HEADER SIGNALING PROTEIN 07-DEC-11 3UZC TITLE THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH 4-(3-AMINO-5- TITLE 2 PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE A2A RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-317; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS 7TM, GPCR, G-PROTEIN, MEMBRANE PROTEIN, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL,C.J.LANGMEAD, AUTHOR 2 J.S.MASON,I.W.NG,A.ZHUKOV,M.WEIR,F.H.MARSHALL REVDAT 1 21-MAR-12 3UZC 0 JRNL AUTH M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL, JRNL AUTH 2 C.J.LANGMEAD,J.S.MASON,I.W.NG,B.TEHAN,A.ZHUKOV,M.WEIR, JRNL AUTH 3 F.H.MARSHALL JRNL TITL DISCOVERY OF 1,2,4-TRIAZINE DERIVATIVES AS ADENOSINE A(2A) JRNL TITL 2 ANTAGONISTS USING STRUCTURE BASED DRUG DESIGN JRNL REF J.MED.CHEM. V. 55 1898 2012 JRNL REFN ISSN 0022-2623 JRNL PMID 22220592 JRNL DOI 10.1021/JM201376W REMARK 2 REMARK 2 RESOLUTION. 3.34 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_84) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.34 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2 REMARK 3 NUMBER OF REFLECTIONS : 10797 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.282 REMARK 3 R VALUE (WORKING SET) : 0.282 REMARK 3 FREE R VALUE : 0.290 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730 REMARK 3 FREE R VALUE TEST SET COUNT : 511 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.8049 - 5.2787 0.91 2608 138 0.2566 0.2355 REMARK 3 2 5.2787 - 4.2030 0.93 2603 113 0.2420 0.2290 REMARK 3 3 4.2030 - 3.6756 0.92 2544 132 0.3112 0.3924 REMARK 3 4 3.6756 - 3.3413 0.93 2531 128 0.4328 0.4763 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.23 REMARK 3 B_SOL : 56.80 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 97.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 155.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 19.30240 REMARK 3 B22 (A**2) : -61.76260 REMARK 3 B33 (A**2) : 42.46010 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 2333 REMARK 3 ANGLE : 0.392 3180 REMARK 3 CHIRALITY : 0.027 377 REMARK 3 PLANARITY : 0.002 390 REMARK 3 DIHEDRAL : 11.047 789 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain A and resid 7:33 REMARK 3 ORIGIN FOR THE GROUP (A): 19.8961 26.4223 42.3237 REMARK 3 T TENSOR REMARK 3 T11: 1.0231 T22: 0.7021 REMARK 3 T33: 2.0473 T12: -0.0170 REMARK 3 T13: 0.0798 T23: 0.0619 REMARK 3 L TENSOR REMARK 3 L11: 0.7822 L22: 0.3730 REMARK 3 L33: 1.8361 L12: 0.4622 REMARK 3 L13: -0.2305 L23: 0.3327 REMARK 3 S TENSOR REMARK 3 S11: -0.1385 S12: -0.8816 S13: -0.2594 REMARK 3 S21: 0.9329 S22: 0.8912 S23: 0.0189 REMARK 3 S31: 0.0662 S32: -0.6210 S33: -0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain A and resid 34:40 REMARK 3 ORIGIN FOR THE GROUP (A): 20.8923 44.5708 30.3390 REMARK 3 T TENSOR REMARK 3 T11: 1.6675 T22: 1.0670 REMARK 3 T33: 2.9131 T12: 0.2578 REMARK 3 T13: 0.1413 T23: 0.0019 REMARK 3 L TENSOR REMARK 3 L11: 0.0116 L22: 0.0137 REMARK 3 L33: -0.0001 L12: -0.0170 REMARK 3 L13: -0.0073 L23: 0.0043 REMARK 3 S TENSOR REMARK 3 S11: -0.3301 S12: 0.4747 S13: 1.0537 REMARK 3 S21: 0.0858 S22: -0.2420 S23: 0.1653 REMARK 3 S31: 0.1167 S32: 0.9460 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain A and resid 41:68 REMARK 3 ORIGIN FOR THE GROUP (A): 17.6095 22.7030 34.0599 REMARK 3 T TENSOR REMARK 3 T11: 1.1542 T22: 0.7971 REMARK 3 T33: 1.5095 T12: 0.0186 REMARK 3 T13: 0.5204 T23: 0.1842 REMARK 3 L TENSOR REMARK 3 L11: 0.0143 L22: 0.5807 REMARK 3 L33: 1.1947 L12: -0.1838 REMARK 3 L13: -0.2603 L23: 0.8284 REMARK 3 S TENSOR REMARK 3 S11: -0.9074 S12: -0.3434 S13: -0.0174 REMARK 3 S21: -1.3947 S22: -0.0631 S23: -0.3487 REMARK 3 S31: 0.8982 S32: -0.2434 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain A and resid 69:76 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5585 4.2447 32.5211 REMARK 3 T TENSOR REMARK 3 T11: 1.7182 T22: 1.4188 REMARK 3 T33: 3.2677 T12: -0.4813 REMARK 3 T13: 0.3004 T23: 0.2640 REMARK 3 L TENSOR REMARK 3 L11: 0.2309 L22: 0.1103 REMARK 3 L33: 0.0642 L12: 0.0122 REMARK 3 L13: -0.1018 L23: 0.0428 REMARK 3 S TENSOR REMARK 3 S11: 0.0115 S12: 0.8587 S13: -0.2868 REMARK 3 S21: -0.8914 S22: 0.6636 S23: 0.0630 REMARK 3 S31: 0.7000 S32: 0.1182 S33: 0.0002 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain A and resid 77:104 REMARK 3 ORIGIN FOR THE GROUP (A): 21.1673 23.3909 24.3474 REMARK 3 T TENSOR REMARK 3 T11: 0.9384 T22: 0.9372 REMARK 3 T33: 2.0417 T12: -0.1808 REMARK 3 T13: 0.2600 T23: 0.2833 REMARK 3 L TENSOR REMARK 3 L11: 0.4029 L22: 0.0441 REMARK 3 L33: 0.5634 L12: -0.0232 REMARK 3 L13: 0.5358 L23: -0.1434 REMARK 3 S TENSOR REMARK 3 S11: -0.1828 S12: 1.1155 S13: -0.2695 REMARK 3 S21: -1.6856 S22: 0.8480 S23: 0.4586 REMARK 3 S31: -0.0157 S32: -0.8079 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain A and resid 105:118 REMARK 3 ORIGIN FOR THE GROUP (A): 26.3813 43.4402 14.5747 REMARK 3 T TENSOR REMARK 3 T11: 1.7762 T22: 0.7503 REMARK 3 T33: 2.6562 T12: 0.0874 REMARK 3 T13: 0.4149 T23: 0.0939 REMARK 3 L TENSOR REMARK 3 L11: 0.1336 L22: 0.0785 REMARK 3 L33: 0.2243 L12: 0.1002 REMARK 3 L13: 0.1680 L23: 0.1343 REMARK 3 S TENSOR REMARK 3 S11: -0.8682 S12: 1.2855 S13: 0.6853 REMARK 3 S21: -1.3287 S22: -0.1364 S23: 0.6300 REMARK 3 S31: 0.5142 S32: 0.1701 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain A and resid 119:141 REMARK 3 ORIGIN FOR THE GROUP (A): 13.9849 23.3359 20.1521 REMARK 3 T TENSOR REMARK 3 T11: 1.0250 T22: 0.7615 REMARK 3 T33: 1.8518 T12: -0.0383 REMARK 3 T13: -0.4225 T23: -0.0596 REMARK 3 L TENSOR REMARK 3 L11: 0.8191 L22: 0.1084 REMARK 3 L33: 0.4180 L12: -0.2908 REMARK 3 L13: 0.2833 L23: -0.0451 REMARK 3 S TENSOR REMARK 3 S11: 0.5249 S12: 1.6907 S13: -0.5014 REMARK 3 S21: -1.4877 S22: 0.4902 S23: 0.9795 REMARK 3 S31: 0.4425 S32: -0.3060 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain A and resid 142:149 REMARK 3 ORIGIN FOR THE GROUP (A): 13.5006 -0.2735 22.2445 REMARK 3 T TENSOR REMARK 3 T11: 1.6294 T22: 1.2959 REMARK 3 T33: 2.7567 T12: 0.1160 REMARK 3 T13: 0.1054 T23: 0.0233 REMARK 3 L TENSOR REMARK 3 L11: 0.1094 L22: 0.0133 REMARK 3 L33: 0.1208 L12: -0.0124 REMARK 3 L13: 0.0827 L23: 0.0190 REMARK 3 S TENSOR REMARK 3 S11: 0.2306 S12: 0.7374 S13: -0.1390 REMARK 3 S21: -0.2607 S22: -0.3527 S23: -0.1246 REMARK 3 S31: 0.2734 S32: -1.0394 S33: -0.0002 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain A and resid 158:175 REMARK 3 ORIGIN FOR THE GROUP (A): 13.2924 0.3982 30.1014 REMARK 3 T TENSOR REMARK 3 T11: 1.4470 T22: 0.8682 REMARK 3 T33: 2.5388 T12: -0.0032 REMARK 3 T13: -0.0409 T23: 0.0041 REMARK 3 L TENSOR REMARK 3 L11: 0.0866 L22: 0.4035 REMARK 3 L33: 0.5261 L12: -0.1382 REMARK 3 L13: 0.1249 L23: 0.0616 REMARK 3 S TENSOR REMARK 3 S11: 1.4071 S12: -0.1516 S13: -0.4675 REMARK 3 S21: -1.7358 S22: 0.1961 S23: 1.1980 REMARK 3 S31: 1.5934 S32: -0.3512 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain A and resid 176:211 REMARK 3 ORIGIN FOR THE GROUP (A): 33.9104 25.9245 17.8107 REMARK 3 T TENSOR REMARK 3 T11: 1.4013 T22: 0.8782 REMARK 3 T33: 2.1758 T12: -0.2641 REMARK 3 T13: 0.0859 T23: 0.1784 REMARK 3 L TENSOR REMARK 3 L11: 0.9021 L22: 0.7475 REMARK 3 L33: 0.3133 L12: -0.8373 REMARK 3 L13: -0.2824 L23: 0.1251 REMARK 3 S TENSOR REMARK 3 S11: -0.3284 S12: 0.1700 S13: 1.3920 REMARK 3 S21: -0.0231 S22: -0.2569 S23: -0.5113 REMARK 3 S31: -0.0053 S32: 0.0241 S33: -0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain A and resid 212:220 REMARK 3 ORIGIN FOR THE GROUP (A): 44.9910 54.1652 18.5103 REMARK 3 T TENSOR REMARK 3 T11: 1.8685 T22: 1.3127 REMARK 3 T33: 3.2693 T12: -0.0862 REMARK 3 T13: 0.7543 T23: 0.5088 REMARK 3 L TENSOR REMARK 3 L11: 0.0374 L22: 0.0068 REMARK 3 L33: 0.1911 L12: -0.0181 REMARK 3 L13: 0.0850 L23: -0.0392 REMARK 3 S TENSOR REMARK 3 S11: 0.4686 S12: -0.1936 S13: 0.1141 REMARK 3 S21: -0.3292 S22: 0.7021 S23: -0.6629 REMARK 3 S31: 0.9089 S32: -0.2057 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: chain A and resid 221:258 REMARK 3 ORIGIN FOR THE GROUP (A): 33.6133 24.7887 26.7588 REMARK 3 T TENSOR REMARK 3 T11: 1.1445 T22: 0.9679 REMARK 3 T33: 1.1601 T12: -0.0516 REMARK 3 T13: -0.1805 T23: -0.0039 REMARK 3 L TENSOR REMARK 3 L11: 1.8711 L22: 0.4612 REMARK 3 L33: 1.1230 L12: 0.1736 REMARK 3 L13: -1.2405 L23: -0.6113 REMARK 3 S TENSOR REMARK 3 S11: -0.5801 S12: 0.7994 S13: -0.7424 REMARK 3 S21: -1.2940 S22: 1.5760 S23: -2.6155 REMARK 3 S31: -0.7585 S32: -0.2122 S33: 0.0001 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: chain A and resid 259:267 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4025 -2.0977 30.1301 REMARK 3 T TENSOR REMARK 3 T11: 1.0940 T22: 0.7869 REMARK 3 T33: 3.3207 T12: -0.1292 REMARK 3 T13: 0.0593 T23: 0.0128 REMARK 3 L TENSOR REMARK 3 L11: 0.2831 L22: 0.0883 REMARK 3 L33: 0.1460 L12: -0.0222 REMARK 3 L13: 0.2208 L23: -0.0038 REMARK 3 S TENSOR REMARK 3 S11: -0.0784 S12: -0.7130 S13: 0.7774 REMARK 3 S21: -0.9300 S22: 0.9518 S23: 0.3694 REMARK 3 S31: -0.7816 S32: 0.7118 S33: 0.0000 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: chain A and resid 268:292 REMARK 3 ORIGIN FOR THE GROUP (A): 29.3387 21.9009 37.3562 REMARK 3 T TENSOR REMARK 3 T11: 0.2323 T22: 0.8151 REMARK 3 T33: -1.4866 T12: 0.0443 REMARK 3 T13: -1.3396 T23: -0.2153 REMARK 3 L TENSOR REMARK 3 L11: -0.0895 L22: 0.4893 REMARK 3 L33: 1.7409 L12: -0.0542 REMARK 3 L13: 0.1088 L23: -0.3201 REMARK 3 S TENSOR REMARK 3 S11: -0.1174 S12: -0.9465 S13: 0.1448 REMARK 3 S21: 0.9190 S22: -0.1173 S23: -0.4923 REMARK 3 S31: -0.6154 S32: 0.6193 S33: 1.3419 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: chain A and resid 293:305 REMARK 3 ORIGIN FOR THE GROUP (A): 25.9277 42.7856 42.7276 REMARK 3 T TENSOR REMARK 3 T11: 1.0979 T22: 0.8537 REMARK 3 T33: 1.8210 T12: -0.0171 REMARK 3 T13: -0.3406 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 0.1290 L22: 0.0934 REMARK 3 L33: 0.1179 L12: -0.0107 REMARK 3 L13: -0.0480 L23: -0.1217 REMARK 3 S TENSOR REMARK 3 S11: -0.3614 S12: -0.5341 S13: 1.1545 REMARK 3 S21: 1.6046 S22: -0.0558 S23: -1.0137 REMARK 3 S31: -2.2735 S32: 1.7330 S33: 0.0000 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 3UZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-11. REMARK 100 THE RCSB ID CODE IS RCSB069398. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10975 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.340 REMARK 200 RESOLUTION RANGE LOW (A) : 49.290 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.09500 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.34 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : 5.50 REMARK 200 R MERGE FOR SHELL (I) : 0.85100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3PWH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 77.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 32-42% PEG1000, 0.25M MGCL2, 0.3% NG, REMARK 280 0.1%(W/V) 1-BUTANOL, 0.05% CYMAL-6, PH 8.0, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.35000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.03200 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.45000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.35000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.03200 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.45000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.35000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.03200 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.45000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.35000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.03200 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.45000 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 MET A 4 REMARK 465 GLY A 5 REMARK 465 SER A 6 REMARK 465 LYS A 150 REMARK 465 GLU A 151 REMARK 465 GLY A 152 REMARK 465 LYS A 153 REMARK 465 ASN A 154 REMARK 465 HIS A 155 REMARK 465 SER A 156 REMARK 465 GLN A 157 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 ALA A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 465 HIS A 329 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 LEU A 58 -53.64 -130.74 REMARK 500 ALA A 73 175.44 -56.11 REMARK 500 VAL A 116 91.81 -68.67 REMARK 500 ALA A 165 101.04 -56.88 REMARK 500 VAL A 178 -66.46 -97.84 REMARK 500 ASN A 181 -70.91 -66.43 REMARK 500 PHE A 182 -71.65 -59.37 REMARK 500 VAL A 186 -58.91 -135.28 REMARK 500 PRO A 217 -74.28 -57.77 REMARK 500 SER A 263 114.40 -39.97 REMARK 500 PRO A 266 170.65 -58.84 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T4E A 330 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3UZA RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED TO COMPOUND 4G REMARK 900 RELATED ID: 3PWH RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED TO ZM241385 REMARK 900 RELATED ID: 3RFM RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED TO CAFFEINE REMARK 900 RELATED ID: 3REY RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED TO XAC DBREF 3UZC A 1 317 UNP P29274 AA2AR_HUMAN 1 317 SEQADV 3UZC LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 3UZC ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 3UZC ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 3UZC ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 3UZC ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 3UZC ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 3UZC ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 3UZC ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 3UZC ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 3UZC ALA A 319 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 328 UNP P29274 EXPRESSION TAG SEQADV 3UZC HIS A 329 UNP P29274 EXPRESSION TAG SEQRES 1 A 329 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU SEQRES 2 A 329 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU SEQRES 3 A 329 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN SEQRES 4 A 329 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP SEQRES 5 A 329 ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR SEQRES 6 A 329 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU SEQRES 7 A 329 PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER SEQRES 8 A 329 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE SEQRES 9 A 329 ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR SEQRES 10 A 329 GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL SEQRES 11 A 329 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP SEQRES 12 A 329 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER SEQRES 13 A 329 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU SEQRES 14 A 329 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE SEQRES 15 A 329 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY SEQRES 16 A 329 VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU SEQRES 17 A 329 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA SEQRES 18 A 329 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER SEQRES 19 A 329 ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP LEU SEQRES 20 A 329 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO SEQRES 21 A 329 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA SEQRES 22 A 329 ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO PHE SEQRES 23 A 329 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE SEQRES 24 A 329 ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU SEQRES 25 A 329 PRO PHE LYS ALA ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 26 A 329 HIS HIS HIS HIS HET T4E A 330 21 HETNAM T4E 4-(3-AMINO-5-PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL FORMUL 2 T4E C15 H11 CL N4 O HELIX 1 1 SER A 7 ASN A 34 1 28 HELIX 2 2 SER A 35 ASN A 39 5 5 HELIX 3 3 VAL A 40 LEU A 58 1 19 HELIX 4 4 LEU A 58 GLY A 69 1 12 HELIX 5 5 ALA A 73 ILE A 108 1 36 HELIX 6 6 ILE A 108 VAL A 116 1 9 HELIX 7 7 THR A 117 LEU A 137 1 21 HELIX 8 8 THR A 138 GLY A 142 5 5 HELIX 9 9 LEU A 167 VAL A 172 1 6 HELIX 10 10 PRO A 173 TYR A 179 1 7 HELIX 11 11 ASN A 181 VAL A 186 1 6 HELIX 12 12 VAL A 186 MET A 211 1 26 HELIX 13 13 GLY A 218 CYS A 259 1 42 HELIX 14 14 PRO A 266 ILE A 292 1 27 HELIX 15 15 ILE A 292 SER A 305 1 14 SHEET 1 A 2 PHE A 70 ALA A 72 0 SHEET 2 A 2 VAL A 164 CYS A 166 -1 O CYS A 166 N PHE A 70 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 SITE 1 AC1 9 VAL A 84 LEU A 85 PHE A 168 LEU A 249 SITE 2 AC1 9 HIS A 250 ASN A 253 ILE A 274 ALA A 277 SITE 3 AC1 9 HIS A 278 CRYST1 110.700 112.064 126.900 90.00 90.00 90.00 I 2 2 2 8 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 0.009033 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008923 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007880 0.00000 ATOM 1 N SER A 7 22.399 6.822 51.127 1.00184.85 N ANISOU 1 N SER A 7 23260 16560 30414 -375 -1730 3785 N ATOM 2 CA SER A 7 21.663 8.071 50.962 1.00183.97 C ANISOU 2 CA SER A 7 22961 16716 30223 -383 -1465 3746 C ATOM 3 C SER A 7 22.606 9.263 50.835 1.00183.85 C ANISOU 3 C SER A 7 22852 16727 30277 -185 -1527 3273 C ATOM 4 O SER A 7 22.238 10.393 51.156 1.00185.85 O ANISOU 4 O SER A 7 23029 17215 30371 -72 -1353 3201 O ATOM 5 CB SER A 7 20.699 8.287 52.131 1.00186.19 C ANISOU 5 CB SER A 7 23336 17291 30118 -285 -1288 4067 C ATOM 6 OG SER A 7 19.713 7.270 52.176 1.00187.83 O ANISOU 6 OG SER A 7 23608 17503 30254 -503 -1195 4509 O ATOM 7 N VAL A 8 23.824 9.004 50.368 1.00181.88 N ANISOU 7 N VAL A 8 22611 16233 30261 -145 -1772 2947 N ATOM 8 CA VAL A 8 24.812 10.061 50.173 1.00178.15 C ANISOU 8 CA VAL A 8 22051 15765 29872 16 -1849 2474 C ATOM 9 C VAL A 8 24.660 10.693 48.793 1.00175.02 C ANISOU 9 C VAL A 8 21413 15323 29766 -194 -1723 2281 C ATOM 10 O VAL A 8 24.640 11.918 48.658 1.00169.67 O ANISOU 10 O VAL A 8 20620 14788 29058 -126 -1594 2063 O ATOM 11 CB VAL A 8 26.249 9.534 50.336 1.00172.04 C ANISOU 11 CB VAL A 8 21389 14776 29204 169 -2177 2186 C ATOM 12 CG1 VAL A 8 27.256 10.642 50.062 1.00161.34 C ANISOU 12 CG1 VAL A 8 19927 13435 27938 304 -2246 1683 C ATOM 13 CG2 VAL A 8 26.448 8.956 51.728 1.00177.11 C ANISOU 13 CG2 VAL A 8 22276 15471 29548 396 -2313 2367 C ATOM 14 N TYR A 9 24.556 9.848 47.772 1.00175.20 N ANISOU 14 N TYR A 9 21365 15139 30063 -454 -1761 2362 N ATOM 15 CA TYR A 9 24.317 10.309 46.411 1.00171.48 C ANISOU 15 CA TYR A 9 20665 14620 29869 -691 -1639 2227 C ATOM 16 C TYR A 9 23.078 11.195 46.372 1.00183.00 C ANISOU 16 C TYR A 9 21998 16346 31187 -752 -1327 2421 C ATOM 17 O TYR A 9 23.061 12.231 45.708 1.00178.87 O ANISOU 17 O TYR A 9 21309 15886 30766 -784 -1211 2199 O ATOM 18 CB TYR A 9 24.139 9.116 45.470 1.00159.59 C ANISOU 18 CB TYR A 9 19126 12886 28626 -983 -1694 2389 C ATOM 19 CG TYR A 9 23.747 9.492 44.059 1.00150.82 C ANISOU 19 CG TYR A 9 17776 11742 27786 -1261 -1552 2308 C ATOM 20 CD1 TYR A 9 24.708 9.847 43.122 1.00153.86 C ANISOU 20 CD1 TYR A 9 18043 11964 28452 -1309 -1671 1894 C ATOM 21 CD2 TYR A 9 22.416 9.484 43.661 1.00146.92 C ANISOU 21 CD2 TYR A 9 17171 11390 27261 -1481 -1301 2645 C ATOM 22 CE1 TYR A 9 24.355 10.187 41.830 1.00157.89 C ANISOU 22 CE1 TYR A 9 18340 12447 29204 -1570 -1545 1824 C ATOM 23 CE2 TYR A 9 22.053 9.822 42.370 1.00150.22 C ANISOU 23 CE2 TYR A 9 17368 11789 27920 -1735 -1177 2579 C ATOM 24 CZ TYR A 9 23.027 10.173 41.459 1.00158.93 C ANISOU 24 CZ TYR A 9 18366 12720 29299 -1780 -1300 2170 C ATOM 25 OH TYR A 9 22.673 10.512 40.173 1.00164.43 O ANISOU 25 OH TYR A 9 18848 13400 30229 -2039 -1179 2106 O ATOM 26 N ILE A 10 22.043 10.776 47.094 1.00197.74 N ANISOU 26 N ILE A 10 23947 18372 32813 -765 -1192 2838 N ATOM 27 CA ILE A 10 20.806 11.539 47.182 1.00195.20 C ANISOU 27 CA ILE A 10 23513 18329 32324 -802 -895 3055 C ATOM 28 C ILE A 10 21.063 12.916 47.785 1.00185.73 C ANISOU 28 C ILE A 10 22305 17315 30948 -535 -821 2804 C ATOM 29 O ILE A 10 20.606 13.930 47.259 1.00185.37 O ANISOU 29 O ILE A 10 22097 17396 30941 -567 -631 2718 O ATOM 30 CB ILE A 10 19.756 10.806 48.038 1.00203.64 C ANISOU 30 CB ILE A 10 24698 19550 33126 -834 -786 3531 C ATOM 31 CG1 ILE A 10 19.547 9.381 47.521 1.00204.79 C ANISOU 31 CG1 ILE A 10 24888 19494 33429 -1098 -868 3781 C ATOM 32 CG2 ILE A 10 18.446 11.580 48.054 1.00202.41 C ANISOU 32 CG2 ILE A 10 24401 19696 32812 -881 -472 3752 C ATOM 33 CD1 ILE A 10 18.588 8.561 48.357 1.00207.13 C ANISOU 33 CD1 ILE A 10 25322 19915 33464 -1151 -779 4243 C ATOM 34 N THR A 11 21.801 12.942 48.890 1.00178.17 N ANISOU 34 N THR A 11 21530 16373 29794 -271 -973 2687 N ATOM 35 CA THR A 11 22.113 14.190 49.576 1.00172.88 C ANISOU 35 CA THR A 11 20880 15876 28932 -11 -916 2441 C ATOM 36 C THR A 11 22.872 15.154 48.668 1.00168.41 C ANISOU 36 C THR A 11 20175 15217 28597 -17 -941 1998 C ATOM 37 O THR A 11 22.532 16.333 48.581 1.00170.02 O ANISOU 37 O THR A 11 20288 15574 28738 46 -755 1884 O ATOM 38 CB THR A 11 22.937 13.941 50.855 1.00172.39 C ANISOU 38 CB THR A 11 21038 15819 28642 256 -1116 2361 C ATOM 39 OG1 THR A 11 22.188 13.117 51.755 1.00175.98 O ANISOU 39 OG1 THR A 11 21634 16376 28854 265 -1078 2781 O ATOM 40 CG2 THR A 11 23.269 15.257 51.540 1.00172.21 C ANISOU 40 CG2 THR A 11 21035 15978 28420 510 -1049 2090 C ATOM 41 N VAL A 12 23.897 14.645 47.992 1.00161.43 N ANISOU 41 N VAL A 12 19280 14079 27977 -93 -1167 1748 N ATOM 42 CA VAL A 12 24.697 15.463 47.086 1.00150.38 C ANISOU 42 CA VAL A 12 17754 12576 26809 -124 -1211 1313 C ATOM 43 C VAL A 12 23.857 16.006 45.934 1.00147.21 C ANISOU 43 C VAL A 12 17143 12210 26580 -351 -987 1371 C ATOM 44 O VAL A 12 23.944 17.186 45.596 1.00148.94 O ANISOU 44 O VAL A 12 17272 12497 26821 -308 -876 1127 O ATOM 45 CB VAL A 12 25.898 14.682 46.521 1.00140.87 C ANISOU 45 CB VAL A 12 16563 11093 25867 -189 -1497 1059 C ATOM 46 CG1 VAL A 12 26.570 15.470 45.407 1.00122.56 C ANISOU 46 CG1 VAL A 12 14086 8671 23810 -286 -1513 644 C ATOM 47 CG2 VAL A 12 26.889 14.361 47.629 1.00146.64 C ANISOU 47 CG2 VAL A 12 17485 11802 26430 72 -1732 923 C ATOM 48 N GLU A 13 23.043 15.142 45.335 1.00147.68 N ANISOU 48 N GLU A 13 17132 12224 26756 -596 -919 1697 N ATOM 49 CA GLU A 13 22.169 15.553 44.241 1.00148.06 C ANISOU 49 CA GLU A 13 16975 12323 26960 -825 -707 1794 C ATOM 50 C GLU A 13 21.199 16.643 44.686 1.00144.98 C ANISOU 50 C GLU A 13 16535 12214 26336 -708 -437 1923 C ATOM 51 O GLU A 13 20.927 17.587 43.942 1.00142.23 O ANISOU 51 O GLU A 13 16038 11917 26086 -766 -288 1798 O ATOM 52 CB GLU A 13 21.400 14.354 43.684 1.00151.87 C ANISOU 52 CB GLU A 13 17407 12737 27560 -1104 -678 2158 C ATOM 53 CG GLU A 13 22.249 13.396 42.864 1.00152.84 C ANISOU 53 CG GLU A 13 17524 12563 27986 -1280 -903 2007 C ATOM 54 CD GLU A 13 22.790 14.033 41.599 1.00156.16 C ANISOU 54 CD GLU A 13 17770 12863 28699 -1418 -917 1654 C ATOM 55 OE1 GLU A 13 22.310 13.676 40.502 1.00156.50 O ANISOU 55 OE1 GLU A 13 17665 12838 28958 -1705 -847 1759 O ATOM 56 OE2 GLU A 13 23.691 14.893 41.699 1.00158.13 O ANISOU 56 OE2 GLU A 13 18033 13094 28957 -1251 -996 1271 O ATOM 57 N LEU A 14 20.679 16.506 45.901 1.00142.99 N ANISOU 57 N LEU A 14 16414 12142 25775 -540 -373 2175 N ATOM 58 CA LEU A 14 19.790 17.513 46.468 1.00138.88 C ANISOU 58 CA LEU A 14 15864 11899 25006 -396 -121 2295 C ATOM 59 C LEU A 14 20.534 18.827 46.683 1.00130.97 C ANISOU 59 C LEU A 14 14884 10922 23954 -176 -120 1888 C ATOM 60 O LEU A 14 19.998 19.903 46.420 1.00126.83 O ANISOU 60 O LEU A 14 14259 10533 23398 -140 87 1843 O ATOM 61 CB LEU A 14 19.187 17.022 47.787 1.00141.12 C ANISOU 61 CB LEU A 14 16298 12362 24959 -262 -75 2628 C ATOM 62 CG LEU A 14 17.849 16.282 47.715 1.00140.50 C ANISOU 62 CG LEU A 14 16156 12416 24811 -454 91 3107 C ATOM 63 CD1 LEU A 14 17.871 15.193 46.654 1.00140.85 C ANISOU 63 CD1 LEU A 14 16126 12248 25144 -761 -9 3207 C ATOM 64 CD2 LEU A 14 17.477 15.707 49.075 1.00141.82 C ANISOU 64 CD2 LEU A 14 16504 12728 24652 -321 89 3393 C ATOM 65 N ALA A 15 21.771 18.730 47.159 1.00129.85 N ANISOU 65 N ALA A 15 14879 10653 23805 -30 -352 1591 N ATOM 66 CA ALA A 15 22.600 19.907 47.386 1.00132.64 C ANISOU 66 CA ALA A 15 15269 11020 24110 164 -374 1178 C ATOM 67 C ALA A 15 22.803 20.688 46.091 1.00141.76 C ANISOU 67 C ALA A 15 16259 12071 25532 19 -314 908 C ATOM 68 O ALA A 15 22.746 21.918 46.080 1.00146.59 O ANISOU 68 O ALA A 15 16845 12776 26078 124 -171 720 O ATOM 69 CB ALA A 15 23.940 19.506 47.982 1.00127.58 C ANISOU 69 CB ALA A 15 14780 10248 23446 306 -659 908 C ATOM 70 N ILE A 16 23.037 19.964 45.002 1.00141.07 N ANISOU 70 N ILE A 16 16068 11788 25744 -228 -422 890 N ATOM 71 CA ILE A 16 23.222 20.585 43.695 1.00139.07 C ANISOU 71 CA ILE A 16 15654 11427 25760 -402 -377 653 C ATOM 72 C ILE A 16 21.941 21.262 43.216 1.00141.10 C ANISOU 72 C ILE A 16 15769 11849 25994 -482 -86 883 C ATOM 73 O ILE A 16 21.969 22.402 42.749 1.00138.16 O ANISOU 73 O ILE A 16 15330 11501 25663 -457 30 669 O ATOM 74 CB ILE A 16 23.681 19.561 42.640 1.00133.26 C ANISOU 74 CB ILE A 16 14835 10454 25345 -665 -551 614 C ATOM 75 CG1 ILE A 16 25.105 19.092 42.940 1.00134.50 C ANISOU 75 CG1 ILE A 16 15107 10434 25564 -574 -845 295 C ATOM 76 CG2 ILE A 16 23.613 20.160 41.247 1.00127.18 C ANISOU 76 CG2 ILE A 16 13879 9605 24837 -880 -464 448 C ATOM 77 CD1 ILE A 16 25.688 18.202 41.866 1.00138.41 C ANISOU 77 CD1 ILE A 16 15518 10684 26387 -816 -1020 188 C ATOM 78 N ALA A 17 20.822 20.555 43.339 1.00143.25 N ANISOU 78 N ALA A 17 15999 12237 26192 -579 31 1320 N ATOM 79 CA ALA A 17 19.529 21.075 42.907 1.00143.10 C ANISOU 79 CA ALA A 17 15830 12400 26141 -659 304 1579 C ATOM 80 C ALA A 17 19.257 22.460 43.482 1.00142.86 C ANISOU 80 C ALA A 17 15830 12552 25898 -412 489 1472 C ATOM 81 O ALA A 17 18.754 23.341 42.787 1.00140.33 O ANISOU 81 O ALA A 17 15382 12291 25646 -454 664 1440 O ATOM 82 CB ALA A 17 18.416 20.111 43.293 1.00146.30 C ANISOU 82 CB ALA A 17 16223 12947 26419 -748 396 2062 C ATOM 83 N VAL A 18 19.594 22.645 44.754 1.00146.44 N ANISOU 83 N VAL A 18 16458 13091 26090 -155 449 1417 N ATOM 84 CA VAL A 18 19.379 23.922 45.425 1.00148.20 C ANISOU 84 CA VAL A 18 16736 13485 26089 93 621 1307 C ATOM 85 C VAL A 18 20.211 25.033 44.791 1.00144.50 C ANISOU 85 C VAL A 18 16253 12889 25763 123 601 863 C ATOM 86 O VAL A 18 19.685 26.086 44.431 1.00142.84 O ANISOU 86 O VAL A 18 15969 12762 25541 163 803 828 O ATOM 87 CB VAL A 18 19.710 23.832 46.927 1.00150.05 C ANISOU 87 CB VAL A 18 17171 13822 26018 349 555 1306 C ATOM 88 CG1 VAL A 18 19.529 25.187 47.592 1.00155.47 C ANISOU 88 CG1 VAL A 18 17918 14675 26479 600 737 1165 C ATOM 89 CG2 VAL A 18 18.838 22.783 47.599 1.00146.68 C ANISOU 89 CG2 VAL A 18 16772 13533 25426 318 590 1755 C ATOM 90 N LEU A 19 21.511 24.791 44.656 1.00141.56 N ANISOU 90 N LEU A 19 15951 12315 25520 104 357 526 N ATOM 91 CA LEU A 19 22.418 25.768 44.063 1.00139.37 C ANISOU 91 CA LEU A 19 15669 11907 25377 111 315 78 C ATOM 92 C LEU A 19 22.044 26.078 42.618 1.00137.25 C ANISOU 92 C LEU A 19 15217 11554 25379 -125 411 66 C ATOM 93 O LEU A 19 22.095 27.230 42.187 1.00131.55 O ANISOU 93 O LEU A 19 14470 10827 24686 -92 528 -149 O ATOM 94 CB LEU A 19 23.866 25.276 44.136 1.00142.49 C ANISOU 94 CB LEU A 19 16152 12113 25873 107 20 -259 C ATOM 95 CG LEU A 19 24.608 25.441 45.464 1.00147.13 C ANISOU 95 CG LEU A 19 16931 12766 26203 372 -89 -431 C ATOM 96 CD1 LEU A 19 23.862 24.769 46.608 1.00151.37 C ANISOU 96 CD1 LEU A 19 17557 13477 26481 500 -45 -41 C ATOM 97 CD2 LEU A 19 26.024 24.895 45.351 1.00145.40 C ANISOU 97 CD2 LEU A 19 16762 12359 26122 341 -389 -762 C ATOM 98 N ALA A 20 21.674 25.042 41.872 1.00147.36 N ANISOU 98 N ALA A 20 16376 12764 26851 -368 359 297 N ATOM 99 CA ALA A 20 21.275 25.205 40.479 1.00149.80 C ANISOU 99 CA ALA A 20 16498 13001 27416 -617 442 317 C ATOM 100 C ALA A 20 20.089 26.156 40.364 1.00144.75 C ANISOU 100 C ALA A 20 15774 12556 26667 -555 733 514 C ATOM 101 O ALA A 20 20.034 26.991 39.461 1.00137.69 O ANISOU 101 O ALA A 20 14788 11617 25909 -633 825 365 O ATOM 102 CB ALA A 20 20.941 23.857 39.860 1.00152.03 C ANISOU 102 CB ALA A 20 16675 13209 27879 -880 358 584 C ATOM 103 N ILE A 21 19.141 26.025 41.286 1.00145.22 N ANISOU 103 N ILE A 21 15866 12834 26476 -411 875 849 N ATOM 104 CA ILE A 21 17.980 26.905 41.313 1.00142.39 C ANISOU 104 CA ILE A 21 15430 12686 25985 -316 1155 1049 C ATOM 105 C ILE A 21 18.380 28.306 41.761 1.00137.31 C ANISOU 105 C ILE A 21 14901 12065 25205 -67 1242 742 C ATOM 106 O ILE A 21 18.272 29.262 40.997 1.00137.50 O ANISOU 106 O ILE A 21 14858 12056 25331 -91 1355 600 O ATOM 107 CB ILE A 21 16.877 26.365 42.243 1.00145.13 C ANISOU 107 CB ILE A 21 15782 13278 26084 -226 1283 1481 C ATOM 108 CG1 ILE A 21 16.414 24.983 41.776 1.00142.26 C ANISOU 108 CG1 ILE A 21 15312 12894 25847 -492 1214 1800 C ATOM 109 CG2 ILE A 21 15.702 27.329 42.288 1.00146.89 C ANISOU 109 CG2 ILE A 21 15916 13731 26164 -105 1574 1666 C ATOM 110 CD1 ILE A 21 15.350 24.364 42.659 1.00142.69 C ANISOU 110 CD1 ILE A 21 15374 13184 25657 -439 1332 2227 C ATOM 111 N LEU A 22 18.848 28.418 43.001 1.00134.30 N ANISOU 111 N LEU A 22 14701 11738 24590 165 1188 639 N ATOM 112 CA LEU A 22 19.254 29.706 43.558 1.00129.84 C ANISOU 112 CA LEU A 22 14266 11200 23866 406 1270 344 C ATOM 113 C LEU A 22 20.137 30.486 42.592 1.00132.71 C ANISOU 113 C LEU A 22 14621 11358 24446 315 1209 -67 C ATOM 114 O LEU A 22 19.866 31.645 42.285 1.00133.83 O ANISOU 114 O LEU A 22 14756 11521 24571 390 1381 -177 O ATOM 115 CB LEU A 22 19.991 29.510 44.884 1.00120.13 C ANISOU 115 CB LEU A 22 13234 10000 22410 610 1140 214 C ATOM 116 CG LEU A 22 19.214 28.844 46.020 1.00118.62 C ANISOU 116 CG LEU A 22 13091 10020 21959 730 1199 585 C ATOM 117 CD1 LEU A 22 20.077 28.754 47.268 1.00117.45 C ANISOU 117 CD1 LEU A 22 13145 9886 21595 929 1054 405 C ATOM 118 CD2 LEU A 22 17.927 29.600 46.307 1.00119.18 C ANISOU 118 CD2 LEU A 22 13108 10326 21848 863 1500 834 C ATOM 119 N GLY A 23 21.193 29.837 42.114 1.00131.04 N ANISOU 119 N GLY A 23 14411 10945 24433 153 964 -292 N ATOM 120 CA GLY A 23 22.154 30.472 41.233 1.00130.39 C ANISOU 120 CA GLY A 23 14325 10665 24551 47 878 -706 C ATOM 121 C GLY A 23 21.546 31.087 39.986 1.00126.29 C ANISOU 121 C GLY A 23 13657 10111 24217 -113 1034 -666 C ATOM 122 O GLY A 23 21.588 32.302 39.803 1.00112.70 O ANISOU 122 O GLY A 23 11980 8379 22462 -25 1163 -866 O ATOM 123 N ASN A 24 20.982 30.248 39.124 1.00133.94 N ANISOU 123 N ASN A 24 14452 11060 25377 -351 1022 -406 N ATOM 124 CA ASN A 24 20.436 30.715 37.853 1.00134.06 C ANISOU 124 CA ASN A 24 14308 11041 25586 -532 1146 -359 C ATOM 125 C ASN A 24 19.186 31.579 38.001 1.00130.08 C ANISOU 125 C ASN A 24 13761 10738 24927 -383 1432 -107 C ATOM 126 O ASN A 24 18.920 32.437 37.162 1.00127.98 O ANISOU 126 O ASN A 24 13427 10440 24759 -435 1554 -176 O ATOM 127 CB ASN A 24 20.168 29.537 36.914 1.00138.97 C ANISOU 127 CB ASN A 24 14755 11601 26445 -837 1055 -146 C ATOM 128 CG ASN A 24 21.444 28.876 36.431 1.00141.49 C ANISOU 128 CG ASN A 24 15092 11689 26981 -1015 787 -453 C ATOM 129 OD1 ASN A 24 22.270 29.505 35.768 1.00135.74 O ANISOU 129 OD1 ASN A 24 14374 10807 26393 -1090 723 -818 O ATOM 130 ND2 ASN A 24 21.611 27.600 36.760 1.00145.16 N ANISOU 130 ND2 ASN A 24 15560 12125 27467 -1083 631 -309 N ATOM 131 N VAL A 25 18.417 31.348 39.061 1.00129.73 N ANISOU 131 N VAL A 25 13754 10901 24636 -198 1537 186 N ATOM 132 CA VAL A 25 17.268 32.197 39.352 1.00130.33 C ANISOU 132 CA VAL A 25 13800 11185 24536 -16 1810 405 C ATOM 133 C VAL A 25 17.760 33.593 39.712 1.00132.87 C ANISOU 133 C VAL A 25 14281 11462 24741 208 1893 69 C ATOM 134 O VAL A 25 17.184 34.598 39.293 1.00133.04 O ANISOU 134 O VAL A 25 14266 11526 24756 277 2086 80 O ATOM 135 CB VAL A 25 16.418 31.638 40.508 1.00134.75 C ANISOU 135 CB VAL A 25 14379 11985 24837 139 1897 764 C ATOM 136 CG1 VAL A 25 15.467 32.701 41.036 1.00136.24 C ANISOU 136 CG1 VAL A 25 14580 12381 24803 392 2169 892 C ATOM 137 CG2 VAL A 25 15.650 30.406 40.053 1.00138.76 C ANISOU 137 CG2 VAL A 25 14710 12567 25444 -92 1879 1150 C ATOM 138 N LEU A 26 18.837 33.642 40.487 1.00133.29 N ANISOU 138 N LEU A 26 14515 11429 24700 319 1746 -233 N ATOM 139 CA LEU A 26 19.479 34.900 40.840 1.00128.30 C ANISOU 139 CA LEU A 26 14053 10733 23960 503 1798 -600 C ATOM 140 C LEU A 26 19.937 35.619 39.579 1.00123.50 C ANISOU 140 C LEU A 26 13405 9932 23587 339 1792 -873 C ATOM 141 O LEU A 26 19.782 36.832 39.453 1.00128.81 O ANISOU 141 O LEU A 26 14143 10594 24204 457 1955 -1008 O ATOM 142 CB LEU A 26 20.675 34.641 41.756 1.00124.86 C ANISOU 142 CB LEU A 26 13794 10231 23417 594 1598 -890 C ATOM 143 CG LEU A 26 21.408 35.867 42.296 1.00118.33 C ANISOU 143 CG LEU A 26 13163 9357 22442 786 1641 -1281 C ATOM 144 CD1 LEU A 26 20.463 36.728 43.115 1.00124.55 C ANISOU 144 CD1 LEU A 26 14020 10337 22964 1057 1904 -1117 C ATOM 145 CD2 LEU A 26 22.610 35.445 43.126 1.00110.31 C ANISOU 145 CD2 LEU A 26 12289 8289 21334 843 1415 -1551 C ATOM 146 N VAL A 27 20.501 34.860 38.646 1.00120.89 N ANISOU 146 N VAL A 27 12971 9445 23516 62 1606 -953 N ATOM 147 CA VAL A 27 20.952 35.409 37.373 1.00117.02 C ANISOU 147 CA VAL A 27 12427 8772 23265 -135 1582 -1200 C ATOM 148 C VAL A 27 19.787 36.009 36.592 1.00115.93 C ANISOU 148 C VAL A 27 12158 8712 23179 -164 1810 -952 C ATOM 149 O VAL A 27 19.897 37.105 36.044 1.00119.62 O ANISOU 149 O VAL A 27 12670 9093 23689 -149 1908 -1150 O ATOM 150 CB VAL A 27 21.650 34.333 36.513 1.00116.61 C ANISOU 150 CB VAL A 27 12262 8560 23483 -440 1346 -1282 C ATOM 151 CG1 VAL A 27 21.966 34.876 35.127 1.00105.32 C ANISOU 151 CG1 VAL A 27 10754 6964 22300 -667 1342 -1494 C ATOM 152 CG2 VAL A 27 22.915 33.842 37.201 1.00125.17 C ANISOU 152 CG2 VAL A 27 13477 9552 24530 -403 1110 -1577 C ATOM 153 N CYS A 28 18.670 35.289 36.549 1.00115.89 N ANISOU 153 N CYS A 28 11994 8875 23165 -204 1893 -517 N ATOM 154 CA CYS A 28 17.481 35.763 35.849 1.00120.16 C ANISOU 154 CA CYS A 28 12386 9527 23742 -224 2106 -243 C ATOM 155 C CYS A 28 16.941 37.032 36.497 1.00126.14 C ANISOU 155 C CYS A 28 13257 10397 24273 87 2338 -245 C ATOM 156 O CYS A 28 16.511 37.960 35.811 1.00124.69 O ANISOU 156 O CYS A 28 13038 10196 24140 105 2487 -254 O ATOM 157 CB CYS A 28 16.396 34.685 35.841 1.00122.60 C ANISOU 157 CB CYS A 28 12509 10027 24047 -317 2149 226 C ATOM 158 SG CYS A 28 16.869 33.146 35.021 1.00148.77 S ANISOU 158 SG CYS A 28 15682 13211 27631 -693 1904 275 S ATOM 159 N TRP A 29 16.967 37.062 37.824 1.00133.61 N ANISOU 159 N TRP A 29 14343 11456 24966 333 2366 -236 N ATOM 160 CA TRP A 29 16.470 38.203 38.580 1.00143.59 C ANISOU 160 CA TRP A 29 15728 12835 25993 644 2586 -241 C ATOM 161 C TRP A 29 17.351 39.431 38.358 1.00139.34 C ANISOU 161 C TRP A 29 15368 12100 25475 707 2595 -678 C ATOM 162 O TRP A 29 16.851 40.532 38.127 1.00141.15 O ANISOU 162 O TRP A 29 15631 12340 25660 840 2791 -689 O ATOM 163 CB TRP A 29 16.403 37.858 40.069 1.00157.67 C ANISOU 163 CB TRP A 29 17626 14779 27502 866 2591 -152 C ATOM 164 CG TRP A 29 15.693 38.880 40.902 1.00172.09 C ANISOU 164 CG TRP A 29 19547 16767 29070 1185 2837 -87 C ATOM 165 CD1 TRP A 29 15.121 40.041 40.468 1.00177.37 C ANISOU 165 CD1 TRP A 29 20215 17444 29733 1303 3048 -95 C ATOM 166 CD2 TRP A 29 15.476 38.832 42.317 1.00180.61 C ANISOU 166 CD2 TRP A 29 20741 18023 29859 1430 2900 -4 C ATOM 167 NE1 TRP A 29 14.563 40.719 41.525 1.00182.11 N ANISOU 167 NE1 TRP A 29 20922 18212 30061 1612 3241 -29 N ATOM 168 CE2 TRP A 29 14.768 39.998 42.672 1.00185.50 C ANISOU 168 CE2 TRP A 29 21420 18753 30310 1689 3157 25 C ATOM 169 CE3 TRP A 29 15.812 37.916 43.319 1.00182.82 C ANISOU 169 CE3 TRP A 29 21083 18379 30001 1456 2764 50 C ATOM 170 CZ2 TRP A 29 14.390 40.272 43.986 1.00190.11 C ANISOU 170 CZ2 TRP A 29 22115 19522 30594 1963 3285 98 C ATOM 171 CZ3 TRP A 29 15.436 38.189 44.623 1.00187.04 C ANISOU 171 CZ3 TRP A 29 21731 19102 30235 1724 2887 130 C ATOM 172 CH2 TRP A 29 14.733 39.357 44.945 1.00190.82 C ANISOU 172 CH2 TRP A 29 22260 19693 30552 1970 3146 149 C ATOM 173 N ALA A 30 18.663 39.231 38.424 1.00135.14 N ANISOU 173 N ALA A 30 14951 11389 25008 610 2382 -1040 N ATOM 174 CA ALA A 30 19.618 40.318 38.237 1.00134.49 C ANISOU 174 CA ALA A 30 15045 11117 24939 637 2369 -1485 C ATOM 175 C ALA A 30 19.480 40.954 36.858 1.00140.73 C ANISOU 175 C ALA A 30 15756 11769 25945 468 2433 -1549 C ATOM 176 O ALA A 30 19.703 42.153 36.693 1.00147.67 O ANISOU 176 O ALA A 30 16773 12547 26787 556 2542 -1787 O ATOM 177 CB ALA A 30 21.037 39.817 38.451 1.00127.64 C ANISOU 177 CB ALA A 30 14271 10104 24123 524 2108 -1840 C ATOM 178 N VAL A 31 19.115 40.144 35.870 1.00137.16 N ANISOU 178 N VAL A 31 15090 11312 25713 217 2365 -1336 N ATOM 179 CA VAL A 31 18.918 40.637 34.512 1.00135.57 C ANISOU 179 CA VAL A 31 14792 10999 25722 33 2418 -1357 C ATOM 180 C VAL A 31 17.623 41.433 34.406 1.00143.95 C ANISOU 180 C VAL A 31 15802 12204 26691 212 2687 -1070 C ATOM 181 O VAL A 31 17.528 42.384 33.631 1.00148.35 O ANISOU 181 O VAL A 31 16384 12660 27323 193 2787 -1171 O ATOM 182 CB VAL A 31 18.896 39.484 33.489 1.00129.60 C ANISOU 182 CB VAL A 31 13812 10206 25224 -301 2266 -1209 C ATOM 183 CG1 VAL A 31 18.471 39.992 32.119 1.00127.44 C ANISOU 183 CG1 VAL A 31 13417 9863 25143 -476 2349 -1160 C ATOM 184 CG2 VAL A 31 20.259 38.814 33.416 1.00125.62 C ANISOU 184 CG2 VAL A 31 13359 9529 24844 -486 1998 -1540 C ATOM 185 N TRP A 32 16.628 41.044 35.196 1.00146.77 N ANISOU 185 N TRP A 32 16088 12801 26878 388 2802 -712 N ATOM 186 CA TRP A 32 15.330 41.708 35.170 1.00149.38 C ANISOU 186 CA TRP A 32 16346 13304 27106 576 3058 -413 C ATOM 187 C TRP A 32 15.360 43.031 35.934 1.00152.04 C ANISOU 187 C TRP A 32 16909 13629 27229 897 3231 -599 C ATOM 188 O TRP A 32 14.565 43.930 35.661 1.00160.99 O ANISOU 188 O TRP A 32 18032 14815 28322 1046 3437 -483 O ATOM 189 CB TRP A 32 14.243 40.788 35.730 1.00150.22 C ANISOU 189 CB TRP A 32 16284 13688 27102 634 3123 35 C ATOM 190 CG TRP A 32 12.849 41.291 35.499 1.00148.99 C ANISOU 190 CG TRP A 32 15991 13735 26882 774 3368 377 C ATOM 191 CD1 TRP A 32 12.280 41.607 34.299 1.00143.75 C ANISOU 191 CD1 TRP A 32 15172 13062 26384 649 3443 503 C ATOM 192 CD2 TRP A 32 11.842 41.519 36.492 1.00154.91 C ANISOU 192 CD2 TRP A 32 16737 14744 27380 1067 3568 638 C ATOM 193 NE1 TRP A 32 10.985 42.026 34.483 1.00146.43 N ANISOU 193 NE1 TRP A 32 15407 13639 26591 857 3674 827 N ATOM 194 CE2 TRP A 32 10.690 41.980 35.822 1.00154.76 C ANISOU 194 CE2 TRP A 32 16549 14862 27389 1114 3757 912 C ATOM 195 CE3 TRP A 32 11.801 41.383 37.884 1.00160.46 C ANISOU 195 CE3 TRP A 32 17558 15582 27829 1293 3605 666 C ATOM 196 CZ2 TRP A 32 9.513 42.305 36.493 1.00161.37 C ANISOU 196 CZ2 TRP A 32 17327 15970 28015 1384 3982 1202 C ATOM 197 CZ3 TRP A 32 10.631 41.706 38.549 1.00166.24 C ANISOU 197 CZ3 TRP A 32 18235 16578 28350 1549 3832 954 C ATOM 198 CH2 TRP A 32 9.504 42.161 37.854 1.00166.03 C ANISOU 198 CH2 TRP A 32 18035 16687 28362 1595 4019 1215 C ATOM 199 N LEU A 33 16.280 43.145 36.887 1.00148.01 N ANISOU 199 N LEU A 33 16604 13050 26581 1004 3146 -889 N ATOM 200 CA LEU A 33 16.422 44.367 37.671 1.00149.50 C ANISOU 200 CA LEU A 33 17028 13216 26559 1292 3299 -1103 C ATOM 201 C LEU A 33 17.323 45.376 36.970 1.00143.99 C ANISOU 201 C LEU A 33 16492 12250 25969 1210 3275 -1513 C ATOM 202 O LEU A 33 16.909 46.497 36.671 1.00148.35 O ANISOU 202 O LEU A 33 17123 12754 26490 1342 3461 -1542 O ATOM 203 CB LEU A 33 16.984 44.057 39.060 1.00150.21 C ANISOU 203 CB LEU A 33 17269 13374 26430 1443 3226 -1229 C ATOM 204 CG LEU A 33 16.138 43.182 39.984 1.00148.60 C ANISOU 204 CG LEU A 33 16958 13440 26062 1563 3267 -852 C ATOM 205 CD1 LEU A 33 16.831 43.006 41.326 1.00144.28 C ANISOU 205 CD1 LEU A 33 16592 12933 25296 1710 3186 -1029 C ATOM 206 CD2 LEU A 33 14.751 43.776 40.167 1.00154.81 C ANISOU 206 CD2 LEU A 33 17675 14429 26716 1794 3544 -532 C ATOM 207 N ASN A 34 18.562 44.969 36.714 1.00181.32 N ANISOU 207 N ASN A 34 21446 13440 34008 2564 1570 -1451 N ATOM 208 CA ASN A 34 19.544 45.839 36.082 1.00172.33 C ANISOU 208 CA ASN A 34 20040 12518 32919 2431 1399 -1124 C ATOM 209 C ASN A 34 19.380 45.865 34.565 1.00168.94 C ANISOU 209 C ASN A 34 19507 12228 32452 2399 1354 -866 C ATOM 210 O ASN A 34 19.624 44.868 33.886 1.00166.01 O ANISOU 210 O ASN A 34 19212 12106 31757 2558 1488 -789 O ATOM 211 CB ASN A 34 20.959 45.399 36.463 1.00167.42 C ANISOU 211 CB ASN A 34 19384 12237 31991 2538 1458 -1030 C ATOM 212 CG ASN A 34 22.008 46.424 36.090 1.00168.48 C ANISOU 212 CG ASN A 34 19241 12555 32217 2384 1270 -728 C ATOM 213 OD1 ASN A 34 21.779 47.285 35.242 1.00170.68 O ANISOU 213 OD1 ASN A 34 19348 12788 32716 2224 1113 -533 O ATOM 214 ND2 ASN A 34 23.170 46.338 36.726 1.00168.86 N ANISOU 214 ND2 ASN A 34 19245 12815 32100 2433 1284 -687 N ATOM 215 N SER A 35 18.965 47.012 34.039 1.00169.20 N ANISOU 215 N SER A 35 19367 12101 32821 2193 1164 -733 N ATOM 216 CA SER A 35 18.726 47.160 32.607 1.00163.51 C ANISOU 216 CA SER A 35 18538 11479 32109 2141 1103 -492 C ATOM 217 C SER A 35 20.028 47.194 31.810 1.00155.75 C ANISOU 217 C SER A 35 17371 10900 30905 2150 1055 -157 C ATOM 218 O SER A 35 20.017 47.107 30.582 1.00153.91 O ANISOU 218 O SER A 35 17060 10822 30596 2145 1034 60 O ATOM 219 CB SER A 35 17.898 48.417 32.327 1.00149.09 C ANISOU 219 CB SER A 35 16577 9351 30718 1912 910 -454 C ATOM 220 OG SER A 35 18.520 49.569 32.867 1.00181.18 O ANISOU 220 OG SER A 35 20453 13374 35013 1743 735 -369 O ATOM 221 N ASN A 36 21.147 47.320 32.516 1.00153.99 N ANISOU 221 N ASN A 36 17082 10847 30582 2163 1039 -118 N ATOM 222 CA ASN A 36 22.457 47.324 31.878 1.00159.55 C ANISOU 222 CA ASN A 36 17618 11941 31064 2179 1000 186 C ATOM 223 C ASN A 36 22.907 45.913 31.516 1.00164.37 C ANISOU 223 C ASN A 36 18372 12857 31226 2415 1205 199 C ATOM 224 O ASN A 36 23.972 45.720 30.929 1.00163.68 O ANISOU 224 O ASN A 36 18171 13115 30903 2460 1203 443 O ATOM 225 CB ASN A 36 23.492 47.995 32.784 1.00160.92 C ANISOU 225 CB ASN A 36 17665 12180 31298 2103 905 221 C ATOM 226 CG ASN A 36 23.191 49.462 33.024 1.00160.21 C ANISOU 226 CG ASN A 36 17400 11829 31644 1858 686 256 C ATOM 227 OD1 ASN A 36 22.773 50.178 32.115 1.00161.82 O ANISOU 227 OD1 ASN A 36 17466 11963 32054 1717 553 423 O ATOM 228 ND2 ASN A 36 23.407 49.918 34.253 1.00153.66 N ANISOU 228 ND2 ASN A 36 16574 10853 30955 1807 646 98 N ATOM 229 N LEU A 37 22.083 44.933 31.872 1.00167.11 N ANISOU 229 N LEU A 37 18967 13070 31457 2566 1382 -64 N ATOM 230 CA LEU A 37 22.368 43.532 31.585 1.00164.57 C ANISOU 230 CA LEU A 37 18807 13004 30717 2798 1591 -87 C ATOM 231 C LEU A 37 21.331 42.955 30.630 1.00158.68 C ANISOU 231 C LEU A 37 18170 12187 29933 2858 1669 -106 C ATOM 232 O LEU A 37 21.331 41.757 30.353 1.00158.60 O ANISOU 232 O LEU A 37 18319 12341 29600 3051 1850 -155 O ATOM 233 CB LEU A 37 22.385 42.716 32.879 1.00165.93 C ANISOU 233 CB LEU A 37 19198 13114 30735 2954 1756 -390 C ATOM 234 CG LEU A 37 23.485 43.042 33.889 1.00169.31 C ANISOU 234 CG LEU A 37 19553 13648 31129 2938 1717 -393 C ATOM 235 CD1 LEU A 37 23.225 42.349 35.217 1.00146.66 C ANISOU 235 CD1 LEU A 37 16912 10633 28179 3069 1869 -731 C ATOM 236 CD2 LEU A 37 24.848 42.660 33.334 1.00148.76 C ANISOU 236 CD2 LEU A 37 16843 11481 28200 3020 1741 -129 C ATOM 237 N GLN A 38 20.447 43.812 30.130 1.00156.72 N ANISOU 237 N GLN A 38 17837 11695 30015 2691 1533 -69 N ATOM 238 CA GLN A 38 19.356 43.367 29.270 1.00156.42 C ANISOU 238 CA GLN A 38 17900 11548 29986 2729 1595 -103 C ATOM 239 C GLN A 38 19.699 43.467 27.786 1.00158.09 C ANISOU 239 C GLN A 38 17953 12009 30104 2697 1531 227 C ATOM 240 O GLN A 38 18.815 43.638 26.948 1.00159.46 O ANISOU 240 O GLN A 38 18118 12053 30415 2638 1493 269 O ATOM 241 CB GLN A 38 18.082 44.159 29.568 1.00155.23 C ANISOU 241 CB GLN A 38 17768 10970 30242 2577 1498 -273 C ATOM 242 CG GLN A 38 17.576 44.005 30.991 1.00156.72 C ANISOU 242 CG GLN A 38 18133 10882 30531 2614 1571 -619 C ATOM 243 CD GLN A 38 16.286 44.760 31.235 1.00162.64 C ANISOU 243 CD GLN A 38 18905 11212 31679 2466 1478 -785 C ATOM 244 OE1 GLN A 38 15.778 45.447 30.348 1.00163.74 O ANISOU 244 OE1 GLN A 38 18921 11261 32031 2329 1352 -637 O ATOM 245 NE2 GLN A 38 15.748 44.637 32.442 1.00165.98 N ANISOU 245 NE2 GLN A 38 19486 11374 32205 2494 1541 -1093 N ATOM 246 N ASN A 39 20.984 43.359 27.465 1.00159.44 N ANISOU 246 N ASN A 39 18000 12538 30042 2736 1519 460 N ATOM 247 CA ASN A 39 21.418 43.380 26.073 1.00165.64 C ANISOU 247 CA ASN A 39 18638 13593 30705 2720 1469 779 C ATOM 248 C ASN A 39 20.996 42.114 25.331 1.00171.04 C ANISOU 248 C ASN A 39 19494 14404 31091 2909 1653 750 C ATOM 249 O ASN A 39 20.624 41.117 25.950 1.00169.06 O ANISOU 249 O ASN A 39 19473 14098 30666 3076 1834 501 O ATOM 250 CB ASN A 39 22.932 43.589 25.979 1.00168.41 C ANISOU 250 CB ASN A 39 18813 14295 30881 2715 1411 1029 C ATOM 251 CG ASN A 39 23.711 42.606 26.829 1.00170.80 C ANISOU 251 CG ASN A 39 19255 14788 30851 2906 1579 902 C ATOM 252 OD1 ASN A 39 23.290 41.466 27.023 1.00175.58 O ANISOU 252 OD1 ASN A 39 20084 15393 31233 3088 1770 712 O ATOM 253 ND2 ASN A 39 24.857 43.041 27.337 1.00170.80 N ANISOU 253 ND2 ASN A 39 19125 14954 30818 2865 1508 1008 N ATOM 254 N VAL A 40 21.049 42.161 24.004 1.00177.20 N ANISOU 254 N VAL A 40 20162 15350 31814 2883 1607 1006 N ATOM 255 CA VAL A 40 20.623 41.034 23.180 1.00177.73 C ANISOU 255 CA VAL A 40 20375 15538 31616 3048 1766 1003 C ATOM 256 C VAL A 40 21.408 39.768 23.510 1.00177.83 C ANISOU 256 C VAL A 40 20531 15837 31200 3278 1964 949 C ATOM 257 O VAL A 40 20.873 38.661 23.448 1.00175.61 O ANISOU 257 O VAL A 40 20459 15557 30710 3449 2144 792 O ATOM 258 CB VAL A 40 20.769 41.345 21.678 1.00181.43 C ANISOU 258 CB VAL A 40 20671 16189 32074 2978 1672 1326 C ATOM 259 CG1 VAL A 40 20.245 40.188 20.843 1.00174.67 C ANISOU 259 CG1 VAL A 40 19973 15434 30959 3146 1837 1308 C ATOM 260 CG2 VAL A 40 20.033 42.631 21.331 1.00188.76 C ANISOU 260 CG2 VAL A 40 21448 16843 33429 2746 1470 1391 C ATOM 261 N THR A 41 22.676 39.940 23.867 1.00131.02 N ANISOU 261 N THR A 41 18063 11145 20574 -40 2053 1594 N ATOM 262 CA THR A 41 23.546 38.817 24.198 1.00137.79 C ANISOU 262 CA THR A 41 18850 11964 21541 32 2607 1792 C ATOM 263 C THR A 41 22.999 38.000 25.362 1.00134.44 C ANISOU 263 C THR A 41 18013 11880 21188 128 2582 1764 C ATOM 264 O THR A 41 22.996 36.771 25.321 1.00139.96 O ANISOU 264 O THR A 41 18864 12502 21812 86 2936 1842 O ATOM 265 CB THR A 41 24.965 39.294 24.563 1.00146.70 C ANISOU 265 CB THR A 41 19716 13093 22930 199 2872 1958 C ATOM 266 OG1 THR A 41 25.508 40.064 23.483 1.00153.98 O ANISOU 266 OG1 THR A 41 21029 13690 23787 101 2915 1983 O ATOM 267 CG2 THR A 41 25.873 38.105 24.847 1.00146.67 C ANISOU 267 CG2 THR A 41 19669 13037 23022 283 3451 2157 C ATOM 268 N ASN A 42 22.536 38.689 26.400 1.00127.65 N ANISOU 268 N ASN A 42 16639 11393 20468 257 2166 1652 N ATOM 269 CA ASN A 42 22.072 38.021 27.611 1.00128.31 C ANISOU 269 CA ASN A 42 16283 11825 20645 366 2127 1625 C ATOM 270 C ASN A 42 20.690 37.386 27.481 1.00133.31 C ANISOU 270 C ASN A 42 17083 12518 21051 208 1916 1453 C ATOM 271 O ASN A 42 20.223 36.713 28.400 1.00131.64 O ANISOU 271 O ASN A 42 16570 12566 20883 267 1911 1422 O ATOM 272 CB ASN A 42 22.119 38.973 28.808 1.00128.06 C ANISOU 272 CB ASN A 42 15623 12178 20857 566 1773 1572 C ATOM 273 CG ASN A 42 23.537 39.300 29.232 1.00132.67 C ANISOU 273 CG ASN A 42 15937 12772 21700 755 2063 1755 C ATOM 274 OD1 ASN A 42 24.501 38.842 28.619 1.00137.49 O ANISOU 274 OD1 ASN A 42 16829 13102 22310 737 2525 1918 O ATOM 275 ND2 ASN A 42 23.672 40.095 30.287 1.00132.20 N ANISOU 275 ND2 ASN A 42 15324 13042 21864 938 1792 1721 N ATOM 276 N TYR A 43 20.038 37.599 26.343 1.00138.66 N ANISOU 276 N TYR A 43 18245 12956 21483 8 1747 1336 N ATOM 277 CA TYR A 43 18.786 36.910 26.059 1.00137.22 C ANISOU 277 CA TYR A 43 18287 12787 21064 -164 1603 1172 C ATOM 278 C TYR A 43 19.036 35.409 26.008 1.00127.76 C ANISOU 278 C TYR A 43 17280 11459 19805 -215 2128 1305 C ATOM 279 O TYR A 43 18.210 34.614 26.457 1.00127.15 O ANISOU 279 O TYR A 43 17122 11542 19648 -268 2098 1213 O ATOM 280 CB TYR A 43 18.180 37.393 24.741 1.00145.07 C ANISOU 280 CB TYR A 43 19810 13508 21801 -361 1373 1038 C ATOM 281 CG TYR A 43 17.384 38.671 24.867 1.00148.84 C ANISOU 281 CG TYR A 43 20113 14179 22262 -344 746 824 C ATOM 282 CD1 TYR A 43 15.997 38.643 24.935 1.00150.62 C ANISOU 282 CD1 TYR A 43 20325 14582 22320 -442 334 580 C ATOM 283 CD2 TYR A 43 18.017 39.904 24.924 1.00145.89 C ANISOU 283 CD2 TYR A 43 19587 13812 22033 -229 568 860 C ATOM 284 CE1 TYR A 43 15.264 39.809 25.051 1.00149.66 C ANISOU 284 CE1 TYR A 43 20046 14642 22178 -416 -246 379 C ATOM 285 CE2 TYR A 43 17.293 41.075 25.041 1.00146.28 C ANISOU 285 CE2 TYR A 43 19489 14032 22060 -207 -5 666 C ATOM 286 CZ TYR A 43 15.917 41.022 25.104 1.00148.59 C ANISOU 286 CZ TYR A 43 19772 14501 22185 -295 -415 428 C ATOM 287 OH TYR A 43 15.190 42.184 25.221 1.00150.30 O ANISOU 287 OH TYR A 43 19842 14892 22372 -263 -992 229 O ATOM 288 N PHE A 44 20.188 35.031 25.464 1.00122.06 N ANISOU 288 N PHE A 44 16812 10445 19119 -199 2613 1517 N ATOM 289 CA PHE A 44 20.579 33.630 25.389 1.00119.77 C ANISOU 289 CA PHE A 44 16718 10009 18782 -228 3148 1667 C ATOM 290 C PHE A 44 21.023 33.118 26.755 1.00122.00 C ANISOU 290 C PHE A 44 16481 10585 19287 -15 3328 1771 C ATOM 291 O PHE A 44 20.748 31.975 27.116 1.00127.11 O ANISOU 291 O PHE A 44 17142 11278 19877 -34 3567 1798 O ATOM 292 CB PHE A 44 21.696 33.437 24.362 1.00119.70 C ANISOU 292 CB PHE A 44 17142 9595 18743 -271 3601 1856 C ATOM 293 CG PHE A 44 21.316 33.851 22.968 1.00128.47 C ANISOU 293 CG PHE A 44 18807 10383 19621 -481 3472 1770 C ATOM 294 CD1 PHE A 44 21.864 34.985 22.394 1.00133.79 C ANISOU 294 CD1 PHE A 44 19587 10907 20339 -470 3343 1785 C ATOM 295 CD2 PHE A 44 20.404 33.109 22.236 1.00132.96 C ANISOU 295 CD2 PHE A 44 19797 10797 19922 -690 3479 1668 C ATOM 296 CE1 PHE A 44 21.516 35.369 21.112 1.00136.33 C ANISOU 296 CE1 PHE A 44 20438 10924 20438 -656 3225 1706 C ATOM 297 CE2 PHE A 44 20.050 33.488 20.954 1.00137.58 C ANISOU 297 CE2 PHE A 44 20899 11088 20288 -873 3355 1584 C ATOM 298 CZ PHE A 44 20.608 34.620 20.392 1.00138.69 C ANISOU 298 CZ PHE A 44 21150 11075 20471 -852 3226 1606 C ATOM 299 N VAL A 45 21.707 33.971 27.512 1.00119.27 N ANISOU 299 N VAL A 45 15687 10437 19192 189 3212 1825 N ATOM 300 CA VAL A 45 22.144 33.615 28.857 1.00118.00 C ANISOU 300 CA VAL A 45 14999 10578 19255 414 3340 1915 C ATOM 301 C VAL A 45 20.948 33.247 29.727 1.00117.06 C ANISOU 301 C VAL A 45 14606 10778 19093 401 3052 1753 C ATOM 302 O VAL A 45 21.040 32.375 30.591 1.00120.58 O ANISOU 302 O VAL A 45 14824 11382 19610 506 3277 1823 O ATOM 303 CB VAL A 45 22.932 34.759 29.522 1.00114.34 C ANISOU 303 CB VAL A 45 14077 10304 19062 624 3174 1959 C ATOM 304 CG1 VAL A 45 23.267 34.409 30.965 1.00108.27 C ANISOU 304 CG1 VAL A 45 12745 9876 18517 863 3259 2030 C ATOM 305 CG2 VAL A 45 24.196 35.059 28.733 1.00112.51 C ANISOU 305 CG2 VAL A 45 14092 9768 18888 642 3507 2122 C ATOM 306 N VAL A 46 19.824 33.915 29.492 1.00115.54 N ANISOU 306 N VAL A 46 14444 10678 18779 273 2555 1531 N ATOM 307 CA VAL A 46 18.590 33.602 30.201 1.00117.06 C ANISOU 307 CA VAL A 46 14413 11161 18905 227 2256 1347 C ATOM 308 C VAL A 46 18.095 32.213 29.809 1.00125.24 C ANISOU 308 C VAL A 46 15818 12041 19728 60 2573 1345 C ATOM 309 O VAL A 46 17.664 31.434 30.659 1.00126.17 O ANISOU 309 O VAL A 46 15715 12365 19859 92 2641 1319 O ATOM 310 CB VAL A 46 17.490 34.639 29.911 1.00110.84 C ANISOU 310 CB VAL A 46 13618 10485 18012 118 1651 1095 C ATOM 311 CG1 VAL A 46 16.184 34.227 30.574 1.00109.17 C ANISOU 311 CG1 VAL A 46 13205 10561 17714 49 1369 890 C ATOM 312 CG2 VAL A 46 17.923 36.016 30.387 1.00106.92 C ANISOU 312 CG2 VAL A 46 12734 10165 17727 288 1321 1089 C ATOM 313 N SER A 47 18.161 31.908 28.516 1.00126.76 N ANISOU 313 N SER A 47 16581 11862 19721 -122 2772 1372 N ATOM 314 CA SER A 47 17.787 30.590 28.022 1.00127.68 C ANISOU 314 CA SER A 47 17096 11787 19629 -291 3111 1384 C ATOM 315 C SER A 47 18.655 29.529 28.687 1.00137.87 C ANISOU 315 C SER A 47 18268 13079 21037 -147 3633 1601 C ATOM 316 O SER A 47 18.183 28.442 29.018 1.00143.24 O ANISOU 316 O SER A 47 18996 13803 21624 -206 3825 1586 O ATOM 317 CB SER A 47 17.937 30.521 26.502 1.00125.72 C ANISOU 317 CB SER A 47 17474 11118 19175 -481 3273 1411 C ATOM 318 OG SER A 47 17.581 29.240 26.011 1.00130.31 O ANISOU 318 OG SER A 47 18446 11511 19553 -648 3606 1423 O ATOM 319 N LEU A 48 19.928 29.858 28.879 1.00140.66 N ANISOU 319 N LEU A 48 18470 13382 21592 43 3863 1797 N ATOM 320 CA LEU A 48 20.852 28.980 29.585 1.00142.31 C ANISOU 320 CA LEU A 48 18516 13618 21938 224 4332 2004 C ATOM 321 C LEU A 48 20.417 28.817 31.035 1.00138.95 C ANISOU 321 C LEU A 48 17554 13596 21645 376 4166 1945 C ATOM 322 O LEU A 48 20.463 27.718 31.587 1.00142.49 O ANISOU 322 O LEU A 48 17975 14086 22079 425 4480 2021 O ATOM 323 CB LEU A 48 22.274 29.542 29.530 1.00145.61 C ANISOU 323 CB LEU A 48 18828 13940 22559 407 4546 2193 C ATOM 324 CG LEU A 48 23.316 28.812 30.381 1.00149.75 C ANISOU 324 CG LEU A 48 19100 14539 23259 643 4982 2397 C ATOM 325 CD1 LEU A 48 23.463 27.367 29.925 1.00151.89 C ANISOU 325 CD1 LEU A 48 19791 14556 23363 557 5491 2512 C ATOM 326 CD2 LEU A 48 24.654 29.533 30.333 1.00151.52 C ANISOU 326 CD2 LEU A 48 19176 14702 23692 818 5126 2545 C ATOM 327 N ALA A 49 19.996 29.919 31.644 1.00133.62 N ANISOU 327 N ALA A 49 16465 13211 21094 450 3671 1809 N ATOM 328 CA ALA A 49 19.538 29.902 33.027 1.00133.15 C ANISOU 328 CA ALA A 49 15873 13550 21167 593 3460 1736 C ATOM 329 C ALA A 49 18.302 29.023 33.184 1.00134.37 C ANISOU 329 C ALA A 49 16141 13787 21127 421 3401 1581 C ATOM 330 O ALA A 49 18.314 28.057 33.943 1.00139.04 O ANISOU 330 O ALA A 49 16611 14481 21737 493 3660 1644 O ATOM 331 CB ALA A 49 19.255 31.313 33.511 1.00134.18 C ANISOU 331 CB ALA A 49 15583 13952 21446 679 2914 1604 C ATOM 332 N ALA A 50 17.239 29.363 32.461 1.00131.50 N ANISOU 332 N ALA A 50 16017 13376 20573 195 3062 1373 N ATOM 333 CA ALA A 50 15.998 28.596 32.509 1.00130.98 C ANISOU 333 CA ALA A 50 16075 13384 20307 4 2979 1193 C ATOM 334 C ALA A 50 16.269 27.109 32.314 1.00131.50 C ANISOU 334 C ALA A 50 16475 13235 20252 -59 3540 1330 C ATOM 335 O ALA A 50 15.753 26.270 33.053 1.00128.87 O ANISOU 335 O ALA A 50 16018 13061 19884 -70 3636 1286 O ATOM 336 CB ALA A 50 15.022 29.099 31.458 1.00130.63 C ANISOU 336 CB ALA A 50 16360 13226 20048 -237 2624 977 C ATOM 337 N ALA A 51 17.087 26.791 31.316 1.00129.72 N ANISOU 337 N ALA A 51 16682 12645 19960 -102 3915 1495 N ATOM 338 CA ALA A 51 17.458 25.410 31.040 1.00122.83 C ANISOU 338 CA ALA A 51 16160 11535 18972 -154 4472 1644 C ATOM 339 C ALA A 51 18.167 24.790 32.238 1.00123.23 C ANISOU 339 C ALA A 51 15866 11755 19202 91 4776 1811 C ATOM 340 O ALA A 51 17.826 23.692 32.671 1.00129.00 O ANISOU 340 O ALA A 51 16652 12515 19845 58 5019 1818 O ATOM 341 CB ALA A 51 18.340 25.335 29.802 1.00117.61 C ANISOU 341 CB ALA A 51 15975 10467 18243 -211 4800 1802 C ATOM 342 N ASP A 52 19.150 25.505 32.775 1.00121.94 N ANISOU 342 N ASP A 52 15348 11701 19284 340 4761 1940 N ATOM 343 CA ASP A 52 19.938 25.003 33.896 1.00125.75 C ANISOU 343 CA ASP A 52 15490 12340 19948 604 5045 2106 C ATOM 344 C ASP A 52 19.198 25.100 35.230 1.00117.59 C ANISOU 344 C ASP A 52 13956 11714 19008 698 4743 1978 C ATOM 345 O ASP A 52 19.688 24.623 36.254 1.00117.79 O ANISOU 345 O ASP A 52 13691 11898 19167 913 4949 2092 O ATOM 346 CB ASP A 52 21.285 25.727 33.978 1.00133.62 C ANISOU 346 CB ASP A 52 16282 13311 21174 837 5148 2281 C ATOM 347 CG ASP A 52 22.229 25.333 32.855 1.00141.01 C ANISOU 347 CG ASP A 52 17692 13847 22037 789 5587 2454 C ATOM 348 OD1 ASP A 52 21.798 24.593 31.945 1.00146.58 O ANISOU 348 OD1 ASP A 52 18897 14288 22510 566 5773 2432 O ATOM 349 OD2 ASP A 52 23.402 25.763 32.882 1.00139.32 O ANISOU 349 OD2 ASP A 52 17349 13587 21999 972 5749 2605 O ATOM 350 N ILE A 53 18.023 25.721 35.217 1.00113.47 N ANISOU 350 N ILE A 53 13337 11362 18416 544 4252 1737 N ATOM 351 CA ILE A 53 17.177 25.762 36.404 1.00116.07 C ANISOU 351 CA ILE A 53 13229 12068 18803 593 3955 1589 C ATOM 352 C ILE A 53 16.328 24.501 36.461 1.00117.68 C ANISOU 352 C ILE A 53 13678 12237 18797 416 4156 1510 C ATOM 353 O ILE A 53 16.186 23.880 37.515 1.00119.78 O ANISOU 353 O ILE A 53 13694 12703 19113 519 4264 1524 O ATOM 354 CB ILE A 53 16.250 26.992 36.414 1.00118.42 C ANISOU 354 CB ILE A 53 13292 12586 19116 510 3324 1348 C ATOM 355 CG1 ILE A 53 17.061 28.272 36.607 1.00107.23 C ANISOU 355 CG1 ILE A 53 11549 11261 17932 712 3101 1419 C ATOM 356 CG2 ILE A 53 15.214 26.869 37.520 1.00120.29 C ANISOU 356 CG2 ILE A 53 13152 13186 19367 508 3040 1168 C ATOM 357 CD1 ILE A 53 16.225 29.531 36.591 1.00 94.97 C ANISOU 357 CD1 ILE A 53 9778 9909 16395 647 2484 1195 C ATOM 358 N LEU A 54 15.771 24.126 35.314 1.00119.63 N ANISOU 358 N LEU A 54 14426 12225 18804 146 4211 1424 N ATOM 359 CA LEU A 54 14.945 22.931 35.212 1.00119.41 C ANISOU 359 CA LEU A 54 14685 12130 18555 -57 4414 1335 C ATOM 360 C LEU A 54 15.745 21.671 35.523 1.00111.56 C ANISOU 360 C LEU A 54 13843 10988 17557 54 5010 1563 C ATOM 361 O LEU A 54 15.175 20.603 35.731 1.00103.78 O ANISOU 361 O LEU A 54 13021 9988 16423 -63 5223 1517 O ATOM 362 CB LEU A 54 14.318 22.829 33.821 1.00119.22 C ANISOU 362 CB LEU A 54 15187 11830 18280 -356 4373 1213 C ATOM 363 CG LEU A 54 13.345 23.947 33.449 1.00107.78 C ANISOU 363 CG LEU A 54 13648 10519 16783 -493 3779 953 C ATOM 364 CD1 LEU A 54 12.836 23.766 32.028 1.00108.39 C ANISOU 364 CD1 LEU A 54 14284 10294 16605 -770 3789 852 C ATOM 365 CD2 LEU A 54 12.189 23.996 34.437 1.00 97.34 C ANISOU 365 CD2 LEU A 54 11950 9573 15464 -533 3424 720 C ATOM 366 N VAL A 55 17.067 21.799 35.546 1.00109.38 N ANISOU 366 N VAL A 55 13521 10600 17440 280 5281 1802 N ATOM 367 CA VAL A 55 17.923 20.691 35.942 1.00111.53 C ANISOU 367 CA VAL A 55 13884 10758 17732 436 5827 2025 C ATOM 368 C VAL A 55 17.713 20.388 37.421 1.00118.78 C ANISOU 368 C VAL A 55 14355 12011 18766 613 5790 2010 C ATOM 369 O VAL A 55 17.413 19.255 37.794 1.00130.34 O ANISOU 369 O VAL A 55 15957 13454 20112 572 6078 2025 O ATOM 370 CB VAL A 55 19.412 20.988 35.681 1.00107.74 C ANISOU 370 CB VAL A 55 13407 10115 17414 657 6097 2268 C ATOM 371 CG1 VAL A 55 20.287 19.923 36.324 1.00103.81 C ANISOU 371 CG1 VAL A 55 12904 9574 16966 871 6609 2483 C ATOM 372 CG2 VAL A 55 19.682 21.075 34.186 1.00105.60 C ANISOU 372 CG2 VAL A 55 13646 9470 17005 473 6227 2306 C ATOM 373 N GLY A 56 17.860 21.408 38.259 1.00115.33 N ANISOU 373 N GLY A 56 13390 11876 18554 807 5435 1977 N ATOM 374 CA GLY A 56 17.653 21.252 39.687 1.00116.27 C ANISOU 374 CA GLY A 56 13050 12331 18796 985 5353 1954 C ATOM 375 C GLY A 56 16.182 21.164 40.046 1.00119.85 C ANISOU 375 C GLY A 56 13418 12994 19125 777 5024 1693 C ATOM 376 O GLY A 56 15.827 20.872 41.189 1.00117.10 O ANISOU 376 O GLY A 56 12751 12907 18835 874 4977 1649 O ATOM 377 N VAL A 57 15.324 21.414 39.063 1.00126.63 N ANISOU 377 N VAL A 57 14565 13738 19809 490 4798 1513 N ATOM 378 CA VAL A 57 13.882 21.401 39.278 1.00122.94 C ANISOU 378 CA VAL A 57 14033 13468 19213 269 4457 1236 C ATOM 379 C VAL A 57 13.246 20.089 38.823 1.00124.03 C ANISOU 379 C VAL A 57 14630 13409 19086 21 4786 1181 C ATOM 380 O VAL A 57 12.329 19.577 39.467 1.00125.55 O ANISOU 380 O VAL A 57 14721 13784 19198 -80 4723 1027 O ATOM 381 CB VAL A 57 13.197 22.581 38.555 1.00113.86 C ANISOU 381 CB VAL A 57 12868 12362 18031 111 3933 1029 C ATOM 382 CG1 VAL A 57 11.685 22.438 38.609 1.00111.35 C ANISOU 382 CG1 VAL A 57 12557 12209 17543 -145 3624 728 C ATOM 383 CG2 VAL A 57 13.634 23.902 39.165 1.00106.84 C ANISOU 383 CG2 VAL A 57 11475 11720 17400 342 3554 1044 C ATOM 384 N LEU A 58 13.741 19.543 37.716 1.00117.11 N ANISOU 384 N LEU A 58 14261 12160 18074 -80 5145 1306 N ATOM 385 CA LEU A 58 13.167 18.331 37.144 1.00107.86 C ANISOU 385 CA LEU A 58 13569 10771 16641 -331 5463 1255 C ATOM 386 C LEU A 58 14.221 17.274 36.826 1.00104.68 C ANISOU 386 C LEU A 58 13529 10052 16193 -243 6085 1527 C ATOM 387 O LEU A 58 14.112 16.132 37.267 1.00112.34 O ANISOU 387 O LEU A 58 14631 10988 17066 -258 6435 1573 O ATOM 388 CB LEU A 58 12.365 18.663 35.884 1.00104.84 C ANISOU 388 CB LEU A 58 13535 10232 16066 -633 5228 1063 C ATOM 389 CG LEU A 58 11.180 19.613 36.070 1.00102.99 C ANISOU 389 CG LEU A 58 13009 10291 15830 -755 4613 761 C ATOM 390 CD1 LEU A 58 10.484 19.867 34.743 1.00102.25 C ANISOU 390 CD1 LEU A 58 13311 10007 15530 -1035 4424 587 C ATOM 391 CD2 LEU A 58 10.204 19.055 37.092 1.00101.08 C ANISOU 391 CD2 LEU A 58 12532 10330 15545 -824 4537 587 C ATOM 392 N ALA A 59 15.238 17.659 36.062 1.00102.20 N ANISOU 392 N ALA A 59 13381 9506 15942 -150 6222 1702 N ATOM 393 CA ALA A 59 16.272 16.723 35.626 1.00107.73 C ANISOU 393 CA ALA A 59 14449 9888 16595 -73 6800 1955 C ATOM 394 C ALA A 59 16.896 15.945 36.783 1.00116.08 C ANISOU 394 C ALA A 59 15302 11051 17752 184 7141 2123 C ATOM 395 O ALA A 59 16.971 14.719 36.741 1.00123.44 O ANISOU 395 O ALA A 59 16556 11809 18538 140 7580 2210 O ATOM 396 CB ALA A 59 17.346 17.446 34.831 1.00106.23 C ANISOU 396 CB ALA A 59 14351 9499 16512 33 6844 2111 C ATOM 397 N ILE A 60 17.349 16.659 37.809 1.00117.20 N ANISOU 397 N ILE A 60 14918 11475 18137 458 6940 2169 N ATOM 398 CA ILE A 60 17.940 16.014 38.978 1.00118.25 C ANISOU 398 CA ILE A 60 14817 11736 18375 730 7223 2319 C ATOM 399 C ILE A 60 16.918 15.163 39.731 1.00118.45 C ANISOU 399 C ILE A 60 14828 11909 18269 616 7250 2185 C ATOM 400 O ILE A 60 17.196 14.011 40.058 1.00125.78 O ANISOU 400 O ILE A 60 15954 12728 19110 678 7689 2307 O ATOM 401 CB ILE A 60 18.595 17.028 39.937 1.00118.31 C ANISOU 401 CB ILE A 60 14238 12036 18677 1046 6966 2378 C ATOM 402 CG1 ILE A 60 19.783 17.712 39.259 1.00119.23 C ANISOU 402 CG1 ILE A 60 14386 11987 18928 1184 7039 2541 C ATOM 403 CG2 ILE A 60 19.042 16.339 41.217 1.00114.06 C ANISOU 403 CG2 ILE A 60 13448 11660 18230 1319 7219 2502 C ATOM 404 CD1 ILE A 60 20.514 18.693 40.151 1.00118.37 C ANISOU 404 CD1 ILE A 60 13716 12148 19109 1496 6820 2604 C ATOM 405 N PRO A 61 15.731 15.728 40.012 1.00114.32 N ANISOU 405 N PRO A 61 14075 11635 17726 449 6785 1928 N ATOM 406 CA PRO A 61 14.672 14.925 40.633 1.00114.41 C ANISOU 406 CA PRO A 61 14101 11776 17594 296 6806 1771 C ATOM 407 C PRO A 61 14.401 13.637 39.856 1.00108.39 C ANISOU 407 C PRO A 61 13932 10693 16559 60 7242 1788 C ATOM 408 O PRO A 61 14.256 12.576 40.463 1.00 98.67 O ANISOU 408 O PRO A 61 12797 9456 15235 70 7558 1823 O ATOM 409 CB PRO A 61 13.456 15.850 40.568 1.00111.15 C ANISOU 409 CB PRO A 61 13466 11598 17168 90 6224 1474 C ATOM 410 CG PRO A 61 14.036 17.217 40.613 1.00106.24 C ANISOU 410 CG PRO A 61 12477 11110 16778 280 5868 1513 C ATOM 411 CD PRO A 61 15.337 17.141 39.865 1.00105.88 C ANISOU 411 CD PRO A 61 12694 10758 16776 414 6218 1769 C ATOM 412 N PHE A 62 14.338 13.735 38.532 1.00113.93 N ANISOU 412 N PHE A 62 15032 11126 17131 -150 7261 1763 N ATOM 413 CA PHE A 62 14.123 12.566 37.687 1.00120.73 C ANISOU 413 CA PHE A 62 16475 11664 17735 -381 7670 1782 C ATOM 414 C PHE A 62 15.310 11.612 37.750 1.00132.95 C ANISOU 414 C PHE A 62 18260 12973 19284 -176 8254 2076 C ATOM 415 O PHE A 62 15.136 10.396 37.819 1.00140.32 O ANISOU 415 O PHE A 62 19506 13765 20045 -260 8646 2113 O ATOM 416 CB PHE A 62 13.872 12.981 36.235 1.00115.65 C ANISOU 416 CB PHE A 62 16189 10786 16968 -626 7541 1699 C ATOM 417 CG PHE A 62 12.560 13.679 36.019 1.00112.26 C ANISOU 417 CG PHE A 62 15643 10545 16468 -875 7020 1384 C ATOM 418 CD1 PHE A 62 11.403 13.212 36.618 1.00115.46 C ANISOU 418 CD1 PHE A 62 15960 11146 16761 -1045 6910 1165 C ATOM 419 CD2 PHE A 62 12.479 14.791 35.200 1.00106.42 C ANISOU 419 CD2 PHE A 62 14892 9779 15762 -941 6646 1299 C ATOM 420 CE1 PHE A 62 10.192 13.850 36.416 1.00112.51 C ANISOU 420 CE1 PHE A 62 15472 10957 16321 -1269 6427 862 C ATOM 421 CE2 PHE A 62 11.271 15.431 34.995 1.00105.67 C ANISOU 421 CE2 PHE A 62 14697 9860 15594 -1156 6160 1003 C ATOM 422 CZ PHE A 62 10.127 14.960 35.603 1.00108.38 C ANISOU 422 CZ PHE A 62 14936 10412 15832 -1318 6047 781 C ATOM 423 N ALA A 63 16.515 12.173 37.722 1.00132.93 N ANISOU 423 N ALA A 63 18109 12927 19472 93 8311 2279 N ATOM 424 CA ALA A 63 17.738 11.377 37.743 1.00133.71 C ANISOU 424 CA ALA A 63 18407 12808 19589 315 8843 2558 C ATOM 425 C ALA A 63 17.837 10.526 39.006 1.00140.95 C ANISOU 425 C ALA A 63 19162 13871 20523 507 9091 2632 C ATOM 426 O ALA A 63 18.241 9.365 38.953 1.00144.25 O ANISOU 426 O ALA A 63 19922 14072 20813 543 9582 2777 O ATOM 427 CB ALA A 63 18.959 12.275 37.607 1.00125.79 C ANISOU 427 CB ALA A 63 17187 11794 18813 577 8797 2727 C ATOM 428 N ILE A 64 17.470 11.112 40.141 1.00144.20 N ANISOU 428 N ILE A 64 19058 14644 21088 636 8750 2532 N ATOM 429 CA ILE A 64 17.511 10.404 41.414 1.00148.57 C ANISOU 429 CA ILE A 64 19421 15363 21666 827 8938 2587 C ATOM 430 C ILE A 64 16.439 9.323 41.459 1.00152.17 C ANISOU 430 C ILE A 64 20190 15758 21868 555 9106 2449 C ATOM 431 O ILE A 64 16.599 8.303 42.130 1.00157.74 O ANISOU 431 O ILE A 64 21000 16433 22502 660 9467 2543 O ATOM 432 CB ILE A 64 17.311 11.366 42.599 1.00154.37 C ANISOU 432 CB ILE A 64 19515 16510 22628 1015 8496 2496 C ATOM 433 CG1 ILE A 64 18.283 12.542 42.500 1.00165.88 C ANISOU 433 CG1 ILE A 64 20653 18038 24336 1251 8287 2603 C ATOM 434 CG2 ILE A 64 17.488 10.629 43.919 1.00150.89 C ANISOU 434 CG2 ILE A 64 18889 16223 22219 1247 8719 2578 C ATOM 435 CD1 ILE A 64 18.006 13.650 43.495 1.00169.93 C ANISOU 435 CD1 ILE A 64 20545 18950 25069 1394 7790 2489 C ATOM 436 N THR A 65 15.345 9.551 40.740 1.00152.15 N ANISOU 436 N THR A 65 20344 15739 21728 205 8845 2218 N ATOM 437 CA THR A 65 14.252 8.589 40.682 1.00157.03 C ANISOU 437 CA THR A 65 21263 16302 22099 -94 8978 2053 C ATOM 438 C THR A 65 14.609 7.413 39.782 1.00166.15 C ANISOU 438 C THR A 65 23037 17055 23036 -213 9517 2189 C ATOM 439 O THR A 65 14.456 6.253 40.165 1.00168.01 O ANISOU 439 O THR A 65 23509 17202 23123 -245 9892 2227 O ATOM 440 CB THR A 65 12.958 9.238 40.153 1.00154.30 C ANISOU 440 CB THR A 65 20881 16075 21671 -431 8512 1744 C ATOM 441 OG1 THR A 65 12.577 10.320 41.012 1.00153.32 O ANISOU 441 OG1 THR A 65 20180 16332 21741 -324 8003 1608 O ATOM 442 CG2 THR A 65 11.833 8.216 40.101 1.00156.93 C ANISOU 442 CG2 THR A 65 21519 16359 21747 -748 8666 1559 C ATOM 443 N ILE A 66 15.090 7.724 38.583 1.00169.14 N ANISOU 443 N ILE A 66 23684 17186 23396 -280 9556 2262 N ATOM 444 CA ILE A 66 15.417 6.705 37.594 1.00173.95 C ANISOU 444 CA ILE A 66 24891 17402 23799 -412 10035 2383 C ATOM 445 C ILE A 66 16.629 5.873 38.013 1.00181.45 C ANISOU 445 C ILE A 66 25961 18198 24783 -109 10551 2675 C ATOM 446 O ILE A 66 16.836 4.767 37.512 1.00186.42 O ANISOU 446 O ILE A 66 27074 18533 25225 -190 11013 2780 O ATOM 447 CB ILE A 66 15.677 7.336 36.210 1.00170.20 C ANISOU 447 CB ILE A 66 24654 16706 23309 -543 9927 2392 C ATOM 448 CG1 ILE A 66 15.675 6.265 35.118 1.00169.64 C ANISOU 448 CG1 ILE A 66 25226 16245 22986 -766 10364 2449 C ATOM 449 CG2 ILE A 66 16.985 8.113 36.212 1.00170.94 C ANISOU 449 CG2 ILE A 66 24520 16791 23638 -224 9914 2604 C ATOM 450 CD1 ILE A 66 15.878 6.819 33.726 1.00167.09 C ANISOU 450 CD1 ILE A 66 25174 15688 22626 -912 10274 2451 C ATOM 451 N SER A 67 17.425 6.409 38.933 1.00183.68 N ANISOU 451 N SER A 67 25803 18686 25302 246 10467 2802 N ATOM 452 CA SER A 67 18.613 5.711 39.412 1.00185.75 C ANISOU 452 CA SER A 67 26123 18839 25614 574 10919 3070 C ATOM 453 C SER A 67 18.227 4.408 40.099 1.00177.43 C ANISOU 453 C SER A 67 25278 17751 24384 554 11275 3079 C ATOM 454 O SER A 67 18.903 3.392 39.948 1.00179.15 O ANISOU 454 O SER A 67 25855 17719 24494 656 11772 3267 O ATOM 455 CB SER A 67 19.405 6.589 40.382 1.00191.92 C ANISOU 455 CB SER A 67 26337 19898 26687 951 10707 3164 C ATOM 456 OG SER A 67 18.775 6.640 41.650 1.00194.16 O ANISOU 456 OG SER A 67 26240 20503 27028 1024 10500 3050 O ATOM 457 N THR A 68 17.136 4.449 40.857 1.00167.10 N ANISOU 457 N THR A 68 23749 16695 23045 422 11019 2871 N ATOM 458 CA THR A 68 16.642 3.270 41.557 1.00167.90 C ANISOU 458 CA THR A 68 24034 16785 22974 374 11322 2848 C ATOM 459 C THR A 68 15.707 2.461 40.662 1.00170.07 C ANISOU 459 C THR A 68 24827 16828 22963 -41 11492 2705 C ATOM 460 O THR A 68 15.502 1.267 40.880 1.00175.05 O ANISOU 460 O THR A 68 25790 17318 23402 -109 11887 2735 O ATOM 461 CB THR A 68 15.905 3.652 42.855 1.00159.45 C ANISOU 461 CB THR A 68 22479 16102 22002 425 10987 2686 C ATOM 462 OG1 THR A 68 14.793 4.500 42.544 1.00153.06 O ANISOU 462 OG1 THR A 68 21483 15473 21200 137 10489 2410 O ATOM 463 CG2 THR A 68 16.843 4.381 43.805 1.00154.15 C ANISOU 463 CG2 THR A 68 21298 15664 21610 848 10844 2831 C ATOM 464 N GLY A 69 15.145 3.121 39.654 1.00210.86 N ANISOU 464 N GLY A 69 21848 19036 39235 -3042 4109 1059 N ATOM 465 CA GLY A 69 14.250 2.470 38.716 1.00198.92 C ANISOU 465 CA GLY A 69 20531 17496 37552 -3244 3886 1128 C ATOM 466 C GLY A 69 12.835 2.348 39.245 1.00184.22 C ANISOU 466 C GLY A 69 18642 15519 35833 -3355 3659 1469 C ATOM 467 O GLY A 69 12.622 2.090 40.429 1.00179.85 O ANISOU 467 O GLY A 69 17995 14822 35516 -3240 3607 1543 O ATOM 468 N PHE A 70 11.862 2.539 38.361 1.00175.13 N ANISOU 468 N PHE A 70 17571 14434 34537 -3581 3525 1679 N ATOM 469 CA PHE A 70 10.457 2.429 38.736 1.00168.10 C ANISOU 469 CA PHE A 70 16667 13444 33760 -3709 3300 2011 C ATOM 470 C PHE A 70 9.646 1.761 37.632 1.00164.21 C ANISOU 470 C PHE A 70 16387 12944 33062 -3920 3085 2046 C ATOM 471 O PHE A 70 10.205 1.257 36.659 1.00164.86 O ANISOU 471 O PHE A 70 16635 13078 32927 -3951 3101 1792 O ATOM 472 CB PHE A 70 9.875 3.806 39.068 1.00173.42 C ANISOU 472 CB PHE A 70 17130 14225 34535 -3774 3379 2363 C ATOM 473 CG PHE A 70 9.960 4.794 37.937 1.00175.16 C ANISOU 473 CG PHE A 70 17344 14666 34544 -3915 3499 2430 C ATOM 474 CD1 PHE A 70 11.071 5.609 37.792 1.00173.68 C ANISOU 474 CD1 PHE A 70 17056 14627 34308 -3814 3768 2280 C ATOM 475 CD2 PHE A 70 8.925 4.914 37.024 1.00175.28 C ANISOU 475 CD2 PHE A 70 17450 14740 34408 -4148 3345 2644 C ATOM 476 CE1 PHE A 70 11.151 6.520 36.755 1.00175.76 C ANISOU 476 CE1 PHE A 70 17312 15091 34377 -3942 3880 2343 C ATOM 477 CE2 PHE A 70 8.999 5.823 35.985 1.00177.12 C ANISOU 477 CE2 PHE A 70 17676 15176 34444 -4277 3455 2709 C ATOM 478 CZ PHE A 70 10.113 6.627 35.851 1.00177.90 C ANISOU 478 CZ PHE A 70 17676 15419 34498 -4174 3724 2559 C ATOM 479 N CYS A 71 8.327 1.760 37.791 1.00164.44 N ANISOU 479 N CYS A 71 16409 12909 33160 -4064 2884 2362 N ATOM 480 CA CYS A 71 7.442 1.143 36.811 1.00172.27 C ANISOU 480 CA CYS A 71 17593 13887 33974 -4272 2664 2426 C ATOM 481 C CYS A 71 6.469 2.156 36.220 1.00181.01 C ANISOU 481 C CYS A 71 18639 15132 35004 -4481 2628 2771 C ATOM 482 O CYS A 71 5.747 2.837 36.949 1.00183.89 O ANISOU 482 O CYS A 71 18842 15481 35546 -4502 2606 3077 O ATOM 483 CB CYS A 71 6.672 -0.021 37.439 1.00172.31 C ANISOU 483 CB CYS A 71 17687 13668 34113 -4269 2416 2467 C ATOM 484 SG CYS A 71 7.705 -1.406 37.967 1.00284.99 S ANISOU 484 SG CYS A 71 32073 27765 48443 -4050 2418 2053 S ATOM 485 N ALA A 72 6.455 2.248 34.895 1.00185.51 N ANISOU 485 N ALA A 72 19339 15838 35308 -4636 2622 2720 N ATOM 486 CA ALA A 72 5.558 3.158 34.193 1.00186.38 C ANISOU 486 CA ALA A 72 19412 16088 35315 -4845 2583 3028 C ATOM 487 C ALA A 72 5.534 2.845 32.702 1.00187.70 C ANISOU 487 C ALA A 72 19780 16363 35176 -5011 2525 2911 C ATOM 488 O ALA A 72 6.401 2.132 32.196 1.00189.81 O ANISOU 488 O ALA A 72 20188 16627 35306 -4948 2569 2576 O ATOM 489 CB ALA A 72 5.975 4.601 34.429 1.00183.84 C ANISOU 489 CB ALA A 72 18875 15925 35050 -4797 2823 3158 C ATOM 490 N ALA A 73 4.539 3.384 32.003 1.00186.37 N ANISOU 490 N ALA A 73 19621 16290 34901 -5224 2426 3188 N ATOM 491 CA ALA A 73 4.407 3.171 30.567 1.00186.46 C ANISOU 491 CA ALA A 73 19814 16413 34618 -5399 2363 3114 C ATOM 492 C ALA A 73 5.673 3.599 29.832 1.00184.62 C ANISOU 492 C ALA A 73 19597 16344 34204 -5336 2603 2847 C ATOM 493 O ALA A 73 6.600 4.132 30.438 1.00177.32 O ANISOU 493 O ALA A 73 18535 15453 33386 -5165 2818 2742 O ATOM 494 CB ALA A 73 3.199 3.925 30.029 1.00186.29 C ANISOU 494 CB ALA A 73 19758 16491 34533 -5622 2257 3483 C ATOM 495 N CYS A 74 5.708 3.365 28.524 1.00192.43 N ANISOU 495 N CYS A 74 20758 17439 34920 -5477 2565 2737 N ATOM 496 CA CYS A 74 6.875 3.717 27.723 1.00202.24 C ANISOU 496 CA CYS A 74 22033 18839 35968 -5433 2781 2479 C ATOM 497 C CYS A 74 7.016 5.232 27.581 1.00211.62 C ANISOU 497 C CYS A 74 23042 20220 37145 -5461 2983 2671 C ATOM 498 O CYS A 74 8.114 5.775 27.704 1.00213.78 O ANISOU 498 O CYS A 74 23225 20578 37422 -5324 3223 2503 O ATOM 499 CB CYS A 74 6.808 3.056 26.345 1.00205.49 C ANISOU 499 CB CYS A 74 22678 19311 36087 -5586 2677 2323 C ATOM 500 SG CYS A 74 8.353 3.142 25.404 1.00242.49 S ANISOU 500 SG CYS A 74 27447 24152 40537 -5508 2920 1927 S ATOM 501 N HIS A 75 5.901 5.909 27.324 1.00217.54 N ANISOU 501 N HIS A 75 23737 21035 37883 -5638 2886 3023 N ATOM 502 CA HIS A 75 5.903 7.362 27.193 1.00217.21 C ANISOU 502 CA HIS A 75 23521 21170 37837 -5680 3061 3240 C ATOM 503 C HIS A 75 6.372 8.041 28.477 1.00207.51 C ANISOU 503 C HIS A 75 22064 19906 36874 -5491 3232 3296 C ATOM 504 O HIS A 75 7.269 8.883 28.454 1.00203.45 O ANISOU 504 O HIS A 75 21439 19518 36345 -5401 3476 3213 O ATOM 505 CB HIS A 75 4.510 7.871 26.809 1.00225.68 C ANISOU 505 CB HIS A 75 24576 22294 38879 -5901 2898 3627 C ATOM 506 CG HIS A 75 4.124 7.573 25.393 1.00234.04 C ANISOU 506 CG HIS A 75 25827 23451 39647 -6102 2783 3604 C ATOM 507 ND1 HIS A 75 3.624 6.351 24.998 1.00237.93 N ANISOU 507 ND1 HIS A 75 26521 23831 40051 -6185 2552 3511 N ATOM 508 CD2 HIS A 75 4.157 8.343 24.279 1.00236.19 C ANISOU 508 CD2 HIS A 75 26119 23925 39698 -6237 2868 3664 C ATOM 509 CE1 HIS A 75 3.371 6.379 23.701 1.00240.20 C ANISOU 509 CE1 HIS A 75 26945 24248 40074 -6363 2499 3512 C ATOM 510 NE2 HIS A 75 3.686 7.577 23.242 1.00239.96 N ANISOU 510 NE2 HIS A 75 26807 24409 39956 -6397 2688 3605 N ATOM 511 N GLY A 76 5.759 7.667 29.596 1.00205.69 N ANISOU 511 N GLY A 76 21765 19502 36885 -5432 3103 3436 N ATOM 512 CA GLY A 76 6.098 8.245 30.884 1.00205.31 C ANISOU 512 CA GLY A 76 21501 19404 37102 -5257 3242 3505 C ATOM 513 C GLY A 76 7.510 7.919 31.328 1.00211.30 C ANISOU 513 C GLY A 76 22246 20131 37906 -5029 3428 3145 C ATOM 514 O GLY A 76 8.154 8.713 32.014 1.00210.90 O ANISOU 514 O GLY A 76 22014 20126 37992 -4890 3633 3146 O ATOM 515 N CYS A 77 7.993 6.745 30.936 1.00159.77 N ANISOU 515 N CYS A 77 12222 17577 30906 -3448 -2678 3956 N ATOM 516 CA CYS A 77 9.336 6.307 31.299 1.00160.14 C ANISOU 516 CA CYS A 77 12387 17353 31107 -3435 -2307 3501 C ATOM 517 C CYS A 77 10.389 7.010 30.450 1.00155.00 C ANISOU 517 C CYS A 77 12169 16583 30140 -3425 -1960 3244 C ATOM 518 O CYS A 77 11.466 7.354 30.939 1.00146.16 O ANISOU 518 O CYS A 77 11095 15287 29151 -3265 -1548 3012 O ATOM 519 CB CYS A 77 9.462 4.788 31.149 1.00163.54 C ANISOU 519 CB CYS A 77 12862 17669 31607 -3717 -2505 3199 C ATOM 520 SG CYS A 77 11.045 4.094 31.685 1.00184.82 S ANISOU 520 SG CYS A 77 15662 20032 34529 -3711 -2088 2637 S ATOM 521 N LEU A 78 10.072 7.223 29.177 1.00157.91 N ANISOU 521 N LEU A 78 12853 17052 30093 -3599 -2131 3289 N ATOM 522 CA LEU A 78 10.989 7.889 28.260 1.00159.66 C ANISOU 522 CA LEU A 78 13500 17187 29977 -3613 -1837 3067 C ATOM 523 C LEU A 78 11.156 9.369 28.591 1.00162.58 C ANISOU 523 C LEU A 78 13826 17604 30341 -3312 -1558 3296 C ATOM 524 O LEU A 78 12.271 9.887 28.587 1.00158.61 O ANISOU 524 O LEU A 78 13517 16948 29799 -3207 -1155 3056 O ATOM 525 CB LEU A 78 10.522 7.728 26.812 1.00158.62 C ANISOU 525 CB LEU A 78 13701 17167 29399 -3881 -2120 3082 C ATOM 526 CG LEU A 78 10.709 6.346 26.184 1.00157.15 C ANISOU 526 CG LEU A 78 13707 16887 29117 -4201 -2312 2741 C ATOM 527 CD1 LEU A 78 10.138 6.323 24.777 1.00164.15 C ANISOU 527 CD1 LEU A 78 14901 17909 29558 -4440 -2603 2813 C ATOM 528 CD2 LEU A 78 12.178 5.957 26.179 1.00151.88 C ANISOU 528 CD2 LEU A 78 13275 15960 28472 -4226 -1925 2230 C ATOM 529 N PHE A 79 10.047 10.046 28.873 1.00163.56 N ANISOU 529 N PHE A 79 13699 17942 30503 -3175 -1777 3758 N ATOM 530 CA PHE A 79 10.091 11.466 29.201 1.00160.77 C ANISOU 530 CA PHE A 79 13287 17649 30149 -2882 -1552 4009 C ATOM 531 C PHE A 79 11.022 11.728 30.378 1.00148.86 C ANISOU 531 C PHE A 79 11606 15963 28993 -2628 -1144 3854 C ATOM 532 O PHE A 79 11.901 12.586 30.306 1.00152.31 O ANISOU 532 O PHE A 79 12228 16297 29346 -2484 -781 3741 O ATOM 533 CB PHE A 79 8.692 12.001 29.511 1.00171.57 C ANISOU 533 CB PHE A 79 14344 19275 31571 -2761 -1876 4530 C ATOM 534 CG PHE A 79 8.685 13.421 30.005 1.00181.64 C ANISOU 534 CG PHE A 79 15509 20610 32897 -2434 -1661 4800 C ATOM 535 CD1 PHE A 79 8.755 14.481 29.114 1.00182.18 C ANISOU 535 CD1 PHE A 79 15870 20739 32613 -2404 -1587 4905 C ATOM 536 CD2 PHE A 79 8.613 13.698 31.362 1.00182.90 C ANISOU 536 CD2 PHE A 79 15275 20763 33456 -2156 -1537 4948 C ATOM 537 CE1 PHE A 79 8.751 15.788 29.566 1.00176.56 C ANISOU 537 CE1 PHE A 79 15064 20075 31948 -2104 -1399 5152 C ATOM 538 CE2 PHE A 79 8.609 15.004 31.819 1.00178.39 C ANISOU 538 CE2 PHE A 79 14608 20242 32931 -1850 -1346 5193 C ATOM 539 CZ PHE A 79 8.677 16.049 30.920 1.00174.52 C ANISOU 539 CZ PHE A 79 14415 19807 32090 -1824 -1280 5294 C ATOM 540 N ILE A 80 10.823 10.983 31.459 1.00135.69 N ANISOU 540 N ILE A 80 9580 14261 27716 -2578 -1209 3853 N ATOM 541 CA ILE A 80 11.640 11.135 32.656 1.00127.23 C ANISOU 541 CA ILE A 80 8308 13024 27010 -2342 -848 3715 C ATOM 542 C ILE A 80 13.100 10.772 32.391 1.00131.24 C ANISOU 542 C ILE A 80 9128 13271 27467 -2425 -480 3209 C ATOM 543 O ILE A 80 14.008 11.290 33.043 1.00128.06 O ANISOU 543 O ILE A 80 8703 12721 27232 -2218 -90 3074 O ATOM 544 CB ILE A 80 11.091 10.281 33.819 1.00113.55 C ANISOU 544 CB ILE A 80 6130 11314 25699 -2306 -1026 3806 C ATOM 545 CG1 ILE A 80 9.722 10.805 34.257 1.00109.51 C ANISOU 545 CG1 ILE A 80 5269 11065 25274 -2163 -1330 4325 C ATOM 546 CG2 ILE A 80 12.058 10.276 34.992 1.00101.92 C ANISOU 546 CG2 ILE A 80 4486 9643 24596 -2100 -642 3596 C ATOM 547 CD1 ILE A 80 9.158 10.103 35.472 1.00105.71 C ANISOU 547 CD1 ILE A 80 4322 10628 25213 -2095 -1490 4455 C ATOM 548 N ALA A 81 13.321 9.892 31.420 1.00139.52 N ANISOU 548 N ALA A 81 10471 14265 28276 -2727 -608 2931 N ATOM 549 CA ALA A 81 14.666 9.422 31.104 1.00144.90 C ANISOU 549 CA ALA A 81 11453 14709 28892 -2832 -293 2434 C ATOM 550 C ALA A 81 15.355 10.281 30.045 1.00147.08 C ANISOU 550 C ALA A 81 12155 14960 28768 -2851 -61 2317 C ATOM 551 O ALA A 81 16.583 10.333 29.981 1.00143.95 O ANISOU 551 O ALA A 81 11975 14375 28344 -2832 308 1966 O ATOM 552 CB ALA A 81 14.626 7.966 30.659 1.00149.59 C ANISOU 552 CB ALA A 81 12141 15243 29453 -3141 -537 2160 C ATOM 553 N CYS A 82 14.562 10.954 29.219 1.00152.20 N ANISOU 553 N CYS A 82 12920 15802 29106 -2891 -280 2615 N ATOM 554 CA CYS A 82 15.104 11.736 28.112 1.00156.57 C ANISOU 554 CA CYS A 82 13885 16355 29249 -2939 -110 2529 C ATOM 555 C CYS A 82 14.923 13.237 28.316 1.00155.21 C ANISOU 555 C CYS A 82 13660 16278 29035 -2671 36 2864 C ATOM 556 O CYS A 82 15.285 14.033 27.450 1.00151.97 O ANISOU 556 O CYS A 82 13565 15885 28290 -2686 168 2853 O ATOM 557 CB CYS A 82 14.459 11.309 26.792 1.00160.02 C ANISOU 557 CB CYS A 82 14579 16924 29298 -3233 -464 2557 C ATOM 558 SG CYS A 82 14.650 9.556 26.394 1.00182.87 S ANISOU 558 SG CYS A 82 17583 19710 32190 -3567 -666 2158 S ATOM 559 N PHE A 83 14.362 13.620 29.458 1.00156.74 N ANISOU 559 N PHE A 83 13455 16534 29566 -2426 8 3161 N ATOM 560 CA PHE A 83 14.137 15.031 29.752 1.00162.51 C ANISOU 560 CA PHE A 83 14102 17355 30289 -2151 129 3492 C ATOM 561 C PHE A 83 15.456 15.774 29.932 1.00160.81 C ANISOU 561 C PHE A 83 14070 16954 30077 -1989 619 3261 C ATOM 562 O PHE A 83 15.560 16.960 29.618 1.00160.86 O ANISOU 562 O PHE A 83 14213 17006 29900 -1853 754 3426 O ATOM 563 CB PHE A 83 13.266 15.198 30.998 1.00164.43 C ANISOU 563 CB PHE A 83 13860 17704 30912 -1919 -8 3841 C ATOM 564 CG PHE A 83 12.998 16.632 31.359 1.00166.42 C ANISOU 564 CG PHE A 83 14007 18050 31175 -1621 102 4186 C ATOM 565 CD1 PHE A 83 11.970 17.333 30.751 1.00164.18 C ANISOU 565 CD1 PHE A 83 13744 17987 30650 -1615 -176 4563 C ATOM 566 CD2 PHE A 83 13.778 17.281 32.303 1.00162.63 C ANISOU 566 CD2 PHE A 83 13412 17433 30946 -1344 480 4131 C ATOM 567 CE1 PHE A 83 11.723 18.651 31.080 1.00157.49 C ANISOU 567 CE1 PHE A 83 12806 17222 29813 -1337 -84 4877 C ATOM 568 CE2 PHE A 83 13.535 18.599 32.635 1.00154.73 C ANISOU 568 CE2 PHE A 83 12321 16514 29956 -1067 573 4444 C ATOM 569 CZ PHE A 83 12.507 19.285 32.023 1.00152.91 C ANISOU 569 CZ PHE A 83 12113 16503 29484 -1061 289 4816 C ATOM 570 N VAL A 84 16.460 15.068 30.442 1.00154.12 N ANISOU 570 N VAL A 84 13224 15896 29439 -2007 880 2880 N ATOM 571 CA VAL A 84 17.780 15.652 30.640 1.00145.75 C ANISOU 571 CA VAL A 84 12336 14646 28397 -1870 1353 2626 C ATOM 572 C VAL A 84 18.456 15.898 29.295 1.00140.82 C ANISOU 572 C VAL A 84 12193 13991 27323 -2055 1472 2406 C ATOM 573 O VAL A 84 19.322 16.763 29.173 1.00134.29 O ANISOU 573 O VAL A 84 11558 13076 26391 -1937 1812 2318 O ATOM 574 CB VAL A 84 18.671 14.748 31.513 1.00143.12 C ANISOU 574 CB VAL A 84 11880 14096 28403 -1857 1587 2262 C ATOM 575 CG1 VAL A 84 18.885 13.399 30.840 1.00145.03 C ANISOU 575 CG1 VAL A 84 12306 14273 28525 -2178 1441 1916 C ATOM 576 CG2 VAL A 84 20.002 15.428 31.804 1.00138.43 C ANISOU 576 CG2 VAL A 84 11435 13314 27849 -1691 2082 2031 C ATOM 577 N LEU A 85 18.049 15.136 28.285 1.00143.60 N ANISOU 577 N LEU A 85 12737 14419 27406 -2346 1185 2322 N ATOM 578 CA LEU A 85 18.588 15.296 26.940 1.00141.25 C ANISOU 578 CA LEU A 85 12893 14115 26659 -2542 1254 2123 C ATOM 579 C LEU A 85 18.076 16.585 26.309 1.00135.80 C ANISOU 579 C LEU A 85 12328 13588 25680 -2461 1192 2472 C ATOM 580 O LEU A 85 18.683 17.116 25.381 1.00132.55 O ANISOU 580 O LEU A 85 12275 13162 24927 -2536 1354 2352 O ATOM 581 CB LEU A 85 18.221 14.095 26.065 1.00145.02 C ANISOU 581 CB LEU A 85 13524 14636 26940 -2872 937 1951 C ATOM 582 CG LEU A 85 18.702 12.724 26.544 1.00138.05 C ANISOU 582 CG LEU A 85 12554 13592 26305 -2991 958 1586 C ATOM 583 CD1 LEU A 85 18.248 11.633 25.587 1.00139.82 C ANISOU 583 CD1 LEU A 85 12950 13876 26301 -3316 612 1451 C ATOM 584 CD2 LEU A 85 20.215 12.705 26.703 1.00130.10 C ANISOU 584 CD2 LEU A 85 11735 12360 25337 -2945 1420 1163 C ATOM 585 N VAL A 86 16.953 17.081 26.821 1.00136.37 N ANISOU 585 N VAL A 86 12102 13822 25892 -2307 953 2905 N ATOM 586 CA VAL A 86 16.370 18.330 26.344 1.00137.29 C ANISOU 586 CA VAL A 86 12292 14098 25773 -2203 872 3271 C ATOM 587 C VAL A 86 17.117 19.533 26.913 1.00134.86 C ANISOU 587 C VAL A 86 11982 13696 25561 -1917 1260 3318 C ATOM 588 O VAL A 86 17.494 20.447 26.179 1.00132.70 O ANISOU 588 O VAL A 86 11994 13438 24989 -1907 1401 3347 O ATOM 589 CB VAL A 86 14.879 18.439 26.723 1.00134.81 C ANISOU 589 CB VAL A 86 11644 13996 25581 -2127 473 3725 C ATOM 590 CG1 VAL A 86 14.326 19.799 26.324 1.00141.75 C ANISOU 590 CG1 VAL A 86 12586 15029 26243 -1987 414 4104 C ATOM 591 CG2 VAL A 86 14.081 17.321 26.070 1.00132.84 C ANISOU 591 CG2 VAL A 86 11416 13854 25204 -2420 66 3710 C ATOM 592 N LEU A 87 17.329 19.524 28.226 1.00130.00 N ANISOU 592 N LEU A 87 11043 12984 25365 -1687 1428 3327 N ATOM 593 CA LEU A 87 18.039 20.605 28.897 1.00118.54 C ANISOU 593 CA LEU A 87 9557 11432 24052 -1401 1796 3366 C ATOM 594 C LEU A 87 19.491 20.684 28.437 1.00114.59 C ANISOU 594 C LEU A 87 9408 10740 23390 -1471 2194 2964 C ATOM 595 O LEU A 87 20.067 21.768 28.354 1.00119.81 O ANISOU 595 O LEU A 87 10217 11357 23948 -1323 2457 3008 O ATOM 596 CB LEU A 87 17.977 20.430 30.416 1.00109.93 C ANISOU 596 CB LEU A 87 8040 10273 23458 -1159 1884 3428 C ATOM 597 CG LEU A 87 16.584 20.365 31.044 1.00110.18 C ANISOU 597 CG LEU A 87 7676 10493 23696 -1057 1518 3828 C ATOM 598 CD1 LEU A 87 16.686 20.271 32.557 1.00105.54 C ANISOU 598 CD1 LEU A 87 6686 9823 23590 -803 1661 3861 C ATOM 599 CD2 LEU A 87 15.750 21.569 30.638 1.00110.87 C ANISOU 599 CD2 LEU A 87 7783 10770 23574 -936 1352 4250 C ATOM 600 N ALA A 88 20.078 19.531 28.139 1.00112.74 N ANISOU 600 N ALA A 88 9306 10395 23133 -1695 2234 2573 N ATOM 601 CA ALA A 88 21.467 19.473 27.700 1.00116.50 C ANISOU 601 CA ALA A 88 10109 10695 23459 -1777 2603 2163 C ATOM 602 C ALA A 88 21.611 19.909 26.245 1.00119.02 C ANISOU 602 C ALA A 88 10851 11097 23275 -1967 2571 2133 C ATOM 603 O ALA A 88 22.664 20.397 25.836 1.00108.04 O ANISOU 603 O ALA A 88 9739 9605 21705 -1967 2895 1924 O ATOM 604 CB ALA A 88 22.027 18.072 27.894 1.00121.21 C ANISOU 604 CB ALA A 88 10696 11150 24208 -1945 2646 1753 C ATOM 605 N GLN A 89 20.548 19.730 25.468 1.00131.32 N ANISOU 605 N GLN A 89 12451 12841 24604 -2131 2177 2346 N ATOM 606 CA GLN A 89 20.556 20.118 24.062 1.00143.02 C ANISOU 606 CA GLN A 89 14318 14421 25601 -2321 2104 2346 C ATOM 607 C GLN A 89 20.273 21.608 23.911 1.00143.39 C ANISOU 607 C GLN A 89 14410 14567 25505 -2137 2146 2704 C ATOM 608 O GLN A 89 20.839 22.272 23.042 1.00145.76 O ANISOU 608 O GLN A 89 15043 14868 25470 -2198 2303 2639 O ATOM 609 CB GLN A 89 19.535 19.298 23.270 1.00153.36 C ANISOU 609 CB GLN A 89 15663 15887 26720 -2579 1658 2423 C ATOM 610 CG GLN A 89 19.504 19.606 21.778 1.00161.12 C ANISOU 610 CG GLN A 89 17046 16978 27195 -2796 1559 2414 C ATOM 611 CD GLN A 89 20.795 19.232 21.070 1.00162.17 C ANISOU 611 CD GLN A 89 17543 16973 27100 -2963 1848 1953 C ATOM 612 OE1 GLN A 89 21.686 18.620 21.658 1.00161.94 O ANISOU 612 OE1 GLN A 89 17472 16767 27290 -2939 2099 1621 O ATOM 613 NE2 GLN A 89 20.899 19.597 19.797 1.00162.32 N ANISOU 613 NE2 GLN A 89 17922 17080 26673 -3133 1812 1932 N ATOM 614 N SER A 90 19.395 22.129 24.762 1.00142.66 N ANISOU 614 N SER A 90 13978 14561 25664 -1911 2002 3081 N ATOM 615 CA SER A 90 19.082 23.553 24.756 1.00143.65 C ANISOU 615 CA SER A 90 14107 14774 25698 -1705 2033 3436 C ATOM 616 C SER A 90 20.315 24.371 25.122 1.00134.82 C ANISOU 616 C SER A 90 13106 13485 24633 -1525 2493 3284 C ATOM 617 O SER A 90 20.516 25.473 24.612 1.00127.04 O ANISOU 617 O SER A 90 12326 12533 23409 -1461 2599 3420 O ATOM 618 CB SER A 90 17.940 23.860 25.728 1.00142.59 C ANISOU 618 CB SER A 90 13553 14757 25868 -1479 1802 3843 C ATOM 619 OG SER A 90 17.605 25.237 25.705 1.00139.11 O ANISOU 619 OG SER A 90 13119 14403 25334 -1276 1814 4189 O ATOM 620 N SER A 91 21.139 23.822 26.009 1.00130.67 N ANISOU 620 N SER A 91 12450 12777 24421 -1447 2761 3002 N ATOM 621 CA SER A 91 22.380 24.474 26.405 1.00121.58 C ANISOU 621 CA SER A 91 11404 11449 23343 -1288 3210 2820 C ATOM 622 C SER A 91 23.353 24.529 25.234 1.00119.56 C ANISOU 622 C SER A 91 11598 11140 22689 -1497 3406 2524 C ATOM 623 O SER A 91 24.123 25.478 25.101 1.00115.34 O ANISOU 623 O SER A 91 11246 10539 22040 -1395 3696 2506 O ATOM 624 CB SER A 91 23.019 23.745 27.589 1.00116.39 C ANISOU 624 CB SER A 91 10503 10609 23110 -1181 3433 2566 C ATOM 625 OG SER A 91 22.197 23.823 28.741 1.00113.78 O ANISOU 625 OG SER A 91 9750 10325 23156 -957 3290 2851 O ATOM 626 N ILE A 92 23.311 23.505 24.388 1.00127.20 N ANISOU 626 N ILE A 92 12743 12142 23446 -1791 3244 2294 N ATOM 627 CA ILE A 92 24.166 23.452 23.208 1.00132.00 C ANISOU 627 CA ILE A 92 13778 12721 23655 -2011 3397 2004 C ATOM 628 C ILE A 92 23.884 24.622 22.271 1.00130.67 C ANISOU 628 C ILE A 92 13852 12689 23108 -2022 3334 2270 C ATOM 629 O ILE A 92 24.805 25.306 21.824 1.00127.68 O ANISOU 629 O ILE A 92 13742 12249 22521 -2017 3622 2150 O ATOM 630 CB ILE A 92 23.986 22.130 22.439 1.00136.05 C ANISOU 630 CB ILE A 92 14420 13270 24001 -2324 3170 1749 C ATOM 631 CG1 ILE A 92 24.597 20.971 23.229 1.00124.92 C ANISOU 631 CG1 ILE A 92 12857 11690 22918 -2339 3310 1392 C ATOM 632 CG2 ILE A 92 24.630 22.222 21.067 1.00144.02 C ANISOU 632 CG2 ILE A 92 15878 14306 24538 -2553 3259 1532 C ATOM 633 CD1 ILE A 92 26.097 21.069 23.391 1.00120.21 C ANISOU 633 CD1 ILE A 92 12432 10899 22341 -2295 3775 1024 C ATOM 634 N PHE A 93 22.607 24.848 21.981 1.00133.88 N ANISOU 634 N PHE A 93 14159 13283 23426 -2039 2953 2634 N ATOM 635 CA PHE A 93 22.203 25.947 21.111 1.00142.81 C ANISOU 635 CA PHE A 93 15497 14555 24209 -2048 2850 2920 C ATOM 636 C PHE A 93 22.534 27.300 21.735 1.00142.98 C ANISOU 636 C PHE A 93 15457 14524 24347 -1754 3096 3133 C ATOM 637 O PHE A 93 23.042 28.196 21.061 1.00140.87 O ANISOU 637 O PHE A 93 15470 14261 23793 -1764 3253 3155 O ATOM 638 CB PHE A 93 20.709 25.867 20.798 1.00147.56 C ANISOU 638 CB PHE A 93 15963 15366 24737 -2108 2381 3278 C ATOM 639 CG PHE A 93 20.313 24.636 20.033 1.00150.56 C ANISOU 639 CG PHE A 93 16440 15815 24949 -2413 2106 3103 C ATOM 640 CD1 PHE A 93 20.613 24.514 18.687 1.00151.39 C ANISOU 640 CD1 PHE A 93 16933 15974 24613 -2675 2077 2939 C ATOM 641 CD2 PHE A 93 19.629 23.607 20.657 1.00150.20 C ANISOU 641 CD2 PHE A 93 16099 15786 25184 -2439 1870 3109 C ATOM 642 CE1 PHE A 93 20.247 23.386 17.979 1.00151.40 C ANISOU 642 CE1 PHE A 93 17030 16037 24458 -2951 1818 2776 C ATOM 643 CE2 PHE A 93 19.260 22.477 19.954 1.00152.03 C ANISOU 643 CE2 PHE A 93 16425 16076 25263 -2721 1607 2951 C ATOM 644 CZ PHE A 93 19.569 22.367 18.613 1.00153.80 C ANISOU 644 CZ PHE A 93 17042 16348 25049 -2974 1581 2782 C ATOM 645 N SER A 94 22.238 27.440 23.024 1.00140.78 N ANISOU 645 N SER A 94 14809 14194 24486 -1493 3122 3291 N ATOM 646 CA SER A 94 22.527 28.672 23.747 1.00130.83 C ANISOU 646 CA SER A 94 13455 12873 23382 -1192 3348 3491 C ATOM 647 C SER A 94 24.020 28.982 23.724 1.00127.91 C ANISOU 647 C SER A 94 13319 12318 22963 -1172 3803 3173 C ATOM 648 O SER A 94 24.424 30.108 23.434 1.00126.84 O ANISOU 648 O SER A 94 13364 12172 22657 -1080 3968 3286 O ATOM 649 CB SER A 94 22.033 28.577 25.193 1.00123.80 C ANISOU 649 CB SER A 94 12115 11949 22974 -928 3313 3656 C ATOM 650 OG SER A 94 20.629 28.403 25.244 1.00126.42 O ANISOU 650 OG SER A 94 12219 12466 23350 -926 2895 3984 O ATOM 651 N LEU A 95 24.834 27.976 24.029 1.00128.81 N ANISOU 651 N LEU A 95 13428 12286 23226 -1259 3998 2778 N ATOM 652 CA LEU A 95 26.283 28.142 24.047 1.00125.48 C ANISOU 652 CA LEU A 95 13214 11686 22775 -1249 4434 2446 C ATOM 653 C LEU A 95 26.832 28.429 22.653 1.00124.70 C ANISOU 653 C LEU A 95 13556 11636 22187 -1476 4503 2310 C ATOM 654 O LEU A 95 27.828 29.138 22.502 1.00120.36 O ANISOU 654 O LEU A 95 13211 10995 21524 -1425 4828 2202 O ATOM 655 CB LEU A 95 26.963 26.902 24.634 1.00120.16 C ANISOU 655 CB LEU A 95 12436 10857 22360 -1311 4594 2046 C ATOM 656 CG LEU A 95 26.741 26.613 26.121 1.00116.10 C ANISOU 656 CG LEU A 95 11500 10253 22360 -1075 4627 2107 C ATOM 657 CD1 LEU A 95 27.482 25.351 26.527 1.00117.91 C ANISOU 657 CD1 LEU A 95 11681 10329 22791 -1176 4784 1681 C ATOM 658 CD2 LEU A 95 27.182 27.791 26.974 1.00115.45 C ANISOU 658 CD2 LEU A 95 11312 10077 22478 -764 4904 2269 C ATOM 659 N LEU A 96 26.178 27.874 21.637 1.00127.11 N ANISOU 659 N LEU A 96 14006 12089 22202 -1729 4195 2319 N ATOM 660 CA LEU A 96 26.595 28.086 20.256 1.00131.44 C ANISOU 660 CA LEU A 96 14968 12705 22268 -1961 4222 2201 C ATOM 661 C LEU A 96 26.214 29.483 19.778 1.00129.57 C ANISOU 661 C LEU A 96 14855 12579 21796 -1871 4163 2569 C ATOM 662 O LEU A 96 26.994 30.149 19.101 1.00129.88 O ANISOU 662 O LEU A 96 15196 12601 21552 -1925 4378 2488 O ATOM 663 CB LEU A 96 25.979 27.029 19.339 1.00139.95 C ANISOU 663 CB LEU A 96 16152 13905 23117 -2256 3896 2098 C ATOM 664 CG LEU A 96 26.309 27.153 17.850 1.00145.48 C ANISOU 664 CG LEU A 96 17276 14698 23303 -2516 3884 1978 C ATOM 665 CD1 LEU A 96 27.814 27.180 17.629 1.00142.32 C ANISOU 665 CD1 LEU A 96 17132 14156 22789 -2562 4310 1594 C ATOM 666 CD2 LEU A 96 25.667 26.024 17.058 1.00149.42 C ANISOU 666 CD2 LEU A 96 17848 15307 23620 -2794 3551 1869 C ATOM 667 N ALA A 97 25.009 29.918 20.135 1.00127.22 N ANISOU 667 N ALA A 97 14321 12400 21617 -1735 3866 2974 N ATOM 668 CA ALA A 97 24.531 31.247 19.770 1.00125.23 C ANISOU 668 CA ALA A 97 14152 12255 21174 -1629 3777 3352 C ATOM 669 C ALA A 97 25.412 32.329 20.388 1.00119.99 C ANISOU 669 C ALA A 97 13503 11454 20634 -1386 4142 3381 C ATOM 670 O ALA A 97 25.830 33.263 19.706 1.00112.21 O ANISOU 670 O ALA A 97 12788 10487 19359 -1406 4258 3448 O ATOM 671 CB ALA A 97 23.085 31.429 20.196 1.00120.78 C ANISOU 671 CB ALA A 97 13287 11834 20769 -1503 3400 3765 C ATOM 672 N ILE A 98 25.687 32.196 21.682 1.00119.93 N ANISOU 672 N ILE A 98 13203 11308 21058 -1159 4317 3332 N ATOM 673 CA ILE A 98 26.560 33.132 22.380 1.00119.34 C ANISOU 673 CA ILE A 98 13118 11083 21142 -919 4674 3336 C ATOM 674 C ILE A 98 27.923 33.217 21.699 1.00123.18 C ANISOU 674 C ILE A 98 13964 11468 21369 -1065 5020 2999 C ATOM 675 O ILE A 98 28.500 34.297 21.579 1.00123.81 O ANISOU 675 O ILE A 98 14204 11503 21335 -965 5230 3082 O ATOM 676 CB ILE A 98 26.754 32.734 23.855 1.00116.62 C ANISOU 676 CB ILE A 98 12412 10593 21304 -690 4826 3258 C ATOM 677 CG1 ILE A 98 25.429 32.833 24.613 1.00112.32 C ANISOU 677 CG1 ILE A 98 11496 10156 21026 -506 4507 3629 C ATOM 678 CG2 ILE A 98 27.805 33.615 24.512 1.00120.67 C ANISOU 678 CG2 ILE A 98 12950 10934 21963 -469 5226 3206 C ATOM 679 CD1 ILE A 98 25.548 32.535 26.091 1.00105.10 C ANISOU 679 CD1 ILE A 98 10210 9114 20611 -263 4642 3592 C ATOM 680 N ALA A 99 28.432 32.073 21.256 1.00132.63 N ANISOU 680 N ALA A 99 15287 12632 22475 -1301 5075 2620 N ATOM 681 CA ALA A 99 29.708 32.027 20.553 1.00143.30 C ANISOU 681 CA ALA A 99 16979 13904 23563 -1461 5389 2275 C ATOM 682 C ALA A 99 29.635 32.828 19.257 1.00154.27 C ANISOU 682 C ALA A 99 18713 15429 24472 -1611 5307 2419 C ATOM 683 O ALA A 99 30.484 33.680 18.993 1.00154.97 O ANISOU 683 O ALA A 99 19016 15464 24401 -1576 5575 2390 O ATOM 684 CB ALA A 99 30.108 30.585 20.268 1.00142.40 C ANISOU 684 CB ALA A 99 16925 13752 23428 -1693 5404 1859 C ATOM 685 N ILE A 100 28.613 32.548 18.454 1.00160.27 N ANISOU 685 N ILE A 100 19523 16368 25004 -1781 4933 2577 N ATOM 686 CA ILE A 100 28.394 33.267 17.205 1.00162.05 C ANISOU 686 CA ILE A 100 20058 16741 24773 -1931 4807 2741 C ATOM 687 C ILE A 100 28.246 34.759 17.473 1.00159.24 C ANISOU 687 C ILE A 100 19686 16390 24426 -1702 4855 3106 C ATOM 688 O ILE A 100 28.849 35.589 16.793 1.00158.60 O ANISOU 688 O ILE A 100 19889 16318 24054 -1750 5013 3120 O ATOM 689 CB ILE A 100 27.129 32.763 16.482 1.00163.25 C ANISOU 689 CB ILE A 100 20200 17085 24744 -2109 4357 2914 C ATOM 690 CG1 ILE A 100 27.226 31.258 16.217 1.00158.26 C ANISOU 690 CG1 ILE A 100 19581 16445 24106 -2338 4283 2558 C ATOM 691 CG2 ILE A 100 26.917 33.525 15.183 1.00167.88 C ANISOU 691 CG2 ILE A 100 21110 17823 24854 -2266 4232 3084 C ATOM 692 CD1 ILE A 100 25.983 30.668 15.585 1.00156.26 C ANISOU 692 CD1 ILE A 100 19297 16370 23707 -2512 3837 2715 C ATOM 693 N ASP A 101 27.438 35.087 18.476 1.00156.74 N ANISOU 693 N ASP A 101 19034 16072 24449 -1451 4714 3402 N ATOM 694 CA ASP A 101 27.196 36.471 18.859 1.00153.26 C ANISOU 694 CA ASP A 101 18536 15633 24064 -1203 4731 3765 C ATOM 695 C ASP A 101 28.496 37.204 19.171 1.00149.70 C ANISOU 695 C ASP A 101 18219 15015 23645 -1083 5159 3623 C ATOM 696 O ASP A 101 28.765 38.271 18.621 1.00152.29 O ANISOU 696 O ASP A 101 18772 15368 23724 -1072 5231 3772 O ATOM 697 CB ASP A 101 26.266 36.523 20.071 1.00151.33 C ANISOU 697 CB ASP A 101 17871 15387 24240 -935 4559 4033 C ATOM 698 CG ASP A 101 26.094 37.923 20.613 1.00155.87 C ANISOU 698 CG ASP A 101 18363 15941 24919 -646 4604 4381 C ATOM 699 OD1 ASP A 101 25.764 38.833 19.823 1.00165.83 O ANISOU 699 OD1 ASP A 101 19824 17309 25876 -682 4478 4625 O ATOM 700 OD2 ASP A 101 26.287 38.113 21.831 1.00151.56 O ANISOU 700 OD2 ASP A 101 17554 15271 24761 -382 4762 4410 O ATOM 701 N ARG A 102 29.299 36.623 20.057 1.00145.51 N ANISOU 701 N ARG A 102 17548 14313 23424 -997 5439 3337 N ATOM 702 CA ARG A 102 30.566 37.226 20.456 1.00143.42 C ANISOU 702 CA ARG A 102 17386 13879 23229 -877 5858 3181 C ATOM 703 C ARG A 102 31.536 37.340 19.285 1.00143.92 C ANISOU 703 C ARG A 102 17863 13954 22866 -1119 6051 2946 C ATOM 704 O ARG A 102 32.510 38.089 19.348 1.00143.82 O ANISOU 704 O ARG A 102 17999 13840 22808 -1045 6362 2887 O ATOM 705 CB ARG A 102 31.204 36.433 21.599 1.00145.08 C ANISOU 705 CB ARG A 102 17362 13912 23852 -761 6102 2896 C ATOM 706 CG ARG A 102 30.434 36.487 22.911 1.00149.77 C ANISOU 706 CG ARG A 102 17538 14470 24899 -478 5984 3128 C ATOM 707 CD ARG A 102 30.424 37.891 23.504 1.00154.58 C ANISOU 707 CD ARG A 102 18077 15031 25627 -187 6077 3444 C ATOM 708 NE ARG A 102 29.576 38.808 22.747 1.00159.75 N ANISOU 708 NE ARG A 102 18853 15848 25996 -201 5803 3813 N ATOM 709 CZ ARG A 102 29.467 40.108 23.001 1.00158.30 C ANISOU 709 CZ ARG A 102 18667 15652 25827 15 5828 4118 C ATOM 710 NH1 ARG A 102 30.155 40.651 23.996 1.00157.16 N ANISOU 710 NH1 ARG A 102 18407 15339 25969 263 6116 4100 N ATOM 711 NH2 ARG A 102 28.671 40.866 22.259 1.00158.42 N ANISOU 711 NH2 ARG A 102 18800 15820 25571 -17 5561 4440 N ATOM 712 N TYR A 103 31.269 36.591 18.221 1.00147.70 N ANISOU 712 N TYR A 103 18524 14561 23034 -1407 5864 2813 N ATOM 713 CA TYR A 103 32.088 36.666 17.018 1.00150.43 C ANISOU 713 CA TYR A 103 19265 14949 22944 -1653 6010 2603 C ATOM 714 C TYR A 103 31.598 37.781 16.103 1.00151.17 C ANISOU 714 C TYR A 103 19570 15187 22679 -1699 5837 2937 C ATOM 715 O TYR A 103 32.396 38.503 15.509 1.00148.61 O ANISOU 715 O TYR A 103 19523 14854 22090 -1758 6044 2897 O ATOM 716 CB TYR A 103 32.082 35.334 16.267 1.00151.69 C ANISOU 716 CB TYR A 103 19538 15177 22920 -1945 5899 2285 C ATOM 717 CG TYR A 103 32.805 35.386 14.939 1.00152.89 C ANISOU 717 CG TYR A 103 20096 15403 22591 -2211 6007 2086 C ATOM 718 CD1 TYR A 103 34.177 35.186 14.864 1.00149.98 C ANISOU 718 CD1 TYR A 103 19904 14921 22162 -2272 6392 1718 C ATOM 719 CD2 TYR A 103 32.115 35.639 13.759 1.00156.79 C ANISOU 719 CD2 TYR A 103 20797 16086 22688 -2399 5726 2267 C ATOM 720 CE1 TYR A 103 34.842 35.235 13.653 1.00152.73 C ANISOU 720 CE1 TYR A 103 20617 15348 22064 -2512 6493 1537 C ATOM 721 CE2 TYR A 103 32.772 35.690 12.544 1.00158.89 C ANISOU 721 CE2 TYR A 103 21431 16428 22510 -2641 5824 2088 C ATOM 722 CZ TYR A 103 34.135 35.487 12.497 1.00156.28 C ANISOU 722 CZ TYR A 103 21266 15990 22125 -2696 6208 1723 C ATOM 723 OH TYR A 103 34.793 35.536 11.289 1.00156.45 O ANISOU 723 OH TYR A 103 21647 16098 21698 -2935 6308 1544 O ATOM 724 N ILE A 104 30.280 37.913 15.997 1.00155.31 N ANISOU 724 N ILE A 104 19961 15849 23200 -1674 5452 3268 N ATOM 725 CA ILE A 104 29.674 38.932 15.149 1.00160.72 C ANISOU 725 CA ILE A 104 20825 16681 23561 -1715 5243 3608 C ATOM 726 C ILE A 104 30.068 40.341 15.587 1.00156.21 C ANISOU 726 C ILE A 104 20275 16027 23052 -1480 5430 3839 C ATOM 727 O ILE A 104 30.283 41.222 14.755 1.00158.30 O ANISOU 727 O ILE A 104 20812 16355 22982 -1558 5449 3964 O ATOM 728 CB ILE A 104 28.137 38.811 15.141 1.00166.45 C ANISOU 728 CB ILE A 104 21350 17558 24334 -1691 4795 3937 C ATOM 729 CG1 ILE A 104 27.717 37.436 14.616 1.00166.77 C ANISOU 729 CG1 ILE A 104 21394 17688 24284 -1942 4586 3721 C ATOM 730 CG2 ILE A 104 27.516 39.924 14.307 1.00170.19 C ANISOU 730 CG2 ILE A 104 22003 18176 24485 -1716 4584 4300 C ATOM 731 CD1 ILE A 104 26.223 37.197 14.645 1.00166.24 C ANISOU 731 CD1 ILE A 104 21115 17768 24280 -1931 4148 4023 C ATOM 732 N ALA A 105 30.164 40.544 16.897 1.00164.49 N ANISOU 732 N ALA A 105 21731 11202 29564 1603 6215 759 N ATOM 733 CA ALA A 105 30.529 41.844 17.449 1.00154.36 C ANISOU 733 CA ALA A 105 20119 9858 28673 1666 5940 1058 C ATOM 734 C ALA A 105 31.957 42.230 17.079 1.00158.53 C ANISOU 734 C ALA A 105 20701 10597 28936 1738 6105 1468 C ATOM 735 O ALA A 105 32.206 43.337 16.601 1.00164.95 O ANISOU 735 O ALA A 105 21381 11491 29803 1663 5753 1823 O ATOM 736 CB ALA A 105 30.353 41.845 18.960 1.00140.99 C ANISOU 736 CB ALA A 105 18179 7924 27468 1840 6063 846 C ATOM 737 N ILE A 106 32.892 41.313 17.301 1.00157.74 N ANISOU 737 N ILE A 106 20797 10588 28550 1882 6640 1416 N ATOM 738 CA ILE A 106 34.299 41.572 17.017 1.00161.58 C ANISOU 738 CA ILE A 106 21345 11275 28772 1966 6850 1779 C ATOM 739 C ILE A 106 34.586 41.583 15.518 1.00175.20 C ANISOU 739 C ILE A 106 23316 13259 29994 1799 6752 2011 C ATOM 740 O ILE A 106 35.313 42.445 15.022 1.00181.52 O ANISOU 740 O ILE A 106 24057 14205 30707 1770 6590 2405 O ATOM 741 CB ILE A 106 35.213 40.543 17.710 1.00153.38 C ANISOU 741 CB ILE A 106 20450 10256 27571 2175 7465 1640 C ATOM 742 CG1 ILE A 106 35.036 40.618 19.228 1.00144.04 C ANISOU 742 CG1 ILE A 106 19008 8824 26896 2349 7562 1447 C ATOM 743 CG2 ILE A 106 36.666 40.777 17.331 1.00154.77 C ANISOU 743 CG2 ILE A 106 20708 10656 27441 2253 7684 2014 C ATOM 744 CD1 ILE A 106 35.947 39.689 19.995 1.00144.36 C ANISOU 744 CD1 ILE A 106 19164 8869 26819 2563 8149 1323 C ATOM 745 N ALA A 107 34.010 40.625 14.799 1.00177.35 N ANISOU 745 N ALA A 107 23864 13587 29935 1686 6850 1766 N ATOM 746 CA ALA A 107 34.205 40.532 13.356 1.00182.38 C ANISOU 746 CA ALA A 107 24752 14466 30077 1520 6770 1949 C ATOM 747 C ALA A 107 33.586 41.725 12.637 1.00187.01 C ANISOU 747 C ALA A 107 25184 15066 30803 1328 6165 2188 C ATOM 748 O ALA A 107 34.264 42.434 11.894 1.00188.95 O ANISOU 748 O ALA A 107 25439 15493 30860 1265 6013 2567 O ATOM 749 CB ALA A 107 33.625 39.230 12.823 1.00184.52 C ANISOU 749 CB ALA A 107 25339 14770 30001 1444 6996 1603 C ATOM 750 N ILE A 108 32.294 41.941 12.864 1.00189.15 N ANISOU 750 N ILE A 108 25315 15147 31407 1233 5821 1962 N ATOM 751 CA ILE A 108 31.584 43.051 12.241 1.00192.99 C ANISOU 751 CA ILE A 108 25644 15621 32061 1050 5228 2151 C ATOM 752 C ILE A 108 30.813 43.855 13.283 1.00190.33 C ANISOU 752 C ILE A 108 24946 15023 32348 1091 4901 2061 C ATOM 753 O ILE A 108 29.625 43.618 13.503 1.00194.11 O ANISOU 753 O ILE A 108 25376 15336 33041 1021 4726 1748 O ATOM 754 CB ILE A 108 30.601 42.558 11.163 1.00195.70 C ANISOU 754 CB ILE A 108 26207 16018 32132 838 5043 1975 C ATOM 755 CG1 ILE A 108 31.256 41.487 10.288 1.00190.38 C ANISOU 755 CG1 ILE A 108 25915 15574 30849 819 5448 1960 C ATOM 756 CG2 ILE A 108 30.110 43.725 10.319 1.00201.16 C ANISOU 756 CG2 ILE A 108 26778 16754 32900 644 4456 2245 C ATOM 757 CD1 ILE A 108 30.342 40.929 9.221 1.00189.51 C ANISOU 757 CD1 ILE A 108 26038 15526 30444 617 5302 1781 C ATOM 758 N PRO A 109 31.492 44.815 13.929 1.00183.15 N ANISOU 758 N PRO A 109 23779 14079 31731 1203 4816 2335 N ATOM 759 CA PRO A 109 30.894 45.639 14.986 1.00183.89 C ANISOU 759 CA PRO A 109 23512 13931 32429 1261 4523 2279 C ATOM 760 C PRO A 109 29.757 46.514 14.468 1.00192.27 C ANISOU 760 C PRO A 109 24425 14917 33713 1065 3915 2314 C ATOM 761 O PRO A 109 28.813 46.795 15.207 1.00193.04 O ANISOU 761 O PRO A 109 24299 14792 34256 1070 3684 2102 O ATOM 762 CB PRO A 109 32.063 46.514 15.451 1.00178.53 C ANISOU 762 CB PRO A 109 22646 13301 31885 1396 4560 2652 C ATOM 763 CG PRO A 109 33.020 46.516 14.306 1.00178.04 C ANISOU 763 CG PRO A 109 22814 13521 31311 1330 4657 2976 C ATOM 764 CD PRO A 109 32.904 45.160 13.692 1.00178.16 C ANISOU 764 CD PRO A 109 23187 13642 30863 1285 5006 2717 C ATOM 765 N LEU A 110 29.848 46.935 13.210 1.00197.94 N ANISOU 765 N LEU A 110 25266 15820 34121 894 3659 2579 N ATOM 766 CA LEU A 110 28.842 47.812 12.623 1.00203.01 C ANISOU 766 CA LEU A 110 25779 16411 34944 701 3069 2648 C ATOM 767 C LEU A 110 27.529 47.081 12.354 1.00205.85 C ANISOU 767 C LEU A 110 26256 16673 35284 576 2974 2254 C ATOM 768 O LEU A 110 26.472 47.489 12.834 1.00203.78 O ANISOU 768 O LEU A 110 25780 16210 35436 535 2645 2077 O ATOM 769 CB LEU A 110 29.370 48.447 11.334 1.00206.72 C ANISOU 769 CB LEU A 110 26361 17116 35066 554 2840 3053 C ATOM 770 CG LEU A 110 30.571 49.382 11.490 1.00204.34 C ANISOU 770 CG LEU A 110 25916 16912 34812 646 2829 3485 C ATOM 771 CD1 LEU A 110 31.053 49.873 10.133 1.00206.74 C ANISOU 771 CD1 LEU A 110 26369 17462 34722 486 2629 3856 C ATOM 772 CD2 LEU A 110 30.227 50.554 12.398 1.00201.24 C ANISOU 772 CD2 LEU A 110 25132 16317 35014 699 2459 3573 C ATOM 773 N ARG A 111 27.603 45.999 11.586 1.00209.64 N ANISOU 773 N ARG A 111 27076 17299 35280 516 3264 2117 N ATOM 774 CA ARG A 111 26.415 45.221 11.252 1.00211.31 C ANISOU 774 CA ARG A 111 27431 17438 35419 394 3206 1745 C ATOM 775 C ARG A 111 25.892 44.447 12.458 1.00204.65 C ANISOU 775 C ARG A 111 26518 16376 34862 529 3472 1322 C ATOM 776 O ARG A 111 24.811 43.859 12.405 1.00204.24 O ANISOU 776 O ARG A 111 26534 16222 34847 444 3408 980 O ATOM 777 CB ARG A 111 26.709 44.260 10.098 1.00217.35 C ANISOU 777 CB ARG A 111 28586 18427 35572 299 3464 1725 C ATOM 778 CG ARG A 111 27.043 44.946 8.784 1.00223.99 C ANISOU 778 CG ARG A 111 29521 19484 36103 133 3171 2104 C ATOM 779 CD ARG A 111 25.863 45.755 8.270 1.00229.51 C ANISOU 779 CD ARG A 111 30083 20101 37019 -63 2570 2116 C ATOM 780 NE ARG A 111 24.659 44.938 8.140 1.00232.82 N ANISOU 780 NE ARG A 111 30620 20418 37424 -158 2545 1707 N ATOM 781 CZ ARG A 111 24.354 44.222 7.063 1.00236.09 C ANISOU 781 CZ ARG A 111 31331 20970 37403 -303 2591 1614 C ATOM 782 NH1 ARG A 111 25.166 44.217 6.014 1.00239.60 N ANISOU 782 NH1 ARG A 111 31988 21663 37387 -372 2667 1900 N ATOM 783 NH2 ARG A 111 23.236 43.508 7.033 1.00235.24 N ANISOU 783 NH2 ARG A 111 31309 20752 37318 -381 2562 1233 N ATOM 784 N TYR A 112 26.663 44.449 13.542 1.00199.74 N ANISOU 784 N TYR A 112 25764 15685 34443 737 3770 1346 N ATOM 785 CA TYR A 112 26.283 43.735 14.758 1.00196.48 C ANISOU 785 CA TYR A 112 25278 15068 34307 880 4050 964 C ATOM 786 C TYR A 112 24.893 44.138 15.237 1.00193.50 C ANISOU 786 C TYR A 112 24668 14458 34395 805 3648 718 C ATOM 787 O TYR A 112 24.040 43.287 15.484 1.00197.57 O ANISOU 787 O TYR A 112 25267 14860 34939 784 3757 327 O ATOM 788 CB TYR A 112 27.309 43.976 15.868 1.00195.29 C ANISOU 788 CB TYR A 112 24957 14868 34376 1107 4331 1089 C ATOM 789 CG TYR A 112 26.892 43.432 17.218 1.00195.97 C ANISOU 789 CG TYR A 112 24915 14724 34822 1257 4560 723 C ATOM 790 CD1 TYR A 112 26.288 44.252 18.163 1.00193.11 C ANISOU 790 CD1 TYR A 112 24204 14143 35027 1298 4257 672 C ATOM 791 CD2 TYR A 112 27.100 42.098 17.547 1.00197.67 C ANISOU 791 CD2 TYR A 112 25357 14939 34810 1355 5078 427 C ATOM 792 CE1 TYR A 112 25.904 43.761 19.398 1.00191.32 C ANISOU 792 CE1 TYR A 112 23858 13708 35129 1431 4465 338 C ATOM 793 CE2 TYR A 112 26.720 41.597 18.780 1.00193.91 C ANISOU 793 CE2 TYR A 112 24767 14253 34659 1488 5288 93 C ATOM 794 CZ TYR A 112 26.122 42.433 19.701 1.00190.72 C ANISOU 794 CZ TYR A 112 24014 13636 34815 1524 4980 50 C ATOM 795 OH TYR A 112 25.741 41.942 20.929 1.00183.95 O ANISOU 795 OH TYR A 112 23040 12572 34282 1654 5186 -282 O ATOM 796 N ASN A 113 24.672 45.441 15.367 1.00186.91 N ANISOU 796 N ASN A 113 23540 13553 33924 765 3183 949 N ATOM 797 CA ASN A 113 23.394 45.953 15.841 1.00180.76 C ANISOU 797 CA ASN A 113 22512 12554 33615 698 2770 747 C ATOM 798 C ASN A 113 22.290 45.795 14.801 1.00175.48 C ANISOU 798 C ASN A 113 21981 11914 32780 473 2449 613 C ATOM 799 O ASN A 113 21.105 45.794 15.135 1.00170.20 O ANISOU 799 O ASN A 113 21191 11068 32409 410 2211 330 O ATOM 800 CB ASN A 113 23.532 47.419 16.254 1.00185.00 C ANISOU 800 CB ASN A 113 22699 13015 34579 723 2363 1050 C ATOM 801 CG ASN A 113 24.631 47.634 17.278 1.00184.93 C ANISOU 801 CG ASN A 113 22542 12977 34744 945 2662 1197 C ATOM 802 OD1 ASN A 113 24.422 47.452 18.477 1.00184.05 O ANISOU 802 OD1 ASN A 113 22261 12678 34991 1084 2807 968 O ATOM 803 ND2 ASN A 113 25.812 48.020 16.806 1.00184.48 N ANISOU 803 ND2 ASN A 113 22552 13110 34431 977 2757 1580 N ATOM 804 N GLY A 114 22.687 45.656 13.540 1.00178.02 N ANISOU 804 N GLY A 114 22557 12460 32621 351 2447 817 N ATOM 805 CA GLY A 114 21.738 45.500 12.453 1.00181.43 C ANISOU 805 CA GLY A 114 23144 12945 32848 133 2156 721 C ATOM 806 C GLY A 114 21.253 44.071 12.296 1.00179.60 C ANISOU 806 C GLY A 114 23193 12713 32333 109 2498 324 C ATOM 807 O GLY A 114 20.106 43.833 11.917 1.00178.12 O ANISOU 807 O GLY A 114 23050 12458 32169 -34 2268 84 O ATOM 808 N LEU A 115 22.130 43.117 12.588 1.00179.28 N ANISOU 808 N LEU A 115 23344 12749 32025 250 3049 253 N ATOM 809 CA LEU A 115 21.790 41.703 12.485 1.00178.87 C ANISOU 809 CA LEU A 115 23573 12704 31687 246 3423 -118 C ATOM 810 C LEU A 115 21.339 41.149 13.832 1.00185.14 C ANISOU 810 C LEU A 115 24237 13267 32840 389 3649 -494 C ATOM 811 O LEU A 115 20.218 40.662 13.970 1.00189.27 O ANISOU 811 O LEU A 115 24774 13659 33483 317 3564 -846 O ATOM 812 CB LEU A 115 22.983 40.903 11.957 1.00168.53 C ANISOU 812 CB LEU A 115 22573 11617 29842 310 3903 6 C ATOM 813 CG LEU A 115 23.528 41.339 10.595 1.00165.54 C ANISOU 813 CG LEU A 115 22354 11488 29055 172 3737 375 C ATOM 814 CD1 LEU A 115 24.743 40.511 10.208 1.00156.46 C ANISOU 814 CD1 LEU A 115 21495 10549 27404 257 4246 476 C ATOM 815 CD2 LEU A 115 22.446 41.248 9.528 1.00171.59 C ANISOU 815 CD2 LEU A 115 23251 12288 29657 -58 3398 267 C ATOM 816 N VAL A 116 22.221 41.229 14.824 1.00186.85 N ANISOU 816 N VAL A 116 24329 13438 33229 592 3936 -418 N ATOM 817 CA VAL A 116 21.906 40.770 16.172 1.00186.09 C ANISOU 817 CA VAL A 116 24091 13124 33489 742 4161 -745 C ATOM 818 C VAL A 116 20.861 41.675 16.815 1.00193.83 C ANISOU 818 C VAL A 116 24727 13885 35036 702 3696 -834 C ATOM 819 O VAL A 116 21.198 42.681 17.441 1.00194.35 O ANISOU 819 O VAL A 116 24507 13879 35458 786 3514 -619 O ATOM 820 CB VAL A 116 23.161 40.743 17.064 1.00175.24 C ANISOU 820 CB VAL A 116 22651 11759 32172 969 4557 -605 C ATOM 821 CG1 VAL A 116 22.825 40.187 18.439 1.00167.38 C ANISOU 821 CG1 VAL A 116 21531 10543 31522 1121 4811 -959 C ATOM 822 CG2 VAL A 116 24.263 39.927 16.407 1.00171.16 C ANISOU 822 CG2 VAL A 116 22466 11471 31097 1012 5003 -487 C ATOM 823 N THR A 117 19.592 41.315 16.658 1.00199.35 N ANISOU 823 N THR A 117 25451 14478 35816 575 3504 -1153 N ATOM 824 CA THR A 117 18.502 42.110 17.210 1.00202.07 C ANISOU 824 CA THR A 117 25481 14616 36682 524 3054 -1269 C ATOM 825 C THR A 117 17.872 41.418 18.414 1.00204.56 C ANISOU 825 C THR A 117 25705 14712 37306 628 3269 -1696 C ATOM 826 O THR A 117 17.983 40.202 18.570 1.00204.84 O ANISOU 826 O THR A 117 25972 14760 37098 683 3709 -1958 O ATOM 827 CB THR A 117 17.411 42.386 16.156 1.00204.01 C ANISOU 827 CB THR A 117 25776 14887 36851 289 2593 -1305 C ATOM 828 OG1 THR A 117 16.739 41.165 15.827 1.00210.19 O ANISOU 828 OG1 THR A 117 26821 15670 37373 215 2803 -1671 O ATOM 829 CG2 THR A 117 18.024 42.981 14.897 1.00202.35 C ANISOU 829 CG2 THR A 117 25686 14903 36295 175 2398 -894 C ATOM 830 N GLY A 118 17.214 42.199 19.263 1.00205.81 N ANISOU 830 N GLY A 118 25528 14671 38000 652 2957 -1765 N ATOM 831 CA GLY A 118 16.555 41.661 20.439 1.00202.68 C ANISOU 831 CA GLY A 118 25012 14058 37941 743 3113 -2162 C ATOM 832 C GLY A 118 15.362 40.798 20.076 1.00200.24 C ANISOU 832 C GLY A 118 24865 13693 37523 605 3080 -2553 C ATOM 833 O GLY A 118 14.900 39.988 20.880 1.00194.10 O ANISOU 833 O GLY A 118 24096 12775 36876 672 3329 -2923 O ATOM 834 N THR A 119 14.861 40.976 18.857 1.00161.29 N ANISOU 834 N THR A 119 18077 17781 25424 597 272 4338 N ATOM 835 CA THR A 119 13.728 40.200 18.372 1.00163.39 C ANISOU 835 CA THR A 119 18291 18067 25723 491 -282 4363 C ATOM 836 C THR A 119 14.182 38.845 17.840 1.00162.89 C ANISOU 836 C THR A 119 18427 18047 25416 445 -577 3819 C ATOM 837 O THR A 119 13.631 37.809 18.210 1.00160.50 O ANISOU 837 O THR A 119 18040 17564 25377 360 -914 3663 O ATOM 838 CB THR A 119 12.960 40.948 17.265 1.00166.72 C ANISOU 838 CB THR A 119 18733 18765 25848 482 -472 4727 C ATOM 839 OG1 THR A 119 12.482 42.199 17.775 1.00166.34 O ANISOU 839 OG1 THR A 119 18490 18665 26045 525 -216 5242 O ATOM 840 CG2 THR A 119 11.781 40.119 16.781 1.00167.47 C ANISOU 840 CG2 THR A 119 18768 18875 25986 371 -1053 4744 C ATOM 841 N ARG A 120 15.189 38.860 16.971 1.00162.29 N ANISOU 841 N ARG A 120 18614 18211 24837 502 -449 3533 N ATOM 842 CA ARG A 120 15.740 37.626 16.420 1.00162.26 C ANISOU 842 CA ARG A 120 18820 18269 24561 474 -697 2994 C ATOM 843 C ARG A 120 16.235 36.709 17.534 1.00162.00 C ANISOU 843 C ARG A 120 18740 17929 24884 459 -620 2649 C ATOM 844 O ARG A 120 16.146 35.487 17.428 1.00164.72 O ANISOU 844 O ARG A 120 19143 18200 25242 395 -964 2295 O ATOM 845 CB ARG A 120 16.878 37.927 15.440 1.00159.64 C ANISOU 845 CB ARG A 120 18767 18241 23648 557 -482 2759 C ATOM 846 CG ARG A 120 16.435 38.588 14.142 1.00163.88 C ANISOU 846 CG ARG A 120 19394 19119 23755 565 -637 3010 C ATOM 847 CD ARG A 120 17.614 38.797 13.200 1.00168.42 C ANISOU 847 CD ARG A 120 20245 19993 23753 647 -426 2746 C ATOM 848 NE ARG A 120 17.218 39.442 11.950 1.00174.56 N ANISOU 848 NE ARG A 120 21110 21109 24108 660 -564 2989 N ATOM 849 CZ ARG A 120 18.053 39.718 10.952 1.00175.99 C ANISOU 849 CZ ARG A 120 21520 21601 23748 727 -433 2833 C ATOM 850 NH1 ARG A 120 17.603 40.308 9.852 1.00178.41 N ANISOU 850 NH1 ARG A 120 21885 22207 23696 736 -575 3085 N ATOM 851 NH2 ARG A 120 19.338 39.406 11.053 1.00174.09 N ANISOU 851 NH2 ARG A 120 21448 21379 23320 788 -160 2430 N ATOM 852 N ALA A 121 16.755 37.309 18.601 1.00159.04 N ANISOU 852 N ALA A 121 18256 17373 24799 522 -169 2756 N ATOM 853 CA ALA A 121 17.224 36.550 19.753 1.00155.82 C ANISOU 853 CA ALA A 121 17781 16665 24757 517 -52 2470 C ATOM 854 C ALA A 121 16.110 35.666 20.302 1.00157.34 C ANISOU 854 C ALA A 121 17780 16623 25379 407 -470 2516 C ATOM 855 O ALA A 121 16.262 34.448 20.403 1.00159.47 O ANISOU 855 O ALA A 121 18112 16780 25699 355 -717 2122 O ATOM 856 CB ALA A 121 17.739 37.488 20.833 1.00152.77 C ANISOU 856 CB ALA A 121 17266 16125 24654 600 480 2675 C ATOM 857 N ALA A 122 14.990 36.291 20.650 1.00156.81 N ANISOU 857 N ALA A 122 17476 16484 25619 373 -550 3001 N ATOM 858 CA ALA A 122 13.833 35.568 21.167 1.00157.97 C ANISOU 858 CA ALA A 122 17414 16421 26185 267 -943 3110 C ATOM 859 C ALA A 122 13.331 34.539 20.158 1.00160.07 C ANISOU 859 C ALA A 122 17803 16808 26207 174 -1490 2876 C ATOM 860 O ALA A 122 12.848 33.470 20.534 1.00158.39 O ANISOU 860 O ALA A 122 17512 16407 26263 87 -1822 2708 O ATOM 861 CB ALA A 122 12.723 36.540 21.534 1.00157.00 C ANISOU 861 CB ALA A 122 17035 16259 26359 255 -931 3695 C ATOM 862 N GLY A 123 13.447 34.870 18.876 1.00160.38 N ANISOU 862 N GLY A 123 18032 17164 25739 196 -1584 2868 N ATOM 863 CA GLY A 123 13.035 33.969 17.816 1.00159.54 C ANISOU 863 CA GLY A 123 18062 17208 25348 122 -2088 2639 C ATOM 864 C GLY A 123 13.909 32.733 17.757 1.00157.01 C ANISOU 864 C GLY A 123 17930 16829 24897 114 -2185 2043 C ATOM 865 O GLY A 123 13.411 31.608 17.746 1.00162.10 O ANISOU 865 O GLY A 123 18554 17358 25678 23 -2603 1830 O ATOM 866 N ILE A 124 15.221 32.944 17.721 1.00150.78 N ANISOU 866 N ILE A 124 17323 16121 23847 211 -1797 1773 N ATOM 867 CA ILE A 124 16.176 31.843 17.689 1.00148.36 C ANISOU 867 CA ILE A 124 17206 15767 23398 220 -1836 1197 C ATOM 868 C ILE A 124 16.002 30.942 18.906 1.00145.64 C ANISOU 868 C ILE A 124 16702 15057 23578 161 -1913 1049 C ATOM 869 O ILE A 124 15.933 29.720 18.779 1.00146.25 O ANISOU 869 O ILE A 124 16844 15049 23677 96 -2266 692 O ATOM 870 CB ILE A 124 17.626 32.354 17.645 1.00143.48 C ANISOU 870 CB ILE A 124 16773 15269 22475 341 -1336 984 C ATOM 871 CG1 ILE A 124 17.843 33.233 16.412 1.00150.14 C ANISOU 871 CG1 ILE A 124 17780 16486 22781 400 -1255 1124 C ATOM 872 CG2 ILE A 124 18.602 31.187 17.650 1.00138.60 C ANISOU 872 CG2 ILE A 124 16345 14594 21723 352 -1381 382 C ATOM 873 CD1 ILE A 124 19.198 33.909 16.373 1.00150.07 C ANISOU 873 CD1 ILE A 124 17929 16606 22484 518 -738 992 C ATOM 874 N ILE A 125 15.931 31.556 20.083 1.00141.20 N ANISOU 874 N ILE A 125 15930 14280 23439 186 -1582 1328 N ATOM 875 CA ILE A 125 15.753 30.817 21.328 1.00137.67 C ANISOU 875 CA ILE A 125 15307 13485 23517 138 -1613 1238 C ATOM 876 C ILE A 125 14.563 29.866 21.249 1.00144.05 C ANISOU 876 C ILE A 125 15996 14176 24559 6 -2176 1260 C ATOM 877 O ILE A 125 14.684 28.680 21.559 1.00148.41 O ANISOU 877 O ILE A 125 16574 14554 25262 -49 -2399 904 O ATOM 878 CB ILE A 125 15.565 31.769 22.525 1.00126.89 C ANISOU 878 CB ILE A 125 13693 11936 22583 180 -1225 1644 C ATOM 879 CG1 ILE A 125 16.840 32.578 22.762 1.00124.54 C ANISOU 879 CG1 ILE A 125 13506 11705 22108 308 -655 1567 C ATOM 880 CG2 ILE A 125 15.196 30.988 23.774 1.00121.27 C ANISOU 880 CG2 ILE A 125 12774 10875 22428 121 -1313 1596 C ATOM 881 CD1 ILE A 125 16.748 33.527 23.933 1.00125.55 C ANISOU 881 CD1 ILE A 125 13403 11658 22644 361 -253 1936 C ATOM 882 N ALA A 126 13.417 30.393 20.831 1.00143.71 N ANISOU 882 N ALA A 126 15826 14231 24548 -44 -2406 1680 N ATOM 883 CA ALA A 126 12.210 29.587 20.689 1.00143.80 C ANISOU 883 CA ALA A 126 15715 14153 24768 -172 -2949 1746 C ATOM 884 C ALA A 126 12.456 28.385 19.783 1.00144.45 C ANISOU 884 C ALA A 126 16021 14326 24535 -221 -3348 1261 C ATOM 885 O ALA A 126 12.087 27.259 20.115 1.00142.47 O ANISOU 885 O ALA A 126 15716 13877 24540 -310 -3682 1052 O ATOM 886 CB ALA A 126 11.068 30.434 20.149 1.00145.87 C ANISOU 886 CB ALA A 126 15853 14573 24999 -203 -3116 2248 C ATOM 887 N ILE A 127 13.086 28.634 18.639 1.00146.67 N ANISOU 887 N ILE A 127 16555 14911 24263 -159 -3310 1086 N ATOM 888 CA ILE A 127 13.397 27.575 17.687 1.00150.11 C ANISOU 888 CA ILE A 127 17222 15470 24342 -188 -3666 617 C ATOM 889 C ILE A 127 14.310 26.526 18.309 1.00144.09 C ANISOU 889 C ILE A 127 16549 14500 23698 -179 -3602 115 C ATOM 890 O ILE A 127 14.073 25.325 18.178 1.00141.19 O ANISOU 890 O ILE A 127 16221 14028 23398 -258 -4005 -195 O ATOM 891 CB ILE A 127 14.080 28.135 16.426 1.00155.27 C ANISOU 891 CB ILE A 127 18133 16499 24364 -100 -3552 515 C ATOM 892 CG1 ILE A 127 13.186 29.177 15.752 1.00157.25 C ANISOU 892 CG1 ILE A 127 18305 16969 24475 -105 -3622 1010 C ATOM 893 CG2 ILE A 127 14.418 27.009 15.459 1.00160.68 C ANISOU 893 CG2 ILE A 127 19056 17314 24680 -122 -3924 10 C ATOM 894 CD1 ILE A 127 13.803 29.801 14.519 1.00160.24 C ANISOU 894 CD1 ILE A 127 18920 17726 24240 -19 -3502 956 C ATOM 895 N CYS A 128 15.356 26.989 18.985 1.00141.34 N ANISOU 895 N CYS A 128 16234 14092 23379 -83 -3095 37 N ATOM 896 CA CYS A 128 16.313 26.095 19.623 1.00141.29 C ANISOU 896 CA CYS A 128 16313 13893 23476 -61 -2975 -429 C ATOM 897 C CYS A 128 15.621 25.144 20.591 1.00144.04 C ANISOU 897 C CYS A 128 16461 13898 24370 -166 -3244 -453 C ATOM 898 O CYS A 128 15.910 23.949 20.609 1.00147.26 O ANISOU 898 O CYS A 128 16963 14188 24801 -205 -3484 -881 O ATOM 899 CB CYS A 128 17.394 26.897 20.348 1.00136.72 C ANISOU 899 CB CYS A 128 15748 13282 22919 55 -2363 -414 C ATOM 900 SG CYS A 128 18.423 27.902 19.254 1.00153.58 S ANISOU 900 SG CYS A 128 18142 15810 24401 181 -2015 -459 S ATOM 901 N TRP A 129 14.703 25.679 21.390 1.00142.23 N ANISOU 901 N TRP A 129 15952 13509 24578 -208 -3205 9 N ATOM 902 CA TRP A 129 13.951 24.864 22.337 1.00142.50 C ANISOU 902 CA TRP A 129 15768 13224 25151 -310 -3455 47 C ATOM 903 C TRP A 129 13.102 23.813 21.628 1.00143.59 C ANISOU 903 C TRP A 129 15933 13368 25258 -431 -4074 -95 C ATOM 904 O TRP A 129 13.043 22.660 22.054 1.00142.75 O ANISOU 904 O TRP A 129 15803 13041 25395 -502 -4325 -376 O ATOM 905 CB TRP A 129 13.075 25.741 23.233 1.00140.73 C ANISOU 905 CB TRP A 129 15237 12869 25365 -325 -3299 605 C ATOM 906 CG TRP A 129 13.834 26.395 24.341 1.00139.85 C ANISOU 906 CG TRP A 129 15041 12622 25475 -229 -2745 681 C ATOM 907 CD1 TRP A 129 14.279 27.683 24.383 1.00140.09 C ANISOU 907 CD1 TRP A 129 15075 12787 25364 -124 -2290 934 C ATOM 908 CD2 TRP A 129 14.247 25.786 25.571 1.00142.45 C ANISOU 908 CD2 TRP A 129 15268 12649 26205 -228 -2590 499 C ATOM 909 NE1 TRP A 129 14.940 27.917 25.565 1.00138.13 N ANISOU 909 NE1 TRP A 129 14733 12342 25409 -56 -1863 916 N ATOM 910 CE2 TRP A 129 14.935 26.768 26.311 1.00139.89 C ANISOU 910 CE2 TRP A 129 14890 12300 25963 -117 -2035 651 C ATOM 911 CE3 TRP A 129 14.100 24.507 26.117 1.00146.18 C ANISOU 911 CE3 TRP A 129 15690 12873 26980 -310 -2869 224 C ATOM 912 CZ2 TRP A 129 15.475 26.510 27.571 1.00140.41 C ANISOU 912 CZ2 TRP A 129 14851 12104 26393 -82 -1751 534 C ATOM 913 CZ3 TRP A 129 14.637 24.254 27.367 1.00144.46 C ANISOU 913 CZ3 TRP A 129 15368 12396 27125 -277 -2584 115 C ATOM 914 CH2 TRP A 129 15.315 25.250 28.080 1.00142.53 C ANISOU 914 CH2 TRP A 129 15070 12138 26946 -162 -2031 269 C ATOM 915 N VAL A 130 12.447 24.218 20.545 1.00141.94 N ANISOU 915 N VAL A 130 15771 13411 24749 -455 -4321 102 N ATOM 916 CA VAL A 130 11.643 23.298 19.751 1.00140.86 C ANISOU 916 CA VAL A 130 15672 13315 24535 -563 -4913 -27 C ATOM 917 C VAL A 130 12.516 22.182 19.187 1.00146.91 C ANISOU 917 C VAL A 130 16703 14115 25000 -553 -5085 -637 C ATOM 918 O VAL A 130 12.142 21.009 19.224 1.00149.86 O ANISOU 918 O VAL A 130 17066 14329 25544 -647 -5496 -882 O ATOM 919 CB VAL A 130 10.921 24.024 18.601 1.00136.47 C ANISOU 919 CB VAL A 130 15147 13064 23642 -570 -5102 274 C ATOM 920 CG1 VAL A 130 10.255 23.022 17.673 1.00133.53 C ANISOU 920 CG1 VAL A 130 14855 12760 23122 -669 -5706 67 C ATOM 921 CG2 VAL A 130 9.901 25.009 19.153 1.00137.44 C ANISOU 921 CG2 VAL A 130 14990 13134 24098 -595 -5008 880 C ATOM 922 N LEU A 131 13.684 22.553 18.673 1.00148.31 N ANISOU 922 N LEU A 131 17116 14500 24735 -436 -4769 -880 N ATOM 923 CA LEU A 131 14.631 21.579 18.143 1.00150.14 C ANISOU 923 CA LEU A 131 17611 14784 24650 -406 -4879 -1468 C ATOM 924 C LEU A 131 15.200 20.714 19.262 1.00151.73 C ANISOU 924 C LEU A 131 17772 14661 25218 -417 -4774 -1774 C ATOM 925 O LEU A 131 15.560 19.557 19.043 1.00155.85 O ANISOU 925 O LEU A 131 18432 15113 25669 -444 -5036 -2235 O ATOM 926 CB LEU A 131 15.766 22.281 17.396 1.00145.36 C ANISOU 926 CB LEU A 131 17250 14484 23496 -273 -4519 -1620 C ATOM 927 CG LEU A 131 15.373 23.084 16.156 1.00144.83 C ANISOU 927 CG LEU A 131 17268 14775 22986 -249 -4615 -1382 C ATOM 928 CD1 LEU A 131 16.593 23.764 15.555 1.00144.81 C ANISOU 928 CD1 LEU A 131 17497 15050 22475 -113 -4214 -1540 C ATOM 929 CD2 LEU A 131 14.694 22.190 15.131 1.00144.75 C ANISOU 929 CD2 LEU A 131 17346 14872 22778 -330 -5213 -1571 C ATOM 930 N SER A 132 15.280 21.284 20.460 1.00147.20 N ANISOU 930 N SER A 132 17005 13889 25034 -391 -4391 -1515 N ATOM 931 CA SER A 132 15.798 20.564 21.618 1.00145.22 C ANISOU 931 CA SER A 132 16692 13326 25160 -395 -4252 -1758 C ATOM 932 C SER A 132 14.853 19.445 22.043 1.00151.95 C ANISOU 932 C SER A 132 17387 13913 26434 -534 -4729 -1792 C ATOM 933 O SER A 132 15.294 18.352 22.397 1.00153.60 O ANISOU 933 O SER A 132 17659 13935 26768 -559 -4853 -2194 O ATOM 934 CB SER A 132 16.043 21.522 22.785 1.00135.81 C ANISOU 934 CB SER A 132 15316 12002 24282 -331 -3728 -1437 C ATOM 935 OG SER A 132 17.078 22.438 22.481 1.00134.81 O ANISOU 935 OG SER A 132 15348 12089 23784 -200 -3266 -1472 O ATOM 936 N PHE A 133 13.554 19.725 22.009 1.00153.71 N ANISOU 936 N PHE A 133 17405 14121 26878 -625 -4996 -1367 N ATOM 937 CA PHE A 133 12.553 18.717 22.338 1.00152.54 C ANISOU 937 CA PHE A 133 17096 13740 27123 -766 -5474 -1357 C ATOM 938 C PHE A 133 12.489 17.641 21.260 1.00156.28 C ANISOU 938 C PHE A 133 17771 14307 27300 -824 -5978 -1761 C ATOM 939 O PHE A 133 12.374 16.453 21.561 1.00156.98 O ANISOU 939 O PHE A 133 17848 14176 27621 -904 -6286 -2044 O ATOM 940 CB PHE A 133 11.178 19.359 22.533 1.00152.55 C ANISOU 940 CB PHE A 133 16825 13723 27413 -843 -5621 -783 C ATOM 941 CG PHE A 133 10.979 19.961 23.894 1.00151.85 C ANISOU 941 CG PHE A 133 16468 13418 27810 -828 -5270 -423 C ATOM 942 CD1 PHE A 133 10.477 19.199 24.935 1.00147.72 C ANISOU 942 CD1 PHE A 133 15734 12573 27818 -917 -5424 -398 C ATOM 943 CD2 PHE A 133 11.295 21.288 24.134 1.00155.48 C ANISOU 943 CD2 PHE A 133 16883 13996 28195 -723 -4787 -109 C ATOM 944 CE1 PHE A 133 10.293 19.746 26.191 1.00144.19 C ANISOU 944 CE1 PHE A 133 15035 11936 27813 -896 -5103 -69 C ATOM 945 CE2 PHE A 133 11.113 21.842 25.388 1.00152.43 C ANISOU 945 CE2 PHE A 133 16248 13413 28254 -702 -4468 214 C ATOM 946 CZ PHE A 133 10.611 21.069 26.417 1.00146.72 C ANISOU 946 CZ PHE A 133 15315 12380 28051 -787 -4626 232 C ATOM 947 N ALA A 134 12.564 18.066 20.002 1.00158.38 N ANISOU 947 N ALA A 134 18222 14902 27054 -782 -6062 -1786 N ATOM 948 CA ALA A 134 12.561 17.134 18.882 1.00161.18 C ANISOU 948 CA ALA A 134 18786 15386 27069 -820 -6521 -2176 C ATOM 949 C ALA A 134 13.726 16.159 19.003 1.00164.72 C ANISOU 949 C ALA A 134 19439 15739 27410 -773 -6470 -2765 C ATOM 950 O ALA A 134 13.546 14.945 18.909 1.00171.48 O ANISOU 950 O ALA A 134 20336 16450 28370 -852 -6878 -3089 O ATOM 951 CB ALA A 134 12.633 17.889 17.564 1.00159.39 C ANISOU 951 CB ALA A 134 18733 15553 26275 -754 -6523 -2106 C ATOM 952 N ILE A 135 14.920 16.701 19.220 1.00161.69 N ANISOU 952 N ILE A 135 19180 15433 26821 -645 -5968 -2901 N ATOM 953 CA ILE A 135 16.124 15.888 19.347 1.00160.34 C ANISOU 953 CA ILE A 135 19210 15191 26521 -584 -5860 -3453 C ATOM 954 C ILE A 135 16.148 15.105 20.657 1.00156.69 C ANISOU 954 C ILE A 135 18592 14338 26606 -639 -5843 -3554 C ATOM 955 O ILE A 135 16.252 13.880 20.656 1.00158.15 O ANISOU 955 O ILE A 135 18849 14368 26872 -692 -6163 -3945 O ATOM 956 CB ILE A 135 17.397 16.754 19.257 1.00155.17 C ANISOU 956 CB ILE A 135 18719 14731 25506 -431 -5300 -3543 C ATOM 957 CG1 ILE A 135 17.479 17.440 17.891 1.00152.63 C ANISOU 957 CG1 ILE A 135 18578 14812 24603 -371 -5326 -3494 C ATOM 958 CG2 ILE A 135 18.634 15.907 19.509 1.00152.23 C ANISOU 958 CG2 ILE A 135 18535 14263 25044 -368 -5171 -4102 C ATOM 959 CD1 ILE A 135 18.678 18.348 17.734 1.00145.40 C ANISOU 959 CD1 ILE A 135 17818 14108 23320 -225 -4786 -3549 C ATOM 960 N GLY A 136 16.047 15.823 21.772 1.00152.01 N ANISOU 960 N GLY A 136 17782 13588 26386 -623 -5469 -3198 N ATOM 961 CA GLY A 136 16.120 15.217 23.089 1.00148.09 C ANISOU 961 CA GLY A 136 17124 12735 26409 -661 -5387 -3256 C ATOM 962 C GLY A 136 15.094 14.126 23.337 1.00154.83 C ANISOU 962 C GLY A 136 17830 13345 27653 -812 -5915 -3265 C ATOM 963 O GLY A 136 15.330 13.214 24.130 1.00158.90 O ANISOU 963 O GLY A 136 18301 13584 28490 -848 -5969 -3504 O ATOM 964 N LEU A 137 13.952 14.218 22.663 1.00157.90 N ANISOU 964 N LEU A 137 18140 13836 28017 -902 -6307 -3001 N ATOM 965 CA LEU A 137 12.891 13.230 22.828 1.00155.83 C ANISOU 965 CA LEU A 137 17730 13360 28119 -1054 -6833 -2977 C ATOM 966 C LEU A 137 12.687 12.393 21.567 1.00163.50 C ANISOU 966 C LEU A 137 18900 14474 28747 -1105 -7353 -3307 C ATOM 967 O LEU A 137 11.586 11.909 21.304 1.00165.43 O ANISOU 967 O LEU A 137 19032 14658 29166 -1230 -7827 -3177 O ATOM 968 CB LEU A 137 11.579 13.904 23.238 1.00148.01 C ANISOU 968 CB LEU A 137 16437 12319 27480 -1136 -6909 -2377 C ATOM 969 CG LEU A 137 11.578 14.624 24.589 1.00137.38 C ANISOU 969 CG LEU A 137 14848 10792 26558 -1102 -6464 -2021 C ATOM 970 CD1 LEU A 137 10.217 15.244 24.866 1.00135.70 C ANISOU 970 CD1 LEU A 137 14347 10554 26660 -1184 -6594 -1442 C ATOM 971 CD2 LEU A 137 11.973 13.671 25.707 1.00131.66 C ANISOU 971 CD2 LEU A 137 14051 9731 26244 -1130 -6428 -2272 C ATOM 972 N THR A 138 13.754 12.228 20.791 1.00169.64 N ANISOU 972 N THR A 138 19973 15447 29037 -1007 -7262 -3737 N ATOM 973 CA THR A 138 13.714 11.384 19.601 1.00179.54 C ANISOU 973 CA THR A 138 21438 16841 29936 -1037 -7732 -4113 C ATOM 974 C THR A 138 13.449 9.913 19.941 1.00185.66 C ANISOU 974 C THR A 138 22186 17319 31035 -1146 -8168 -4435 C ATOM 975 O THR A 138 12.737 9.226 19.209 1.00189.43 O ANISOU 975 O THR A 138 22692 17823 31458 -1237 -8690 -4533 O ATOM 976 CB THR A 138 15.014 11.499 18.773 1.00179.18 C ANISOU 976 CB THR A 138 21715 17064 29303 -896 -7509 -4530 C ATOM 977 OG1 THR A 138 15.176 12.848 18.318 1.00177.03 O ANISOU 977 OG1 THR A 138 21473 17088 28703 -804 -7158 -4221 O ATOM 978 CG2 THR A 138 14.966 10.569 17.570 1.00183.05 C ANISOU 978 CG2 THR A 138 22419 17693 29439 -923 -8011 -4938 C ATOM 979 N PRO A 139 14.030 9.421 21.050 1.00184.45 N ANISOU 979 N PRO A 139 21978 16884 31222 -1137 -7956 -4605 N ATOM 980 CA PRO A 139 13.734 8.050 21.480 1.00184.30 C ANISOU 980 CA PRO A 139 21907 16556 31562 -1247 -8356 -4870 C ATOM 981 C PRO A 139 12.240 7.819 21.699 1.00184.47 C ANISOU 981 C PRO A 139 21665 16424 32001 -1408 -8774 -4495 C ATOM 982 O PRO A 139 11.780 6.681 21.620 1.00190.30 O ANISOU 982 O PRO A 139 22391 16985 32929 -1517 -9245 -4706 O ATOM 983 CB PRO A 139 14.484 7.935 22.809 1.00181.13 C ANISOU 983 CB PRO A 139 21426 15892 31504 -1202 -7949 -4945 C ATOM 984 CG PRO A 139 15.617 8.883 22.674 1.00179.75 C ANISOU 984 CG PRO A 139 21409 15942 30948 -1040 -7401 -5001 C ATOM 985 CD PRO A 139 15.086 10.037 21.874 1.00180.57 C ANISOU 985 CD PRO A 139 21499 16356 30754 -1017 -7351 -4616 C ATOM 986 N MET A 140 11.496 8.886 21.971 1.00181.41 N ANISOU 986 N MET A 140 21068 16102 31756 -1423 -8605 -3945 N ATOM 987 CA MET A 140 10.053 8.778 22.157 1.00181.36 C ANISOU 987 CA MET A 140 20803 15977 32128 -1569 -8979 -3552 C ATOM 988 C MET A 140 9.332 8.650 20.820 1.00186.77 C ANISOU 988 C MET A 140 21585 16893 32486 -1625 -9453 -3559 C ATOM 989 O MET A 140 8.167 8.257 20.767 1.00191.05 O ANISOU 989 O MET A 140 21960 17337 33293 -1760 -9883 -3356 O ATOM 990 CB MET A 140 9.510 9.981 22.932 1.00178.12 C ANISOU 990 CB MET A 140 20131 15561 31986 -1558 -8627 -2960 C ATOM 991 CG MET A 140 10.046 10.100 24.348 1.00176.22 C ANISOU 991 CG MET A 140 19749 15072 32136 -1516 -8192 -2899 C ATOM 992 SD MET A 140 9.124 11.287 25.341 1.00171.45 S ANISOU 992 SD MET A 140 18785 14405 31955 -1534 -7909 -2188 S ATOM 993 CE MET A 140 7.493 10.548 25.324 1.00134.10 C ANISOU 993 CE MET A 140 13816 9512 27622 -1733 -8547 -1939 C ATOM 994 N LEU A 141 10.034 8.984 19.742 1.00187.23 N ANISOU 994 N LEU A 141 21910 17262 31966 -1519 -9370 -3794 N ATOM 995 CA LEU A 141 9.464 8.911 18.402 1.00190.16 C ANISOU 995 CA LEU A 141 22397 17888 31967 -1551 -9789 -3829 C ATOM 996 C LEU A 141 9.418 7.471 17.898 1.00188.18 C ANISOU 996 C LEU A 141 22277 17528 31693 -1627 -10323 -4308 C ATOM 997 O LEU A 141 8.916 7.202 16.806 1.00191.77 O ANISOU 997 O LEU A 141 22828 18161 31876 -1666 -10740 -4393 O ATOM 998 CB LEU A 141 10.262 9.786 17.432 1.00192.15 C ANISOU 998 CB LEU A 141 22887 18522 31600 -1405 -9501 -3910 C ATOM 999 CG LEU A 141 10.372 11.268 17.802 1.00188.61 C ANISOU 999 CG LEU A 141 22336 18210 31117 -1319 -8969 -3452 C ATOM 1000 CD1 LEU A 141 11.273 12.005 16.822 1.00190.50 C ANISOU 1000 CD1 LEU A 141 22833 18818 30732 -1175 -8696 -3593 C ATOM 1001 CD2 LEU A 141 8.995 11.910 17.862 1.00186.98 C ANISOU 1001 CD2 LEU A 141 21872 18018 31152 -1411 -9131 -2880 C ATOM 1002 N GLY A 142 9.942 6.550 18.701 1.00212.91 N ANISOU 1002 N GLY A 142 23536 22715 34645 2593 1085 731 N ATOM 1003 CA GLY A 142 9.952 5.141 18.349 1.00208.82 C ANISOU 1003 CA GLY A 142 23075 22181 34088 2373 1071 542 C ATOM 1004 C GLY A 142 11.330 4.521 18.473 1.00201.65 C ANISOU 1004 C GLY A 142 22345 20873 33400 2310 1122 581 C ATOM 1005 O GLY A 142 11.476 3.299 18.472 1.00201.60 O ANISOU 1005 O GLY A 142 22410 20773 33416 2096 1108 435 O ATOM 1006 N TRP A 143 12.345 5.372 18.582 1.00195.22 N ANISOU 1006 N TRP A 143 21602 19822 32752 2500 1180 779 N ATOM 1007 CA TRP A 143 13.727 4.921 18.700 1.00187.72 C ANISOU 1007 CA TRP A 143 20822 18481 32022 2469 1234 840 C ATOM 1008 C TRP A 143 14.046 4.551 20.146 1.00181.63 C ANISOU 1008 C TRP A 143 20138 17406 31467 2271 1210 852 C ATOM 1009 O TRP A 143 14.840 5.221 20.805 1.00178.94 O ANISOU 1009 O TRP A 143 19866 16799 31322 2362 1243 1020 O ATOM 1010 CB TRP A 143 14.677 6.022 18.222 1.00185.79 C ANISOU 1010 CB TRP A 143 20615 18112 31863 2759 1306 1053 C ATOM 1011 CG TRP A 143 16.071 5.551 17.935 1.00186.73 C ANISOU 1011 CG TRP A 143 20895 17897 32156 2766 1369 1103 C ATOM 1012 CD1 TRP A 143 16.952 5.006 18.823 1.00187.68 C ANISOU 1012 CD1 TRP A 143 21155 17642 32512 2619 1380 1125 C ATOM 1013 CD2 TRP A 143 16.752 5.603 16.675 1.00188.93 C ANISOU 1013 CD2 TRP A 143 21209 18187 32387 2933 1429 1139 C ATOM 1014 NE1 TRP A 143 18.136 4.705 18.193 1.00190.15 N ANISOU 1014 NE1 TRP A 143 21590 17732 32928 2683 1444 1171 N ATOM 1015 CE2 TRP A 143 18.039 5.063 16.873 1.00190.86 C ANISOU 1015 CE2 TRP A 143 21619 18054 32847 2875 1475 1180 C ATOM 1016 CE3 TRP A 143 16.397 6.050 15.398 1.00189.22 C ANISOU 1016 CE3 TRP A 143 21155 18518 32220 3125 1448 1139 C ATOM 1017 CZ2 TRP A 143 18.972 4.958 15.842 1.00190.97 C ANISOU 1017 CZ2 TRP A 143 21707 17977 32877 3002 1539 1222 C ATOM 1018 CZ3 TRP A 143 17.325 5.944 14.376 1.00189.78 C ANISOU 1018 CZ3 TRP A 143 21301 18499 32308 3251 1511 1181 C ATOM 1019 CH2 TRP A 143 18.596 5.402 14.604 1.00190.33 C ANISOU 1019 CH2 TRP A 143 21533 18190 32592 3189 1556 1221 C ATOM 1020 N ASN A 144 13.423 3.483 20.637 1.00178.84 N ANISOU 1020 N ASN A 144 19780 17094 31078 2000 1153 672 N ATOM 1021 CA ASN A 144 13.608 3.070 22.025 1.00173.71 C ANISOU 1021 CA ASN A 144 19204 16181 30618 1794 1124 667 C ATOM 1022 C ASN A 144 13.687 1.554 22.207 1.00173.00 C ANISOU 1022 C ASN A 144 19198 15974 30560 1504 1097 482 C ATOM 1023 O ASN A 144 13.449 0.789 21.272 1.00170.42 O ANISOU 1023 O ASN A 144 18858 15804 30089 1449 1092 342 O ATOM 1024 CB ASN A 144 12.499 3.652 22.906 1.00169.47 C ANISOU 1024 CB ASN A 144 18543 15831 30016 1759 1064 669 C ATOM 1025 CG ASN A 144 11.116 3.207 22.473 1.00170.07 C ANISOU 1025 CG ASN A 144 18481 16303 29833 1657 1003 486 C ATOM 1026 OD1 ASN A 144 10.845 2.012 22.355 1.00175.22 O ANISOU 1026 OD1 ASN A 144 19158 16986 30432 1439 972 307 O ATOM 1027 ND2 ASN A 144 10.230 4.168 22.240 1.00167.06 N ANISOU 1027 ND2 ASN A 144 17955 16227 29292 1815 983 529 N ATOM 1028 N ASN A 145 14.027 1.130 23.421 1.00172.07 N ANISOU 1028 N ASN A 145 19167 15578 30635 1320 1078 485 N ATOM 1029 CA ASN A 145 14.122 -0.289 23.742 1.00171.11 C ANISOU 1029 CA ASN A 145 19130 15318 30565 1034 1049 318 C ATOM 1030 C ASN A 145 13.101 -0.715 24.791 1.00173.32 C ANISOU 1030 C ASN A 145 19348 15694 30814 801 972 205 C ATOM 1031 O ASN A 145 13.432 -1.424 25.741 1.00178.92 O ANISOU 1031 O ASN A 145 20150 16150 31683 591 953 165 O ATOM 1032 CB ASN A 145 15.534 -0.643 24.213 1.00169.10 C ANISOU 1032 CB ASN A 145 19055 14619 30578 990 1096 401 C ATOM 1033 CG ASN A 145 16.560 -0.555 23.102 1.00146.30 C ANISOU 1033 CG ASN A 145 16243 11630 27714 1168 1169 470 C ATOM 1034 OD1 ASN A 145 16.211 -0.473 21.924 1.00147.64 O ANISOU 1034 OD1 ASN A 145 16343 12061 27695 1286 1180 423 O ATOM 1035 ND2 ASN A 145 17.835 -0.575 23.471 1.00146.81 N ANISOU 1035 ND2 ASN A 145 16453 11316 28012 1188 1218 581 N ATOM 1036 N CYS A 146 11.859 -0.277 24.614 1.00170.90 N ANISOU 1036 N CYS A 146 18882 15752 30299 840 928 154 N ATOM 1037 CA CYS A 146 10.790 -0.619 25.544 1.00170.70 C ANISOU 1037 CA CYS A 146 18781 15857 30219 631 853 44 C ATOM 1038 C CYS A 146 10.298 -2.046 25.326 1.00174.29 C ANISOU 1038 C CYS A 146 19245 16400 30576 368 808 -183 C ATOM 1039 O CYS A 146 9.616 -2.334 24.343 1.00176.80 O ANISOU 1039 O CYS A 146 19481 17018 30679 383 792 -301 O ATOM 1040 CB CYS A 146 9.624 0.363 25.407 1.00167.72 C ANISOU 1040 CB CYS A 146 18228 15848 29650 770 821 68 C ATOM 1041 SG CYS A 146 10.035 2.076 25.809 1.00222.60 S ANISOU 1041 SG CYS A 146 25151 22718 36708 1063 861 329 S ATOM 1042 N GLY A 147 10.652 -2.936 26.247 1.00174.05 N ANISOU 1042 N GLY A 147 19319 16106 30705 128 786 -244 N ATOM 1043 CA GLY A 147 10.205 -4.315 26.183 1.00177.88 C ANISOU 1043 CA GLY A 147 19821 16647 31117 -141 739 -457 C ATOM 1044 C GLY A 147 11.121 -5.213 25.374 1.00183.77 C ANISOU 1044 C GLY A 147 20691 17224 31911 -177 779 -516 C ATOM 1045 O GLY A 147 10.738 -6.321 24.996 1.00187.71 O ANISOU 1045 O GLY A 147 21193 17818 32310 -360 746 -698 O ATOM 1046 N GLN A 148 12.332 -4.737 25.105 1.00184.25 N ANISOU 1046 N GLN A 148 20852 17034 32122 -2 850 -364 N ATOM 1047 CA GLN A 148 13.314 -5.527 24.372 1.00189.11 C ANISOU 1047 CA GLN A 148 21593 17459 32802 -22 893 -403 C ATOM 1048 C GLN A 148 13.863 -6.652 25.241 1.00195.64 C ANISOU 1048 C GLN A 148 22555 17966 33813 -289 874 -480 C ATOM 1049 O GLN A 148 14.180 -6.438 26.412 1.00200.27 O ANISOU 1049 O GLN A 148 23195 18318 34582 -354 868 -396 O ATOM 1050 CB GLN A 148 14.455 -4.641 23.866 1.00182.65 C ANISOU 1050 CB GLN A 148 20840 16464 32095 248 974 -210 C ATOM 1051 CG GLN A 148 14.029 -3.619 22.826 1.00179.88 C ANISOU 1051 CG GLN A 148 20367 16420 31558 519 999 -140 C ATOM 1052 CD GLN A 148 13.434 -4.260 21.587 1.00179.95 C ANISOU 1052 CD GLN A 148 20313 16725 31335 501 985 -303 C ATOM 1053 OE1 GLN A 148 13.718 -5.416 21.273 1.00181.29 O ANISOU 1053 OE1 GLN A 148 20561 16809 31513 338 980 -437 O ATOM 1054 NE2 GLN A 148 12.604 -3.508 20.874 1.00180.15 N ANISOU 1054 NE2 GLN A 148 20196 17102 31153 670 979 -292 N ATOM 1055 N PRO A 149 13.975 -7.859 24.665 1.00191.18 N ANISOU 1055 N PRO A 149 22048 17392 33201 -443 865 -640 N ATOM 1056 CA PRO A 149 14.443 -9.056 25.372 1.00187.70 C ANISOU 1056 CA PRO A 149 21735 16669 32914 -710 843 -737 C ATOM 1057 C PRO A 149 15.711 -8.793 26.178 1.00182.54 C ANISOU 1057 C PRO A 149 21225 15591 32543 -681 889 -579 C ATOM 1058 O PRO A 149 15.610 -8.597 27.389 1.00179.30 O ANISOU 1058 O PRO A 149 20823 15045 32256 -776 863 -530 O ATOM 1059 CB PRO A 149 14.734 -10.035 24.234 1.00189.12 C ANISOU 1059 CB PRO A 149 21965 16883 33008 -755 858 -870 C ATOM 1060 CG PRO A 149 13.787 -9.635 23.159 1.00189.01 C ANISOU 1060 CG PRO A 149 21803 17285 32728 -619 848 -924 C ATOM 1061 CD PRO A 149 13.672 -8.138 23.249 1.00189.36 C ANISOU 1061 CD PRO A 149 21762 17423 32761 -362 875 -739 C ATOM 1062 N GLY A 158 7.305 -8.648 37.445 1.00255.41 N ANISOU 1062 N GLY A 158 29401 24036 43606 -3901 -5380 2810 N ATOM 1063 CA GLY A 158 8.099 -7.453 37.663 1.00250.18 C ANISOU 1063 CA GLY A 158 28406 23766 42884 -3627 -4469 2539 C ATOM 1064 C GLY A 158 7.246 -6.213 37.851 1.00246.52 C ANISOU 1064 C GLY A 158 27289 23618 42760 -3824 -4024 2789 C ATOM 1065 O GLY A 158 6.969 -5.803 38.979 1.00244.44 O ANISOU 1065 O GLY A 158 26374 23709 42792 -4108 -3642 2961 O ATOM 1066 N CYS A 159 6.828 -5.614 36.741 1.00245.21 N ANISOU 1066 N CYS A 159 27301 23320 42549 -3668 -4075 2807 N ATOM 1067 CA CYS A 159 6.003 -4.412 36.780 1.00241.81 C ANISOU 1067 CA CYS A 159 26299 23159 42418 -3824 -3677 3035 C ATOM 1068 C CYS A 159 4.604 -4.682 36.235 1.00240.63 C ANISOU 1068 C CYS A 159 26185 22749 42494 -4133 -4351 3438 C ATOM 1069 O CYS A 159 3.679 -3.899 36.456 1.00238.23 O ANISOU 1069 O CYS A 159 25351 22653 42514 -4383 -4164 3723 O ATOM 1070 CB CYS A 159 6.667 -3.279 35.992 1.00240.94 C ANISOU 1070 CB CYS A 159 26277 23173 42095 -3385 -3060 2723 C ATOM 1071 SG CYS A 159 8.300 -2.792 36.604 1.00191.85 S ANISOU 1071 SG CYS A 159 19967 17299 35629 -3012 -2191 2244 S ATOM 1072 N GLY A 160 4.456 -5.794 35.523 1.00241.79 N ANISOU 1072 N GLY A 160 26960 22442 42466 -4112 -5137 3457 N ATOM 1073 CA GLY A 160 3.178 -6.167 34.945 1.00242.29 C ANISOU 1073 CA GLY A 160 27129 22217 42714 -4389 -5841 3821 C ATOM 1074 C GLY A 160 2.997 -5.623 33.541 1.00236.54 C ANISOU 1074 C GLY A 160 26771 21281 41823 -4100 -5923 3738 C ATOM 1075 O GLY A 160 3.707 -4.709 33.123 1.00229.89 O ANISOU 1075 O GLY A 160 25949 20598 40801 -3735 -5323 3450 O ATOM 1076 N GLU A 161 2.042 -6.190 32.810 1.00236.65 N ANISOU 1076 N GLU A 161 27081 20935 41900 -4265 -6670 3991 N ATOM 1077 CA GLU A 161 1.766 -5.757 31.445 1.00231.20 C ANISOU 1077 CA GLU A 161 26767 20012 41067 -4018 -6833 3944 C ATOM 1078 C GLU A 161 1.363 -4.287 31.413 1.00217.57 C ANISOU 1078 C GLU A 161 24496 18629 39544 -4008 -6187 4021 C ATOM 1079 O GLU A 161 0.606 -3.822 32.265 1.00211.10 O ANISOU 1079 O GLU A 161 23012 18099 39097 -4368 -5977 4317 O ATOM 1080 CB GLU A 161 0.675 -6.624 30.812 1.00240.16 C ANISOU 1080 CB GLU A 161 28228 20729 42294 -4267 -7762 4256 C ATOM 1081 CG GLU A 161 -0.666 -6.569 31.528 1.00244.67 C ANISOU 1081 CG GLU A 161 28200 21432 43332 -4805 -7972 4737 C ATOM 1082 CD GLU A 161 -1.690 -7.509 30.919 1.00251.30 C ANISOU 1082 CD GLU A 161 29389 21844 44249 -5050 -8916 5032 C ATOM 1083 OE1 GLU A 161 -2.875 -7.431 31.306 1.00253.86 O ANISOU 1083 OE1 GLU A 161 29273 22237 44945 -5472 -9141 5433 O ATOM 1084 OE2 GLU A 161 -1.310 -8.327 30.054 1.00253.56 O ANISOU 1084 OE2 GLU A 161 30390 21727 44224 -4821 -9433 4862 O ATOM 1085 N GLY A 162 1.876 -3.561 30.426 1.00215.75 N ANISOU 1085 N GLY A 162 24552 18361 39061 -3592 -5873 3752 N ATOM 1086 CA GLY A 162 1.616 -2.138 30.312 1.00214.28 C ANISOU 1086 CA GLY A 162 23906 18487 39022 -3527 -5229 3779 C ATOM 1087 C GLY A 162 2.759 -1.313 30.869 1.00209.38 C ANISOU 1087 C GLY A 162 23019 18254 38281 -3259 -4326 3447 C ATOM 1088 O GLY A 162 3.278 -0.420 30.200 1.00205.70 O ANISOU 1088 O GLY A 162 22658 17867 37631 -2901 -3850 3200 O ATOM 1089 N GLN A 163 3.154 -1.617 32.102 1.00209.46 N ANISOU 1089 N GLN A 163 22685 18505 38394 -3434 -4092 3439 N ATOM 1090 CA GLN A 163 4.258 -0.919 32.749 1.00205.95 C ANISOU 1090 CA GLN A 163 21967 18436 37848 -3206 -3252 3129 C ATOM 1091 C GLN A 163 5.594 -1.580 32.421 1.00199.31 C ANISOU 1091 C GLN A 163 21738 17416 36575 -2811 -3271 2704 C ATOM 1092 O GLN A 163 5.690 -2.805 32.346 1.00197.60 O ANISOU 1092 O GLN A 163 21963 16886 36230 -2860 -3902 2704 O ATOM 1093 CB GLN A 163 4.049 -0.870 34.265 1.00208.54 C ANISOU 1093 CB GLN A 163 21603 19131 38501 -3581 -2954 3323 C ATOM 1094 CG GLN A 163 2.802 -0.112 34.697 1.00208.69 C ANISOU 1094 CG GLN A 163 20953 19386 38954 -3961 -2834 3726 C ATOM 1095 CD GLN A 163 2.650 -0.048 36.205 1.00206.35 C ANISOU 1095 CD GLN A 163 19978 19461 38965 -4314 -2510 3901 C ATOM 1096 OE1 GLN A 163 3.419 -0.661 36.945 1.00206.38 O ANISOU 1096 OE1 GLN A 163 20023 19523 38867 -4301 -2439 3744 O ATOM 1097 NE2 GLN A 163 1.653 0.698 36.669 1.00204.21 N ANISOU 1097 NE2 GLN A 163 19077 19443 39070 -4628 -2312 4229 N ATOM 1098 N VAL A 164 6.622 -0.760 32.226 1.00191.74 N ANISOU 1098 N VAL A 164 20801 16660 35393 -2421 -2575 2341 N ATOM 1099 CA VAL A 164 7.949 -1.256 31.882 1.00184.47 C ANISOU 1099 CA VAL A 164 20438 15601 34053 -2011 -2511 1911 C ATOM 1100 C VAL A 164 8.986 -0.802 32.903 1.00173.42 C ANISOU 1100 C VAL A 164 18662 14608 32621 -1904 -1742 1658 C ATOM 1101 O VAL A 164 8.961 0.343 33.355 1.00168.81 O ANISOU 1101 O VAL A 164 17522 14408 32211 -1926 -1053 1671 O ATOM 1102 CB VAL A 164 8.382 -0.773 30.481 1.00183.00 C ANISOU 1102 CB VAL A 164 20769 15219 33542 -1559 -2430 1644 C ATOM 1103 CG1 VAL A 164 9.815 -1.196 30.188 1.00180.49 C ANISOU 1103 CG1 VAL A 164 20980 14804 32794 -1124 -2282 1182 C ATOM 1104 CG2 VAL A 164 7.432 -1.306 29.419 1.00188.46 C ANISOU 1104 CG2 VAL A 164 21898 15478 34230 -1636 -3228 1866 C ATOM 1105 N ALA A 165 9.891 -1.705 33.270 1.00167.75 N ANISOU 1105 N ALA A 165 18251 13804 31684 -1788 -1867 1430 N ATOM 1106 CA ALA A 165 10.975 -1.371 34.186 1.00158.25 C ANISOU 1106 CA ALA A 165 16761 12956 30411 -1652 -1173 1155 C ATOM 1107 C ALA A 165 11.780 -0.206 33.628 1.00151.64 C ANISOU 1107 C ALA A 165 15934 12312 29371 -1233 -440 822 C ATOM 1108 O ALA A 165 12.614 -0.384 32.739 1.00143.58 O ANISOU 1108 O ALA A 165 15493 11084 27976 -825 -471 491 O ATOM 1109 CB ALA A 165 11.869 -2.578 34.415 1.00160.91 C ANISOU 1109 CB ALA A 165 17557 13100 30480 -1527 -1492 926 C ATOM 1110 N CYS A 166 11.522 0.987 34.155 1.00154.61 N ANISOU 1110 N CYS A 166 15664 13086 29993 -1337 219 913 N ATOM 1111 CA CYS A 166 12.136 2.207 33.644 1.00148.06 C ANISOU 1111 CA CYS A 166 14778 12461 29019 -981 932 644 C ATOM 1112 C CYS A 166 13.597 2.334 34.060 1.00139.10 C ANISOU 1112 C CYS A 166 13694 11534 27623 -656 1522 215 C ATOM 1113 O CYS A 166 13.918 2.969 35.065 1.00119.47 O ANISOU 1113 O CYS A 166 10649 9453 25291 -736 2157 177 O ATOM 1114 CB CYS A 166 11.348 3.434 34.103 1.00143.39 C ANISOU 1114 CB CYS A 166 13467 12228 28788 -1213 1433 895 C ATOM 1115 SG CYS A 166 11.863 4.979 33.322 1.00245.15 S ANISOU 1115 SG CYS A 166 26297 25322 41526 -810 2228 627 S ATOM 1116 N LEU A 167 14.478 1.721 33.277 1.00152.86 N ANISOU 1116 N LEU A 167 16113 12996 28969 -288 1302 -110 N ATOM 1117 CA LEU A 167 15.912 1.801 33.515 1.00157.46 C ANISOU 1117 CA LEU A 167 16827 13738 29265 64 1822 -545 C ATOM 1118 C LEU A 167 16.569 2.464 32.311 1.00155.68 C ANISOU 1118 C LEU A 167 17009 13425 28716 533 2120 -866 C ATOM 1119 O LEU A 167 16.408 2.008 31.181 1.00160.22 O ANISOU 1119 O LEU A 167 18173 13617 29086 699 1601 -894 O ATOM 1120 CB LEU A 167 16.495 0.404 33.738 1.00165.70 C ANISOU 1120 CB LEU A 167 18322 14535 30103 98 1310 -675 C ATOM 1121 CG LEU A 167 15.738 -0.502 34.715 1.00167.01 C ANISOU 1121 CG LEU A 167 18238 14666 30552 -369 810 -332 C ATOM 1122 CD1 LEU A 167 16.446 -1.839 34.867 1.00164.86 C ANISOU 1122 CD1 LEU A 167 18458 14149 30033 -279 350 -509 C ATOM 1123 CD2 LEU A 167 15.565 0.172 36.068 1.00167.18 C ANISOU 1123 CD2 LEU A 167 17455 15156 30910 -657 1392 -186 C ATOM 1124 N PHE A 168 17.306 3.542 32.558 1.00150.83 N ANISOU 1124 N PHE A 168 16082 13168 28058 745 2955 -1107 N ATOM 1125 CA PHE A 168 17.864 4.355 31.480 1.00157.21 C ANISOU 1125 CA PHE A 168 17184 13947 28600 1166 3330 -1388 C ATOM 1126 C PHE A 168 18.552 3.533 30.391 1.00161.69 C ANISOU 1126 C PHE A 168 18582 14111 28743 1536 2889 -1670 C ATOM 1127 O PHE A 168 18.255 3.691 29.208 1.00166.51 O ANISOU 1127 O PHE A 168 19592 14461 29215 1711 2643 -1673 O ATOM 1128 CB PHE A 168 18.828 5.406 32.040 1.00161.27 C ANISOU 1128 CB PHE A 168 17303 14899 29075 1368 4282 -1674 C ATOM 1129 CG PHE A 168 19.357 6.357 31.002 1.00162.85 C ANISOU 1129 CG PHE A 168 17735 15109 29033 1775 4731 -1945 C ATOM 1130 CD1 PHE A 168 18.542 7.342 30.466 1.00159.41 C ANISOU 1130 CD1 PHE A 168 17087 14723 28760 1720 4891 -1754 C ATOM 1131 CD2 PHE A 168 20.669 6.270 30.567 1.00161.69 C ANISOU 1131 CD2 PHE A 168 18014 14924 28495 2214 4997 -2389 C ATOM 1132 CE1 PHE A 168 19.024 8.218 29.512 1.00154.89 C ANISOU 1132 CE1 PHE A 168 16732 14156 27963 2092 5304 -2001 C ATOM 1133 CE2 PHE A 168 21.158 7.144 29.615 1.00156.37 C ANISOU 1133 CE2 PHE A 168 17554 14260 27597 2585 5415 -2636 C ATOM 1134 CZ PHE A 168 20.334 8.119 29.086 1.00153.71 C ANISOU 1134 CZ PHE A 168 17009 13968 27424 2523 5568 -2441 C ATOM 1135 N GLU A 169 19.463 2.654 30.794 1.00162.27 N ANISOU 1135 N GLU A 169 18914 14130 28610 1655 2785 -1904 N ATOM 1136 CA GLU A 169 20.230 1.860 29.837 1.00167.37 C ANISOU 1136 CA GLU A 169 20341 14415 28836 2026 2409 -2202 C ATOM 1137 C GLU A 169 19.370 0.821 29.116 1.00167.14 C ANISOU 1137 C GLU A 169 20800 13914 28791 1888 1456 -1963 C ATOM 1138 O GLU A 169 19.699 0.395 28.009 1.00164.75 O ANISOU 1138 O GLU A 169 21155 13272 28170 2191 1109 -2144 O ATOM 1139 CB GLU A 169 21.417 1.177 30.525 1.00173.60 C ANISOU 1139 CB GLU A 169 21254 15284 29423 2177 2546 -2508 C ATOM 1140 CG GLU A 169 21.036 0.086 31.517 1.00182.61 C ANISOU 1140 CG GLU A 169 22265 16371 30748 1810 2055 -2284 C ATOM 1141 CD GLU A 169 20.443 0.633 32.802 1.00189.02 C ANISOU 1141 CD GLU A 169 22267 17572 31979 1405 2421 -2008 C ATOM 1142 OE1 GLU A 169 20.606 1.844 33.069 1.00190.13 O ANISOU 1142 OE1 GLU A 169 21939 18072 32228 1456 3159 -2068 O ATOM 1143 OE2 GLU A 169 19.819 -0.150 33.549 1.00190.68 O ANISOU 1143 OE2 GLU A 169 22313 17729 32409 1035 1973 -1731 O ATOM 1144 N ASP A 170 18.268 0.423 29.744 1.00169.70 N ANISOU 1144 N ASP A 170 20798 14219 29459 1429 1039 -1555 N ATOM 1145 CA ASP A 170 17.402 -0.615 29.193 1.00174.02 C ANISOU 1145 CA ASP A 170 21760 14333 30026 1248 116 -1300 C ATOM 1146 C ASP A 170 16.289 -0.063 28.304 1.00171.40 C ANISOU 1146 C ASP A 170 21435 13854 29835 1156 -114 -1035 C ATOM 1147 O ASP A 170 15.810 -0.750 27.403 1.00176.09 O ANISOU 1147 O ASP A 170 22547 14040 30321 1176 -808 -940 O ATOM 1148 CB ASP A 170 16.798 -1.463 30.317 1.00180.50 C ANISOU 1148 CB ASP A 170 22274 15176 31130 794 -283 -998 C ATOM 1149 CG ASP A 170 17.828 -2.336 31.010 1.00186.63 C ANISOU 1149 CG ASP A 170 23221 15970 31721 890 -291 -1247 C ATOM 1150 OD1 ASP A 170 18.997 -2.344 30.570 1.00188.00 O ANISOU 1150 OD1 ASP A 170 23782 16115 31536 1313 -32 -1653 O ATOM 1151 OD2 ASP A 170 17.467 -3.018 31.992 1.00190.16 O ANISOU 1151 OD2 ASP A 170 23416 16458 32378 544 -558 -1036 O ATOM 1152 N VAL A 171 15.879 1.175 28.559 1.00166.69 N ANISOU 1152 N VAL A 171 20267 13587 29479 1058 465 -916 N ATOM 1153 CA VAL A 171 14.778 1.777 27.813 1.00169.54 C ANISOU 1153 CA VAL A 171 20562 13847 30008 947 292 -646 C ATOM 1154 C VAL A 171 15.262 2.766 26.754 1.00168.00 C ANISOU 1154 C VAL A 171 20594 13663 29575 1362 742 -907 C ATOM 1155 O VAL A 171 14.510 3.140 25.854 1.00167.60 O ANISOU 1155 O VAL A 171 20680 13441 29561 1369 521 -754 O ATOM 1156 CB VAL A 171 13.778 2.487 28.750 1.00171.32 C ANISOU 1156 CB VAL A 171 19991 14405 30699 515 553 -276 C ATOM 1157 CG1 VAL A 171 13.182 1.496 29.737 1.00175.84 C ANISOU 1157 CG1 VAL A 171 20348 14941 31521 82 57 17 C ATOM 1158 CG2 VAL A 171 14.456 3.635 29.481 1.00168.19 C ANISOU 1158 CG2 VAL A 171 19048 14493 30365 615 1512 -459 C ATOM 1159 N VAL A 172 16.518 3.187 26.866 1.00165.05 N ANISOU 1159 N VAL A 172 20260 13494 28958 1705 1372 -1302 N ATOM 1160 CA VAL A 172 17.096 4.128 25.913 1.00157.49 C ANISOU 1160 CA VAL A 172 19517 12567 27755 2116 1850 -1580 C ATOM 1161 C VAL A 172 18.216 3.478 25.105 1.00161.48 C ANISOU 1161 C VAL A 172 20760 12801 27795 2558 1692 -1979 C ATOM 1162 O VAL A 172 19.206 3.014 25.671 1.00164.81 O ANISOU 1162 O VAL A 172 21250 13314 28057 2684 1868 -2233 O ATOM 1163 CB VAL A 172 17.643 5.386 26.616 1.00140.86 C ANISOU 1163 CB VAL A 172 16815 10955 25749 2181 2821 -1726 C ATOM 1164 CG1 VAL A 172 18.249 6.339 25.598 1.00137.63 C ANISOU 1164 CG1 VAL A 172 16653 10564 25077 2610 3303 -2017 C ATOM 1165 CG2 VAL A 172 16.541 6.074 27.407 1.00130.98 C ANISOU 1165 CG2 VAL A 172 14828 9982 24956 1755 3002 -1337 C ATOM 1166 N PRO A 173 18.057 3.445 23.774 1.00161.27 N ANISOU 1166 N PRO A 173 21288 12439 27548 2798 1356 -2033 N ATOM 1167 CA PRO A 173 19.033 2.845 22.857 1.00163.97 C ANISOU 1167 CA PRO A 173 22375 12488 27437 3231 1160 -2396 C ATOM 1168 C PRO A 173 20.419 3.465 23.000 1.00166.68 C ANISOU 1168 C PRO A 173 22694 13106 27532 3607 1948 -2832 C ATOM 1169 O PRO A 173 20.533 4.645 23.331 1.00164.34 O ANISOU 1169 O PRO A 173 21907 13170 27363 3623 2671 -2868 O ATOM 1170 CB PRO A 173 18.458 3.170 21.476 1.00160.82 C ANISOU 1170 CB PRO A 173 22377 11797 26931 3389 873 -2333 C ATOM 1171 CG PRO A 173 17.004 3.345 21.706 1.00159.77 C ANISOU 1171 CG PRO A 173 21844 11662 27199 2952 555 -1866 C ATOM 1172 CD PRO A 173 16.883 3.972 23.060 1.00158.32 C ANISOU 1172 CD PRO A 173 20859 11941 27353 2660 1123 -1736 C ATOM 1173 N MET A 174 21.456 2.673 22.748 1.00171.51 N ANISOU 1173 N MET A 174 23830 13547 27791 3908 1804 -3159 N ATOM 1174 CA MET A 174 22.831 3.156 22.832 1.00173.64 C ANISOU 1174 CA MET A 174 24134 14048 27793 4286 2505 -3593 C ATOM 1175 C MET A 174 23.305 3.738 21.505 1.00178.72 C ANISOU 1175 C MET A 174 25245 14548 28114 4725 2701 -3855 C ATOM 1176 O MET A 174 24.103 4.675 21.479 1.00181.47 O ANISOU 1176 O MET A 174 25440 15167 28346 4985 3442 -4126 O ATOM 1177 CB MET A 174 23.769 2.036 23.282 1.00177.13 C ANISOU 1177 CB MET A 174 24883 14404 28016 4398 2294 -3830 C ATOM 1178 CG MET A 174 23.577 1.611 24.728 1.00178.80 C ANISOU 1178 CG MET A 174 24578 14841 28516 4018 2293 -3649 C ATOM 1179 SD MET A 174 23.894 2.954 25.888 1.00214.11 S ANISOU 1179 SD MET A 174 28183 19923 33246 3915 3326 -3689 S ATOM 1180 CE MET A 174 25.594 3.358 25.491 1.00112.81 C ANISOU 1180 CE MET A 174 15663 7221 19980 4480 3988 -4264 C ATOM 1181 N ASN A 175 22.815 3.174 20.405 1.00182.62 N ANISOU 1181 N ASN A 175 26313 14614 28462 4806 2033 -3775 N ATOM 1182 CA ASN A 175 23.141 3.683 19.078 1.00185.86 C ANISOU 1182 CA ASN A 175 27194 14852 28574 5203 2146 -3989 C ATOM 1183 C ASN A 175 22.689 5.130 18.916 1.00187.72 C ANISOU 1183 C ASN A 175 26982 15348 28995 5177 2736 -3889 C ATOM 1184 O ASN A 175 23.288 5.903 18.166 1.00187.02 O ANISOU 1184 O ASN A 175 27079 15303 28678 5532 3189 -4148 O ATOM 1185 CB ASN A 175 22.524 2.801 17.989 1.00187.70 C ANISOU 1185 CB ASN A 175 28078 14573 28665 5237 1269 -3863 C ATOM 1186 CG ASN A 175 21.018 2.669 18.123 1.00189.59 C ANISOU 1186 CG ASN A 175 28058 14702 29274 4792 746 -3381 C ATOM 1187 OD1 ASN A 175 20.433 3.072 19.128 1.00189.12 O ANISOU 1187 OD1 ASN A 175 27339 14935 29583 4431 974 -3129 O ATOM 1188 ND2 ASN A 175 20.382 2.098 17.106 1.00191.34 N ANISOU 1188 ND2 ASN A 175 28801 14501 29400 4817 38 -3251 N ATOM 1189 N TYR A 176 21.627 5.489 19.628 1.00155.63 N ANISOU 1189 N TYR A 176 22277 16567 20289 -2729 4507 -1184 N ATOM 1190 CA TYR A 176 21.142 6.860 19.646 1.00151.73 C ANISOU 1190 CA TYR A 176 21607 15953 20090 -2729 4233 -1220 C ATOM 1191 C TYR A 176 22.061 7.733 20.493 1.00145.73 C ANISOU 1191 C TYR A 176 20756 15052 19562 -2678 4037 -1173 C ATOM 1192 O TYR A 176 22.534 8.774 20.042 1.00148.75 O ANISOU 1192 O TYR A 176 20983 15346 20190 -2681 3832 -987 O ATOM 1193 CB TYR A 176 19.715 6.916 20.195 1.00156.37 C ANISOU 1193 CB TYR A 176 22210 16530 20675 -2735 4227 -1544 C ATOM 1194 CG TYR A 176 19.244 8.312 20.526 1.00164.14 C ANISOU 1194 CG TYR A 176 23028 17375 21962 -2721 3945 -1625 C ATOM 1195 CD1 TYR A 176 18.545 9.070 19.597 1.00166.48 C ANISOU 1195 CD1 TYR A 176 23197 17663 22394 -2757 3808 -1569 C ATOM 1196 CD2 TYR A 176 19.506 8.877 21.769 1.00165.83 C ANISOU 1196 CD2 TYR A 176 23213 17468 22326 -2665 3812 -1760 C ATOM 1197 CE1 TYR A 176 18.116 10.349 19.897 1.00165.82 C ANISOU 1197 CE1 TYR A 176 22964 17449 22590 -2743 3554 -1640 C ATOM 1198 CE2 TYR A 176 19.083 10.155 22.076 1.00165.55 C ANISOU 1198 CE2 TYR A 176 23026 17302 22573 -2651 3552 -1839 C ATOM 1199 CZ TYR A 176 18.389 10.886 21.138 1.00165.49 C ANISOU 1199 CZ TYR A 176 22896 17284 22700 -2693 3427 -1776 C ATOM 1200 OH TYR A 176 17.968 12.159 21.444 1.00167.24 O ANISOU 1200 OH TYR A 176 22968 17372 23203 -2678 3172 -1851 O ATOM 1201 N MET A 177 22.311 7.296 21.722 1.00138.65 N ANISOU 1201 N MET A 177 19958 14134 18588 -2625 4104 -1345 N ATOM 1202 CA MET A 177 23.129 8.053 22.662 1.00136.21 C ANISOU 1202 CA MET A 177 19573 13697 18482 -2565 3922 -1348 C ATOM 1203 C MET A 177 24.526 8.328 22.114 1.00131.23 C ANISOU 1203 C MET A 177 18868 13040 17954 -2566 3858 -1028 C ATOM 1204 O MET A 177 25.187 9.281 22.528 1.00129.20 O ANISOU 1204 O MET A 177 18483 12655 17952 -2534 3645 -971 O ATOM 1205 CB MET A 177 23.230 7.310 23.996 1.00141.52 C ANISOU 1205 CB MET A 177 20394 14385 18992 -2494 4051 -1571 C ATOM 1206 CG MET A 177 21.895 7.101 24.691 1.00145.61 C ANISOU 1206 CG MET A 177 20980 14911 19435 -2480 4109 -1895 C ATOM 1207 SD MET A 177 21.128 8.654 25.185 1.00130.39 S ANISOU 1207 SD MET A 177 18871 12824 17846 -2463 3784 -2061 S ATOM 1208 CE MET A 177 22.407 9.330 26.241 1.00114.53 C ANISOU 1208 CE MET A 177 16798 10693 16026 -2373 3595 -2030 C ATOM 1209 N VAL A 178 24.969 7.492 21.181 1.00130.07 N ANISOU 1209 N VAL A 178 18798 13011 17610 -2600 4044 -821 N ATOM 1210 CA VAL A 178 26.319 7.595 20.639 1.00133.01 C ANISOU 1210 CA VAL A 178 19119 13374 18045 -2598 4023 -507 C ATOM 1211 C VAL A 178 26.364 8.349 19.312 1.00136.87 C ANISOU 1211 C VAL A 178 19462 13844 18700 -2644 3907 -246 C ATOM 1212 O VAL A 178 26.929 9.439 19.231 1.00142.20 O ANISOU 1212 O VAL A 178 19972 14393 19665 -2636 3694 -104 O ATOM 1213 CB VAL A 178 26.959 6.203 20.460 1.00134.31 C ANISOU 1213 CB VAL A 178 19461 13679 17891 -2594 4302 -412 C ATOM 1214 CG1 VAL A 178 28.286 6.322 19.734 1.00134.27 C ANISOU 1214 CG1 VAL A 178 19395 13673 17949 -2597 4285 -67 C ATOM 1215 CG2 VAL A 178 27.142 5.525 21.811 1.00134.00 C ANISOU 1215 CG2 VAL A 178 19558 13648 17709 -2530 4409 -631 C ATOM 1216 N TYR A 179 25.767 7.767 18.277 1.00140.93 N ANISOU 1216 N TYR A 179 20035 14481 19031 -2686 4051 -185 N ATOM 1217 CA TYR A 179 25.795 8.363 16.944 1.00153.48 C ANISOU 1217 CA TYR A 179 21505 16075 20734 -2715 3969 73 C ATOM 1218 C TYR A 179 24.983 9.654 16.862 1.00159.54 C ANISOU 1218 C TYR A 179 22107 16730 21782 -2723 3727 0 C ATOM 1219 O TYR A 179 25.542 10.740 16.699 1.00163.70 O ANISOU 1219 O TYR A 179 22471 17131 22594 -2713 3529 167 O ATOM 1220 CB TYR A 179 25.299 7.362 15.898 1.00158.37 C ANISOU 1220 CB TYR A 179 22240 16868 21068 -2747 4185 127 C ATOM 1221 CG TYR A 179 26.191 6.151 15.747 1.00164.11 C ANISOU 1221 CG TYR A 179 23115 17706 21531 -2741 4420 257 C ATOM 1222 CD1 TYR A 179 27.221 6.135 14.816 1.00166.65 C ANISOU 1222 CD1 TYR A 179 23404 18059 21855 -2736 4446 596 C ATOM 1223 CD2 TYR A 179 26.007 5.025 16.538 1.00167.45 C ANISOU 1223 CD2 TYR A 179 23714 18202 21706 -2735 4622 47 C ATOM 1224 CE1 TYR A 179 28.041 5.032 14.674 1.00168.16 C ANISOU 1224 CE1 TYR A 179 23733 18355 21806 -2728 4661 718 C ATOM 1225 CE2 TYR A 179 26.821 3.916 16.405 1.00168.14 C ANISOU 1225 CE2 TYR A 179 23941 18391 21554 -2726 4841 167 C ATOM 1226 CZ TYR A 179 27.837 3.925 15.471 1.00168.19 C ANISOU 1226 CZ TYR A 179 23912 18430 21565 -2725 4856 500 C ATOM 1227 OH TYR A 179 28.650 2.824 15.335 1.00167.33 O ANISOU 1227 OH TYR A 179 23941 18421 21214 -2715 5073 621 O ATOM 1228 N PHE A 180 23.665 9.526 16.974 1.00155.14 N ANISOU 1228 N PHE A 180 21588 16213 21147 -2740 3749 -249 N ATOM 1229 CA PHE A 180 22.762 10.665 16.849 1.00148.45 C ANISOU 1229 CA PHE A 180 20596 15275 20534 -2747 3537 -335 C ATOM 1230 C PHE A 180 23.030 11.728 17.909 1.00143.98 C ANISOU 1230 C PHE A 180 19914 14530 20263 -2717 3309 -432 C ATOM 1231 O PHE A 180 23.331 12.878 17.586 1.00144.12 O ANISOU 1231 O PHE A 180 19762 14429 20568 -2713 3104 -279 O ATOM 1232 CB PHE A 180 21.307 10.198 16.933 1.00145.14 C ANISOU 1232 CB PHE A 180 20254 14936 19955 -2769 3623 -619 C ATOM 1233 CG PHE A 180 20.302 11.296 16.719 1.00147.27 C ANISOU 1233 CG PHE A 180 20383 15132 20440 -2776 3420 -709 C ATOM 1234 CD1 PHE A 180 19.852 11.601 15.445 1.00148.08 C ANISOU 1234 CD1 PHE A 180 20414 15292 20556 -2792 3389 -559 C ATOM 1235 CD2 PHE A 180 19.803 12.017 17.790 1.00149.05 C ANISOU 1235 CD2 PHE A 180 20551 15234 20847 -2757 3262 -944 C ATOM 1236 CE1 PHE A 180 18.924 12.608 15.245 1.00147.77 C ANISOU 1236 CE1 PHE A 180 20249 15188 20711 -2792 3205 -640 C ATOM 1237 CE2 PHE A 180 18.875 13.025 17.597 1.00149.76 C ANISOU 1237 CE2 PHE A 180 20513 15255 21133 -2762 3078 -1026 C ATOM 1238 CZ PHE A 180 18.435 13.321 16.323 1.00148.34 C ANISOU 1238 CZ PHE A 180 20262 15133 20967 -2780 3050 -873 C ATOM 1239 N ASN A 181 22.921 11.337 19.174 1.00136.41 N ANISOU 1239 N ASN A 181 19046 13551 19234 -2690 3349 -687 N ATOM 1240 CA ASN A 181 23.056 12.275 20.283 1.00128.64 C ANISOU 1240 CA ASN A 181 17965 12407 18504 -2650 3136 -828 C ATOM 1241 C ASN A 181 24.461 12.858 20.423 1.00128.70 C ANISOU 1241 C ASN A 181 17871 12308 18723 -2625 3009 -611 C ATOM 1242 O ASN A 181 24.680 14.035 20.147 1.00137.58 O ANISOU 1242 O ASN A 181 18819 13303 20154 -2629 2793 -489 O ATOM 1243 CB ASN A 181 22.620 11.620 21.597 1.00125.29 C ANISOU 1243 CB ASN A 181 17679 12003 17922 -2611 3230 -1150 C ATOM 1244 CG ASN A 181 22.544 12.608 22.746 1.00122.34 C ANISOU 1244 CG ASN A 181 17210 11474 17799 -2560 3002 -1337 C ATOM 1245 OD1 ASN A 181 22.993 13.748 22.631 1.00121.60 O ANISOU 1245 OD1 ASN A 181 16948 11249 18007 -2557 2775 -1218 O ATOM 1246 ND2 ASN A 181 21.971 12.174 23.862 1.00123.46 N ANISOU 1246 ND2 ASN A 181 17459 11628 17820 -2516 3066 -1632 N ATOM 1247 N PHE A 182 25.407 12.030 20.852 1.00126.28 N ANISOU 1247 N PHE A 182 17671 12051 18258 -2600 3147 -564 N ATOM 1248 CA PHE A 182 26.758 12.500 21.141 1.00127.75 C ANISOU 1248 CA PHE A 182 17767 12138 18635 -2571 3034 -393 C ATOM 1249 C PHE A 182 27.450 13.136 19.933 1.00134.15 C ANISOU 1249 C PHE A 182 18434 12906 19632 -2604 2956 -38 C ATOM 1250 O PHE A 182 27.628 14.350 19.885 1.00141.46 O ANISOU 1250 O PHE A 182 19179 13681 20889 -2604 2729 35 O ATOM 1251 CB PHE A 182 27.612 11.370 21.727 1.00129.42 C ANISOU 1251 CB PHE A 182 18136 12435 18602 -2534 3224 -400 C ATOM 1252 CG PHE A 182 29.037 11.764 21.999 1.00129.41 C ANISOU 1252 CG PHE A 182 18045 12344 18780 -2503 3121 -224 C ATOM 1253 CD1 PHE A 182 29.327 12.879 22.768 1.00133.00 C ANISOU 1253 CD1 PHE A 182 18350 12631 19554 -2468 2865 -305 C ATOM 1254 CD2 PHE A 182 30.085 11.014 21.495 1.00126.59 C ANISOU 1254 CD2 PHE A 182 17752 12070 18277 -2507 3278 16 C ATOM 1255 CE1 PHE A 182 30.637 13.243 23.021 1.00134.62 C ANISOU 1255 CE1 PHE A 182 18462 12750 19939 -2440 2765 -154 C ATOM 1256 CE2 PHE A 182 31.397 11.372 21.745 1.00126.01 C ANISOU 1256 CE2 PHE A 182 17589 11913 18375 -2479 3184 176 C ATOM 1257 CZ PHE A 182 31.673 12.488 22.510 1.00131.21 C ANISOU 1257 CZ PHE A 182 18091 12402 19361 -2446 2926 87 C ATOM 1258 N PHE A 183 27.832 12.323 18.957 1.00137.25 N ANISOU 1258 N PHE A 183 18907 13427 19815 -2629 3148 184 N ATOM 1259 CA PHE A 183 28.593 12.825 17.818 1.00146.41 C ANISOU 1259 CA PHE A 183 19946 14557 21128 -2648 3101 542 C ATOM 1260 C PHE A 183 27.915 13.979 17.085 1.00150.52 C ANISOU 1260 C PHE A 183 20302 14993 21897 -2667 2923 614 C ATOM 1261 O PHE A 183 28.519 15.033 16.873 1.00151.64 O ANISOU 1261 O PHE A 183 20268 14992 22355 -2663 2745 794 O ATOM 1262 CB PHE A 183 28.898 11.693 16.842 1.00151.96 C ANISOU 1262 CB PHE A 183 20779 15432 21526 -2665 3350 739 C ATOM 1263 CG PHE A 183 29.898 10.709 17.362 1.00156.69 C ANISOU 1263 CG PHE A 183 21506 16095 21934 -2642 3511 770 C ATOM 1264 CD1 PHE A 183 31.236 11.051 17.448 1.00160.43 C ANISOU 1264 CD1 PHE A 183 21892 16486 22577 -2623 3443 983 C ATOM 1265 CD2 PHE A 183 29.505 9.445 17.766 1.00154.28 C ANISOU 1265 CD2 PHE A 183 21404 15929 21287 -2638 3733 586 C ATOM 1266 CE1 PHE A 183 32.165 10.152 17.927 1.00160.18 C ANISOU 1266 CE1 PHE A 183 21976 16518 22368 -2597 3587 1012 C ATOM 1267 CE2 PHE A 183 30.429 8.540 18.245 1.00152.59 C ANISOU 1267 CE2 PHE A 183 21310 15775 20894 -2611 3885 619 C ATOM 1268 CZ PHE A 183 31.762 8.893 18.326 1.00156.10 C ANISOU 1268 CZ PHE A 183 21668 16144 21500 -2588 3809 831 C ATOM 1269 N ALA A 184 26.660 13.778 16.700 1.00151.04 N ANISOU 1269 N ALA A 184 20421 15142 21824 -2687 2974 474 N ATOM 1270 CA ALA A 184 25.961 14.751 15.869 1.00151.36 C ANISOU 1270 CA ALA A 184 20324 15132 22054 -2699 2833 556 C ATOM 1271 C ALA A 184 25.436 15.954 16.650 1.00148.17 C ANISOU 1271 C ALA A 184 19782 14558 21957 -2689 2585 367 C ATOM 1272 O ALA A 184 25.587 17.094 16.213 1.00145.94 O ANISOU 1272 O ALA A 184 19326 14149 21975 -2687 2406 524 O ATOM 1273 CB ALA A 184 24.826 14.073 15.106 1.00150.02 C ANISOU 1273 CB ALA A 184 20258 15126 21619 -2719 2978 479 C ATOM 1274 N CYS A 185 24.829 15.704 17.805 1.00145.80 N ANISOU 1274 N CYS A 185 19560 14251 21586 -2679 2578 36 N ATOM 1275 CA CYS A 185 24.156 16.766 18.547 1.00143.26 C ANISOU 1275 CA CYS A 185 19126 13786 21519 -2665 2355 -177 C ATOM 1276 C CYS A 185 25.004 17.366 19.670 1.00142.43 C ANISOU 1276 C CYS A 185 18942 13524 21651 -2630 2193 -241 C ATOM 1277 O CYS A 185 24.552 18.263 20.381 1.00151.55 O ANISOU 1277 O CYS A 185 20003 14550 23030 -2612 1997 -423 O ATOM 1278 CB CYS A 185 22.821 16.262 19.104 1.00142.95 C ANISOU 1278 CB CYS A 185 19204 13826 21284 -2667 2426 -515 C ATOM 1279 SG CYS A 185 21.680 15.634 17.848 1.00114.36 S ANISOU 1279 SG CYS A 185 15658 10382 17412 -2706 2589 -491 S ATOM 1280 N VAL A 186 26.230 16.877 19.826 1.00135.36 N ANISOU 1280 N VAL A 186 18083 12641 20706 -2617 2270 -96 N ATOM 1281 CA VAL A 186 27.107 17.375 20.880 1.00136.37 C ANISOU 1281 CA VAL A 186 18137 12630 21046 -2578 2121 -158 C ATOM 1282 C VAL A 186 28.530 17.630 20.388 1.00131.80 C ANISOU 1282 C VAL A 186 17457 11989 20632 -2582 2093 165 C ATOM 1283 O VAL A 186 29.031 18.751 20.474 1.00124.77 O ANISOU 1283 O VAL A 186 16381 10926 20099 -2577 1882 253 O ATOM 1284 CB VAL A 186 27.147 16.415 22.086 1.00142.69 C ANISOU 1284 CB VAL A 186 19110 13506 21601 -2532 2239 -418 C ATOM 1285 CG1 VAL A 186 28.181 16.880 23.100 1.00146.34 C ANISOU 1285 CG1 VAL A 186 19496 13840 22268 -2480 2088 -460 C ATOM 1286 CG2 VAL A 186 25.771 16.309 22.728 1.00141.45 C ANISOU 1286 CG2 VAL A 186 19031 13379 21333 -2520 2242 -753 C ATOM 1287 N LEU A 187 29.176 16.589 19.874 1.00136.31 N ANISOU 1287 N LEU A 187 18145 12694 20951 -2590 2308 341 N ATOM 1288 CA LEU A 187 30.552 16.700 19.403 1.00140.43 C ANISOU 1288 CA LEU A 187 18586 13173 21599 -2592 2310 653 C ATOM 1289 C LEU A 187 30.673 17.706 18.261 1.00140.62 C ANISOU 1289 C LEU A 187 18428 13102 21898 -2620 2198 942 C ATOM 1290 O LEU A 187 31.539 18.580 18.284 1.00136.56 O ANISOU 1290 O LEU A 187 17744 12432 21709 -2616 2043 1098 O ATOM 1291 CB LEU A 187 31.088 15.336 18.965 1.00139.91 C ANISOU 1291 CB LEU A 187 18694 13286 21178 -2596 2580 788 C ATOM 1292 CG LEU A 187 32.575 15.291 18.605 1.00141.28 C ANISOU 1292 CG LEU A 187 18807 13429 21444 -2591 2606 1092 C ATOM 1293 CD1 LEU A 187 33.428 15.665 19.808 1.00136.76 C ANISOU 1293 CD1 LEU A 187 18167 12733 21065 -2550 2462 978 C ATOM 1294 CD2 LEU A 187 32.962 13.921 18.076 1.00143.33 C ANISOU 1294 CD2 LEU A 187 19248 13878 21331 -2595 2883 1223 C ATOM 1295 N VAL A 188 29.802 17.578 17.264 1.00142.66 N ANISOU 1295 N VAL A 188 18720 13455 22028 -2644 2279 1011 N ATOM 1296 CA VAL A 188 29.801 18.497 16.128 1.00143.31 C ANISOU 1296 CA VAL A 188 18644 13465 22343 -2657 2189 1284 C ATOM 1297 C VAL A 188 29.635 19.951 16.569 1.00139.71 C ANISOU 1297 C VAL A 188 17986 12793 22304 -2652 1915 1217 C ATOM 1298 O VAL A 188 30.435 20.807 16.190 1.00136.00 O ANISOU 1298 O VAL A 188 17346 12182 22146 -2652 1802 1458 O ATOM 1299 CB VAL A 188 28.717 18.135 15.089 1.00145.21 C ANISOU 1299 CB VAL A 188 18960 13851 22361 -2670 2305 1311 C ATOM 1300 CG1 VAL A 188 28.542 19.269 14.087 1.00147.20 C ANISOU 1300 CG1 VAL A 188 19036 14008 22886 -2667 2174 1541 C ATOM 1301 CG2 VAL A 188 29.069 16.833 14.383 1.00143.74 C ANISOU 1301 CG2 VAL A 188 18939 13861 21814 -2674 2566 1461 C ATOM 1302 N PRO A 189 28.595 20.237 17.371 1.00139.05 N ANISOU 1302 N PRO A 189 17919 12678 22236 -2648 1812 891 N ATOM 1303 CA PRO A 189 28.415 21.601 17.878 1.00135.60 C ANISOU 1303 CA PRO A 189 17297 12035 22192 -2640 1548 801 C ATOM 1304 C PRO A 189 29.653 22.105 18.614 1.00124.97 C ANISOU 1304 C PRO A 189 15834 10528 21123 -2624 1414 846 C ATOM 1305 O PRO A 189 30.098 23.222 18.361 1.00115.47 O ANISOU 1305 O PRO A 189 14434 9150 20291 -2628 1245 1005 O ATOM 1306 CB PRO A 189 27.243 21.457 18.851 1.00136.47 C ANISOU 1306 CB PRO A 189 17498 12174 22181 -2628 1508 406 C ATOM 1307 CG PRO A 189 26.472 20.298 18.332 1.00134.07 C ANISOU 1307 CG PRO A 189 17382 12086 21473 -2642 1740 358 C ATOM 1308 CD PRO A 189 27.496 19.347 17.788 1.00135.19 C ANISOU 1308 CD PRO A 189 17612 12339 21414 -2648 1937 599 C ATOM 1309 N LEU A 190 30.201 21.287 19.508 1.00125.97 N ANISOU 1309 N LEU A 190 16076 10713 21073 -2602 1492 706 N ATOM 1310 CA LEU A 190 31.388 21.671 20.266 1.00125.49 C ANISOU 1310 CA LEU A 190 15914 10517 21249 -2579 1369 723 C ATOM 1311 C LEU A 190 32.597 21.887 19.361 1.00131.98 C ANISOU 1311 C LEU A 190 16621 11286 22239 -2598 1396 1112 C ATOM 1312 O LEU A 190 33.537 22.592 19.728 1.00138.30 O ANISOU 1312 O LEU A 190 17265 11924 23359 -2590 1246 1183 O ATOM 1313 CB LEU A 190 31.710 20.626 21.338 1.00122.53 C ANISOU 1313 CB LEU A 190 15709 10244 20603 -2539 1475 506 C ATOM 1314 CG LEU A 190 30.748 20.554 22.526 1.00122.75 C ANISOU 1314 CG LEU A 190 15824 10282 20534 -2500 1412 103 C ATOM 1315 CD1 LEU A 190 31.081 19.367 23.414 1.00128.78 C ANISOU 1315 CD1 LEU A 190 16778 11174 20979 -2453 1568 -66 C ATOM 1316 CD2 LEU A 190 30.779 21.848 23.323 1.00110.29 C ANISOU 1316 CD2 LEU A 190 14063 8492 19351 -2474 1121 -46 C ATOM 1317 N LEU A 191 32.573 21.277 18.181 1.00133.48 N ANISOU 1317 N LEU A 191 16886 11613 22218 -2620 1589 1359 N ATOM 1318 CA LEU A 191 33.637 21.474 17.204 1.00138.28 C ANISOU 1318 CA LEU A 191 17391 12180 22970 -2632 1633 1750 C ATOM 1319 C LEU A 191 33.419 22.772 16.434 1.00143.63 C ANISOU 1319 C LEU A 191 17864 12701 24009 -2645 1480 1938 C ATOM 1320 O LEU A 191 34.374 23.467 16.085 1.00143.93 O ANISOU 1320 O LEU A 191 17733 12596 24359 -2648 1403 2190 O ATOM 1321 CB LEU A 191 33.723 20.287 16.244 1.00137.20 C ANISOU 1321 CB LEU A 191 17420 12256 22454 -2639 1902 1944 C ATOM 1322 CG LEU A 191 34.244 18.983 16.849 1.00136.92 C ANISOU 1322 CG LEU A 191 17572 12365 22086 -2626 2078 1845 C ATOM 1323 CD1 LEU A 191 34.180 17.855 15.831 1.00140.75 C ANISOU 1323 CD1 LEU A 191 18220 13059 22200 -2634 2340 2024 C ATOM 1324 CD2 LEU A 191 35.662 19.160 17.373 1.00131.03 C ANISOU 1324 CD2 LEU A 191 16732 11511 21542 -2611 2013 1950 C ATOM 1325 N LEU A 192 32.155 23.092 16.174 1.00144.31 N ANISOU 1325 N LEU A 192 17964 12812 24055 -2649 1441 1814 N ATOM 1326 CA LEU A 192 31.804 24.359 15.545 1.00142.63 C ANISOU 1326 CA LEU A 192 17564 12450 24179 -2652 1286 1952 C ATOM 1327 C LEU A 192 32.114 25.507 16.495 1.00141.17 C ANISOU 1327 C LEU A 192 17196 12026 24415 -2650 1030 1818 C ATOM 1328 O LEU A 192 32.748 26.488 16.110 1.00144.73 O ANISOU 1328 O LEU A 192 17450 12300 25239 -2654 915 2041 O ATOM 1329 CB LEU A 192 30.322 24.383 15.164 1.00142.94 C ANISOU 1329 CB LEU A 192 17671 12581 24057 -2652 1299 1809 C ATOM 1330 CG LEU A 192 29.874 23.425 14.058 1.00142.13 C ANISOU 1330 CG LEU A 192 17721 12702 23580 -2650 1527 1949 C ATOM 1331 CD1 LEU A 192 28.367 23.500 13.865 1.00139.78 C ANISOU 1331 CD1 LEU A 192 17479 12484 23149 -2648 1512 1750 C ATOM 1332 CD2 LEU A 192 30.600 23.731 12.757 1.00141.66 C ANISOU 1332 CD2 LEU A 192 17564 12623 23636 -2637 1587 2376 C ATOM 1333 N MET A 193 31.665 25.373 17.739 1.00135.98 N ANISOU 1333 N MET A 193 16604 11363 23699 -2639 945 1451 N ATOM 1334 CA MET A 193 31.916 26.378 18.763 1.00133.10 C ANISOU 1334 CA MET A 193 16083 10787 23702 -2627 697 1276 C ATOM 1335 C MET A 193 33.407 26.656 18.898 1.00140.26 C ANISOU 1335 C MET A 193 16857 11564 24872 -2628 643 1467 C ATOM 1336 O MET A 193 33.844 27.802 18.799 1.00146.92 O ANISOU 1336 O MET A 193 17485 12198 26140 -2636 470 1585 O ATOM 1337 CB MET A 193 31.346 25.927 20.108 1.00127.92 C ANISOU 1337 CB MET A 193 15556 10184 22865 -2599 657 861 C ATOM 1338 CG MET A 193 29.847 25.687 20.098 1.00130.81 C ANISOU 1338 CG MET A 193 16043 10663 22997 -2599 700 642 C ATOM 1339 SD MET A 193 29.218 25.221 21.721 1.00176.58 S ANISOU 1339 SD MET A 193 21980 16504 28609 -2554 654 166 S ATOM 1340 CE MET A 193 29.772 26.616 22.692 1.00189.18 C ANISOU 1340 CE MET A 193 23350 17828 30704 -2527 334 48 C ATOM 1341 N LEU A 194 34.184 25.603 19.124 1.00140.16 N ANISOU 1341 N LEU A 194 16968 11673 24612 -2619 795 1496 N ATOM 1342 CA LEU A 194 35.631 25.736 19.236 1.00144.63 C ANISOU 1342 CA LEU A 194 17421 12139 25393 -2618 764 1679 C ATOM 1343 C LEU A 194 36.203 26.403 17.990 1.00144.03 C ANISOU 1343 C LEU A 194 17179 11963 25584 -2644 776 2087 C ATOM 1344 O LEU A 194 37.070 27.271 18.083 1.00139.82 O ANISOU 1344 O LEU A 194 16442 11231 25452 -2650 633 2211 O ATOM 1345 CB LEU A 194 36.284 24.370 19.449 1.00145.01 C ANISOU 1345 CB LEU A 194 17653 12370 25073 -2602 969 1687 C ATOM 1346 CG LEU A 194 37.804 24.384 19.622 1.00149.04 C ANISOU 1346 CG LEU A 194 18063 12798 25770 -2597 950 1860 C ATOM 1347 CD1 LEU A 194 38.206 25.341 20.736 1.00156.06 C ANISOU 1347 CD1 LEU A 194 18779 13477 27040 -2576 684 1655 C ATOM 1348 CD2 LEU A 194 38.334 22.984 19.892 1.00145.61 C ANISOU 1348 CD2 LEU A 194 17830 12558 24937 -2575 1158 1838 C ATOM 1349 N GLY A 195 35.708 25.994 16.826 1.00143.77 N ANISOU 1349 N GLY A 195 17231 12066 25328 -2654 948 2293 N ATOM 1350 CA GLY A 195 36.139 26.570 15.566 1.00141.02 C ANISOU 1350 CA GLY A 195 16746 11644 25189 -2663 982 2690 C ATOM 1351 C GLY A 195 35.807 28.046 15.474 1.00134.81 C ANISOU 1351 C GLY A 195 15740 10631 24851 -2668 765 2713 C ATOM 1352 O GLY A 195 36.544 28.822 14.867 1.00134.60 O ANISOU 1352 O GLY A 195 15528 10447 25165 -2673 720 3006 O ATOM 1353 N VAL A 196 34.687 28.432 16.077 1.00132.66 N ANISOU 1353 N VAL A 196 15487 10337 24582 -2665 638 2407 N ATOM 1354 CA VAL A 196 34.279 29.830 16.114 1.00135.06 C ANISOU 1354 CA VAL A 196 15591 10424 25302 -2668 422 2385 C ATOM 1355 C VAL A 196 35.268 30.654 16.929 1.00139.51 C ANISOU 1355 C VAL A 196 15958 10751 26300 -2674 224 2346 C ATOM 1356 O VAL A 196 35.810 31.645 16.442 1.00138.81 O ANISOU 1356 O VAL A 196 15660 10467 26614 -2684 135 2583 O ATOM 1357 CB VAL A 196 32.868 29.996 16.710 1.00131.73 C ANISOU 1357 CB VAL A 196 15244 10037 24769 -2660 326 2031 C ATOM 1358 CG1 VAL A 196 32.596 31.455 17.032 1.00133.60 C ANISOU 1358 CG1 VAL A 196 15269 10028 25467 -2660 74 1959 C ATOM 1359 CG2 VAL A 196 31.819 29.451 15.754 1.00131.36 C ANISOU 1359 CG2 VAL A 196 15341 10187 24382 -2654 489 2094 C ATOM 1360 N TYR A 197 35.502 30.236 18.169 1.00144.44 N ANISOU 1360 N TYR A 197 16648 11391 26842 -2664 160 2046 N ATOM 1361 CA TYR A 197 36.435 30.934 19.046 1.00154.41 C ANISOU 1361 CA TYR A 197 17735 12445 28490 -2662 -36 1965 C ATOM 1362 C TYR A 197 37.817 31.048 18.413 1.00157.11 C ANISOU 1362 C TYR A 197 17942 12700 29054 -2679 21 2326 C ATOM 1363 O TYR A 197 38.577 31.966 18.721 1.00155.42 O ANISOU 1363 O TYR A 197 17511 12259 29282 -2688 -148 2369 O ATOM 1364 CB TYR A 197 36.533 30.236 20.404 1.00161.93 C ANISOU 1364 CB TYR A 197 18815 13477 29235 -2630 -73 1607 C ATOM 1365 CG TYR A 197 35.264 30.302 21.223 1.00165.33 C ANISOU 1365 CG TYR A 197 19342 13947 29528 -2605 -168 1225 C ATOM 1366 CD1 TYR A 197 34.930 31.449 21.932 1.00165.60 C ANISOU 1366 CD1 TYR A 197 19221 13781 29919 -2594 -424 1018 C ATOM 1367 CD2 TYR A 197 34.402 29.216 21.292 1.00167.75 C ANISOU 1367 CD2 TYR A 197 19893 14489 29356 -2592 3 1071 C ATOM 1368 CE1 TYR A 197 33.771 31.512 22.683 1.00166.29 C ANISOU 1368 CE1 TYR A 197 19398 13906 29880 -2566 -508 673 C ATOM 1369 CE2 TYR A 197 33.242 29.270 22.040 1.00169.92 C ANISOU 1369 CE2 TYR A 197 20253 14797 29512 -2567 -75 727 C ATOM 1370 CZ TYR A 197 32.932 30.420 22.734 1.00169.79 C ANISOU 1370 CZ TYR A 197 20083 14584 29846 -2553 -330 532 C ATOM 1371 OH TYR A 197 31.776 30.477 23.480 1.00171.60 O ANISOU 1371 OH TYR A 197 20397 14848 29955 -2523 -405 194 O ATOM 1372 N LEU A 198 38.140 30.110 17.529 1.00160.36 N ANISOU 1372 N LEU A 198 18478 13287 29163 -2682 262 2582 N ATOM 1373 CA LEU A 198 39.416 30.139 16.824 1.00162.83 C ANISOU 1373 CA LEU A 198 18679 13537 29652 -2695 345 2952 C ATOM 1374 C LEU A 198 39.527 31.389 15.961 1.00166.55 C ANISOU 1374 C LEU A 198 18920 13799 30564 -2708 263 3237 C ATOM 1375 O LEU A 198 40.567 32.044 15.933 1.00168.10 O ANISOU 1375 O LEU A 198 18915 13803 31154 -2721 183 3412 O ATOM 1376 CB LEU A 198 39.586 28.890 15.957 1.00156.83 C ANISOU 1376 CB LEU A 198 18113 13021 28454 -2689 627 3172 C ATOM 1377 CG LEU A 198 39.790 27.561 16.687 1.00149.24 C ANISOU 1377 CG LEU A 198 17369 12260 27074 -2675 748 2970 C ATOM 1378 CD1 LEU A 198 39.835 26.413 15.691 1.00152.85 C ANISOU 1378 CD1 LEU A 198 18010 12950 27115 -2670 1027 3203 C ATOM 1379 CD2 LEU A 198 41.056 27.597 17.529 1.00142.46 C ANISOU 1379 CD2 LEU A 198 16413 11295 26422 -2670 659 2929 C ATOM 1380 N ARG A 199 38.446 31.713 15.259 1.00168.27 N ANISOU 1380 N ARG A 199 19166 14053 30717 -2702 285 3282 N ATOM 1381 CA ARG A 199 38.418 32.886 14.395 1.00174.89 C ANISOU 1381 CA ARG A 199 19802 14705 31942 -2703 222 3553 C ATOM 1382 C ARG A 199 38.264 34.164 15.217 1.00174.55 C ANISOU 1382 C ARG A 199 19557 14401 32363 -2715 -53 3348 C ATOM 1383 O ARG A 199 38.786 35.216 14.847 1.00172.27 O ANISOU 1383 O ARG A 199 19041 13885 32529 -2724 -144 3561 O ATOM 1384 CB ARG A 199 37.280 32.777 13.377 1.00179.04 C ANISOU 1384 CB ARG A 199 20434 15372 32221 -2680 337 3657 C ATOM 1385 CG ARG A 199 37.239 31.461 12.614 1.00181.33 C ANISOU 1385 CG ARG A 199 20945 15940 32012 -2663 600 3803 C ATOM 1386 CD ARG A 199 38.534 31.202 11.859 1.00189.49 C ANISOU 1386 CD ARG A 199 21920 16962 33115 -2658 744 4193 C ATOM 1387 NE ARG A 199 38.447 30.005 11.024 1.00196.56 N ANISOU 1387 NE ARG A 199 23022 18120 33541 -2635 995 4352 N ATOM 1388 CZ ARG A 199 38.749 28.777 11.438 1.00195.73 C ANISOU 1388 CZ ARG A 199 23100 18198 33070 -2643 1122 4236 C ATOM 1389 NH1 ARG A 199 39.160 28.574 12.682 1.00196.58 N ANISOU 1389 NH1 ARG A 199 23215 18262 33214 -2666 1023 3964 N ATOM 1390 NH2 ARG A 199 38.639 27.749 10.606 1.00190.33 N ANISOU 1390 NH2 ARG A 199 22594 17742 31980 -2621 1348 4391 N ATOM 1391 N ILE A 200 37.547 34.064 16.332 1.00173.32 N ANISOU 1391 N ILE A 200 19485 14277 32092 -2712 -181 2935 N ATOM 1392 CA ILE A 200 37.317 35.211 17.206 1.00171.66 C ANISOU 1392 CA ILE A 200 19103 13836 32283 -2716 -449 2696 C ATOM 1393 C ILE A 200 38.622 35.822 17.702 1.00181.80 C ANISOU 1393 C ILE A 200 20172 14893 34010 -2732 -584 2752 C ATOM 1394 O ILE A 200 38.920 36.982 17.421 1.00187.80 O ANISOU 1394 O ILE A 200 20700 15411 35243 -2747 -707 2903 O ATOM 1395 CB ILE A 200 36.452 34.837 18.427 1.00160.20 C ANISOU 1395 CB ILE A 200 17799 12479 30592 -2698 -547 2231 C ATOM 1396 CG1 ILE A 200 35.035 34.465 17.989 1.00152.93 C ANISOU 1396 CG1 ILE A 200 17052 11738 29317 -2686 -452 2146 C ATOM 1397 CG2 ILE A 200 36.407 35.986 19.420 1.00159.17 C ANISOU 1397 CG2 ILE A 200 17485 12104 30889 -2696 -832 1980 C ATOM 1398 CD1 ILE A 200 34.095 34.188 19.141 1.00149.20 C ANISOU 1398 CD1 ILE A 200 16712 11343 28635 -2666 -546 1701 C ATOM 1399 N PHE A 201 39.397 35.036 18.442 1.00184.47 N ANISOU 1399 N PHE A 201 20583 15309 34199 -2727 -560 2628 N ATOM 1400 CA PHE A 201 40.639 35.523 19.031 1.00190.07 C ANISOU 1400 CA PHE A 201 21096 15821 35301 -2737 -698 2635 C ATOM 1401 C PHE A 201 41.723 35.754 17.983 1.00193.50 C ANISOU 1401 C PHE A 201 21380 16157 35983 -2762 -587 3085 C ATOM 1402 O PHE A 201 42.590 36.610 18.156 1.00196.91 O ANISOU 1402 O PHE A 201 21573 16349 36894 -2780 -723 3167 O ATOM 1403 CB PHE A 201 41.137 34.561 20.111 1.00190.16 C ANISOU 1403 CB PHE A 201 21241 15962 35049 -2712 -695 2373 C ATOM 1404 CG PHE A 201 40.194 34.415 21.269 1.00190.13 C ANISOU 1404 CG PHE A 201 21362 16025 34852 -2677 -820 1922 C ATOM 1405 CD1 PHE A 201 40.236 35.304 22.331 1.00192.29 C ANISOU 1405 CD1 PHE A 201 21485 16103 35472 -2660 -1089 1638 C ATOM 1406 CD2 PHE A 201 39.262 33.391 21.296 1.00186.37 C ANISOU 1406 CD2 PHE A 201 21152 15805 33855 -2657 -666 1781 C ATOM 1407 CE1 PHE A 201 39.368 35.173 23.397 1.00192.01 C ANISOU 1407 CE1 PHE A 201 21568 16133 35256 -2617 -1200 1229 C ATOM 1408 CE2 PHE A 201 38.391 33.254 22.359 1.00185.19 C ANISOU 1408 CE2 PHE A 201 21116 15714 33533 -2619 -770 1375 C ATOM 1409 CZ PHE A 201 38.444 34.147 23.411 1.00189.29 C ANISOU 1409 CZ PHE A 201 21489 16042 34390 -2596 -1036 1102 C ATOM 1410 N ALA A 202 41.673 34.989 16.898 1.00193.05 N ANISOU 1410 N ALA A 202 21460 16285 35606 -2759 -339 3373 N ATOM 1411 CA ALA A 202 42.628 35.166 15.812 1.00196.17 C ANISOU 1411 CA ALA A 202 21730 16606 36201 -2771 -210 3822 C ATOM 1412 C ALA A 202 42.438 36.528 15.155 1.00199.07 C ANISOU 1412 C ALA A 202 21870 16732 37038 -2780 -306 4027 C ATOM 1413 O ALA A 202 43.408 37.194 14.796 1.00202.49 O ANISOU 1413 O ALA A 202 22086 16962 37889 -2796 -329 4287 O ATOM 1414 CB ALA A 202 42.487 34.054 14.787 1.00194.86 C ANISOU 1414 CB ALA A 202 21773 16702 35561 -2753 73 4066 C ATOM 1415 N ALA A 203 41.182 36.938 15.007 1.00196.81 N ANISOU 1415 N ALA A 203 21630 16463 36686 -2767 -357 3908 N ATOM 1416 CA ALA A 203 40.862 38.230 14.410 1.00195.36 C ANISOU 1416 CA ALA A 203 21247 16060 36921 -2767 -448 4080 C ATOM 1417 C ALA A 203 40.984 39.361 15.426 1.00194.64 C ANISOU 1417 C ALA A 203 20942 15693 37319 -2789 -730 3832 C ATOM 1418 O ALA A 203 41.428 40.459 15.093 1.00197.13 O ANISOU 1418 O ALA A 203 21016 15751 38134 -2802 -815 4026 O ATOM 1419 CB ALA A 203 39.467 38.208 13.801 1.00193.82 C ANISOU 1419 CB ALA A 203 21188 16004 36453 -2738 -387 4061 C ATOM 1420 N ALA A 204 40.588 39.087 16.666 1.00192.61 N ANISOU 1420 N ALA A 204 20775 15488 36920 -2788 -872 3402 N ATOM 1421 CA ALA A 204 40.657 40.083 17.730 1.00194.92 C ANISOU 1421 CA ALA A 204 20885 15539 37636 -2798 -1151 3120 C ATOM 1422 C ALA A 204 42.078 40.608 17.914 1.00200.66 C ANISOU 1422 C ALA A 204 21371 16037 38834 -2825 -1233 3260 C ATOM 1423 O ALA A 204 42.282 41.797 18.161 1.00205.94 O ANISOU 1423 O ALA A 204 21801 16429 40019 -2842 -1423 3236 O ATOM 1424 CB ALA A 204 40.130 39.506 19.035 1.00191.16 C ANISOU 1424 CB ALA A 204 20571 15192 36869 -2777 -1259 2651 C ATOM 1425 N ARG A 205 43.056 39.717 17.793 1.00198.70 N ANISOU 1425 N ARG A 205 21183 15902 38411 -2828 -1089 3402 N ATOM 1426 CA ARG A 205 44.457 40.099 17.927 1.00197.77 C ANISOU 1426 CA ARG A 205 20845 15588 38711 -2853 -1146 3548 C ATOM 1427 C ARG A 205 44.956 40.820 16.678 1.00194.95 C ANISOU 1427 C ARG A 205 20298 15061 38714 -2872 -1045 4015 C ATOM 1428 O ARG A 205 45.925 41.577 16.735 1.00194.15 O ANISOU 1428 O ARG A 205 19945 14710 39113 -2899 -1137 4138 O ATOM 1429 CB ARG A 205 45.331 38.879 18.232 1.00198.52 C ANISOU 1429 CB ARG A 205 21072 15869 38486 -2845 -1022 3540 C ATOM 1430 CG ARG A 205 45.391 38.501 19.709 1.00200.92 C ANISOU 1430 CG ARG A 205 21446 16223 38673 -2822 -1189 3088 C ATOM 1431 CD ARG A 205 44.006 38.248 20.286 1.00203.67 C ANISOU 1431 CD ARG A 205 21993 16719 38673 -2791 -1243 2739 C ATOM 1432 NE ARG A 205 44.052 37.844 21.689 1.00206.02 N ANISOU 1432 NE ARG A 205 22370 17076 38832 -2754 -1386 2315 N ATOM 1433 CZ ARG A 205 44.072 36.581 22.104 1.00204.64 C ANISOU 1433 CZ ARG A 205 22432 17155 38167 -2721 -1259 2181 C ATOM 1434 NH1 ARG A 205 44.049 35.591 21.222 1.00201.07 N ANISOU 1434 NH1 ARG A 205 22159 16920 37320 -2728 -991 2430 N ATOM 1435 NH2 ARG A 205 44.113 36.308 23.401 1.00204.61 N ANISOU 1435 NH2 ARG A 205 22487 17189 38068 -2674 -1399 1798 N ATOM 1436 N ARG A 206 44.289 40.582 15.553 1.00194.58 N ANISOU 1436 N ARG A 206 20370 15149 38414 -2853 -854 4272 N ATOM 1437 CA ARG A 206 44.605 41.292 14.319 1.00197.77 C ANISOU 1437 CA ARG A 206 20611 15405 39128 -2853 -749 4718 C ATOM 1438 C ARG A 206 44.069 42.718 14.379 1.00198.39 C ANISOU 1438 C ARG A 206 20483 15213 39682 -2861 -937 4670 C ATOM 1439 O ARG A 206 44.675 43.643 13.837 1.00202.41 O ANISOU 1439 O ARG A 206 20755 15477 40676 -2873 -948 4952 O ATOM 1440 CB ARG A 206 44.033 40.560 13.102 1.00202.25 C ANISOU 1440 CB ARG A 206 21381 16218 39248 -2815 -489 4994 C ATOM 1441 CG ARG A 206 44.681 39.212 12.826 1.00208.34 C ANISOU 1441 CG ARG A 206 22331 17233 39594 -2806 -274 5124 C ATOM 1442 CD ARG A 206 44.347 38.709 11.427 1.00212.45 C ANISOU 1442 CD ARG A 206 22986 17937 39797 -2763 -16 5486 C ATOM 1443 NE ARG A 206 42.920 38.455 11.249 1.00212.19 N ANISOU 1443 NE ARG A 206 23145 18086 39391 -2734 5 5323 N ATOM 1444 CZ ARG A 206 42.352 37.260 11.377 1.00206.22 C ANISOU 1444 CZ ARG A 206 22657 17622 38074 -2721 117 5154 C ATOM 1445 NH1 ARG A 206 43.089 36.202 11.684 1.00203.43 N ANISOU 1445 NH1 ARG A 206 22422 17415 37459 -2731 220 5130 N ATOM 1446 NH2 ARG A 206 41.045 37.122 11.195 1.00203.48 N ANISOU 1446 NH2 ARG A 206 22458 17418 37435 -2696 128 5008 N ATOM 1447 N GLN A 207 42.930 42.888 15.043 1.00193.58 N ANISOU 1447 N GLN A 207 19966 14649 38938 -2851 -1080 4315 N ATOM 1448 CA GLN A 207 42.355 44.210 15.248 1.00188.81 C ANISOU 1448 CA GLN A 207 19181 13798 38762 -2856 -1279 4214 C ATOM 1449 C GLN A 207 43.319 45.067 16.055 1.00189.76 C ANISOU 1449 C GLN A 207 19032 13617 39452 -2894 -1492 4107 C ATOM 1450 O GLN A 207 43.534 46.238 15.746 1.00191.84 O ANISOU 1450 O GLN A 207 19052 13600 40237 -2909 -1575 4265 O ATOM 1451 CB GLN A 207 41.015 44.108 15.981 1.00183.33 C ANISOU 1451 CB GLN A 207 18649 13224 37783 -2838 -1400 3806 C ATOM 1452 CG GLN A 207 39.971 43.266 15.266 1.00180.06 C ANISOU 1452 CG GLN A 207 18498 13107 36809 -2803 -1208 3864 C ATOM 1453 CD GLN A 207 39.531 43.872 13.949 1.00184.35 C ANISOU 1453 CD GLN A 207 18981 13601 37462 -2777 -1094 4228 C ATOM 1454 OE1 GLN A 207 39.783 45.046 13.677 1.00193.99 O ANISOU 1454 OE1 GLN A 207 19967 14552 39190 -2784 -1183 4388 O ATOM 1455 NE2 GLN A 207 38.864 43.073 13.124 1.00178.38 N ANISOU 1455 NE2 GLN A 207 18436 13107 36233 -2741 -894 4357 N ATOM 1456 N LEU A 208 43.899 44.469 17.090 1.00192.27 N ANISOU 1456 N LEU A 208 19393 13993 39668 -2904 -1576 3835 N ATOM 1457 CA LEU A 208 44.845 45.167 17.952 1.00200.32 C ANISOU 1457 CA LEU A 208 20168 14751 41191 -2933 -1789 3690 C ATOM 1458 C LEU A 208 46.141 45.492 17.217 1.00211.24 C ANISOU 1458 C LEU A 208 21336 15958 42969 -2963 -1692 4094 C ATOM 1459 O LEU A 208 46.825 46.458 17.553 1.00218.83 O ANISOU 1459 O LEU A 208 22025 16624 44496 -2992 -1855 4085 O ATOM 1460 CB LEU A 208 45.145 44.336 19.201 1.00198.53 C ANISOU 1460 CB LEU A 208 20064 14666 40703 -2920 -1886 3308 C ATOM 1461 CG LEU A 208 43.960 44.050 20.126 1.00197.25 C ANISOU 1461 CG LEU A 208 20096 14654 40194 -2885 -2005 2866 C ATOM 1462 CD1 LEU A 208 44.372 43.119 21.255 1.00196.03 C ANISOU 1462 CD1 LEU A 208 20073 14657 39751 -2859 -2058 2544 C ATOM 1463 CD2 LEU A 208 43.382 45.345 20.676 1.00199.19 C ANISOU 1463 CD2 LEU A 208 20166 14650 40867 -2888 -2264 2642 C ATOM 1464 N LYS A 209 46.476 44.684 16.216 1.00215.87 N ANISOU 1464 N LYS A 209 22040 16720 43260 -2952 -1425 4445 N ATOM 1465 CA LYS A 209 47.685 44.910 15.432 1.00225.71 C ANISOU 1465 CA LYS A 209 23100 17820 44839 -2972 -1301 4860 C ATOM 1466 C LYS A 209 47.500 46.074 14.463 1.00235.29 C ANISOU 1466 C LYS A 209 24118 18799 46483 -2972 -1271 5188 C ATOM 1467 O LYS A 209 48.408 46.881 14.268 1.00240.28 O ANISOU 1467 O LYS A 209 24481 19157 47659 -3001 -1308 5391 O ATOM 1468 CB LYS A 209 48.090 43.645 14.672 1.00225.09 C ANISOU 1468 CB LYS A 209 23222 18016 44287 -2952 -1020 5130 C ATOM 1469 CG LYS A 209 49.388 43.788 13.890 1.00229.15 C ANISOU 1469 CG LYS A 209 23554 18395 45116 -2967 -880 5560 C ATOM 1470 CD LYS A 209 49.767 42.493 13.190 1.00229.61 C ANISOU 1470 CD LYS A 209 23825 18737 44680 -2942 -608 5804 C ATOM 1471 CE LYS A 209 51.071 42.645 12.421 1.00234.18 C ANISOU 1471 CE LYS A 209 24221 19179 45579 -2952 -467 6236 C ATOM 1472 NZ LYS A 209 51.461 41.386 11.728 1.00233.19 N ANISOU 1472 NZ LYS A 209 24301 19328 44971 -2923 -201 6480 N ATOM 1473 N GLN A 210 46.320 46.153 13.855 1.00236.74 N ANISOU 1473 N GLN A 210 24436 19092 46423 -2937 -1200 5240 N ATOM 1474 CA GLN A 210 45.994 47.265 12.971 1.00239.00 C ANISOU 1474 CA GLN A 210 24556 19171 47081 -2922 -1177 5525 C ATOM 1475 C GLN A 210 45.900 48.552 13.780 1.00238.71 C ANISOU 1475 C GLN A 210 24278 18816 47606 -2955 -1455 5283 C ATOM 1476 O GLN A 210 46.233 49.632 13.293 1.00242.13 O ANISOU 1476 O GLN A 210 24466 18967 48565 -2965 -1474 5523 O ATOM 1477 CB GLN A 210 44.678 47.005 12.239 1.00240.41 C ANISOU 1477 CB GLN A 210 24949 19563 46833 -2869 -1057 5582 C ATOM 1478 CG GLN A 210 44.685 45.757 11.374 1.00242.98 C ANISOU 1478 CG GLN A 210 25515 20206 46599 -2830 -782 5819 C ATOM 1479 CD GLN A 210 43.381 45.563 10.627 1.00245.03 C ANISOU 1479 CD GLN A 210 25966 20664 46469 -2773 -676 5871 C ATOM 1480 OE1 GLN A 210 42.533 46.455 10.592 1.00246.46 O ANISOU 1480 OE1 GLN A 210 26079 20725 46838 -2758 -786 5800 O ATOM 1481 NE2 GLN A 210 43.214 44.392 10.021 1.00243.40 N ANISOU 1481 NE2 GLN A 210 25999 20763 45718 -2738 -462 5991 N ATOM 1482 N MET A 211 45.442 48.424 15.021 1.00235.35 N ANISOU 1482 N MET A 211 23924 18435 47064 -2967 -1666 4805 N ATOM 1483 CA MET A 211 45.360 49.558 15.930 1.00236.27 C ANISOU 1483 CA MET A 211 23826 18267 47678 -2994 -1950 4519 C ATOM 1484 C MET A 211 46.711 49.808 16.589 1.00240.96 C ANISOU 1484 C MET A 211 24196 18654 48706 -3038 -2072 4465 C ATOM 1485 O MET A 211 46.888 50.784 17.317 1.00248.24 O ANISOU 1485 O MET A 211 24898 19305 50115 -3063 -2308 4257 O ATOM 1486 CB MET A 211 44.292 49.315 16.996 1.00231.79 C ANISOU 1486 CB MET A 211 23434 17840 46796 -2976 -2125 4026 C ATOM 1487 CG MET A 211 42.888 49.151 16.441 1.00230.39 C ANISOU 1487 CG MET A 211 23461 17850 46226 -2936 -2034 4034 C ATOM 1488 SD MET A 211 41.664 48.952 17.747 1.00180.01 S ANISOU 1488 SD MET A 211 17260 11604 39533 -2915 -2247 3451 S ATOM 1489 CE MET A 211 41.939 50.452 18.683 1.00277.84 C ANISOU 1489 CE MET A 211 29333 23596 52635 -2943 -2576 3209 C ATOM 1490 N GLU A 212 47.660 48.915 16.333 1.00249.15 N ANISOU 1490 N GLU A 212 30003 22179 42486 -704 6440 4433 N ATOM 1491 CA GLU A 212 49.016 49.067 16.846 1.00250.65 C ANISOU 1491 CA GLU A 212 30033 22260 42943 -460 6503 3974 C ATOM 1492 C GLU A 212 49.834 49.925 15.888 1.00245.50 C ANISOU 1492 C GLU A 212 29234 21511 42533 -337 6909 3698 C ATOM 1493 O GLU A 212 50.862 50.490 16.262 1.00244.25 O ANISOU 1493 O GLU A 212 28852 21313 42637 -138 7088 3337 O ATOM 1494 CB GLU A 212 49.674 47.698 17.030 1.00260.06 C ANISOU 1494 CB GLU A 212 31484 23257 44071 -391 6125 3800 C ATOM 1495 CG GLU A 212 51.069 47.744 17.630 1.00266.21 C ANISOU 1495 CG GLU A 212 32115 23921 45110 -140 6151 3330 C ATOM 1496 CD GLU A 212 51.667 46.362 17.819 1.00271.01 C ANISOU 1496 CD GLU A 212 32989 24341 45640 -79 5764 3175 C ATOM 1497 OE1 GLU A 212 50.977 45.366 17.513 1.00272.06 O ANISOU 1497 OE1 GLU A 212 33421 24435 45513 -236 5471 3439 O ATOM 1498 OE2 GLU A 212 52.827 46.271 18.275 1.00273.06 O ANISOU 1498 OE2 GLU A 212 33160 24491 46099 124 5753 2790 O ATOM 1499 N SER A 213 49.361 50.022 14.650 1.00241.99 N ANISOU 1499 N SER A 213 28916 21032 41998 -458 7052 3874 N ATOM 1500 CA SER A 213 50.029 50.816 13.628 1.00239.03 C ANISOU 1500 CA SER A 213 28423 20569 41828 -364 7438 3650 C ATOM 1501 C SER A 213 49.141 51.967 13.164 1.00232.84 C ANISOU 1501 C SER A 213 27473 19962 41035 -488 7770 3912 C ATOM 1502 O SER A 213 49.125 52.312 11.983 1.00230.52 O ANISOU 1502 O SER A 213 27218 19606 40764 -526 8005 3930 O ATOM 1503 CB SER A 213 50.414 49.938 12.435 1.00242.83 C ANISOU 1503 CB SER A 213 29201 20825 42239 -376 7345 3576 C ATOM 1504 OG SER A 213 51.244 48.863 12.837 1.00246.36 O ANISOU 1504 OG SER A 213 29809 21104 42694 -259 7037 3331 O ATOM 1505 N GLN A 214 48.400 52.553 14.099 1.00231.59 N ANISOU 1505 N GLN A 214 27130 20024 40840 -551 7788 4116 N ATOM 1506 CA GLN A 214 47.520 53.674 13.785 1.00232.47 C ANISOU 1506 CA GLN A 214 27067 20320 40940 -667 8094 4373 C ATOM 1507 C GLN A 214 48.135 55.001 14.225 1.00238.36 C ANISOU 1507 C GLN A 214 27437 21151 41978 -508 8458 4121 C ATOM 1508 O GLN A 214 48.694 55.100 15.318 1.00239.49 O ANISOU 1508 O GLN A 214 27419 21324 42251 -372 8392 3914 O ATOM 1509 CB GLN A 214 46.147 53.483 14.433 1.00228.47 C ANISOU 1509 CB GLN A 214 26615 20016 40176 -867 7886 4815 C ATOM 1510 CG GLN A 214 46.183 53.372 15.947 1.00225.49 C ANISOU 1510 CG GLN A 214 26112 19750 39816 -804 7681 4776 C ATOM 1511 CD GLN A 214 44.805 53.184 16.552 1.00222.96 C ANISOU 1511 CD GLN A 214 25847 19632 39234 -1006 7478 5221 C ATOM 1512 OE1 GLN A 214 43.797 53.198 15.846 1.00223.93 O ANISOU 1512 OE1 GLN A 214 26090 19823 39169 -1195 7505 5564 O ATOM 1513 NE2 GLN A 214 44.756 53.007 17.868 1.00220.10 N ANISOU 1513 NE2 GLN A 214 25397 19370 38862 -967 7272 5217 N ATOM 1514 N PRO A 215 48.037 56.024 13.363 1.00240.99 N ANISOU 1514 N PRO A 215 27630 21519 42415 -525 8844 4137 N ATOM 1515 CA PRO A 215 48.596 57.358 13.614 1.00241.65 C ANISOU 1515 CA PRO A 215 27359 21678 42778 -383 9227 3907 C ATOM 1516 C PRO A 215 47.840 58.127 14.697 1.00244.75 C ANISOU 1516 C PRO A 215 27516 22320 43156 -432 9277 4105 C ATOM 1517 O PRO A 215 47.977 59.347 14.783 1.00242.99 O ANISOU 1517 O PRO A 215 27006 22198 43120 -366 9620 4019 O ATOM 1518 CB PRO A 215 48.430 58.068 12.263 1.00238.23 C ANISOU 1518 CB PRO A 215 26909 21220 42388 -441 9576 3966 C ATOM 1519 CG PRO A 215 48.205 56.976 11.264 1.00238.47 C ANISOU 1519 CG PRO A 215 27294 21097 42217 -552 9368 4094 C ATOM 1520 CD PRO A 215 47.469 55.916 12.010 1.00240.89 C ANISOU 1520 CD PRO A 215 27806 21455 42266 -673 8938 4353 C ATOM 1521 N LEU A 216 47.055 57.425 15.508 1.00250.29 N ANISOU 1521 N LEU A 216 28338 23121 43640 -545 8938 4367 N ATOM 1522 CA LEU A 216 46.281 58.071 16.564 1.00250.66 C ANISOU 1522 CA LEU A 216 28179 23408 43652 -601 8955 4576 C ATOM 1523 C LEU A 216 46.066 57.152 17.766 1.00246.77 C ANISOU 1523 C LEU A 216 27785 22957 43019 -617 8543 4652 C ATOM 1524 O LEU A 216 46.070 55.929 17.626 1.00248.80 O ANISOU 1524 O LEU A 216 28328 23090 43113 -665 8211 4695 O ATOM 1525 CB LEU A 216 44.939 58.574 16.017 1.00252.60 C ANISOU 1525 CB LEU A 216 28439 23820 43716 -816 9085 5007 C ATOM 1526 CG LEU A 216 44.109 57.631 15.139 1.00254.64 C ANISOU 1526 CG LEU A 216 29038 24023 43689 -1016 8871 5327 C ATOM 1527 CD1 LEU A 216 43.536 56.475 15.947 1.00255.62 C ANISOU 1527 CD1 LEU A 216 29371 24180 43571 -1114 8416 5537 C ATOM 1528 CD2 LEU A 216 42.992 58.399 14.448 1.00253.27 C ANISOU 1528 CD2 LEU A 216 28823 24003 43407 -1193 9106 5679 C ATOM 1529 N PRO A 217 45.888 57.745 18.957 1.00239.45 N ANISOU 1529 N PRO A 217 26618 22205 42157 -575 8563 4666 N ATOM 1530 CA PRO A 217 45.632 56.984 20.185 1.00236.74 C ANISOU 1530 CA PRO A 217 26337 21926 41687 -591 8190 4750 C ATOM 1531 C PRO A 217 44.389 56.105 20.065 1.00235.97 C ANISOU 1531 C PRO A 217 26514 21896 41250 -823 7882 5188 C ATOM 1532 O PRO A 217 44.508 54.886 19.932 1.00242.06 O ANISOU 1532 O PRO A 217 27564 22528 41880 -855 7557 5193 O ATOM 1533 CB PRO A 217 45.404 58.079 21.231 1.00231.56 C ANISOU 1533 CB PRO A 217 25347 21486 41150 -543 8367 4766 C ATOM 1534 CG PRO A 217 46.147 59.256 20.707 1.00230.72 C ANISOU 1534 CG PRO A 217 24991 21348 41322 -407 8803 4495 C ATOM 1535 CD PRO A 217 46.001 59.190 19.218 1.00233.14 C ANISOU 1535 CD PRO A 217 25466 21543 41571 -495 8949 4575 C ATOM 1536 N GLY A 218 43.213 56.723 20.114 1.00225.51 N ANISOU 1536 N GLY A 218 25108 20780 39797 -983 7985 5550 N ATOM 1537 CA GLY A 218 41.961 55.999 19.987 1.00215.50 C ANISOU 1537 CA GLY A 218 24078 19594 38206 -1212 7722 5987 C ATOM 1538 C GLY A 218 41.824 54.860 20.979 1.00207.94 C ANISOU 1538 C GLY A 218 23284 18633 37089 -1236 7274 6052 C ATOM 1539 O GLY A 218 41.648 53.705 20.591 1.00208.84 O ANISOU 1539 O GLY A 218 23704 18630 37013 -1324 6978 6157 O ATOM 1540 N GLU A 219 41.906 55.185 22.265 1.00199.16 N ANISOU 1540 N GLU A 219 21967 17650 36054 -1157 7223 5988 N ATOM 1541 CA GLU A 219 41.772 54.183 23.316 1.00192.41 C ANISOU 1541 CA GLU A 219 21238 16810 35059 -1173 6807 6046 C ATOM 1542 C GLU A 219 40.315 53.783 23.512 1.00197.58 C ANISOU 1542 C GLU A 219 22037 17633 35401 -1411 6586 6535 C ATOM 1543 O GLU A 219 40.016 52.823 24.219 1.00201.07 O ANISOU 1543 O GLU A 219 22638 18086 35672 -1468 6212 6653 O ATOM 1544 CB GLU A 219 42.370 54.691 24.630 1.00184.55 C ANISOU 1544 CB GLU A 219 19968 15896 34258 -1004 6835 5806 C ATOM 1545 CG GLU A 219 43.870 54.917 24.569 1.00182.92 C ANISOU 1545 CG GLU A 219 19639 15512 34350 -762 6992 5308 C ATOM 1546 CD GLU A 219 44.627 53.674 24.142 1.00180.71 C ANISOU 1546 CD GLU A 219 19640 14985 34035 -707 6730 5112 C ATOM 1547 OE1 GLU A 219 45.598 53.803 23.367 1.00175.88 O ANISOU 1547 OE1 GLU A 219 19026 14197 33602 -581 6912 4805 O ATOM 1548 OE2 GLU A 219 44.245 52.567 24.575 1.00184.82 O ANISOU 1548 OE2 GLU A 219 20387 15489 34349 -792 6341 5267 O ATOM 1549 N ARG A 220 39.413 54.529 22.883 1.00200.97 N ANISOU 1549 N ARG A 220 22408 18196 35757 -1550 6821 6816 N ATOM 1550 CA ARG A 220 37.995 54.193 22.908 1.00205.76 C ANISOU 1550 CA ARG A 220 23158 18960 36063 -1787 6641 7294 C ATOM 1551 C ARG A 220 37.754 52.873 22.191 1.00207.22 C ANISOU 1551 C ARG A 220 23723 18992 36019 -1910 6331 7435 C ATOM 1552 O ARG A 220 37.010 52.019 22.671 1.00203.84 O ANISOU 1552 O ARG A 220 23475 18624 35351 -2043 5987 7701 O ATOM 1553 CB ARG A 220 37.171 55.303 22.255 1.00209.47 C ANISOU 1553 CB ARG A 220 23486 19584 36519 -1899 6987 7537 C ATOM 1554 CG ARG A 220 36.845 56.454 23.185 1.00212.71 C ANISOU 1554 CG ARG A 220 23563 20224 37034 -1863 7190 7584 C ATOM 1555 CD ARG A 220 35.766 56.064 24.180 1.00218.86 C ANISOU 1555 CD ARG A 220 24381 21197 37579 -2006 6902 7934 C ATOM 1556 NE ARG A 220 35.548 57.102 25.182 1.00225.38 N ANISOU 1556 NE ARG A 220 24886 22234 38513 -1952 7070 7947 N ATOM 1557 CZ ARG A 220 36.026 57.055 26.421 1.00232.37 C ANISOU 1557 CZ ARG A 220 25634 23159 39496 -1825 6940 7767 C ATOM 1558 NH1 ARG A 220 36.744 56.012 26.816 1.00235.28 N ANISOU 1558 NH1 ARG A 220 26159 23371 39866 -1741 6638 7562 N ATOM 1559 NH2 ARG A 220 35.780 58.046 27.268 1.00233.75 N ANISOU 1559 NH2 ARG A 220 25516 23530 39766 -1784 7111 7795 N ATOM 1560 N ALA A 221 38.393 52.713 21.037 1.00169.00 N ANISOU 1560 N ALA A 221 29084 16522 18606 -2087 6564 1405 N ATOM 1561 CA ALA A 221 38.268 51.490 20.257 1.00170.80 C ANISOU 1561 CA ALA A 221 29124 17056 18715 -2325 6565 1299 C ATOM 1562 C ALA A 221 39.006 50.335 20.927 1.00170.01 C ANISOU 1562 C ALA A 221 28417 16811 19367 -2346 6103 715 C ATOM 1563 O ALA A 221 38.528 49.203 20.926 1.00165.82 O ANISOU 1563 O ALA A 221 27713 16615 18678 -2295 5733 794 O ATOM 1564 CB ALA A 221 38.778 51.706 18.843 1.00172.24 C ANISOU 1564 CB ALA A 221 29426 17150 18866 -2809 7351 1090 C ATOM 1565 N ARG A 222 40.172 50.627 21.498 1.00174.09 N ANISOU 1565 N ARG A 222 28607 16833 20707 -2424 6136 137 N ATOM 1566 CA ARG A 222 40.947 49.614 22.207 1.00174.46 C ANISOU 1566 CA ARG A 222 28052 16717 21520 -2425 5707 -418 C ATOM 1567 C ARG A 222 40.218 49.131 23.454 1.00171.53 C ANISOU 1567 C ARG A 222 27559 16591 21024 -1944 4889 -115 C ATOM 1568 O ARG A 222 40.085 47.929 23.678 1.00176.26 O ANISOU 1568 O ARG A 222 27829 17392 21751 -1886 4477 -206 O ATOM 1569 CB ARG A 222 42.328 50.148 22.592 1.00180.10 C ANISOU 1569 CB ARG A 222 28457 16865 23109 -2597 5919 -1063 C ATOM 1570 CG ARG A 222 43.450 49.711 21.665 1.00186.35 C ANISOU 1570 CG ARG A 222 28952 17391 24459 -3092 6444 -1686 C ATOM 1571 CD ARG A 222 44.806 49.930 22.314 1.00193.36 C ANISOU 1571 CD ARG A 222 29398 17770 26301 -3198 6451 -2350 C ATOM 1572 NE ARG A 222 45.908 49.541 21.438 1.00204.43 N ANISOU 1572 NE ARG A 222 30512 18902 28259 -3666 6967 -2946 N ATOM 1573 CZ ARG A 222 46.617 50.394 20.706 1.00218.28 C ANISOU 1573 CZ ARG A 222 32410 20332 30194 -3993 7639 -3189 C ATOM 1574 NH1 ARG A 222 46.343 51.692 20.745 1.00223.03 N ANISOU 1574 NH1 ARG A 222 33441 20828 30474 -3905 7886 -2889 N ATOM 1575 NH2 ARG A 222 47.603 49.951 19.938 1.00223.38 N ANISOU 1575 NH2 ARG A 222 32770 20750 31354 -4406 8074 -3729 N ATOM 1576 N SER A 223 39.749 50.074 24.265 1.00165.76 N ANISOU 1576 N SER A 223 27094 15836 20050 -1598 4669 247 N ATOM 1577 CA SER A 223 39.039 49.738 25.493 1.00166.52 C ANISOU 1577 CA SER A 223 27107 16158 20005 -1119 3901 563 C ATOM 1578 C SER A 223 37.787 48.918 25.200 1.00167.20 C ANISOU 1578 C SER A 223 27363 16799 19365 -953 3601 1115 C ATOM 1579 O SER A 223 37.481 47.964 25.913 1.00165.20 O ANISOU 1579 O SER A 223 26817 16748 19203 -715 2993 1148 O ATOM 1580 CB SER A 223 38.672 51.005 26.268 1.00167.53 C ANISOU 1580 CB SER A 223 27576 16176 19903 -800 3810 903 C ATOM 1581 OG SER A 223 38.024 50.687 27.487 1.00166.82 O ANISOU 1581 OG SER A 223 27391 16296 19699 -335 3065 1188 O ATOM 1582 N THR A 224 37.068 49.294 24.147 1.00170.06 N ANISOU 1582 N THR A 224 28191 17416 19007 -1083 4036 1554 N ATOM 1583 CA THR A 224 35.863 48.576 23.744 1.00162.80 C ANISOU 1583 CA THR A 224 27464 17049 17344 -972 3815 2092 C ATOM 1584 C THR A 224 36.208 47.191 23.207 1.00155.70 C ANISOU 1584 C THR A 224 26173 16257 16727 -1254 3787 1704 C ATOM 1585 O THR A 224 35.539 46.205 23.518 1.00145.30 O ANISOU 1585 O THR A 224 24722 15284 15203 -1070 3291 1908 O ATOM 1586 CB THR A 224 35.075 49.351 22.672 1.00162.65 C ANISOU 1586 CB THR A 224 28024 17285 16490 -1079 4341 2640 C ATOM 1587 OG1 THR A 224 34.657 50.615 23.203 1.00158.92 O ANISOU 1587 OG1 THR A 224 27933 16728 15722 -781 4354 3057 O ATOM 1588 CG2 THR A 224 33.850 48.562 22.234 1.00160.86 C ANISOU 1588 CG2 THR A 224 27968 17656 15495 -991 4108 3177 C ATOM 1589 N LEU A 225 37.259 47.128 22.397 1.00153.62 N ANISOU 1589 N LEU A 225 25731 15690 16947 -1704 4335 1141 N ATOM 1590 CA LEU A 225 37.719 45.870 21.825 1.00139.19 C ANISOU 1590 CA LEU A 225 23528 13900 15457 -2014 4395 707 C ATOM 1591 C LEU A 225 38.116 44.900 22.931 1.00134.05 C ANISOU 1591 C LEU A 225 22330 13150 15452 -1802 3761 375 C ATOM 1592 O LEU A 225 37.722 43.736 22.915 1.00139.52 O ANISOU 1592 O LEU A 225 22821 14115 16075 -1774 3447 407 O ATOM 1593 CB LEU A 225 38.901 46.123 20.884 1.00139.76 C ANISOU 1593 CB LEU A 225 23492 13590 16020 -2509 5106 127 C ATOM 1594 CG LEU A 225 39.330 45.020 19.912 1.00143.73 C ANISOU 1594 CG LEU A 225 23738 14143 16728 -2924 5392 -277 C ATOM 1595 CD1 LEU A 225 40.035 43.885 20.637 1.00151.24 C ANISOU 1595 CD1 LEU A 225 24079 14917 18469 -2887 4968 -791 C ATOM 1596 CD2 LEU A 225 38.132 44.506 19.128 1.00141.24 C ANISOU 1596 CD2 LEU A 225 23736 14387 15540 -2958 5401 236 C ATOM 1597 N GLN A 226 38.891 45.388 23.895 1.00137.11 N ANISOU 1597 N GLN A 226 22477 13156 16465 -1655 3580 65 N ATOM 1598 CA GLN A 226 39.351 44.559 25.004 1.00147.97 C ANISOU 1598 CA GLN A 226 23308 14421 18493 -1444 2988 -258 C ATOM 1599 C GLN A 226 38.195 44.098 25.886 1.00149.96 C ANISOU 1599 C GLN A 226 23613 15077 18289 -968 2270 284 C ATOM 1600 O GLN A 226 38.275 43.050 26.526 1.00152.95 O ANISOU 1600 O GLN A 226 23568 15523 19024 -818 1780 129 O ATOM 1601 CB GLN A 226 40.386 45.308 25.845 1.00158.35 C ANISOU 1601 CB GLN A 226 24387 15272 20509 -1390 2961 -670 C ATOM 1602 CG GLN A 226 41.655 45.674 25.092 1.00166.07 C ANISOU 1602 CG GLN A 226 25225 15815 22060 -1854 3623 -1273 C ATOM 1603 CD GLN A 226 42.668 46.385 25.968 1.00166.45 C ANISOU 1603 CD GLN A 226 25017 15423 22802 -1804 3567 -1685 C ATOM 1604 OE1 GLN A 226 42.611 46.301 27.195 1.00166.45 O ANISOU 1604 OE1 GLN A 226 24793 15430 23019 -1451 2976 -1652 O ATOM 1605 NE2 GLN A 226 43.605 47.089 25.342 1.00166.09 N ANISOU 1605 NE2 GLN A 226 24999 15003 23106 -2164 4184 -2079 N ATOM 1606 N LYS A 227 37.125 44.886 25.922 1.00150.75 N ANISOU 1606 N LYS A 227 24229 15441 17608 -724 2218 931 N ATOM 1607 CA LYS A 227 35.942 44.526 26.697 1.00154.21 C ANISOU 1607 CA LYS A 227 24771 16285 17536 -269 1567 1505 C ATOM 1608 C LYS A 227 35.056 43.554 25.924 1.00153.79 C ANISOU 1608 C LYS A 227 24821 16690 16920 -358 1537 1814 C ATOM 1609 O LYS A 227 34.343 42.743 26.517 1.00145.62 O ANISOU 1609 O LYS A 227 23662 15960 15706 -67 964 2084 O ATOM 1610 CB LYS A 227 35.150 45.774 27.095 1.00159.41 C ANISOU 1610 CB LYS A 227 25935 17036 17597 46 1518 2086 C ATOM 1611 CG LYS A 227 35.854 46.650 28.119 1.00166.55 C ANISOU 1611 CG LYS A 227 26723 17540 19017 222 1392 1838 C ATOM 1612 CD LYS A 227 35.026 47.878 28.468 1.00168.67 C ANISOU 1612 CD LYS A 227 27519 17897 18672 528 1380 2427 C ATOM 1613 CE LYS A 227 35.754 48.767 29.466 1.00170.31 C ANISOU 1613 CE LYS A 227 27618 17694 19399 672 1285 2144 C ATOM 1614 NZ LYS A 227 34.974 49.991 29.798 1.00168.20 N ANISOU 1614 NZ LYS A 227 27874 17478 18557 961 1314 2700 N ATOM 1615 N GLU A 228 35.106 43.642 24.599 1.00160.71 N ANISOU 1615 N GLU A 228 25924 17622 17518 -767 2159 1770 N ATOM 1616 CA GLU A 228 34.395 42.702 23.741 1.00160.17 C ANISOU 1616 CA GLU A 228 25930 17969 16957 -936 2210 1974 C ATOM 1617 C GLU A 228 35.106 41.353 23.741 1.00155.03 C ANISOU 1617 C GLU A 228 24725 17202 16978 -1128 2082 1405 C ATOM 1618 O GLU A 228 34.475 40.305 23.608 1.00155.11 O ANISOU 1618 O GLU A 228 24647 17548 16741 -1102 1816 1559 O ATOM 1619 CB GLU A 228 34.294 43.244 22.314 1.00166.76 C ANISOU 1619 CB GLU A 228 27162 18896 17304 -1333 2941 2074 C ATOM 1620 CG GLU A 228 33.354 44.428 22.163 1.00167.63 C ANISOU 1620 CG GLU A 228 27857 19234 16602 -1139 3077 2757 C ATOM 1621 CD GLU A 228 31.900 44.043 22.352 1.00164.97 C ANISOU 1621 CD GLU A 228 27766 19466 15452 -825 2623 3464 C ATOM 1622 OE1 GLU A 228 31.581 42.841 22.235 1.00164.42 O ANISOU 1622 OE1 GLU A 228 27475 19659 15337 -875 2354 3423 O ATOM 1623 OE2 GLU A 228 31.074 44.943 22.612 1.00163.21 O ANISOU 1623 OE2 GLU A 228 27955 19422 14636 -532 2548 4063 O ATOM 1624 N VAL A 229 36.426 41.390 23.893 1.00149.83 N ANISOU 1624 N VAL A 229 23690 16061 17177 -1321 2283 749 N ATOM 1625 CA VAL A 229 37.225 40.174 23.967 1.00145.85 C ANISOU 1625 CA VAL A 229 22624 15387 17404 -1488 2184 179 C ATOM 1626 C VAL A 229 37.084 39.521 25.338 1.00142.39 C ANISOU 1626 C VAL A 229 21808 14987 17305 -1052 1417 221 C ATOM 1627 O VAL A 229 37.049 38.296 25.451 1.00147.63 O ANISOU 1627 O VAL A 229 22129 15762 18201 -1047 1148 79 O ATOM 1628 CB VAL A 229 38.712 40.455 23.681 1.00147.75 C ANISOU 1628 CB VAL A 229 22573 15101 18463 -1836 2663 -527 C ATOM 1629 CG1 VAL A 229 39.556 39.226 23.983 1.00153.76 C ANISOU 1629 CG1 VAL A 229 22709 15667 20045 -1928 2481 -1090 C ATOM 1630 CG2 VAL A 229 38.899 40.892 22.237 1.00146.65 C ANISOU 1630 CG2 VAL A 229 22750 14935 18036 -2303 3438 -618 C ATOM 1631 N HIS A 230 37.000 40.345 26.378 1.00133.99 N ANISOU 1631 N HIS A 230 20809 13831 16268 -687 1077 418 N ATOM 1632 CA HIS A 230 36.816 39.843 27.735 1.00132.00 C ANISOU 1632 CA HIS A 230 20229 13641 16286 -242 335 505 C ATOM 1633 C HIS A 230 35.492 39.096 27.853 1.00131.82 C ANISOU 1633 C HIS A 230 20354 14124 15607 21 -114 1073 C ATOM 1634 O HIS A 230 35.385 38.115 28.590 1.00128.96 O ANISOU 1634 O HIS A 230 19617 13859 15525 251 -639 1042 O ATOM 1635 CB HIS A 230 36.868 40.988 28.748 1.00133.90 C ANISOU 1635 CB HIS A 230 20592 13723 16562 85 98 659 C ATOM 1636 CG HIS A 230 36.727 40.545 30.172 1.00132.26 C ANISOU 1636 CG HIS A 230 20041 13576 16637 543 -657 736 C ATOM 1637 ND1 HIS A 230 37.809 40.310 30.989 1.00131.90 N ANISOU 1637 ND1 HIS A 230 19456 13203 17457 582 -864 214 N ATOM 1638 CD2 HIS A 230 35.626 40.295 30.922 1.00126.25 C ANISOU 1638 CD2 HIS A 230 19392 13178 15398 983 -1253 1287 C ATOM 1639 CE1 HIS A 230 37.384 39.934 32.184 1.00124.59 C ANISOU 1639 CE1 HIS A 230 18323 12443 16572 1028 -1556 438 C ATOM 1640 NE2 HIS A 230 36.064 39.917 32.168 1.00121.46 N ANISOU 1640 NE2 HIS A 230 18317 12457 15373 1279 -1803 1085 N ATOM 1641 N ALA A 231 34.486 39.565 27.122 1.00136.61 N ANISOU 1641 N ALA A 231 21503 15061 15343 -13 102 1601 N ATOM 1642 CA ALA A 231 33.186 38.908 27.100 1.00130.85 C ANISOU 1642 CA ALA A 231 20955 14841 13921 194 -266 2163 C ATOM 1643 C ALA A 231 33.249 37.631 26.271 1.00132.76 C ANISOU 1643 C ALA A 231 20975 15213 14254 -137 -105 1907 C ATOM 1644 O ALA A 231 32.650 36.618 26.628 1.00137.70 O ANISOU 1644 O ALA A 231 21427 16109 14785 45 -556 2081 O ATOM 1645 CB ALA A 231 32.123 39.847 26.553 1.00127.42 C ANISOU 1645 CB ALA A 231 21160 14728 12528 249 -59 2811 C ATOM 1646 N ALA A 232 33.982 37.688 25.163 1.00135.32 N ANISOU 1646 N ALA A 232 21308 15338 14769 -626 552 1488 N ATOM 1647 CA ALA A 232 34.152 36.529 24.295 1.00133.56 C ANISOU 1647 CA ALA A 232 20881 15194 14672 -993 789 1179 C ATOM 1648 C ALA A 232 34.939 35.431 25.004 1.00131.90 C ANISOU 1648 C ALA A 232 20036 14734 15344 -933 462 679 C ATOM 1649 O ALA A 232 34.679 34.243 24.812 1.00128.65 O ANISOU 1649 O ALA A 232 19414 14497 14968 -1003 322 618 O ATOM 1650 CB ALA A 232 34.843 36.931 23.002 1.00132.55 C ANISOU 1650 CB ALA A 232 20898 14874 14591 -1520 1580 821 C ATOM 1651 N LYS A 233 35.903 35.838 25.825 1.00134.12 N ANISOU 1651 N LYS A 233 20008 14612 16340 -805 352 326 N ATOM 1652 CA LYS A 233 36.703 34.892 26.591 1.00134.56 C ANISOU 1652 CA LYS A 233 19437 14424 17264 -713 30 -129 C ATOM 1653 C LYS A 233 35.870 34.259 27.699 1.00127.84 C ANISOU 1653 C LYS A 233 18440 13859 16274 -221 -737 271 C ATOM 1654 O LYS A 233 35.945 33.053 27.932 1.00133.56 O ANISOU 1654 O LYS A 233 18768 14619 17358 -186 -991 103 O ATOM 1655 CB LYS A 233 37.936 35.577 27.184 1.00143.28 C ANISOU 1655 CB LYS A 233 20260 15054 19127 -709 112 -585 C ATOM 1656 CG LYS A 233 38.827 34.642 27.986 1.00151.51 C ANISOU 1656 CG LYS A 233 20626 15848 21092 -614 -204 -1054 C ATOM 1657 CD LYS A 233 40.096 35.334 28.459 1.00159.66 C ANISOU 1657 CD LYS A 233 21376 16423 22863 -668 -65 -1533 C ATOM 1658 CE LYS A 233 41.000 34.361 29.207 1.00163.49 C ANISOU 1658 CE LYS A 233 21164 16687 24269 -585 -358 -1991 C ATOM 1659 NZ LYS A 233 42.279 34.989 29.641 1.00168.80 N ANISOU 1659 NZ LYS A 233 21526 16931 25679 -665 -215 -2480 N ATOM 1660 N SER A 234 35.076 35.080 28.378 1.00120.84 N ANISOU 1660 N SER A 234 17876 13168 14870 161 -1090 804 N ATOM 1661 CA SER A 234 34.192 34.592 29.429 1.00119.17 C ANISOU 1661 CA SER A 234 17581 13255 14442 650 -1818 1246 C ATOM 1662 C SER A 234 33.210 33.572 28.865 1.00115.50 C ANISOU 1662 C SER A 234 17221 13203 13463 597 -1911 1548 C ATOM 1663 O SER A 234 32.908 32.566 29.507 1.00110.27 O ANISOU 1663 O SER A 234 16244 12678 12976 837 -2402 1618 O ATOM 1664 CB SER A 234 33.434 35.752 30.075 1.00125.13 C ANISOU 1664 CB SER A 234 18753 14166 14624 1026 -2086 1801 C ATOM 1665 OG SER A 234 34.325 36.672 30.680 1.00131.38 O ANISOU 1665 OG SER A 234 19435 14579 15904 1087 -2034 1513 O ATOM 1666 N ALA A 235 32.716 33.840 27.661 1.00116.49 N ANISOU 1666 N ALA A 235 17781 13530 12948 275 -1433 1729 N ATOM 1667 CA ALA A 235 31.798 32.931 26.987 1.00113.50 C ANISOU 1667 CA ALA A 235 17533 13559 12033 156 -1449 1993 C ATOM 1668 C ALA A 235 32.503 31.628 26.630 1.00113.04 C ANISOU 1668 C ALA A 235 17000 13331 12620 -135 -1311 1433 C ATOM 1669 O ALA A 235 31.899 30.556 26.654 1.00113.20 O ANISOU 1669 O ALA A 235 16893 13609 12508 -79 -1583 1568 O ATOM 1670 CB ALA A 235 31.227 33.585 25.739 1.00113.31 C ANISOU 1670 CB ALA A 235 18063 13779 11209 -158 -917 2270 C ATOM 1671 N ALA A 236 33.786 31.731 26.298 1.00113.39 N ANISOU 1671 N ALA A 236 16781 12932 13370 -447 -874 806 N ATOM 1672 CA ALA A 236 34.588 30.561 25.966 1.00110.67 C ANISOU 1672 CA ALA A 236 15967 12367 13718 -730 -690 233 C ATOM 1673 C ALA A 236 34.780 29.678 27.192 1.00107.77 C ANISOU 1673 C ALA A 236 15068 11915 13965 -355 -1305 145 C ATOM 1674 O ALA A 236 34.817 28.453 27.085 1.00113.94 O ANISOU 1674 O ALA A 236 15533 12722 15039 -437 -1374 -46 O ATOM 1675 CB ALA A 236 35.932 30.981 25.397 1.00115.20 C ANISOU 1675 CB ALA A 236 16387 12477 14909 -1118 -92 -390 C ATOM 1676 N ILE A 237 34.902 30.308 28.356 1.00102.90 N ANISOU 1676 N ILE A 237 14352 11200 13543 56 -1739 287 N ATOM 1677 CA ILE A 237 35.078 29.575 29.603 1.00107.26 C ANISOU 1677 CA ILE A 237 14401 11694 14657 450 -2351 242 C ATOM 1678 C ILE A 237 33.797 28.840 29.988 1.00112.80 C ANISOU 1678 C ILE A 237 15192 12842 14825 766 -2877 785 C ATOM 1679 O ILE A 237 33.844 27.734 30.525 1.00109.89 O ANISOU 1679 O ILE A 237 14395 12479 14878 926 -3222 691 O ATOM 1680 CB ILE A 237 35.506 30.502 30.755 1.00107.47 C ANISOU 1680 CB ILE A 237 14322 11534 14978 803 -2683 266 C ATOM 1681 CG1 ILE A 237 36.760 31.288 30.370 1.00109.35 C ANISOU 1681 CG1 ILE A 237 14488 11336 15726 480 -2154 -263 C ATOM 1682 CG2 ILE A 237 35.756 29.699 32.020 1.00106.94 C ANISOU 1682 CG2 ILE A 237 13692 11416 15523 1193 -3297 194 C ATOM 1683 CD1 ILE A 237 37.292 32.168 31.480 1.00103.92 C ANISOU 1683 CD1 ILE A 237 13657 10437 15392 778 -2445 -315 C ATOM 1684 N ILE A 238 32.655 29.459 29.707 1.00125.29 N ANISOU 1684 N ILE A 238 17326 14796 15484 857 -2927 1364 N ATOM 1685 CA ILE A 238 31.364 28.838 29.978 1.00128.13 C ANISOU 1685 CA ILE A 238 17824 15610 15250 1133 -3393 1919 C ATOM 1686 C ILE A 238 31.187 27.590 29.119 1.00129.60 C ANISOU 1686 C ILE A 238 17891 15919 15431 803 -3174 1743 C ATOM 1687 O ILE A 238 30.773 26.539 29.610 1.00130.27 O ANISOU 1687 O ILE A 238 17708 16154 15636 1007 -3586 1851 O ATOM 1688 CB ILE A 238 30.200 29.809 29.704 1.00130.56 C ANISOU 1688 CB ILE A 238 18772 16297 14536 1247 -3407 2572 C ATOM 1689 CG1 ILE A 238 30.378 31.096 30.511 1.00140.40 C ANISOU 1689 CG1 ILE A 238 20167 17399 15779 1553 -3573 2735 C ATOM 1690 CG2 ILE A 238 28.869 29.152 30.035 1.00120.32 C ANISOU 1690 CG2 ILE A 238 17595 15478 12642 1547 -3916 3154 C ATOM 1691 CD1 ILE A 238 29.323 32.147 30.230 1.00147.43 C ANISOU 1691 CD1 ILE A 238 21690 18615 15713 1664 -3527 3364 C ATOM 1692 N ALA A 239 31.507 27.713 27.835 1.00129.27 N ANISOU 1692 N ALA A 239 18049 15813 15255 289 -2511 1467 N ATOM 1693 CA ALA A 239 31.392 26.598 26.904 1.00128.30 C ANISOU 1693 CA ALA A 239 17846 15792 15109 -87 -2221 1252 C ATOM 1694 C ALA A 239 32.401 25.504 27.228 1.00135.04 C ANISOU 1694 C ALA A 239 18068 16282 16957 -150 -2237 670 C ATOM 1695 O ALA A 239 32.083 24.316 27.174 1.00136.19 O ANISOU 1695 O ALA A 239 18000 16548 17197 -175 -2374 638 O ATOM 1696 CB ALA A 239 31.579 27.082 25.478 1.00125.05 C ANISOU 1696 CB ALA A 239 17791 15381 14341 -622 -1490 1072 C ATOM 1697 N GLY A 240 33.621 25.913 27.564 1.00137.30 N ANISOU 1697 N GLY A 240 18054 16124 17991 -176 -2084 214 N ATOM 1698 CA GLY A 240 34.675 24.975 27.901 1.00135.50 C ANISOU 1698 CA GLY A 240 17206 15527 18749 -224 -2075 -341 C ATOM 1699 C GLY A 240 34.288 24.065 29.049 1.00128.74 C ANISOU 1699 C GLY A 240 15973 14784 18159 232 -2751 -133 C ATOM 1700 O GLY A 240 34.568 22.866 29.024 1.00126.74 O ANISOU 1700 O GLY A 240 15323 14432 18402 155 -2751 -408 O ATOM 1701 N LEU A 241 33.639 24.636 30.058 1.00126.60 N ANISOU 1701 N LEU A 241 15825 14716 17561 712 -3317 359 N ATOM 1702 CA LEU A 241 33.216 23.871 31.224 1.00127.29 C ANISOU 1702 CA LEU A 241 15574 14936 17854 1190 -3997 611 C ATOM 1703 C LEU A 241 32.081 22.910 30.885 1.00128.24 C ANISOU 1703 C LEU A 241 15833 15441 17452 1192 -4158 956 C ATOM 1704 O LEU A 241 31.845 21.942 31.604 1.00131.88 O ANISOU 1704 O LEU A 241 15941 15967 18199 1474 -4597 1046 O ATOM 1705 CB LEU A 241 32.793 24.804 32.360 1.00127.74 C ANISOU 1705 CB LEU A 241 15763 15123 17649 1693 -4540 1056 C ATOM 1706 CG LEU A 241 33.885 25.702 32.944 1.00133.61 C ANISOU 1706 CG LEU A 241 16308 15501 18955 1764 -4498 736 C ATOM 1707 CD1 LEU A 241 33.326 26.557 34.070 1.00137.71 C ANISOU 1707 CD1 LEU A 241 16989 16193 19143 2267 -5057 1211 C ATOM 1708 CD2 LEU A 241 35.061 24.872 33.431 1.00128.39 C ANISOU 1708 CD2 LEU A 241 14957 14483 19343 1762 -4531 193 C ATOM 1709 N PHE A 242 31.377 23.182 29.791 1.00123.37 N ANISOU 1709 N PHE A 242 15724 15087 16064 875 -3801 1154 N ATOM 1710 CA PHE A 242 30.293 22.309 29.358 1.00119.91 C ANISOU 1710 CA PHE A 242 15447 15036 15080 819 -3905 1464 C ATOM 1711 C PHE A 242 30.849 20.979 28.861 1.00126.38 C ANISOU 1711 C PHE A 242 15865 15657 16499 503 -3626 960 C ATOM 1712 O PHE A 242 30.508 19.917 29.383 1.00125.26 O ANISOU 1712 O PHE A 242 15423 15598 16572 710 -3992 1045 O ATOM 1713 CB PHE A 242 29.458 22.977 28.265 1.00116.58 C ANISOU 1713 CB PHE A 242 15657 14959 13679 529 -3557 1785 C ATOM 1714 CG PHE A 242 28.252 22.179 27.852 1.00121.86 C ANISOU 1714 CG PHE A 242 16524 16081 13696 482 -3698 2159 C ATOM 1715 CD1 PHE A 242 27.015 22.419 28.428 1.00122.17 C ANISOU 1715 CD1 PHE A 242 16838 16549 13034 878 -4224 2847 C ATOM 1716 CD2 PHE A 242 28.356 21.185 26.892 1.00129.37 C ANISOU 1716 CD2 PHE A 242 17384 17031 14738 35 -3300 1818 C ATOM 1717 CE1 PHE A 242 25.904 21.685 28.052 1.00123.87 C ANISOU 1717 CE1 PHE A 242 17226 17193 12646 827 -4358 3194 C ATOM 1718 CE2 PHE A 242 27.250 20.448 26.513 1.00131.53 C ANISOU 1718 CE2 PHE A 242 17835 17729 14411 -28 -3427 2146 C ATOM 1719 CZ PHE A 242 26.022 20.699 27.093 1.00127.79 C ANISOU 1719 CZ PHE A 242 17627 17690 13237 367 -3961 2838 C ATOM 1720 N ALA A 243 31.708 21.043 27.850 1.00128.37 N ANISOU 1720 N ALA A 243 16112 15636 17027 2 -2965 437 N ATOM 1721 CA ALA A 243 32.347 19.847 27.316 1.00124.17 C ANISOU 1721 CA ALA A 243 15205 14866 17107 -332 -2624 -93 C ATOM 1722 C ALA A 243 33.148 19.137 28.402 1.00120.48 C ANISOU 1722 C ALA A 243 14088 14068 17623 -19 -2958 -363 C ATOM 1723 O ALA A 243 33.219 17.911 28.437 1.00121.68 O ANISOU 1723 O ALA A 243 13890 14152 18191 -53 -2991 -549 O ATOM 1724 CB ALA A 243 33.243 20.204 26.140 1.00126.82 C ANISOU 1724 CB ALA A 243 15640 14930 17616 -887 -1862 -615 C ATOM 1725 N LEU A 244 33.745 19.921 29.293 1.00119.45 N ANISOU 1725 N LEU A 244 13792 13738 17855 285 -3202 -376 N ATOM 1726 CA LEU A 244 34.566 19.379 30.369 1.00119.91 C ANISOU 1726 CA LEU A 244 13221 13498 18840 594 -3526 -619 C ATOM 1727 C LEU A 244 33.738 18.575 31.370 1.00115.57 C ANISOU 1727 C LEU A 244 12467 13203 18240 1071 -4201 -198 C ATOM 1728 O LEU A 244 34.265 17.708 32.066 1.00106.77 O ANISOU 1728 O LEU A 244 10799 11893 17877 1269 -4421 -397 O ATOM 1729 CB LEU A 244 35.310 20.510 31.086 1.00121.41 C ANISOU 1729 CB LEU A 244 13331 13471 19329 801 -3645 -695 C ATOM 1730 CG LEU A 244 36.309 20.115 32.175 1.00123.39 C ANISOU 1730 CG LEU A 244 12919 13406 20557 1088 -3936 -986 C ATOM 1731 CD1 LEU A 244 37.374 19.187 31.615 1.00132.19 C ANISOU 1731 CD1 LEU A 244 13589 14148 22489 735 -3461 -1609 C ATOM 1732 CD2 LEU A 244 36.942 21.351 32.795 1.00120.35 C ANISOU 1732 CD2 LEU A 244 12534 12856 20337 1248 -4032 -1038 C ATOM 1733 N CYS A 245 32.442 18.862 31.435 1.00125.61 N ANISOU 1733 N CYS A 245 14179 14916 18630 1259 -4522 397 N ATOM 1734 CA CYS A 245 31.563 18.204 32.397 1.00137.27 C ANISOU 1734 CA CYS A 245 15511 16667 19976 1732 -5184 856 C ATOM 1735 C CYS A 245 30.669 17.156 31.743 1.00142.79 C ANISOU 1735 C CYS A 245 16336 17637 20282 1548 -5120 1004 C ATOM 1736 O CYS A 245 29.972 16.411 32.432 1.00141.91 O ANISOU 1736 O CYS A 245 16064 17730 20126 1887 -5613 1331 O ATOM 1737 CB CYS A 245 30.699 19.234 33.128 1.00138.37 C ANISOU 1737 CB CYS A 245 16014 17123 19437 2152 -5680 1466 C ATOM 1738 SG CYS A 245 31.617 20.371 34.193 1.00176.92 S ANISOU 1738 SG CYS A 245 20701 21730 24792 2475 -5909 1358 S ATOM 1739 N TRP A 246 30.691 17.100 30.416 1.00146.08 N ANISOU 1739 N TRP A 246 17033 18059 20410 1005 -4511 760 N ATOM 1740 CA TRP A 246 29.850 16.156 29.687 1.00143.10 C ANISOU 1740 CA TRP A 246 16807 17952 19611 765 -4395 867 C ATOM 1741 C TRP A 246 30.653 15.099 28.930 1.00137.14 C ANISOU 1741 C TRP A 246 15725 16877 19503 325 -3869 244 C ATOM 1742 O TRP A 246 30.192 13.971 28.763 1.00138.12 O ANISOU 1742 O TRP A 246 15724 17108 19649 256 -3906 249 O ATOM 1743 CB TRP A 246 28.901 16.897 28.740 1.00147.50 C ANISOU 1743 CB TRP A 246 18031 18913 19101 508 -4175 1217 C ATOM 1744 CG TRP A 246 27.799 17.615 29.459 1.00151.99 C ANISOU 1744 CG TRP A 246 18929 19884 18938 960 -4743 1927 C ATOM 1745 CD1 TRP A 246 27.843 18.874 29.981 1.00157.26 C ANISOU 1745 CD1 TRP A 246 19803 20556 19392 1226 -4924 2175 C ATOM 1746 CD2 TRP A 246 26.489 17.109 29.741 1.00154.21 C ANISOU 1746 CD2 TRP A 246 19368 20613 18611 1199 -5194 2481 C ATOM 1747 NE1 TRP A 246 26.639 19.185 30.568 1.00158.12 N ANISOU 1747 NE1 TRP A 246 20195 21087 18798 1622 -5454 2854 N ATOM 1748 CE2 TRP A 246 25.791 18.118 30.435 1.00156.70 C ANISOU 1748 CE2 TRP A 246 19986 21190 18361 1616 -5636 3059 C ATOM 1749 CE3 TRP A 246 25.837 15.901 29.473 1.00154.99 C ANISOU 1749 CE3 TRP A 246 19382 20913 18593 1096 -5259 2541 C ATOM 1750 CZ2 TRP A 246 24.475 17.955 30.863 1.00158.62 C ANISOU 1750 CZ2 TRP A 246 20437 21639 18191 1677 -5611 3366 C ATOM 1751 CZ3 TRP A 246 24.531 15.742 29.899 1.00153.31 C ANISOU 1751 CZ3 TRP A 246 19381 21160 17711 1407 -5765 3172 C ATOM 1752 CH2 TRP A 246 23.864 16.763 30.587 1.00156.57 C ANISOU 1752 CH2 TRP A 246 20083 21538 17869 1546 -5609 3386 C ATOM 1753 N LEU A 247 31.849 15.462 28.479 1.00132.93 N ANISOU 1753 N LEU A 247 15055 15948 19504 28 -3372 -292 N ATOM 1754 CA LEU A 247 32.708 14.517 27.770 1.00132.69 C ANISOU 1754 CA LEU A 247 14702 15575 20139 -387 -2839 -910 C ATOM 1755 C LEU A 247 32.928 13.226 28.558 1.00134.78 C ANISOU 1755 C LEU A 247 14386 15669 21157 -124 -3139 -1023 C ATOM 1756 O LEU A 247 32.721 12.139 28.025 1.00135.27 O ANISOU 1756 O LEU A 247 14355 15736 21306 -367 -2926 -1190 O ATOM 1757 CB LEU A 247 34.051 15.151 27.393 1.00129.35 C ANISOU 1757 CB LEU A 247 14149 14721 20279 -655 -2340 -1447 C ATOM 1758 CG LEU A 247 34.059 16.061 26.164 1.00125.22 C ANISOU 1758 CG LEU A 247 14141 14270 19166 -1128 -1768 -1548 C ATOM 1759 CD1 LEU A 247 35.470 16.546 25.872 1.00124.44 C ANISOU 1759 CD1 LEU A 247 13833 13701 19749 -1373 -1288 -2116 C ATOM 1760 CD2 LEU A 247 33.480 15.336 24.960 1.00125.60 C ANISOU 1760 CD2 LEU A 247 14444 14527 18753 -1596 -1356 -1633 C ATOM 1761 N PRO A 248 33.344 13.341 29.831 1.00130.41 N ANISOU 1761 N PRO A 248 13436 14969 21145 371 -3627 -929 N ATOM 1762 CA PRO A 248 33.573 12.143 30.646 1.00129.49 C ANISOU 1762 CA PRO A 248 12740 14696 21766 660 -3929 -1003 C ATOM 1763 C PRO A 248 32.386 11.189 30.599 1.00125.60 C ANISOU 1763 C PRO A 248 12355 14538 20830 729 -4175 -653 C ATOM 1764 O PRO A 248 32.570 9.985 30.428 1.00127.46 O ANISOU 1764 O PRO A 248 12264 14614 21549 607 -4014 -909 O ATOM 1765 CB PRO A 248 33.725 12.709 32.059 1.00124.35 C ANISOU 1765 CB PRO A 248 11844 14047 21357 1247 -4557 -717 C ATOM 1766 CG PRO A 248 34.240 14.080 31.852 1.00123.26 C ANISOU 1766 CG PRO A 248 11969 13819 21044 1131 -4353 -816 C ATOM 1767 CD PRO A 248 33.592 14.577 30.594 1.00123.93 C ANISOU 1767 CD PRO A 248 12685 14138 20266 692 -3929 -735 C ATOM 1768 N LEU A 249 31.181 11.730 30.745 1.00122.20 N ANISOU 1768 N LEU A 249 12377 14563 19490 920 -4550 -70 N ATOM 1769 CA LEU A 249 29.971 10.917 30.716 1.00115.71 C ANISOU 1769 CA LEU A 249 11694 14103 18166 995 -4816 312 C ATOM 1770 C LEU A 249 29.750 10.265 29.350 1.00112.69 C ANISOU 1770 C LEU A 249 11533 13768 17514 398 -4228 30 C ATOM 1771 O LEU A 249 29.326 9.113 29.272 1.00106.70 O ANISOU 1771 O LEU A 249 10616 13067 16859 353 -4260 23 O ATOM 1772 CB LEU A 249 28.753 11.751 31.123 1.00109.57 C ANISOU 1772 CB LEU A 249 11380 13812 16440 1315 -5317 1007 C ATOM 1773 CG LEU A 249 27.421 11.009 31.253 1.00 98.50 C ANISOU 1773 CG LEU A 249 10124 12829 14474 1468 -5690 1488 C ATOM 1774 CD1 LEU A 249 27.568 9.770 32.124 1.00107.79 C ANISOU 1774 CD1 LEU A 249 10727 13843 16385 1786 -6023 1441 C ATOM 1775 CD2 LEU A 249 26.345 11.931 31.803 1.00 74.21 C ANISOU 1775 CD2 LEU A 249 7455 10191 10548 1848 -6214 2179 C ATOM 1776 N HIS A 250 30.037 10.999 28.278 1.00119.14 N ANISOU 1776 N HIS A 250 12714 14566 17990 -62 -3684 -207 N ATOM 1777 CA HIS A 250 29.911 10.455 26.929 1.00124.01 C ANISOU 1777 CA HIS A 250 13545 15226 18348 -664 -3082 -516 C ATOM 1778 C HIS A 250 31.050 9.488 26.631 1.00126.88 C ANISOU 1778 C HIS A 250 13423 15093 19691 -934 -2624 -1187 C ATOM 1779 O HIS A 250 30.841 8.437 26.029 1.00132.04 O ANISOU 1779 O HIS A 250 14017 15745 20407 -1233 -2355 -1394 O ATOM 1780 CB HIS A 250 29.885 11.573 25.885 1.00136.97 C ANISOU 1780 CB HIS A 250 15716 17009 19318 -1059 -2637 -547 C ATOM 1781 CG HIS A 250 28.634 12.398 25.909 1.00144.19 C ANISOU 1781 CG HIS A 250 17165 18457 19162 -895 -2976 112 C ATOM 1782 ND1 HIS A 250 27.483 12.022 25.248 1.00147.27 N ANISOU 1782 ND1 HIS A 250 17913 19299 18744 -1105 -2959 405 N ATOM 1783 CD2 HIS A 250 28.358 13.581 26.504 1.00143.34 C ANISOU 1783 CD2 HIS A 250 17295 18506 18662 -546 -3324 537 C ATOM 1784 CE1 HIS A 250 26.551 12.938 25.441 1.00143.79 C ANISOU 1784 CE1 HIS A 250 17898 19275 17460 -879 -3288 999 C ATOM 1785 NE2 HIS A 250 27.054 13.894 26.200 1.00141.82 N ANISOU 1785 NE2 HIS A 250 17591 18847 17447 -536 -3508 1090 N ATOM 1786 N ILE A 251 32.254 9.856 27.057 1.00125.02 N ANISOU 1786 N ILE A 251 12842 14439 20221 -829 -2529 -1522 N ATOM 1787 CA ILE A 251 33.426 9.005 26.897 1.00126.48 C ANISOU 1787 CA ILE A 251 12521 14127 21410 -1026 -2121 -2138 C ATOM 1788 C ILE A 251 33.160 7.621 27.475 1.00125.20 C ANISOU 1788 C ILE A 251 11942 13917 21711 -802 -2387 -2097 C ATOM 1789 O ILE A 251 33.551 6.608 26.896 1.00127.52 O ANISOU 1789 O ILE A 251 12017 13971 22465 -1124 -1955 -2520 O ATOM 1790 CB ILE A 251 34.661 9.618 27.580 1.00125.33 C ANISOU 1790 CB ILE A 251 12005 13592 22025 -808 -2153 -2386 C ATOM 1791 CG1 ILE A 251 35.125 10.860 26.817 1.00129.80 C ANISOU 1791 CG1 ILE A 251 12940 14108 22270 -1135 -1729 -2565 C ATOM 1792 CG2 ILE A 251 35.786 8.602 27.665 1.00125.44 C ANISOU 1792 CG2 ILE A 251 11410 13118 23133 -890 -1857 -2929 C ATOM 1793 CD1 ILE A 251 36.342 11.531 27.416 1.00133.38 C ANISOU 1793 CD1 ILE A 251 13060 14188 23432 -968 -1726 -2827 C ATOM 1794 N ILE A 252 32.486 7.591 28.620 1.00122.62 N ANISOU 1794 N ILE A 252 11514 13817 21261 -247 -3090 -1581 N ATOM 1795 CA ILE A 252 32.098 6.337 29.253 1.00118.15 C ANISOU 1795 CA ILE A 252 10580 13255 21058 22 -3409 -1451 C ATOM 1796 C ILE A 252 31.208 5.503 28.333 1.00117.74 C ANISOU 1796 C ILE A 252 10803 13436 20495 -358 -3158 -1440 C ATOM 1797 O ILE A 252 31.416 4.300 28.177 1.00124.89 O ANISOU 1797 O ILE A 252 11388 14128 21934 -490 -2944 -1725 O ATOM 1798 CB ILE A 252 31.366 6.586 30.587 1.00111.67 C ANISOU 1798 CB ILE A 252 9694 12716 20022 680 -4230 -826 C ATOM 1799 CG1 ILE A 252 32.361 7.026 31.662 1.00112.45 C ANISOU 1799 CG1 ILE A 252 9340 12523 20862 1089 -4502 -908 C ATOM 1800 CG2 ILE A 252 30.622 5.339 31.031 1.00105.94 C ANISOU 1800 CG2 ILE A 252 8747 12117 19389 897 -4547 -593 C ATOM 1801 CD1 ILE A 252 31.751 7.169 33.040 1.00111.44 C ANISOU 1801 CD1 ILE A 252 9073 12637 20631 1749 -5301 -340 C ATOM 1802 N ASN A 253 30.223 6.152 27.722 1.00115.52 N ANISOU 1802 N ASN A 253 11114 13597 19181 -538 -3173 -1109 N ATOM 1803 CA ASN A 253 29.294 5.472 26.826 1.00123.32 C ANISOU 1803 CA ASN A 253 12410 14880 19567 -914 -2958 -1060 C ATOM 1804 C ASN A 253 29.945 5.031 25.519 1.00130.50 C ANISOU 1804 C ASN A 253 13355 15538 20692 -1578 -2154 -1696 C ATOM 1805 O ASN A 253 29.493 4.080 24.884 1.00133.12 O ANISOU 1805 O ASN A 253 13734 15953 20893 -1898 -1911 -1830 O ATOM 1806 CB ASN A 253 28.078 6.356 26.540 1.00126.49 C ANISOU 1806 CB ASN A 253 13427 15850 18782 -915 -3198 -505 C ATOM 1807 CG ASN A 253 27.268 6.653 27.786 1.00126.31 C ANISOU 1807 CG ASN A 253 13397 16117 18478 -273 -3995 155 C ATOM 1808 OD1 ASN A 253 27.505 6.075 28.847 1.00130.45 O ANISOU 1808 OD1 ASN A 253 13456 16455 19652 164 -4388 216 O ATOM 1809 ND2 ASN A 253 26.304 7.559 27.662 1.00120.60 N ANISOU 1809 ND2 ASN A 253 13186 15858 16779 -207 -4230 664 N ATOM 1810 N CYS A 254 31.005 5.726 25.120 1.00137.30 N ANISOU 1810 N CYS A 254 14194 16093 21881 -1791 -1738 -2091 N ATOM 1811 CA CYS A 254 31.742 5.363 23.916 1.00145.22 C ANISOU 1811 CA CYS A 254 15204 16820 23155 -2405 -959 -2720 C ATOM 1812 C CYS A 254 32.518 4.069 24.132 1.00146.80 C ANISOU 1812 C CYS A 254 14825 16557 24394 -2419 -752 -3171 C ATOM 1813 O CYS A 254 32.667 3.262 23.214 1.00147.63 O ANISOU 1813 O CYS A 254 14928 16533 24632 -2893 -214 -3585 O ATOM 1814 CB CYS A 254 32.693 6.488 23.504 1.00146.96 C ANISOU 1814 CB CYS A 254 15535 16824 23478 -2591 -594 -3001 C ATOM 1815 SG CYS A 254 31.862 7.996 22.962 1.00162.90 S ANISOU 1815 SG CYS A 254 18274 19349 24272 -2696 -651 -2553 S ATOM 1816 N PHE A 255 33.012 3.879 25.352 1.00143.93 N ANISOU 1816 N PHE A 255 13969 15951 24766 -1897 -1173 -3083 N ATOM 1817 CA PHE A 255 33.720 2.657 25.716 1.00143.26 C ANISOU 1817 CA PHE A 255 13291 15439 25700 -1822 -1043 -3433 C ATOM 1818 C PHE A 255 32.761 1.472 25.767 1.00142.90 C ANISOU 1818 C PHE A 255 13217 15583 25494 -1797 -1208 -3243 C ATOM 1819 O PHE A 255 33.049 0.402 25.230 1.00146.73 O ANISOU 1819 O PHE A 255 13503 15816 26429 -2111 -764 -3650 O ATOM 1820 CB PHE A 255 34.416 2.825 27.070 1.00138.56 C ANISOU 1820 CB PHE A 255 12180 14604 25861 -1233 -1508 -3316 C ATOM 1821 CG PHE A 255 35.774 3.467 26.985 1.00143.48 C ANISOU 1821 CG PHE A 255 12588 14829 27099 -1332 -1167 -3744 C ATOM 1822 CD1 PHE A 255 35.971 4.617 26.237 1.00146.46 C ANISOU 1822 CD1 PHE A 255 13390 15280 26977 -1646 -865 -3850 C ATOM 1823 CD2 PHE A 255 36.852 2.927 27.669 1.00144.93 C ANISOU 1823 CD2 PHE A 255 12132 14573 28362 -1100 -1152 -4023 C ATOM 1824 CE1 PHE A 255 37.220 5.208 26.162 1.00147.69 C ANISOU 1824 CE1 PHE A 255 13344 15067 27705 -1742 -549 -4244 C ATOM 1825 CE2 PHE A 255 38.102 3.514 27.600 1.00145.85 C ANISOU 1825 CE2 PHE A 255 12037 14335 29043 -1195 -846 -4411 C ATOM 1826 CZ PHE A 255 38.286 4.655 26.846 1.00146.70 C ANISOU 1826 CZ PHE A 255 12580 14511 28650 -1520 -545 -4528 C ATOM 1827 N THR A 256 31.618 1.673 26.415 1.00136.70 N ANISOU 1827 N THR A 256 12634 15238 24069 -1426 -1839 -2625 N ATOM 1828 CA THR A 256 30.623 0.618 26.570 1.00134.06 C ANISOU 1828 CA THR A 256 12280 15122 23535 -1352 -2073 -2376 C ATOM 1829 C THR A 256 30.082 0.144 25.222 1.00136.92 C ANISOU 1829 C THR A 256 13026 15657 23341 -1992 -1544 -2610 C ATOM 1830 O THR A 256 29.950 -1.056 24.984 1.00145.85 O ANISOU 1830 O THR A 256 13968 16663 24784 -2167 -1335 -2821 O ATOM 1831 CB THR A 256 29.450 1.076 27.461 1.00125.15 C ANISOU 1831 CB THR A 256 11358 14478 21717 -848 -2850 -1635 C ATOM 1832 OG1 THR A 256 29.939 1.407 28.767 1.00116.66 O ANISOU 1832 OG1 THR A 256 9889 13245 21191 -245 -3357 -1428 O ATOM 1833 CG2 THR A 256 28.406 -0.024 27.579 1.00125.64 C ANISOU 1833 CG2 THR A 256 11407 14771 21559 -794 -3075 -1381 C ATOM 1834 N PHE A 257 29.777 1.092 24.343 1.00130.95 N ANISOU 1834 N PHE A 257 12802 15189 21763 -2342 -1318 -2574 N ATOM 1835 CA PHE A 257 29.199 0.781 23.040 1.00130.46 C ANISOU 1835 CA PHE A 257 13149 15370 21050 -2958 -842 -2753 C ATOM 1836 C PHE A 257 30.225 0.214 22.064 1.00142.13 C ANISOU 1836 C PHE A 257 14467 16407 23128 -3506 -45 -3498 C ATOM 1837 O PHE A 257 30.156 -0.955 21.689 1.00147.39 O ANISOU 1837 O PHE A 257 14978 16939 24086 -3763 244 -3785 O ATOM 1838 CB PHE A 257 28.550 2.030 22.438 1.00124.12 C ANISOU 1838 CB PHE A 257 12956 15040 19163 -3131 -864 -2438 C ATOM 1839 CG PHE A 257 27.933 1.804 21.085 1.00115.55 C ANISOU 1839 CG PHE A 257 12304 14264 17334 -3767 -389 -2591 C ATOM 1840 CD1 PHE A 257 26.595 1.471 20.966 1.00105.40 C ANISOU 1840 CD1 PHE A 257 11309 13494 15243 -3794 -673 -2168 C ATOM 1841 CD2 PHE A 257 28.689 1.933 19.931 1.00118.70 C ANISOU 1841 CD2 PHE A 257 12817 14458 17827 -4342 341 -3154 C ATOM 1842 CE1 PHE A 257 26.023 1.267 19.723 1.00106.52 C ANISOU 1842 CE1 PHE A 257 11840 13953 14678 -4392 -243 -2308 C ATOM 1843 CE2 PHE A 257 28.123 1.729 18.686 1.00117.95 C ANISOU 1843 CE2 PHE A 257 13115 14673 17028 -4935 777 -3298 C ATOM 1844 CZ PHE A 257 26.789 1.395 18.582 1.00112.25 C ANISOU 1844 CZ PHE A 257 12672 14478 15498 -4964 482 -2877 C ATOM 1845 N PHE A 258 31.170 1.051 21.649 1.00150.16 N ANISOU 1845 N PHE A 258 15530 17195 24327 -3688 321 -3809 N ATOM 1846 CA PHE A 258 32.159 0.658 20.648 1.00159.58 C ANISOU 1846 CA PHE A 258 16620 17990 26022 -4230 1106 -4509 C ATOM 1847 C PHE A 258 32.988 -0.546 21.086 1.00159.06 C ANISOU 1847 C PHE A 258 15943 17388 27106 -4127 1272 -4905 C ATOM 1848 O PHE A 258 33.503 -1.292 20.251 1.00162.10 O ANISOU 1848 O PHE A 258 16234 17486 27869 -4591 1902 -5449 O ATOM 1849 CB PHE A 258 33.078 1.832 20.301 1.00163.80 C ANISOU 1849 CB PHE A 258 17264 18353 26620 -4356 1398 -4728 C ATOM 1850 CG PHE A 258 32.393 2.937 19.551 1.00164.08 C ANISOU 1850 CG PHE A 258 17921 18862 25559 -4606 1450 -4465 C ATOM 1851 CD1 PHE A 258 31.948 4.069 20.212 1.00166.10 C ANISOU 1851 CD1 PHE A 258 18393 19408 25308 -4200 918 -3923 C ATOM 1852 CD2 PHE A 258 32.193 2.841 18.184 1.00166.57 C ANISOU 1852 CD2 PHE A 258 18601 19337 25350 -5247 2041 -4755 C ATOM 1853 CE1 PHE A 258 31.318 5.086 19.526 1.00171.22 C ANISOU 1853 CE1 PHE A 258 19606 20487 24962 -4415 983 -3659 C ATOM 1854 CE2 PHE A 258 31.562 3.854 17.490 1.00170.34 C ANISOU 1854 CE2 PHE A 258 19635 20269 24816 -5469 2096 -4490 C ATOM 1855 CZ PHE A 258 31.124 4.979 18.162 1.00173.96 C ANISOU 1855 CZ PHE A 258 20301 21004 24792 -5046 1571 -3934 C ATOM 1856 N CYS A 259 33.116 -0.731 22.395 1.00183.67 N ANISOU 1856 N CYS A 259 19266 11606 38913 -2953 401 790 N ATOM 1857 CA CYS A 259 33.891 -1.843 22.927 1.00182.90 C ANISOU 1857 CA CYS A 259 18875 12020 38599 -2819 409 602 C ATOM 1858 C CYS A 259 33.096 -2.635 23.962 1.00181.67 C ANISOU 1858 C CYS A 259 18374 12113 38540 -2424 234 807 C ATOM 1859 O CYS A 259 33.209 -2.385 25.163 1.00183.87 O ANISOU 1859 O CYS A 259 18313 12692 38858 -2256 365 579 O ATOM 1860 CB CYS A 259 35.201 -1.339 23.538 1.00179.67 C ANISOU 1860 CB CYS A 259 18273 11964 38029 -2954 732 43 C ATOM 1861 SG CYS A 259 36.336 -2.651 24.049 1.00389.77 S ANISOU 1861 SG CYS A 259 44561 39192 64342 -2847 769 -234 S ATOM 1862 N PRO A 260 32.283 -3.594 23.493 1.00174.25 N ANISOU 1862 N PRO A 260 17522 11047 37641 -2273 -64 1244 N ATOM 1863 CA PRO A 260 31.481 -4.442 24.381 1.00176.00 C ANISOU 1863 CA PRO A 260 17434 11486 37950 -1898 -259 1482 C ATOM 1864 C PRO A 260 32.371 -5.242 25.322 1.00178.56 C ANISOU 1864 C PRO A 260 17367 12397 38079 -1750 -166 1168 C ATOM 1865 O PRO A 260 31.936 -5.622 26.409 1.00178.90 O ANISOU 1865 O PRO A 260 17069 12710 38195 -1450 -221 1209 O ATOM 1866 CB PRO A 260 30.761 -5.382 23.410 1.00175.65 C ANISOU 1866 CB PRO A 260 17624 11195 37920 -1853 -574 1955 C ATOM 1867 CG PRO A 260 30.757 -4.658 22.107 1.00173.67 C ANISOU 1867 CG PRO A 260 17829 10464 37693 -2176 -556 2043 C ATOM 1868 CD PRO A 260 32.050 -3.907 22.074 1.00171.12 C ANISOU 1868 CD PRO A 260 17529 10277 37213 -2453 -239 1546 C ATOM 1869 N ASP A 261 33.606 -5.494 24.902 1.00179.09 N ANISOU 1869 N ASP A 261 17484 12660 37901 -1958 -27 858 N ATOM 1870 CA ASP A 261 34.565 -6.207 25.737 1.00178.07 C ANISOU 1870 CA ASP A 261 17001 13087 37570 -1849 81 525 C ATOM 1871 C ASP A 261 35.035 -5.333 26.894 1.00177.38 C ANISOU 1871 C ASP A 261 16628 13254 37512 -1819 357 116 C ATOM 1872 O ASP A 261 35.178 -5.805 28.023 1.00177.66 O ANISOU 1872 O ASP A 261 16279 13708 37514 -1578 385 -23 O ATOM 1873 CB ASP A 261 35.762 -6.676 24.908 1.00177.38 C ANISOU 1873 CB ASP A 261 17065 13118 37212 -2095 156 306 C ATOM 1874 CG ASP A 261 35.416 -7.829 23.984 1.00174.38 C ANISOU 1874 CG ASP A 261 16870 12623 36765 -2062 -129 674 C ATOM 1875 OD1 ASP A 261 34.294 -8.368 24.095 1.00171.36 O ANISOU 1875 OD1 ASP A 261 16455 12123 36533 -1823 -385 1084 O ATOM 1876 OD2 ASP A 261 36.269 -8.199 23.149 1.00172.12 O ANISOU 1876 OD2 ASP A 261 16759 12364 36273 -2274 -96 552 O ATOM 1877 N CYS A 262 35.270 -4.057 26.605 1.00175.08 N ANISOU 1877 N CYS A 262 16530 12708 37286 -2065 559 -73 N ATOM 1878 CA CYS A 262 35.731 -3.112 27.615 1.00172.43 C ANISOU 1878 CA CYS A 262 15960 12570 36984 -2068 832 -469 C ATOM 1879 C CYS A 262 34.802 -3.112 28.823 1.00166.89 C ANISOU 1879 C CYS A 262 14938 11998 36474 -1726 758 -336 C ATOM 1880 O CYS A 262 33.621 -2.780 28.708 1.00167.12 O ANISOU 1880 O CYS A 262 15080 11687 36730 -1628 605 16 O ATOM 1881 CB CYS A 262 35.832 -1.703 27.025 1.00177.74 C ANISOU 1881 CB CYS A 262 16932 12850 37750 -2368 1007 -590 C ATOM 1882 SG CYS A 262 36.984 -1.557 25.636 1.00147.05 S ANISOU 1882 SG CYS A 262 13421 8813 33639 -2793 1127 -784 S ATOM 1883 N SER A 263 35.346 -3.492 29.977 1.00159.19 N ANISOU 1883 N SER A 263 13562 11519 35404 -1546 866 -619 N ATOM 1884 CA SER A 263 34.573 -3.585 31.211 1.00156.00 C ANISOU 1884 CA SER A 263 12813 11306 35155 -1208 807 -526 C ATOM 1885 C SER A 263 33.584 -2.434 31.352 1.00161.74 C ANISOU 1885 C SER A 263 13642 11657 36154 -1191 816 -373 C ATOM 1886 O SER A 263 33.979 -1.275 31.479 1.00165.79 O ANISOU 1886 O SER A 263 14208 12077 36709 -1366 1049 -660 O ATOM 1887 CB SER A 263 35.503 -3.635 32.427 1.00155.86 C ANISOU 1887 CB SER A 263 12390 11823 35007 -1111 1028 -981 C ATOM 1888 OG SER A 263 36.343 -2.495 32.476 1.00166.61 O ANISOU 1888 OG SER A 263 13807 13167 36331 -1358 1326 -1397 O ATOM 1889 N HIS A 264 32.296 -2.761 31.320 1.00160.66 N ANISOU 1889 N HIS A 264 13537 11304 36205 -981 560 83 N ATOM 1890 CA HIS A 264 31.250 -1.756 31.454 1.00164.43 C ANISOU 1890 CA HIS A 264 14106 11419 36951 -938 539 272 C ATOM 1891 C HIS A 264 31.487 -0.919 32.706 1.00164.69 C ANISOU 1891 C HIS A 264 13831 11695 37049 -847 774 -80 C ATOM 1892 O HIS A 264 31.689 -1.459 33.795 1.00161.90 O ANISOU 1892 O HIS A 264 13094 11784 36638 -612 802 -224 O ATOM 1893 CB HIS A 264 29.867 -2.412 31.506 1.00166.22 C ANISOU 1893 CB HIS A 264 14311 11493 37353 -660 227 789 C ATOM 1894 CG HIS A 264 29.572 -3.299 30.336 1.00166.05 C ANISOU 1894 CG HIS A 264 14571 11246 37275 -721 -21 1153 C ATOM 1895 ND1 HIS A 264 29.256 -2.807 29.088 1.00170.71 N ANISOU 1895 ND1 HIS A 264 15594 11337 37932 -962 -85 1360 N ATOM 1896 CD2 HIS A 264 29.534 -4.649 30.228 1.00162.59 C ANISOU 1896 CD2 HIS A 264 14043 11013 36721 -569 -225 1351 C ATOM 1897 CE1 HIS A 264 29.043 -3.814 28.259 1.00133.78 C ANISOU 1897 CE1 HIS A 264 11081 6568 33181 -957 -315 1666 C ATOM 1898 NE2 HIS A 264 29.205 -4.943 28.927 1.00132.10 N ANISOU 1898 NE2 HIS A 264 10558 6776 32858 -720 -405 1666 N ATOM 1899 N ALA A 265 31.468 0.400 32.542 1.00168.78 N ANISOU 1899 N ALA A 265 14519 11922 37687 -1035 939 -219 N ATOM 1900 CA ALA A 265 31.747 1.320 33.639 1.00169.28 C ANISOU 1900 CA ALA A 265 14327 12178 37814 -986 1179 -577 C ATOM 1901 C ALA A 265 30.933 0.994 34.888 1.00159.61 C ANISOU 1901 C ALA A 265 12728 11196 36722 -606 1085 -450 C ATOM 1902 O ALA A 265 29.715 0.826 34.816 1.00150.38 O ANISOU 1902 O ALA A 265 11610 9790 35739 -431 861 -32 O ATOM 1903 CB ALA A 265 31.494 2.754 33.200 1.00173.53 C ANISOU 1903 CB ALA A 265 15138 12277 38518 -1206 1301 -619 C ATOM 1904 N PRO A 266 31.613 0.901 36.042 1.00157.98 N ANISOU 1904 N PRO A 266 12140 11469 36418 -478 1256 -813 N ATOM 1905 CA PRO A 266 30.975 0.622 37.333 1.00161.29 C ANISOU 1905 CA PRO A 266 12168 12173 36942 -121 1200 -752 C ATOM 1906 C PRO A 266 29.928 1.676 37.678 1.00180.46 C ANISOU 1906 C PRO A 266 14625 14293 39647 -39 1195 -607 C ATOM 1907 O PRO A 266 29.837 2.696 36.996 1.00189.81 O ANISOU 1907 O PRO A 266 16113 15078 40929 -272 1272 -619 O ATOM 1908 CB PRO A 266 32.141 0.695 38.330 1.00152.21 C ANISOU 1908 CB PRO A 266 10682 11526 35625 -108 1461 -1269 C ATOM 1909 CG PRO A 266 33.255 1.379 37.599 1.00149.48 C ANISOU 1909 CG PRO A 266 10578 11073 35145 -477 1684 -1611 C ATOM 1910 CD PRO A 266 33.074 1.026 36.164 1.00152.74 C ANISOU 1910 CD PRO A 266 11397 11113 35526 -672 1516 -1309 C ATOM 1911 N LEU A 267 29.150 1.429 38.727 1.00189.53 N ANISOU 1911 N LEU A 267 15462 15631 40920 290 1106 -473 N ATOM 1912 CA LEU A 267 28.103 2.361 39.134 1.00200.17 C ANISOU 1912 CA LEU A 267 16808 16714 42533 401 1089 -324 C ATOM 1913 C LEU A 267 28.671 3.542 39.917 1.00215.96 C ANISOU 1913 C LEU A 267 18660 18833 44564 330 1386 -773 C ATOM 1914 O LEU A 267 28.220 4.678 39.760 1.00217.61 O ANISOU 1914 O LEU A 267 19035 18695 44952 232 1451 -762 O ATOM 1915 CB LEU A 267 27.031 1.642 39.955 1.00196.11 C ANISOU 1915 CB LEU A 267 16014 16357 42142 784 876 -1 C ATOM 1916 CG LEU A 267 26.305 0.499 39.241 1.00196.42 C ANISOU 1916 CG LEU A 267 16189 16257 42184 885 560 484 C ATOM 1917 CD1 LEU A 267 25.303 -0.170 40.170 1.00199.57 C ANISOU 1917 CD1 LEU A 267 16277 16850 42702 1269 371 767 C ATOM 1918 CD2 LEU A 267 25.620 1.002 37.978 1.00191.69 C ANISOU 1918 CD2 LEU A 267 16043 15065 41724 690 435 807 C ATOM 1919 N TRP A 268 29.664 3.271 40.758 1.00132.33 N ANISOU 1919 N TRP A 268 17205 20387 12687 1801 -3238 -338 N ATOM 1920 CA TRP A 268 30.290 4.315 41.560 1.00143.68 C ANISOU 1920 CA TRP A 268 18677 21941 13972 1743 -3434 -361 C ATOM 1921 C TRP A 268 31.035 5.305 40.670 1.00144.38 C ANISOU 1921 C TRP A 268 18729 21965 14165 1654 -3448 -374 C ATOM 1922 O TRP A 268 31.291 6.440 41.066 1.00148.56 O ANISOU 1922 O TRP A 268 19302 22520 14623 1591 -3578 -413 O ATOM 1923 CB TRP A 268 31.247 3.702 42.581 1.00154.56 C ANISOU 1923 CB TRP A 268 20044 23553 15130 1755 -3611 -299 C ATOM 1924 CG TRP A 268 32.413 3.011 41.953 1.00164.74 C ANISOU 1924 CG TRP A 268 21237 24918 16438 1747 -3613 -224 C ATOM 1925 CD1 TRP A 268 32.492 1.698 41.592 1.00169.78 C ANISOU 1925 CD1 TRP A 268 21832 25567 17109 1817 -3518 -166 C ATOM 1926 CD2 TRP A 268 33.669 3.601 41.603 1.00168.86 C ANISOU 1926 CD2 TRP A 268 21695 25522 16940 1666 -3718 -197 C ATOM 1927 NE1 TRP A 268 33.723 1.433 41.041 1.00173.60 N ANISOU 1927 NE1 TRP A 268 22229 26140 17593 1796 -3556 -105 N ATOM 1928 CE2 TRP A 268 34.464 2.586 41.036 1.00173.88 C ANISOU 1928 CE2 TRP A 268 22243 26226 17597 1701 -3677 -120 C ATOM 1929 CE3 TRP A 268 34.200 4.890 41.716 1.00166.71 C ANISOU 1929 CE3 TRP A 268 21435 25278 16629 1566 -3848 -227 C ATOM 1930 CZ2 TRP A 268 35.760 2.819 40.584 1.00175.33 C ANISOU 1930 CZ2 TRP A 268 22339 26517 17763 1641 -3758 -71 C ATOM 1931 CZ3 TRP A 268 35.486 5.119 41.266 1.00168.05 C ANISOU 1931 CZ3 TRP A 268 21519 25548 16785 1494 -3932 -176 C ATOM 1932 CH2 TRP A 268 36.252 4.089 40.707 1.00172.53 C ANISOU 1932 CH2 TRP A 268 21987 26194 17372 1534 -3885 -97 C ATOM 1933 N LEU A 269 31.388 4.861 39.468 1.00139.90 N ANISOU 1933 N LEU A 269 18087 21310 13758 1647 -3318 -342 N ATOM 1934 CA LEU A 269 32.045 5.722 38.493 1.00134.19 C ANISOU 1934 CA LEU A 269 17327 20510 13150 1564 -3308 -349 C ATOM 1935 C LEU A 269 31.011 6.300 37.539 1.00126.53 C ANISOU 1935 C LEU A 269 16387 19294 12393 1566 -3133 -413 C ATOM 1936 O LEU A 269 31.230 7.344 36.922 1.00128.24 O ANISOU 1936 O LEU A 269 16611 19418 12697 1500 -3136 -443 O ATOM 1937 CB LEU A 269 33.098 4.942 37.709 1.00133.86 C ANISOU 1937 CB LEU A 269 17187 20524 13151 1556 -3273 -275 C ATOM 1938 CG LEU A 269 33.874 5.743 36.665 1.00133.60 C ANISOU 1938 CG LEU A 269 17105 20428 13228 1467 -3262 -271 C ATOM 1939 CD1 LEU A 269 34.627 6.889 37.323 1.00136.70 C ANISOU 1939 CD1 LEU A 269 17515 20944 13482 1373 -3474 -278 C ATOM 1940 CD2 LEU A 269 34.826 4.844 35.895 1.00136.22 C ANISOU 1940 CD2 LEU A 269 17338 20824 13597 1477 -3213 -197 C ATOM 1941 N MET A 270 29.881 5.611 37.420 1.00120.56 N ANISOU 1941 N MET A 270 15648 18439 11719 1641 -2984 -429 N ATOM 1942 CA MET A 270 28.803 6.060 36.551 1.00122.83 C ANISOU 1942 CA MET A 270 15958 18506 12206 1653 -2813 -485 C ATOM 1943 C MET A 270 28.127 7.311 37.104 1.00128.12 C ANISOU 1943 C MET A 270 16707 19136 12837 1646 -2882 -557 C ATOM 1944 O MET A 270 27.944 8.295 36.386 1.00129.52 O ANISOU 1944 O MET A 270 16903 19170 13138 1613 -2837 -601 O ATOM 1945 CB MET A 270 27.773 4.948 36.355 1.00124.24 C ANISOU 1945 CB MET A 270 16129 18612 12465 1727 -2652 -476 C ATOM 1946 CG MET A 270 26.678 5.293 35.361 1.00125.59 C ANISOU 1946 CG MET A 270 16307 18561 12852 1739 -2466 -526 C ATOM 1947 SD MET A 270 27.318 5.596 33.701 1.00169.15 S ANISOU 1947 SD MET A 270 21775 23910 18585 1679 -2346 -522 S ATOM 1948 CE MET A 270 28.076 4.015 33.336 1.00105.89 C ANISOU 1948 CE MET A 270 13698 15971 10565 1695 -2299 -443 C ATOM 1949 N TYR A 271 27.760 7.273 38.381 1.00130.59 N ANISOU 1949 N TYR A 271 17073 19575 12971 1683 -2994 -570 N ATOM 1950 CA TYR A 271 27.087 8.404 39.006 1.00134.40 C ANISOU 1950 CA TYR A 271 17641 20034 13392 1688 -3068 -642 C ATOM 1951 C TYR A 271 27.991 9.635 39.005 1.00130.97 C ANISOU 1951 C TYR A 271 17238 19616 12909 1600 -3219 -662 C ATOM 1952 O TYR A 271 27.518 10.760 38.847 1.00132.42 O ANISOU 1952 O TYR A 271 17483 19693 13139 1589 -3227 -725 O ATOM 1953 CB TYR A 271 26.655 8.063 40.436 1.00145.27 C ANISOU 1953 CB TYR A 271 19072 21563 14562 1740 -3175 -646 C ATOM 1954 CG TYR A 271 27.709 8.344 41.482 1.00156.71 C ANISOU 1954 CG TYR A 271 20553 23202 15790 1690 -3404 -629 C ATOM 1955 CD1 TYR A 271 27.924 9.638 41.950 1.00160.79 C ANISOU 1955 CD1 TYR A 271 21146 23732 16216 1638 -3554 -682 C ATOM 1956 CD2 TYR A 271 28.483 7.319 42.009 1.00162.28 C ANISOU 1956 CD2 TYR A 271 21217 24073 16371 1696 -3477 -558 C ATOM 1957 CE1 TYR A 271 28.888 9.901 42.905 1.00165.06 C ANISOU 1957 CE1 TYR A 271 21718 24447 16551 1581 -3771 -665 C ATOM 1958 CE2 TYR A 271 29.445 7.574 42.966 1.00169.31 C ANISOU 1958 CE2 TYR A 271 22130 25144 17056 1649 -3691 -540 C ATOM 1959 CZ TYR A 271 29.644 8.865 43.410 1.00171.04 C ANISOU 1959 CZ TYR A 271 22423 25374 17190 1586 -3838 -593 C ATOM 1960 OH TYR A 271 30.604 9.117 44.364 1.00176.44 O ANISOU 1960 OH TYR A 271 23132 26241 17667 1529 -4059 -573 O ATOM 1961 N LEU A 272 29.291 9.413 39.184 1.00120.71 N ANISOU 1961 N LEU A 272 15896 18457 11512 1536 -3343 -607 N ATOM 1962 CA LEU A 272 30.256 10.504 39.229 1.00108.63 C ANISOU 1962 CA LEU A 272 14388 16971 9918 1434 -3505 -614 C ATOM 1963 C LEU A 272 30.211 11.306 37.937 1.00103.16 C ANISOU 1963 C LEU A 272 13687 16083 9427 1390 -3400 -639 C ATOM 1964 O LEU A 272 30.326 12.533 37.952 1.00111.02 O ANISOU 1964 O LEU A 272 14747 17029 10406 1330 -3494 -682 O ATOM 1965 CB LEU A 272 31.664 9.961 39.472 1.00108.13 C ANISOU 1965 CB LEU A 272 14250 17099 9735 1377 -3632 -535 C ATOM 1966 CG LEU A 272 32.785 10.979 39.692 1.00109.92 C ANISOU 1966 CG LEU A 272 14487 17421 9855 1255 -3832 -528 C ATOM 1967 CD1 LEU A 272 33.907 10.365 40.514 1.00108.09 C ANISOU 1967 CD1 LEU A 272 14201 17440 9427 1225 -4002 -457 C ATOM 1968 CD2 LEU A 272 33.320 11.532 38.374 1.00109.92 C ANISOU 1968 CD2 LEU A 272 14437 17301 10024 1180 -3763 -516 C ATOM 1969 N ALA A 273 30.045 10.607 36.820 1.00 96.07 N ANISOU 1969 N ALA A 273 12719 15070 8715 1419 -3209 -613 N ATOM 1970 CA ALA A 273 29.948 11.257 35.522 1.00 94.79 C ANISOU 1970 CA ALA A 273 12548 14711 8756 1386 -3089 -635 C ATOM 1971 C ALA A 273 28.581 11.911 35.362 1.00101.22 C ANISOU 1971 C ALA A 273 13435 15352 9672 1448 -2990 -711 C ATOM 1972 O ALA A 273 28.436 12.900 34.644 1.00102.45 O ANISOU 1972 O ALA A 273 13625 15359 9942 1419 -2959 -748 O ATOM 1973 CB ALA A 273 30.193 10.254 34.411 1.00 87.63 C ANISOU 1973 CB ALA A 273 11551 13738 8005 1400 -2918 -585 C ATOM 1974 N ILE A 274 27.584 11.351 36.041 1.00104.98 N ANISOU 1974 N ILE A 274 13931 15856 10100 1536 -2946 -730 N ATOM 1975 CA ILE A 274 26.231 11.893 36.017 1.00107.27 C ANISOU 1975 CA ILE A 274 14278 16017 10462 1607 -2860 -798 C ATOM 1976 C ILE A 274 26.142 13.137 36.897 1.00111.65 C ANISOU 1976 C ILE A 274 14936 16613 10872 1593 -3035 -856 C ATOM 1977 O ILE A 274 25.553 14.147 36.505 1.00115.98 O ANISOU 1977 O ILE A 274 15542 17024 11502 1609 -3008 -913 O ATOM 1978 CB ILE A 274 25.203 10.855 36.492 1.00109.22 C ANISOU 1978 CB ILE A 274 14506 16302 10690 1698 -2764 -793 C ATOM 1979 CG1 ILE A 274 25.280 9.594 35.628 1.00115.73 C ANISOU 1979 CG1 ILE A 274 15243 17080 11650 1707 -2599 -736 C ATOM 1980 CG2 ILE A 274 23.801 11.438 36.461 1.00 98.49 C ANISOU 1980 CG2 ILE A 274 13193 14831 9399 1773 -2679 -859 C ATOM 1981 CD1 ILE A 274 24.333 8.496 36.062 1.00117.19 C ANISOU 1981 CD1 ILE A 274 15409 17305 11814 1781 -2511 -721 C ATOM 1982 N VAL A 275 26.726 13.056 38.089 1.00109.51 N ANISOU 1982 N VAL A 275 14697 16531 10382 1566 -3218 -842 N ATOM 1983 CA VAL A 275 26.772 14.191 39.000 1.00107.49 C ANISOU 1983 CA VAL A 275 14551 16327 9962 1539 -3407 -896 C ATOM 1984 C VAL A 275 27.594 15.317 38.388 1.00111.84 C ANISOU 1984 C VAL A 275 15132 16805 10557 1436 -3492 -905 C ATOM 1985 O VAL A 275 27.260 16.493 38.536 1.00119.66 O ANISOU 1985 O VAL A 275 16224 17722 11521 1428 -3567 -968 O ATOM 1986 CB VAL A 275 27.381 13.799 40.359 1.00100.85 C ANISOU 1986 CB VAL A 275 13734 15710 8875 1517 -3592 -871 C ATOM 1987 CG1 VAL A 275 27.567 15.027 41.238 1.00 93.79 C ANISOU 1987 CG1 VAL A 275 12965 14864 7808 1469 -3802 -927 C ATOM 1988 CG2 VAL A 275 26.505 12.769 41.054 1.00 99.01 C ANISOU 1988 CG2 VAL A 275 13489 15549 8582 1619 -3522 -864 C ATOM 1989 N LEU A 276 28.667 14.949 37.693 1.00107.67 N ANISOU 1989 N LEU A 276 14519 16301 10091 1357 -3481 -841 N ATOM 1990 CA LEU A 276 29.524 15.928 37.037 1.00110.71 C ANISOU 1990 CA LEU A 276 14918 16627 10520 1247 -3557 -837 C ATOM 1991 C LEU A 276 28.733 16.763 36.034 1.00118.38 C ANISOU 1991 C LEU A 276 15933 17364 11682 1278 -3429 -889 C ATOM 1992 O LEU A 276 28.941 17.971 35.916 1.00127.20 O ANISOU 1992 O LEU A 276 17131 18414 12785 1217 -3530 -923 O ATOM 1993 CB LEU A 276 30.694 15.234 36.339 1.00106.64 C ANISOU 1993 CB LEU A 276 14285 16176 10057 1176 -3531 -754 C ATOM 1994 CG LEU A 276 31.735 16.158 35.706 1.00106.99 C ANISOU 1994 CG LEU A 276 14328 16197 10126 1046 -3624 -734 C ATOM 1995 CD1 LEU A 276 32.301 17.115 36.744 1.00109.93 C ANISOU 1995 CD1 LEU A 276 14787 16694 10286 953 -3881 -754 C ATOM 1996 CD2 LEU A 276 32.847 15.350 35.056 1.00109.20 C ANISOU 1996 CD2 LEU A 276 14480 16564 10447 992 -3591 -648 C ATOM 1997 N ALA A 277 27.823 16.112 35.317 1.00114.39 N ANISOU 1997 N ALA A 277 15378 16735 11350 1372 -3213 -893 N ATOM 1998 CA ALA A 277 26.990 16.795 34.333 1.00112.14 C ANISOU 1998 CA ALA A 277 15123 16229 11254 1416 -3076 -939 C ATOM 1999 C ALA A 277 25.989 17.729 35.007 1.00116.51 C ANISOU 1999 C ALA A 277 15790 16742 11735 1485 -3140 -1018 C ATOM 2000 O ALA A 277 25.683 18.803 34.489 1.00111.46 O ANISOU 2000 O ALA A 277 15218 15957 11173 1486 -3140 -1062 O ATOM 2001 CB ALA A 277 26.268 15.784 33.457 1.00107.27 C ANISOU 2001 CB ALA A 277 14421 15507 10828 1493 -2836 -920 C ATOM 2002 N HIS A 278 25.481 17.310 36.162 1.00125.49 N ANISOU 2002 N HIS A 278 16952 18011 12718 1546 -3196 -1036 N ATOM 2003 CA HIS A 278 24.516 18.107 36.908 1.00129.79 C ANISOU 2003 CA HIS A 278 17604 18542 13167 1621 -3261 -1112 C ATOM 2004 C HIS A 278 25.181 19.308 37.566 1.00128.93 C ANISOU 2004 C HIS A 278 17619 18478 12892 1539 -3493 -1146 C ATOM 2005 O HIS A 278 24.511 20.262 37.958 1.00134.14 O ANISOU 2005 O HIS A 278 18392 19085 13488 1587 -3559 -1216 O ATOM 2006 CB HIS A 278 23.819 17.257 37.971 1.00132.54 C ANISOU 2006 CB HIS A 278 17943 19030 13387 1705 -3255 -1115 C ATOM 2007 CG HIS A 278 23.001 16.137 37.409 1.00123.80 C ANISOU 2007 CG HIS A 278 16733 17878 12429 1784 -3037 -1087 C ATOM 2008 ND1 HIS A 278 22.792 14.956 38.088 1.00118.61 N ANISOU 2008 ND1 HIS A 278 16024 17356 11686 1821 -3011 -1051 N ATOM 2009 CD2 HIS A 278 22.344 16.016 36.231 1.00116.96 C ANISOU 2009 CD2 HIS A 278 15809 16844 11785 1827 -2841 -1089 C ATOM 2010 CE1 HIS A 278 22.036 14.158 37.355 1.00115.88 C ANISOU 2010 CE1 HIS A 278 15597 16929 11503 1876 -2811 -1031 C ATOM 2011 NE2 HIS A 278 21.753 14.776 36.223 1.00113.05 N ANISOU 2011 NE2 HIS A 278 15231 16388 11334 1880 -2704 -1054 N ATOM 2012 N THR A 279 26.503 19.253 37.687 1.00124.70 N ANISOU 2012 N THR A 279 17062 18044 12277 1413 -3621 -1096 N ATOM 2013 CA THR A 279 27.264 20.331 38.306 1.00127.70 C ANISOU 2013 CA THR A 279 17553 18480 12488 1307 -3855 -1119 C ATOM 2014 C THR A 279 27.410 21.522 37.361 1.00126.67 C ANISOU 2014 C THR A 279 17483 18174 12474 1251 -3862 -1144 C ATOM 2015 O THR A 279 27.526 22.667 37.800 1.00123.54 O ANISOU 2015 O THR A 279 17221 17759 11961 1201 -4029 -1192 O ATOM 2016 CB THR A 279 28.659 19.847 38.745 1.00128.54 C ANISOU 2016 CB THR A 279 17601 18774 12466 1183 -3997 -1049 C ATOM 2017 OG1 THR A 279 28.518 18.801 39.714 1.00134.44 O ANISOU 2017 OG1 THR A 279 18309 19686 13085 1240 -4010 -1028 O ATOM 2018 CG2 THR A 279 29.460 20.987 39.355 1.00128.79 C ANISOU 2018 CG2 THR A 279 17748 18865 12321 1055 -4247 -1071 C ATOM 2019 N ASN A 280 27.394 21.242 36.062 1.00127.32 N ANISOU 2019 N ASN A 280 17474 18122 12781 1260 -3683 -1110 N ATOM 2020 CA ASN A 280 27.568 22.273 35.046 1.00130.02 C ANISOU 2020 CA ASN A 280 17861 18290 13250 1208 -3672 -1122 C ATOM 2021 C ASN A 280 26.578 23.428 35.190 1.00136.08 C ANISOU 2021 C ASN A 280 18771 18926 14006 1284 -3706 -1207 C ATOM 2022 O ASN A 280 26.926 24.587 34.960 1.00146.92 O ANISOU 2022 O ASN A 280 20247 20217 15360 1210 -3820 -1230 O ATOM 2023 CB ASN A 280 27.459 21.660 33.649 1.00131.15 C ANISOU 2023 CB ASN A 280 17888 18299 13645 1238 -3443 -1079 C ATOM 2024 CG ASN A 280 27.873 22.621 32.553 1.00132.96 C ANISOU 2024 CG ASN A 280 18151 18367 14002 1166 -3438 -1074 C ATOM 2025 OD1 ASN A 280 28.333 23.731 32.823 1.00138.15 O ANISOU 2025 OD1 ASN A 280 18915 19019 14556 1079 -3615 -1096 O ATOM 2026 ND2 ASN A 280 27.717 22.197 31.306 1.00128.20 N ANISOU 2026 ND2 ASN A 280 17465 17627 13618 1196 -3239 -1044 N ATOM 2027 N SER A 281 25.346 23.110 35.573 1.00132.16 N ANISOU 2027 N SER A 281 18282 18417 13515 1430 -3611 -1252 N ATOM 2028 CA SER A 281 24.306 24.124 35.711 1.00130.18 C ANISOU 2028 CA SER A 281 18156 18054 13251 1527 -3630 -1333 C ATOM 2029 C SER A 281 24.616 25.104 36.841 1.00128.57 C ANISOU 2029 C SER A 281 18120 17929 12802 1471 -3881 -1385 C ATOM 2030 O SER A 281 24.065 26.204 36.890 1.00127.76 O ANISOU 2030 O SER A 281 18154 17722 12667 1515 -3945 -1451 O ATOM 2031 CB SER A 281 22.947 23.464 35.953 1.00128.15 C ANISOU 2031 CB SER A 281 17854 17804 13034 1693 -3479 -1363 C ATOM 2032 OG SER A 281 22.932 22.780 37.193 1.00131.62 O ANISOU 2032 OG SER A 281 18290 18435 13285 1708 -3556 -1362 O ATOM 2033 N VAL A 282 25.509 24.700 37.739 1.00126.42 N ANISOU 2033 N VAL A 282 17842 17838 12353 1374 -4026 -1354 N ATOM 2034 CA VAL A 282 25.818 25.486 38.930 1.00129.98 C ANISOU 2034 CA VAL A 282 18453 18384 12552 1314 -4269 -1401 C ATOM 2035 C VAL A 282 26.967 26.476 38.719 1.00139.74 C ANISOU 2035 C VAL A 282 19772 19595 13728 1137 -4451 -1388 C ATOM 2036 O VAL A 282 26.975 27.561 39.305 1.00146.70 O ANISOU 2036 O VAL A 282 20830 20455 14453 1096 -4630 -1447 O ATOM 2037 CB VAL A 282 26.140 24.566 40.131 1.00123.38 C ANISOU 2037 CB VAL A 282 17579 17769 11532 1303 -4351 -1377 C ATOM 2038 CG1 VAL A 282 26.638 25.378 41.315 1.00123.96 C ANISOU 2038 CG1 VAL A 282 17819 17940 11339 1215 -4616 -1418 C ATOM 2039 CG2 VAL A 282 24.915 23.749 40.515 1.00120.07 C ANISOU 2039 CG2 VAL A 282 17112 17380 11130 1473 -4203 -1399 C ATOM 2040 N VAL A 283 27.926 26.107 37.877 1.00140.22 N ANISOU 2040 N VAL A 283 19712 19660 13906 1029 -4406 -1311 N ATOM 2041 CA VAL A 283 29.132 26.911 37.692 1.00142.47 C ANISOU 2041 CA VAL A 283 20050 19957 14125 841 -4581 -1284 C ATOM 2042 C VAL A 283 28.869 28.266 37.037 1.00143.04 C ANISOU 2042 C VAL A 283 20261 19830 14257 821 -4617 -1331 C ATOM 2043 O VAL A 283 29.623 29.217 37.244 1.00147.02 O ANISOU 2043 O VAL A 283 20881 20342 14637 671 -4815 -1337 O ATOM 2044 CB VAL A 283 30.192 26.157 36.865 1.00140.65 C ANISOU 2044 CB VAL A 283 19644 19785 14013 742 -4509 -1185 C ATOM 2045 CG1 VAL A 283 30.547 24.841 37.536 1.00140.72 C ANISOU 2045 CG1 VAL A 283 19526 19998 13944 757 -4495 -1135 C ATOM 2046 CG2 VAL A 283 29.693 25.924 35.448 1.00137.41 C ANISOU 2046 CG2 VAL A 283 19144 19189 13876 823 -4267 -1167 C ATOM 2047 N ASN A 284 27.802 28.353 36.250 1.00136.96 N ANISOU 2047 N ASN A 284 19483 18885 13672 966 -4431 -1361 N ATOM 2048 CA ASN A 284 27.491 29.579 35.518 1.00133.72 C ANISOU 2048 CA ASN A 284 19196 18274 13339 967 -4445 -1400 C ATOM 2049 C ASN A 284 27.268 30.802 36.411 1.00131.24 C ANISOU 2049 C ASN A 284 19113 17940 12811 947 -4660 -1482 C ATOM 2050 O ASN A 284 27.936 31.820 36.245 1.00124.30 O ANISOU 2050 O ASN A 284 18354 17005 11867 808 -4816 -1485 O ATOM 2051 CB ASN A 284 26.298 29.366 34.582 1.00129.72 C ANISOU 2051 CB ASN A 284 18627 17599 13062 1146 -4203 -1417 C ATOM 2052 CG ASN A 284 26.575 28.328 33.516 1.00127.22 C ANISOU 2052 CG ASN A 284 18112 17259 12965 1146 -3995 -1340 C ATOM 2053 OD1 ASN A 284 27.725 28.101 33.139 1.00124.16 O ANISOU 2053 OD1 ASN A 284 17653 16928 12593 1004 -4031 -1272 O ATOM 2054 ND2 ASN A 284 25.520 27.691 33.021 1.00130.31 N ANISOU 2054 ND2 ASN A 284 18418 17574 13522 1304 -3778 -1348 N ATOM 2055 N PRO A 285 26.328 30.706 37.364 1.00134.70 N ANISOU 2055 N PRO A 285 19622 18426 13131 1082 -4673 -1548 N ATOM 2056 CA PRO A 285 26.067 31.847 38.248 1.00132.28 C ANISOU 2056 CA PRO A 285 19554 18098 12608 1076 -4876 -1633 C ATOM 2057 C PRO A 285 27.341 32.356 38.915 1.00128.61 C ANISOU 2057 C PRO A 285 19192 17741 11934 857 -5132 -1618 C ATOM 2058 O PRO A 285 27.478 33.557 39.145 1.00136.81 O ANISOU 2058 O PRO A 285 20438 18702 12843 782 -5307 -1668 O ATOM 2059 CB PRO A 285 25.121 31.263 39.300 1.00137.98 C ANISOU 2059 CB PRO A 285 20284 18926 13217 1233 -4844 -1682 C ATOM 2060 CG PRO A 285 24.438 30.140 38.603 1.00141.30 C ANISOU 2060 CG PRO A 285 20496 19334 13860 1368 -4580 -1643 C ATOM 2061 CD PRO A 285 25.460 29.556 37.675 1.00140.52 C ANISOU 2061 CD PRO A 285 20234 19239 13918 1243 -4505 -1549 C ATOM 2062 N PHE A 286 28.262 31.446 39.216 1.00118.82 N ANISOU 2062 N PHE A 286 17811 16680 10658 753 -5157 -1547 N ATOM 2063 CA PHE A 286 29.515 31.811 39.866 1.00116.90 C ANISOU 2063 CA PHE A 286 17635 16568 10215 539 -5401 -1522 C ATOM 2064 C PHE A 286 30.542 32.331 38.867 1.00104.72 C ANISOU 2064 C PHE A 286 16060 14965 8763 360 -5443 -1461 C ATOM 2065 O PHE A 286 31.408 33.132 39.217 1.00 84.12 O ANISOU 2065 O PHE A 286 13572 12397 5993 173 -5665 -1461 O ATOM 2066 CB PHE A 286 30.090 30.619 40.634 1.00124.32 C ANISOU 2066 CB PHE A 286 18432 17740 11065 509 -5421 -1466 C ATOM 2067 CG PHE A 286 29.245 30.180 41.793 1.00130.59 C ANISOU 2067 CG PHE A 286 19279 18620 11720 651 -5426 -1522 C ATOM 2068 CD1 PHE A 286 28.272 29.210 41.629 1.00133.16 C ANISOU 2068 CD1 PHE A 286 19478 18939 12177 841 -5204 -1521 C ATOM 2069 CD2 PHE A 286 29.424 30.738 43.048 1.00132.20 C ANISOU 2069 CD2 PHE A 286 19664 18912 11653 589 -5656 -1574 C ATOM 2070 CE1 PHE A 286 27.493 28.804 42.696 1.00137.71 C ANISOU 2070 CE1 PHE A 286 20102 19604 12620 967 -5210 -1568 C ATOM 2071 CE2 PHE A 286 28.648 30.336 44.118 1.00135.61 C ANISOU 2071 CE2 PHE A 286 20149 19426 11951 722 -5660 -1624 C ATOM 2072 CZ PHE A 286 27.681 29.368 43.942 1.00139.40 C ANISOU 2072 CZ PHE A 286 20495 19906 12565 912 -5436 -1619 C ATOM 2073 N ILE A 287 30.443 31.872 37.624 1.00114.23 N ANISOU 2073 N ILE A 287 17107 16075 10220 412 -5232 -1410 N ATOM 2074 CA ILE A 287 31.371 32.305 36.587 1.00125.81 C ANISOU 2074 CA ILE A 287 18532 17482 11789 256 -5248 -1348 C ATOM 2075 C ILE A 287 31.011 33.704 36.101 1.00130.10 C ANISOU 2075 C ILE A 287 19271 17816 12344 238 -5312 -1403 C ATOM 2076 O ILE A 287 31.837 34.392 35.505 1.00140.51 O ANISOU 2076 O ILE A 287 20626 19090 13671 71 -5402 -1366 O ATOM 2077 CB ILE A 287 31.395 31.335 35.392 1.00132.86 C ANISOU 2077 CB ILE A 287 19202 18335 12944 321 -4998 -1275 C ATOM 2078 CG1 ILE A 287 32.698 31.488 34.605 1.00135.36 C ANISOU 2078 CG1 ILE A 287 19438 18686 13307 125 -5050 -1191 C ATOM 2079 CG2 ILE A 287 30.199 31.566 34.485 1.00134.96 C ANISOU 2079 CG2 ILE A 287 19487 18374 13418 497 -4796 -1315 C ATOM 2080 CD1 ILE A 287 32.773 30.599 33.386 1.00134.97 C ANISOU 2080 CD1 ILE A 287 19190 18587 13506 183 -4810 -1121 C ATOM 2081 N TYR A 288 29.773 34.117 36.357 1.00119.56 N ANISOU 2081 N TYR A 288 18065 16360 11003 411 -5267 -1488 N ATOM 2082 CA TYR A 288 29.333 35.466 36.021 1.00103.52 C ANISOU 2082 CA TYR A 288 16245 14133 8956 417 -5340 -1549 C ATOM 2083 C TYR A 288 29.769 36.447 37.100 1.00 93.39 C ANISOU 2083 C TYR A 288 15201 12899 7383 276 -5627 -1604 C ATOM 2084 O TYR A 288 30.289 37.522 36.802 1.00 91.10 O ANISOU 2084 O TYR A 288 15063 12520 7033 128 -5771 -1610 O ATOM 2085 CB TYR A 288 27.814 35.517 35.849 1.00103.68 C ANISOU 2085 CB TYR A 288 16303 14013 9078 669 -5179 -1617 C ATOM 2086 CG TYR A 288 27.305 34.725 34.668 1.00110.95 C ANISOU 2086 CG TYR A 288 17017 14848 10291 799 -4902 -1569 C ATOM 2087 CD1 TYR A 288 27.761 34.990 33.385 1.00113.56 C ANISOU 2087 CD1 TYR A 288 17291 15053 10805 729 -4825 -1512 C ATOM 2088 CD2 TYR A 288 26.361 33.721 34.834 1.00115.65 C ANISOU 2088 CD2 TYR A 288 17484 15486 10971 987 -4718 -1580 C ATOM 2089 CE1 TYR A 288 27.299 34.272 32.300 1.00115.03 C ANISOU 2089 CE1 TYR A 288 17302 15152 11251 845 -4574 -1469 C ATOM 2090 CE2 TYR A 288 25.893 32.997 33.755 1.00117.62 C ANISOU 2090 CE2 TYR A 288 17558 15652 11480 1094 -4470 -1538 C ATOM 2091 CZ TYR A 288 26.365 33.277 32.490 1.00117.95 C ANISOU 2091 CZ TYR A 288 17552 15564 11701 1024 -4398 -1484 C ATOM 2092 OH TYR A 288 25.902 32.561 31.410 1.00118.27 O ANISOU 2092 OH TYR A 288 17430 15513 11994 1128 -4152 -1443 O ATOM 2093 N ALA A 289 29.555 36.066 38.354 1.00 90.51 N ANISOU 2093 N ALA A 289 14878 12678 6835 320 -5709 -1645 N ATOM 2094 CA ALA A 289 29.939 36.896 39.488 1.00 93.41 C ANISOU 2094 CA ALA A 289 15478 13102 6910 193 -5982 -1701 C ATOM 2095 C ALA A 289 31.449 37.119 39.535 1.00111.29 C ANISOU 2095 C ALA A 289 17731 15483 9071 -90 -6171 -1633 C ATOM 2096 O ALA A 289 31.922 38.103 40.101 1.00121.85 O ANISOU 2096 O ALA A 289 19285 16815 10197 -249 -6408 -1670 O ATOM 2097 CB ALA A 289 29.452 36.273 40.788 1.00 85.59 C ANISOU 2097 CB ALA A 289 14505 12259 5757 301 -6013 -1745 C ATOM 2098 N TYR A 290 32.204 36.205 38.938 1.00121.86 N ANISOU 2098 N TYR A 290 18820 16930 10551 -154 -6070 -1534 N ATOM 2099 CA TYR A 290 33.659 36.307 38.947 1.00132.33 C ANISOU 2099 CA TYR A 290 20097 18397 11787 -416 -6239 -1460 C ATOM 2100 C TYR A 290 34.198 37.038 37.719 1.00123.11 C ANISOU 2100 C TYR A 290 18933 17097 10744 -547 -6233 -1416 C ATOM 2101 O TYR A 290 35.006 37.959 37.841 1.00122.80 O ANISOU 2101 O TYR A 290 19031 17068 10559 -768 -6447 -1411 O ATOM 2102 CB TYR A 290 34.299 34.919 39.057 1.00146.11 C ANISOU 2102 CB TYR A 290 21574 20359 13581 -425 -6159 -1372 C ATOM 2103 CG TYR A 290 35.806 34.937 38.915 1.00158.58 C ANISOU 2103 CG TYR A 290 23063 22099 15093 -681 -6310 -1282 C ATOM 2104 CD1 TYR A 290 36.627 35.108 40.023 1.00164.17 C ANISOU 2104 CD1 TYR A 290 23839 22996 15544 -853 -6563 -1276 C ATOM 2105 CD2 TYR A 290 36.406 34.791 37.671 1.00160.20 C ANISOU 2105 CD2 TYR A 290 23112 22272 15485 -751 -6202 -1201 C ATOM 2106 CE1 TYR A 290 38.005 35.129 39.894 1.00165.28 C ANISOU 2106 CE1 TYR A 290 23882 23301 15616 -1092 -6707 -1189 C ATOM 2107 CE2 TYR A 290 37.781 34.812 37.533 1.00161.80 C ANISOU 2107 CE2 TYR A 290 23221 22638 15619 -983 -6341 -1115 C ATOM 2108 CZ TYR A 290 38.576 34.980 38.647 1.00164.12 C ANISOU 2108 CZ TYR A 290 23572 23129 15656 -1155 -6595 -1108 C ATOM 2109 OH TYR A 290 39.946 35.000 38.512 1.00164.28 O ANISOU 2109 OH TYR A 290 23485 23330 15603 -1390 -6740 -1017 O ATOM 2110 N ARG A 291 33.751 36.621 36.539 1.00117.19 N ANISOU 2110 N ARG A 291 18038 16226 10261 -418 -5989 -1383 N ATOM 2111 CA ARG A 291 34.246 37.183 35.286 1.00121.21 C ANISOU 2111 CA ARG A 291 18528 16614 10913 -525 -5954 -1332 C ATOM 2112 C ARG A 291 33.697 38.577 35.008 1.00131.28 C ANISOU 2112 C ARG A 291 20061 17664 12156 -526 -6032 -1404 C ATOM 2113 O ARG A 291 34.440 39.481 34.627 1.00145.81 O ANISOU 2113 O ARG A 291 22004 19458 13938 -724 -6174 -1382 O ATOM 2114 CB ARG A 291 33.921 36.252 34.117 1.00122.40 C ANISOU 2114 CB ARG A 291 18449 16701 11355 -380 -5665 -1275 C ATOM 2115 CG ARG A 291 34.746 34.978 34.097 1.00129.98 C ANISOU 2115 CG ARG A 291 19156 17871 12358 -426 -5598 -1185 C ATOM 2116 CD ARG A 291 36.205 35.282 33.802 1.00132.34 C ANISOU 2116 CD ARG A 291 19405 18290 12590 -688 -5751 -1103 C ATOM 2117 NE ARG A 291 36.375 35.864 32.474 1.00129.38 N ANISOU 2117 NE ARG A 291 19029 17748 12382 -737 -5672 -1068 N ATOM 2118 CZ ARG A 291 37.549 36.199 31.949 1.00129.52 C ANISOU 2118 CZ ARG A 291 18998 17835 12378 -954 -5772 -993 C ATOM 2119 NH1 ARG A 291 38.664 36.013 32.642 1.00132.75 N ANISOU 2119 NH1 ARG A 291 19347 18484 12606 -1145 -5959 -944 N ATOM 2120 NH2 ARG A 291 37.609 36.722 30.732 1.00124.91 N ANISOU 2120 NH2 ARG A 291 18421 17088 11951 -982 -5688 -964 N ATOM 2121 N ILE A 292 32.393 38.748 35.195 1.00122.63 N ANISOU 2121 N ILE A 292 19070 16432 11090 -304 -5940 -1487 N ATOM 2122 CA ILE A 292 31.756 40.028 34.911 1.00113.66 C ANISOU 2122 CA ILE A 292 18182 15076 9929 -268 -5999 -1557 C ATOM 2123 C ILE A 292 31.602 40.890 36.162 1.00116.97 C ANISOU 2123 C ILE A 292 18883 15506 10053 -320 -6240 -1650 C ATOM 2124 O ILE A 292 30.837 40.561 37.069 1.00107.69 O ANISOU 2124 O ILE A 292 17751 14380 8787 -166 -6229 -1713 O ATOM 2125 CB ILE A 292 30.389 39.844 34.230 1.00100.78 C ANISOU 2125 CB ILE A 292 16511 13272 8510 10 -5759 -1593 C ATOM 2126 CG1 ILE A 292 30.551 39.046 32.934 1.00 96.52 C ANISOU 2126 CG1 ILE A 292 15715 12699 8258 50 -5523 -1503 C ATOM 2127 CG2 ILE A 292 29.751 41.193 33.949 1.00107.85 C ANISOU 2127 CG2 ILE A 292 17668 13947 9365 53 -5831 -1663 C ATOM 2128 CD1 ILE A 292 29.280 38.920 32.125 1.00 99.50 C ANISOU 2128 CD1 ILE A 292 16050 12899 8858 299 -5291 -1528 C ATOM 2129 N ARG A 293 32.338 41.997 36.195 1.00161.66 N ANISOU 2129 N ARG A 293 14485 18991 27947 -2807 -3925 1913 N ATOM 2130 CA ARG A 293 32.290 42.930 37.315 1.00171.53 C ANISOU 2130 CA ARG A 293 16463 19786 28924 -3015 -4240 1597 C ATOM 2131 C ARG A 293 30.930 43.618 37.409 1.00163.85 C ANISOU 2131 C ARG A 293 16226 18144 27884 -2682 -3973 1397 C ATOM 2132 O ARG A 293 30.568 44.160 38.454 1.00165.98 O ANISOU 2132 O ARG A 293 17150 18029 27886 -2650 -4133 1104 O ATOM 2133 CB ARG A 293 33.396 43.979 37.178 1.00181.37 C ANISOU 2133 CB ARG A 293 17721 20940 30250 -3777 -4669 1625 C ATOM 2134 CG ARG A 293 34.806 43.407 37.205 1.00185.83 C ANISOU 2134 CG ARG A 293 17616 22135 30856 -4159 -4988 1797 C ATOM 2135 CD ARG A 293 35.833 44.471 36.854 1.00193.47 C ANISOU 2135 CD ARG A 293 18559 22995 31954 -4906 -5359 1862 C ATOM 2136 NE ARG A 293 35.705 44.912 35.467 1.00194.82 N ANISOU 2136 NE ARG A 293 18515 23042 32467 -5058 -5135 2091 N ATOM 2137 CZ ARG A 293 36.365 45.940 34.945 1.00198.71 C ANISOU 2137 CZ ARG A 293 19033 23347 33119 -5658 -5368 2162 C ATOM 2138 NH1 ARG A 293 37.198 46.645 35.696 1.00204.61 N ANISOU 2138 NH1 ARG A 293 20022 24005 33717 -6166 -5833 2020 N ATOM 2139 NH2 ARG A 293 36.187 46.268 33.672 1.00196.24 N ANISOU 2139 NH2 ARG A 293 18512 22935 33118 -5749 -5134 2374 N ATOM 2140 N GLU A 294 30.183 43.596 36.311 1.00143.02 N ANISOU 2140 N GLU A 294 13478 15371 25490 -2436 -3566 1556 N ATOM 2141 CA GLU A 294 28.850 44.183 36.284 1.00131.56 C ANISOU 2141 CA GLU A 294 12675 13308 24002 -2089 -3270 1394 C ATOM 2142 C GLU A 294 27.844 43.274 36.982 1.00121.83 C ANISOU 2142 C GLU A 294 11626 12106 22556 -1380 -2990 1251 C ATOM 2143 O GLU A 294 26.911 43.746 37.632 1.00110.52 O ANISOU 2143 O GLU A 294 10880 10180 20934 -1121 -2909 999 O ATOM 2144 CB GLU A 294 28.411 44.452 34.844 1.00139.61 C ANISOU 2144 CB GLU A 294 13494 14189 25362 -2071 -2928 1624 C ATOM 2145 CG GLU A 294 26.994 44.991 34.712 1.00155.72 C ANISOU 2145 CG GLU A 294 16156 15621 27388 -1682 -2583 1483 C ATOM 2146 CD GLU A 294 26.814 46.356 35.357 1.00175.25 C ANISOU 2146 CD GLU A 294 19422 17457 29706 -1989 -2832 1214 C ATOM 2147 OE1 GLU A 294 25.653 46.780 35.534 1.00175.38 O ANISOU 2147 OE1 GLU A 294 20032 16964 29642 -1648 -2596 1044 O ATOM 2148 OE2 GLU A 294 27.830 47.005 35.686 1.00186.27 O ANISOU 2148 OE2 GLU A 294 20851 18861 31062 -2570 -3262 1173 O ATOM 2149 N PHE A 295 28.044 41.967 36.847 1.00129.70 N ANISOU 2149 N PHE A 295 12006 13689 23587 -1071 -2843 1415 N ATOM 2150 CA PHE A 295 27.146 40.986 37.447 1.00121.92 C ANISOU 2150 CA PHE A 295 11108 12798 22416 -389 -2566 1308 C ATOM 2151 C PHE A 295 27.312 40.887 38.960 1.00120.58 C ANISOU 2151 C PHE A 295 11315 12619 21879 -345 -2867 1027 C ATOM 2152 O PHE A 295 26.333 40.958 39.702 1.00122.88 O ANISOU 2152 O PHE A 295 12177 12557 21954 60 -2735 790 O ATOM 2153 CB PHE A 295 27.344 39.609 36.807 1.00115.20 C ANISOU 2153 CB PHE A 295 9457 12590 21723 -85 -2319 1579 C ATOM 2154 CG PHE A 295 26.431 39.342 35.644 1.00112.51 C ANISOU 2154 CG PHE A 295 8944 12169 21634 293 -1823 1759 C ATOM 2155 CD1 PHE A 295 25.151 38.860 35.849 1.00109.66 C ANISOU 2155 CD1 PHE A 295 8867 11622 21177 952 -1440 1655 C ATOM 2156 CD2 PHE A 295 26.854 39.567 34.345 1.00111.39 C ANISOU 2156 CD2 PHE A 295 8355 12142 21827 -10 -1741 2034 C ATOM 2157 CE1 PHE A 295 24.309 38.611 34.782 1.00102.61 C ANISOU 2157 CE1 PHE A 295 7815 10657 20514 1300 -985 1821 C ATOM 2158 CE2 PHE A 295 26.015 39.319 33.273 1.00105.55 C ANISOU 2158 CE2 PHE A 295 7456 11332 21318 337 -1286 2201 C ATOM 2159 CZ PHE A 295 24.742 38.841 33.493 1.00100.90 C ANISOU 2159 CZ PHE A 295 7153 10555 20628 992 -908 2094 C ATOM 2160 N ARG A 296 28.551 40.721 39.413 1.00114.01 N ANISOU 2160 N ARG A 296 10162 12179 20978 -760 -3269 1056 N ATOM 2161 CA ARG A 296 28.826 40.539 40.835 1.00113.84 C ANISOU 2161 CA ARG A 296 10421 12220 20614 -739 -3573 811 C ATOM 2162 C ARG A 296 28.267 41.674 41.690 1.00131.95 C ANISOU 2162 C ARG A 296 13606 13849 22681 -817 -3725 486 C ATOM 2163 O ARG A 296 27.812 41.451 42.811 1.00139.79 O ANISOU 2163 O ARG A 296 15004 14731 23378 -510 -3766 243 O ATOM 2164 CB ARG A 296 30.328 40.374 41.083 1.00104.54 C ANISOU 2164 CB ARG A 296 8774 11522 19426 -1270 -4013 905 C ATOM 2165 CG ARG A 296 31.180 41.541 40.619 1.00104.53 C ANISOU 2165 CG ARG A 296 8814 11330 19575 -1985 -4329 963 C ATOM 2166 CD ARG A 296 32.646 41.323 40.962 1.00117.42 C ANISOU 2166 CD ARG A 296 9995 13448 21173 -2481 -4769 1043 C ATOM 2167 NE ARG A 296 33.438 42.530 40.748 1.00143.43 N ANISOU 2167 NE ARG A 296 13441 16501 24553 -3173 -5120 1042 N ATOM 2168 CZ ARG A 296 34.733 42.637 41.029 1.00163.79 C ANISOU 2168 CZ ARG A 296 15731 19392 27108 -3705 -5547 1091 C ATOM 2169 NH1 ARG A 296 35.372 43.779 40.802 1.00170.57 N ANISOU 2169 NH1 ARG A 296 16763 19994 28053 -4318 -5843 1086 N ATOM 2170 NH2 ARG A 296 35.391 41.603 41.537 1.00169.60 N ANISOU 2170 NH2 ARG A 296 16005 20698 27737 -3624 -5678 1144 N ATOM 2171 N GLN A 297 28.303 42.890 41.156 1.00140.69 N ANISOU 2171 N GLN A 297 15014 14515 23926 -1228 -3807 484 N ATOM 2172 CA GLN A 297 27.801 44.051 41.878 1.00149.63 C ANISOU 2172 CA GLN A 297 16990 14996 24867 -1343 -3953 188 C ATOM 2173 C GLN A 297 26.277 44.064 41.902 1.00144.85 C ANISOU 2173 C GLN A 297 16885 13949 24204 -740 -3531 55 C ATOM 2174 O GLN A 297 25.666 44.529 42.863 1.00149.32 O ANISOU 2174 O GLN A 297 18129 14094 24511 -587 -3593 -233 O ATOM 2175 CB GLN A 297 28.335 45.337 41.251 1.00162.21 C ANISOU 2175 CB GLN A 297 18723 16266 26641 -1977 -4166 240 C ATOM 2176 CG GLN A 297 29.850 45.400 41.201 1.00173.98 C ANISOU 2176 CG GLN A 297 19737 18169 28198 -2601 -4591 372 C ATOM 2177 CD GLN A 297 30.358 46.633 40.486 1.00186.34 C ANISOU 2177 CD GLN A 297 21403 19431 29967 -3213 -4774 446 C ATOM 2178 OE1 GLN A 297 29.597 47.561 40.206 1.00190.09 O ANISOU 2178 OE1 GLN A 297 22400 19334 30490 -3207 -4637 352 O ATOM 2179 NE2 GLN A 297 31.653 46.651 40.185 1.00190.08 N ANISOU 2179 NE2 GLN A 297 21373 20287 30561 -3749 -5086 616 N ATOM 2180 N THR A 298 25.670 43.549 40.838 1.00138.24 N ANISOU 2180 N THR A 298 15707 13211 23608 -400 -3103 267 N ATOM 2181 CA THR A 298 24.218 43.455 40.765 1.00138.95 C ANISOU 2181 CA THR A 298 16200 12929 23665 200 -2672 172 C ATOM 2182 C THR A 298 23.699 42.485 41.820 1.00143.75 C ANISOU 2182 C THR A 298 16919 13709 23989 755 -2581 7 C ATOM 2183 O THR A 298 22.779 42.806 42.572 1.00139.11 O ANISOU 2183 O THR A 298 16986 12685 23185 1064 -2500 -249 O ATOM 2184 CB THR A 298 23.748 42.989 39.376 1.00134.66 C ANISOU 2184 CB THR A 298 15190 12526 23447 451 -2232 457 C ATOM 2185 OG1 THR A 298 24.299 43.846 38.369 1.00139.15 O ANISOU 2185 OG1 THR A 298 15608 12976 24288 -79 -2324 626 O ATOM 2186 CG2 THR A 298 22.231 43.023 39.289 1.00130.18 C ANISOU 2186 CG2 THR A 298 15091 11520 22849 1037 -1798 349 C ATOM 2187 N PHE A 299 24.298 41.297 41.868 1.00154.88 N ANISOU 2187 N PHE A 299 17685 15760 25402 878 -2596 156 N ATOM 2188 CA PHE A 299 23.930 40.289 42.857 1.00160.34 C ANISOU 2188 CA PHE A 299 18404 16686 25833 1382 -2531 21 C ATOM 2189 C PHE A 299 24.138 40.826 44.268 1.00167.51 C ANISOU 2189 C PHE A 299 19896 17352 26399 1214 -2911 -295 C ATOM 2190 O PHE A 299 23.272 40.687 45.132 1.00174.21 O ANISOU 2190 O PHE A 299 21234 17956 27003 1647 -2802 -526 O ATOM 2191 CB PHE A 299 24.761 39.016 42.674 1.00160.49 C ANISOU 2191 CB PHE A 299 17599 17458 25921 1427 -2557 244 C ATOM 2192 CG PHE A 299 24.697 38.438 41.290 1.00159.12 C ANISOU 2192 CG PHE A 299 16791 17582 26086 1552 -2216 569 C ATOM 2193 CD1 PHE A 299 23.487 38.051 40.740 1.00157.91 C ANISOU 2193 CD1 PHE A 299 16701 17271 26026 2116 -1730 615 C ATOM 2194 CD2 PHE A 299 25.853 38.259 40.548 1.00158.83 C ANISOU 2194 CD2 PHE A 299 16086 17991 26271 1110 -2382 829 C ATOM 2195 CE1 PHE A 299 23.428 37.511 39.470 1.00153.19 C ANISOU 2195 CE1 PHE A 299 15517 16950 25737 2232 -1417 913 C ATOM 2196 CE2 PHE A 299 25.801 37.720 39.278 1.00155.39 C ANISOU 2196 CE2 PHE A 299 15063 17833 26145 1225 -2069 1128 C ATOM 2197 CZ PHE A 299 24.586 37.346 38.738 1.00152.35 C ANISOU 2197 CZ PHE A 299 14753 17284 25850 1786 -1586 1169 C ATOM 2198 N ARG A 300 25.298 41.439 44.489 1.00161.77 N ANISOU 2198 N ARG A 300 19109 16698 25658 580 -3358 -302 N ATOM 2199 CA ARG A 300 25.668 41.976 45.793 1.00153.61 C ANISOU 2199 CA ARG A 300 18576 15476 24314 341 -3765 -584 C ATOM 2200 C ARG A 300 24.574 42.882 46.351 1.00149.03 C ANISOU 2200 C ARG A 300 18878 14188 23560 532 -3680 -872 C ATOM 2201 O ARG A 300 24.330 42.913 47.556 1.00143.02 O ANISOU 2201 O ARG A 300 18583 13270 22488 685 -3828 -1137 O ATOM 2202 CB ARG A 300 26.993 42.734 45.686 1.00154.44 C ANISOU 2202 CB ARG A 300 18523 15664 24492 -421 -4222 -525 C ATOM 2203 CG ARG A 300 27.556 43.227 47.006 1.00160.97 C ANISOU 2203 CG ARG A 300 19777 16375 25010 -725 -4681 -791 C ATOM 2204 CD ARG A 300 28.925 43.854 46.798 1.00172.90 C ANISOU 2204 CD ARG A 300 21032 18040 26622 -1472 -5115 -693 C ATOM 2205 NE ARG A 300 29.435 44.493 48.007 1.00189.06 N ANISOU 2205 NE ARG A 300 23547 19904 28385 -1807 -5562 -956 N ATOM 2206 CZ ARG A 300 30.588 45.153 48.072 1.00201.06 C ANISOU 2206 CZ ARG A 300 24978 21487 29930 -2466 -5989 -934 C ATOM 2207 NH1 ARG A 300 31.354 45.260 46.995 1.00203.80 N ANISOU 2207 NH1 ARG A 300 24783 22075 30575 -2860 -6028 -660 N ATOM 2208 NH2 ARG A 300 30.976 45.707 49.213 1.00207.03 N ANISOU 2208 NH2 ARG A 300 26187 22063 30413 -2731 -6378 -1185 N ATOM 2209 N LYS A 301 23.912 43.609 45.460 1.00155.80 N ANISOU 2209 N LYS A 301 19956 14620 24620 528 -3435 -814 N ATOM 2210 CA LYS A 301 22.827 44.500 45.846 1.00164.47 C ANISOU 2210 CA LYS A 301 21875 15029 25589 712 -3317 -1063 C ATOM 2211 C LYS A 301 21.557 43.732 46.211 1.00164.10 C ANISOU 2211 C LYS A 301 22042 14905 25405 1470 -2921 -1166 C ATOM 2212 O LYS A 301 20.916 44.016 47.223 1.00166.83 O ANISOU 2212 O LYS A 301 23021 14891 25477 1695 -2956 -1447 O ATOM 2213 CB LYS A 301 22.541 45.477 44.708 1.00165.18 C ANISOU 2213 CB LYS A 301 22087 14717 25958 469 -3168 -948 C ATOM 2214 CG LYS A 301 21.304 46.327 44.900 1.00164.15 C ANISOU 2214 CG LYS A 301 22748 13882 25741 717 -2966 -1164 C ATOM 2215 CD LYS A 301 20.395 46.222 43.683 1.00157.89 C ANISOU 2215 CD LYS A 301 21820 12950 25221 1044 -2483 -978 C ATOM 2216 CE LYS A 301 21.169 46.416 42.382 1.00156.12 C ANISOU 2216 CE LYS A 301 21019 12951 25348 606 -2498 -672 C ATOM 2217 NZ LYS A 301 20.474 45.800 41.213 1.00149.81 N ANISOU 2217 NZ LYS A 301 19830 12277 24813 1004 -2015 -433 N ATOM 2218 N ILE A 302 21.197 42.762 45.377 1.00160.43 N ANISOU 2218 N ILE A 302 21046 14777 25133 1859 -2543 -935 N ATOM 2219 CA ILE A 302 19.994 41.966 45.598 1.00157.29 C ANISOU 2219 CA ILE A 302 20785 14341 24639 2589 -2138 -1000 C ATOM 2220 C ILE A 302 20.024 41.259 46.951 1.00157.34 C ANISOU 2220 C ILE A 302 20922 14554 24306 2866 -2288 -1203 C ATOM 2221 O ILE A 302 19.049 41.293 47.702 1.00157.21 O ANISOU 2221 O ILE A 302 21463 14200 24070 3286 -2151 -1433 O ATOM 2222 CB ILE A 302 19.801 40.911 44.490 1.00152.02 C ANISOU 2222 CB ILE A 302 19416 14109 24237 2921 -1748 -694 C ATOM 2223 CG1 ILE A 302 19.798 41.572 43.109 1.00153.23 C ANISOU 2223 CG1 ILE A 302 19401 14085 24736 2647 -1594 -478 C ATOM 2224 CG2 ILE A 302 18.515 40.133 44.716 1.00145.38 C ANISOU 2224 CG2 ILE A 302 18744 13198 23295 3678 -1323 -767 C ATOM 2225 CD1 ILE A 302 19.630 40.591 41.964 1.00144.30 C ANISOU 2225 CD1 ILE A 302 17580 13368 23879 2944 -1215 -171 C ATOM 2226 N ILE A 303 21.149 40.619 47.255 1.00159.91 N ANISOU 2226 N ILE A 303 20731 15436 24591 2628 -2571 -1115 N ATOM 2227 CA ILE A 303 21.305 39.881 48.506 1.00161.79 C ANISOU 2227 CA ILE A 303 21017 15937 24520 2858 -2735 -1283 C ATOM 2228 C ILE A 303 21.128 40.785 49.723 1.00167.98 C ANISOU 2228 C ILE A 303 22595 16236 24995 2724 -3021 -1627 C ATOM 2229 O ILE A 303 20.322 40.498 50.609 1.00165.59 O ANISOU 2229 O ILE A 303 22710 15765 24443 3182 -2911 -1841 O ATOM 2230 CB ILE A 303 22.682 39.189 48.587 1.00157.95 C ANISOU 2230 CB ILE A 303 19842 16115 24058 2524 -3041 -1124 C ATOM 2231 CG1 ILE A 303 22.877 38.249 47.396 1.00143.36 C ANISOU 2231 CG1 ILE A 303 17190 14768 22513 2665 -2759 -781 C ATOM 2232 CG2 ILE A 303 22.826 38.431 49.900 1.00157.41 C ANISOU 2232 CG2 ILE A 303 19833 16310 23664 2769 -3210 -1302 C ATOM 2233 CD1 ILE A 303 24.226 37.569 47.372 1.00140.23 C ANISOU 2233 CD1 ILE A 303 16087 15029 22166 2334 -3039 -602 C ATOM 2234 N ARG A 304 21.887 41.875 49.759 1.00175.65 N ANISOU 2234 N ARG A 304 23770 16986 25984 2094 -3388 -1678 N ATOM 2235 CA ARG A 304 21.813 42.823 50.864 1.00186.43 C ANISOU 2235 CA ARG A 304 25881 17883 27070 1899 -3689 -1997 C ATOM 2236 C ARG A 304 20.399 43.362 51.044 1.00185.55 C ANISOU 2236 C ARG A 304 26491 17141 26868 2311 -3393 -2196 C ATOM 2237 O ARG A 304 19.851 43.339 52.146 1.00186.25 O ANISOU 2237 O ARG A 304 27090 17016 26661 2599 -3428 -2459 O ATOM 2238 CB ARG A 304 22.790 43.979 50.643 1.00197.78 C ANISOU 2238 CB ARG A 304 27399 19150 28599 1146 -4082 -1986 C ATOM 2239 CG ARG A 304 24.252 43.575 50.704 1.00205.44 C ANISOU 2239 CG ARG A 304 27761 20698 29601 687 -4451 -1842 C ATOM 2240 CD ARG A 304 25.159 44.778 50.499 1.00213.97 C ANISOU 2240 CD ARG A 304 28966 21567 30766 -52 -4834 -1842 C ATOM 2241 NE ARG A 304 26.558 44.463 50.776 1.00218.44 N ANISOU 2241 NE ARG A 304 29045 22644 31308 -502 -5236 -1753 N ATOM 2242 CZ ARG A 304 27.554 45.336 50.674 1.00222.23 C ANISOU 2242 CZ ARG A 304 29523 23066 31851 -1171 -5619 -1734 C ATOM 2243 NH1 ARG A 304 28.797 44.961 50.948 1.00224.87 N ANISOU 2243 NH1 ARG A 304 29394 23892 32157 -1541 -5969 -1650 N ATOM 2244 NH2 ARG A 304 27.309 46.584 50.298 1.00223.23 N ANISOU 2244 NH2 ARG A 304 30107 22641 32067 -1473 -5652 -1799 N ATOM 2245 N SER A 305 19.813 43.846 49.954 1.00183.73 N ANISOU 2245 N SER A 305 26299 16616 26894 2339 -3101 -2068 N ATOM 2246 CA SER A 305 18.464 44.400 49.990 1.00181.17 C ANISOU 2246 CA SER A 305 26635 15684 26519 2714 -2800 -2232 C ATOM 2247 C SER A 305 17.429 43.360 49.573 1.00174.05 C ANISOU 2247 C SER A 305 25516 14930 25685 3417 -2297 -2128 C ATOM 2248 O SER A 305 17.003 42.533 50.380 1.00172.15 O ANISOU 2248 O SER A 305 25333 14850 25227 3881 -2208 -2245 O ATOM 2249 CB SER A 305 18.366 45.634 49.090 1.00181.50 C ANISOU 2249 CB SER A 305 26917 15258 26787 2331 -2779 -2175 C ATOM 2250 OG SER A 305 17.075 46.213 49.155 1.00179.40 O ANISOU 2250 OG SER A 305 27311 14388 26464 2678 -2501 -2340 O TER 2251 SER A 305 HETATM 2252 N2 T4E A 330 23.684 6.666 32.080 1.00119.27 N HETATM 2253 N1 T4E A 330 23.105 7.781 32.548 1.00118.43 N HETATM 2254 C6 T4E A 330 23.167 8.937 31.828 1.00118.04 C HETATM 2255 C5 T4E A 330 23.852 8.945 30.571 1.00117.97 C HETATM 2256 N4 T4E A 330 24.432 7.799 30.123 1.00118.08 N HETATM 2257 C3 T4E A 330 24.308 6.738 30.908 1.00118.73 C HETATM 2258 C10 T4E A 330 21.114 12.259 33.687 1.00114.66 C HETATM 2259 C11 T4E A 330 20.430 11.061 33.407 1.00115.14 C HETATM 2260 C12 T4E A 330 21.110 9.987 32.803 1.00117.02 C HETATM 2261 C7 T4E A 330 22.480 10.083 32.466 1.00116.84 C HETATM 2262 C8 T4E A 330 23.155 11.292 32.750 1.00115.62 C HETATM 2263 C9 T4E A 330 22.484 12.376 33.356 1.00115.01 C HETATM 2264 C16 T4E A 330 24.362 12.344 27.927 1.00115.74 C HETATM 2265 C17 T4E A 330 23.174 12.204 28.663 1.00115.36 C HETATM 2266 C18 T4E A 330 23.004 11.102 29.521 1.00116.32 C HETATM 2267 C13 T4E A 330 24.011 10.116 29.668 1.00117.31 C HETATM 2268 C14 T4E A 330 25.200 10.281 28.914 1.00116.86 C HETATM 2269 C15 T4E A 330 25.380 11.381 28.053 1.00116.02 C HETATM 2270 N3 T4E A 330 24.883 5.599 30.462 1.00118.82 N HETATM 2271 CL1 T4E A 330 23.352 13.836 33.683 1.00114.91 CL HETATM 2272 O1 T4E A 330 20.443 13.293 34.273 1.00114.91 O CONECT 484 1071 CONECT 500 1041 CONECT 520 1115 CONECT 1041 500 CONECT 1071 484 CONECT 1115 520 CONECT 1861 1882 CONECT 1882 1861 CONECT 2252 2253 2257 CONECT 2253 2252 2254 CONECT 2254 2253 2255 2261 CONECT 2255 2254 2256 2267 CONECT 2256 2255 2257 CONECT 2257 2252 2256 2270 CONECT 2258 2259 2263 2272 CONECT 2259 2258 2260 CONECT 2260 2259 2261 CONECT 2261 2254 2260 2262 CONECT 2262 2261 2263 CONECT 2263 2258 2262 2271 CONECT 2264 2265 2269 CONECT 2265 2264 2266 CONECT 2266 2265 2267 CONECT 2267 2255 2266 2268 CONECT 2268 2267 2269 CONECT 2269 2264 2268 CONECT 2270 2257 CONECT 2271 2263 CONECT 2272 2258 MASTER 524 0 1 15 2 0 3 6 2271 1 29 26 END