13670 10107 7377 3216 2694 38 C ATOM 820 CD1 LEU A 225 38.964 -14.067 31.586 1.00 77.89 C ANISOU 820 CD1 LEU A 225 13320 9465 6810 3204 2653 -40 C ATOM 821 CD2 LEU A 225 38.941 -16.439 30.801 1.00 69.52 C ANISOU 821 CD2 LEU A 225 11672 8540 6203 3114 2902 100 C ATOM 822 N SER A 226 44.189 -14.905 33.046 1.00 76.41 N ANISOU 822 N SER A 226 13406 10229 5396 2940 1546 -280 N ATOM 823 CA SER A 226 45.345 -15.594 33.635 1.00 71.75 C ANISOU 823 CA SER A 226 12732 9992 4538 3020 1368 -196 C ATOM 824 C SER A 226 45.486 -17.042 33.151 1.00 70.44 C ANISOU 824 C SER A 226 12236 9920 4607 3189 1591 14 C ATOM 825 O SER A 226 46.583 -17.479 32.804 1.00 68.65 O ANISOU 825 O SER A 226 11793 10038 4252 3153 1401 78 O ATOM 826 CB SER A 226 45.282 -15.562 35.166 1.00 81.86 C ANISOU 826 CB SER A 226 14306 11237 5561 3255 1397 -158 C ATOM 827 OG SER A 226 46.570 -15.745 35.721 1.00 86.17 O ANISOU 827 OG SER A 226 14793 12207 5739 3237 1083 -150 O ATOM 828 N LYS A 227 44.380 -17.781 33.131 1.00 66.11 N ANISOU 828 N LYS A 227 11648 9058 4413 3353 1993 138 N ATOM 829 CA LYS A 227 44.383 -19.162 32.661 1.00 74.80 C ANISOU 829 CA LYS A 227 12511 10129 5782 3452 2239 314 C ATOM 830 C LYS A 227 42.978 -19.618 32.280 1.00 76.30 C ANISOU 830 C LYS A 227 12625 9948 6418 3420 2609 363 C ATOM 831 O LYS A 227 41.991 -19.172 32.866 1.00 74.01 O ANISOU 831 O LYS A 227 12472 9449 6199 3483 2756 376 O ATOM 832 CB LYS A 227 44.964 -20.091 33.730 1.00 85.85 C ANISOU 832 CB LYS A 227 13975 11635 7010 3766 2317 518 C ATOM 833 N PHE A 228 42.896 -20.508 31.296 1.00 68.51 N ANISOU 833 N PHE A 228 11413 8899 5717 3310 2751 396 N ATOM 834 CA PHE A 228 41.618 -21.055 30.852 1.00 68.37 C ANISOU 834 CA PHE A 228 11276 8585 6117 3202 3076 423 C ATOM 835 C PHE A 228 41.293 -22.349 31.591 1.00 74.95 C ANISOU 835 C PHE A 228 12187 9204 7088 3360 3405 645 C ATOM 836 O PHE A 228 42.194 -23.122 31.920 1.00 75.24 O ANISOU 836 O PHE A 228 12297 9312 6980 3525 3395 772 O ATOM 837 CB PHE A 228 41.631 -21.323 29.343 1.00 59.64 C ANISOU 837 CB PHE A 228 9932 7494 5233 2954 3058 298 C ATOM 838 CG PHE A 228 41.922 -20.110 28.501 1.00 64.06 C ANISOU 838 CG PHE A 228 10398 8235 5706 2779 2725 109 C ATOM 839 CD1 PHE A 228 41.616 -18.836 28.953 1.00 67.79 C ANISOU 839 CD1 PHE A 228 10994 8723 6040 2785 2578 36 C ATOM 840 CD2 PHE A 228 42.494 -20.250 27.244 1.00 56.89 C ANISOU 840 CD2 PHE A 228 9271 7431 4914 2558 2507 31 C ATOM 841 CE1 PHE A 228 41.881 -17.725 28.173 1.00 69.74 C ANISOU 841 CE1 PHE A 228 11151 9067 6281 2557 2234 -109 C ATOM 842 CE2 PHE A 228 42.762 -19.143 26.458 1.00 61.75 C ANISOU 842 CE2 PHE A 228 9758 8177 5525 2345 2152 -102 C ATOM 843 CZ PHE A 228 42.455 -17.879 26.922 1.00 67.11 C ANISOU 843 CZ PHE A 228 10564 8851 6083 2335 2023 -170 C ATOM 844 N ASP A 229 40.010 -22.594 31.841 1.00 73.82 N ANISOU 844 N ASP A 229 12022 8808 7219 3323 3713 715 N ATOM 845 CA ASP A 229 39.591 -23.870 32.410 1.00 66.27 C ANISOU 845 CA ASP A 229 11150 7594 6434 3415 4076 925 C ATOM 846 C ASP A 229 39.602 -24.943 31.325 1.00 78.73 C ANISOU 846 C ASP A 229 12610 9031 8272 3189 4246 876 C ATOM 847 O ASP A 229 39.862 -24.651 30.155 1.00 71.57 O ANISOU 847 O ASP A 229 11538 8244 7412 2981 4074 683 O ATOM 848 CB ASP A 229 38.206 -23.764 33.064 1.00 70.28 C ANISOU 848 CB ASP A 229 11662 7898 7142 3445 4380 1041 C ATOM 849 CG ASP A 229 37.179 -23.090 32.173 1.00 84.00 C ANISOU 849 CG ASP A 229 13122 9656 9136 3199 4418 895 C ATOM 850 OD1 ASP A 229 37.200 -23.310 30.945 1.00 89.86 O ANISOU 850 OD1 ASP A 229 13653 10435 10055 2938 4391 730 O ATOM 851 OD2 ASP A 229 36.336 -22.340 32.711 1.00 90.74 O ANISOU 851 OD2 ASP A 229 13976 10500 10001 3300 4488 963 O ATOM 852 N GLU A 230 39.325 -26.184 31.711 1.00 67.15 N ANISOU 852 N GLU A 230 10471 8091 6953 297 2608 791 N ATOM 853 CA GLU A 230 39.415 -27.303 30.780 1.00 68.22 C ANISOU 853 CA GLU A 230 10096 8120 7705 -106 2485 840 C ATOM 854 C GLU A 230 38.366 -27.228 29.673 1.00 79.30 C ANISOU 854 C GLU A 230 10921 9909 9299 38 2612 635 C ATOM 855 O GLU A 230 38.613 -27.667 28.550 1.00 70.71 O ANISOU 855 O GLU A 230 9563 8672 8632 -146 2409 497 O ATOM 856 CB GLU A 230 39.296 -28.629 31.531 1.00 60.58 C ANISOU 856 CB GLU A 230 8927 7167 6925 -579 2600 1206 C ATOM 857 CG GLU A 230 40.422 -28.862 32.522 1.00 71.71 C ANISOU 857 CG GLU A 230 10840 8194 8212 -777 2412 1471 C ATOM 858 CD GLU A 230 40.526 -30.306 32.960 1.00 82.01 C ANISOU 858 CD GLU A 230 11925 9354 9879 -1281 2421 1860 C ATOM 859 OE1 GLU A 230 39.618 -30.786 33.672 1.00 91.13 O ANISOU 859 OE1 GLU A 230 12847 10886 10893 -1427 2725 2119 O ATOM 860 OE2 GLU A 230 41.520 -30.963 32.587 1.00 85.37 O ANISOU 860 OE2 GLU A 230 12405 9293 10739 -1515 2131 1936 O ATOM 861 N GLN A 231 37.203 -26.667 29.987 1.00 68.43 N ANISOU 861 N GLN A 231 9348 9068 7585 391 2948 619 N ATOM 862 CA GLN A 231 36.140 -26.532 28.997 1.00 70.78 C ANISOU 862 CA GLN A 231 9045 9826 8023 553 3059 484 C ATOM 863 C GLN A 231 36.538 -25.566 27.883 1.00 74.32 C ANISOU 863 C GLN A 231 9640 10091 8509 888 2802 186 C ATOM 864 O GLN A 231 36.356 -25.857 26.701 1.00 78.01 O ANISOU 864 O GLN A 231 9692 10653 9295 756 2654 63 O ATOM 865 CB GLN A 231 34.844 -26.065 29.658 1.00 87.73 C ANISOU 865 CB GLN A 231 10927 12640 9769 946 3504 587 C ATOM 866 CG GLN A 231 33.690 -25.884 28.686 1.00 97.98 C ANISOU 866 CG GLN A 231 11531 14506 11191 1140 3613 516 C ATOM 867 CD GLN A 231 32.417 -25.436 29.374 1.00105.06 C ANISOU 867 CD GLN A 231 12094 16132 11692 1588 4091 671 C ATOM 868 OE1 GLN A 231 32.363 -25.332 30.599 1.00119.84 O ANISOU 868 OE1 GLN A 231 14258 18104 13171 1733 4373 814 O ATOM 869 NE2 GLN A 231 31.382 -25.168 28.586 1.00102.88 N ANISOU 869 NE2 GLN A 231 11207 16369 11515 1791 4130 637 N ATOM 870 N ARG A 232 37.089 -24.419 28.268 1.00 65.42 N ANISOU 870 N ARG A 232 9129 8694 7033 1291 2729 83 N ATOM 871 CA ARG A 232 37.488 -23.398 27.308 1.00 71.13 C ANISOU 871 CA ARG A 232 10051 9211 7762 1605 2477 -127 C ATOM 872 C ARG A 232 38.693 -23.850 26.491 1.00 79.84 C ANISOU 872 C ARG A 232 11220 9883 9235 1213 2089 -159 C ATOM 873 O ARG A 232 38.746 -23.652 25.274 1.00 66.46 O ANISOU 873 O ARG A 232 9285 8237 7729 1257 1918 -286 O ATOM 874 CB ARG A 232 37.804 -22.088 28.030 1.00 71.63 C ANISOU 874 CB ARG A 232 10841 9005 7369 2071 2464 -213 C ATOM 875 CG ARG A 232 37.951 -20.889 27.112 1.00 76.44 C ANISOU 875 CG ARG A 232 11648 9442 7953 2467 2251 -377 C ATOM 876 CD ARG A 232 38.199 -19.624 27.915 1.00 84.45 C ANISOU 876 CD ARG A 232 13458 10103 8526 2898 2223 -480 C ATOM 877 NE ARG A 232 37.706 -18.438 27.223 1.00 96.34 N ANISOU 877 NE ARG A 232 14909 11634 10061 3290 2067 -532 N ATOM 878 CZ ARG A 232 36.459 -17.988 27.315 1.00107.00 C ANISOU 878 CZ ARG A 232 15936 13397 11322 3690 2293 -534 C ATOM 879 NH1 ARG A 232 35.576 -18.625 28.072 1.00109.08 N ANISOU 879 NH1 ARG A 232 15851 14126 11469 3725 2667 -483 N ATOM 880 NH2 ARG A 232 36.093 -16.901 26.650 1.00116.87 N ANISOU 880 NH2 ARG A 232 17209 14606 12591 4045 2147 -546 N ATOM 881 N THR A 233 39.657 -24.459 27.173 1.00 76.09 N ANISOU 881 N THR A 233 11048 9031 8832 858 1965 -18 N ATOM 882 CA THR A 233 40.878 -24.932 26.536 1.00 66.50 C ANISOU 882 CA THR A 233 9888 7427 7952 539 1638 -4 C ATOM 883 C THR A 233 40.581 -25.989 25.476 1.00 66.62 C ANISOU 883 C THR A 233 9319 7594 8401 269 1633 -98 C ATOM 884 O THR A 233 41.040 -25.882 24.340 1.00 65.58 O ANISOU 884 O THR A 233 9070 7407 8440 275 1435 -242 O ATOM 885 CB THR A 233 41.859 -25.506 27.576 1.00 61.98 C ANISOU 885 CB THR A 233 9671 6488 7389 227 1532 232 C ATOM 886 OG1 THR A 233 42.325 -24.449 28.424 1.00 61.54 O ANISOU 886 OG1 THR A 233 10235 6242 6905 424 1432 272 O ATOM 887 CG2 THR A 233 43.051 -26.157 26.893 1.00 57.82 C ANISOU 887 CG2 THR A 233 9078 5628 7261 -57 1250 281 C ATOM 888 N ALA A 234 39.802 -27.000 25.851 1.00 57.41 N ANISOU 888 N ALA A 234 7805 6627 7380 13 1843 -12 N ATOM 889 CA ALA A 234 39.443 -28.078 24.936 1.00 58.73 C ANISOU 889 CA ALA A 234 7479 6884 7952 -312 1813 -126 C ATOM 890 C ALA A 234 38.640 -27.561 23.745 1.00 67.34 C ANISOU 890 C ALA A 234 8177 8406 9003 -105 1800 -360 C ATOM 891 O ALA A 234 38.762 -28.075 22.633 1.00 67.83 O ANISOU 891 O ALA A 234 7989 8467 9317 -284 1642 -559 O ATOM 892 CB ALA A 234 38.663 -29.153 25.669 1.00 53.97 C ANISOU 892 CB ALA A 234 6601 6415 7489 -669 2023 71 C ATOM 893 N THR A 235 37.819 -26.544 23.987 1.00 64.93 N ANISOU 893 N THR A 235 7831 8480 8360 301 1967 -335 N ATOM 894 CA THR A 235 37.025 -25.934 22.929 1.00 65.48 C ANISOU 894 CA THR A 235 7519 8998 8361 565 1948 -483 C ATOM 895 C THR A 235 37.931 -25.247 21.911 1.00 67.25 C ANISOU 895 C THR A 235 7969 9000 8584 731 1659 -632 C ATOM 896 O THR A 235 37.760 -25.415 20.703 1.00 59.63 O ANISOU 896 O THR A 235 6662 8258 7736 658 1519 -790 O ATOM 897 CB THR A 235 36.017 -24.917 23.495 1.00 62.90 C ANISOU 897 CB THR A 235 7146 9082 7672 1078 2212 -388 C ATOM 898 OG1 THR A 235 35.169 -25.564 24.451 1.00 76.41 O ANISOU 898 OG1 THR A 235 8587 11100 9345 923 2519 -200 O ATOM 899 CG2 THR A 235 35.160 -24.334 22.383 1.00 59.94 C ANISOU 899 CG2 THR A 235 6310 9207 7258 1367 2176 -476 C ATOM 900 N TYR A 236 38.902 -24.485 22.408 1.00 57.62 N ANISOU 900 N TYR A 236 7321 7368 7205 913 1555 -560 N ATOM 901 CA TYR A 236 39.853 -23.789 21.549 1.00 60.07 C ANISOU 901 CA TYR A 236 7857 7464 7505 1023 1276 -610 C ATOM 902 C TYR A 236 40.724 -24.764 20.762 1.00 63.20 C ANISOU 902 C TYR A 236 8105 7701 8208 654 1103 -701 C ATOM 903 O TYR A 236 41.034 -24.526 19.595 1.00 63.10 O ANISOU 903 O TYR A 236 7950 7809 8214 701 940 -803 O ATOM 904 CB TYR A 236 40.741 -22.856 22.375 1.00 48.19 C ANISOU 904 CB TYR A 236 7008 5519 5782 1185 1163 -473 C ATOM 905 CG TYR A 236 40.074 -21.561 22.780 1.00 55.19 C ANISOU 905 CG TYR A 236 8168 6473 6329 1680 1256 -464 C ATOM 906 CD1 TYR A 236 38.863 -21.175 22.221 1.00 63.82 C ANISOU 906 CD1 TYR A 236 8866 8034 7351 2021 1409 -529 C ATOM 907 CD2 TYR A 236 40.656 -20.724 23.724 1.00 50.85 C ANISOU 907 CD2 TYR A 236 8288 5510 5524 1823 1175 -394 C ATOM 908 CE1 TYR A 236 38.250 -19.992 22.591 1.00 71.23 C ANISOU 908 CE1 TYR A 236 10065 9000 7998 2567 1518 -521 C ATOM 909 CE2 TYR A 236 40.051 -19.540 24.099 1.00 51.61 C ANISOU 909 CE2 TYR A 236 8720 5585 5306 2327 1264 -440 C ATOM 910 CZ TYR A 236 38.849 -19.179 23.531 1.00 60.80 C ANISOU 910 CZ TYR A 236 9479 7192 6432 2736 1456 -502 C ATOM 911 OH TYR A 236 38.247 -17.999 23.902 1.00 62.93 O ANISOU 911 OH TYR A 236 10047 7425 6438 3244 1522 -517 O ATOM 912 N ILE A 237 41.119 -25.856 21.409 1.00 57.70 N ANISOU 912 N ILE A 237 7451 6739 7732 321 1152 -650 N ATOM 913 CA ILE A 237 41.958 -26.862 20.770 1.00 52.25 C ANISOU 913 CA ILE A 237 6665 5832 7355 40 1027 -750 C ATOM 914 C ILE A 237 41.199 -27.557 19.646 1.00 64.33 C ANISOU 914 C ILE A 237 7722 7687 9033 -103 1036 -1030 C ATOM 915 O ILE A 237 41.753 -27.811 18.577 1.00 66.67 O ANISOU 915 O ILE A 237 7926 7991 9416 -135 903 -1218 O ATOM 916 CB ILE A 237 42.459 -27.910 21.787 1.00 51.13 C ANISOU 916 CB ILE A 237 6684 5294 7447 -251 1079 -592 C ATOM 917 CG1 ILE A 237 43.374 -27.255 22.823 1.00 54.56 C ANISOU 917 CG1 ILE A 237 7598 5427 7703 -163 997 -315 C ATOM 918 CG2 ILE A 237 43.191 -29.043 21.086 1.00 50.60 C ANISOU 918 CG2 ILE A 237 6501 4980 7744 -468 986 -730 C ATOM 919 CD1 ILE A 237 44.555 -26.520 22.231 1.00 53.05 C ANISOU 919 CD1 ILE A 237 7598 5105 7454 -37 755 -268 C ATOM 920 N THR A 238 39.926 -27.848 19.890 1.00 63.25 N ANISOU 920 N THR A 238 7277 7862 8891 -198 1190 -1048 N ATOM 921 CA THR A 238 39.074 -28.489 18.895 1.00 62.87 C ANISOU 921 CA THR A 238 6763 8168 8955 -409 1154 -1294 C ATOM 922 C THR A 238 38.921 -27.625 17.646 1.00 67.85 C ANISOU 922 C THR A 238 7216 9204 9360 -143 1015 -1440 C ATOM 923 O THR A 238 39.088 -28.107 16.524 1.00 60.95 O ANISOU 923 O THR A 238 6175 8434 8548 -288 871 -1705 O ATOM 924 CB THR A 238 37.678 -28.798 19.466 1.00 64.06 C ANISOU 924 CB THR A 238 6548 8683 9107 -565 1336 -1183 C ATOM 925 OG1 THR A 238 37.801 -29.721 20.556 1.00 67.45 O ANISOU 925 OG1 THR A 238 7113 8760 9754 -880 1454 -1010 O ATOM 926 CG2 THR A 238 36.785 -29.404 18.394 1.00 64.32 C ANISOU 926 CG2 THR A 238 6079 9123 9237 -848 1229 -1418 C ATOM 927 N GLU A 239 38.602 -26.349 17.846 1.00 59.00 N ANISOU 927 N GLU A 239 6159 8299 7958 262 1056 -1266 N ATOM 928 CA GLU A 239 38.470 -25.410 16.738 1.00 65.91 C ANISOU 928 CA GLU A 239 6897 9533 8614 551 913 -1310 C ATOM 929 C GLU A 239 39.782 -25.272 15.976 1.00 71.27 C ANISOU 929 C GLU A 239 7817 9976 9288 555 723 -1373 C ATOM 930 O GLU A 239 39.797 -25.212 14.746 1.00 74.19 O ANISOU 930 O GLU A 239 7964 10665 9561 564 585 -1519 O ATOM 931 CB GLU A 239 38.016 -24.040 17.243 1.00 57.77 C ANISOU 931 CB GLU A 239 6013 8612 7323 1034 992 -1080 C ATOM 932 CG GLU A 239 36.579 -23.995 17.731 1.00 66.49 C ANISOU 932 CG GLU A 239 6745 10157 8360 1166 1208 -1000 C ATOM 933 CD GLU A 239 36.190 -22.624 18.247 1.00 73.85 C ANISOU 933 CD GLU A 239 7895 11135 9031 1751 1318 -813 C ATOM 934 OE1 GLU A 239 36.943 -22.065 19.070 1.00 69.29 O ANISOU 934 OE1 GLU A 239 7897 10067 8363 1909 1334 -734 O ATOM 935 OE2 GLU A 239 35.139 -22.100 17.823 1.00 80.49 O ANISOU 935 OE2 GLU A 239 8343 12490 9751 2062 1371 -747 O ATOM 936 N LEU A 240 40.883 -25.229 16.719 1.00 62.14 N ANISOU 936 N LEU A 240 7083 8319 8207 541 717 -1233 N ATOM 937 CA LEU A 240 42.201 -25.068 16.124 1.00 54.64 C ANISOU 937 CA LEU A 240 6319 7184 7257 549 559 -1204 C ATOM 938 C LEU A 240 42.647 -26.325 15.384 1.00 66.56 C ANISOU 938 C LEU A 240 7645 8674 8971 295 546 -1483 C ATOM 939 O LEU A 240 43.221 -26.241 14.299 1.00 59.38 O ANISOU 939 O LEU A 240 6644 7953 7963 352 446 -1584 O ATOM 940 CB LEU A 240 43.227 -24.700 17.195 1.00 53.55 C ANISOU 940 CB LEU A 240 6641 6557 7147 565 527 -934 C ATOM 941 CG LEU A 240 44.655 -24.488 16.691 1.00 65.53 C ANISOU 941 CG LEU A 240 8297 7927 8675 551 358 -804 C ATOM 942 CD1 LEU A 240 44.680 -23.477 15.567 1.00 61.50 C ANISOU 942 CD1 LEU A 240 7684 7758 7925 746 219 -745 C ATOM 943 CD2 LEU A 240 45.546 -24.030 17.819 1.00 63.18 C ANISOU 943 CD2 LEU A 240 8431 7200 8376 516 271 -495 C ATOM 944 N ALA A 241 42.384 -27.488 15.974 1.00 58.72 N ANISOU 944 N ALA A 241 6623 7443 8247 29 652 -1602 N ATOM 945 CA ALA A 241 42.765 -28.752 15.355 1.00 57.37 C ANISOU 945 CA ALA A 241 6363 7128 8306 -191 640 -1909 C ATOM 946 C ALA A 241 41.968 -28.985 14.076 1.00 60.95 C ANISOU 946 C ALA A 241 6476 8056 8626 -269 566 -2263 C ATOM 947 O ALA A 241 42.485 -29.546 13.112 1.00 60.13 O ANISOU 947 O ALA A 241 6343 7982 8522 -298 510 -2560 O ATOM 948 CB ALA A 241 42.567 -29.906 16.322 1.00 52.77 C ANISOU 948 CB ALA A 241 5859 6125 8066 -484 741 -1906 C ATOM 949 N ASN A 242 40.710 -28.554 14.075 1.00 60.54 N ANISOU 949 N ASN A 242 6160 8409 8433 -284 566 -2228 N ATOM 950 CA ASN A 242 39.879 -28.634 12.880 1.00 66.95 C ANISOU 950 CA ASN A 242 6606 9767 9065 -371 445 -2499 C ATOM 951 C ASN A 242 40.457 -27.793 11.750 1.00 64.31 C ANISOU 951 C ASN A 242 6257 9772 8407 -91 325 -2509 C ATOM 952 O ASN A 242 40.567 -28.250 10.613 1.00 69.42 O ANISOU 952 O ASN A 242 6780 10671 8924 -183 224 -2835 O ATOM 953 CB ASN A 242 38.450 -28.185 13.182 1.00 62.43 C ANISOU 953 CB ASN A 242 5689 9634 8397 -374 474 -2343 C ATOM 954 CG ASN A 242 37.657 -29.231 13.937 1.00 76.23 C ANISOU 954 CG ASN A 242 7290 11246 10427 -777 561 -2378 C ATOM 955 OD1 ASN A 242 37.869 -30.430 13.764 1.00 83.48 O ANISOU 955 OD1 ASN A 242 8272 11856 11589 -1148 509 -2650 O ATOM 956 ND2 ASN A 242 36.732 -28.781 14.776 1.00 75.93 N ANISOU 956 ND2 ASN A 242 7060 11436 10353 -695 701 -2088 N ATOM 957 N ALA A 243 40.830 -26.561 12.079 1.00 61.97 N ANISOU 957 N ALA A 243 6116 9471 7959 234 328 -2143 N ATOM 958 CA ALA A 243 41.389 -25.639 11.103 1.00 69.45 C ANISOU 958 CA ALA A 243 7058 10722 8608 478 205 -2029 C ATOM 959 C ALA A 243 42.742 -26.126 10.590 1.00 70.21 C ANISOU 959 C ALA A 243 7306 10644 8727 450 204 -2146 C ATOM 960 O ALA A 243 43.044 -26.008 9.403 1.00 63.99 O ANISOU 960 O ALA A 243 6377 10257 7679 516 126 -2260 O ATOM 961 CB ALA A 243 41.516 -24.254 11.706 1.00 48.50 C ANISOU 961 CB ALA A 243 4621 7958 5850 783 184 -1595 C ATOM 962 N LEU A 244 43.550 -26.676 11.491 1.00 56.79 N ANISOU 962 N LEU A 244 5866 8396 7314 378 302 -2089 N ATOM 963 CA LEU A 244 44.857 -27.204 11.121 1.00 56.53 C ANISOU 963 CA LEU A 244 5935 8196 7348 408 337 -2158 C ATOM 964 C LEU A 244 44.727 -28.464 10.273 1.00 65.08 C ANISOU 964 C LEU A 244 6894 9362 8474 275 378 -2686 C ATOM 965 O LEU A 244 45.508 -28.678 9.345 1.00 70.78 O ANISOU 965 O LEU A 244 7576 10278 9038 401 400 -2849 O ATOM 966 CB LEU A 244 45.692 -27.498 12.365 1.00 53.05 C ANISOU 966 CB LEU A 244 5772 7162 7221 372 408 -1916 C ATOM 967 CG LEU A 244 46.245 -26.301 13.137 1.00 58.57 C ANISOU 967 CG LEU A 244 6695 7712 7848 483 326 -1419 C ATOM 968 CD1 LEU A 244 46.834 -26.767 14.456 1.00 61.25 C ANISOU 968 CD1 LEU A 244 7291 7505 8476 377 371 -1227 C ATOM 969 CD2 LEU A 244 47.289 -25.559 12.312 1.00 49.31 C ANISOU 969 CD2 LEU A 244 5476 6800 6460 627 229 -1189 C ATOM 970 N SER A 245 43.743 -29.297 10.601 1.00 68.28 N ANISOU 970 N SER A 245 7250 9620 9075 12 387 -2952 N ATOM 971 CA SER A 245 43.492 -30.520 9.845 1.00 73.33 C ANISOU 971 CA SER A 245 7843 10248 9770 -187 373 -3498 C ATOM 972 C SER A 245 43.149 -30.176 8.403 1.00 75.19 C ANISOU 972 C SER A 245 7851 11164 9553 -133 252 -3757 C ATOM 973 O SER A 245 43.545 -30.876 7.470 1.00 68.64 O ANISOU 973 O SER A 245 7064 10420 8595 -122 256 -4190 O ATOM 974 CB SER A 245 42.365 -31.334 10.484 1.00 70.87 C ANISOU 974 CB SER A 245 7486 9701 9742 -571 349 -3642 C ATOM 975 OG SER A 245 42.190 -32.572 9.819 1.00 87.75 O ANISOU 975 OG SER A 245 9670 11690 11979 -821 292 -4184 O ATOM 976 N TYR A 246 42.414 -29.083 8.232 1.00 69.27 N ANISOU 976 N TYR A 246 6876 10903 8539 -65 149 -3484 N ATOM 977 CA TYR A 246 42.082 -28.581 6.908 1.00 66.27 C ANISOU 977 CA TYR A 246 6254 11235 7691 8 7 -3602 C ATOM 978 C TYR A 246 43.326 -28.050 6.200 1.00 70.91 C ANISOU 978 C TYR A 246 6915 12023 8007 307 57 -3464 C ATOM 979 O TYR A 246 43.501 -28.262 5.000 1.00 63.54 O ANISOU 979 O TYR A 246 5886 11546 6712 343 17 -3761 O ATOM 980 CB TYR A 246 41.012 -27.492 7.007 1.00 61.90 C ANISOU 980 CB TYR A 246 5439 11105 6977 72 -110 -3248 C ATOM 981 CG TYR A 246 40.879 -26.635 5.770 1.00 71.34 C ANISOU 981 CG TYR A 246 6406 13019 7682 244 -264 -3150 C ATOM 982 CD1 TYR A 246 40.202 -27.097 4.646 1.00 74.02 C ANISOU 982 CD1 TYR A 246 6494 13923 7709 53 -429 -3529 C ATOM 983 CD2 TYR A 246 41.425 -25.359 5.729 1.00 61.61 C ANISOU 983 CD2 TYR A 246 5227 11894 6285 561 -277 -2654 C ATOM 984 CE1 TYR A 246 40.078 -26.311 3.513 1.00 66.40 C ANISOU 984 CE1 TYR A 246 5309 13666 6254 206 -584 -3391 C ATOM 985 CE2 TYR A 246 41.306 -24.568 4.610 1.00 63.30 C ANISOU 985 CE2 TYR A 246 5235 12756 6060 706 -428 -2490 C ATOM 986 CZ TYR A 246 40.634 -25.047 3.505 1.00 75.68 C ANISOU 986 CZ TYR A 246 6526 14932 7297 544 -571 -2847 C ATOM 987 OH TYR A 246 40.521 -24.249 2.394 1.00 74.55 O ANISOU 987 OH TYR A 246 6200 15409 6715 689 -693 -2605 O ATOM 988 N CYS A 247 44.188 -27.365 6.948 1.00 58.63 N ANISOU 988 N CYS A 247 5521 10161 6596 496 137 -3000 N ATOM 989 CA CYS A 247 45.434 -26.839 6.394 1.00 57.82 C ANISOU 989 CA CYS A 247 5441 10250 6278 728 181 -2759 C ATOM 990 C CYS A 247 46.354 -27.948 5.897 1.00 62.48 C ANISOU 990 C CYS A 247 6096 10753 6892 789 341 -3153 C ATOM 991 O CYS A 247 46.935 -27.847 4.816 1.00 67.01 O ANISOU 991 O CYS A 247 6552 11816 7093 952 383 -3230 O ATOM 992 CB CYS A 247 46.175 -25.988 7.432 1.00 59.76 C ANISOU 992 CB CYS A 247 5872 10107 6728 823 188 -2185 C ATOM 993 SG CYS A 247 45.438 -24.369 7.754 1.00 61.78 S ANISOU 993 SG CYS A 247 6136 10499 6839 907 6 -1673 S ATOM 994 N HIS A 248 46.488 -29.004 6.693 1.00 57.32 N ANISOU 994 N HIS A 248 5633 9481 6665 690 445 -3382 N ATOM 995 CA HIS A 248 47.399 -30.094 6.364 1.00 59.67 C ANISOU 995 CA HIS A 248 6043 9565 7065 826 618 -3740 C ATOM 996 C HIS A 248 46.846 -30.962 5.237 1.00 64.00 C ANISOU 996 C HIS A 248 6604 10301 7411 707 549 -4242 C ATOM 997 O HIS A 248 47.601 -31.636 4.537 1.00 66.86 O ANISOU 997 O HIS A 248 7063 10652 7690 879 656 -4428 O ATOM 998 CB HIS A 248 47.686 -30.948 7.602 1.00 66.43 C ANISOU 998 CB HIS A 248 7132 9622 8487 750 706 -3716 C ATOM 999 CG HIS A 248 48.466 -30.230 8.662 1.00 56.53 C ANISOU 999 CG HIS A 248 5929 8115 7437 831 718 -3078 C ATOM 1000 ND1 HIS A 248 49.088 -30.888 9.702 1.00 54.46 N ANISOU 1000 ND1 HIS A 248 5843 7237 7614 837 800 -2933 N ATOM 1001 CD2 HIS A 248 48.722 -28.914 8.844 1.00 53.90 C ANISOU 1001 CD2 HIS A 248 5522 8040 6917 881 622 -2543 C ATOM 1002 CE1 HIS A 248 49.696 -30.008 10.476 1.00 48.25 C ANISOU 1002 CE1 HIS A 248 5074 6390 6867 866 743 -2353 C ATOM 1003 NE2 HIS A 248 49.489 -28.802 9.979 1.00 58.52 N ANISOU 1003 NE2 HIS A 248 6251 8179 7804 883 631 -2124 N ATOM 1004 N SER A 249 45.528 -30.941 5.061 1.00 69.77 N ANISOU 1004 N SER A 249 7229 11230 8050 424 376 -4453 N ATOM 1005 CA SER A 249 44.907 -31.641 3.943 1.00 73.05 C ANISOU 1005 CA SER A 249 7626 11899 8231 266 265 -4893 C ATOM 1006 C SER A 249 45.273 -30.940 2.643 1.00 65.79 C ANISOU 1006 C SER A 249 6527 11716 6756 478 238 -4810 C ATOM 1007 O SER A 249 45.274 -31.548 1.576 1.00 70.82 O ANISOU 1007 O SER A 249 7216 12551 7141 476 220 -5150 O ATOM 1008 CB SER A 249 43.387 -31.704 4.101 1.00 73.75 C ANISOU 1008 CB SER A 249 7562 12109 8349 -120 64 -5046 C ATOM 1009 OG SER A 249 42.806 -30.422 3.940 1.00 78.84 O ANISOU 1009 OG SER A 249 7901 13387 8670 -74 -57 -4748 O ATOM 1010 N LYS A 250 45.580 -29.651 2.742 1.00 67.91 N ANISOU 1010 N LYS A 250 6611 12371 6822 652 230 -4329 N ATOM 1011 CA LYS A 250 46.021 -28.879 1.588 1.00 73.18 C ANISOU 1011 CA LYS A 250 7089 13732 6983 843 203 -4113 C ATOM 1012 C LYS A 250 47.541 -28.772 1.577 1.00 78.94 C ANISOU 1012 C LYS A 250 7883 14402 7710 1139 411 -3845 C ATOM 1013 O LYS A 250 48.115 -27.997 0.809 1.00 70.16 O ANISOU 1013 O LYS A 250 6595 13845 6218 1301 415 -3520 O ATOM 1014 CB LYS A 250 45.376 -27.493 1.596 1.00 75.91 C ANISOU 1014 CB LYS A 250 7191 14572 7081 841 36 -3671 C ATOM 1015 CG LYS A 250 43.860 -27.535 1.475 1.00 71.99 C ANISOU 1015 CG LYS A 250 6538 14282 6534 589 -167 -3868 C ATOM 1016 CD LYS A 250 43.444 -28.259 0.196 1.00 76.05 C ANISOU 1016 CD LYS A 250 6983 15137 6776 457 -241 -4273 C ATOM 1017 CE LYS A 250 41.943 -28.492 0.155 1.00 85.93 C ANISOU 1017 CE LYS A 250 8077 16532 8040 143 -434 -4460 C ATOM 1018 NZ LYS A 250 41.522 -29.184 -1.097 1.00 87.89 N ANISOU 1018 NZ LYS A 250 8309 17100 7986 -22 -530 -4846 N ATOM 1019 N ARG A 251 48.173 -29.568 2.438 1.00 65.09 N ANISOU 1019 N ARG A 251 6448 10231 8051 298 666 -2645 N ATOM 1020 CA ARG A 251 49.629 -29.641 2.564 1.00 54.51 C ANISOU 1020 CA ARG A 251 5431 8699 6583 315 576 -2189 C ATOM 1021 C ARG A 251 50.233 -28.303 2.987 1.00 51.28 C ANISOU 1021 C ARG A 251 5318 8275 5893 434 417 -1717 C ATOM 1022 O ARG A 251 51.359 -27.971 2.616 1.00 54.55 O ANISOU 1022 O ARG A 251 5827 8740 6158 512 290 -1482 O ATOM 1023 CB ARG A 251 50.264 -30.117 1.252 1.00 62.18 C ANISOU 1023 CB ARG A 251 6159 9987 7479 453 407 -2341 C ATOM 1024 CG ARG A 251 49.636 -31.377 0.666 1.00 62.45 C ANISOU 1024 CG ARG A 251 5796 10105 7828 337 560 -2947 C ATOM 1025 CD ARG A 251 49.576 -32.499 1.688 1.00 67.46 C ANISOU 1025 CD ARG A 251 6643 10136 8852 16 1000 -2995 C ATOM 1026 NE ARG A 251 50.902 -32.907 2.140 1.00 79.66 N ANISOU 1026 NE ARG A 251 8605 11373 10290 57 1009 -2541 N ATOM 1027 CZ ARG A 251 51.152 -33.439 3.333 1.00101.97 C ANISOU 1027 CZ ARG A 251 11874 13676 13194 12 1334 -2287 C ATOM 1028 NH1 ARG A 251 50.165 -33.620 4.202 1.00 98.38 N ANISOU 1028 NH1 ARG A 251 11545 12860 12975 -140 1748 -2387 N ATOM 1029 NH2 ARG A 251 52.390 -33.783 3.662 1.00109.10 N ANISOU 1029 NH2 ARG A 251 13105 14447 13899 191 1267 -1952 N ATOM 1030 N VAL A 252 49.479 -27.545 3.773 1.00 59.14 N ANISOU 1030 N VAL A 252 6429 9175 6865 415 475 -1641 N ATOM 1031 CA VAL A 252 49.941 -26.256 4.274 1.00 55.85 C ANISOU 1031 CA VAL A 252 6274 8688 6260 482 396 -1278 C ATOM 1032 C VAL A 252 50.397 -26.367 5.727 1.00 50.50 C ANISOU 1032 C VAL A 252 5884 7655 5648 355 472 -1093 C ATOM 1033 O VAL A 252 49.713 -26.968 6.555 1.00 54.41 O ANISOU 1033 O VAL A 252 6467 7932 6273 277 658 -1167 O ATOM 1034 CB VAL A 252 48.834 -25.186 4.155 1.00 57.48 C ANISOU 1034 CB VAL A 252 6446 9072 6323 645 387 -1307 C ATOM 1035 CG1 VAL A 252 49.223 -23.910 4.890 1.00 50.67 C ANISOU 1035 CG1 VAL A 252 5884 8009 5358 645 409 -970 C ATOM 1036 CG2 VAL A 252 48.531 -24.900 2.687 1.00 53.96 C ANISOU 1036 CG2 VAL A 252 5787 9074 5641 997 286 -1452 C ATOM 1037 N ILE A 253 51.562 -25.801 6.028 1.00 51.93 N ANISOU 1037 N ILE A 253 6196 7798 5735 375 370 -910 N ATOM 1038 CA ILE A 253 52.055 -25.745 7.401 1.00 50.22 C ANISOU 1038 CA ILE A 253 6201 7399 5483 397 363 -824 C ATOM 1039 C ILE A 253 52.078 -24.301 7.893 1.00 50.36 C ANISOU 1039 C ILE A 253 6275 7406 5454 374 326 -752 C ATOM 1040 O ILE A 253 52.664 -23.434 7.250 1.00 46.45 O ANISOU 1040 O ILE A 253 5699 6978 4972 325 326 -742 O ATOM 1041 CB ILE A 253 53.468 -26.346 7.527 1.00 45.15 C ANISOU 1041 CB ILE A 253 5571 6806 4777 490 251 -860 C ATOM 1042 CG1 ILE A 253 53.633 -27.545 6.594 1.00 48.87 C ANISOU 1042 CG1 ILE A 253 5940 7318 5310 490 286 -931 C ATOM 1043 CG2 ILE A 253 53.754 -26.730 8.979 1.00 49.36 C ANISOU 1043 CG2 ILE A 253 6361 7229 5165 717 254 -833 C ATOM 1044 CD1 ILE A 253 55.025 -28.143 6.597 1.00 47.47 C ANISOU 1044 CD1 ILE A 253 5761 7237 5037 626 158 -979 C ATOM 1045 N HIS A 254 51.444 -24.043 9.035 1.00 54.32 N ANISOU 1045 N HIS A 254 6938 7776 5925 409 369 -710 N ATOM 1046 CA HIS A 254 51.353 -22.682 9.561 1.00 39.70 C ANISOU 1046 CA HIS A 254 5135 5891 4057 378 356 -681 C ATOM 1047 C HIS A 254 52.678 -22.207 10.152 1.00 44.77 C ANISOU 1047 C HIS A 254 5723 6587 4702 388 247 -837 C ATOM 1048 O HIS A 254 53.127 -21.093 9.871 1.00 38.94 O ANISOU 1048 O HIS A 254 4893 5822 4080 250 322 -919 O ATOM 1049 CB HIS A 254 50.251 -22.587 10.620 1.00 37.48 C ANISOU 1049 CB HIS A 254 5021 5486 3735 432 426 -621 C ATOM 1050 CG HIS A 254 49.977 -21.186 11.072 1.00 47.00 C ANISOU 1050 CG HIS A 254 6275 6652 4932 402 425 -597 C ATOM 1051 ND1 HIS A 254 50.712 -20.564 12.059 1.00 38.13 N ANISOU 1051 ND1 HIS A 254 5178 5520 3790 437 341 -710 N ATOM 1052 CD2 HIS A 254 49.062 -20.279 10.656 1.00 43.83 C ANISOU 1052 CD2 HIS A 254 5890 6237 4525 385 512 -522 C ATOM 1053 CE1 HIS A 254 50.256 -19.337 12.236 1.00 50.80 C ANISOU 1053 CE1 HIS A 254 6821 7038 5443 368 416 -693 C ATOM 1054 NE2 HIS A 254 49.255 -19.139 11.397 1.00 51.38 N ANISOU 1054 NE2 HIS A 254 6932 7091 5499 361 529 -534 N ATOM 1055 N ARG A 255 53.270 -23.053 10.995 1.00 45.29 N ANISOU 1055 N ARG A 255 5846 6726 4635 596 125 -929 N ATOM 1056 CA ARG A 255 54.596 -22.837 11.586 1.00 52.62 C ANISOU 1056 CA ARG A 255 6622 7868 5505 725 -56 -1242 C ATOM 1057 C ARG A 255 54.696 -21.663 12.572 1.00 45.37 C ANISOU 1057 C ARG A 255 5629 6999 4612 728 -109 -1479 C ATOM 1058 O ARG A 255 55.787 -21.349 13.045 1.00 51.57 O ANISOU 1058 O ARG A 255 6162 8034 5400 813 -262 -1913 O ATOM 1059 CB ARG A 255 55.646 -22.652 10.480 1.00 53.85 C ANISOU 1059 CB ARG A 255 6494 8127 5838 515 -47 -1421 C ATOM 1060 CG ARG A 255 55.719 -23.809 9.486 1.00 52.88 C ANISOU 1060 CG ARG A 255 6391 8019 5680 540 -39 -1259 C ATOM 1061 CD ARG A 255 57.027 -23.817 8.705 1.00 61.76 C ANISOU 1061 CD ARG A 255 7239 9318 6910 442 -79 -1498 C ATOM 1062 NE ARG A 255 57.199 -22.631 7.869 1.00 50.80 N ANISOU 1062 NE ARG A 255 5719 7808 5773 132 166 -1530 N ATOM 1063 CZ ARG A 255 58.205 -22.459 7.016 1.00 52.31 C ANISOU 1063 CZ ARG A 255 5697 8051 6127 -23 289 -1702 C ATOM 1064 NH1 ARG A 255 59.136 -23.396 6.886 1.00 44.18 N ANISOU 1064 NH1 ARG A 255 4497 7266 5023 90 94 -1896 N ATOM 1065 NH2 ARG A 255 58.286 -21.350 6.295 1.00 51.50 N ANISOU 1065 NH2 ARG A 255 5592 7725 6250 -257 672 -1667 N ATOM 1066 N ASP A 256 53.583 -21.011 12.889 1.00 48.55 N ANISOU 1066 N ASP A 256 6194 7208 5045 646 7 -1287 N ATOM 1067 CA ASP A 256 53.639 -19.922 13.864 1.00 47.76 C ANISOU 1067 CA ASP A 256 6028 7143 4977 657 -36 -1533 C ATOM 1068 C ASP A 256 52.415 -19.885 14.784 1.00 46.24 C ANISOU 1068 C ASP A 256 6119 6834 4614 826 -12 -1292 C ATOM 1069 O ASP A 256 51.884 -18.818 15.094 1.00 48.77 O ANISOU 1069 O ASP A 256 6450 7045 5034 699 60 -1312 O ATOM 1070 CB ASP A 256 53.803 -18.575 13.155 1.00 50.41 C ANISOU 1070 CB ASP A 256 6207 7295 5651 271 200 -1649 C ATOM 1071 CG ASP A 256 54.293 -17.477 14.092 1.00 63.35 C ANISOU 1071 CG ASP A 256 7641 8985 7444 210 195 -2119 C ATOM 1072 OD1 ASP A 256 54.888 -17.808 15.141 1.00 69.24 O ANISOU 1072 OD1 ASP A 256 8227 10068 8012 504 -93 -2497 O ATOM 1073 OD2 ASP A 256 54.082 -16.285 13.786 1.00 64.73 O ANISOU 1073 OD2 ASP A 256 7822 8877 7896 -74 505 -2146 O ATOM 1074 N ILE A 257 51.976 -21.057 15.225 1.00 43.24 N ANISOU 1074 N ILE A 257 5997 6435 3999 1116 1 -1070 N ATOM 1075 CA ILE A 257 50.869 -21.144 16.168 1.00 52.25 C ANISOU 1075 CA ILE A 257 7430 7433 4992 1294 116 -860 C ATOM 1076 C ILE A 257 51.266 -20.565 17.526 1.00 46.34 C ANISOU 1076 C ILE A 257 6695 6895 4018 1642 -70 -1100 C ATOM 1077 O ILE A 257 52.232 -21.019 18.139 1.00 49.57 O ANISOU 1077 O ILE A 257 7084 7592 4159 2073 -258 -1329 O ATOM 1078 CB ILE A 257 50.402 -22.596 16.357 1.00 54.10 C ANISOU 1078 CB ILE A 257 7985 7491 5080 1528 347 -598 C ATOM 1079 CG1 ILE A 257 49.910 -23.175 15.032 1.00 61.47 C ANISOU 1079 CG1 ILE A 257 8814 8267 6275 1174 524 -495 C ATOM 1080 CG2 ILE A 257 49.305 -22.672 17.413 1.00 56.80 C ANISOU 1080 CG2 ILE A 257 8653 7632 5297 1714 582 -403 C ATOM 1081 CD1 ILE A 257 49.623 -24.656 15.096 1.00 62.11 C ANISOU 1081 CD1 ILE A 257 9155 8111 6331 1320 846 -349 C ATOM 1082 N LYS A 258 50.518 -19.557 17.973 1.00 45.62 N ANISOU 1082 N LYS A 258 6616 6716 4003 1517 -38 -1095 N ATOM 1083 CA LYS A 258 50.712 -18.931 19.282 1.00 55.64 C ANISOU 1083 CA LYS A 258 7877 8196 5069 1847 -211 -1355 C ATOM 1084 C LYS A 258 49.495 -18.051 19.579 1.00 53.12 C ANISOU 1084 C LYS A 258 7672 7659 4854 1655 -79 -1184 C ATOM 1085 O LYS A 258 48.777 -17.668 18.652 1.00 49.00 O ANISOU 1085 O LYS A 258 7135 6903 4581 1261 90 -988 O ATOM 1086 CB LYS A 258 52.013 -18.117 19.322 1.00 62.15 C ANISOU 1086 CB LYS A 258 8249 9332 6031 1786 -449 -1969 C ATOM 1087 CG LYS A 258 52.035 -16.889 18.430 1.00 51.53 C ANISOU 1087 CG LYS A 258 6654 7757 5167 1184 -278 -2107 C ATOM 1088 CD LYS A 258 53.375 -16.178 18.532 1.00 53.10 C ANISOU 1088 CD LYS A 258 6366 8204 5607 1067 -375 -2833 C ATOM 1089 CE LYS A 258 53.427 -14.942 17.648 1.00 65.61 C ANISOU 1089 CE LYS A 258 7804 9411 7714 476 -4 -2938 C ATOM 1090 NZ LYS A 258 54.755 -14.267 17.716 1.00 71.02 N ANISOU 1090 NZ LYS A 258 7958 10258 8769 257 49 -3758 N ATOM 1091 N PRO A 259 49.245 -17.742 20.868 1.00 49.27 N ANISOU 1091 N PRO A 259 7308 7296 4117 2018 -166 -1270 N ATOM 1092 CA PRO A 259 48.054 -16.976 21.258 1.00 49.31 C ANISOU 1092 CA PRO A 259 7444 7112 4180 1889 -45 -1102 C ATOM 1093 C PRO A 259 47.897 -15.636 20.539 1.00 51.18 C ANISOU 1093 C PRO A 259 7455 7206 4784 1407 -5 -1231 C ATOM 1094 O PRO A 259 46.768 -15.219 20.283 1.00 45.38 O ANISOU 1094 O PRO A 259 6852 6264 4126 1235 156 -976 O ATOM 1095 CB PRO A 259 48.264 -16.750 22.760 1.00 56.00 C ANISOU 1095 CB PRO A 259 8365 8236 4677 2427 -229 -1327 C ATOM 1096 CG PRO A 259 49.085 -17.898 23.197 1.00 54.12 C ANISOU 1096 CG PRO A 259 8264 8246 4052 3001 -316 -1362 C ATOM 1097 CD PRO A 259 50.016 -18.179 22.046 1.00 52.60 C ANISOU 1097 CD PRO A 259 7786 8095 4105 2689 -385 -1522 C ATOM 1098 N GLU A 260 49.006 -14.973 20.227 1.00 53.59 N ANISOU 1098 N GLU A 260 7441 7608 5312 1230 -86 -1649 N ATOM 1099 CA GLU A 260 48.955 -13.698 19.520 1.00 61.86 C ANISOU 1099 CA GLU A 260 8373 8398 6731 809 126 -1744 C ATOM 1100 C GLU A 260 48.392 -13.862 18.106 1.00 47.88 C ANISOU 1100 C GLU A 260 6749 6378 5064 576 363 -1323 C ATOM 1101 O GLU A 260 47.816 -12.929 17.546 1.00 49.29 O ANISOU 1101 O GLU A 260 7039 6313 5376 419 598 -1178 O ATOM 1102 CB GLU A 260 50.345 -13.059 19.455 1.00 60.65 C ANISOU 1102 CB GLU A 260 7824 8335 6887 618 135 -2365 C ATOM 1103 CG GLU A 260 50.958 -12.733 20.811 1.00 87.33 C ANISOU 1103 CG GLU A 260 10921 12083 10178 892 -137 -2993 C ATOM 1104 CD GLU A 260 51.821 -13.858 21.351 1.00 94.60 C ANISOU 1104 CD GLU A 260 11698 13506 10741 1373 -494 -3250 C ATOM 1105 OE1 GLU A 260 51.357 -15.018 21.362 1.00 86.87 O ANISOU 1105 OE1 GLU A 260 11064 12548 9393 1690 -553 -2739 O ATOM 1106 OE2 GLU A 260 52.968 -13.581 21.762 1.00101.52 O ANISOU 1106 OE2 GLU A 260 12106 14758 11711 1462 -673 -4016 O ATOM 1107 N ASN A 261 48.555 -15.051 17.536 1.00 49.01 N ANISOU 1107 N ASN A 261 6906 6611 5105 634 308 -1151 N ATOM 1108 CA ASN A 261 48.112 -15.298 16.163 1.00 54.53 C ANISOU 1108 CA ASN A 261 7666 7187 5865 488 476 -862 C ATOM 1109 C ASN A 261 46.781 -16.032 16.091 1.00 57.51 C ANISOU 1109 C ASN A 261 8194 7577 6079 597 497 -580 C ATOM 1110 O ASN A 261 46.408 -16.560 15.043 1.00 54.62 O ANISOU 1110 O ASN A 261 7796 7237 5721 556 567 -459 O ATOM 1111 CB ASN A 261 49.166 -16.090 15.395 1.00 41.17 C ANISOU 1111 CB ASN A 261 5819 5587 4237 425 439 -944 C ATOM 1112 CG ASN A 261 50.427 -15.296 15.155 1.00 43.55 C ANISOU 1112 CG ASN A 261 5900 5847 4802 225 535 -1296 C ATOM 1113 OD1 ASN A 261 50.415 -14.066 15.200 1.00 46.17 O ANISOU 1113 OD1 ASN A 261 6238 5970 5337 67 759 -1416 O ATOM 1114 ND2 ASN A 261 51.521 -15.994 14.877 1.00 44.27 N ANISOU 1114 ND2 ASN A 261 5788 6105 4929 214 432 -1502 N ATOM 1115 N LEU A 262 46.075 -16.073 17.214 1.00 52.56 N ANISOU 1115 N LEU A 262 7694 6954 5324 742 465 -549 N ATOM 1116 CA LEU A 262 44.752 -16.678 17.258 1.00 42.41 C ANISOU 1116 CA LEU A 262 6503 5642 3971 783 585 -389 C ATOM 1117 C LEU A 262 43.720 -15.618 17.612 1.00 55.66 C ANISOU 1117 C LEU A 262 8248 7288 5614 804 622 -357 C ATOM 1118 O LEU A 262 43.815 -14.971 18.658 1.00 53.11 O ANISOU 1118 O LEU A 262 8011 6938 5232 895 557 -410 O ATOM 1119 CB LEU A 262 44.717 -17.824 18.265 1.00 43.40 C ANISOU 1119 CB LEU A 262 6791 5727 3972 974 661 -338 C ATOM 1120 CG LEU A 262 45.710 -18.956 18.010 1.00 44.97 C ANISOU 1120 CG LEU A 262 6996 5948 4144 1055 655 -347 C ATOM 1121 CD1 LEU A 262 45.662 -19.958 19.149 1.00 49.60 C ANISOU 1121 CD1 LEU A 262 7895 6433 4517 1403 835 -230 C ATOM 1122 CD2 LEU A 262 45.420 -19.635 16.681 1.00 46.21 C ANISOU 1122 CD2 LEU A 262 6998 6078 4480 826 772 -336 C ATOM 1123 N LEU A 263 42.739 -15.439 16.735 1.00 48.33 N ANISOU 1123 N LEU A 263 7257 6420 4687 782 702 -320 N ATOM 1124 CA LEU A 263 41.747 -14.386 16.909 1.00 51.65 C ANISOU 1124 CA LEU A 263 7746 6857 5023 877 728 -298 C ATOM 1125 C LEU A 263 40.381 -14.947 17.276 1.00 51.56 C ANISOU 1125 C LEU A 263 7666 6946 4980 909 813 -373 C ATOM 1126 O LEU A 263 40.125 -16.139 17.114 1.00 58.02 O ANISOU 1126 O LEU A 263 8360 7787 5898 816 931 -472 O ATOM 1127 CB LEU A 263 41.644 -13.544 15.639 1.00 51.13 C ANISOU 1127 CB LEU A 263 7692 6846 4890 990 780 -242 C ATOM 1128 CG LEU A 263 42.937 -12.867 15.184 1.00 54.93 C ANISOU 1128 CG LEU A 263 8266 7123 5481 912 872 -187 C ATOM 1129 CD1 LEU A 263 42.721 -12.119 13.879 1.00 51.01 C ANISOU 1129 CD1 LEU A 263 7909 6625 4848 1148 1063 -44 C ATOM 1130 CD2 LEU A 263 43.449 -11.925 16.257 1.00 55.05 C ANISOU 1130 CD2 LEU A 263 8377 6919 5619 813 906 -270 C ATOM 1131 N LEU A 264 39.508 -14.075 17.773 1.00 52.23 N ANISOU 1131 N LEU A 264 7819 7059 4967 1016 813 -374 N ATOM 1132 CA LEU A 264 38.167 -14.474 18.182 1.00 45.56 C ANISOU 1132 CA LEU A 264 6865 6319 4127 1024 933 -522 C ATOM 1133 C LEU A 264 37.095 -13.744 17.377 1.00 60.92 C ANISOU 1133 C LEU A 264 8659 8562 5925 1226 875 -677 C ATOM 1134 O LEU A 264 37.132 -12.520 17.242 1.00 56.30 O ANISOU 1134 O LEU A 264 8253 7972 5165 1433 794 -539 O ATOM 1135 CB LEU A 264 37.968 -14.215 19.676 1.00 51.21 C ANISOU 1135 CB LEU A 264 7788 6870 4799 1058 986 -428 C ATOM 1136 CG LEU A 264 38.909 -14.977 20.612 1.00 49.51 C ANISOU 1136 CG LEU A 264 7764 6460 4589 1070 1045 -306 C ATOM 1137 CD1 LEU A 264 38.712 -14.534 22.056 1.00 49.44 C ANISOU 1137 CD1 LEU A 264 7975 6379 4431 1255 1053 -229 C ATOM 1138 CD2 LEU A 264 38.699 -16.476 20.472 1.00 54.70 C ANISOU 1138 CD2 LEU A 264 8384 7009 5391 963 1351 -350 C ATOM 1139 N GLY A 265 36.141 -14.503 16.847 1.00 63.28 N ANISOU 1139 N GLY A 265 8619 9132 6292 1209 954 -1023 N ATOM 1140 CA GLY A 265 35.060 -13.937 16.060 1.00 63.31 C ANISOU 1140 CA GLY A 265 8391 9581 6082 1528 848 -1308 C ATOM 1141 C GLY A 265 34.005 -13.258 16.913 1.00 65.32 C ANISOU 1141 C GLY A 265 8668 9905 6245 1633 867 -1391 C ATOM 1142 O GLY A 265 34.173 -13.115 18.123 1.00 65.51 O ANISOU 1142 O GLY A 265 8933 9601 6358 1463 960 -1171 O ATOM 1143 N SER A 266 32.911 -12.843 16.281 1.00 66.68 N ANISOU 1143 N SER A 266 8575 10570 6193 1986 761 -1746 N ATOM 1144 CA SER A 266 31.857 -12.107 16.973 1.00 72.97 C ANISOU 1144 CA SER A 266 9367 11508 6850 2156 747 -1863 C ATOM 1145 C SER A 266 31.102 -12.983 17.971 1.00 64.40 C ANISOU 1145 C SER A 266 8022 10320 6125 1745 1020 -2180 C ATOM 1146 O SER A 266 30.446 -12.478 18.884 1.00 73.96 O ANISOU 1146 O SER A 266 9317 11486 7298 1766 1076 -2167 O ATOM 1147 CB SER A 266 30.877 -11.509 15.962 1.00 71.90 C ANISOU 1147 CB SER A 266 8966 11917 6435 2652 499 -2138 C ATOM 1148 OG SER A 266 30.257 -12.525 15.194 1.00 76.93 O ANISOU 1148 OG SER A 266 9008 12929 7295 2538 443 -2685 O ATOM 1149 N ALA A 267 31.195 -14.296 17.790 1.00 74.26 N ANISOU 1149 N ALA A 267 8989 11487 7740 1383 1265 -2462 N ATOM 1150 CA ALA A 267 30.527 -15.240 18.676 1.00 77.19 C ANISOU 1150 CA ALA A 267 9183 11624 8523 974 1729 -2755 C ATOM 1151 C ALA A 267 31.541 -15.997 19.528 1.00 76.22 C ANISOU 1151 C ALA A 267 9501 10857 8602 686 2031 -2270 C ATOM 1152 O ALA A 267 31.200 -16.967 20.203 1.00 83.15 O ANISOU 1152 O ALA A 267 10372 11398 9824 385 2564 -2405 O ATOM 1153 CB ALA A 267 29.675 -16.211 17.873 1.00 72.60 C ANISOU 1153 CB ALA A 267 7941 11351 8292 774 1894 -3503 C ATOM 1154 N GLY A 268 32.791 -15.549 19.485 1.00 76.09 N ANISOU 1154 N GLY A 268 9876 10674 8362 828 1745 -1743 N ATOM 1155 CA GLY A 268 33.840 -16.141 20.292 1.00 67.09 C ANISOU 1155 CA GLY A 268 9144 9064 7285 721 1922 -1327 C ATOM 1156 C GLY A 268 34.526 -17.332 19.651 1.00 67.68 C ANISOU 1156 C GLY A 268 9142 8997 7575 537 2091 -1382 C ATOM 1157 O GLY A 268 35.288 -18.040 20.310 1.00 71.81 O ANISOU 1157 O GLY A 268 9999 9149 8136 513 2318 -1095 O ATOM 1158 N GLU A 269 34.263 -17.560 18.368 1.00 68.25 N ANISOU 1158 N GLU A 269 8789 9405 7737 488 1976 -1767 N ATOM 1159 CA GLU A 269 34.900 -18.665 17.662 1.00 72.77 C ANISOU 1159 CA GLU A 269 9250 9876 8522 313 2112 -1864 C ATOM 1160 C GLU A 269 36.364 -18.341 17.384 1.00 66.31 C ANISOU 1160 C GLU A 269 8736 8983 7474 460 1772 -1401 C ATOM 1161 O GLU A 269 36.715 -17.198 17.088 1.00 60.84 O ANISOU 1161 O GLU A 269 8137 8469 6508 681 1405 -1210 O ATOM 1162 CB GLU A 269 34.163 -18.986 16.354 1.00 71.33 C ANISOU 1162 CB GLU A 269 8453 10171 8478 278 2051 -2514 C ATOM 1163 CG GLU A 269 34.224 -17.899 15.290 1.00 68.32 C ANISOU 1163 CG GLU A 269 7949 10322 7687 693 1514 -2520 C ATOM 1164 CD GLU A 269 33.178 -16.819 15.487 1.00 82.92 C ANISOU 1164 CD GLU A 269 9705 12515 9284 983 1350 -2677 C ATOM 1165 OE1 GLU A 269 32.565 -16.772 16.574 1.00 79.97 O ANISOU 1165 OE1 GLU A 269 9410 11932 9043 823 1587 -2686 O ATOM 1166 OE2 GLU A 269 32.967 -16.019 14.552 1.00 87.80 O ANISOU 1166 OE2 GLU A 269 10214 13614 9532 1438 1015 -2775 O ATOM 1167 N LEU A 270 37.216 -19.352 17.498 1.00 57.60 N ANISOU 1167 N LEU A 270 7362 8063 6461 1721 1117 -31 N ATOM 1168 CA LEU A 270 38.644 -19.178 17.272 1.00 59.45 C ANISOU 1168 CA LEU A 270 7836 8229 6523 1550 946 -125 C ATOM 1169 C LEU A 270 38.955 -19.192 15.779 1.00 56.01 C ANISOU 1169 C LEU A 270 7125 8140 6017 1459 739 -314 C ATOM 1170 O LEU A 270 38.394 -19.988 15.027 1.00 60.63 O ANISOU 1170 O LEU A 270 7259 8979 6799 1412 670 -513 O ATOM 1171 CB LEU A 270 39.435 -20.273 17.996 1.00 59.97 C ANISOU 1171 CB LEU A 270 7917 8079 6792 1376 952 -216 C ATOM 1172 CG LEU A 270 40.965 -20.232 17.941 1.00 65.60 C ANISOU 1172 CG LEU A 270 8836 8738 7351 1203 783 -306 C ATOM 1173 CD1 LEU A 270 41.552 -20.754 19.241 1.00 60.78 C ANISOU 1173 CD1 LEU A 270 8447 7867 6779 1208 866 -239 C ATOM 1174 CD2 LEU A 270 41.499 -21.040 16.765 1.00 64.19 C ANISOU 1174 CD2 LEU A 270 8306 8785 7298 1015 612 -554 C ATOM 1175 N LYS A 271 39.852 -18.305 15.359 1.00 54.47 N ANISOU 1175 N LYS A 271 7195 7956 5546 1441 652 -261 N ATOM 1176 CA LYS A 271 40.294 -18.257 13.969 1.00 57.58 C ANISOU 1176 CA LYS A 271 7376 8680 5821 1401 488 -389 C ATOM 1177 C LYS A 271 41.803 -18.052 13.883 1.00 63.33 C ANISOU 1177 C LYS A 271 8329 9295 6439 1211 395 -408 C ATOM 1178 O LYS A 271 42.346 -17.129 14.492 1.00 48.11 O ANISOU 1178 O LYS A 271 6797 7112 4371 1193 460 -249 O ATOM 1179 CB LYS A 271 39.568 -17.145 13.208 1.00 59.36 C ANISOU 1179 CB LYS A 271 7617 9148 5789 1678 541 -218 C ATOM 1180 CG LYS A 271 38.074 -17.378 13.048 1.00 76.39 C ANISOU 1180 CG LYS A 271 9434 11558 8034 1883 591 -227 C ATOM 1181 CD LYS A 271 37.412 -16.261 12.265 1.00 75.00 C ANISOU 1181 CD LYS A 271 9271 11678 7549 2224 648 -26 C ATOM 1182 CE LYS A 271 35.919 -16.503 12.132 1.00 74.36 C ANISOU 1182 CE LYS A 271 8793 11914 7548 2440 679 -42 C ATOM 1183 NZ LYS A 271 35.259 -15.451 11.316 1.00 84.72 N ANISOU 1183 NZ LYS A 271 10084 13591 8516 2841 733 171 N ATOM 1184 N ILE A 272 42.475 -18.919 13.130 1.00 58.01 N ANISOU 1184 N ILE A 272 7387 8812 5841 1065 246 -622 N ATOM 1185 CA ILE A 272 43.909 -18.775 12.903 1.00 60.88 C ANISOU 1185 CA ILE A 272 7883 9143 6105 899 160 -632 C ATOM 1186 C ILE A 272 44.189 -17.556 12.038 1.00 57.59 C ANISOU 1186 C ILE A 272 7597 8861 5424 997 186 -462 C ATOM 1187 O ILE A 272 43.483 -17.303 11.062 1.00 64.01 O ANISOU 1187 O ILE A 272 8229 9983 6110 1205 190 -440 O ATOM 1188 CB ILE A 272 44.520 -20.004 12.206 1.00 70.46 C ANISOU 1188 CB ILE A 272 8772 10557 7442 775 20 -889 C ATOM 1189 CG1 ILE A 272 43.950 -21.301 12.770 1.00 78.12 C ANISOU 1189 CG1 ILE A 272 9537 11416 8729 723 46 -1068 C ATOM 1190 CG2 ILE A 272 46.037 -19.989 12.331 1.00 73.71 C ANISOU 1190 CG2 ILE A 272 9322 10889 7797 599 -41 -870 C ATOM 1191 CD1 ILE A 272 44.565 -22.528 12.137 1.00 82.67 C ANISOU 1191 CD1 ILE A 272 9842 12118 9453 609 -58 -1338 C ATOM 1192 N ALA A 273 45.229 -16.811 12.391 1.00 52.30 N ANISOU 1192 N ALA A 273 7224 7970 4678 856 216 -342 N ATOM 1193 CA ALA A 273 45.633 -15.657 11.605 1.00 52.58 C ANISOU 1193 CA ALA A 273 7400 8053 4525 914 301 -149 C ATOM 1194 C ALA A 273 47.145 -15.642 11.423 1.00 48.90 C ANISOU 1194 C ALA A 273 6953 7552 4075 662 239 -169 C ATOM 1195 O ALA A 273 47.844 -16.535 11.911 1.00 54.87 O ANISOU 1195 O ALA A 273 7609 8284 4954 475 112 -336 O ATOM 1196 CB ALA A 273 45.157 -14.369 12.266 1.00 52.53 C ANISOU 1196 CB ALA A 273 7795 7722 4443 1011 486 71 C ATOM 1197 N ASP A 274 47.634 -14.624 10.720 1.00 51.10 N ANISOU 1197 N ASP A 274 7345 7833 4237 680 359 30 N ATOM 1198 CA ASP A 274 49.062 -14.424 10.484 1.00 53.21 C ANISOU 1198 CA ASP A 274 7610 8066 4543 434 346 60 C ATOM 1199 C ASP A 274 49.738 -15.642 9.857 1.00 49.63 C ANISOU 1199 C ASP A 274 6795 7954 4108 385 182 -115 C ATOM 1200 O ASP A 274 50.385 -16.432 10.544 1.00 50.74 O ANISOU 1200 O ASP A 274 6869 8037 4373 192 48 -282 O ATOM 1201 CB ASP A 274 49.773 -14.049 11.788 1.00 62.40 C ANISOU 1201 CB ASP A 274 9038 8835 5837 135 317 4 C ATOM 1202 CG ASP A 274 51.243 -13.734 11.578 1.00 78.66 C ANISOU 1202 CG ASP A 274 11054 10867 7967 -152 306 30 C ATOM 1203 OD1 ASP A 274 51.636 -13.448 10.425 1.00 72.43 O ANISOU 1203 OD1 ASP A 274 10128 10268 7125 -96 413 190 O ATOM 1204 OD2 ASP A 274 52.004 -13.764 12.568 1.00 78.79 O ANISOU 1204 OD2 ASP A 274 11153 10701 8081 -415 196 -102 O ATOM 1205 N PHE A 275 49.596 -15.777 8.542 1.00 51.34 N ANISOU 1205 N PHE A 275 6791 8544 4174 601 205 -70 N ATOM 1206 CA PHE A 275 50.265 -16.847 7.810 1.00 50.36 C ANISOU 1206 CA PHE A 275 6350 8752 4032 597 75 -239 C ATOM 1207 C PHE A 275 51.628 -16.376 7.320 1.00 43.46 C ANISOU 1207 C PHE A 275 5462 7916 3133 463 158 -66 C ATOM 1208 O PHE A 275 52.133 -16.838 6.300 1.00 52.35 O ANISOU 1208 O PHE A 275 6357 9388 4147 579 141 -81 O ATOM 1209 CB PHE A 275 49.392 -17.325 6.647 1.00 43.09 C ANISOU 1209 CB PHE A 275 5174 8267 2930 926 27 -344 C ATOM 1210 CG PHE A 275 48.258 -18.211 7.077 1.00 53.52 C ANISOU 1210 CG PHE A 275 6367 9603 4364 977 -98 -613 C ATOM 1211 CD1 PHE A 275 47.172 -17.688 7.764 1.00 53.42 C ANISOU 1211 CD1 PHE A 275 6512 9394 4391 1043 -29 -533 C ATOM 1212 CD2 PHE A 275 48.283 -19.568 6.804 1.00 48.32 C ANISOU 1212 CD2 PHE A 275 5430 9129 3802 956 -254 -942 C ATOM 1213 CE1 PHE A 275 46.132 -18.503 8.171 1.00 57.03 C ANISOU 1213 CE1 PHE A 275 6812 9861 4997 1074 -110 -754 C ATOM 1214 CE2 PHE A 275 47.247 -20.389 7.209 1.00 52.70 C ANISOU 1214 CE2 PHE A 275 5845 9645 4535 961 -329 -1188 C ATOM 1215 CZ PHE A 275 46.169 -19.856 7.891 1.00 53.46 C ANISOU 1215 CZ PHE A 275 6062 9567 4685 1012 -255 -1084 C ATOM 1216 N GLY A 276 52.225 -15.463 8.081 1.00 46.32 N ANISOU 1216 N GLY A 276 6064 7918 3615 212 251 79 N ATOM 1217 CA GLY A 276 53.493 -14.857 7.726 1.00 52.10 C ANISOU 1217 CA GLY A 276 6775 8624 4397 23 364 259 C ATOM 1218 C GLY A 276 54.701 -15.762 7.862 1.00 60.06 C ANISOU 1218 C GLY A 276 7539 9787 5492 -175 212 116 C ATOM 1219 O GLY A 276 55.811 -15.351 7.547 1.00 66.03 O ANISOU 1219 O GLY A 276 8208 10571 6309 -342 300 261 O ATOM 1220 N TRP A 277 54.497 -16.982 8.347 1.00 49.24 N ANISOU 1220 N TRP A 277 6053 8507 4150 -149 15 -146 N ATOM 1221 CA TRP A 277 55.575 -17.967 8.406 1.00 50.24 C ANISOU 1221 CA TRP A 277 5944 8817 4329 -250 -108 -268 C ATOM 1222 C TRP A 277 55.183 -19.248 7.680 1.00 50.22 C ANISOU 1222 C TRP A 277 5720 9118 4242 4 -190 -461 C ATOM 1223 O TRP A 277 55.949 -20.214 7.647 1.00 51.30 O ANISOU 1223 O TRP A 277 5672 9409 4410 -8 -270 -576 O ATOM 1224 CB TRP A 277 55.945 -18.295 9.858 1.00 46.60 C ANISOU 1224 CB TRP A 277 5567 8130 4007 -469 -247 -406 C ATOM 1225 CG TRP A 277 56.948 -17.373 10.474 1.00 44.88 C ANISOU 1225 CG TRP A 277 5424 7747 3882 -782 -240 -316 C ATOM 1226 CD1 TRP A 277 56.770 -16.596 11.583 1.00 52.16 C ANISOU 1226 CD1 TRP A 277 6610 8337 4871 -964 -264 -352 C ATOM 1227 CD2 TRP A 277 58.294 -17.139 10.035 1.00 51.75 C ANISOU 1227 CD2 TRP A 277 6078 8782 4802 -964 -210 -210 C ATOM 1228 NE1 TRP A 277 57.917 -15.890 11.857 1.00 51.56 N ANISOU 1228 NE1 TRP A 277 6490 8202 4900 -1277 -275 -320 N ATOM 1229 CE2 TRP A 277 58.867 -16.207 10.924 1.00 54.93 C ANISOU 1229 CE2 TRP A 277 6602 8932 5337 -1295 -234 -215 C ATOM 1230 CE3 TRP A 277 59.067 -17.624 8.976 1.00 60.97 C ANISOU 1230 CE3 TRP A 277 6950 10296 5918 -872 -159 -118 C ATOM 1231 CZ2 TRP A 277 60.176 -15.749 10.784 1.00 65.57 C ANISOU 1231 CZ2 TRP A 277 7746 10360 6808 -1577 -212 -138 C ATOM 1232 CZ3 TRP A 277 60.367 -17.170 8.841 1.00 58.67 C ANISOU 1232 CZ3 TRP A 277 6471 10094 5728 -1112 -112 9 C ATOM 1233 CH2 TRP A 277 60.907 -16.242 9.739 1.00 60.57 C ANISOU 1233 CH2 TRP A 277 6797 10075 6141 -1481 -140 -3 C ATOM 1234 N SER A 278 53.986 -19.248 7.100 1.00 41.66 N ANISOU 1234 N SER A 278 4649 8126 3053 240 -169 -513 N ATOM 1235 CA SER A 278 53.422 -20.450 6.501 1.00 50.28 C ANISOU 1235 CA SER A 278 5536 9465 4105 446 -271 -783 C ATOM 1236 C SER A 278 54.101 -20.807 5.183 1.00 59.64 C ANISOU 1236 C SER A 278 6500 11056 5106 628 -256 -791 C ATOM 1237 O SER A 278 54.761 -19.973 4.564 1.00 53.68 O ANISOU 1237 O SER A 278 5748 10427 4223 659 -126 -524 O ATOM 1238 CB SER A 278 51.919 -20.281 6.274 1.00 57.22 C ANISOU 1238 CB SER A 278 6442 10375 4923 635 -276 -864 C ATOM 1239 OG SER A 278 51.662 -19.343 5.244 1.00 60.15 O ANISOU 1239 OG SER A 278 6821 10985 5049 856 -170 -661 O ATOM 1240 N VAL A 279 53.925 -22.054 4.760 1.00 48.07 N ANISOU 1240 N VAL A 279 4849 9775 3640 759 -365 -1100 N ATOM 1241 CA VAL A 279 54.509 -22.530 3.510 1.00 64.03 C ANISOU 1241 CA VAL A 279 6672 12202 5456 981 -365 -1169 C ATOM 1242 C VAL A 279 53.670 -23.666 2.925 1.00 60.64 C ANISOU 1242 C VAL A 279 6081 11960 5000 1172 -499 -1597 C ATOM 1243 O VAL A 279 53.131 -24.499 3.658 1.00 60.51 O ANISOU 1243 O VAL A 279 6063 11691 5236 1050 -573 -1851 O ATOM 1244 CB VAL A 279 55.976 -22.999 3.715 1.00 66.04 C ANISOU 1244 CB VAL A 279 6849 12464 5780 864 -337 -1094 C ATOM 1245 CG1 VAL A 279 56.048 -24.148 4.713 1.00 48.58 C ANISOU 1245 CG1 VAL A 279 4637 9999 3820 730 -425 -1329 C ATOM 1246 CG2 VAL A 279 56.617 -23.390 2.388 1.00 65.00 C ANISOU 1246 CG2 VAL A 279 6529 12767 5402 1137 -299 -1119 C ATOM 1247 N HIS A 280 53.536 -23.671 1.602 1.00 56.71 N ANISOU 1247 N HIS A 280 5441 11793 4314 1458 -493 -1633 N ATOM 1248 CA HIS A 280 52.860 -24.751 0.895 1.00 54.35 C ANISOU 1248 CA HIS A 280 4954 11581 4117 1611 -602 -2024 C ATOM 1249 C HIS A 280 53.875 -25.828 0.534 1.00 62.98 C ANISOU 1249 C HIS A 280 5948 12744 5237 1659 -609 -2191 C ATOM 1250 O HIS A 280 54.702 -25.637 -0.361 1.00 67.71 O ANISOU 1250 O HIS A 280 6481 13630 5617 1858 -549 -2038 O ATOM 1251 CB HIS A 280 52.163 -24.224 -0.361 1.00 60.72 C ANISOU 1251 CB HIS A 280 5639 12728 4704 1931 -612 -1994 C ATOM 1252 CG HIS A 280 51.379 -25.261 -1.101 1.00 74.64 C ANISOU 1252 CG HIS A 280 7181 14625 6554 2074 -743 -2434 C ATOM 1253 ND1 HIS A 280 50.903 -26.407 -0.499 1.00 75.14 N ANISOU 1253 ND1 HIS A 280 7190 14429 6931 1876 -827 -2819 N ATOM 1254 CD2 HIS A 280 50.995 -25.332 -2.398 1.00 64.90 C ANISOU 1254 CD2 HIS A 280 5760 13764 5137 2397 -798 -2562 C ATOM 1255 CE1 HIS A 280 50.254 -27.133 -1.390 1.00 77.43 C ANISOU 1255 CE1 HIS A 280 7266 14910 7243 2035 -929 -3184 C ATOM 1256 NE2 HIS A 280 50.295 -26.504 -2.551 1.00 78.47 N ANISOU 1256 NE2 HIS A 280 7310 15446 7058 2360 -927 -3049 N ATOM 1257 N ALA A 281 53.812 -26.960 1.227 1.00 56.39 N ANISOU 1257 N ALA A 281 5108 11651 4667 1507 -660 -2487 N ATOM 1258 CA ALA A 281 54.826 -27.999 1.066 1.00 60.54 C ANISOU 1258 CA ALA A 281 5580 12206 5216 1560 -643 -2630 C ATOM 1259 C ALA A 281 54.241 -29.383 0.786 1.00 65.62 C ANISOU 1259 C ALA A 281 6119 12728 6088 1596 -722 -3108 C ATOM 1260 O ALA A 281 54.235 -30.242 1.667 1.00 74.02 O ANISOU 1260 O ALA A 281 7239 13475 7412 1440 -697 -3299 O ATOM 1261 CB ALA A 281 55.712 -28.052 2.310 1.00 57.71 C ANISOU 1261 CB ALA A 281 5345 11653 4929 1356 -579 -2471 C ATOM 1262 N APRO A 282 53.741 -29.600 -0.440 0.38 70.68 N ANISOU 1262 N APRO A 282 6604 13615 6636 1807 -807 -3310 N ATOM 1263 N BPRO A 282 53.758 -29.606 -0.447 0.62 71.26 N ANISOU 1263 N BPRO A 282 6677 13690 6707 1809 -806 -3310 N ATOM 1264 CA APRO A 282 53.189 -30.910 -0.794 0.38 74.45 C ANISOU 1264 CA APRO A 282 6963 13983 7340 1813 -894 -3799 C ATOM 1265 CA BPRO A 282 53.265 -30.933 -0.826 0.62 74.68 C ANISOU 1265 CA BPRO A 282 6995 14022 7359 1823 -892 -3795 C ATOM 1266 C APRO A 282 54.280 -31.930 -1.099 0.38 79.33 C ANISOU 1266 C APRO A 282 7603 14596 7943 1917 -863 -3932 C ATOM 1267 C BPRO A 282 54.409 -31.880 -1.165 0.62 80.52 C ANISOU 1267 C BPRO A 282 7757 14781 8056 1941 -858 -3900 C ATOM 1268 O APRO A 282 54.063 -33.130 -0.933 0.38 85.60 O ANISOU 1268 O APRO A 282 8390 15122 9012 1834 -869 -4302 O ATOM 1269 O BPRO A 282 54.212 -33.093 -1.223 0.62 88.46 O ANISOU 1269 O BPRO A 282 8737 15580 9295 1902 -882 -4287 O ATOM 1270 CB APRO A 282 52.359 -30.610 -2.043 0.38 77.12 C ANISOU 1270 CB APRO A 282 7119 14676 7509 2038 -1006 -3935 C ATOM 1271 CB BPRO A 282 52.414 -30.644 -2.062 0.62 77.15 C ANISOU 1271 CB BPRO A 282 7123 14682 7509 2044 -1005 -3938 C ATOM 1272 CG APRO A 282 53.059 -29.460 -2.673 0.38 73.89 C ANISOU 1272 CG APRO A 282 6743 14614 6718 2269 -945 -3508 C ATOM 1273 CG BPRO A 282 53.083 -29.471 -2.686 0.62 72.33 C ANISOU 1273 CG BPRO A 282 6545 14419 6517 2272 -945 -3508 C ATOM 1274 CD APRO A 282 53.606 -28.628 -1.540 0.38 70.64 C ANISOU 1274 CD APRO A 282 6522 14001 6318 2060 -819 -3107 C ATOM 1275 CD BPRO A 282 53.604 -28.631 -1.541 0.62 70.19 C ANISOU 1275 CD BPRO A 282 6464 13943 6260 2060 -819 -3108 C ATOM 1276 N ASER A 283 55.442 -31.452 -1.535 0.38 74.41 N ANISOU 1276 N ASER A 283 7010 14247 7014 2100 -802 -3620 N ATOM 1277 N BSER A 283 55.595 -31.320 -1.385 0.62 74.54 N ANISOU 1277 N BSER A 283 7048 14258 7016 2083 -779 -3546 N ATOM 1278 CA ASER A 283 56.532 -32.336 -1.925 0.38 74.53 C ANISOU 1278 CA ASER A 283 7043 14319 6955 2260 -755 -3696 C ATOM 1279 CA BSER A 283 56.753 -32.108 -1.783 0.62 77.56 C ANISOU 1279 CA BSER A 283 7445 14726 7300 2252 -725 -3582 C ATOM 1280 C ASER A 283 57.898 -31.784 -1.523 0.38 80.16 C ANISOU 1280 C ASER A 283 7819 15164 7476 2298 -608 -3261 C ATOM 1281 C BSER A 283 57.878 -32.052 -0.748 0.62 87.81 C ANISOU 1281 C BSER A 283 8849 15910 8606 2160 -566 -3301 C ATOM 1282 O ASER A 283 58.783 -31.631 -2.366 0.38 64.43 O ANISOU 1282 O ASER A 283 5772 13492 5216 2538 -570 -3080 O ATOM 1283 O BSER A 283 58.212 -33.061 -0.125 0.62 97.07 O ANISOU 1283 O BSER A 283 10093 16808 9983 2120 -482 -3465 O ATOM 1284 CB ASER A 283 56.496 -32.581 -3.435 0.38 80.99 C ANISOU 1284 CB ASER A 283 7738 15487 7547 2565 -861 -3865 C ATOM 1285 CB BSER A 283 57.275 -31.630 -3.142 0.62 79.11 C ANISOU 1285 CB BSER A 283 7545 15385 7128 2577 -751 -3415 C ATOM 1286 OG ASER A 283 55.272 -33.173 -3.836 0.38 83.56 O ANISOU 1286 OG ASER A 283 7956 15738 8054 2526 -1003 -4313 O ATOM 1287 OG BSER A 283 56.282 -31.741 -4.153 0.62 68.49 O ANISOU 1287 OG BSER A 283 6072 14213 5736 2726 -899 -3696 O ATOM 1288 N ASER A 284 58.063 -31.498 -0.233 0.38 78.20 N ANISOU 1288 N ASER A 284 7660 14689 7363 2069 -520 -3096 N ATOM 1289 N BSER A 284 58.452 -30.868 -0.564 0.62 79.29 N ANISOU 1289 N BSER A 284 7766 15041 7321 2137 -498 -2870 N ATOM 1290 CA ASER A 284 59.331 -31.006 0.304 0.38 69.92 C ANISOU 1290 CA ASER A 284 6618 13780 6166 2061 -381 -2710 C ATOM 1291 CA BSER A 284 59.662 -30.718 0.240 0.62 67.10 C ANISOU 1291 CA BSER A 284 6240 13527 5726 2080 -353 -2576 C ATOM 1292 C ASER A 284 59.303 -30.962 1.828 0.38 68.11 C ANISOU 1292 C ASER A 284 6489 13192 6199 1784 -334 -2591 C ATOM 1293 C BSER A 284 59.436 -30.750 1.748 0.62 68.53 C ANISOU 1293 C BSER A 284 6529 13311 6200 1790 -331 -2519 C ATOM 1294 O ASER A 284 58.271 -30.660 2.426 0.38 63.50 O ANISOU 1294 O ASER A 284 5986 12349 5791 1586 -400 -2658 O ATOM 1295 O BSER A 284 58.396 -30.326 2.251 0.62 62.98 O ANISOU 1295 O BSER A 284 5904 12388 5638 1600 -404 -2571 O ATOM 1296 CB ASER A 284 59.650 -29.611 -0.244 0.38 63.57 C ANISOU 1296 CB ASER A 284 5755 13310 5089 2095 -355 -2307 C ATOM 1297 CB BSER A 284 60.370 -29.409 -0.119 0.62 68.46 C ANISOU 1297 CB BSER A 284 6342 14039 5629 2100 -278 -2116 C ATOM 1298 OG ASER A 284 58.604 -28.698 0.042 0.38 54.10 O ANISOU 1298 OG ASER A 284 4621 11994 3938 1928 -417 -2251 O ATOM 1299 OG BSER A 284 60.937 -29.468 -1.412 0.62 86.51 O ANISOU 1299 OG BSER A 284 8526 16647 7697 2397 -253 -2032 O ATOM 1300 N ARG A 285 60.434 -31.267 2.456 1.00 69.87 N ANISOU 1300 N ARG A 285 6694 13364 6488 1778 -236 -2351 N ATOM 1301 CA ARG A 285 60.555 -31.082 3.893 1.00 73.27 C ANISOU 1301 CA ARG A 285 7206 13480 7152 1535 -225 -2126 C ATOM 1302 C ARG A 285 61.378 -29.814 4.056 1.00 74.16 C ANISOU 1302 C ARG A 285 7242 13820 7114 1395 -235 -1703 C ATOM 1303 O ARG A 285 62.230 -29.515 3.219 1.00 86.88 O ANISOU 1303 O ARG A 285 8709 15792 8510 1528 -181 -1543 O ATOM 1304 CB ARG A 285 61.211 -32.283 4.577 1.00 73.94 C ANISOU 1304 CB ARG A 285 7311 13374 7410 1646 -112 -2151 C ATOM 1305 CG ARG A 285 60.343 -33.533 4.574 1.00 83.77 C ANISOU 1305 CG ARG A 285 8657 14262 8909 1727 -48 -2563 C ATOM 1306 CD ARG A 285 60.943 -34.641 5.423 1.00 88.68 C ANISOU 1306 CD ARG A 285 9342 14619 9733 1852 123 -2504 C ATOM 1307 NE ARG A 285 60.612 -34.507 6.838 1.00 84.50 N ANISOU 1307 NE ARG A 285 8924 13769 9414 1685 152 -2310 N ATOM 1308 CZ ARG A 285 60.428 -35.536 7.660 1.00 79.78 C ANISOU 1308 CZ ARG A 285 8444 12776 9095 1770 331 -2346 C ATOM 1309 NH1 ARG A 285 60.542 -36.778 7.208 1.00 81.07 N ANISOU 1309 NH1 ARG A 285 8638 12762 9403 1985 505 -2588 N ATOM 1310 NH2 ARG A 285 60.131 -35.324 8.933 1.00 92.14 N ANISOU 1310 NH2 ARG A 285 10111 14108 10791 1666 363 -2134 N ATOM 1311 N ARG A 286 61.115 -29.056 5.111 1.00 59.98 N ANISOU 1311 N ARG A 286 5539 11806 5443 1127 -288 -1532 N ATOM 1312 CA ARG A 286 61.641 -27.700 5.199 1.00 58.57 C ANISOU 1312 CA ARG A 286 5313 11768 5172 933 -302 -1205 C ATOM 1313 C ARG A 286 62.886 -27.590 6.071 1.00 60.71 C ANISOU 1313 C ARG A 286 5472 12105 5491 808 -305 -966 C ATOM 1314 O ARG A 286 63.189 -28.482 6.861 1.00 75.46 O ANISOU 1314 O ARG A 286 7346 13872 7454 877 -309 -1020 O ATOM 1315 CB ARG A 286 60.558 -26.760 5.723 1.00 53.11 C ANISOU 1315 CB ARG A 286 4804 10818 4559 719 -363 -1191 C ATOM 1316 CG ARG A 286 59.202 -26.934 5.059 1.00 56.10 C ANISOU 1316 CG ARG A 286 5260 11142 4912 839 -388 -1450 C ATOM 1317 CD ARG A 286 59.300 -26.842 3.544 1.00 59.22 C ANISOU 1317 CD ARG A 286 5531 11922 5046 1085 -352 -1488 C ATOM 1318 NE ARG A 286 59.972 -25.619 3.119 1.00 66.66 N ANISOU 1318 NE ARG A 286 6423 13072 5833 1035 -267 -1124 N ATOM 1319 CZ ARG A 286 60.079 -25.228 1.854 1.00 64.13 C ANISOU 1319 CZ ARG A 286 6016 13099 5252 1266 -186 -1034 C ATOM 1320 NH1 ARG A 286 59.553 -25.965 0.887 1.00 65.18 N ANISOU 1320 NH1 ARG A 286 6100 13458 5206 1570 -230 -1333 N ATOM 1321 NH2 ARG A 286 60.712 -24.100 1.558 1.00 55.01 N ANISOU 1321 NH2 ARG A 286 4820 12064 4018 1201 -49 -654 N ATOM 1322 N THR A 287 63.602 -26.481 5.916 1.00 58.36 N ANISOU 1322 N THR A 287 5057 11985 5134 633 -290 -700 N ATOM 1323 CA THR A 287 64.832 -26.238 6.660 1.00 63.47 C ANISOU 1323 CA THR A 287 5524 12763 5827 472 -322 -500 C ATOM 1324 C THR A 287 64.830 -24.863 7.327 1.00 55.10 C ANISOU 1324 C THR A 287 4516 11558 4862 97 -385 -361 C ATOM 1325 O THR A 287 65.771 -24.508 8.034 1.00 66.22 O ANISOU 1325 O THR A 287 5764 13066 6329 -103 -452 -250 O ATOM 1326 CB THR A 287 66.070 -26.341 5.747 1.00 65.54 C ANISOU 1326 CB THR A 287 5487 13444 5972 610 -209 -312 C ATOM 1327 OG1 THR A 287 65.963 -25.385 4.685 1.00 73.16 O ANISOU 1327 OG1 THR A 287 6420 14525 6853 580 -93 -156 O ATOM 1328 CG2 THR A 287 66.190 -27.739 5.157 1.00 69.75 C ANISOU 1328 CG2 THR A 287 5987 14111 6402 1005 -138 -469 C HETATM 1329 N TPO A 288 63.769 -24.095 7.098 1.00 48.70 N ANISOU 1329 N TPO A 288 3921 10520 4062 12 -364 -389 N HETATM 1330 CA TPO A 288 63.690 -22.721 7.585 1.00 62.18 C ANISOU 1330 CA TPO A 288 5726 12034 5865 -319 -376 -263 C HETATM 1331 CB TPO A 288 62.634 -21.936 6.793 1.00 59.90 C ANISOU 1331 CB TPO A 288 5625 11612 5523 -271 -265 -216 C HETATM 1332 CG2 TPO A 288 62.536 -20.505 7.327 1.00 55.36 C ANISOU 1332 CG2 TPO A 288 5198 10765 5072 -599 -233 -83 C HETATM 1333 OG1 TPO A 288 63.011 -21.896 5.418 1.00 58.83 O ANISOU 1333 OG1 TPO A 288 5325 11782 5247 -70 -107 -66 O HETATM 1334 P TPO A 288 61.765 -22.346 4.499 1.00 60.01 P ANISOU 1334 P TPO A 288 5601 11984 5217 270 -88 -233 P HETATM 1335 O1P TPO A 288 62.290 -22.537 2.988 1.00 78.05 O ANISOU 1335 O1P TPO A 288 7690 14697 7269 586 63 -111 O HETATM 1336 O2P TPO A 288 61.153 -23.736 5.028 1.00 57.18 O ANISOU 1336 O2P TPO A 288 5301 11522 4903 402 -238 -584 O HETATM 1337 O3P TPO A 288 60.713 -21.306 4.525 1.00 59.27 O ANISOU 1337 O3P TPO A 288 5734 11661 5124 205 -45 -168 O HETATM 1338 C TPO A 288 63.414 -22.628 9.088 1.00 61.94 C ANISOU 1338 C TPO A 288 5862 11735 5936 -505 -534 -383 C HETATM 1339 O TPO A 288 62.460 -23.216 9.597 1.00 60.67 O ANISOU 1339 O TPO A 288 5901 11368 5781 -378 -582 -546 O ATOM 1340 N LEU A 289 64.264 -21.892 9.796 1.00 61.05 N ANISOU 1340 N LEU A 289 5651 11641 5905 -800 -609 -311 N ATOM 1341 CA LEU A 289 64.004 -21.566 11.191 1.00 56.37 C ANISOU 1341 CA LEU A 289 5238 10818 5361 -975 -767 -436 C ATOM 1342 C LEU A 289 62.818 -20.605 11.233 1.00 58.83 C ANISOU 1342 C LEU A 289 5883 10753 5716 -1077 -708 -454 C ATOM 1343 O LEU A 289 62.979 -19.398 11.051 1.00 73.75 O ANISOU 1343 O LEU A 289 7813 12515 7694 -1333 -640 -357 O ATOM 1344 CB LEU A 289 65.247 -20.956 11.846 1.00 54.63 C ANISOU 1344 CB LEU A 289 4790 10757 5209 -1283 -889 -415 C ATOM 1345 CG LEU A 289 65.319 -20.797 13.372 1.00 74.60 C ANISOU 1345 CG LEU A 289 7422 13205 7719 -1414 -1109 -589 C ATOM 1346 CD1 LEU A 289 64.711 -19.478 13.818 1.00 85.50 C ANISOU 1346 CD1 LEU A 289 9087 14205 9194 -1709 -1120 -664 C ATOM 1347 CD2 LEU A 289 64.658 -21.967 14.096 1.00 59.01 C ANISOU 1347 CD2 LEU A 289 5618 11187 5617 -1066 -1161 -683 C ATOM 1348 N ALA A 290 61.626 -21.152 11.452 1.00 54.34 N ANISOU 1348 N ALA A 290 5542 9997 5106 -866 -705 -563 N ATOM 1349 CA ALA A 290 60.395 -20.372 11.380 1.00 58.48 C ANISOU 1349 CA ALA A 290 6357 10218 5646 -881 -630 -562 C ATOM 1350 C ALA A 290 59.560 -20.494 12.651 1.00 64.56 C ANISOU 1350 C ALA A 290 7389 10718 6424 -855 -715 -692 C ATOM 1351 O ALA A 290 59.400 -21.584 13.191 1.00 64.75 O ANISOU 1351 O ALA A 290 7396 10769 6435 -675 -763 -783 O ATOM 1352 CB ALA A 290 59.572 -20.807 10.175 1.00 44.63 C ANISOU 1352 CB ALA A 290 4587 8545 3826 -621 -514 -554 C ATOM 1353 N GLY A 291 59.018 -19.371 13.113 1.00 69.87 N ANISOU 1353 N GLY A 291 8317 11110 7119 -1005 -695 -678 N ATOM 1354 CA GLY A 291 58.132 -19.376 14.263 1.00 69.69 C ANISOU 1354 CA GLY A 291 8571 10832 7076 -939 -742 -776 C ATOM 1355 C GLY A 291 58.511 -18.382 15.343 1.00 70.33 C ANISOU 1355 C GLY A 291 8831 10741 7151 -1177 -840 -842 C ATOM 1356 O GLY A 291 59.082 -17.327 15.061 1.00 67.86 O ANISOU 1356 O GLY A 291 8510 10364 6908 -1443 -816 -805 O ATOM 1357 N THR A 292 58.182 -18.729 16.586 1.00 64.02 N ANISOU 1357 N THR A 292 8195 9855 6273 -1070 -935 -950 N ATOM 1358 CA THR A 292 58.459 -17.886 17.745 1.00 59.35 C ANISOU 1358 CA THR A 292 7802 9129 5621 -1239 -1063 -1081 C ATOM 1359 C THR A 292 59.154 -18.709 18.831 1.00 59.11 C ANISOU 1359 C THR A 292 7660 9345 5452 -1125 -1249 -1188 C ATOM 1360 O THR A 292 58.831 -19.882 19.022 1.00 56.41 O ANISOU 1360 O THR A 292 7271 9098 5065 -827 -1205 -1130 O ATOM 1361 CB THR A 292 57.162 -17.258 18.306 1.00 69.51 C ANISOU 1361 CB THR A 292 9489 10054 6869 -1134 -967 -1091 C ATOM 1362 OG1 THR A 292 56.501 -16.518 17.270 1.00 69.27 O ANISOU 1362 OG1 THR A 292 9546 9838 6934 -1175 -779 -959 O ATOM 1363 CG2 THR A 292 57.459 -16.332 19.493 1.00 55.55 C ANISOU 1363 CG2 THR A 292 7960 8132 5013 -1297 -1105 -1277 C ATOM 1364 N LEU A 293 60.101 -18.080 19.528 1.00 48.85 N ANISOU 1364 N LEU A 293 7204 6337 5022 -133 -1168 -31 N ATOM 1365 CA LEU A 293 60.983 -18.732 20.504 1.00 58.12 C ANISOU 1365 CA LEU A 293 8413 7592 6079 -178 -1282 -64 C ATOM 1366 C LEU A 293 60.345 -19.818 21.374 1.00 58.37 C ANISOU 1366 C LEU A 293 8552 7746 5878 -14 -1120 -171 C ATOM 1367 O LEU A 293 60.766 -20.973 21.331 1.00 57.87 O ANISOU 1367 O LEU A 293 8359 7851 5778 9 -1018 -61 O ATOM 1368 CB LEU A 293 61.601 -17.672 21.424 1.00 62.47 C ANISOU 1368 CB LEU A 293 9116 7951 6667 -298 -1573 -193 C ATOM 1369 CG LEU A 293 62.429 -18.206 22.596 1.00 63.85 C ANISOU 1369 CG LEU A 293 9345 8258 6658 -329 -1744 -251 C ATOM 1370 CD1 LEU A 293 63.678 -18.904 22.088 1.00 65.81 C ANISOU 1370 CD1 LEU A 293 9311 8682 7012 -442 -1792 16 C ATOM 1371 CD2 LEU A 293 62.793 -17.094 23.569 1.00 63.23 C ANISOU 1371 CD2 LEU A 293 9458 7998 6568 -438 -2049 -488 C ATOM 1372 N ASP A 294 59.337 -19.449 22.161 1.00 59.95 N ANISOU 1372 N ASP A 294 8979 7849 5951 116 -1068 -360 N ATOM 1373 CA ASP A 294 58.779 -20.369 23.151 1.00 63.05 C ANISOU 1373 CA ASP A 294 9477 8353 6125 287 -911 -421 C ATOM 1374 C ASP A 294 58.009 -21.529 22.531 1.00 63.16 C ANISOU 1374 C ASP A 294 9332 8470 6194 382 -614 -337 C ATOM 1375 O ASP A 294 57.662 -22.489 23.221 1.00 51.19 O ANISOU 1375 O ASP A 294 7834 7038 4579 509 -443 -315 O ATOM 1376 CB ASP A 294 57.867 -19.621 24.128 1.00 54.83 C ANISOU 1376 CB ASP A 294 8717 7191 4926 430 -899 -637 C ATOM 1377 CG ASP A 294 58.646 -18.869 25.191 1.00 55.69 C ANISOU 1377 CG ASP A 294 9025 7254 4882 372 -1183 -799 C ATOM 1378 OD1 ASP A 294 59.230 -19.535 26.068 1.00 57.75 O ANISOU 1378 OD1 ASP A 294 9311 7709 4925 410 -1248 -771 O ATOM 1379 OD2 ASP A 294 58.662 -17.620 25.160 1.00 53.45 O ANISOU 1379 OD2 ASP A 294 8863 6744 4702 294 -1342 -959 O ATOM 1380 N TYR A 295 57.756 -21.445 21.229 1.00 50.38 N ANISOU 1380 N TYR A 295 7544 6854 4743 319 -553 -285 N ATOM 1381 CA TYR A 295 56.920 -22.426 20.548 1.00 57.94 C ANISOU 1381 CA TYR A 295 8346 7902 5767 382 -309 -280 C ATOM 1382 C TYR A 295 57.704 -23.224 19.513 1.00 51.37 C ANISOU 1382 C TYR A 295 7284 7197 5037 285 -272 -180 C ATOM 1383 O TYR A 295 57.153 -24.106 18.854 1.00 51.18 O ANISOU 1383 O TYR A 295 7116 7246 5082 308 -90 -224 O ATOM 1384 CB TYR A 295 55.725 -21.726 19.893 1.00 56.89 C ANISOU 1384 CB TYR A 295 8201 7725 5688 431 -253 -344 C ATOM 1385 CG TYR A 295 54.875 -20.974 20.891 1.00 72.46 C ANISOU 1385 CG TYR A 295 10397 9556 7579 563 -234 -446 C ATOM 1386 CD1 TYR A 295 55.225 -19.694 21.302 1.00 85.24 C ANISOU 1386 CD1 TYR A 295 12198 11012 9179 541 -418 -497 C ATOM 1387 CD2 TYR A 295 53.736 -21.549 21.438 1.00 64.54 C ANISOU 1387 CD2 TYR A 295 9416 8562 6542 716 -16 -496 C ATOM 1388 CE1 TYR A 295 54.464 -19.007 22.224 1.00 79.76 C ANISOU 1388 CE1 TYR A 295 11730 10177 8399 684 -379 -631 C ATOM 1389 CE2 TYR A 295 52.966 -20.866 22.364 1.00 62.36 C ANISOU 1389 CE2 TYR A 295 9348 8174 6172 873 38 -579 C ATOM 1390 CZ TYR A 295 53.337 -19.595 22.750 1.00 71.30 C ANISOU 1390 CZ TYR A 295 10687 9154 7251 866 -142 -664 C ATOM 1391 OH TYR A 295 52.584 -18.901 23.667 1.00 91.89 O ANISOU 1391 OH TYR A 295 13523 11636 9755 1042 -70 -788 O ATOM 1392 N LEU A 296 58.993 -22.923 19.386 1.00 52.70 N ANISOU 1392 N LEU A 296 7409 7387 5227 177 -441 -61 N ATOM 1393 CA LEU A 296 59.839 -23.589 18.398 1.00 48.26 C ANISOU 1393 CA LEU A 296 6632 6952 4754 110 -389 55 C ATOM 1394 C LEU A 296 59.991 -25.078 18.689 1.00 48.15 C ANISOU 1394 C LEU A 296 6537 6985 4773 175 -186 63 C ATOM 1395 O LEU A 296 60.303 -25.468 19.814 1.00 52.13 O ANISOU 1395 O LEU A 296 7117 7461 5228 228 -191 120 O ATOM 1396 CB LEU A 296 61.219 -22.929 18.341 1.00 46.43 C ANISOU 1396 CB LEU A 296 6347 6722 4574 -12 -603 226 C ATOM 1397 CG LEU A 296 61.319 -21.561 17.665 1.00 47.65 C ANISOU 1397 CG LEU A 296 6487 6812 4805 -100 -758 291 C ATOM 1398 CD1 LEU A 296 62.714 -20.990 17.851 1.00 48.87 C ANISOU 1398 CD1 LEU A 296 6570 6926 5070 -243 -975 463 C ATOM 1399 CD2 LEU A 296 60.967 -21.659 16.181 1.00 52.73 C ANISOU 1399 CD2 LEU A 296 6961 7605 5468 -74 -621 347 C ATOM 1400 N PRO A 297 59.768 -25.918 17.669 1.00 52.39 N ANISOU 1400 N PRO A 297 6914 7598 5395 182 -2 5 N ATOM 1401 CA PRO A 297 59.947 -27.367 17.810 1.00 45.30 C ANISOU 1401 CA PRO A 297 5917 6684 4611 238 224 1 C ATOM 1402 C PRO A 297 61.421 -27.745 17.937 1.00 45.75 C ANISOU 1402 C PRO A 297 5881 6784 4719 223 198 211 C ATOM 1403 O PRO A 297 62.283 -26.986 17.489 1.00 47.21 O ANISOU 1403 O PRO A 297 6018 7046 4874 145 28 331 O ATOM 1404 CB PRO A 297 59.345 -27.920 16.516 1.00 51.18 C ANISOU 1404 CB PRO A 297 6523 7499 5426 221 376 -186 C ATOM 1405 CG PRO A 297 59.504 -26.809 15.531 1.00 51.66 C ANISOU 1405 CG PRO A 297 6557 7704 5370 162 207 -157 C ATOM 1406 CD PRO A 297 59.296 -25.547 16.323 1.00 53.01 C ANISOU 1406 CD PRO A 297 6893 7787 5463 149 5 -76 C ATOM 1407 N PRO A 298 61.706 -28.905 18.548 1.00 45.25 N ANISOU 1407 N PRO A 298 5765 6665 4763 307 380 292 N ATOM 1408 CA PRO A 298 63.081 -29.379 18.743 1.00 53.62 C ANISOU 1408 CA PRO A 298 6704 7774 5894 326 382 533 C ATOM 1409 C PRO A 298 63.854 -29.560 17.439 1.00 48.26 C ANISOU 1409 C PRO A 298 5853 7179 5305 286 450 555 C ATOM 1410 O PRO A 298 65.054 -29.284 17.414 1.00 50.53 O ANISOU 1410 O PRO A 298 6041 7553 5606 257 338 781 O ATOM 1411 CB PRO A 298 62.888 -30.728 19.443 1.00 50.26 C ANISOU 1411 CB PRO A 298 6234 7241 5620 458 655 599 C ATOM 1412 CG PRO A 298 61.570 -30.619 20.113 1.00 55.49 C ANISOU 1412 CG PRO A 298 7045 7821 6219 502 696 464 C ATOM 1413 CD PRO A 298 60.724 -29.800 19.187 1.00 44.29 C ANISOU 1413 CD PRO A 298 5676 6421 4731 404 603 213 C ATOM 1414 N GLU A 299 63.185 -30.011 16.378 1.00 49.72 N ANISOU 1414 N GLU A 299 5990 7363 5537 291 627 321 N ATOM 1415 CA GLU A 299 63.868 -30.261 15.108 1.00 51.38 C ANISOU 1415 CA GLU A 299 6051 7693 5778 293 729 309 C ATOM 1416 C GLU A 299 64.454 -28.980 14.522 1.00 51.14 C ANISOU 1416 C GLU A 299 5994 7829 5608 216 501 460 C ATOM 1417 O GLU A 299 65.528 -29.003 13.922 1.00 55.61 O ANISOU 1417 O GLU A 299 6415 8504 6208 230 538 638 O ATOM 1418 CB GLU A 299 62.924 -30.926 14.094 1.00 44.65 C ANISOU 1418 CB GLU A 299 5169 6851 4946 308 921 -39 C ATOM 1419 CG GLU A 299 61.562 -30.259 13.932 1.00 40.85 C ANISOU 1419 CG GLU A 299 4784 6403 4335 249 800 -251 C ATOM 1420 CD GLU A 299 60.523 -30.815 14.889 1.00 59.19 C ANISOU 1420 CD GLU A 299 7180 8523 6788 266 891 -364 C ATOM 1421 OE1 GLU A 299 60.855 -31.025 16.078 1.00 48.15 O ANISOU 1421 OE1 GLU A 299 5836 6996 5463 314 907 -167 O ATOM 1422 OE2 GLU A 299 59.376 -31.047 14.451 1.00 51.56 O ANISOU 1422 OE2 GLU A 299 6195 7551 5846 237 946 -631 O ATOM 1423 N MET A 300 63.758 -27.863 14.705 1.00 59.71 N ANISOU 1423 N MET A 300 7201 8913 6573 145 292 417 N ATOM 1424 CA MET A 300 64.265 -26.577 14.236 1.00 57.88 C ANISOU 1424 CA MET A 300 6937 8775 6280 66 87 592 C ATOM 1425 C MET A 300 65.463 -26.125 15.058 1.00 63.81 C ANISOU 1425 C MET A 300 7650 9476 7119 -3 -98 865 C ATOM 1426 O MET A 300 66.462 -25.657 14.511 1.00 62.43 O ANISOU 1426 O MET A 300 7323 9389 7008 -52 -160 1094 O ATOM 1427 CB MET A 300 63.173 -25.510 14.287 1.00 54.46 C ANISOU 1427 CB MET A 300 6643 8299 5749 26 -64 481 C ATOM 1428 CG MET A 300 62.100 -25.660 13.231 1.00 47.90 C ANISOU 1428 CG MET A 300 5786 7602 4814 75 52 273 C ATOM 1429 SD MET A 300 61.061 -24.192 13.160 1.00 53.76 S ANISOU 1429 SD MET A 300 6631 8320 5477 52 -129 272 S ATOM 1430 CE MET A 300 59.782 -24.735 12.027 1.00 53.87 C ANISOU 1430 CE MET A 300 6562 8553 5354 123 9 14 C ATOM 1431 N ILE A 301 65.349 -26.260 16.377 1.00 56.14 N ANISOU 1431 N ILE A 301 6800 8388 6143 -4 -192 849 N ATOM 1432 CA ILE A 301 66.422 -25.885 17.288 1.00 59.24 C ANISOU 1432 CA ILE A 301 7154 8773 6581 -75 -413 1063 C ATOM 1433 C ILE A 301 67.681 -26.698 17.014 1.00 57.37 C ANISOU 1433 C ILE A 301 6682 8638 6479 -34 -296 1312 C ATOM 1434 O ILE A 301 68.793 -26.169 17.032 1.00 54.03 O ANISOU 1434 O ILE A 301 6110 8272 6148 -126 -469 1553 O ATOM 1435 CB ILE A 301 66.008 -26.089 18.765 1.00 69.12 C ANISOU 1435 CB ILE A 301 8580 9956 7728 -30 -496 988 C ATOM 1436 CG1 ILE A 301 64.706 -25.347 19.070 1.00 69.45 C ANISOU 1436 CG1 ILE A 301 8855 9890 7641 -33 -560 741 C ATOM 1437 CG2 ILE A 301 67.115 -25.634 19.703 1.00 71.11 C ANISOU 1437 CG2 ILE A 301 8786 10258 7975 -115 -783 1172 C ATOM 1438 CD1 ILE A 301 64.790 -23.861 18.845 1.00 75.34 C ANISOU 1438 CD1 ILE A 301 9658 10570 8399 -170 -814 725 C ATOM 1439 N GLU A 302 67.494 -27.989 16.755 1.00 48.59 N ANISOU 1439 N GLU A 302 5521 7526 5417 104 10 1255 N ATOM 1440 CA GLU A 302 68.611 -28.911 16.579 1.00 44.68 C ANISOU 1440 CA GLU A 302 4810 7090 5075 190 182 1486 C ATOM 1441 C GLU A 302 69.126 -28.931 15.139 1.00 66.51 C ANISOU 1441 C GLU A 302 7412 9968 7892 213 343 1535 C ATOM 1442 O GLU A 302 69.891 -29.817 14.757 1.00 71.03 O ANISOU 1442 O GLU A 302 7815 10578 8593 325 576 1666 O ATOM 1443 CB GLU A 302 68.193 -30.316 17.015 1.00 44.75 C ANISOU 1443 CB GLU A 302 4839 6993 5172 344 472 1409 C ATOM 1444 CG GLU A 302 67.878 -30.424 18.506 1.00 55.17 C ANISOU 1444 CG GLU A 302 6277 8260 6427 374 358 1466 C ATOM 1445 CD GLU A 302 67.047 -31.645 18.845 1.00 63.85 C ANISOU 1445 CD GLU A 302 7425 9207 7629 515 670 1355 C ATOM 1446 OE1 GLU A 302 66.478 -32.256 17.914 1.00 64.74 O ANISOU 1446 OE1 GLU A 302 7520 9221 7856 542 923 1127 O ATOM 1447 OE2 GLU A 302 66.957 -31.992 20.043 1.00 69.17 O ANISOU 1447 OE2 GLU A 302 8142 9867 8273 600 661 1496 O ATOM 1448 N GLY A 303 68.702 -27.950 14.347 1.00 60.01 N ANISOU 1448 N GLY A 303 6633 9207 6960 132 241 1449 N ATOM 1449 CA GLY A 303 69.180 -27.797 12.983 1.00 66.04 C ANISOU 1449 CA GLY A 303 7243 10139 7711 172 376 1539 C ATOM 1450 C GLY A 303 68.803 -28.942 12.061 1.00 56.28 C ANISOU 1450 C GLY A 303 5992 8965 6426 325 719 1299 C ATOM 1451 O GLY A 303 69.531 -29.258 11.122 1.00 62.59 O ANISOU 1451 O GLY A 303 6635 9913 7233 422 913 1402 O ATOM 1452 N ARG A 304 67.666 -29.569 12.336 1.00 61.53 N ANISOU 1452 N ARG A 304 6813 9510 7054 348 802 965 N ATOM 1453 CA ARG A 304 67.182 -30.665 11.511 1.00 66.70 C ANISOU 1453 CA ARG A 304 7463 10181 7700 456 1099 651 C ATOM 1454 C ARG A 304 66.167 -30.146 10.501 1.00 66.08 C ANISOU 1454 C ARG A 304 7450 10275 7383 430 1051 382 C ATOM 1455 O ARG A 304 65.842 -28.960 10.491 1.00 67.40 O ANISOU 1455 O ARG A 304 7664 10519 7426 348 818 484 O ATOM 1456 CB ARG A 304 66.553 -31.762 12.378 1.00 45.30 C ANISOU 1456 CB ARG A 304 4832 7216 5165 488 1241 463 C ATOM 1457 CG ARG A 304 67.391 -32.175 13.582 1.00 55.19 C ANISOU 1457 CG ARG A 304 6028 8329 6614 529 1247 778 C ATOM 1458 CD ARG A 304 66.647 -33.187 14.449 1.00 52.24 C ANISOU 1458 CD ARG A 304 5727 7712 6412 580 1408 645 C ATOM 1459 NE ARG A 304 66.599 -34.510 13.834 1.00 67.51 N ANISOU 1459 NE ARG A 304 7585 9506 8560 687 1773 437 N ATOM 1460 CZ ARG A 304 65.859 -35.518 14.284 1.00 66.75 C ANISOU 1460 CZ ARG A 304 7518 9154 8691 725 1984 267 C ATOM 1461 NH1 ARG A 304 65.089 -35.353 15.350 1.00 69.96 N ANISOU 1461 NH1 ARG A 304 8024 9459 9099 688 1878 315 N ATOM 1462 NH2 ARG A 304 65.880 -36.689 13.662 1.00 69.39 N ANISOU 1462 NH2 ARG A 304 7776 9319 9269 808 2318 45 N ATOM 1463 N MET A 305 65.672 -31.037 9.651 1.00 59.98 N ANISOU 1463 N MET A 305 6670 9564 6558 505 1268 33 N ATOM 1464 CA MET A 305 64.591 -30.685 8.741 1.00 56.23 C ANISOU 1464 CA MET A 305 6238 9292 5835 484 1203 -261 C ATOM 1465 C MET A 305 63.253 -30.892 9.439 1.00 61.27 C ANISOU 1465 C MET A 305 6992 9736 6550 397 1128 -526 C ATOM 1466 O MET A 305 63.169 -31.628 10.424 1.00 56.73 O ANISOU 1466 O MET A 305 6456 8877 6222 387 1217 -548 O ATOM 1467 CB MET A 305 64.668 -31.513 7.460 1.00 51.50 C ANISOU 1467 CB MET A 305 5569 8898 5102 597 1437 -565 C ATOM 1468 CG MET A 305 66.020 -31.436 6.775 1.00 59.33 C ANISOU 1468 CG MET A 305 6434 10084 6026 725 1581 -288 C ATOM 1469 SD MET A 305 66.009 -32.178 5.138 1.00 70.23 S ANISOU 1469 SD MET A 305 7763 11804 7117 892 1837 -681 S ATOM 1470 CE MET A 305 64.820 -31.121 4.324 1.00 62.55 C ANISOU 1470 CE MET A 305 6822 11215 5730 842 1575 -806 C ATOM 1471 N HIS A 306 62.210 -30.239 8.940 1.00 49.87 N ANISOU 1471 N HIS A 306 5580 8462 4906 353 979 -680 N ATOM 1472 CA HIS A 306 60.903 -30.338 9.577 1.00 59.78 C ANISOU 1472 CA HIS A 306 6914 9556 6244 279 909 -891 C ATOM 1473 C HIS A 306 59.764 -30.430 8.566 1.00 60.86 C ANISOU 1473 C HIS A 306 7000 9924 6201 262 876 -1250 C ATOM 1474 O HIS A 306 59.929 -30.100 7.388 1.00 56.17 O ANISOU 1474 O HIS A 306 6333 9676 5332 317 848 -1286 O ATOM 1475 CB HIS A 306 60.681 -29.145 10.513 1.00 56.59 C ANISOU 1475 CB HIS A 306 6612 9057 5832 228 686 -614 C ATOM 1476 CG HIS A 306 60.465 -27.843 9.803 1.00 53.13 C ANISOU 1476 CG HIS A 306 6158 8863 5166 227 502 -474 C ATOM 1477 ND1 HIS A 306 61.490 -26.960 9.538 1.00 52.03 N ANISOU 1477 ND1 HIS A 306 5977 8822 4969 240 421 -134 N ATOM 1478 CD2 HIS A 306 59.338 -27.267 9.321 1.00 44.63 C ANISOU 1478 CD2 HIS A 306 5073 7942 3941 224 395 -585 C ATOM 1479 CE1 HIS A 306 61.005 -25.900 8.917 1.00 49.67 C ANISOU 1479 CE1 HIS A 306 5656 8708 4510 251 292 -32 C ATOM 1480 NE2 HIS A 306 59.701 -26.060 8.774 1.00 48.63 N ANISOU 1480 NE2 HIS A 306 5545 8629 4304 252 271 -296 N ATOM 1481 N ASP A 307 58.613 -30.897 9.043 1.00 52.36 N ANISOU 1481 N ASP A 307 5938 8678 5277 193 881 -1497 N ATOM 1482 CA ASP A 307 57.410 -31.005 8.227 1.00 57.66 C ANISOU 1482 CA ASP A 307 6528 9559 5821 149 810 -1847 C ATOM 1483 C ASP A 307 56.205 -30.453 8.987 1.00 56.78 C ANISOU 1483 C ASP A 307 6447 9336 5792 92 678 -1801 C ATOM 1484 O ASP A 307 56.355 -29.604 9.863 1.00 52.63 O ANISOU 1484 O ASP A 307 6027 8681 5287 112 595 -1480 O ATOM 1485 CB ASP A 307 57.159 -32.458 7.809 1.00 56.16 C ANISOU 1485 CB ASP A 307 6259 9269 5810 107 1000 -2310 C ATOM 1486 CG ASP A 307 57.230 -33.432 8.976 1.00 70.69 C ANISOU 1486 CG ASP A 307 8132 10634 8093 76 1202 -2301 C ATOM 1487 OD1 ASP A 307 57.061 -33.004 10.138 1.00 68.18 O ANISOU 1487 OD1 ASP A 307 7892 10116 7897 74 1160 -2011 O ATOM 1488 OD2 ASP A 307 57.447 -34.636 8.727 1.00 72.97 O ANISOU 1488 OD2 ASP A 307 8368 10752 8607 69 1419 -2585 O ATOM 1489 N GLU A 308 55.017 -30.953 8.660 1.00 54.56 N ANISOU 1489 N GLU A 308 6061 9100 5571 22 663 -2140 N ATOM 1490 CA GLU A 308 53.778 -30.447 9.247 1.00 53.64 C ANISOU 1490 CA GLU A 308 5928 8920 5531 -14 558 -2097 C ATOM 1491 C GLU A 308 53.642 -30.779 10.731 1.00 57.23 C ANISOU 1491 C GLU A 308 6480 8956 6311 -19 689 -1950 C ATOM 1492 O GLU A 308 52.764 -30.249 11.412 1.00 58.97 O ANISOU 1492 O GLU A 308 6722 9098 6586 -8 636 -1838 O ATOM 1493 CB GLU A 308 52.571 -31.005 8.491 1.00 48.62 C ANISOU 1493 CB GLU A 308 5104 8453 4915 -105 505 -2502 C ATOM 1494 CG GLU A 308 52.399 -32.504 8.643 1.00 64.91 C ANISOU 1494 CG GLU A 308 7088 10232 7341 -209 701 -2868 C ATOM 1495 CD GLU A 308 51.334 -33.063 7.724 1.00 87.72 C ANISOU 1495 CD GLU A 308 9767 13321 10242 -332 607 -3339 C ATOM 1496 OE1 GLU A 308 50.976 -34.249 7.883 1.00 96.10 O ANISOU 1496 OE1 GLU A 308 10731 14099 11683 -450 755 -3666 O ATOM 1497 OE2 GLU A 308 50.859 -32.319 6.840 1.00 95.44 O ANISOU 1497 OE2 GLU A 308 10657 14742 10864 -312 382 -3375 O ATOM 1498 N LYS A 309 54.509 -31.655 11.229 1.00 59.43 N ANISOU 1498 N LYS A 309 6804 8985 6790 -8 879 -1926 N ATOM 1499 CA LYS A 309 54.463 -32.060 12.632 1.00 61.05 C ANISOU 1499 CA LYS A 309 7085 8842 7270 21 1025 -1746 C ATOM 1500 C LYS A 309 54.890 -30.941 13.577 1.00 55.70 C ANISOU 1500 C LYS A 309 6584 8147 6434 100 904 -1371 C ATOM 1501 O LYS A 309 54.784 -31.081 14.796 1.00 52.87 O ANISOU 1501 O LYS A 309 6309 7575 6205 152 990 -1204 O ATOM 1502 CB LYS A 309 55.338 -33.294 12.862 1.00 62.61 C ANISOU 1502 CB LYS A 309 7260 8804 7727 38 1267 -1773 C ATOM 1503 CG LYS A 309 54.766 -34.572 12.271 1.00 64.55 C ANISOU 1503 CG LYS A 309 7343 8914 8269 -51 1442 -2179 C ATOM 1504 CD LYS A 309 53.388 -34.862 12.841 1.00 67.41 C ANISOU 1504 CD LYS A 309 7614 9099 8900 -119 1490 -2265 C ATOM 1505 CE LYS A 309 52.804 -36.138 12.264 1.00 71.91 C ANISOU 1505 CE LYS A 309 7993 9489 9840 -248 1646 -2698 C ATOM 1506 NZ LYS A 309 51.429 -36.393 12.774 1.00 77.75 N ANISOU 1506 NZ LYS A 309 8592 10061 10887 -333 1688 -2756 N ATOM 1507 N VAL A 310 55.375 -29.834 13.021 1.00 45.98 N ANISOU 1507 N VAL A 310 5403 7141 4927 115 711 -1243 N ATOM 1508 CA VAL A 310 55.740 -28.688 13.846 1.00 46.02 C ANISOU 1508 CA VAL A 310 5569 7101 4816 162 571 -948 C ATOM 1509 C VAL A 310 54.492 -27.990 14.381 1.00 58.59 C ANISOU 1509 C VAL A 310 7216 8650 6396 192 509 -944 C ATOM 1510 O VAL A 310 54.537 -27.359 15.437 1.00 56.80 O ANISOU 1510 O VAL A 310 7149 8291 6142 247 464 -776 O ATOM 1511 CB VAL A 310 56.613 -27.669 13.078 1.00 43.04 C ANISOU 1511 CB VAL A 310 5199 6926 4229 159 403 -784 C ATOM 1512 CG1 VAL A 310 57.902 -28.320 12.613 1.00 47.92 C ANISOU 1512 CG1 VAL A 310 5752 7592 4864 156 490 -743 C ATOM 1513 CG2 VAL A 310 55.851 -27.063 11.902 1.00 39.62 C ANISOU 1513 CG2 VAL A 310 4663 6764 3628 158 302 -876 C ATOM 1514 N ASP A 311 53.379 -28.115 13.659 1.00 50.70 N ANISOU 1514 N ASP A 311 6077 7777 5410 163 506 -1139 N ATOM 1515 CA ASP A 311 52.119 -27.510 14.083 1.00 41.34 C ANISOU 1515 CA ASP A 311 4897 6566 4244 208 475 -1118 C ATOM 1516 C ASP A 311 51.526 -28.243 15.284 1.00 55.86 C ANISOU 1516 C ASP A 311 6765 8150 6311 244 665 -1118 C ATOM 1517 O ASP A 311 50.801 -27.653 16.085 1.00 52.75 O ANISOU 1517 O ASP A 311 6454 7673 5916 331 679 -1010 O ATOM 1518 CB ASP A 311 51.101 -27.503 12.940 1.00 44.00 C ANISOU 1518 CB ASP A 311 5023 7156 4541 165 402 -1306 C ATOM 1519 CG ASP A 311 51.391 -26.435 11.899 1.00 53.76 C ANISOU 1519 CG ASP A 311 6233 8687 5508 194 215 -1197 C ATOM 1520 OD1 ASP A 311 52.154 -25.491 12.193 1.00 49.02 O ANISOU 1520 OD1 ASP A 311 5784 8029 4814 244 143 -953 O ATOM 1521 OD2 ASP A 311 50.840 -26.539 10.784 1.00 53.28 O ANISOU 1521 OD2 ASP A 311 5983 8924 5335 167 138 -1349 O ATOM 1522 N LEU A 312 51.827 -29.532 15.398 1.00 54.45 N ANISOU 1522 N LEU A 312 6508 7839 6340 196 839 -1221 N ATOM 1523 CA LEU A 312 51.298 -30.333 16.494 1.00 53.97 C ANISOU 1523 CA LEU A 312 6436 7533 6536 243 1062 -1167 C ATOM 1524 C LEU A 312 52.142 -30.190 17.753 1.00 56.49 C ANISOU 1524 C LEU A 312 6961 7727 6776 358 1113 -898 C ATOM 1525 O LEU A 312 51.638 -30.350 18.866 1.00 62.72 O ANISOU 1525 O LEU A 312 7806 8387 7638 464 1257 -760 O ATOM 1526 CB LEU A 312 51.190 -31.800 16.084 1.00 48.96 C ANISOU 1526 CB LEU A 312 5604 6765 6232 144 1253 -1379 C ATOM 1527 CG LEU A 312 50.028 -32.035 15.118 1.00 69.53 C ANISOU 1527 CG LEU A 312 7980 9480 8960 23 1204 -1680 C ATOM 1528 CD1 LEU A 312 50.515 -32.201 13.685 1.00 50.91 C ANISOU 1528 CD1 LEU A 312 5535 7347 6463 -80 1072 -1962 C ATOM 1529 CD2 LEU A 312 49.176 -33.213 15.562 1.00 82.48 C ANISOU 1529 CD2 LEU A 312 9432 10851 11056 -35 1446 -1775 C ATOM 1530 N TRP A 313 53.424 -29.889 17.576 1.00 49.27 N ANISOU 1530 N TRP A 313 6141 6881 5698 347 993 -813 N ATOM 1531 CA TRP A 313 54.271 -29.542 18.706 1.00 53.70 C ANISOU 1531 CA TRP A 313 6886 7392 6124 439 955 -575 C ATOM 1532 C TRP A 313 53.776 -28.234 19.305 1.00 58.14 C ANISOU 1532 C TRP A 313 7628 7987 6474 510 806 -514 C ATOM 1533 O TRP A 313 53.538 -28.147 20.507 1.00 47.63 O ANISOU 1533 O TRP A 313 6431 6586 5082 631 874 -402 O ATOM 1534 CB TRP A 313 55.738 -29.424 18.288 1.00 40.55 C ANISOU 1534 CB TRP A 313 5235 5809 4364 389 831 -493 C ATOM 1535 CG TRP A 313 56.604 -28.751 19.311 1.00 50.16 C ANISOU 1535 CG TRP A 313 6624 7033 5400 445 686 -280 C ATOM 1536 CD1 TRP A 313 56.842 -27.411 19.431 1.00 52.34 C ANISOU 1536 CD1 TRP A 313 7043 7367 5478 423 440 -245 C ATOM 1537 CD2 TRP A 313 57.353 -29.385 20.357 1.00 53.05 C ANISOU 1537 CD2 TRP A 313 7023 7354 5779 528 764 -83 C ATOM 1538 NE1 TRP A 313 57.687 -27.172 20.487 1.00 55.00 N ANISOU 1538 NE1 TRP A 313 7504 7700 5694 463 334 -93 N ATOM 1539 CE2 TRP A 313 58.015 -28.367 21.073 1.00 56.53 C ANISOU 1539 CE2 TRP A 313 7628 7866 5983 539 520 26 C ATOM 1540 CE3 TRP A 313 57.524 -30.714 20.760 1.00 55.60 C ANISOU 1540 CE3 TRP A 313 7238 7580 6308 601 1018 24 C ATOM 1541 CZ2 TRP A 313 58.838 -28.636 22.169 1.00 52.80 C ANISOU 1541 CZ2 TRP A 313 7209 7437 5415 618 488 227 C ATOM 1542 CZ3 TRP A 313 58.342 -30.980 21.850 1.00 60.86 C ANISOU 1542 CZ3 TRP A 313 7951 8276 6896 707 1022 283 C ATOM 1543 CH2 TRP A 313 58.988 -29.945 22.541 1.00 53.22 C ANISOU 1543 CH2 TRP A 313 7144 7446 5633 714 741 377 C ATOM 1544 N SER A 314 53.606 -27.224 18.455 1.00 48.26 N ANISOU 1544 N SER A 314 6379 6846 5111 455 624 -584 N ATOM 1545 CA SER A 314 53.143 -25.915 18.909 1.00 54.74 C ANISOU 1545 CA SER A 314 7365 7652 5783 525 498 -540 C ATOM 1546 C SER A 314 51.735 -25.991 19.490 1.00 49.60 C ANISOU 1546 C SER A 314 6708 6934 5203 637 659 -571 C ATOM 1547 O SER A 314 51.364 -25.194 20.351 1.00 51.07 O ANISOU 1547 O SER A 314 7075 7055 5274 757 648 -522 O ATOM 1548 CB SER A 314 53.192 -24.904 17.762 1.00 56.57 C ANISOU 1548 CB SER A 314 7547 8002 5945 459 315 -556 C ATOM 1549 OG SER A 314 54.529 -24.692 17.341 1.00 46.36 O ANISOU 1549 OG SER A 314 6260 6761 4593 375 180 -474 O ATOM 1550 N LEU A 315 50.954 -26.955 19.015 1.00 52.22 N ANISOU 1550 N LEU A 315 6824 7277 5742 597 816 -664 N ATOM 1551 CA LEU A 315 49.624 -27.196 19.556 1.00 50.31 C ANISOU 1551 CA LEU A 315 6512 6966 5637 690 1000 -657 C ATOM 1552 C LEU A 315 49.730 -27.693 20.996 1.00 55.70 C ANISOU 1552 C LEU A 315 7325 7520 6319 832 1194 -503 C ATOM 1553 O LEU A 315 48.901 -27.364 21.843 1.00 54.83 O ANISOU 1553 O LEU A 315 7291 7368 6174 988 1316 -422 O ATOM 1554 CB LEU A 315 48.871 -28.210 18.695 1.00 52.74 C ANISOU 1554 CB LEU A 315 6519 7298 6222 572 1101 -813 C ATOM 1555 CG LEU A 315 47.419 -28.503 19.074 1.00 51.15 C ANISOU 1555 CG LEU A 315 6159 7033 6241 631 1283 -799 C ATOM 1556 CD1 LEU A 315 46.592 -27.235 19.012 1.00 46.07 C ANISOU 1556 CD1 LEU A 315 5558 6489 5457 733 1183 -747 C ATOM 1557 CD2 LEU A 315 46.834 -29.569 18.163 1.00 59.23 C ANISOU 1557 CD2 LEU A 315 6862 8067 7577 460 1337 -1007 C ATOM 1558 N GLY A 316 50.762 -28.489 21.259 1.00 60.93 N ANISOU 1558 N GLY A 316 8001 8144 7005 802 1236 -438 N ATOM 1559 CA GLY A 316 51.015 -29.007 22.589 1.00 60.37 C ANISOU 1559 CA GLY A 316 8034 8009 6895 954 1409 -240 C ATOM 1560 C GLY A 316 51.521 -27.923 23.518 1.00 59.42 C ANISOU 1560 C GLY A 316 8206 7961 6409 1075 1247 -171 C ATOM 1561 O GLY A 316 51.133 -27.863 24.685 1.00 52.40 O ANISOU 1561 O GLY A 316 7446 7078 5383 1265 1378 -54 O ATOM 1562 N VAL A 317 52.395 -27.067 22.998 1.00 54.21 N ANISOU 1562 N VAL A 317 7642 7360 5595 968 965 -250 N ATOM 1563 CA VAL A 317 52.887 -25.924 23.757 1.00 57.10 C ANISOU 1563 CA VAL A 317 8275 7758 5663 1033 764 -255 C ATOM 1564 C VAL A 317 51.732 -24.989 24.091 1.00 62.51 C ANISOU 1564 C VAL A 317 9087 8395 6270 1161 806 -335 C ATOM 1565 O VAL A 317 51.648 -24.453 25.197 1.00 51.04 O ANISOU 1565 O VAL A 317 7864 6946 4584 1319 807 -339 O ATOM 1566 CB VAL A 317 53.967 -25.144 22.983 1.00 48.10 C ANISOU 1566 CB VAL A 317 7157 6643 4475 862 467 -312 C ATOM 1567 CG1 VAL A 317 54.446 -23.952 23.799 1.00 46.70 C ANISOU 1567 CG1 VAL A 317 7242 6448 4055 899 247 -361 C ATOM 1568 CG2 VAL A 317 55.132 -26.057 22.627 1.00 48.94 C ANISOU 1568 CG2 VAL A 317 7121 6806 4667 760 450 -213 C ATOM 1569 N LEU A 318 50.835 -24.814 23.126 1.00 51.13 N ANISOU 1569 N LEU A 318 7487 6929 5012 1109 846 -402 N ATOM 1570 CA LEU A 318 49.699 -23.921 23.290 1.00 55.25 C ANISOU 1570 CA LEU A 318 8079 7403 5511 1239 902 -444 C ATOM 1571 C LEU A 318 48.711 -24.433 24.335 1.00 55.24 C ANISOU 1571 C LEU A 318 8092 7384 5514 1450 1198 -354 C ATOM 1572 O LEU A 318 48.194 -23.659 25.138 1.00 56.30 O ANISOU 1572 O LEU A 318 8423 7485 5485 1639 1259 -368 O ATOM 1573 CB LEU A 318 48.976 -23.730 21.961 1.00 54.79 C ANISOU 1573 CB LEU A 318 7787 7382 5650 1140 869 -490 C ATOM 1574 CG LEU A 318 47.823 -22.732 22.020 1.00 52.61 C ANISOU 1574 CG LEU A 318 7544 7061 5383 1285 922 -489 C ATOM 1575 CD1 LEU A 318 48.356 -21.314 22.088 1.00 48.32 C ANISOU 1575 CD1 LEU A 318 7238 6425 4697 1308 726 -532 C ATOM 1576 CD2 LEU A 318 46.900 -22.908 20.838 1.00 56.98 C ANISOU 1576 CD2 LEU A 318 7787 7721 6142 1214 936 -489 C ATOM 1577 N CYS A 319 48.440 -25.735 24.308 1.00 48.22 N ANISOU 1577 N CYS A 319 6984 6501 4837 1425 1404 -258 N ATOM 1578 CA CYS A 319 47.489 -26.336 25.237 1.00 52.77 C ANISOU 1578 CA CYS A 319 7511 7053 5485 1620 1727 -108 C ATOM 1579 C CYS A 319 47.986 -26.200 26.671 1.00 50.18 C ANISOU 1579 C CYS A 319 7463 6785 4819 1835 1787 -3 C ATOM 1580 O CYS A 319 47.197 -26.031 27.600 1.00 55.83 O ANISOU 1580 O CYS A 319 8270 7522 5420 2076 2005 89 O ATOM 1581 CB CYS A 319 47.255 -27.809 24.896 1.00 56.47 C ANISOU 1581 CB CYS A 319 7670 7465 6321 1520 1932 -19 C ATOM 1582 SG CYS A 319 45.876 -28.570 25.791 1.00 61.27 S ANISOU 1582 SG CYS A 319 8107 8006 7168 1724 2365 212 S ATOM 1583 N TYR A 320 49.303 -26.273 26.835 1.00 52.20 N ANISOU 1583 N TYR A 320 7837 7099 4897 1757 1591 -12 N ATOM 1584 CA TYR A 320 49.933 -26.082 28.132 1.00 62.36 C ANISOU 1584 CA TYR A 320 9383 8509 5803 1936 1564 55 C ATOM 1585 C TYR A 320 49.734 -24.651 28.614 1.00 68.49 C ANISOU 1585 C TYR A 320 10463 9287 6272 2048 1418 -142 C ATOM 1586 O TYR A 320 49.385 -24.423 29.771 1.00 69.00 O ANISOU 1586 O TYR A 320 10727 9442 6045 2303 1550 -116 O ATOM 1587 CB TYR A 320 51.427 -26.414 28.059 1.00 56.98 C ANISOU 1587 CB TYR A 320 8711 7903 5037 1794 1337 86 C ATOM 1588 CG TYR A 320 52.142 -26.362 29.394 1.00 65.25 C ANISOU 1588 CG TYR A 320 9974 9141 5676 1969 1277 178 C ATOM 1589 CD1 TYR A 320 52.653 -25.167 29.888 1.00 67.28 C ANISOU 1589 CD1 TYR A 320 10517 9468 5579 1981 986 -34 C ATOM 1590 CD2 TYR A 320 52.317 -27.511 30.156 1.00 52.25 C ANISOU 1590 CD2 TYR A 320 8232 7613 4008 2124 1507 477 C ATOM 1591 CE1 TYR A 320 53.307 -25.115 31.103 1.00 63.55 C ANISOU 1591 CE1 TYR A 320 10234 9223 4690 2134 889 6 C ATOM 1592 CE2 TYR A 320 52.974 -27.469 31.371 1.00 66.61 C ANISOU 1592 CE2 TYR A 320 10229 9681 5399 2306 1434 585 C ATOM 1593 CZ TYR A 320 53.467 -26.269 31.840 1.00 64.82 C ANISOU 1593 CZ TYR A 320 10290 9565 4772 2305 1106 327 C ATOM 1594 OH TYR A 320 54.120 -26.220 33.051 1.00 75.53 O ANISOU 1594 OH TYR A 320 11819 11220 5659 2480 992 391 O ATOM 1595 N GLU A 321 49.953 -23.687 27.724 1.00 58.91 N ANISOU 1595 N GLU A 321 9283 7969 5131 1875 1165 -336 N ATOM 1596 CA GLU A 321 49.866 -22.284 28.111 1.00 67.92 C ANISOU 1596 CA GLU A 321 10709 9041 6058 1957 1019 -543 C ATOM 1597 C GLU A 321 48.430 -21.868 28.411 1.00 58.00 C ANISOU 1597 C GLU A 321 9489 7718 4830 2191 1288 -546 C ATOM 1598 O GLU A 321 48.198 -20.966 29.211 1.00 59.56 O ANISOU 1598 O GLU A 321 9966 7881 4781 2377 1297 -693 O ATOM 1599 CB GLU A 321 50.457 -21.378 27.029 1.00 58.53 C ANISOU 1599 CB GLU A 321 9502 7723 5015 1719 719 -682 C ATOM 1600 CG GLU A 321 50.652 -19.944 27.503 1.00 66.21 C ANISOU 1600 CG GLU A 321 10779 8564 5816 1767 537 -911 C ATOM 1601 CD GLU A 321 51.178 -19.027 26.425 1.00 67.31 C ANISOU 1601 CD GLU A 321 10866 8541 6167 1545 285 -982 C ATOM 1602 OE1 GLU A 321 51.202 -19.440 25.247 1.00 74.22 O ANISOU 1602 OE1 GLU A 321 11472 9447 7280 1393 276 -848 O ATOM 1603 OE2 GLU A 321 51.568 -17.888 26.758 1.00 62.30 O ANISOU 1603 OE2 GLU A 321 10457 7748 5467 1528 102 -1173 O ATOM 1604 N PHE A 322 47.468 -22.523 27.768 1.00 57.63 N ANISOU 1604 N PHE A 322 9149 7653 5094 2181 1507 -399 N ATOM 1605 CA PHE A 322 46.058 -22.244 28.027 1.00 53.86 C ANISOU 1605 CA PHE A 322 8636 7134 4695 2405 1787 -343 C ATOM 1606 C PHE A 322 45.666 -22.647 29.450 1.00 61.00 C ANISOU 1606 C PHE A 322 9684 8147 5346 2712 2080 -222 C ATOM 1607 O PHE A 322 44.864 -21.975 30.100 1.00 67.11 O ANISOU 1607 O PHE A 322 10615 8901 5980 2974 2260 -255 O ATOM 1608 CB PHE A 322 45.168 -22.974 27.015 1.00 59.49 C ANISOU 1608 CB PHE A 322 8948 7835 5822 2291 1922 -211 C ATOM 1609 CG PHE A 322 45.089 -22.301 25.668 1.00 63.12 C ANISOU 1609 CG PHE A 322 9270 8241 6471 2101 1700 -310 C ATOM 1610 CD1 PHE A 322 45.632 -21.041 25.470 1.00 61.89 C ANISOU 1610 CD1 PHE A 322 9337 7999 6179 2076 1465 -456 C ATOM 1611 CD2 PHE A 322 44.462 -22.928 24.604 1.00 61.13 C ANISOU 1611 CD2 PHE A 322 8651 8035 6540 1952 1728 -251 C ATOM 1612 CE1 PHE A 322 45.557 -20.422 24.236 1.00 64.23 C ANISOU 1612 CE1 PHE A 322 9487 8269 6649 1934 1292 -476 C ATOM 1613 CE2 PHE A 322 44.384 -22.313 23.365 1.00 61.50 C ANISOU 1613 CE2 PHE A 322 8562 8107 6700 1810 1523 -313 C ATOM 1614 CZ PHE A 322 44.931 -21.059 23.182 1.00 63.47 C ANISOU 1614 CZ PHE A 322 9029 8283 6803 1816 1320 -392 C ATOM 1615 N LEU A 323 46.243 -23.745 29.929 1.00 58.84 N ANISOU 1615 N LEU A 323 9348 7998 5010 2704 2148 -57 N ATOM 1616 CA LEU A 323 45.892 -24.295 31.234 1.00 67.85 C ANISOU 1616 CA LEU A 323 10571 9290 5918 3011 2460 146 C ATOM 1617 C LEU A 323 46.755 -23.734 32.360 1.00 71.56 C ANISOU 1617 C LEU A 323 11425 9930 5834 3169 2304 10 C ATOM 1618 O LEU A 323 46.278 -23.526 33.476 1.00 79.21 O ANISOU 1618 O LEU A 323 12544 11009 6546 3436 2463 58 O ATOM 1619 CB LEU A 323 46.004 -25.820 31.210 1.00 69.07 C ANISOU 1619 CB LEU A 323 10428 9485 6332 2953 2658 453 C ATOM 1620 CG LEU A 323 44.996 -26.560 30.330 1.00 67.48 C ANISOU 1620 CG LEU A 323 9824 9131 6685 2829 2870 583 C ATOM 1621 CD1 LEU A 323 45.320 -28.042 30.276 1.00 65.80 C ANISOU 1621 CD1 LEU A 323 9341 8888 6770 2733 3032 827 C ATOM 1622 CD2 LEU A 323 43.581 -26.338 30.841 1.00 76.64 C ANISOU 1622 CD2 LEU A 323 10927 10287 7907 3096 3217 720 C ATOM 1623 N VAL A 324 48.028 -23.496 32.064 1.00 64.86 N ANISOU 1623 N VAL A 324 10668 9093 4881 2941 1925 -151 N ATOM 1624 CA VAL A 324 48.972 -23.035 33.075 1.00 75.16 C ANISOU 1624 CA VAL A 324 12291 10585 5680 3034 1707 -301 C ATOM 1625 C VAL A 324 49.085 -21.513 33.089 1.00 72.35 C ANISOU 1625 C VAL A 324 12241 10094 5156 3008 1450 -705 C ATOM 1626 O VAL A 324 49.229 -20.903 34.149 1.00 66.43 O ANISOU 1626 O VAL A 324 11707 9430 4103 3119 1350 -868 O ATOM 1627 CB VAL A 324 50.366 -23.657 32.853 1.00 74.57 C ANISOU 1627 CB VAL A 324 12116 10614 5604 2804 1433 -222 C ATOM 1628 CG1 VAL A 324 51.351 -23.160 33.898 1.00 69.09 C ANISOU 1628 CG1 VAL A 324 11715 10155 4383 2882 1157 -385 C ATOM 1629 CG2 VAL A 324 50.274 -25.174 32.890 1.00 59.72 C ANISOU 1629 CG2 VAL A 324 9940 8818 3932 2852 1721 180 C ATOM 1630 N GLY A 325 49.009 -20.900 31.913 1.00 58.09 N ANISOU 1630 N GLY A 325 11570 5420 5083 1763 2686 -389 N ATOM 1631 CA GLY A 325 49.113 -19.456 31.806 1.00 55.14 C ANISOU 1631 CA GLY A 325 11195 4974 4780 1700 2427 -474 C ATOM 1632 C GLY A 325 50.517 -19.027 31.435 1.00 56.95 C ANISOU 1632 C GLY A 325 11352 5404 4882 1544 1844 -530 C ATOM 1633 O GLY A 325 50.817 -17.836 31.358 1.00 61.23 O ANISOU 1633 O GLY A 325 11863 5839 5562 1461 1606 -605 O ATOM 1634 N LYS A 326 51.379 -20.011 31.198 1.00 61.94 N ANISOU 1634 N LYS A 326 11921 6283 5331 1505 1657 -489 N ATOM 1635 CA LYS A 326 52.771 -19.756 30.847 1.00 69.20 C ANISOU 1635 CA LYS A 326 12717 7396 6178 1366 1140 -526 C ATOM 1636 C LYS A 326 53.316 -20.891 29.976 1.00 62.13 C ANISOU 1636 C LYS A 326 11503 6804 5300 1268 1064 -391 C ATOM 1637 O LYS A 326 52.994 -22.056 30.204 1.00 59.49 O ANISOU 1637 O LYS A 326 11263 6481 4860 1382 1349 -353 O ATOM 1638 CB LYS A 326 53.611 -19.595 32.120 1.00 86.84 C ANISOU 1638 CB LYS A 326 15439 9570 7985 1549 891 -751 C ATOM 1639 CG LYS A 326 55.071 -19.249 31.884 1.00 92.99 C ANISOU 1639 CG LYS A 326 16041 10507 8786 1399 327 -852 C ATOM 1640 N PRO A 327 54.123 -20.551 28.957 1.00 61.97 N ANISOU 1640 N PRO A 327 11095 6994 5457 1071 740 -309 N ATOM 1641 CA PRO A 327 54.789 -21.561 28.125 1.00 64.89 C ANISOU 1641 CA PRO A 327 11181 7663 5812 999 651 -216 C ATOM 1642 C PRO A 327 55.681 -22.492 28.949 1.00 53.94 C ANISOU 1642 C PRO A 327 10078 6310 4109 1142 554 -273 C ATOM 1643 O PRO A 327 56.349 -22.028 29.870 1.00 70.59 O ANISOU 1643 O PRO A 327 12470 8338 6012 1235 298 -388 O ATOM 1644 CB PRO A 327 55.622 -20.719 27.155 1.00 68.01 C ANISOU 1644 CB PRO A 327 11209 8213 6420 823 345 -95 C ATOM 1645 CG PRO A 327 54.893 -19.432 27.063 1.00 71.60 C ANISOU 1645 CG PRO A 327 11621 8467 7115 788 416 -49 C ATOM 1646 CD PRO A 327 54.318 -19.189 28.428 1.00 66.42 C ANISOU 1646 CD PRO A 327 11435 7491 6312 926 547 -256 C ATOM 1647 N PRO A 328 55.697 -23.792 28.611 1.00 62.75 N ANISOU 1647 N PRO A 328 11096 7544 5200 1182 743 -215 N ATOM 1648 CA PRO A 328 56.372 -24.824 29.411 1.00 61.70 C ANISOU 1648 CA PRO A 328 11245 7409 4788 1392 765 -192 C ATOM 1649 C PRO A 328 57.897 -24.748 29.397 1.00 68.77 C ANISOU 1649 C PRO A 328 12055 8504 5570 1384 297 -184 C ATOM 1650 O PRO A 328 58.536 -25.323 30.277 1.00 72.71 O ANISOU 1650 O PRO A 328 12835 9020 5772 1624 208 -169 O ATOM 1651 CB PRO A 328 55.902 -26.128 28.761 1.00 56.83 C ANISOU 1651 CB PRO A 328 10416 6811 4366 1372 1136 -149 C ATOM 1652 CG PRO A 328 55.604 -25.751 27.346 1.00 53.51 C ANISOU 1652 CG PRO A 328 9503 6595 4233 1121 1050 -193 C ATOM 1653 CD PRO A 328 55.041 -24.359 27.419 1.00 51.56 C ANISOU 1653 CD PRO A 328 9278 6271 4043 1056 950 -195 C ATOM 1654 N PHE A 329 58.475 -24.064 28.416 1.00 60.02 N ANISOU 1654 N PHE A 329 10546 7548 4710 1148 29 -162 N ATOM 1655 CA PHE A 329 59.928 -23.993 28.316 1.00 55.06 C ANISOU 1655 CA PHE A 329 9737 7080 4105 1113 -369 -146 C ATOM 1656 C PHE A 329 60.437 -22.573 28.530 1.00 60.22 C ANISOU 1656 C PHE A 329 10312 7635 4933 976 -732 -259 C ATOM 1657 O PHE A 329 61.566 -22.248 28.159 1.00 59.80 O ANISOU 1657 O PHE A 329 9945 7672 5104 856 -1032 -239 O ATOM 1658 CB PHE A 329 60.398 -24.522 26.959 1.00 60.93 C ANISOU 1658 CB PHE A 329 10030 8061 5062 977 -312 0 C ATOM 1659 CG PHE A 329 59.817 -25.859 26.594 1.00 62.68 C ANISOU 1659 CG PHE A 329 10254 8332 5231 1060 59 16 C ATOM 1660 CD1 PHE A 329 60.246 -27.012 27.230 1.00 64.05 C ANISOU 1660 CD1 PHE A 329 10621 8469 5248 1267 150 40 C ATOM 1661 CD2 PHE A 329 58.852 -25.964 25.604 1.00 58.88 C ANISOU 1661 CD2 PHE A 329 9550 7926 4895 951 311 -11 C ATOM 1662 CE1 PHE A 329 59.715 -28.245 26.895 1.00 60.76 C ANISOU 1662 CE1 PHE A 329 10173 8003 4911 1322 547 28 C ATOM 1663 CE2 PHE A 329 58.318 -27.194 25.263 1.00 55.32 C ANISOU 1663 CE2 PHE A 329 9041 7479 4498 994 631 -102 C ATOM 1664 CZ PHE A 329 58.751 -28.336 25.909 1.00 53.35 C ANISOU 1664 CZ PHE A 329 8980 7106 4183 1158 779 -87 C ATOM 1665 N GLU A 330 59.603 -21.734 29.136 1.00 55.22 N ANISOU 1665 N GLU A 330 9939 6773 4269 993 -667 -392 N ATOM 1666 CA GLU A 330 59.939 -20.327 29.330 1.00 68.39 C ANISOU 1666 CA GLU A 330 11528 8254 6205 845 -944 -551 C ATOM 1667 C GLU A 330 61.165 -20.153 30.223 1.00 62.89 C ANISOU 1667 C GLU A 330 10897 7578 5422 908 -1446 -820 C ATOM 1668 O GLU A 330 61.296 -20.814 31.253 1.00 76.20 O ANISOU 1668 O GLU A 330 12962 9356 6634 1190 -1557 -956 O ATOM 1669 CB GLU A 330 58.746 -19.572 29.922 1.00 70.93 C ANISOU 1669 CB GLU A 330 12168 8301 6480 903 -731 -680 C ATOM 1670 CG GLU A 330 58.956 -18.071 30.021 1.00 75.47 C ANISOU 1670 CG GLU A 330 12636 8597 7444 734 -931 -856 C ATOM 1671 CD GLU A 330 57.725 -17.340 30.518 1.00 89.19 C ANISOU 1671 CD GLU A 330 14669 10044 9174 809 -658 -963 C ATOM 1672 OE1 GLU A 330 56.901 -16.919 29.678 1.00 82.14 O ANISOU 1672 OE1 GLU A 330 13560 9074 8574 721 -356 -718 O ATOM 1673 OE2 GLU A 330 57.582 -17.185 31.749 1.00108.67 O ANISOU 1673 OE2 GLU A 330 17587 12388 11315 999 -743 -1287 O ATOM 1674 N ALA A 331 62.064 -19.265 29.811 1.00 58.41 N ANISOU 1674 N ALA A 331 9927 6927 5337 669 -1737 -886 N ATOM 1675 CA ALA A 331 63.272 -18.973 30.575 1.00 73.13 C ANISOU 1675 CA ALA A 331 11719 8800 7267 680 -2285 -1223 C ATOM 1676 C ALA A 331 63.746 -17.548 30.303 1.00 82.62 C ANISOU 1676 C ALA A 331 12540 9682 9169 369 -2472 -1398 C ATOM 1677 O ALA A 331 63.256 -16.885 29.388 1.00 77.11 O ANISOU 1677 O ALA A 331 11614 8794 8891 176 -2132 -1133 O ATOM 1678 CB ALA A 331 64.368 -19.973 30.245 1.00 71.36 C ANISOU 1678 CB ALA A 331 11219 8880 7016 735 -2461 -1064 C ATOM 1679 N ASN A 332 64.702 -17.084 31.102 1.00 84.20 N ANISOU 1679 N ASN A 332 12648 9819 9524 344 -3010 -1850 N ATOM 1680 CA ASN A 332 65.206 -15.720 30.981 1.00 97.37 C ANISOU 1680 CA ASN A 332 13921 11090 11985 28 -3194 -2114 C ATOM 1681 C ASN A 332 66.038 -15.516 29.720 1.00 97.23 C ANISOU 1681 C ASN A 332 13221 11006 12717 -258 -3049 -1728 C ATOM 1682 O ASN A 332 66.036 -14.433 29.134 1.00109.94 O ANISOU 1682 O ASN A 332 14498 12224 15051 -518 -2841 -1630 O ATOM 1683 CB ASN A 332 66.030 -15.349 32.214 1.00106.59 C ANISOU 1683 CB ASN A 332 15129 12238 13133 88 -3878 -2816 C ATOM 1684 CG ASN A 332 65.214 -15.387 33.491 1.00115.90 C ANISOU 1684 CG ASN A 332 17023 13476 13537 425 -3989 -3215 C ATOM 1685 OD1 ASN A 332 63.991 -15.249 33.463 1.00115.80 O ANISOU 1685 OD1 ASN A 332 17391 13322 13286 500 -3520 -3042 O ATOM 1686 ND2 ASN A 332 65.888 -15.572 34.620 1.00122.57 N ANISOU 1686 ND2 ASN A 332 18045 14557 13970 671 -4606 -3748 N ATOM 1687 N THR A 333 66.751 -16.558 29.309 1.00 85.00 N ANISOU 1687 N THR A 333 11472 9818 11006 -176 -3102 -1478 N ATOM 1688 CA THR A 333 67.548 -16.505 28.089 1.00 85.82 C ANISOU 1688 CA THR A 333 10963 9915 11729 -381 -2892 -1065 C ATOM 1689 C THR A 333 67.012 -17.493 27.059 1.00 82.70 C ANISOU 1689 C THR A 333 10650 9849 10922 -244 -2409 -517 C ATOM 1690 O THR A 333 66.324 -18.453 27.408 1.00 78.41 O ANISOU 1690 O THR A 333 10550 9558 9682 -5 -2342 -516 O ATOM 1691 CB THR A 333 69.028 -16.813 28.363 1.00 83.29 C ANISOU 1691 CB THR A 333 10203 9715 11729 -420 -3369 -1274 C ATOM 1692 OG1 THR A 333 69.151 -18.137 28.898 1.00 89.70 O ANISOU 1692 OG1 THR A 333 11326 10966 11791 -95 -3574 -1300 O ATOM 1693 CG2 THR A 333 69.605 -15.812 29.353 1.00 91.78 C ANISOU 1693 CG2 THR A 333 11114 10480 13280 -572 -3926 -1933 C ATOM 1694 N TYR A 334 67.329 -17.259 25.790 1.00 80.30 N ANISOU 1694 N TYR A 334 9909 9534 11067 -375 -2049 -67 N ATOM 1695 CA TYR A 334 66.850 -18.136 24.730 1.00 82.87 C ANISOU 1695 CA TYR A 334 10282 10209 10996 -229 -1625 374 C ATOM 1696 C TYR A 334 67.734 -19.376 24.611 1.00 72.73 C ANISOU 1696 C TYR A 334 8865 9263 9506 -106 -1737 420 C ATOM 1697 O TYR A 334 67.293 -20.414 24.118 1.00 66.62 O ANISOU 1697 O TYR A 334 8259 8794 8258 63 -1495 589 O ATOM 1698 CB TYR A 334 66.779 -17.387 23.393 1.00 86.79 C ANISOU 1698 CB TYR A 334 10424 10626 11924 -319 -1165 867 C ATOM 1699 CG TYR A 334 68.117 -17.089 22.755 0.96 90.09 C ANISOU 1699 CG TYR A 334 10253 10963 13014 -453 -1098 1104 C ATOM 1700 CD1 TYR A 334 68.816 -15.931 23.066 0.89 93.71 C ANISOU 1700 CD1 TYR A 334 10341 10946 14320 -702 -1220 981 C ATOM 1701 CD2 TYR A 334 68.673 -17.958 21.824 0.82 87.35 C ANISOU 1701 CD2 TYR A 334 9692 10978 12520 -332 -868 1431 C ATOM 1702 CE1 TYR A 334 70.037 -15.653 22.478 0.00 96.53 C ANISOU 1702 CE1 TYR A 334 10094 11172 15412 -837 -1094 1216 C ATOM 1703 CE2 TYR A 334 69.891 -17.691 21.233 0.73 89.82 C ANISOU 1703 CE2 TYR A 334 9449 11201 13479 -431 -732 1686 C ATOM 1704 CZ TYR A 334 70.569 -16.538 21.562 0.99 92.27 C ANISOU 1704 CZ TYR A 334 9362 11017 14680 -689 -833 1599 C ATOM 1705 OH TYR A 334 71.783 -16.269 20.972 0.45 95.30 O ANISOU 1705 OH TYR A 334 9129 11258 15824 -801 -638 1869 O ATOM 1706 N GLN A 335 68.979 -19.264 25.066 1.00 76.85 N ANISOU 1706 N GLN A 335 9049 9712 10440 -188 -2108 235 N ATOM 1707 CA GLN A 335 69.887 -20.407 25.082 1.00 84.27 C ANISOU 1707 CA GLN A 335 9839 10947 11233 -39 -2253 266 C ATOM 1708 C GLN A 335 69.355 -21.490 26.013 1.00 83.05 C ANISOU 1708 C GLN A 335 10231 11005 10320 246 -2423 61 C ATOM 1709 O GLN A 335 69.381 -22.676 25.683 1.00 72.65 O ANISOU 1709 O GLN A 335 8994 9942 8667 433 -2231 237 O ATOM 1710 CB GLN A 335 71.294 -19.985 25.514 1.00 91.29 C ANISOU 1710 CB GLN A 335 10212 11707 12769 -169 -2693 51 C ATOM 1711 CG GLN A 335 72.007 -19.057 24.541 1.00101.59 C ANISOU 1711 CG GLN A 335 10878 12753 14969 -439 -2423 329 C ATOM 1712 CD GLN A 335 71.660 -17.596 24.756 1.00106.82 C ANISOU 1712 CD GLN A 335 11465 12944 16177 -696 -2434 164 C ATOM 1713 OE1 GLN A 335 70.654 -17.268 25.385 1.00110.33 O ANISOU 1713 OE1 GLN A 335 12391 13291 16238 -661 -2521 -77 O ATOM 1714 NE2 GLN A 335 72.500 -16.708 24.235 1.00108.09 N ANISOU 1714 NE2 GLN A 335 11000 12764 17305 -947 -2291 305 N ATOM 1715 N GLU A 336 68.870 -21.068 27.177 1.00 82.15 N ANISOU 1715 N GLU A 336 10495 10756 9962 300 -2732 -305 N ATOM 1716 CA GLU A 336 68.266 -21.983 28.136 1.00 75.87 C ANISOU 1716 CA GLU A 336 10271 10118 8438 619 -2804 -440 C ATOM 1717 C GLU A 336 66.960 -22.547 27.588 1.00 63.02 C ANISOU 1717 C GLU A 336 8976 8527 6442 683 -2257 -201 C ATOM 1718 O GLU A 336 66.647 -23.720 27.785 1.00 67.73 O ANISOU 1718 O GLU A 336 9846 9275 6614 920 -2084 -117 O ATOM 1719 CB GLU A 336 68.022 -21.279 29.472 1.00 72.12 C ANISOU 1719 CB GLU A 336 10142 9504 7756 698 -3217 -892 C ATOM 1720 CG GLU A 336 68.836 -21.843 30.622 1.00100.01 C ANISOU 1720 CG GLU A 336 13798 13265 10937 1011 -3757 -1159 C ATOM 1721 CD GLU A 336 68.455 -23.271 30.957 1.00103.03 C ANISOU 1721 CD GLU A 336 14613 13889 10646 1409 -3520 -914 C ATOM 1722 OE1 GLU A 336 67.243 -23.557 31.055 1.00105.22 O ANISOU 1722 OE1 GLU A 336 15351 14085 10543 1507 -3093 -800 O ATOM 1723 OE2 GLU A 336 69.366 -24.108 31.118 1.00107.00 O ANISOU 1723 OE2 GLU A 336 14959 14625 11069 1631 -3728 -822 O ATOM 1724 N THR A 337 66.203 -21.703 26.895 1.00 60.74 N ANISOU 1724 N THR A 337 8624 8080 6374 482 -1981 -97 N ATOM 1725 CA THR A 337 64.956 -22.132 26.275 1.00 60.64 C ANISOU 1725 CA THR A 337 8820 8131 6091 528 -1522 82 C ATOM 1726 C THR A 337 65.228 -23.184 25.201 1.00 60.17 C ANISOU 1726 C THR A 337 8530 8344 5988 577 -1251 328 C ATOM 1727 O THR A 337 64.512 -24.181 25.106 1.00 62.25 O ANISOU 1727 O THR A 337 9013 8710 5932 712 -995 334 O ATOM 1728 CB THR A 337 64.193 -20.944 25.658 1.00 74.88 C ANISOU 1728 CB THR A 337 10528 9758 8167 350 -1320 186 C ATOM 1729 OG1 THR A 337 63.959 -19.951 26.665 1.00 75.56 O ANISOU 1729 OG1 THR A 337 10825 9540 8343 302 -1546 -94 O ATOM 1730 CG2 THR A 337 62.859 -21.400 25.087 1.00 77.07 C ANISOU 1730 CG2 THR A 337 10980 10147 8155 430 -928 307 C ATOM 1731 N TYR A 338 66.271 -22.962 24.405 1.00 65.78 N ANISOU 1731 N TYR A 338 8784 9140 7070 472 -1278 507 N ATOM 1732 CA TYR A 338 66.688 -23.932 23.395 1.00 69.49 C ANISOU 1732 CA TYR A 338 9028 9880 7495 550 -1026 707 C ATOM 1733 C TYR A 338 67.016 -25.272 24.039 1.00 62.99 C ANISOU 1733 C TYR A 338 8391 9145 6398 761 -1093 598 C ATOM 1734 O TYR A 338 66.634 -26.328 23.531 1.00 56.08 O ANISOU 1734 O TYR A 338 7589 8407 5314 873 -794 629 O ATOM 1735 CB TYR A 338 67.902 -23.424 22.613 1.00 67.53 C ANISOU 1735 CB TYR A 338 8255 9670 7733 438 -1025 935 C ATOM 1736 CG TYR A 338 67.592 -22.343 21.602 1.00 83.30 C ANISOU 1736 CG TYR A 338 10034 11630 9988 314 -758 1206 C ATOM 1737 CD1 TYR A 338 66.287 -21.928 21.376 1.00 85.41 C ANISOU 1737 CD1 TYR A 338 10550 11888 10015 325 -583 1222 C ATOM 1738 CD2 TYR A 338 68.606 -21.745 20.867 1.00 94.41 C ANISOU 1738 CD2 TYR A 338 10963 13003 11906 225 -637 1493 C ATOM 1739 CE1 TYR A 338 66.001 -20.944 20.450 1.00 87.95 C ANISOU 1739 CE1 TYR A 338 10678 12199 10538 289 -327 1537 C ATOM 1740 CE2 TYR A 338 68.330 -20.760 19.939 1.00103.85 C ANISOU 1740 CE2 TYR A 338 11979 14151 13330 181 -314 1836 C ATOM 1741 CZ TYR A 338 67.026 -20.362 19.735 1.00102.23 C ANISOU 1741 CZ TYR A 338 12056 13969 12817 233 -174 1867 C ATOM 1742 OH TYR A 338 66.746 -19.381 18.812 1.00107.62 O ANISOU 1742 OH TYR A 338 12568 14628 13695 262 157 2272 O ATOM 1743 N LYS A 339 67.730 -25.218 25.159 1.00 57.06 N ANISOU 1743 N LYS A 339 7701 8312 5666 841 -1491 455 N ATOM 1744 CA LYS A 339 68.092 -26.417 25.902 1.00 59.84 C ANISOU 1744 CA LYS A 339 8253 8746 5739 1123 -1572 420 C ATOM 1745 C LYS A 339 66.850 -27.170 26.370 1.00 58.41 C ANISOU 1745 C LYS A 339 8577 8489 5127 1291 -1274 372 C ATOM 1746 O LYS A 339 66.724 -28.373 26.145 1.00 59.21 O ANISOU 1746 O LYS A 339 8749 8631 5118 1447 -972 455 O ATOM 1747 CB LYS A 339 68.973 -26.059 27.104 1.00 69.88 C ANISOU 1747 CB LYS A 339 9528 10003 7021 1238 -2134 242 C ATOM 1748 CG LYS A 339 69.322 -27.244 27.996 1.00 75.55 C ANISOU 1748 CG LYS A 339 10502 10838 7367 1632 -2238 268 C ATOM 1749 CD LYS A 339 69.963 -26.800 29.305 1.00 84.19 C ANISOU 1749 CD LYS A 339 11691 11995 8301 1824 -2863 25 C ATOM 1750 CE LYS A 339 71.264 -26.051 29.067 1.00 90.41 C ANISOU 1750 CE LYS A 339 11858 12831 9662 1624 -3323 -97 C ATOM 1751 N ARG A 340 65.931 -26.452 27.010 1.00 60.59 N ANISOU 1751 N ARG A 340 9177 8610 5237 1256 -1313 233 N ATOM 1752 CA AARG A 340 64.721 -27.058 27.558 0.38 63.77 C ANISOU 1752 CA AARG A 340 10037 8887 5305 1417 -990 201 C ATOM 1753 CA BARG A 340 64.730 -27.072 27.561 0.62 64.44 C ANISOU 1753 CA BARG A 340 10122 8974 5390 1420 -990 202 C ATOM 1754 C ARG A 340 63.836 -27.651 26.467 1.00 56.24 C ANISOU 1754 C ARG A 340 8974 7945 4449 1308 -516 255 C ATOM 1755 O ARG A 340 63.255 -28.722 26.640 1.00 59.03 O ANISOU 1755 O ARG A 340 9522 8210 4697 1455 -174 260 O ATOM 1756 CB AARG A 340 63.932 -26.030 28.371 0.38 63.76 C ANISOU 1756 CB AARG A 340 10356 8714 5157 1392 -1100 35 C ATOM 1757 CB BARG A 340 63.952 -26.063 28.408 0.62 63.95 C ANISOU 1757 CB BARG A 340 10389 8740 5170 1404 -1104 36 C ATOM 1758 CG AARG A 340 64.621 -25.606 29.658 0.38 69.02 C ANISOU 1758 CG AARG A 340 11239 9387 5597 1585 -1577 -138 C ATOM 1759 CG BARG A 340 64.737 -25.554 29.609 0.62 69.16 C ANISOU 1759 CG BARG A 340 11213 9417 5650 1566 -1615 -142 C ATOM 1760 CD AARG A 340 63.729 -25.854 30.862 0.38 73.02 C ANISOU 1760 CD AARG A 340 12348 9783 5615 1892 -1421 -201 C ATOM 1761 CD BARG A 340 63.900 -24.650 30.498 0.62 72.50 C ANISOU 1761 CD BARG A 340 12028 9661 5858 1601 -1674 -362 C ATOM 1762 NE AARG A 340 62.640 -24.886 30.952 0.38 71.13 N ANISOU 1762 NE AARG A 340 12282 9338 5405 1741 -1274 -338 N ATOM 1763 NE BARG A 340 64.691 -24.100 31.596 0.62 79.48 N ANISOU 1763 NE BARG A 340 13041 10607 6553 1761 -2235 -643 N ATOM 1764 CZ AARG A 340 61.489 -25.115 31.577 0.38 62.56 C ANISOU 1764 CZ AARG A 340 11636 8096 4039 1923 -897 -322 C ATOM 1765 CZ BARG A 340 64.190 -23.374 32.590 0.62 73.32 C ANISOU 1765 CZ BARG A 340 12655 9717 5486 1881 -2379 -922 C ATOM 1766 NH1AARG A 340 61.270 -26.288 32.154 0.38 63.46 N ANISOU 1766 NH1AARG A 340 11999 8192 3921 2228 -577 -146 N ATOM 1767 NH1BARG A 340 62.892 -23.111 32.634 0.62 78.77 N ANISOU 1767 NH1BARG A 340 13643 10199 6087 1856 -1951 -895 N ATOM 1768 NH2AARG A 340 60.554 -24.176 31.617 0.38 64.99 N ANISOU 1768 NH2AARG A 340 12048 8214 4432 1788 -772 -445 N ATOM 1769 NH2BARG A 340 64.989 -22.914 33.542 0.62 72.25 N ANISOU 1769 NH2BARG A 340 12598 9694 5160 2045 -2963 -1266 N ATOM 1770 N ILE A 341 63.731 -26.948 25.344 1.00 47.56 N ANISOU 1770 N ILE A 341 7548 6953 3570 1073 -488 286 N ATOM 1771 CA ILE A 341 62.949 -27.441 24.214 1.00 56.36 C ANISOU 1771 CA ILE A 341 8512 8181 4720 1004 -136 271 C ATOM 1772 C ILE A 341 63.557 -28.724 23.653 1.00 46.67 C ANISOU 1772 C ILE A 341 7123 7083 3529 1104 40 281 C ATOM 1773 O ILE A 341 62.855 -29.709 23.423 1.00 55.02 O ANISOU 1773 O ILE A 341 8242 8091 4572 1155 357 149 O ATOM 1774 CB ILE A 341 62.852 -26.392 23.086 1.00 57.05 C ANISOU 1774 CB ILE A 341 8287 8438 4950 831 -161 369 C ATOM 1775 CG1 ILE A 341 61.990 -25.209 23.527 1.00 54.14 C ANISOU 1775 CG1 ILE A 341 8077 7892 4602 747 -228 349 C ATOM 1776 CG2 ILE A 341 62.267 -27.015 21.833 1.00 46.35 C ANISOU 1776 CG2 ILE A 341 6741 7332 3537 839 115 313 C ATOM 1777 CD1 ILE A 341 61.996 -24.060 22.543 1.00 53.57 C ANISOU 1777 CD1 ILE A 341 7713 7929 4712 631 -234 540 C ATOM 1778 N SER A 342 64.870 -28.705 23.441 1.00 53.82 N ANISOU 1778 N SER A 342 7785 8114 4552 1125 -145 414 N ATOM 1779 CA SER A 342 65.580 -29.848 22.873 1.00 57.18 C ANISOU 1779 CA SER A 342 8025 8653 5047 1238 33 441 C ATOM 1780 C SER A 342 65.473 -31.083 23.764 1.00 60.46 C ANISOU 1780 C SER A 342 8723 8864 5384 1463 198 404 C ATOM 1781 O SER A 342 65.392 -32.210 23.275 1.00 58.02 O ANISOU 1781 O SER A 342 8357 8530 5157 1539 524 327 O ATOM 1782 CB SER A 342 67.051 -29.498 22.642 1.00 55.54 C ANISOU 1782 CB SER A 342 7479 8578 5046 1237 -200 624 C ATOM 1783 OG SER A 342 67.761 -30.605 22.112 1.00 65.33 O ANISOU 1783 OG SER A 342 8539 9915 6368 1374 5 660 O ATOM 1784 N ARG A 343 65.474 -30.863 25.073 1.00 55.80 N ANISOU 1784 N ARG A 343 8446 8118 4637 1601 -2 458 N ATOM 1785 CA ARG A 343 65.338 -31.954 26.030 1.00 59.38 C ANISOU 1785 CA ARG A 343 9225 8370 4965 1898 203 525 C ATOM 1786 C ARG A 343 63.872 -32.305 26.269 1.00 64.09 C ANISOU 1786 C ARG A 343 10111 8715 5527 1886 616 417 C ATOM 1787 O ARG A 343 63.569 -33.357 26.832 1.00 72.61 O ANISOU 1787 O ARG A 343 11416 9551 6619 2112 977 494 O ATOM 1788 CB ARG A 343 65.998 -31.585 27.362 1.00 56.59 C ANISOU 1788 CB ARG A 343 9111 8033 4358 2146 -202 637 C ATOM 1789 CG ARG A 343 67.492 -31.315 27.281 1.00 60.23 C ANISOU 1789 CG ARG A 343 9225 8716 4945 2181 -648 709 C ATOM 1790 CD ARG A 343 68.019 -30.840 28.623 1.00 69.21 C ANISOU 1790 CD ARG A 343 10579 9919 5798 2427 -1149 697 C ATOM 1791 NE ARG A 343 69.472 -30.699 28.642 1.00 71.65 N ANISOU 1791 NE ARG A 343 10493 10433 6296 2491 -1610 729 N ATOM 1792 CZ ARG A 343 70.170 -30.351 29.718 1.00 79.66 C ANISOU 1792 CZ ARG A 343 11572 11588 7109 2731 -2162 652 C ATOM 1793 NH1 ARG A 343 69.545 -30.111 30.864 1.00 68.20 N ANISOU 1793 NH1 ARG A 343 10630 10112 5171 2963 -2294 553 N ATOM 1794 NH2 ARG A 343 71.489 -30.247 29.652 1.00 86.97 N ANISOU 1794 NH2 ARG A 343 12035 12695 8313 2765 -2588 649 N ATOM 1795 N VAL A 344 62.976 -31.426 25.820 1.00 52.84 N ANISOU 1795 N VAL A 344 7963 6635 5480 2342 -110 1026 N ATOM 1796 CA VAL A 344 61.566 -31.470 26.206 1.00 51.49 C ANISOU 1796 CA VAL A 344 8063 6276 5226 2330 42 857 C ATOM 1797 C VAL A 344 61.505 -31.508 27.734 1.00 61.72 C ANISOU 1797 C VAL A 344 9416 7874 6160 2499 -71 1082 C ATOM 1798 O VAL A 344 60.909 -32.401 28.338 1.00 55.66 O ANISOU 1798 O VAL A 344 8726 7017 5404 2703 205 1295 O ATOM 1799 CB VAL A 344 60.819 -32.672 25.592 1.00 55.87 C ANISOU 1799 CB VAL A 344 8693 6425 6111 2397 532 879 C ATOM 1800 CG1 VAL A 344 59.315 -32.471 25.704 1.00 49.11 C ANISOU 1800 CG1 VAL A 344 8058 5418 5183 2279 630 657 C ATOM 1801 CG2 VAL A 344 61.210 -32.840 24.121 1.00 57.39 C ANISOU 1801 CG2 VAL A 344 8795 6411 6602 2213 680 708 C ATOM 1802 N GLU A 345 62.159 -30.526 28.343 1.00 58.61 N ANISOU 1802 N GLU A 345 8986 7863 5418 2366 -473 1030 N ATOM 1803 CA GLU A 345 62.307 -30.461 29.791 1.00 59.49 C ANISOU 1803 CA GLU A 345 9134 8397 5075 2430 -639 1227 C ATOM 1804 C GLU A 345 61.299 -29.499 30.406 1.00 59.04 C ANISOU 1804 C GLU A 345 9407 8324 4702 2259 -699 824 C ATOM 1805 O GLU A 345 61.475 -28.282 30.347 1.00 66.07 O ANISOU 1805 O GLU A 345 10399 9274 5431 1986 -952 475 O ATOM 1806 CB GLU A 345 63.732 -30.040 30.152 1.00 62.71 C ANISOU 1806 CB GLU A 345 9280 9316 5232 2318 -1036 1432 C ATOM 1807 CG GLU A 345 63.968 -29.803 31.633 1.00 80.74 C ANISOU 1807 CG GLU A 345 11589 12169 6918 2248 -1287 1595 C ATOM 1808 CD GLU A 345 65.353 -29.257 31.912 1.00 85.91 C ANISOU 1808 CD GLU A 345 11960 13398 7282 2017 -1734 1760 C ATOM 1809 OE1 GLU A 345 65.459 -28.253 32.648 1.00102.41 O ANISOU 1809 OE1 GLU A 345 14214 15837 8861 1656 -2041 1472 O ATOM 1810 OE2 GLU A 345 66.335 -29.833 31.396 1.00 85.58 O ANISOU 1810 OE2 GLU A 345 11531 13461 7525 2175 -1749 2171 O ATOM 1811 N PHE A 346 60.242 -30.053 30.990 1.00 68.74 N ANISOU 1811 N PHE A 346 10803 9438 5878 2423 -416 881 N ATOM 1812 CA PHE A 346 59.212 -29.250 31.640 1.00 68.63 C ANISOU 1812 CA PHE A 346 11089 9394 5593 2325 -372 538 C ATOM 1813 C PHE A 346 58.440 -30.080 32.660 1.00 76.54 C ANISOU 1813 C PHE A 346 12190 10491 6400 2539 -107 781 C ATOM 1814 O PHE A 346 58.529 -31.307 32.667 1.00 78.22 O ANISOU 1814 O PHE A 346 12256 10667 6796 2765 88 1199 O ATOM 1815 CB PHE A 346 58.246 -28.672 30.606 1.00 63.17 C ANISOU 1815 CB PHE A 346 10499 8243 5260 2237 -224 190 C ATOM 1816 CG PHE A 346 57.256 -29.671 30.079 1.00 66.71 C ANISOU 1816 CG PHE A 346 10917 8381 6048 2390 138 330 C ATOM 1817 CD1 PHE A 346 57.628 -30.588 29.110 1.00 68.18 C ANISOU 1817 CD1 PHE A 346 10923 8390 6592 2422 256 511 C ATOM 1818 CD2 PHE A 346 55.952 -29.691 30.550 1.00 63.65 C ANISOU 1818 CD2 PHE A 346 10687 7882 5616 2464 393 262 C ATOM 1819 CE1 PHE A 346 56.720 -31.510 28.622 1.00 67.78 C ANISOU 1819 CE1 PHE A 346 10879 8053 6821 2466 606 584 C ATOM 1820 CE2 PHE A 346 55.040 -30.611 30.066 1.00 68.65 C ANISOU 1820 CE2 PHE A 346 11273 8269 6540 2531 709 394 C ATOM 1821 CZ PHE A 346 55.425 -31.522 29.100 1.00 67.11 C ANISOU 1821 CZ PHE A 346 10928 7896 6674 2501 808 536 C ATOM 1822 N THR A 347 57.681 -29.402 33.516 1.00 82.27 N ANISOU 1822 N THR A 347 13176 11307 6777 2468 -54 518 N ATOM 1823 CA THR A 347 56.817 -30.076 34.478 1.00 65.78 C ANISOU 1823 CA THR A 347 11199 9313 4480 2647 227 712 C ATOM 1824 C THR A 347 55.416 -29.472 34.471 1.00 71.86 C ANISOU 1824 C THR A 347 12199 9781 5325 2642 504 352 C ATOM 1825 O THR A 347 55.216 -28.352 34.002 1.00 62.98 O ANISOU 1825 O THR A 347 11179 8449 4300 2493 445 -51 O ATOM 1826 CB THR A 347 57.391 -30.007 35.910 1.00 79.23 C ANISOU 1826 CB THR A 347 12961 11630 5514 2582 47 869 C ATOM 1827 OG1 THR A 347 57.635 -28.641 36.267 1.00 79.61 O ANISOU 1827 OG1 THR A 347 13224 11842 5182 2266 -169 375 O ATOM 1828 CG2 THR A 347 58.691 -30.795 36.010 1.00 72.98 C ANISOU 1828 CG2 THR A 347 11844 11206 4680 2660 -188 1410 C ATOM 1829 N PHE A 348 54.448 -30.226 34.984 1.00 75.60 N ANISOU 1829 N PHE A 348 12718 10221 5787 2821 830 551 N ATOM 1830 CA PHE A 348 53.087 -29.729 35.151 1.00 66.00 C ANISOU 1830 CA PHE A 348 11668 8799 4611 2856 1133 296 C ATOM 1831 C PHE A 348 52.856 -29.245 36.575 1.00 72.24 C ANISOU 1831 C PHE A 348 12712 9931 4805 2837 1219 151 C ATOM 1832 O PHE A 348 53.371 -29.838 37.524 1.00 73.73 O ANISOU 1832 O PHE A 348 12901 10548 4563 2857 1144 436 O ATOM 1833 CB PHE A 348 52.055 -30.813 34.828 1.00 70.94 C ANISOU 1833 CB PHE A 348 12180 9193 5581 3013 1475 580 C ATOM 1834 CG PHE A 348 52.066 -31.269 33.400 1.00 72.34 C ANISOU 1834 CG PHE A 348 12156 9028 6301 2951 1468 637 C ATOM 1835 CD1 PHE A 348 51.401 -30.547 32.423 1.00 69.59 C ANISOU 1835 CD1 PHE A 348 11754 8420 6268 2839 1489 387 C ATOM 1836 CD2 PHE A 348 52.717 -32.438 33.039 1.00 77.70 C ANISOU 1836 CD2 PHE A 348 12697 9653 7174 2998 1482 962 C ATOM 1837 CE1 PHE A 348 51.401 -30.973 31.106 1.00 69.97 C ANISOU 1837 CE1 PHE A 348 11620 8239 6726 2708 1475 429 C ATOM 1838 CE2 PHE A 348 52.720 -32.868 31.725 1.00 76.45 C ANISOU 1838 CE2 PHE A 348 12402 9180 7466 2884 1533 943 C ATOM 1839 CZ PHE A 348 52.060 -32.135 30.758 1.00 67.80 C ANISOU 1839 CZ PHE A 348 11262 7906 6592 2706 1508 661 C ATOM 1840 N PRO A 349 52.079 -28.164 36.734 1.00 70.58 N ANISOU 1840 N PRO A 349 12711 9544 4562 2794 1407 -273 N ATOM 1841 CA PRO A 349 51.569 -27.854 38.073 1.00 75.45 C ANISOU 1841 CA PRO A 349 13598 10427 4644 2797 1647 -433 C ATOM 1842 C PRO A 349 50.591 -28.944 38.496 1.00 75.98 C ANISOU 1842 C PRO A 349 13579 10543 4746 3028 1985 -50 C ATOM 1843 O PRO A 349 50.032 -29.613 37.626 1.00 72.92 O ANISOU 1843 O PRO A 349 12971 9854 4881 3152 2099 189 O ATOM 1844 CB PRO A 349 50.868 -26.505 37.890 1.00 80.30 C ANISOU 1844 CB PRO A 349 14417 10673 5420 2765 1880 -946 C ATOM 1845 CG PRO A 349 51.443 -25.937 36.616 1.00 79.73 C ANISOU 1845 CG PRO A 349 14206 10279 5809 2658 1602 -1062 C ATOM 1846 CD PRO A 349 51.738 -27.121 35.752 1.00 68.09 C ANISOU 1846 CD PRO A 349 12399 8801 4671 2738 1425 -609 C ATOM 1847 N ASP A 350 50.385 -29.118 39.797 1.00 80.71 N ANISOU 1847 N ASP A 350 14353 11539 4774 3037 2148 2 N ATOM 1848 CA ASP A 350 49.622 -30.254 40.307 1.00 81.86 C ANISOU 1848 CA ASP A 350 14405 11802 4897 3233 2438 447 C ATOM 1849 C ASP A 350 48.179 -30.315 39.805 1.00 85.79 C ANISOU 1849 C ASP A 350 14819 11895 5882 3402 2849 433 C ATOM 1850 O ASP A 350 47.620 -31.401 39.654 1.00 79.01 O ANISOU 1850 O ASP A 350 13779 10968 5273 3521 3023 844 O ATOM 1851 CB ASP A 350 49.628 -30.240 41.839 1.00102.74 C ANISOU 1851 CB ASP A 350 17165 14953 6918 3093 2487 451 C ATOM 1852 CG ASP A 350 51.002 -30.515 42.417 1.00108.35 C ANISOU 1852 CG ASP A 350 17825 16203 7138 2904 2065 680 C ATOM 1853 OD1 ASP A 350 51.842 -31.104 41.702 1.00110.11 O ANISOU 1853 OD1 ASP A 350 17866 16398 7574 3002 1807 1021 O ATOM 1854 OD2 ASP A 350 51.245 -30.143 43.583 1.00114.22 O ANISOU 1854 OD2 ASP A 350 18684 17424 7291 2631 2002 537 O ATOM 1855 N PHE A 351 47.579 -29.162 39.538 1.00 82.45 N ANISOU 1855 N PHE A 351 14487 11197 5642 3390 3006 0 N ATOM 1856 CA PHE A 351 46.161 -29.126 39.200 1.00 90.32 C ANISOU 1856 CA PHE A 351 15325 11905 7088 3539 3384 51 C ATOM 1857 C PHE A 351 45.836 -29.617 37.790 1.00 80.57 C ANISOU 1857 C PHE A 351 13792 10358 6463 3574 3333 282 C ATOM 1858 O PHE A 351 44.671 -29.845 37.466 1.00 87.37 O ANISOU 1858 O PHE A 351 14455 11085 7655 3665 3621 447 O ATOM 1859 CB PHE A 351 45.623 -27.719 39.370 1.00 81.73 C ANISOU 1859 CB PHE A 351 14341 10597 6115 3516 3571 -398 C ATOM 1860 CG PHE A 351 46.290 -26.699 38.497 1.00 93.14 C ANISOU 1860 CG PHE A 351 15849 11759 7779 3429 3344 -719 C ATOM 1861 CD1 PHE A 351 45.895 -26.526 37.171 1.00 89.55 C ANISOU 1861 CD1 PHE A 351 15160 10961 7904 3528 3341 -617 C ATOM 1862 CD2 PHE A 351 47.263 -25.856 39.020 1.00 88.26 C ANISOU 1862 CD2 PHE A 351 15504 11242 6789 3201 3145 -1123 C ATOM 1863 CE1 PHE A 351 46.474 -25.548 36.383 1.00 74.04 C ANISOU 1863 CE1 PHE A 351 13235 8729 6167 3444 3140 -878 C ATOM 1864 CE2 PHE A 351 47.845 -24.878 38.232 1.00 81.75 C ANISOU 1864 CE2 PHE A 351 14736 10122 6205 3094 2956 -1413 C ATOM 1865 CZ PHE A 351 47.454 -24.729 36.913 1.00 80.81 C ANISOU 1865 CZ PHE A 351 14385 9632 6689 3236 2954 -1275 C ATOM 1866 N VAL A 352 46.851 -29.759 36.946 1.00 76.41 N ANISOU 1866 N VAL A 352 13182 9744 6107 3436 2940 294 N ATOM 1867 CA VAL A 352 46.620 -30.259 35.596 1.00 78.85 C ANISOU 1867 CA VAL A 352 13202 9792 6965 3360 2857 473 C ATOM 1868 C VAL A 352 46.136 -31.707 35.653 1.00 78.79 C ANISOU 1868 C VAL A 352 13057 9816 7062 3372 3043 887 C ATOM 1869 O VAL A 352 46.810 -32.574 36.207 1.00 84.48 O ANISOU 1869 O VAL A 352 13846 10689 7564 3398 2989 1119 O ATOM 1870 CB VAL A 352 47.886 -30.167 34.721 1.00 79.55 C ANISOU 1870 CB VAL A 352 13250 9800 7176 3204 2442 391 C ATOM 1871 CG1 VAL A 352 47.599 -30.700 33.331 1.00 60.43 C ANISOU 1871 CG1 VAL A 352 10562 7146 5254 3071 2403 532 C ATOM 1872 CG2 VAL A 352 48.375 -28.728 34.644 1.00 71.57 C ANISOU 1872 CG2 VAL A 352 12380 8725 6088 3148 2265 -10 C ATOM 1873 N THR A 353 44.960 -31.955 35.082 1.00 79.12 N ANISOU 1873 N THR A 353 12884 9722 7454 3338 3273 1014 N ATOM 1874 CA THR A 353 44.330 -33.271 35.141 1.00 75.46 C ANISOU 1874 CA THR A 353 12304 9254 7114 3288 3510 1372 C ATOM 1875 C THR A 353 45.089 -34.309 34.323 1.00 85.32 C ANISOU 1875 C THR A 353 13498 10322 8596 3108 3360 1512 C ATOM 1876 O THR A 353 45.883 -33.965 33.447 1.00 84.04 O ANISOU 1876 O THR A 353 13312 10046 8576 2996 3080 1333 O ATOM 1877 CB THR A 353 42.874 -33.218 34.644 1.00 75.40 C ANISOU 1877 CB THR A 353 12030 9200 7420 3217 3764 1472 C ATOM 1878 OG1 THR A 353 42.849 -32.753 33.288 1.00 79.69 O ANISOU 1878 OG1 THR A 353 12364 9603 8313 3019 3553 1358 O ATOM 1879 CG2 THR A 353 42.048 -32.279 35.510 1.00 70.67 C ANISOU 1879 CG2 THR A 353 11466 8736 6650 3457 4032 1380 C ATOM 1880 N GLU A 354 44.829 -35.582 34.612 1.00 88.94 N ANISOU 1880 N GLU A 354 13948 10728 9118 3081 3598 1834 N ATOM 1881 CA GLU A 354 45.511 -36.688 33.947 1.00 86.15 C ANISOU 1881 CA GLU A 354 13586 10120 9027 2939 3591 1977 C ATOM 1882 C GLU A 354 45.248 -36.703 32.444 1.00 84.70 C ANISOU 1882 C GLU A 354 13244 9713 9223 2600 3529 1786 C ATOM 1883 O GLU A 354 46.131 -37.046 31.658 1.00 78.56 O ANISOU 1883 O GLU A 354 12490 8742 8619 2479 3411 1704 O ATOM 1884 CB GLU A 354 45.085 -38.023 34.563 1.00 86.02 C ANISOU 1884 CB GLU A 354 13600 10016 9067 2961 3953 2372 C ATOM 1885 N GLY A 355 44.033 -36.334 32.053 1.00 82.08 N ANISOU 1885 N GLY A 355 12727 9457 9002 2437 3619 1744 N ATOM 1886 CA GLY A 355 43.667 -36.284 30.649 1.00 66.84 C ANISOU 1886 CA GLY A 355 10597 7450 7351 2054 3531 1610 C ATOM 1887 C GLY A 355 44.403 -35.184 29.911 1.00 73.64 C ANISOU 1887 C GLY A 355 11425 8340 8215 2055 3169 1347 C ATOM 1888 O GLY A 355 44.800 -35.351 28.756 1.00 69.16 O ANISOU 1888 O GLY A 355 10795 7672 7812 1759 3036 1217 O ATOM 1889 N ALA A 356 44.586 -34.052 30.582 1.00 70.48 N ANISOU 1889 N ALA A 356 11088 8071 7622 2357 3039 1250 N ATOM 1890 CA ALA A 356 45.311 -32.927 30.006 1.00 67.50 C ANISOU 1890 CA ALA A 356 10704 7688 7253 2371 2717 1011 C ATOM 1891 C ALA A 356 46.802 -33.238 29.911 1.00 73.39 C ANISOU 1891 C ALA A 356 11622 8340 7923 2385 2512 916 C ATOM 1892 O ALA A 356 47.458 -32.883 28.931 1.00 66.10 O ANISOU 1892 O ALA A 356 10639 7355 7120 2224 2279 765 O ATOM 1893 CB ALA A 356 45.079 -31.670 30.826 1.00 60.97 C ANISOU 1893 CB ALA A 356 9951 6956 6258 2658 2719 898 C ATOM 1894 N ARG A 357 47.328 -33.902 30.936 1.00 72.37 N ANISOU 1894 N ARG A 357 11668 8237 7593 2584 2608 1058 N ATOM 1895 CA ARG A 357 48.730 -34.306 30.957 1.00 61.37 C ANISOU 1895 CA ARG A 357 10369 6802 6149 2646 2449 1088 C ATOM 1896 C ARG A 357 49.029 -35.283 29.828 1.00 72.64 C ANISOU 1896 C ARG A 357 11725 7966 7909 2411 2544 1114 C ATOM 1897 O ARG A 357 50.076 -35.206 29.187 1.00 73.66 O ANISOU 1897 O ARG A 357 11841 8026 8120 2363 2367 1015 O ATOM 1898 CB ARG A 357 49.090 -34.939 32.303 1.00 66.71 C ANISOU 1898 CB ARG A 357 11175 7619 6552 2904 2566 1367 C ATOM 1899 CG ARG A 357 49.105 -33.966 33.468 1.00 60.99 C ANISOU 1899 CG ARG A 357 10579 7209 5385 3078 2453 1274 C ATOM 1900 CD ARG A 357 49.176 -34.700 34.801 1.00 65.95 C ANISOU 1900 CD ARG A 357 11303 8063 5693 3273 2613 1613 C ATOM 1901 NE ARG A 357 49.231 -33.776 35.931 1.00 72.22 N ANISOU 1901 NE ARG A 357 12255 9212 5973 3362 2521 1467 N ATOM 1902 CZ ARG A 357 50.352 -33.410 36.543 1.00 83.50 C ANISOU 1902 CZ ARG A 357 13760 10949 7016 3380 2240 1459 C ATOM 1903 NH1 ARG A 357 51.519 -33.894 36.141 1.00 81.83 N ANISOU 1903 NH1 ARG A 357 13432 10739 6922 3382 2021 1657 N ATOM 1904 NH2 ARG A 357 50.307 -32.564 37.565 1.00 80.91 N ANISOU 1904 NH2 ARG A 357 13619 10950 6173 3371 2201 1252 N ATOM 1905 N ASP A 358 48.095 -36.198 29.594 1.00 74.44 N ANISOU 1905 N ASP A 358 11915 8047 8320 2235 2858 1227 N ATOM 1906 CA ASP A 358 48.246 -37.208 28.557 1.00 76.01 C ANISOU 1906 CA ASP A 358 12107 7955 8818 1935 3046 1188 C ATOM 1907 C ASP A 358 48.306 -36.589 27.162 1.00 67.43 C ANISOU 1907 C ASP A 358 10894 6895 7831 1593 2833 896 C ATOM 1908 O ASP A 358 49.186 -36.922 26.369 1.00 74.39 O ANISOU 1908 O ASP A 358 11810 7611 8845 1464 2825 771 O ATOM 1909 CB ASP A 358 47.101 -38.219 28.635 1.00 81.53 C ANISOU 1909 CB ASP A 358 12805 8520 9654 1726 3429 1332 C ATOM 1910 CG ASP A 358 47.130 -39.221 27.501 1.00 76.48 C ANISOU 1910 CG ASP A 358 12202 7558 9300 1299 3675 1196 C ATOM 1911 OD1 ASP A 358 47.875 -40.218 27.606 1.00 82.34 O ANISOU 1911 OD1 ASP A 358 13101 7957 10227 1394 3944 1298 O ATOM 1912 OD2 ASP A 358 46.404 -39.014 26.507 1.00 86.04 O ANISOU 1912 OD2 ASP A 358 13278 8867 10545 856 3626 1002 O ATOM 1913 N LEU A 359 47.371 -35.688 26.871 1.00 67.01 N ANISOU 1913 N LEU A 359 10672 7067 7723 1464 2686 831 N ATOM 1914 CA LEU A 359 47.302 -35.046 25.560 1.00 64.74 C ANISOU 1914 CA LEU A 359 10208 6883 7506 1127 2467 649 C ATOM 1915 C LEU A 359 48.551 -34.223 25.264 1.00 68.64 C ANISOU 1915 C LEU A 359 10739 7388 7954 1261 2155 497 C ATOM 1916 O LEU A 359 49.141 -34.334 24.187 1.00 61.97 O ANISOU 1916 O LEU A 359 9859 6495 7190 996 2079 347 O ATOM 1917 CB LEU A 359 46.061 -34.153 25.463 1.00 62.38 C ANISOU 1917 CB LEU A 359 9661 6847 7192 1066 2380 739 C ATOM 1918 CG LEU A 359 45.944 -33.323 24.180 1.00 66.98 C ANISOU 1918 CG LEU A 359 9999 7617 7834 763 2115 668 C ATOM 1919 CD1 LEU A 359 45.843 -34.224 22.959 1.00 68.46 C ANISOU 1919 CD1 LEU A 359 10122 7822 8067 193 2193 569 C ATOM 1920 CD2 LEU A 359 44.758 -32.373 24.247 1.00 69.43 C ANISOU 1920 CD2 LEU A 359 10018 8174 8190 830 2064 874 C ATOM 1921 N ILE A 360 48.944 -33.394 26.226 1.00 56.07 N ANISOU 1921 N ILE A 360 9222 5875 6205 1629 1994 518 N ATOM 1922 CA ILE A 360 50.114 -32.537 26.082 1.00 59.44 C ANISOU 1922 CA ILE A 360 9681 6337 6565 1730 1685 381 C ATOM 1923 C ILE A 360 51.392 -33.347 25.879 1.00 66.93 C ANISOU 1923 C ILE A 360 10708 7159 7563 1748 1707 384 C ATOM 1924 O ILE A 360 52.208 -33.028 25.012 1.00 67.32 O ANISOU 1924 O ILE A 360 10696 7203 7679 1612 1532 255 O ATOM 1925 CB ILE A 360 50.274 -31.616 27.306 1.00 56.88 C ANISOU 1925 CB ILE A 360 9476 6127 6010 2053 1564 367 C ATOM 1926 CG1 ILE A 360 49.126 -30.607 27.352 1.00 59.18 C ANISOU 1926 CG1 ILE A 360 9676 6476 6334 2073 1585 338 C ATOM 1927 CG2 ILE A 360 51.616 -30.901 27.282 1.00 51.82 C ANISOU 1927 CG2 ILE A 360 8887 5534 5267 2103 1255 233 C ATOM 1928 CD1 ILE A 360 49.164 -29.695 28.550 1.00 63.75 C ANISOU 1928 CD1 ILE A 360 10428 7108 6685 2347 1572 243 C ATOM 1929 N SER A 361 51.552 -34.404 26.670 1.00 61.94 N ANISOU 1929 N SER A 361 10186 6423 6927 1933 1954 578 N ATOM 1930 CA SER A 361 52.743 -35.246 26.597 1.00 56.55 C ANISOU 1930 CA SER A 361 9539 5589 6357 2039 2052 684 C ATOM 1931 C SER A 361 52.869 -35.948 25.246 1.00 67.31 C ANISOU 1931 C SER A 361 10878 6704 7991 1711 2260 526 C ATOM 1932 O SER A 361 53.976 -36.176 24.761 1.00 70.37 O ANISOU 1932 O SER A 361 11246 6996 8497 1742 2267 502 O ATOM 1933 CB SER A 361 52.733 -36.282 27.723 1.00 61.36 C ANISOU 1933 CB SER A 361 10241 6119 6956 2318 2331 1017 C ATOM 1934 OG SER A 361 52.810 -35.653 28.991 1.00 76.10 O ANISOU 1934 OG SER A 361 12141 8287 8487 2584 2131 1151 O ATOM 1935 N ARG A 362 51.734 -36.289 24.643 1.00 66.11 N ANISOU 1935 N ARG A 362 10721 6483 7916 1368 2446 417 N ATOM 1936 CA ARG A 362 51.732 -36.930 23.331 1.00 70.13 C ANISOU 1936 CA ARG A 362 11239 6811 8596 935 2660 198 C ATOM 1937 C ARG A 362 52.118 -35.941 22.237 1.00 60.65 C ANISOU 1937 C ARG A 362 9900 5824 7319 693 2331 -20 C ATOM 1938 O ARG A 362 52.826 -36.291 21.296 1.00 60.59 O ANISOU 1938 O ARG A 362 9915 5700 7405 484 2440 -195 O ATOM 1939 CB ARG A 362 50.362 -37.540 23.025 1.00 62.12 C ANISOU 1939 CB ARG A 362 10231 5761 7613 540 2910 153 C ATOM 1940 CG ARG A 362 50.008 -38.738 23.884 1.00 64.38 C ANISOU 1940 CG ARG A 362 10674 5750 8035 680 3331 353 C ATOM 1941 CD ARG A 362 48.622 -39.267 23.550 1.00 68.15 C ANISOU 1941 CD ARG A 362 11129 6238 8526 215 3549 301 C ATOM 1942 NE ARG A 362 48.218 -40.337 24.456 1.00 79.53 N ANISOU 1942 NE ARG A 362 12716 7398 10105 354 3947 530 N ATOM 1943 CZ ARG A 362 48.489 -41.624 24.263 1.00 88.06 C ANISOU 1943 CZ ARG A 362 14005 8001 11452 216 4433 495 C ATOM 1944 NH1 ARG A 362 49.166 -42.009 23.189 1.00 86.68 N ANISOU 1944 NH1 ARG A 362 13938 7581 11418 -71 4609 191 N ATOM 1945 NH2 ARG A 362 48.082 -42.527 25.145 1.00 89.18 N ANISOU 1945 NH2 ARG A 362 14261 7886 11736 365 4789 767 N ATOM 1946 N LEU A 363 51.648 -34.704 22.371 1.00 59.23 N ANISOU 1946 N LEU A 363 9581 5934 6988 733 1972 6 N ATOM 1947 CA LEU A 363 51.934 -33.660 21.394 1.00 61.28 C ANISOU 1947 CA LEU A 363 9686 6400 7197 526 1650 -121 C ATOM 1948 C LEU A 363 53.364 -33.142 21.507 1.00 64.34 C ANISOU 1948 C LEU A 363 10092 6779 7575 770 1438 -149 C ATOM 1949 O LEU A 363 53.935 -32.654 20.529 1.00 55.86 O ANISOU 1949 O LEU A 363 8922 5798 6505 562 1273 -269 O ATOM 1950 CB LEU A 363 50.949 -32.498 21.553 1.00 58.99 C ANISOU 1950 CB LEU A 363 9232 6350 6832 544 1405 -22 C ATOM 1951 CG LEU A 363 49.505 -32.752 21.116 1.00 60.80 C ANISOU 1951 CG LEU A 363 9303 6731 7067 211 1524 62 C ATOM 1952 CD1 LEU A 363 48.608 -31.599 21.536 1.00 45.44 C ANISOU 1952 CD1 LEU A 363 7174 4970 5120 397 1354 249 C ATOM 1953 CD2 LEU A 363 49.435 -32.964 19.607 1.00 58.11 C ANISOU 1953 CD2 LEU A 363 8826 6555 6697 -356 1497 -61 C ATOM 1954 N LEU A 364 53.940 -33.243 22.700 1.00 61.63 N ANISOU 1954 N LEU A 364 10036 6280 7101 673 932 -195 N ATOM 1955 CA LEU A 364 55.289 -32.737 22.926 1.00 53.29 C ANISOU 1955 CA LEU A 364 8921 5552 5775 755 668 -149 C ATOM 1956 C LEU A 364 56.335 -33.847 22.881 1.00 60.58 C ANISOU 1956 C LEU A 364 9742 6517 6758 1050 609 -159 C ATOM 1957 O LEU A 364 57.258 -33.871 23.692 1.00 67.94 O ANISOU 1957 O LEU A 364 10724 7618 7472 1261 453 -17 O ATOM 1958 CB LEU A 364 55.369 -31.999 24.262 1.00 62.36 C ANISOU 1958 CB LEU A 364 10373 6690 6631 775 598 76 C ATOM 1959 CG LEU A 364 54.559 -30.704 24.352 1.00 63.03 C ANISOU 1959 CG LEU A 364 10617 6770 6562 529 656 111 C ATOM 1960 CD1 LEU A 364 54.842 -29.990 25.663 1.00 62.28 C ANISOU 1960 CD1 LEU A 364 10862 6671 6128 545 567 295 C ATOM 1961 CD2 LEU A 364 54.847 -29.795 23.166 1.00 52.23 C ANISOU 1961 CD2 LEU A 364 9013 5708 5123 303 572 -78 C ATOM 1962 N LYS A 365 56.191 -34.763 21.930 1.00 63.85 N ANISOU 1962 N LYS A 365 10022 6805 7435 1090 738 -335 N ATOM 1963 CA LYS A 365 57.203 -35.788 21.713 1.00 63.06 C ANISOU 1963 CA LYS A 365 9845 6743 7372 1415 725 -349 C ATOM 1964 C LYS A 365 58.401 -35.184 20.988 1.00 61.42 C ANISOU 1964 C LYS A 365 9270 7071 6998 1404 467 -452 C ATOM 1965 O LYS A 365 58.234 -34.367 20.083 1.00 45.77 O ANISOU 1965 O LYS A 365 7091 5289 5009 1122 408 -618 O ATOM 1966 CB LYS A 365 56.631 -36.962 20.915 1.00 65.70 C ANISOU 1966 CB LYS A 365 10226 6711 8028 1428 990 -536 C ATOM 1967 CG LYS A 365 55.620 -37.805 21.676 1.00 68.46 C ANISOU 1967 CG LYS A 365 10944 6491 8575 1445 1319 -440 C ATOM 1968 CD LYS A 365 56.278 -38.556 22.822 1.00 74.20 C ANISOU 1968 CD LYS A 365 11993 7019 9180 1903 1415 -149 C ATOM 1969 CE LYS A 365 55.261 -39.365 23.611 1.00 76.52 C ANISOU 1969 CE LYS A 365 12716 6690 9669 1915 1819 -27 C ATOM 1970 NZ LYS A 365 54.551 -40.356 22.757 1.00 82.73 N ANISOU 1970 NZ LYS A 365 13447 7193 10792 1636 2076 -281 N ATOM 1971 N HIS A 366 59.605 -35.573 21.392 1.00 60.91 N ANISOU 1971 N HIS A 366 9105 7261 6776 1735 337 -341 N ATOM 1972 CA HIS A 366 60.809 -35.075 20.737 1.00 55.71 C ANISOU 1972 CA HIS A 366 8038 7154 5976 1720 122 -436 C ATOM 1973 C HIS A 366 60.867 -35.576 19.298 1.00 62.49 C ANISOU 1973 C HIS A 366 8715 7994 7037 1734 241 -652 C ATOM 1974 O HIS A 366 61.166 -34.814 18.380 1.00 55.38 O ANISOU 1974 O HIS A 366 7548 7396 6099 1503 164 -803 O ATOM 1975 CB HIS A 366 62.065 -35.499 21.499 1.00 54.00 C ANISOU 1975 CB HIS A 366 7686 7296 5536 2132 -43 -269 C ATOM 1976 CG HIS A 366 63.331 -34.929 20.936 1.00 71.01 C ANISOU 1976 CG HIS A 366 9344 10097 7539 2071 -261 -367 C ATOM 1977 ND1 HIS A 366 64.155 -35.636 20.088 1.00 66.94 N ANISOU 1977 ND1 HIS A 366 8549 9797 7088 2371 -216 -422 N ATOM 1978 CD2 HIS A 366 63.910 -33.715 21.097 1.00 58.72 C ANISOU 1978 CD2 HIS A 366 7531 9005 5776 1716 -484 -429 C ATOM 1979 CE1 HIS A 366 65.191 -34.886 19.756 1.00 55.22 C ANISOU 1979 CE1 HIS A 366 6606 8922 5455 2213 -407 -499 C ATOM 1980 NE2 HIS A 366 65.066 -33.716 20.355 1.00 57.24 N ANISOU 1980 NE2 HIS A 366 6868 9328 5552 1782 -567 -520 N ATOM 1981 N ASN A 367 60.574 -36.861 19.114 1.00 61.55 N ANISOU 1981 N ASN A 367 8791 7484 7109 2005 463 -671 N ATOM 1982 CA ASN A 367 60.486 -37.459 17.788 1.00 61.96 C ANISOU 1982 CA ASN A 367 8764 7434 7344 2013 603 -912 C ATOM 1983 C ASN A 367 59.195 -37.027 17.096 1.00 66.72 C ANISOU 1983 C ASN A 367 9412 7838 8099 1593 679 -1132 C ATOM 1984 O ASN A 367 58.105 -37.406 17.523 1.00 69.47 O ANISOU 1984 O ASN A 367 10015 7776 8603 1470 841 -1139 O ATOM 1985 CB ASN A 367 60.559 -38.986 17.885 1.00 57.66 C ANISOU 1985 CB ASN A 367 8505 6469 6934 2414 865 -880 C ATOM 1986 CG ASN A 367 60.842 -39.653 16.545 1.00 78.47 C ANISOU 1986 CG ASN A 367 11063 9072 9680 2514 989 -1124 C ATOM 1987 OD1 ASN A 367 60.495 -39.129 15.485 1.00 82.66 O ANISOU 1987 OD1 ASN A 367 11407 9741 10258 2210 933 -1369 O ATOM 1988 ND2 ASN A 367 61.471 -40.822 16.591 1.00 67.84 N ANISOU 1988 ND2 ASN A 367 9903 7535 8336 2991 1182 -1045 N ATOM 1989 N PRO A 368 59.319 -36.231 16.022 1.00 62.42 N ANISOU 1989 N PRO A 368 8605 7620 7492 1397 578 -1304 N ATOM 1990 CA PRO A 368 58.174 -35.639 15.319 1.00 59.48 C ANISOU 1990 CA PRO A 368 8222 7208 7171 1074 608 -1492 C ATOM 1991 C PRO A 368 57.173 -36.675 14.819 1.00 55.36 C ANISOU 1991 C PRO A 368 7834 6315 6887 1020 793 -1726 C ATOM 1992 O PRO A 368 55.969 -36.418 14.828 1.00 59.32 O ANISOU 1992 O PRO A 368 8373 6707 7460 770 841 -1814 O ATOM 1993 CB PRO A 368 58.826 -34.910 14.138 1.00 55.65 C ANISOU 1993 CB PRO A 368 7465 7135 6543 1039 519 -1619 C ATOM 1994 CG PRO A 368 60.227 -34.660 14.570 1.00 64.37 C ANISOU 1994 CG PRO A 368 8403 8549 7504 1190 407 -1445 C ATOM 1995 CD PRO A 368 60.600 -35.847 15.405 1.00 65.39 C ANISOU 1995 CD PRO A 368 8666 8460 7719 1514 455 -1313 C ATOM 1996 N SER A 369 57.669 -37.831 14.393 1.00 63.52 N ANISOU 1996 N SER A 369 8937 7169 8028 1244 914 -1838 N ATOM 1997 CA SER A 369 56.811 -38.865 13.828 1.00 71.56 C ANISOU 1997 CA SER A 369 10111 7813 9265 1130 1116 -2131 C ATOM 1998 C SER A 369 56.037 -39.614 14.908 1.00 74.67 C ANISOU 1998 C SER A 369 10823 7693 9856 1058 1342 -2036 C ATOM 1999 O SER A 369 55.115 -40.371 14.607 1.00 73.30 O ANISOU 1999 O SER A 369 10777 7180 9893 830 1542 -2294 O ATOM 2000 CB SER A 369 57.637 -39.850 12.997 1.00 66.58 C ANISOU 2000 CB SER A 369 9539 7102 8656 1408 1224 -2288 C ATOM 2001 OG SER A 369 58.677 -40.425 13.768 1.00 80.35 O ANISOU 2001 OG SER A 369 11429 8746 10355 1821 1300 -2008 O ATOM 2002 N GLN A 370 56.411 -39.400 16.165 1.00 73.37 N ANISOU 2002 N GLN A 370 10788 7480 9609 1234 1325 -1682 N ATOM 2003 CA GLN A 370 55.730 -40.056 17.275 1.00 70.43 C ANISOU 2003 CA GLN A 370 10763 6609 9389 1221 1577 -1534 C ATOM 2004 C GLN A 370 54.592 -39.193 17.810 1.00 66.64 C ANISOU 2004 C GLN A 370 10228 6165 8929 885 1540 -1477 C ATOM 2005 O GLN A 370 53.790 -39.646 18.626 1.00 70.64 O ANISOU 2005 O GLN A 370 10981 6269 9589 791 1783 -1389 O ATOM 2006 CB GLN A 370 56.717 -40.392 18.395 1.00 74.81 C ANISOU 2006 CB GLN A 370 11539 7092 9795 1682 1601 -1168 C ATOM 2007 CG GLN A 370 57.745 -41.446 18.006 1.00 88.02 C ANISOU 2007 CG GLN A 370 13334 8663 11448 2117 1729 -1175 C ATOM 2008 CD GLN A 370 58.741 -41.737 19.113 1.00102.92 C ANISOU 2008 CD GLN A 370 15383 10602 13120 2662 1722 -793 C ATOM 2009 OE1 GLN A 370 58.974 -40.906 19.991 1.00103.84 O ANISOU 2009 OE1 GLN A 370 15391 11025 13039 2692 1492 -564 O ATOM 2010 NE2 GLN A 370 59.341 -42.922 19.071 1.00104.54 N ANISOU 2010 NE2 GLN A 370 15841 10552 13326 3092 1960 -723 N ATOM 2011 N ARG A 371 54.525 -37.948 17.349 1.00 61.33 N ANISOU 2011 N ARG A 371 9260 5957 8086 733 1284 -1509 N ATOM 2012 CA ARG A 371 53.417 -37.070 17.706 1.00 65.11 C ANISOU 2012 CA ARG A 371 9687 6508 8545 470 1271 -1459 C ATOM 2013 C ARG A 371 52.158 -37.546 16.991 1.00 71.16 C ANISOU 2013 C ARG A 371 10334 7167 9537 165 1420 -1783 C ATOM 2014 O ARG A 371 52.232 -38.033 15.863 1.00 71.86 O ANISOU 2014 O ARG A 371 10281 7332 9690 107 1402 -2104 O ATOM 2015 CB ARG A 371 53.734 -35.616 17.351 1.00 58.11 C ANISOU 2015 CB ARG A 371 8594 6106 7378 437 1017 -1398 C ATOM 2016 CG ARG A 371 54.954 -35.063 18.069 1.00 57.42 C ANISOU 2016 CG ARG A 371 8572 6185 7061 628 857 -1138 C ATOM 2017 CD ARG A 371 55.344 -33.695 17.539 1.00 41.61 C ANISOU 2017 CD ARG A 371 6398 4606 4807 524 678 -1142 C ATOM 2018 NE ARG A 371 56.746 -33.395 17.813 1.00 51.44 N ANISOU 2018 NE ARG A 371 7575 6096 5875 647 520 -1027 N ATOM 2019 CZ ARG A 371 57.475 -32.536 17.109 1.00 56.02 C ANISOU 2019 CZ ARG A 371 7963 7037 6287 568 411 -1088 C ATOM 2020 NH1 ARG A 371 56.936 -31.892 16.082 1.00 54.29 N ANISOU 2020 NH1 ARG A 371 7663 6941 6023 436 455 -1233 N ATOM 2021 NH2 ARG A 371 58.747 -32.329 17.423 1.00 46.45 N ANISOU 2021 NH2 ARG A 371 6626 6088 4934 633 277 -1007 N ATOM 2022 N PRO A 372 50.995 -37.415 17.646 1.00 73.88 N ANISOU 2022 N PRO A 372 10717 7367 9988 -36 1570 -1718 N ATOM 2023 CA PRO A 372 49.754 -37.956 17.082 1.00 76.97 C ANISOU 2023 CA PRO A 372 10933 7697 10614 -376 1727 -2049 C ATOM 2024 C PRO A 372 49.290 -37.201 15.843 1.00 77.94 C ANISOU 2024 C PRO A 372 10652 8373 10589 -491 1501 -2319 C ATOM 2025 O PRO A 372 49.923 -36.230 15.436 1.00 70.66 O ANISOU 2025 O PRO A 372 9646 7810 9392 -302 1273 -2217 O ATOM 2026 CB PRO A 372 48.752 -37.785 18.227 1.00 69.87 C ANISOU 2026 CB PRO A 372 10138 6596 9812 -500 1937 -1825 C ATOM 2027 CG PRO A 372 49.261 -36.616 18.985 1.00 63.76 C ANISOU 2027 CG PRO A 372 9483 6002 8740 -251 1768 -1440 C ATOM 2028 CD PRO A 372 50.759 -36.719 18.923 1.00 68.32 C ANISOU 2028 CD PRO A 372 10194 6594 9170 31 1602 -1351 C ATOM 2029 N MET A 373 48.197 -37.659 15.246 1.00 76.54 N ANISOU 2029 N MET A 373 10230 8275 10577 -799 1581 -2671 N ATOM 2030 CA MET A 373 47.577 -36.935 14.147 1.00 73.74 C ANISOU 2030 CA MET A 373 9470 8516 10034 -856 1367 -2915 C ATOM 2031 C MET A 373 46.474 -36.036 14.686 1.00 76.07 C ANISOU 2031 C MET A 373 9586 9077 10242 -896 1392 -2727 C ATOM 2032 O MET A 373 45.974 -36.251 15.790 1.00 84.34 O ANISOU 2032 O MET A 373 10776 9807 11464 -999 1617 -2523 O ATOM 2033 CB MET A 373 47.019 -37.901 13.101 1.00 75.33 C ANISOU 2033 CB MET A 373 9442 8783 10397 -1157 1386 -3458 C ATOM 2034 CG MET A 373 48.084 -38.693 12.361 1.00 85.53 C ANISOU 2034 CG MET A 373 10917 9881 11701 -1052 1351 -3633 C ATOM 2035 SD MET A 373 47.409 -39.624 10.974 1.00136.96 S ANISOU 2035 SD MET A 373 17154 16614 18272 -1352 1281 -4127 S ATOM 2036 CE MET A 373 46.227 -40.675 11.812 1.00 69.67 C ANISOU 2036 CE MET A 373 8652 7668 10151 -1856 1642 -4272 C ATOM 2037 N LEU A 374 46.100 -35.027 13.907 1.00 68.61 N ANISOU 2037 N LEU A 374 8361 8708 8999 -761 1196 -2774 N ATOM 2038 CA LEU A 374 45.076 -34.080 14.327 1.00 70.98 C ANISOU 2038 CA LEU A 374 8502 9318 9147 -695 1233 -2568 C ATOM 2039 C LEU A 374 43.725 -34.765 14.487 1.00 71.93 C ANISOU 2039 C LEU A 374 8289 9508 9533 -1035 1393 -2802 C ATOM 2040 O LEU A 374 42.901 -34.347 15.297 1.00 69.04 O ANISOU 2040 O LEU A 374 7874 9179 9180 -1033 1548 -2565 O ATOM 2041 CB LEU A 374 44.981 -32.927 13.331 1.00 66.50 C ANISOU 2041 CB LEU A 374 7742 9361 8164 -405 1028 -2579 C ATOM 2042 CG LEU A 374 46.205 -32.010 13.352 1.00 68.40 C ANISOU 2042 CG LEU A 374 8335 9524 8132 -114 952 -2285 C ATOM 2043 CD1 LEU A 374 46.227 -31.098 12.141 1.00 66.76 C ANISOU 2043 CD1 LEU A 374 7989 9844 7534 161 808 -2361 C ATOM 2044 CD2 LEU A 374 46.227 -31.195 14.641 1.00 59.17 C ANISOU 2044 CD2 LEU A 374 7497 8112 6873 -11 1090 -1831 C ATOM 2045 N ARG A 375 43.507 -35.823 13.714 1.00 77.12 N ANISOU 2045 N ARG A 375 8722 10179 10399 -1350 1379 -3283 N ATOM 2046 CA ARG A 375 42.299 -36.625 13.849 1.00 84.20 C ANISOU 2046 CA ARG A 375 9293 11099 11601 -1799 1566 -3585 C ATOM 2047 C ARG A 375 42.288 -37.338 15.198 1.00 85.80 C ANISOU 2047 C ARG A 375 9863 10579 12160 -1993 1944 -3347 C ATOM 2048 O ARG A 375 41.231 -37.552 15.790 1.00 88.21 O ANISOU 2048 O ARG A 375 9970 10875 12670 -2261 2184 -3348 O ATOM 2049 CB ARG A 375 42.193 -37.640 12.709 1.00 80.91 C ANISOU 2049 CB ARG A 375 8641 10790 11312 -2147 1481 -4205 C ATOM 2050 N GLU A 376 43.474 -37.697 15.680 1.00 86.23 N ANISOU 2050 N GLU A 376 10440 10061 12260 -1820 2011 -3130 N ATOM 2051 CA GLU A 376 43.608 -38.387 16.958 1.00 74.80 C ANISOU 2051 CA GLU A 376 9427 7914 11081 -1888 2372 -2865 C ATOM 2052 C GLU A 376 43.437 -37.421 18.123 1.00 78.08 C ANISOU 2052 C GLU A 376 10007 8320 11340 -1618 2434 -2339 C ATOM 2053 O GLU A 376 42.977 -37.807 19.198 1.00 85.88 O ANISOU 2053 O GLU A 376 11199 8900 12530 -1719 2770 -2133 O ATOM 2054 CB GLU A 376 44.964 -39.091 17.046 1.00 76.69 C ANISOU 2054 CB GLU A 376 10147 7639 11353 -1696 2402 -2800 C ATOM 2055 CG GLU A 376 45.122 -40.249 16.071 1.00 89.76 C ANISOU 2055 CG GLU A 376 11787 9121 13197 -1965 2460 -3300 C ATOM 2056 CD GLU A 376 46.509 -40.861 16.110 1.00 94.66 C ANISOU 2056 CD GLU A 376 12827 9403 13737 -1616 2435 -3085 C ATOM 2057 OE1 GLU A 376 47.497 -40.099 16.102 1.00 92.22 O ANISOU 2057 OE1 GLU A 376 12611 9242 13186 -1240 2209 -2885 O ATOM 2058 OE2 GLU A 376 46.611 -42.105 16.150 1.00101.24 O ANISOU 2058 OE2 GLU A 376 13883 9861 14724 -1708 2654 -3113 O ATOM 2059 N VAL A 377 43.812 -36.166 17.904 1.00 72.36 N ANISOU 2059 N VAL A 377 9243 8010 10241 -1276 2148 -2128 N ATOM 2060 CA VAL A 377 43.642 -35.129 18.914 1.00 71.43 C ANISOU 2060 CA VAL A 377 9319 7907 9913 -1021 2199 -1666 C ATOM 2061 C VAL A 377 42.164 -34.786 19.078 1.00 76.71 C ANISOU 2061 C VAL A 377 9622 8902 10621 -1148 2357 -1663 C ATOM 2062 O VAL A 377 41.674 -34.607 20.194 1.00 76.04 O ANISOU 2062 O VAL A 377 9723 8590 10580 -1104 2609 -1344 O ATOM 2063 CB VAL A 377 44.433 -33.856 18.556 1.00 65.72 C ANISOU 2063 CB VAL A 377 8696 7506 8769 -672 1905 -1482 C ATOM 2064 CG1 VAL A 377 44.178 -32.760 19.580 1.00 65.83 C ANISOU 2064 CG1 VAL A 377 8965 7507 8542 -445 1992 -1046 C ATOM 2065 CG2 VAL A 377 45.919 -34.168 18.462 1.00 60.66 C ANISOU 2065 CG2 VAL A 377 8346 6611 8091 -553 1760 -1469 C ATOM 2066 N LEU A 378 41.455 -34.710 17.955 1.00 70.59 N ANISOU 2066 N LEU A 378 8309 8703 9808 -1278 2208 -2022 N ATOM 2067 CA LEU A 378 40.030 -34.394 17.963 1.00 69.83 C ANISOU 2067 CA LEU A 378 7734 9080 9719 -1373 2320 -2063 C ATOM 2068 C LEU A 378 39.204 -35.503 18.608 1.00 75.79 C ANISOU 2068 C LEU A 378 8367 9502 10929 -1835 2694 -2197 C ATOM 2069 O LEU A 378 38.095 -35.264 19.087 1.00 84.60 O ANISOU 2069 O LEU A 378 9194 10850 12099 -1900 2902 -2087 O ATOM 2070 CB LEU A 378 39.538 -34.140 16.538 1.00 67.98 C ANISOU 2070 CB LEU A 378 6916 9619 9294 -1377 2032 -2462 C ATOM 2071 CG LEU A 378 40.045 -32.859 15.877 1.00 69.06 C ANISOU 2071 CG LEU A 378 7132 10179 8929 -871 1751 -2287 C ATOM 2072 CD1 LEU A 378 39.853 -32.923 14.368 1.00 56.93 C ANISOU 2072 CD1 LEU A 378 5125 9284 7222 -874 1459 -2742 C ATOM 2073 CD2 LEU A 378 39.328 -31.653 16.462 1.00 69.60 C ANISOU 2073 CD2 LEU A 378 7204 10538 8701 -500 1865 -1868 C ATOM 2074 N GLU A 379 39.751 -36.714 18.617 1.00 75.70 N ANISOU 2074 N GLU A 379 8598 8929 11235 -2141 2824 -2423 N ATOM 2075 CA GLU A 379 39.055 -37.865 19.179 1.00 77.40 C ANISOU 2075 CA GLU A 379 8795 8712 11902 -2628 3256 -2580 C ATOM 2076 C GLU A 379 39.589 -38.228 20.561 1.00 73.93 C ANISOU 2076 C GLU A 379 9036 7462 11591 -2482 3605 -2138 C ATOM 2077 O GLU A 379 39.211 -39.251 21.130 1.00 75.21 O ANISOU 2077 O GLU A 379 9361 7096 12120 -2827 4041 -2202 O ATOM 2078 CB GLU A 379 39.172 -39.066 18.239 1.00 86.83 C ANISOU 2078 CB GLU A 379 9860 9773 13360 -3095 3260 -3169 C ATOM 2079 CG GLU A 379 38.506 -38.862 16.887 1.00 94.36 C ANISOU 2079 CG GLU A 379 10103 11560 14191 -3298 2933 -3679 C ATOM 2080 CD GLU A 379 38.803 -39.987 15.915 1.00113.15 C ANISOU 2080 CD GLU A 379 12463 13774 16756 -3714 2896 -4274 C ATOM 2081 OE1 GLU A 379 39.521 -40.935 16.299 1.00114.75 O ANISOU 2081 OE1 GLU A 379 13233 13185 17182 -3806 3160 -4252 O ATOM 2082 OE2 GLU A 379 38.319 -39.924 14.764 1.00122.38 O ANISOU 2082 OE2 GLU A 379 13081 15619 17800 -3894 2608 -4750 O ATOM 2083 N HIS A 380 40.469 -37.387 21.095 1.00 71.35 N ANISOU 2083 N HIS A 380 9123 7046 10939 -1976 3429 -1703 N ATOM 2084 CA HIS A 380 41.040 -37.617 22.417 1.00 76.56 C ANISOU 2084 CA HIS A 380 10423 7045 11619 -1751 3687 -1273 C ATOM 2085 C HIS A 380 39.957 -37.510 23.487 1.00 77.57 C ANISOU 2085 C HIS A 380 10562 7040 11870 -1819 4092 -997 C ATOM 2086 O HIS A 380 39.170 -36.564 23.482 1.00 84.93 O ANISOU 2086 O HIS A 380 11163 8474 12631 -1724 4029 -883 O ATOM 2087 CB HIS A 380 42.170 -36.622 22.697 1.00 74.90 C ANISOU 2087 CB HIS A 380 10564 6902 10991 -1250 3357 -931 C ATOM 2088 CG HIS A 380 42.999 -36.970 23.893 1.00 83.47 C ANISOU 2088 CG HIS A 380 12286 7390 12038 -986 3519 -569 C ATOM 2089 ND1 HIS A 380 42.602 -36.687 25.183 1.00 84.72 N ANISOU 2089 ND1 HIS A 380 12761 7300 12128 -818 3780 -169 N ATOM 2090 CD2 HIS A 380 44.205 -37.577 23.996 1.00 81.70 C ANISOU 2090 CD2 HIS A 380 12404 6869 11768 -796 3428 -537 C ATOM 2091 CE1 HIS A 380 43.527 -37.106 26.028 1.00 80.22 C ANISOU 2091 CE1 HIS A 380 12521 6632 11326 -479 3652 40 C ATOM 2092 NE2 HIS A 380 44.511 -37.649 25.334 1.00 81.13 N ANISOU 2092 NE2 HIS A 380 12651 6712 11462 -469 3460 -139 N ATOM 2093 N PRO A 381 39.911 -38.491 24.403 1.00 83.18 N ANISOU 2093 N PRO A 381 11680 7063 12860 -1941 4552 -869 N ATOM 2094 CA PRO A 381 38.900 -38.568 25.466 1.00 82.98 C ANISOU 2094 CA PRO A 381 11683 6933 12912 -1930 4912 -626 C ATOM 2095 C PRO A 381 38.783 -37.282 26.280 1.00 83.17 C ANISOU 2095 C PRO A 381 11872 7136 12592 -1503 4849 -150 C ATOM 2096 O PRO A 381 37.672 -36.863 26.602 1.00 99.96 O ANISOU 2096 O PRO A 381 13718 9505 14758 -1563 5053 -39 O ATOM 2097 CB PRO A 381 39.402 -39.718 26.341 1.00 82.14 C ANISOU 2097 CB PRO A 381 12080 6329 12801 -1718 5085 -519 C ATOM 2098 CG PRO A 381 40.166 -40.584 25.402 1.00 87.69 C ANISOU 2098 CG PRO A 381 12791 6928 13598 -1881 4959 -857 C ATOM 2099 CD PRO A 381 40.832 -39.642 24.438 1.00 79.14 C ANISOU 2099 CD PRO A 381 11535 6167 12366 -1831 4535 -958 C ATOM 2100 N TRP A 382 39.915 -36.664 26.599 1.00 77.20 N ANISOU 2100 N TRP A 382 11538 6338 11457 -1051 4524 96 N ATOM 2101 CA TRP A 382 39.916 -35.423 27.363 1.00 72.31 C ANISOU 2101 CA TRP A 382 11128 5916 10431 -623 4375 471 C ATOM 2102 C TRP A 382 39.338 -34.269 26.548 1.00 78.16 C ANISOU 2102 C TRP A 382 11470 7213 11014 -659 4280 468 C ATOM 2103 O TRP A 382 38.688 -33.377 27.093 1.00 84.59 O ANISOU 2103 O TRP A 382 12316 8214 11612 -430 4380 751 O ATOM 2104 CB TRP A 382 41.332 -35.079 27.827 1.00 69.58 C ANISOU 2104 CB TRP A 382 11181 5579 9677 -214 3960 600 C ATOM 2105 CG TRP A 382 41.401 -33.831 28.650 1.00 71.34 C ANISOU 2105 CG TRP A 382 11587 6043 9477 153 3744 841 C ATOM 2106 CD1 TRP A 382 41.228 -33.730 30.001 1.00 70.62 C ANISOU 2106 CD1 TRP A 382 11695 5922 9215 403 3775 995 C ATOM 2107 CD2 TRP A 382 41.661 -32.506 28.179 1.00 70.44 C ANISOU 2107 CD2 TRP A 382 11469 6238 9056 286 3467 890 C ATOM 2108 NE1 TRP A 382 41.365 -32.422 30.398 1.00 67.67 N ANISOU 2108 NE1 TRP A 382 11412 5807 8492 638 3515 1079 N ATOM 2109 CE2 TRP A 382 41.633 -31.649 29.296 1.00 58.87 C ANISOU 2109 CE2 TRP A 382 10186 4896 7286 582 3319 1019 C ATOM 2110 CE3 TRP A 382 41.918 -31.957 26.916 1.00 69.84 C ANISOU 2110 CE3 TRP A 382 11257 6363 8918 171 3356 812 C ATOM 2111 CZ2 TRP A 382 41.849 -30.278 29.194 1.00 59.71 C ANISOU 2111 CZ2 TRP A 382 10338 5262 7086 743 3046 1029 C ATOM 2112 CZ3 TRP A 382 42.132 -30.596 26.816 1.00 67.04 C ANISOU 2112 CZ3 TRP A 382 10979 6314 8180 400 3090 887 C ATOM 2113 CH2 TRP A 382 42.097 -29.772 27.947 1.00 66.06 C ANISOU 2113 CH2 TRP A 382 11031 6241 7829 666 2926 971 C ATOM 2114 N ILE A 383 39.581 -34.292 25.241 1.00 71.14 N ANISOU 2114 N ILE A 383 10162 6729 10138 -813 3947 82 N ATOM 2115 CA ILE A 383 39.065 -33.260 24.350 1.00 69.67 C ANISOU 2115 CA ILE A 383 9518 7253 9699 -705 3700 -15 C ATOM 2116 C ILE A 383 37.552 -33.373 24.199 1.00 76.42 C ANISOU 2116 C ILE A 383 9778 8511 10747 -915 3956 -123 C ATOM 2117 O ILE A 383 36.829 -32.389 24.351 1.00 81.38 O ANISOU 2117 O ILE A 383 10260 9542 11118 -642 4002 104 O ATOM 2118 CB ILE A 383 39.721 -33.338 22.954 1.00 72.96 C ANISOU 2118 CB ILE A 383 9652 8004 10066 -791 3297 -411 C ATOM 2119 CG1 ILE A 383 41.176 -32.873 23.019 1.00 68.70 C ANISOU 2119 CG1 ILE A 383 9601 7256 9246 -522 3016 -267 C ATOM 2120 CG2 ILE A 383 38.958 -32.487 21.953 1.00 68.95 C ANISOU 2120 CG2 ILE A 383 8601 8268 9330 -688 3112 -554 C ATOM 2121 CD1 ILE A 383 41.329 -31.401 23.342 1.00 65.05 C ANISOU 2121 CD1 ILE A 383 9405 6987 8323 -146 2911 66 C ATOM 2122 N THR A 384 37.079 -34.582 23.917 1.00 76.97 N ANISOU 2122 N THR A 384 9512 8473 11259 -1404 4149 -475 N ATOM 2123 CA THR A 384 35.665 -34.812 23.640 1.00 82.39 C ANISOU 2123 CA THR A 384 9501 9633 12169 -1722 4364 -687 C ATOM 2124 C THR A 384 34.788 -34.726 24.887 1.00 89.21 C ANISOU 2124 C THR A 384 10471 10287 13138 -1672 4856 -301 C ATOM 2125 O THR A 384 33.561 -34.765 24.790 1.00 97.91 O ANISOU 2125 O THR A 384 10960 11852 14390 -1880 5068 -403 O ATOM 2126 CB THR A 384 35.447 -36.187 22.986 1.00 87.37 C ANISOU 2126 CB THR A 384 9781 10154 13262 -2367 4466 -1239 C ATOM 2127 OG1 THR A 384 35.927 -37.215 23.861 1.00 89.65 O ANISOU 2127 OG1 THR A 384 10658 9544 13861 -2553 4844 -1133 O ATOM 2128 CG2 THR A 384 36.191 -36.269 21.661 1.00 83.50 C ANISOU 2128 CG2 THR A 384 9133 9947 12648 -2405 3992 -1651 C ATOM 2129 N ALA A 385 35.412 -34.612 26.055 1.00 86.63 N ANISOU 2129 N ALA A 385 10896 9309 12710 -1384 5037 137 N ATOM 2130 CA ALA A 385 34.666 -34.563 27.307 1.00 86.17 C ANISOU 2130 CA ALA A 385 11064 9002 12673 -1220 5331 493 C ATOM 2131 C ALA A 385 34.584 -33.147 27.868 1.00 90.59 C ANISOU 2131 C ALA A 385 11891 9782 12747 -633 5179 925 C ATOM 2132 O ALA A 385 33.861 -32.897 28.829 1.00 83.64 O ANISOU 2132 O ALA A 385 11135 8819 11824 -432 5342 1196 O ATOM 2133 CB ALA A 385 35.291 -35.498 28.333 1.00 79.37 C ANISOU 2133 CB ALA A 385 10869 7328 11961 -1178 5458 593 C ATOM 2134 N ASN A 386 35.322 -32.220 27.266 1.00 93.01 N ANISOU 2134 N ASN A 386 12318 10345 12677 -356 4857 959 N ATOM 2135 CA ASN A 386 35.351 -30.849 27.764 1.00 82.84 C ANISOU 2135 CA ASN A 386 11383 9181 10912 182 4632 1300 C ATOM 2136 C ASN A 386 35.008 -29.817 26.695 1.00 84.58 C ANISOU 2136 C ASN A 386 11200 10134 10802 392 4444 1245 C ATOM 2137 O ASN A 386 34.660 -28.680 27.013 1.00 84.60 O ANISOU 2137 O ASN A 386 11379 10303 10461 798 4303 1490 O ATOM 2138 CB ASN A 386 36.723 -30.536 28.363 1.00 70.06 C ANISOU 2138 CB ASN A 386 10477 7076 9067 430 4302 1394 C ATOM 2139 CG ASN A 386 37.048 -31.407 29.561 1.00 81.49 C ANISOU 2139 CG ASN A 386 12301 7957 10704 432 4405 1417 C ATOM 2140 OD1 ASN A 386 36.768 -31.041 30.702 1.00 87.51 O ANISOU 2140 OD1 ASN A 386 13310 8592 11348 717 4417 1564 O ATOM 2141 ND2 ASN A 386 37.641 -32.568 29.307 1.00 79.15 N ANISOU 2141 ND2 ASN A 386 12024 7379 10671 148 4479 1223 N ATOM 2142 N SER A 387 35.102 -30.216 25.431 1.00 82.66 N ANISOU 2142 N SER A 387 10425 10307 10676 144 4391 868 N ATOM 2143 CA SER A 387 34.840 -29.300 24.327 1.00 74.65 C ANISOU 2143 CA SER A 387 9025 10026 9311 422 4115 762 C ATOM 2144 C SER A 387 33.358 -28.967 24.203 1.00 76.88 C ANISOU 2144 C SER A 387 8667 10998 9547 566 4310 818 C ATOM 2145 O SER A 387 32.497 -29.810 24.452 1.00 78.95 O ANISOU 2145 O SER A 387 8445 11348 10205 206 4592 689 O ATOM 2146 CB SER A 387 35.348 -29.888 23.009 1.00 76.07 C ANISOU 2146 CB SER A 387 8810 10468 9624 125 3734 253 C ATOM 2147 OG SER A 387 35.059 -29.025 21.925 1.00 76.38 O ANISOU 2147 OG SER A 387 8489 11241 9292 445 3488 162 O ATOM 2148 N SER A 388 33.071 -27.729 23.813 1.00 88.34 N ANISOU 2148 N SER A 388 10147 12895 10523 1047 4065 962 N ATOM 2149 CA SER A 388 31.699 -27.285 23.599 1.00 90.91 C ANISOU 2149 CA SER A 388 9904 13903 10737 1254 4116 986 C ATOM 2150 C SER A 388 31.342 -27.331 22.118 1.00 97.78 C ANISOU 2150 C SER A 388 10012 15612 11527 1268 3877 603 C ATOM 2151 O SER A 388 30.210 -27.039 21.733 1.00110.83 O ANISOU 2151 O SER A 388 11113 17896 13100 1435 3835 560 O ATOM 2152 CB SER A 388 31.499 -25.871 24.147 1.00 89.88 C ANISOU 2152 CB SER A 388 10358 13600 10192 1798 3989 1403 C ATOM 2153 OG SER A 388 31.771 -25.819 25.536 1.00 92.99 O ANISOU 2153 OG SER A 388 11404 13257 10673 1806 4125 1712 O ATOM 2154 N LYS A 389 32.318 -27.695 21.292 1.00 90.93 N ANISOU 2154 N LYS A 389 9140 14747 10662 1119 3664 328 N ATOM 2155 CA LYS A 389 32.117 -27.779 19.849 1.00 96.87 C ANISOU 2155 CA LYS A 389 9265 16236 11306 1111 3295 -90 C ATOM 2156 C LYS A 389 32.669 -29.089 19.291 1.00 98.20 C ANISOU 2156 C LYS A 389 9141 16281 11891 456 3128 -635 C ATOM 2157 O LYS A 389 33.735 -29.544 19.706 1.00 91.44 O ANISOU 2157 O LYS A 389 8879 14623 11240 212 3119 -622 O ATOM 2158 CB LYS A 389 32.770 -26.586 19.146 1.00 94.21 C ANISOU 2158 CB LYS A 389 9444 15887 10465 1624 2967 68 C ATOM 2159 CG LYS A 389 32.156 -25.243 19.508 1.00100.33 C ANISOU 2159 CG LYS A 389 10594 16656 10872 2168 2967 518 C ATOM 2160 CD LYS A 389 32.817 -24.107 18.748 1.00 94.60 C ANISOU 2160 CD LYS A 389 10359 15854 9732 2571 2661 657 C ATOM 2161 N PRO A 390 31.941 -29.699 18.343 1.00102.79 N ANISOU 2161 N PRO A 390 8866 17591 12600 160 2949 -1132 N ATOM 2162 CA PRO A 390 32.332 -30.983 17.752 1.00104.46 C ANISOU 2162 CA PRO A 390 8852 17608 13229 -521 2776 -1710 C ATOM 2163 C PRO A 390 33.474 -30.856 16.749 1.00111.85 C ANISOU 2163 C PRO A 390 10092 18465 13939 -391 2387 -1910 C ATOM 2164 O PRO A 390 34.036 -29.774 16.579 1.00112.88 O ANISOU 2164 O PRO A 390 10655 18616 13620 182 2280 -1586 O ATOM 2165 CB PRO A 390 31.052 -31.443 17.054 1.00108.56 C ANISOU 2165 CB PRO A 390 8481 18922 13845 -792 2627 -2103 C ATOM 2166 CG PRO A 390 30.378 -30.173 16.672 1.00113.10 C ANISOU 2166 CG PRO A 390 8933 20170 13872 -58 2448 -1773 C ATOM 2167 CD PRO A 390 30.666 -29.206 17.791 1.00107.65 C ANISOU 2167 CD PRO A 390 8912 18997 12995 448 2781 -1120 C ATOM 2168 N SER A 391 33.805 -31.962 16.092 1.00118.38 N ANISOU 2168 N SER A 391 10723 19180 15076 -934 2224 -2446 N ATOM 2169 CA SER A 391 34.865 -31.977 15.092 1.00113.36 C ANISOU 2169 CA SER A 391 10330 18482 14260 -844 1881 -2674 C ATOM 2170 C SER A 391 34.359 -31.457 13.750 1.00120.08 C ANISOU 2170 C SER A 391 10593 20357 14673 -529 1537 -2954 C ATOM 2171 O SER A 391 33.222 -30.997 13.641 1.00117.30 O ANISOU 2171 O SER A 391 9760 20693 14116 -309 1514 -2885 O ATOM 2172 CB SER A 391 35.428 -33.390 14.935 1.00112.51 C ANISOU 2172 CB SER A 391 10316 17808 14625 -1497 1885 -3122 C ATOM 2173 OG SER A 391 35.884 -33.896 16.178 1.00109.38 O ANISOU 2173 OG SER A 391 10483 16492 14585 -1707 2222 -2839 O ATOM 2174 N ASN A 392 35.210 -31.533 12.731 1.00123.46 N ANISOU 2174 N ASN A 392 11172 20806 14929 -460 1239 -3211 N ATOM 2175 CA ASN A 392 34.861 -31.050 11.399 1.00127.34 C ANISOU 2175 CA ASN A 392 11214 22221 14947 -96 900 -3467 C ATOM 2176 C ASN A 392 33.714 -31.837 10.771 1.00134.63 C ANISOU 2176 C ASN A 392 11481 23711 15960 -511 703 -3970 C ATOM 2177 O ASN A 392 32.796 -31.258 10.190 1.00141.63 O ANISOU 2177 O ASN A 392 12047 25341 16424 -153 510 -3942 O ATOM 2178 CB ASN A 392 36.086 -31.097 10.483 1.00129.58 C ANISOU 2178 CB ASN A 392 11887 22278 15069 14 664 -3636 C ATOM 2179 CG ASN A 392 36.801 -32.434 10.531 1.00133.52 C ANISOU 2179 CG ASN A 392 12582 22077 16073 -643 677 -4009 C ATOM 2180 OD1 ASN A 392 36.245 -33.435 10.985 1.00139.84 O ANISOU 2180 OD1 ASN A 392 13117 22694 17322 -1235 828 -4282 O ATOM 2181 ND2 ASN A 392 38.043 -32.457 10.061 1.00127.61 N ANISOU 2181 ND2 ASN A 392 12320 20922 15245 -525 564 -4012 N TER 2182 ASN A 392 ATOM 2183 N SER D 6 57.948 -11.324 -10.440 1.00119.02 N ANISOU 2183 N SER D 6 15869 18065 11289 -836 6242 -2299 N ATOM 2184 CA SER D 6 58.253 -9.950 -10.058 1.00118.38 C ANISOU 2184 CA SER D 6 16242 17511 11224 -1039 6581 -1586 C ATOM 2185 C SER D 6 57.822 -9.672 -8.622 1.00108.42 C ANISOU 2185 C SER D 6 14598 15973 10623 -1135 5957 -1315 C ATOM 2186 O SER D 6 56.967 -10.366 -8.073 1.00 89.43 O ANISOU 2186 O SER D 6 11743 13788 8447 -796 4954 -1432 O ATOM 2187 CB SER D 6 57.578 -8.964 -11.013 1.00132.06 C ANISOU 2187 CB SER D 6 19108 19397 11673 -595 6593 -984 C ATOM 2188 OG SER D 6 56.306 -9.437 -11.421 1.00134.22 O ANISOU 2188 OG SER D 6 19710 20224 11064 -43 5896 -1019 O ATOM 2189 N SER D 7 58.419 -8.647 -8.022 1.00111.95 N ANISOU 2189 N SER D 7 15214 15883 11440 -1550 6386 -888 N ATOM 2190 CA SER D 7 58.167 -8.319 -6.625 1.00109.05 C ANISOU 2190 CA SER D 7 14519 15132 11785 -1654 5747 -596 C ATOM 2191 C SER D 7 56.770 -7.747 -6.405 1.00102.38 C ANISOU 2191 C SER D 7 14446 14352 10102 -1017 5066 15 C ATOM 2192 O SER D 7 56.276 -6.957 -7.210 1.00119.38 O ANISOU 2192 O SER D 7 17658 16599 11102 -699 5414 477 O ATOM 2193 CB SER D 7 59.218 -7.329 -6.117 1.00114.85 C ANISOU 2193 CB SER D 7 15336 15232 13071 -2296 6311 -309 C ATOM 2194 OG SER D 7 60.516 -7.894 -6.165 1.00114.19 O ANISOU 2194 OG SER D 7 14381 15075 13932 -2755 6548 -760 O ATOM 2195 N TYR D 8 56.143 -8.175 -5.311 1.00 93.87 N ANISOU 2195 N TYR D 8 12796 13242 9629 -794 4108 47 N ATOM 2196 CA TYR D 8 54.843 -7.666 -4.867 1.00 82.63 C ANISOU 2196 CA TYR D 8 11944 11831 7619 -173 3425 695 C ATOM 2197 C TYR D 8 53.713 -7.910 -5.868 1.00 89.60 C ANISOU 2197 C TYR D 8 13328 13352 7362 494 3094 861 C ATOM 2198 O TYR D 8 52.623 -7.356 -5.727 1.00 88.83 O ANISOU 2198 O TYR D 8 13831 13337 6583 1060 2677 1525 O ATOM 2199 CB TYR D 8 54.945 -6.173 -4.545 1.00 82.70 C ANISOU 2199 CB TYR D 8 12958 11243 7221 -288 3942 1399 C ATOM 2200 CG TYR D 8 56.047 -5.847 -3.562 1.00 73.06 C ANISOU 2200 CG TYR D 8 11331 9376 7053 -1021 4215 1268 C ATOM 2201 CD1 TYR D 8 55.965 -6.257 -2.237 1.00 78.18 C ANISOU 2201 CD1 TYR D 8 11240 9798 8666 -1067 3467 1175 C ATOM 2202 CD2 TYR D 8 57.171 -5.135 -3.959 1.00 85.10 C ANISOU 2202 CD2 TYR D 8 13165 10538 8633 -1661 5134 1246 C ATOM 2203 CE1 TYR D 8 56.971 -5.965 -1.334 1.00 77.98 C ANISOU 2203 CE1 TYR D 8 10848 9218 9564 -1765 3648 1058 C ATOM 2204 CE2 TYR D 8 58.182 -4.837 -3.064 1.00 83.09 C ANISOU 2204 CE2 TYR D 8 12456 9749 9364 -2329 5178 1119 C ATOM 2205 CZ TYR D 8 58.076 -5.255 -1.754 1.00 93.05 C ANISOU 2205 CZ TYR D 8 13079 10790 11488 -2463 4571 1050 C ATOM 2206 OH TYR D 8 59.079 -4.962 -0.859 1.00102.90 O ANISOU 2206 OH TYR D 8 13846 11649 13603 -2951 4287 882 O ATOM 2207 N SER D 9 53.976 -8.743 -6.870 1.00 91.54 N ANISOU 2207 N SER D 9 13338 14051 7391 432 3277 280 N ATOM 2208 CA SER D 9 52.944 -9.171 -7.805 1.00 81.89 C ANISOU 2208 CA SER D 9 12469 13482 5162 980 2827 311 C ATOM 2209 C SER D 9 52.528 -10.600 -7.477 1.00 76.65 C ANISOU 2209 C SER D 9 10782 13176 5166 1088 1896 -257 C ATOM 2210 O SER D 9 53.106 -11.560 -7.987 1.00 79.03 O ANISOU 2210 O SER D 9 10607 13659 5761 834 2062 -996 O ATOM 2211 CB SER D 9 53.439 -9.071 -9.249 1.00 91.55 C ANISOU 2211 CB SER D 9 14340 14953 5490 877 3677 73 C ATOM 2212 OG SER D 9 52.435 -9.486 -10.156 1.00 95.36 O ANISOU 2212 OG SER D 9 15086 15937 5212 1227 3057 59 O ATOM 2213 N TYR D 10 51.524 -10.733 -6.615 1.00 69.89 N ANISOU 2213 N TYR D 10 9616 12387 4552 1486 957 118 N ATOM 2214 CA TYR D 10 51.155 -12.032 -6.063 1.00 71.65 C ANISOU 2214 CA TYR D 10 8787 12832 5605 1555 61 -352 C ATOM 2215 C TYR D 10 49.966 -12.665 -6.778 1.00 69.64 C ANISOU 2215 C TYR D 10 8632 13246 4580 2007 -714 -327 C ATOM 2216 O TYR D 10 49.123 -11.969 -7.340 1.00 75.39 O ANISOU 2216 O TYR D 10 10125 14056 4463 2319 -772 289 O ATOM 2217 CB TYR D 10 50.839 -11.897 -4.570 1.00 60.40 C ANISOU 2217 CB TYR D 10 6830 11041 5076 1688 -514 21 C ATOM 2218 CG TYR D 10 51.956 -11.285 -3.754 1.00 64.15 C ANISOU 2218 CG TYR D 10 7192 10853 6330 1199 99 8 C ATOM 2219 CD1 TYR D 10 53.287 -11.475 -4.106 1.00 60.27 C ANISOU 2219 CD1 TYR D 10 6442 10179 6280 583 888 -579 C ATOM 2220 CD2 TYR D 10 51.679 -10.518 -2.629 1.00 64.58 C ANISOU 2220 CD2 TYR D 10 7410 10462 6667 1349 -117 610 C ATOM 2221 CE1 TYR D 10 54.310 -10.915 -3.360 1.00 78.14 C ANISOU 2221 CE1 TYR D 10 8540 11873 9275 70 1385 -556 C ATOM 2222 CE2 TYR D 10 52.694 -9.956 -1.877 1.00 56.44 C ANISOU 2222 CE2 TYR D 10 6316 8816 6312 835 369 581 C ATOM 2223 CZ TYR D 10 54.007 -10.158 -2.246 1.00 67.27 C ANISOU 2223 CZ TYR D 10 7357 10058 8143 167 1088 3 C ATOM 2224 OH TYR D 10 55.021 -9.601 -1.502 1.00 76.69 O ANISOU 2224 OH TYR D 10 8430 10680 10028 -406 1514 7 O ATOM 2225 N ASP D 11 49.907 -13.993 -6.747 1.00 83.47 N ANISOU 2225 N ASP D 11 10515 16455 4746 3842 882 806 N ATOM 2226 CA ASP D 11 48.753 -14.722 -7.258 1.00 84.64 C ANISOU 2226 CA ASP D 11 10852 16581 4725 3787 786 408 C ATOM 2227 C ASP D 11 47.636 -14.684 -6.218 1.00 85.65 C ANISOU 2227 C ASP D 11 10987 16602 4955 3505 680 149 C ATOM 2228 O ASP D 11 47.404 -15.657 -5.499 1.00 81.89 O ANISOU 2228 O ASP D 11 10687 15930 4497 3345 724 -84 O ATOM 2229 CB ASP D 11 49.136 -16.163 -7.605 1.00 86.44 C ANISOU 2229 CB ASP D 11 11342 16687 4814 3882 880 223 C ATOM 2230 CG ASP D 11 48.001 -16.931 -8.260 1.00 94.91 C ANISOU 2230 CG ASP D 11 12628 17743 5689 3853 744 -166 C ATOM 2231 OD1 ASP D 11 46.992 -16.302 -8.642 1.00 88.66 O ANISOU 2231 OD1 ASP D 11 11758 17081 4849 3810 583 -268 O ATOM 2232 OD2 ASP D 11 48.129 -18.165 -8.415 1.00 89.80 O ANISOU 2232 OD2 ASP D 11 12230 16962 4927 3892 773 -371 O ATOM 2233 N ALA D 12 46.950 -13.549 -6.143 1.00 85.66 N ANISOU 2233 N ALA D 12 10797 16740 5010 3456 551 196 N ATOM 2234 CA ALA D 12 45.950 -13.319 -5.107 1.00 82.84 C ANISOU 2234 CA ALA D 12 10392 16331 4750 3231 485 -12 C ATOM 2235 C ALA D 12 44.990 -12.207 -5.521 1.00 85.81 C ANISOU 2235 C ALA D 12 10566 16938 5099 3267 295 -43 C ATOM 2236 O ALA D 12 45.347 -11.362 -6.341 1.00 84.46 O ANISOU 2236 O ALA D 12 10286 16913 4891 3432 220 205 O ATOM 2237 CB ALA D 12 46.633 -12.975 -3.787 1.00 77.67 C ANISOU 2237 CB ALA D 12 9723 15506 4281 3121 566 180 C ATOM 2238 N PRO D 13 43.767 -12.208 -4.958 1.00 92.65 N ANISOU 2238 N PRO D 13 11374 17849 5979 3117 224 -351 N ATOM 2239 CA PRO D 13 42.793 -11.151 -5.257 1.00 87.44 C ANISOU 2239 CA PRO D 13 10496 17430 5298 3168 13 -422 C ATOM 2240 C PRO D 13 43.355 -9.756 -4.996 1.00 91.64 C ANISOU 2240 C PRO D 13 10877 17995 5946 3242 -60 -59 C ATOM 2241 O PRO D 13 43.939 -9.516 -3.935 1.00 77.80 O ANISOU 2241 O PRO D 13 9143 16087 4329 3162 36 99 O ATOM 2242 CB PRO D 13 41.639 -11.454 -4.295 1.00 97.79 C ANISOU 2242 CB PRO D 13 11740 18763 6651 2975 46 -792 C ATOM 2243 CG PRO D 13 41.743 -12.912 -4.031 1.00 91.15 C ANISOU 2243 CG PRO D 13 11123 17726 5783 2833 220 -984 C ATOM 2244 CD PRO D 13 43.212 -13.223 -4.042 1.00 87.04 C ANISOU 2244 CD PRO D 13 10787 16985 5299 2898 345 -660 C ATOM 2245 N SER D 14 43.186 -8.854 -5.958 1.00 81.06 N ANISOU 2245 N SER D 14 9422 16823 4555 3388 -257 75 N ATOM 2246 CA SER D 14 43.671 -7.487 -5.814 1.00 88.03 C ANISOU 2246 CA SER D 14 10169 17705 5572 3438 -372 430 C ATOM 2247 C SER D 14 42.667 -6.480 -6.367 1.00 86.85 C ANISOU 2247 C SER D 14 9866 17712 5422 3506 -677 348 C ATOM 2248 O SER D 14 42.951 -5.285 -6.440 1.00 91.53 O ANISOU 2248 O SER D 14 10366 18257 6153 3536 -827 627 O ATOM 2249 CB SER D 14 45.022 -7.321 -6.512 1.00106.94 C ANISOU 2249 CB SER D 14 12604 20054 7974 3539 -261 841 C ATOM 2250 OG SER D 14 45.513 -6.001 -6.364 1.00114.46 O ANISOU 2250 OG SER D 14 13426 20964 9099 3539 -384 1198 O ATOM 2251 N ASP D 15 41.492 -6.969 -6.748 1.00 83.27 N ANISOU 2251 N ASP D 15 9385 17405 4850 3514 -801 -45 N ATOM 2252 CA ASP D 15 40.460 -6.118 -7.333 1.00 92.10 C ANISOU 2252 CA ASP D 15 10343 18652 5998 3589 -1145 -174 C ATOM 2253 C ASP D 15 39.482 -5.618 -6.276 1.00 91.10 C ANISOU 2253 C ASP D 15 9987 18600 6026 3532 -1285 -423 C ATOM 2254 O ASP D 15 39.335 -6.227 -5.220 1.00 83.21 O ANISOU 2254 O ASP D 15 8985 17452 5178 3361 -1030 -606 O ATOM 2255 CB ASP D 15 39.696 -6.870 -8.425 1.00 87.80 C ANISOU 2255 CB ASP D 15 9873 18219 5269 3654 -1290 -477 C ATOM 2256 CG ASP D 15 40.600 -7.358 -9.543 1.00105.48 C ANISOU 2256 CG ASP D 15 12374 20392 7313 3761 -1160 -262 C ATOM 2257 OD1 ASP D 15 41.609 -6.682 -9.835 1.00102.17 O ANISOU 2257 OD1 ASP D 15 11991 19908 6920 3817 -1062 148 O ATOM 2258 OD2 ASP D 15 40.296 -8.416 -10.133 1.00100.99 O ANISOU 2258 OD2 ASP D 15 11970 19835 6567 3794 -1164 -513 O ATOM 2259 N PHE D 16 38.808 -4.511 -6.576 1.00 90.40 N ANISOU 2259 N PHE D 16 9714 18530 6104 3608 -1612 -435 N ATOM 2260 CA PHE D 16 37.828 -3.934 -5.665 1.00 88.88 C ANISOU 2260 CA PHE D 16 9271 18220 6279 3532 -1685 -687 C ATOM 2261 C PHE D 16 36.630 -4.860 -5.483 1.00 96.26 C ANISOU 2261 C PHE D 16 10042 19137 7397 3385 -1587 -1173 C ATOM 2262 O PHE D 16 36.046 -5.336 -6.456 1.00 89.55 O ANISOU 2262 O PHE D 16 9161 18385 6479 3412 -1770 -1368 O ATOM 2263 CB PHE D 16 37.363 -2.567 -6.175 1.00 90.93 C ANISOU 2263 CB PHE D 16 9375 18515 6658 3688 -2114 -604 C ATOM 2264 CG PHE D 16 36.389 -1.878 -5.262 1.00 96.86 C ANISOU 2264 CG PHE D 16 9867 19140 7795 3667 -2189 -860 C ATOM 2265 CD1 PHE D 16 36.840 -1.134 -4.183 1.00100.49 C ANISOU 2265 CD1 PHE D 16 10368 19434 8382 3676 -2126 -693 C ATOM 2266 CD2 PHE D 16 35.025 -1.971 -5.482 1.00 90.44 C ANISOU 2266 CD2 PHE D 16 8772 18362 7229 3659 -2336 -1271 C ATOM 2267 CE1 PHE D 16 35.948 -0.499 -3.339 1.00 96.24 C ANISOU 2267 CE1 PHE D 16 9629 18783 8157 3708 -2171 -945 C ATOM 2268 CE2 PHE D 16 34.129 -1.338 -4.642 1.00 93.71 C ANISOU 2268 CE2 PHE D 16 8918 18680 8007 3676 -2358 -1508 C ATOM 2269 CZ PHE D 16 34.591 -0.601 -3.570 1.00 99.82 C ANISOU 2269 CZ PHE D 16 9770 19305 8852 3716 -2257 -1352 C ATOM 2270 N ILE D 17 36.270 -5.112 -4.229 1.00 98.72 N ANISOU 2270 N ILE D 17 10262 19306 7942 3228 -1307 -1353 N ATOM 2271 CA ILE D 17 35.139 -5.975 -3.912 1.00 96.58 C ANISOU 2271 CA ILE D 17 9791 19003 7903 3048 -1158 -1770 C ATOM 2272 C ILE D 17 33.973 -5.161 -3.363 1.00 91.98 C ANISOU 2272 C ILE D 17 8843 18388 7718 3063 -1239 -2004 C ATOM 2273 O ILE D 17 34.155 -4.309 -2.495 1.00106.54 O ANISOU 2273 O ILE D 17 10686 20142 9651 3131 -1173 -1898 O ATOM 2274 CB ILE D 17 35.525 -7.060 -2.885 1.00 98.84 C ANISOU 2274 CB ILE D 17 10255 19152 8146 2836 -707 -1813 C ATOM 2275 CG1 ILE D 17 36.774 -7.814 -3.345 1.00 99.48 C ANISOU 2275 CG1 ILE D 17 10695 19250 7853 2861 -622 -1572 C ATOM 2276 CG2 ILE D 17 34.367 -8.022 -2.658 1.00 99.39 C ANISOU 2276 CG2 ILE D 17 10113 19187 8465 2614 -556 -2201 C ATOM 2277 CD1 ILE D 17 37.280 -8.823 -2.337 1.00 98.07 C ANISOU 2277 CD1 ILE D 17 10739 18906 7617 2676 -232 -1582 C ATOM 2278 N ASN D 18 32.776 -5.421 -3.877 1.00 93.24 N ANISOU 2278 N ASN D 18 8693 18606 8128 3017 -1405 -2328 N ATOM 2279 CA ASN D 18 31.578 -4.764 -3.377 1.00 97.86 C ANISOU 2279 CA ASN D 18 8862 19175 9145 3040 -1449 -2586 C ATOM 2280 C ASN D 18 31.000 -5.544 -2.202 1.00105.08 C ANISOU 2280 C ASN D 18 9626 20003 10295 2807 -961 -2807 C ATOM 2281 O ASN D 18 30.266 -6.514 -2.389 1.00102.94 O ANISOU 2281 O ASN D 18 9164 19738 10210 2610 -884 -3045 O ATOM 2282 CB ASN D 18 30.540 -4.619 -4.491 1.00103.80 C ANISOU 2282 CB ASN D 18 9306 20014 10118 3107 -1898 -2818 C ATOM 2283 CG ASN D 18 29.485 -3.581 -4.171 1.00108.19 C ANISOU 2283 CG ASN D 18 9436 20568 11103 3235 -2061 -3012 C ATOM 2284 OD1 ASN D 18 29.662 -2.756 -3.274 1.00113.42 O ANISOU 2284 OD1 ASN D 18 10101 21176 11817 3341 -1912 -2928 O ATOM 2285 ND2 ASN D 18 28.380 -3.612 -4.907 1.00106.10 N ANISOU 2285 ND2 ASN D 18 8814 20344 11155 3249 -2402 -3284 N ATOM 2286 N PHE D 19 31.337 -5.113 -0.989 1.00102.82 N ANISOU 2286 N PHE D 19 9452 19619 9996 2829 -647 -2713 N ATOM 2287 CA PHE D 19 30.990 -5.857 0.221 1.00104.09 C ANISOU 2287 CA PHE D 19 9590 19684 10275 2616 -120 -2854 C ATOM 2288 C PHE D 19 29.498 -5.847 0.545 1.00113.36 C ANISOU 2288 C PHE D 19 10239 20906 11925 2551 17 -3191 C ATOM 2289 O PHE D 19 29.057 -6.536 1.463 1.00113.44 O ANISOU 2289 O PHE D 19 10174 20859 12068 2348 485 -3311 O ATOM 2290 CB PHE D 19 31.772 -5.312 1.421 1.00 97.75 C ANISOU 2290 CB PHE D 19 9115 18738 9286 2702 132 -2660 C ATOM 2291 CG PHE D 19 33.231 -5.670 1.408 1.00 92.79 C ANISOU 2291 CG PHE D 19 8975 18021 8260 2677 138 -2339 C ATOM 2292 CD1 PHE D 19 33.637 -6.973 1.639 1.00 89.15 C ANISOU 2292 CD1 PHE D 19 8740 17491 7641 2444 430 -2331 C ATOM 2293 CD2 PHE D 19 34.196 -4.703 1.178 1.00 92.67 C ANISOU 2293 CD2 PHE D 19 9173 17975 8063 2885 -158 -2036 C ATOM 2294 CE1 PHE D 19 34.979 -7.309 1.632 1.00 85.75 C ANISOU 2294 CE1 PHE D 19 8724 16976 6883 2447 431 -2046 C ATOM 2295 CE2 PHE D 19 35.540 -5.033 1.171 1.00 84.51 C ANISOU 2295 CE2 PHE D 19 8522 16862 6726 2863 -141 -1724 C ATOM 2296 CZ PHE D 19 35.931 -6.337 1.399 1.00 83.68 C ANISOU 2296 CZ PHE D 19 8623 16701 6471 2658 157 -1740 C ATOM 2297 N SER D 20 28.724 -5.068 -0.200 1.00125.03 N ANISOU 2297 N SER D 20 11348 22484 13674 2723 -383 -3329 N ATOM 2298 CA SER D 20 27.286 -5.010 0.015 1.00136.04 C ANISOU 2298 CA SER D 20 12167 23933 15591 2687 -295 -3647 C ATOM 2299 C SER D 20 26.592 -6.179 -0.677 1.00145.54 C ANISOU 2299 C SER D 20 13106 25162 17031 2417 -367 -3833 C ATOM 2300 O SER D 20 25.555 -6.659 -0.217 1.00152.97 O ANISOU 2300 O SER D 20 13616 26108 18397 2236 -91 -4050 O ATOM 2301 CB SER D 20 26.720 -3.682 -0.488 1.00138.25 C ANISOU 2301 CB SER D 20 12148 24276 16103 2999 -748 -3734 C ATOM 2302 OG SER D 20 25.522 -3.347 0.190 1.00146.70 O ANISOU 2302 OG SER D 20 12710 25381 17650 3050 -519 -4000 O ATOM 2303 N SER D 21 27.179 -6.634 -1.780 1.00144.35 N ANISOU 2303 N SER D 21 13224 25016 16605 2397 -738 -3736 N ATOM 2304 CA SER D 21 26.600 -7.715 -2.570 1.00148.94 C ANISOU 2304 CA SER D 21 13645 25582 17365 2178 -928 -3915 C ATOM 2305 C SER D 21 26.722 -9.066 -1.869 1.00150.13 C ANISOU 2305 C SER D 21 13927 25629 17487 1834 -455 -3926 C ATOM 2306 O SER D 21 25.729 -9.629 -1.409 1.00151.25 O ANISOU 2306 O SER D 21 13662 25737 18068 1595 -220 -4117 O ATOM 2307 CB SER D 21 27.265 -7.782 -3.946 1.00150.19 C ANISOU 2307 CB SER D 21 14149 25767 17149 2313 -1450 -3806 C ATOM 2308 OG SER D 21 28.657 -8.017 -3.828 1.00148.48 O ANISOU 2308 OG SER D 21 14493 25532 16390 2348 -1272 -3516 O ATOM 2309 N LEU D 22 27.945 -9.582 -1.792 1.00149.85 N ANISOU 2309 N LEU D 22 14446 25535 16955 1807 -322 -3706 N ATOM 2310 CA LEU D 22 28.183 -10.903 -1.221 1.00149.29 C ANISOU 2310 CA LEU D 22 14586 25335 16802 1496 55 -3701 C ATOM 2311 C LEU D 22 29.047 -10.817 0.034 1.00140.66 C ANISOU 2311 C LEU D 22 13851 24166 15427 1485 549 -3495 C ATOM 2312 O LEU D 22 28.919 -11.636 0.945 1.00138.79 O ANISOU 2312 O LEU D 22 13674 23814 15245 1224 987 -3516 O ATOM 2313 CB LEU D 22 28.839 -11.817 -2.262 1.00149.29 C ANISOU 2313 CB LEU D 22 14960 25290 16476 1467 -252 -3665 C ATOM 2314 CG LEU D 22 28.907 -13.323 -1.990 1.00149.50 C ANISOU 2314 CG LEU D 22 15176 25151 16476 1142 -34 -3723 C ATOM 2315 CD1 LEU D 22 28.756 -14.094 -3.291 1.00150.62 C ANISOU 2315 CD1 LEU D 22 15407 25251 16568 1128 -522 -3863 C ATOM 2316 CD2 LEU D 22 30.210 -13.703 -1.301 1.00144.40 C ANISOU 2316 CD2 LEU D 22 15073 24419 15374 1140 306 -3483 C ATOM 2317 N THR D 28 33.256 -20.210 -2.833 1.00104.04 N ANISOU 2317 N THR D 28 12101 18488 8942 692 33 -3579 N ATOM 2318 CA THR D 28 32.996 -21.632 -2.685 1.00112.61 C ANISOU 2318 CA THR D 28 13375 19295 10115 394 4 -3731 C ATOM 2319 C THR D 28 34.165 -22.335 -1.999 1.00112.55 C ANISOU 2319 C THR D 28 13870 19125 9769 392 282 -3575 C ATOM 2320 O THR D 28 35.136 -21.700 -1.570 1.00112.94 O ANISOU 2320 O THR D 28 14078 19273 9561 599 508 -3345 O ATOM 2321 CB THR D 28 32.703 -22.290 -4.054 1.00114.38 C ANISOU 2321 CB THR D 28 13726 19464 10271 501 -544 -3959 C ATOM 2322 OG1 THR D 28 33.789 -22.040 -4.954 1.00105.95 O ANISOU 2322 OG1 THR D 28 13035 18544 8678 948 -710 -3864 O ATOM 2323 CG2 THR D 28 31.422 -21.710 -4.651 1.00118.64 C ANISOU 2323 CG2 THR D 28 13751 20097 11228 448 -871 -4136 C ATOM 2324 N GLN D 29 34.046 -23.652 -1.886 1.00114.77 N ANISOU 2324 N GLN D 29 14395 19128 10086 145 224 -3700 N ATOM 2325 CA GLN D 29 35.021 -24.473 -1.186 1.00112.20 C ANISOU 2325 CA GLN D 29 14549 18587 9497 96 447 -3587 C ATOM 2326 C GLN D 29 36.040 -25.005 -2.197 1.00116.55 C ANISOU 2326 C GLN D 29 15549 19132 9603 463 156 -3620 C ATOM 2327 O GLN D 29 37.019 -25.639 -1.804 1.00117.61 O ANISOU 2327 O GLN D 29 16100 19110 9477 525 282 -3529 O ATOM 2328 CB GLN D 29 34.294 -25.606 -0.432 1.00111.19 C ANISOU 2328 CB GLN D 29 14445 18133 9669 -395 556 -3686 C ATOM 2329 CG GLN D 29 35.111 -26.359 0.615 1.00108.57 C ANISOU 2329 CG GLN D 29 14570 17540 9141 -534 853 -3547 C ATOM 2330 CD GLN D 29 35.466 -25.503 1.811 1.00106.01 C ANISOU 2330 CD GLN D 29 14206 17293 8781 -543 1316 -3312 C ATOM 2331 OE1 GLN D 29 34.677 -24.666 2.249 1.00102.47 O ANISOU 2331 OE1 GLN D 29 13338 16993 8601 -654 1528 -3286 O ATOM 2332 NE2 GLN D 29 36.670 -25.695 2.336 1.00 99.23 N ANISOU 2332 NE2 GLN D 29 13796 16317 7592 -399 1448 -3149 N ATOM 2333 N ASN D 30 35.821 -24.715 -3.490 1.00103.83 N ANISOU 2333 N ASN D 30 13866 17692 7894 733 -225 -3746 N ATOM 2334 CA ASN D 30 36.682 -25.268 -4.540 1.00104.25 C ANISOU 2334 CA ASN D 30 14364 17748 7498 1113 -491 -3805 C ATOM 2335 C ASN D 30 37.947 -24.452 -4.591 1.00116.92 C ANISOU 2335 C ASN D 30 16084 19596 8743 1503 -268 -3524 C ATOM 2336 O ASN D 30 38.988 -24.955 -4.997 1.00102.92 O ANISOU 2336 O ASN D 30 14702 17807 6595 1799 -281 -3479 O ATOM 2337 CB ASN D 30 36.105 -25.211 -5.953 1.00110.26 C ANISOU 2337 CB ASN D 30 15098 18605 8191 1323 -978 -4019 C ATOM 2338 CG ASN D 30 36.831 -26.169 -6.909 1.00109.18 C ANISOU 2338 CG ASN D 30 15518 18365 7598 1654 -1252 -4152 C ATOM 2339 OD1 ASN D 30 38.021 -26.426 -6.804 1.00116.40 O ANISOU 2339 OD1 ASN D 30 16773 19297 8157 1907 -1047 -4014 O ATOM 2340 ND2 ASN D 30 36.175 -26.470 -7.969 1.00125.14 N ANISOU 2340 ND2 ASN D 30 17614 20337 9596 1745 -1726 -4401 N ATOM 2341 N ILE D 31 37.871 -23.187 -4.191 1.00105.72 N ANISOU 2341 N ILE D 31 8130 21861 10178 1806 -737 -5652 N ATOM 2342 CA ILE D 31 39.000 -22.296 -4.440 1.00101.53 C ANISOU 2342 CA ILE D 31 8055 20984 9538 2218 -840 -4946 C ATOM 2343 C ILE D 31 40.271 -22.870 -3.789 1.00 83.38 C ANISOU 2343 C ILE D 31 5991 18487 7203 1791 -527 -4447 C ATOM 2344 O ILE D 31 41.409 -22.554 -4.169 1.00 84.52 O ANISOU 2344 O ILE D 31 6578 18218 7318 1986 -540 -3999 O ATOM 2345 CB ILE D 31 38.721 -20.884 -3.936 1.00101.30 C ANISOU 2345 CB ILE D 31 8146 20990 9352 2541 -908 -4735 C ATOM 2346 CG1 ILE D 31 39.753 -19.894 -4.493 1.00102.92 C ANISOU 2346 CG1 ILE D 31 8981 20640 9484 2992 -931 -4209 C ATOM 2347 CG2 ILE D 31 38.648 -20.888 -2.432 1.00103.58 C ANISOU 2347 CG2 ILE D 31 8375 21438 9542 2022 -600 -4601 C ATOM 2348 CD1 ILE D 31 39.632 -18.559 -3.887 1.00109.64 C ANISOU 2348 CD1 ILE D 31 10114 21349 10196 3143 -855 -3997 C ATOM 2349 N ASP D 32 40.035 -23.787 -2.856 1.00 92.22 N ANISOU 2349 N ASP D 32 6896 19710 8434 1217 -114 -4467 N ATOM 2350 CA ASP D 32 41.055 -24.653 -2.285 1.00 95.40 C ANISOU 2350 CA ASP D 32 7442 19899 8907 833 269 -3950 C ATOM 2351 C ASP D 32 41.837 -25.444 -3.334 1.00 75.55 C ANISOU 2351 C ASP D 32 4976 17145 6583 866 209 -3887 C ATOM 2352 O ASP D 32 42.967 -25.850 -3.078 1.00 72.85 O ANISOU 2352 O ASP D 32 4991 16464 6224 689 311 -3316 O ATOM 2353 CB ASP D 32 40.407 -25.636 -1.311 1.00103.70 C ANISOU 2353 CB ASP D 32 8189 20937 10276 296 814 -3924 C ATOM 2354 CG ASP D 32 39.597 -24.948 -0.243 1.00110.09 C ANISOU 2354 CG ASP D 32 8953 21954 10921 263 943 -3983 C ATOM 2355 OD1 ASP D 32 39.493 -23.705 -0.283 1.00127.01 O ANISOU 2355 OD1 ASP D 32 11244 24274 12739 626 562 -4068 O ATOM 2356 OD2 ASP D 32 39.046 -25.651 0.629 1.00116.26 O ANISOU 2356 OD2 ASP D 32 9580 22648 11946 -114 1484 -3919 O ATOM 2357 N SER D 33 41.239 -25.673 -4.504 1.00 77.40 N ANISOU 2357 N SER D 33 5002 17392 7015 1083 -72 -4415 N ATOM 2358 CA SER D 33 41.898 -26.460 -5.552 1.00 76.02 C ANISOU 2358 CA SER D 33 4863 16958 7062 1130 -161 -4391 C ATOM 2359 C SER D 33 43.153 -25.787 -6.076 1.00 71.11 C ANISOU 2359 C SER D 33 4920 15987 6111 1515 -384 -3918 C ATOM 2360 O SER D 33 43.956 -26.418 -6.760 1.00 69.23 O ANISOU 2360 O SER D 33 4913 15351 6039 1473 -422 -3677 O ATOM 2361 CB SER D 33 40.957 -26.726 -6.725 1.00 85.01 C ANISOU 2361 CB SER D 33 5772 18172 8354 1387 -482 -5133 C ATOM 2362 OG SER D 33 39.822 -27.468 -6.317 1.00 85.50 O ANISOU 2362 OG SER D 33 5328 18296 8861 912 -227 -5615 O ATOM 2363 N TRP D 34 43.311 -24.506 -5.764 1.00 73.98 N ANISOU 2363 N TRP D 34 5596 16357 6154 1842 -482 -3754 N ATOM 2364 CA TRP D 34 44.507 -23.768 -6.143 1.00 73.46 C ANISOU 2364 CA TRP D 34 6138 15741 6034 2103 -525 -3281 C ATOM 2365 C TRP D 34 45.760 -24.453 -5.607 1.00 70.38 C ANISOU 2365 C TRP D 34 5934 15193 5613 1686 -332 -2872 C ATOM 2366 O TRP D 34 46.807 -24.451 -6.259 1.00 61.90 O ANISOU 2366 O TRP D 34 5235 13670 4613 1807 -353 -2624 O ATOM 2367 CB TRP D 34 44.424 -22.329 -5.635 1.00 65.72 C ANISOU 2367 CB TRP D 34 5376 14619 4974 2315 -516 -3130 C ATOM 2368 CG TRP D 34 45.633 -21.502 -5.941 1.00 71.99 C ANISOU 2368 CG TRP D 34 6747 14833 5773 2488 -421 -2801 C ATOM 2369 CD1 TRP D 34 45.929 -20.885 -7.124 1.00 66.17 C ANISOU 2369 CD1 TRP D 34 6481 13609 5052 2965 -443 -2727 C ATOM 2370 CD2 TRP D 34 46.705 -21.187 -5.045 1.00 61.27 C ANISOU 2370 CD2 TRP D 34 5541 13335 4405 2187 -239 -2577 C ATOM 2371 NE1 TRP D 34 47.123 -20.213 -7.020 1.00 68.35 N ANISOU 2371 NE1 TRP D 34 7196 13394 5381 2906 -182 -2500 N ATOM 2372 CE2 TRP D 34 47.618 -20.381 -5.753 1.00 70.20 C ANISOU 2372 CE2 TRP D 34 7177 13879 5618 2440 -98 -2471 C ATOM 2373 CE3 TRP D 34 46.983 -21.512 -3.713 1.00 68.63 C ANISOU 2373 CE3 TRP D 34 6232 14592 5251 1769 -170 -2483 C ATOM 2374 CZ2 TRP D 34 48.789 -19.895 -5.174 1.00 62.25 C ANISOU 2374 CZ2 TRP D 34 6316 12653 4684 2236 112 -2418 C ATOM 2375 CZ3 TRP D 34 48.147 -21.029 -3.139 1.00 60.38 C ANISOU 2375 CZ3 TRP D 34 5349 13382 4212 1651 -79 -2383 C ATOM 2376 CH2 TRP D 34 49.035 -20.229 -3.868 1.00 74.96 C ANISOU 2376 CH2 TRP D 34 7572 14701 6206 1856 57 -2424 C ATOM 2377 N PHE D 35 45.647 -25.052 -4.425 1.00 64.32 N ANISOU 2377 N PHE D 35 4926 14598 4917 1207 -134 -2666 N ATOM 2378 CA PHE D 35 46.781 -25.738 -3.813 1.00 64.94 C ANISOU 2378 CA PHE D 35 5180 14412 5081 885 0 -2132 C ATOM 2379 C PHE D 35 47.176 -26.987 -4.602 1.00 62.48 C ANISOU 2379 C PHE D 35 4887 13728 5122 709 45 -1955 C ATOM 2380 O PHE D 35 48.353 -27.204 -4.880 1.00 60.11 O ANISOU 2380 O PHE D 35 4874 13066 4898 713 3 -1616 O ATOM 2381 CB PHE D 35 46.467 -26.103 -2.360 1.00 65.54 C ANISOU 2381 CB PHE D 35 5097 14778 5026 588 260 -1933 C ATOM 2382 CG PHE D 35 46.298 -24.907 -1.465 1.00 67.19 C ANISOU 2382 CG PHE D 35 5331 15336 4863 745 210 -2055 C ATOM 2383 CD1 PHE D 35 47.402 -24.277 -0.914 1.00 64.58 C ANISOU 2383 CD1 PHE D 35 5233 14979 4323 840 100 -1885 C ATOM 2384 CD2 PHE D 35 45.039 -24.400 -1.195 1.00 68.16 C ANISOU 2384 CD2 PHE D 35 5192 15822 4884 798 275 -2426 C ATOM 2385 CE1 PHE D 35 47.251 -23.170 -0.107 1.00 65.42 C ANISOU 2385 CE1 PHE D 35 5335 15214 4306 942 46 -2012 C ATOM 2386 CE2 PHE D 35 44.883 -23.293 -0.387 1.00 68.58 C ANISOU 2386 CE2 PHE D 35 5310 15971 4776 910 192 -2450 C ATOM 2387 CZ PHE D 35 45.991 -22.678 0.157 1.00 67.18 C ANISOU 2387 CZ PHE D 35 5381 15621 4525 969 94 -2231 C ATOM 2388 N GLU D 36 46.191 -27.807 -4.950 1.00 65.27 N ANISOU 2388 N GLU D 36 4888 14168 5742 535 161 -2253 N ATOM 2389 CA GLU D 36 46.437 -28.998 -5.756 1.00 75.80 C ANISOU 2389 CA GLU D 36 6190 15150 7459 348 240 -2197 C ATOM 2390 C GLU D 36 47.028 -28.618 -7.108 1.00 62.73 C ANISOU 2390 C GLU D 36 4833 13228 5774 761 -95 -2284 C ATOM 2391 O GLU D 36 47.980 -29.248 -7.573 1.00 69.12 O ANISOU 2391 O GLU D 36 5893 13611 6758 679 -64 -1938 O ATOM 2392 CB GLU D 36 45.148 -29.800 -5.952 1.00 73.07 C ANISOU 2392 CB GLU D 36 5296 14976 7490 89 447 -2740 C ATOM 2393 CG GLU D 36 44.714 -30.606 -4.733 1.00 97.82 C ANISOU 2393 CG GLU D 36 8232 18110 10825 -407 1044 -2544 C ATOM 2394 CD GLU D 36 44.184 -29.740 -3.603 1.00104.91 C ANISOU 2394 CD GLU D 36 9076 19405 11380 -344 1122 -2553 C ATOM 2395 OE1 GLU D 36 43.870 -28.556 -3.849 1.00105.52 O ANISOU 2395 OE1 GLU D 36 9122 19810 11162 28 721 -2877 O ATOM 2396 OE2 GLU D 36 44.084 -30.246 -2.465 1.00107.95 O ANISOU 2396 OE2 GLU D 36 9508 19747 11760 -614 1635 -2213 O HETATM 2397 C MK8 D 37 48.359 -26.681 -8.906 1.00 65.00 C ANISOU 2397 C MK8 D 37 6059 12987 5652 1829 -460 -2255 C HETATM 2398 N MK8 D 37 46.458 -27.577 -7.716 1.00 66.38 N ANISOU 2398 N MK8 D 37 5321 13922 5978 1270 -361 -2719 N HETATM 2399 O MK8 D 37 49.167 -27.061 -9.795 1.00 64.74 O ANISOU 2399 O MK8 D 37 6340 12491 5769 1940 -457 -2061 O HETATM 2400 CA MK8 D 37 46.897 -27.070 -8.977 1.00 74.43 C ANISOU 2400 CA MK8 D 37 6739 14681 6859 1828 -580 -2799 C HETATM 2401 CB MK8 D 37 46.113 -25.816 -9.305 1.00 76.27 C ANISOU 2401 CB MK8 D 37 7043 15252 6686 2473 -760 -3231 C HETATM 2402 CD MK8 D 37 47.020 -23.954 -10.681 1.00 69.06 C ANISOU 2402 CD MK8 D 37 7185 13439 5616 3442 -763 -2796 C HETATM 2403 CE MK8 D 37 47.442 -23.544 -12.076 1.00 65.86 C ANISOU 2403 CE MK8 D 37 7393 12466 5165 4020 -791 -2601 C HETATM 2404 CG MK8 D 37 46.452 -25.358 -10.709 1.00 72.78 C ANISOU 2404 CG MK8 D 37 7099 14371 6184 3140 -909 -3184 C HETATM 2405 CB1 MK8 D 37 46.667 -28.091 -10.072 1.00 63.16 C ANISOU 2405 CB1 MK8 D 37 5171 13141 5687 1867 -698 -3068 C ATOM 2406 N LYS D 38 48.715 -25.932 -7.865 1.00 62.64 N ANISOU 2406 N LYS D 38 5808 12780 5210 1708 -350 -2079 N ATOM 2407 CA LYS D 38 50.078 -25.446 -7.682 1.00 56.52 C ANISOU 2407 CA LYS D 38 5376 11602 4498 1687 -228 -1755 C ATOM 2408 C LYS D 38 51.077 -26.581 -7.488 1.00 53.38 C ANISOU 2408 C LYS D 38 4963 10931 4388 1295 -178 -1336 C ATOM 2409 O LYS D 38 52.218 -26.496 -7.941 1.00 57.30 O ANISOU 2409 O LYS D 38 5736 10967 5067 1351 -111 -1151 O ATOM 2410 CB LYS D 38 50.145 -24.492 -6.485 1.00 62.84 C ANISOU 2410 CB LYS D 38 6092 12679 5105 1607 -160 -1806 C ATOM 2411 CG LYS D 38 49.845 -23.041 -6.824 1.00 71.52 C ANISOU 2411 CG LYS D 38 7447 13736 5991 2072 -64 -2110 C ATOM 2412 CD LYS D 38 50.997 -22.410 -7.590 1.00 79.20 C ANISOU 2412 CD LYS D 38 8892 14045 7157 2311 189 -2041 C ATOM 2413 CE LYS D 38 50.730 -20.945 -7.887 1.00 93.83 C ANISOU 2413 CE LYS D 38 11109 15526 9018 2653 392 -2141 C ATOM 2414 NZ LYS D 38 51.905 -20.279 -8.513 1.00103.67 N ANISOU 2414 NZ LYS D 38 12831 15994 10566 2764 827 -2075 N ATOM 2415 N ALA D 39 50.650 -27.637 -6.801 1.00 54.82 N ANISOU 2415 N ALA D 39 4845 11359 4626 928 -133 -1190 N ATOM 2416 CA ALA D 39 51.518 -28.785 -6.565 1.00 54.48 C ANISOU 2416 CA ALA D 39 4839 11071 4790 641 -25 -747 C ATOM 2417 C ALA D 39 51.862 -29.478 -7.882 1.00 53.17 C ANISOU 2417 C ALA D 39 4847 10437 4918 689 -34 -694 C ATOM 2418 O ALA D 39 52.994 -29.908 -8.091 1.00 52.36 O ANISOU 2418 O ALA D 39 4941 9959 4993 634 6 -361 O ATOM 2419 CB ALA D 39 50.862 -29.762 -5.606 1.00 57.45 C ANISOU 2419 CB ALA D 39 4965 11713 5149 319 201 -587 C ATOM 2420 N ASN D 40 50.879 -29.579 -8.769 1.00 55.25 N ANISOU 2420 N ASN D 40 5010 10766 5217 838 -113 -1080 N ATOM 2421 CA ASN D 40 51.100 -30.216 -10.062 1.00 60.92 C ANISOU 2421 CA ASN D 40 5891 11105 6153 959 -160 -1121 C ATOM 2422 C ASN D 40 51.953 -29.353 -10.990 1.00 51.48 C ANISOU 2422 C ASN D 40 5193 9492 4876 1423 -217 -1065 C ATOM 2423 O ASN D 40 52.939 -29.831 -11.551 1.00 57.86 O ANISOU 2423 O ASN D 40 6264 9813 5907 1392 -133 -769 O ATOM 2424 CB ASN D 40 49.765 -30.546 -10.725 1.00 63.25 C ANISOU 2424 CB ASN D 40 5857 11697 6477 1071 -286 -1712 C ATOM 2425 CG ASN D 40 49.006 -31.637 -9.996 1.00 76.87 C ANISOU 2425 CG ASN D 40 7089 13626 8494 520 -33 -1810 C ATOM 2426 OD1 ASN D 40 49.598 -32.461 -9.297 1.00 76.55 O ANISOU 2426 OD1 ASN D 40 7093 13356 8635 115 277 -1319 O ATOM 2427 ND2 ASN D 40 47.688 -31.651 -10.157 1.00 72.21 N ANISOU 2427 ND2 ASN D 40 6032 13447 7959 549 -104 -2477 N HETATM 2428 C MK8 D 41 53.750 -27.104 -11.600 1.00 58.34 C ANISOU 2428 C MK8 D 41 6933 9546 5686 2074 102 -921 C HETATM 2429 N MK8 D 41 51.568 -28.085 -11.134 1.00 51.92 N ANISOU 2429 N MK8 D 41 5407 9686 4632 1866 -270 -1339 N HETATM 2430 O MK8 D 41 54.610 -27.170 -12.516 1.00 60.52 O ANISOU 2430 O MK8 D 41 7609 9224 6161 2259 284 -760 O HETATM 2431 CA MK8 D 41 52.272 -27.136 -11.938 1.00 57.02 C ANISOU 2431 CA MK8 D 41 6601 9863 5203 2357 -132 -1299 C HETATM 2432 CB MK8 D 41 51.739 -25.750 -11.637 1.00 58.73 C ANISOU 2432 CB MK8 D 41 6923 10303 5089 2733 -71 -1563 C HETATM 2433 CD MK8 D 41 49.806 -24.243 -11.698 1.00 67.43 C ANISOU 2433 CD MK8 D 41 7987 12029 5603 3468 -265 -2135 C HETATM 2434 CE MK8 D 41 48.676 -23.708 -12.550 1.00 59.98 C ANISOU 2434 CE MK8 D 41 7124 11152 4512 4000 -544 -2289 C HETATM 2435 CG MK8 D 41 50.431 -25.461 -12.344 1.00 59.23 C ANISOU 2435 CG MK8 D 41 6988 10751 4766 3328 -290 -2007 C HETATM 2436 CB1 MK8 D 41 52.089 -27.447 -13.410 1.00 60.86 C ANISOU 2436 CB1 MK8 D 41 7418 10091 5615 2864 -207 -1436 C ATOM 2437 N GLU D 42 54.067 -27.008 -10.313 1.00 63.25 N ANISOU 2437 N GLU D 42 7241 10437 6354 1679 100 -830 N ATOM 2438 CA GLU D 42 55.453 -26.868 -9.873 1.00 55.20 C ANISOU 2438 CA GLU D 42 6245 9105 5624 1471 248 -649 C ATOM 2439 C GLU D 42 56.147 -28.213 -9.673 1.00 49.88 C ANISOU 2439 C GLU D 42 5423 8354 5174 1134 171 -275 C ATOM 2440 O GLU D 42 57.330 -28.256 -9.326 1.00 57.94 O ANISOU 2440 O GLU D 42 6395 9184 6436 1007 226 -161 O ATOM 2441 CB GLU D 42 55.518 -26.053 -8.578 1.00 52.58 C ANISOU 2441 CB GLU D 42 5633 9176 5168 1332 227 -836 C ATOM 2442 CG GLU D 42 54.890 -24.672 -8.684 1.00 61.83 C ANISOU 2442 CG GLU D 42 6970 10384 6139 1652 381 -1192 C ATOM 2443 CD GLU D 42 55.027 -23.861 -7.408 1.00 69.69 C ANISOU 2443 CD GLU D 42 7675 11752 7053 1486 379 -1432 C ATOM 2444 OE1 GLU D 42 55.860 -24.225 -6.553 1.00 73.10 O ANISOU 2444 OE1 GLU D 42 7816 12348 7612 1209 261 -1385 O ATOM 2445 OE2 GLU D 42 54.302 -22.856 -7.261 1.00 73.74 O ANISOU 2445 OE2 GLU D 42 8254 12425 7340 1693 480 -1698 O ATOM 2446 N ASN D 43 55.409 -29.299 -9.895 1.00 52.88 N ANISOU 2446 N ASN D 43 5707 8880 5507 1012 81 -148 N ATOM 2447 CA ASN D 43 55.938 -30.657 -9.761 1.00 67.67 C ANISOU 2447 CA ASN D 43 7510 10621 7580 727 115 240 C ATOM 2448 C ASN D 43 56.461 -30.927 -8.351 1.00 76.89 C ANISOU 2448 C ASN D 43 8451 12126 8636 542 93 475 C ATOM 2449 O ASN D 43 57.642 -31.210 -8.156 1.00 70.33 O ANISOU 2449 O ASN D 43 7646 11117 7959 531 91 692 O ATOM 2450 CB ASN D 43 57.045 -30.910 -10.796 1.00 68.61 C ANISOU 2450 CB ASN D 43 7943 10098 8028 819 219 419 C ATOM 2451 CG ASN D 43 57.466 -32.368 -10.863 1.00 64.83 C ANISOU 2451 CG ASN D 43 7444 9436 7752 574 284 817 C ATOM 2452 OD1 ASN D 43 56.644 -33.273 -10.712 1.00 74.09 O ANISOU 2452 OD1 ASN D 43 8471 10794 8887 381 331 871 O ATOM 2453 ND2 ASN D 43 58.757 -32.602 -11.070 1.00 55.85 N ANISOU 2453 ND2 ASN D 43 6438 7901 6882 571 356 1061 N TER 2454 ASN D 43 HETATM 2455 PB ADP A 501 52.911 -10.013 11.891 1.00163.92 P HETATM 2456 O1B ADP A 501 52.391 -10.824 10.730 1.00169.80 O HETATM 2457 O2B ADP A 501 53.850 -8.904 11.481 1.00165.38 O HETATM 2458 O3B ADP A 501 53.369 -10.828 13.077 1.00156.95 O HETATM 2459 PA ADP A 501 50.257 -9.985 12.875 1.00 78.32 P HETATM 2460 O1A ADP A 501 49.181 -9.730 11.846 1.00 74.18 O HETATM 2461 O2A ADP A 501 50.540 -11.394 13.333 1.00 84.03 O HETATM 2462 O3A ADP A 501 51.619 -9.234 12.451 1.00 62.39 O HETATM 2463 O5' ADP A 501 49.910 -9.149 14.201 1.00 93.80 O HETATM 2464 C5' ADP A 501 48.979 -8.082 14.137 1.00 85.32 C HETATM 2465 C4' ADP A 501 48.337 -7.881 15.495 1.00 80.05 C HETATM 2466 O4' ADP A 501 47.182 -7.066 15.294 1.00 73.59 O HETATM 2467 C3' ADP A 501 47.862 -9.199 16.084 1.00 83.67 C HETATM 2468 O3' ADP A 501 48.724 -9.645 17.136 1.00 88.88 O HETATM 2469 C2' ADP A 501 46.475 -8.895 16.604 1.00 84.18 C HETATM 2470 O2' ADP A 501 46.568 -8.501 17.975 1.00 81.25 O HETATM 2471 C1' ADP A 501 46.006 -7.703 15.793 1.00 77.25 C HETATM 2472 N9 ADP A 501 45.203 -8.177 14.636 1.00 68.46 N HETATM 2473 C8 ADP A 501 45.706 -8.681 13.490 1.00 70.38 C HETATM 2474 N7 ADP A 501 44.724 -9.027 12.622 1.00 66.74 N HETATM 2475 C5 ADP A 501 43.552 -8.740 13.214 1.00 65.12 C HETATM 2476 C6 ADP A 501 42.124 -8.860 12.844 1.00 66.97 C HETATM 2477 N6 ADP A 501 41.758 -9.366 11.640 1.00 63.84 N HETATM 2478 N1 ADP A 501 41.204 -8.449 13.745 1.00 57.19 N HETATM 2479 C2 ADP A 501 41.568 -7.946 14.940 1.00 62.20 C HETATM 2480 N3 ADP A 501 42.846 -7.810 15.340 1.00 50.79 N HETATM 2481 C4 ADP A 501 43.870 -8.183 14.539 1.00 64.89 C HETATM 2482 O1 PG4 A 502 35.479 -13.033 28.419 1.00106.86 O HETATM 2483 C1 PG4 A 502 34.691 -13.244 29.586 1.00106.90 C HETATM 2484 C2 PG4 A 502 34.939 -12.110 30.585 1.00106.14 C HETATM 2485 O2 PG4 A 502 34.998 -10.881 29.907 1.00105.15 O HETATM 2486 C3 PG4 A 502 34.738 -9.762 30.737 1.00107.53 C HETATM 2487 C4 PG4 A 502 35.521 -8.522 30.226 1.00111.53 C HETATM 2488 O3 PG4 A 502 34.970 -8.072 28.967 1.00111.29 O HETATM 2489 C5 PG4 A 502 35.798 -8.385 27.809 1.00108.30 C HETATM 2490 C6 PG4 A 502 34.913 -8.573 26.578 1.00105.36 C HETATM 2491 O4 PG4 A 502 35.696 -8.437 25.407 1.00 98.75 O HETATM 2492 C7 PG4 A 502 36.531 -9.556 25.129 1.00 97.95 C HETATM 2493 C8 PG4 A 502 35.669 -10.764 24.792 1.00 96.15 C HETATM 2494 O5 PG4 A 502 36.508 -11.956 24.694 1.00 93.91 O HETATM 2495 S SO4 A 503 64.800 -38.541 18.578 1.00145.36 S HETATM 2496 O1 SO4 A 503 65.020 -37.997 17.240 1.00145.76 O HETATM 2497 O2 SO4 A 503 64.450 -39.955 18.477 1.00146.12 O HETATM 2498 O3 SO4 A 503 66.019 -38.396 19.369 1.00143.47 O HETATM 2499 O4 SO4 A 503 63.709 -37.818 19.223 1.00142.69 O HETATM 2500 C1 PEG A 504 44.489 -35.048 10.072 1.00 59.87 C HETATM 2501 O1 PEG A 504 44.590 -36.161 10.933 1.00 61.99 O HETATM 2502 C2 PEG A 504 45.823 -34.251 10.108 1.00 67.55 C HETATM 2503 O2 PEG A 504 46.919 -35.182 10.130 1.00 85.97 O HETATM 2504 C3 PEG A 504 47.861 -34.941 11.149 1.00 74.76 C HETATM 2505 C4 PEG A 504 49.119 -34.365 10.556 1.00 73.03 C HETATM 2506 O4 PEG A 504 48.841 -33.082 10.043 1.00 66.17 O HETATM 2507 C1 PEG A 505 58.183 -13.180 7.917 1.00 91.34 C HETATM 2508 O1 PEG A 505 58.629 -13.418 9.235 1.00 91.78 O HETATM 2509 C2 PEG A 505 57.323 -11.884 7.885 1.00 95.04 C HETATM 2510 O2 PEG A 505 56.420 -11.932 6.766 1.00 98.75 O HETATM 2511 C3 PEG A 505 55.441 -10.916 6.766 1.00101.60 C HETATM 2512 C4 PEG A 505 54.582 -11.035 7.999 1.00105.50 C HETATM 2513 O4 PEG A 505 54.915 -10.017 8.916 1.00110.00 O HETATM 2514 O1 MES A 506 53.873 -26.991 -4.591 1.00 80.97 O HETATM 2515 C2 MES A 506 53.431 -25.681 -4.866 1.00 83.98 C HETATM 2516 C3 MES A 506 54.093 -24.650 -3.978 1.00 86.33 C HETATM 2517 N4 MES A 506 55.299 -25.055 -3.331 1.00 79.67 N HETATM 2518 C5 MES A 506 56.047 -26.110 -3.934 1.00 85.25 C HETATM 2519 C6 MES A 506 55.267 -27.101 -4.772 1.00 82.55 C HETATM 2520 C7 MES A 506 56.161 -23.906 -3.267 1.00 82.64 C HETATM 2521 C8 MES A 506 56.978 -23.944 -1.995 1.00 89.12 C HETATM 2522 S MES A 506 58.144 -22.608 -1.998 1.00112.13 S HETATM 2523 O1S MES A 506 59.386 -22.962 -2.781 1.00109.26 O HETATM 2524 O2S MES A 506 57.500 -21.348 -2.527 1.00 96.44 O HETATM 2525 O3S MES A 506 58.720 -22.388 -0.620 1.00125.44 O HETATM 2526 C8 P4G A 507 68.367 -16.613 17.806 1.00 96.43 C HETATM 2527 C7 P4G A 507 67.029 -15.924 17.549 1.00105.09 C HETATM 2528 O4 P4G A 507 65.987 -16.701 18.082 1.00107.41 O HETATM 2529 C6 P4G A 507 64.761 -15.999 18.219 1.00104.82 C HETATM 2530 C5 P4G A 507 63.617 -16.877 17.768 1.00103.69 C HETATM 2531 O3 P4G A 507 63.557 -16.906 16.379 1.00101.55 O HETATM 2532 C4 P4G A 507 62.250 -16.967 15.872 1.00100.38 C HETATM 2533 C3 P4G A 507 62.278 -16.901 14.365 1.00 89.94 C HETATM 2534 O2 P4G A 507 63.328 -15.999 13.938 1.00 91.82 O HETATM 2535 C2 P4G A 507 63.534 -15.963 12.502 1.00 84.92 C HETATM 2536 C1 P4G A 507 64.560 -14.851 12.153 1.00 69.83 C HETATM 2537 CL CL A 508 70.770 -25.854 22.115 1.00116.71 CL HETATM 2538 MG MG A 509 52.081 -12.166 14.339 1.00143.25 MG HETATM 2539 MG MG A 510 53.867 -12.477 10.135 1.00144.32 MG HETATM 2540 N NH3 D 101 55.571 -30.830 -7.368 1.00 49.41 N HETATM 2541 O HOH A 601 59.675 -39.060 21.099 1.00 51.67 O HETATM 2542 O HOH A 602 39.767 -10.562 25.927 1.00 60.98 O HETATM 2543 O HOH A 603 44.389 -33.101 7.431 1.00 74.15 O HETATM 2544 O HOH A 604 36.056 -17.292 23.201 1.00 56.54 O HETATM 2545 O HOH A 605 37.119 -16.590 8.569 1.00 56.09 O HETATM 2546 O HOH A 606 48.341 -13.316 7.601 1.00 51.32 O HETATM 2547 O HOH A 607 43.990 -24.233 34.038 1.00 53.78 O HETATM 2548 O HOH A 608 39.466 -33.242 33.608 1.00 82.04 O HETATM 2549 O HOH A 609 40.826 -10.871 23.274 1.00 50.58 O HETATM 2550 O HOH A 610 57.086 -28.597 -1.967 1.00 51.43 O HETATM 2551 O HOH A 611 33.988 -23.044 15.757 1.00 70.07 O HETATM 2552 O HOH A 612 56.028 -19.313 -3.002 1.00 68.12 O HETATM 2553 O HOH A 613 35.812 -7.851 8.219 1.00 56.97 O HETATM 2554 O HOH A 614 64.193 -26.986 10.345 1.00 51.78 O HETATM 2555 O HOH A 615 31.007 -14.541 13.709 1.00 85.36 O HETATM 2556 O HOH A 616 63.691 -25.347 3.393 1.00 64.52 O HETATM 2557 O HOH A 617 56.961 -23.103 14.589 1.00 57.43 O HETATM 2558 O HOH A 618 55.301 -13.503 20.548 1.00 64.92 O HETATM 2559 O HOH A 619 58.906 -31.911 11.723 1.00 45.19 O HETATM 2560 O HOH A 620 58.491 -16.805 22.621 1.00 57.59 O HETATM 2561 O HOH A 621 35.738 -26.025 14.732 1.00 71.58 O HETATM 2562 O HOH A 622 61.478 -18.395 26.965 1.00 65.49 O HETATM 2563 O HOH A 623 52.461 -18.508 9.676 1.00 48.93 O HETATM 2564 O HOH A 624 55.799 -14.378 14.573 1.00 71.57 O HETATM 2565 O HOH A 625 35.676 -12.459 12.411 1.00 51.23 O HETATM 2566 O HOH A 626 60.933 -24.768 -1.526 1.00 78.40 O HETATM 2567 O HOH A 627 54.821 -22.204 -0.258 1.00 54.33 O HETATM 2568 O HOH A 628 43.810 -29.776 33.368 1.00 55.86 O HETATM 2569 O HOH A 629 64.028 -33.512 17.026 1.00 56.71 O HETATM 2570 O HOH A 630 50.760 -29.862 5.693 1.00 67.96 O HETATM 2571 O HOH A 631 54.180 -14.691 11.212 1.00 70.72 O HETATM 2572 O HOH A 632 63.820 -22.129 35.889 1.00 85.90 O HETATM 2573 O HOH A 633 60.848 -15.470 18.903 1.00 72.10 O HETATM 2574 O HOH A 634 35.115 -20.912 20.837 1.00 64.65 O HETATM 2575 O HOH A 635 58.648 -24.837 22.053 1.00 43.25 O HETATM 2576 O HOH A 636 58.906 -13.205 -4.587 1.00 69.77 O HETATM 2577 O HOH A 637 46.073 -12.849 9.139 1.00 42.88 O HETATM 2578 O HOH A 638 32.958 -12.524 13.436 1.00 59.79 O HETATM 2579 O HOH A 639 48.346 -35.107 7.137 1.00 79.44 O HETATM 2580 O HOH A 640 54.727 -19.978 17.188 1.00 48.40 O HETATM 2581 O HOH A 641 56.978 -21.324 16.811 1.00 50.02 O HETATM 2582 O HOH A 642 38.355 -20.352 31.149 1.00 66.37 O HETATM 2583 O HOH A 643 47.827 -12.010 14.077 1.00 77.55 O HETATM 2584 O HOH A 644 70.587 -30.711 25.970 1.00 63.80 O HETATM 2585 O HOH A 645 58.186 -22.252 26.129 1.00 53.31 O HETATM 2586 O HOH A 646 54.882 -11.771 16.211 1.00 89.51 O HETATM 2587 O HOH A 647 39.062 -19.000 5.624 1.00 57.97 O HETATM 2588 O HOH A 648 43.113 -4.382 19.739 1.00 65.71 O HETATM 2589 O HOH A 649 69.117 -32.444 23.977 1.00 65.12 O HETATM 2590 O HOH A 650 53.915 -19.180 -5.774 1.00 61.54 O HETATM 2591 O HOH A 651 53.761 -13.203 14.891 1.00 69.05 O HETATM 2592 O HOH A 652 46.481 -11.071 11.336 1.00 54.67 O HETATM 2593 O HOH A 653 53.269 -30.556 4.484 1.00 59.15 O HETATM 2594 O HOH A 654 51.354 -11.226 16.220 1.00 65.40 O HETATM 2595 O HOH A 655 53.130 -23.826 14.502 1.00 58.34 O HETATM 2596 O HOH A 656 35.811 -26.721 32.690 1.00 64.66 O HETATM 2597 O HOH A 657 60.238 -37.297 23.825 1.00 53.33 O HETATM 2598 O HOH A 658 53.380 -15.930 24.156 1.00 72.27 O HETATM 2599 O HOH A 659 65.472 -24.960 11.136 1.00 68.16 O HETATM 2600 O HOH A 660 63.718 -14.735 26.884 1.00 89.35 O HETATM 2601 O HOH A 661 56.731 -42.634 21.865 1.00 83.75 O HETATM 2602 O HOH A 662 47.481 -8.862 -8.075 1.00 68.98 O HETATM 2603 O HOH A 663 65.540 -35.378 24.163 1.00 89.44 O HETATM 2604 O HOH A 664 43.764 -7.981 21.155 1.00 70.88 O HETATM 2605 O HOH A 665 48.481 -29.499 -2.150 1.00 66.26 O HETATM 2606 O HOH A 666 44.810 -8.934 34.296 1.00 79.98 O HETATM 2607 O HOH A 667 27.872 4.407 -1.994 1.00 95.26 O HETATM 2608 O HOH A 668 53.315 -40.450 26.494 1.00 80.37 O HETATM 2609 O HOH A 669 40.579 -34.523 6.694 1.00 80.56 O HETATM 2610 O HOH A 670 65.887 -13.994 22.931 1.00 79.24 O HETATM 2611 O HOH D 201 58.420 -13.604 -9.885 1.00 80.57 O HETATM 2612 O HOH D 202 32.325 -2.541 -1.065 1.00 66.94 O HETATM 2613 O HOH D 203 44.256 -17.305 -8.068 1.00 79.81 O HETATM 2614 O HOH D 204 57.567 -36.178 -11.326 1.00 68.57 O HETATM 2615 O HOH D 205 59.344 -23.755 -7.289 1.00 80.66 O HETATM 2616 O HOH D 206 38.804 -24.852 -10.097 1.00 72.65 O HETATM 2617 O HOH D 207 63.449 -10.858 -7.552 1.00 96.96 O CONECT 1113 2538 CONECT 1203 2539 CONECT 1204 2538 CONECT 1324 1329 CONECT 1329 1324 1330 CONECT 1330 1329 1331 1338 CONECT 1331 1330 1332 1333 CONECT 1332 1331 CONECT 1333 1331 1334 CONECT 1334 1333 1335 1336 1337 CONECT 1335 1334 CONECT 1336 1334 CONECT 1337 1334 CONECT 1338 1330 1339 1340 CONECT 1339 1338 CONECT 1340 1338 CONECT 2390 2398 CONECT 2397 2399 2400 2406 CONECT 2398 2390 2400 CONECT 2399 2397 CONECT 2400 2397 2398 2401 2405 CONECT 2401 2400 2404 CONECT 2402 2403 2404 CONECT 2403 2402 2434 CONECT 2404 2401 2402 CONECT 2405 2400 CONECT 2406 2397 CONECT 2422 2429 CONECT 2428 2430 2431 2437 CONECT 2429 2422 2431 CONECT 2430 2428 CONECT 2431 2428 2429 2432 2436 CONECT 2432 2431 2435 CONECT 2433 2434 2435 CONECT 2434 2403 2433 CONECT 2435 2432 2433 CONECT 2436 2431 CONECT 2437 2428 CONECT 2448 2540 CONECT 2455 2456 2457 2458 2462 CONECT 2456 2455 2539 CONECT 2457 2455 CONECT 2458 2455 2538 CONECT 2459 2460 2461 2462 2463 CONECT 2460 2459 CONECT 2461 2459 2538 CONECT 2462 2455 2459 CONECT 2463 2459 2464 CONECT 2464 2463 2465 CONECT 2465 2464 2466 2467 CONECT 2466 2465 2471 CONECT 2467 2465 2468 2469 CONECT 2468 2467 CONECT 2469 2467 2470 2471 CONECT 2470 2469 CONECT 2471 2466 2469 2472 CONECT 2472 2471 2473 2481 CONECT 2473 2472 2474 CONECT 2474 2473 2475 CONECT 2475 2474 2476 2481 CONECT 2476 2475 2477 2478 CONECT 2477 2476 CONECT 2478 2476 2479 CONECT 2479 2478 2480 CONECT 2480 2479 2481 CONECT 2481 2472 2475 2480 CONECT 2482 2483 CONECT 2483 2482 2484 CONECT 2484 2483 2485 CONECT 2485 2484 2486 CONECT 2486 2485 2487 CONECT 2487 2486 2488 CONECT 2488 2487 2489 CONECT 2489 2488 2490 CONECT 2490 2489 2491 CONECT 2491 2490 2492 CONECT 2492 2491 2493 CONECT 2493 2492 2494 CONECT 2494 2493 CONECT 2495 2496 2497 2498 2499 CONECT 2496 2495 CONECT 2497 2495 CONECT 2498 2495 CONECT 2499 2495 CONECT 2500 2501 2502 CONECT 2501 2500 CONECT 2502 2500 2503 CONECT 2503 2502 2504 CONECT 2504 2503 2505 CONECT 2505 2504 2506 CONECT 2506 2505 CONECT 2507 2508 2509 CONECT 2508 2507 CONECT 2509 2507 2510 CONECT 2510 2509 2511 CONECT 2511 2510 2512 CONECT 2512 2511 2513 CONECT 2513 2512 2539 CONECT 2514 2515 2519 CONECT 2515 2514 2516 CONECT 2516 2515 2517 CONECT 2517 2516 2518 2520 CONECT 2518 2517 2519 CONECT 2519 2514 2518 CONECT 2520 2517 2521 CONECT 2521 2520 2522 CONECT 2522 2521 2523 2524 2525 CONECT 2523 2522 CONECT 2524 2522 CONECT 2525 2522 CONECT 2526 2527 CONECT 2527 2526 2528 CONECT 2528 2527 2529 CONECT 2529 2528 2530 CONECT 2530 2529 2531 CONECT 2531 2530 2532 CONECT 2532 2531 2533 CONECT 2533 2532 2534 CONECT 2534 2533 2535 CONECT 2535 2534 2536 CONECT 2536 2535 CONECT 2538 1113 1204 2458 2461 CONECT 2538 2591 2594 CONECT 2539 1203 2456 2513 2571 CONECT 2540 2448 CONECT 2571 2539 CONECT 2591 2538 CONECT 2594 2538 MASTER 568 0 14 16 9 0 22 6 2582 2 128 25 END
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Related entries of code: 5lxm
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3e5a
RCSB PDB
PDBbind
44aa, >3E5A_2|Chain... *
3ha6
RCSB PDB
PDBbind
44aa, >3HA6_2|Chain... at 100%
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
5lxm
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Aurora kinase A
Ligand Name
Targeting protein for Xklp2 (stapled TPX2 protein 10)
EC.Number
E.C.2.7.11.1
Resolution
2.08(Å)
Affinity (Kd/Ki/IC50)
Kd=0.18uM
Release Year
2016
Protein/NA Sequence
Check fasta file
Primary Reference
(2016) ACS Chem. Biol. Vol. 11: pp. 3383-3390
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):
Q9ULW0
O14965
Entrez Gene ID
NCBI Entrez Gene ID:
22974
6790
ASD
Information of known allosteric effects of PDB entries
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