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*** CHAPERONE 25-APR-17 5NRO ***elNémo ID: 2309051504233478392Job options:ID = 2309051504233478392 JOBID = CHAPERONE 25-APR-17 5NRO USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER CHAPERONE 25-APR-17 5NRO TITLE STRUCTURE OF FULL-LENGTH DNAK WITH BOUND J-DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHAPERONE PROTEIN DNAK; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HSP70,HEAT SHOCK 70 KDA PROTEIN,HEAT SHOCK PROTEIN 70; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: CHAPERONE PROTEIN DNAJ; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: HSP40,HEAT SHOCK PROTEIN J; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: DNAK, GROP, GRPF, SEG, B0014, JW0013; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 9 ORGANISM_TAXID: 562; SOURCE 10 GENE: DNAJ, GROP, B0015, JW0014; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DNAK, DNAJ, CHAPERONE, HSP70, HSP40 EXPDTA X-RAY DIFFRACTION AUTHOR J.KOPP,R.KITYK,M.P.MAYER REVDAT 2 31-JAN-18 5NRO 1 JRNL REVDAT 1 17-JAN-18 5NRO 0 JRNL AUTH R.KITYK,J.KOPP,M.P.MAYER JRNL TITL MOLECULAR MECHANISM OF J-DOMAIN-TRIGGERED ATP HYDROLYSIS BY JRNL TITL 2 HSP70 CHAPERONES. JRNL REF MOL. CELL V. 69 227 2018 JRNL REFN ISSN 1097-4164 JRNL PMID 29290615 JRNL DOI 10.1016/J.MOLCEL.2017.12.003 REMARK 2 REMARK 2 RESOLUTION. 3.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.12 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 19808 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920 REMARK 3 FREE R VALUE TEST SET COUNT : 974 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 46.1251 - 6.2129 1.00 2901 154 0.1763 0.1889 REMARK 3 2 6.2129 - 4.9332 1.00 2705 156 0.2131 0.2282 REMARK 3 3 4.9332 - 4.3101 1.00 2695 131 0.2038 0.2378 REMARK 3 4 4.3101 - 3.9163 1.00 2655 136 0.2119 0.2340 REMARK 3 5 3.9163 - 3.6357 1.00 2617 144 0.2575 0.2778 REMARK 3 6 3.6357 - 3.4214 1.00 2632 134 0.2983 0.3301 REMARK 3 7 3.4214 - 3.2501 1.00 2629 119 0.3560 0.3714 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.150 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 5200 REMARK 3 ANGLE : 0.647 7016 REMARK 3 CHIRALITY : 0.043 811 REMARK 3 PLANARITY : 0.003 924 REMARK 3 DIHEDRAL : 11.703 3236 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8749 16.1723 -29.0949 REMARK 3 T TENSOR REMARK 3 T11: 1.0002 T22: 0.9292 REMARK 3 T33: 0.9794 T12: 0.0526 REMARK 3 T13: 0.0607 T23: -0.0731 REMARK 3 L TENSOR REMARK 3 L11: 2.8870 L22: 5.5893 REMARK 3 L33: 4.8800 L12: 0.6368 REMARK 3 L13: -0.8141 L23: 1.1593 REMARK 3 S TENSOR REMARK 3 S11: 0.0695 S12: 0.1635 S13: -0.2997 REMARK 3 S21: -0.1938 S22: 0.0533 S23: -0.1996 REMARK 3 S31: 0.4016 S32: 0.1665 S33: -0.2243 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.4167 30.7065 -23.9073 REMARK 3 T TENSOR REMARK 3 T11: 0.9096 T22: 1.1066 REMARK 3 T33: 0.9829 T12: -0.1186 REMARK 3 T13: 0.1691 T23: -0.0769 REMARK 3 L TENSOR REMARK 3 L11: 2.0699 L22: 5.7370 REMARK 3 L33: 3.4198 L12: -0.5892 REMARK 3 L13: 0.5976 L23: 1.3209 REMARK 3 S TENSOR REMARK 3 S11: 0.2604 S12: -0.0206 S13: 0.4546 REMARK 3 S21: -0.2248 S22: -0.1062 S23: -0.7791 REMARK 3 S31: -0.3204 S32: 0.7589 S33: -0.2257 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 327 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8118 22.7915 -25.1984 REMARK 3 T TENSOR REMARK 3 T11: 1.0436 T22: 0.7660 REMARK 3 T33: 0.8759 T12: -0.0811 REMARK 3 T13: 0.1807 T23: -0.0709 REMARK 3 L TENSOR REMARK 3 L11: 4.2522 L22: 3.2619 REMARK 3 L33: 1.9188 L12: 2.2295 REMARK 3 L13: 0.8034 L23: 0.3455 REMARK 3 S TENSOR REMARK 3 S11: 0.3320 S12: -0.1939 S13: -0.0397 REMARK 3 S21: -0.0682 S22: -0.1193 S23: 0.0508 REMARK 3 S31: 0.2935 S32: 0.0409 S33: -0.0841 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 328 THROUGH 369 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.3146 41.7727 -21.2029 REMARK 3 T TENSOR REMARK 3 T11: 1.1760 T22: 0.8785 REMARK 3 T33: 1.1891 T12: -0.1156 REMARK 3 T13: 0.2088 T23: -0.0972 REMARK 3 L TENSOR REMARK 3 L11: 6.2636 L22: 4.9433 REMARK 3 L33: 3.5134 L12: 3.0566 REMARK 3 L13: 3.0281 L23: 1.5367 REMARK 3 S TENSOR REMARK 3 S11: 0.0870 S12: 0.2094 S13: 1.2741 REMARK 3 S21: 0.0624 S22: 0.0954 S23: 0.2781 REMARK 3 S31: -0.7378 S32: 0.4820 S33: 0.0855 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 370 THROUGH 508 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.7743 22.3997 -2.6395 REMARK 3 T TENSOR REMARK 3 T11: 1.1044 T22: 1.4956 REMARK 3 T33: 1.0242 T12: -0.0217 REMARK 3 T13: -0.0010 T23: -0.1338 REMARK 3 L TENSOR REMARK 3 L11: 2.5862 L22: 5.0206 REMARK 3 L33: 2.3055 L12: -0.8246 REMARK 3 L13: 0.6140 L23: -1.2439 REMARK 3 S TENSOR REMARK 3 S11: -0.1910 S12: -0.6245 S13: -0.1719 REMARK 3 S21: 0.9057 S22: 0.1129 S23: -0.7239 REMARK 3 S31: 0.0321 S32: 0.8781 S33: -0.0522 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 509 THROUGH 553 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.2488 9.9581 -48.9870 REMARK 3 T TENSOR REMARK 3 T11: 0.9628 T22: 1.1337 REMARK 3 T33: 1.2242 T12: -0.0088 REMARK 3 T13: 0.1649 T23: -0.0625 REMARK 3 L TENSOR REMARK 3 L11: 2.3876 L22: 2.9107 REMARK 3 L33: 3.2938 L12: -1.2334 REMARK 3 L13: 1.6488 L23: -0.3271 REMARK 3 S TENSOR REMARK 3 S11: -0.5602 S12: -0.0967 S13: 0.1468 REMARK 3 S21: 0.2509 S22: -0.1732 S23: -0.5476 REMARK 3 S31: -0.0021 S32: 0.7466 S33: 0.5244 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 554 THROUGH 604 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.6992 3.3938 -69.7612 REMARK 3 T TENSOR REMARK 3 T11: 1.2741 T22: 1.0949 REMARK 3 T33: 1.0958 T12: 0.0202 REMARK 3 T13: 0.1523 T23: -0.1418 REMARK 3 L TENSOR REMARK 3 L11: 3.7911 L22: 3.6399 REMARK 3 L33: 2.9608 L12: -0.3235 REMARK 3 L13: 1.9487 L23: 1.1943 REMARK 3 S TENSOR REMARK 3 S11: 0.2916 S12: 0.6850 S13: 0.1382 REMARK 3 S21: -0.3705 S22: -0.0485 S23: -0.4619 REMARK 3 S31: 0.3486 S32: 0.3939 S33: -0.2329 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 10 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.7177 44.2103 2.6541 REMARK 3 T TENSOR REMARK 3 T11: 2.0917 T22: 1.6477 REMARK 3 T33: 1.8132 T12: -0.1384 REMARK 3 T13: -0.0316 T23: -0.0459 REMARK 3 L TENSOR REMARK 3 L11: -0.0064 L22: 0.2350 REMARK 3 L33: 0.0518 L12: -0.0517 REMARK 3 L13: 0.0287 L23: -0.1238 REMARK 3 S TENSOR REMARK 3 S11: -0.5478 S12: -1.0775 S13: 1.4142 REMARK 3 S21: 0.7833 S22: 0.1502 S23: -0.0818 REMARK 3 S31: -0.9291 S32: 0.6516 S33: -0.1054 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.7870 53.7996 3.4084 REMARK 3 T TENSOR REMARK 3 T11: 2.4959 T22: 2.1421 REMARK 3 T33: 2.1931 T12: 0.0353 REMARK 3 T13: -0.0851 T23: -0.3376 REMARK 3 L TENSOR REMARK 3 L11: 0.0101 L22: 0.0003 REMARK 3 L33: 0.1023 L12: -0.0067 REMARK 3 L13: -0.0270 L23: 0.0050 REMARK 3 S TENSOR REMARK 3 S11: 0.2408 S12: 0.2467 S13: 1.5889 REMARK 3 S21: -0.3043 S22: 0.8620 S23: -0.0674 REMARK 3 S31: -0.5973 S32: 0.4779 S33: 0.2104 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.7317 44.2769 -11.0391 REMARK 3 T TENSOR REMARK 3 T11: 2.1610 T22: 1.8337 REMARK 3 T33: 2.1551 T12: -0.2032 REMARK 3 T13: 0.2632 T23: 0.0174 REMARK 3 L TENSOR REMARK 3 L11: 0.0027 L22: 0.5387 REMARK 3 L33: 0.5393 L12: -0.0356 REMARK 3 L13: 0.0110 L23: -0.5831 REMARK 3 S TENSOR REMARK 3 S11: 0.8087 S12: 0.9069 S13: 0.6805 REMARK 3 S21: 0.0814 S22: -0.1374 S23: -3.1286 REMARK 3 S31: -0.2322 S32: 0.8900 S33: -0.0130 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 41 THROUGH 58 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.6065 38.2259 -4.4138 REMARK 3 T TENSOR REMARK 3 T11: 2.1063 T22: 2.3102 REMARK 3 T33: 1.6872 T12: 0.0768 REMARK 3 T13: 0.0701 T23: -0.2802 REMARK 3 L TENSOR REMARK 3 L11: 1.4980 L22: 5.8180 REMARK 3 L33: 5.4750 L12: 2.9275 REMARK 3 L13: 2.8428 L23: 5.5599 REMARK 3 S TENSOR REMARK 3 S11: 0.2045 S12: 1.0765 S13: 1.0731 REMARK 3 S21: 1.2149 S22: 0.4193 S23: -1.5800 REMARK 3 S31: -0.9283 S32: 1.7106 S33: -1.3180 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 65 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.9800 44.9055 9.0342 REMARK 3 T TENSOR REMARK 3 T11: 3.3099 T22: 1.8539 REMARK 3 T33: 2.2956 T12: -0.7396 REMARK 3 T13: 0.7735 T23: -0.4195 REMARK 3 L TENSOR REMARK 3 L11: 0.0341 L22: 0.1035 REMARK 3 L33: 0.2468 L12: 0.0298 REMARK 3 L13: -0.0999 L23: -0.0238 REMARK 3 S TENSOR REMARK 3 S11: 1.5895 S12: -0.9921 S13: 1.2473 REMARK 3 S21: 0.9916 S22: 0.3187 S23: 0.8871 REMARK 3 S31: -2.5276 S32: -1.0095 S33: -0.7525 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 5NRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-APR-17. REMARK 100 THE DEPOSITION ID IS D_1200004603. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-MAR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.872899 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19859 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250 REMARK 200 RESOLUTION RANGE LOW (A) : 46.121 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 19.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 20.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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: 4B9Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 9% W/V PEG 8000 0.1M CALCIUM ACETATE REMARK 280 0.1 M IMIDAZOLE PH 6.5 PROTEIN AT 18 MG/ML CRYSTALIZATION DROP REMARK 280 CONTAINED 200 NL PROTEIN + 100 NL RESERVOIR SOLUTION, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+2/3 REMARK 290 6555 X-Y,X,Z+1/3 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+2/3 REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 168.59000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.29500 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 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 168.59000 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.29500 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 168.59000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 84.29500 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 168.59000 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 84.29500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31330 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLN A 605 REMARK 465 HIS A 606 REMARK 465 HIS A 607 REMARK 465 HIS A 608 REMARK 465 HIS A 609 REMARK 465 HIS A 610 REMARK 465 HIS A 611 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 TYR B 66 REMARK 465 ASP B 67 REMARK 465 GLN B 68 REMARK 465 TYR B 69 REMARK 465 GLY B 70 REMARK 465 HIS B 71 REMARK 465 ALA B 72 REMARK 465 ALA B 73 REMARK 465 PHE B 74 REMARK 465 GLU B 75 REMARK 465 GLN B 76 REMARK 465 GLY B 77 REMARK 465 GLY B 78 REMARK 465 MET B 79 REMARK 465 GLY B 80 REMARK 465 GLY B 81 REMARK 465 GLY B 82 REMARK 465 GLY B 83 REMARK 465 PHE B 84 REMARK 465 GLY B 85 REMARK 465 GLY B 86 REMARK 465 GLY B 87 REMARK 465 ALA B 88 REMARK 465 ASP B 89 REMARK 465 PHE B 90 REMARK 465 SER B 91 REMARK 465 ASP B 92 REMARK 465 ILE B 93 REMARK 465 PHE B 94 REMARK 465 GLY B 95 REMARK 465 ASP B 96 REMARK 465 VAL B 97 REMARK 465 PHE B 98 REMARK 465 GLY B 99 REMARK 465 ASP B 100 REMARK 465 ILE B 101 REMARK 465 PHE B 102 REMARK 465 GLY B 103 REMARK 465 GLY B 104 REMARK 465 GLY B 105 REMARK 465 SER B 106 REMARK 465 SER B 107 REMARK 465 HIS B 108 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 MG MG A 701 O HOH A 802 1.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 22 -13.37 76.68 REMARK 500 SER A 38 59.96 -94.09 REMARK 500 LYS A 556 46.34 -84.85 REMARK 500 LYS B 14 -12.50 77.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 701 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ATP A 700 O1G REMARK 620 2 ATP A 700 O2B 62.1 REMARK 620 3 HOH A 801 O 102.9 154.6 REMARK 620 4 HOH A 803 O 81.7 79.5 78.0 REMARK 620 5 HOH A 804 O 150.9 95.2 90.6 76.0 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 700 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701 DBREF 5NRO A 1 605 UNP P0A6Y8 DNAK_ECOLI 1 605 DBREF 5NRO B 1 105 UNP P08622 DNAJ_ECOLI 1 105 SEQADV 5NRO CYS A 47 UNP P0A6Y8 GLU 47 ENGINEERED MUTATION SEQADV 5NRO ALA A 199 UNP P0A6Y8 THR 199 ENGINEERED MUTATION SEQADV 5NRO CYS A 529 UNP P0A6Y8 PHE 529 ENGINEERED MUTATION SEQADV 5NRO HIS A 606 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO HIS A 607 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO HIS A 608 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO HIS A 609 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO HIS A 610 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO HIS A 611 UNP P0A6Y8 EXPRESSION TAG SEQADV 5NRO SER B 106 UNP P08622 EXPRESSION TAG SEQADV 5NRO SER B 107 UNP P08622 EXPRESSION TAG SEQADV 5NRO HIS B 108 UNP P08622 EXPRESSION TAG SEQRES 1 A 611 MET GLY LYS ILE ILE GLY ILE ASP LEU GLY THR THR ASN SEQRES 2 A 611 SER CYS VAL ALA ILE MET ASP GLY THR THR PRO ARG VAL SEQRES 3 A 611 LEU GLU ASN ALA GLU GLY ASP ARG THR THR PRO SER ILE SEQRES 4 A 611 ILE ALA TYR THR GLN ASP GLY CYS THR LEU VAL GLY GLN SEQRES 5 A 611 PRO ALA LYS ARG GLN ALA VAL THR ASN PRO GLN ASN THR SEQRES 6 A 611 LEU PHE ALA ILE LYS ARG LEU ILE GLY ARG ARG PHE GLN SEQRES 7 A 611 ASP GLU GLU VAL GLN ARG ASP VAL SER ILE MET PRO PHE SEQRES 8 A 611 LYS ILE ILE ALA ALA ASP ASN GLY ASP ALA TRP VAL GLU SEQRES 9 A 611 VAL LYS GLY GLN LYS MET ALA PRO PRO GLN ILE SER ALA SEQRES 10 A 611 GLU VAL LEU LYS LYS MET LYS LYS THR ALA GLU ASP TYR SEQRES 11 A 611 LEU GLY GLU PRO VAL THR GLU ALA VAL ILE THR VAL PRO SEQRES 12 A 611 ALA TYR PHE ASN ASP ALA GLN ARG GLN ALA THR LYS ASP SEQRES 13 A 611 ALA GLY ARG ILE ALA GLY LEU GLU VAL LYS ARG ILE ILE SEQRES 14 A 611 ASN GLU PRO THR ALA ALA ALA LEU ALA TYR GLY LEU ASP SEQRES 15 A 611 LYS GLY THR GLY ASN ARG THR ILE ALA VAL TYR ASP LEU SEQRES 16 A 611 GLY GLY GLY ALA PHE ASP ILE SER ILE ILE GLU ILE ASP SEQRES 17 A 611 GLU VAL ASP GLY GLU LYS THR PHE GLU VAL LEU ALA THR SEQRES 18 A 611 ASN GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP SER SEQRES 19 A 611 ARG LEU ILE ASN TYR LEU VAL GLU GLU PHE LYS LYS ASP SEQRES 20 A 611 GLN GLY ILE ASP LEU ARG ASN ASP PRO LEU ALA MET GLN SEQRES 21 A 611 ARG LEU LYS GLU ALA ALA GLU LYS ALA LYS ILE GLU LEU SEQRES 22 A 611 SER SER ALA GLN GLN THR ASP VAL ASN LEU PRO TYR ILE SEQRES 23 A 611 THR ALA ASP ALA THR GLY PRO LYS HIS MET ASN ILE LYS SEQRES 24 A 611 VAL THR ARG ALA LYS LEU GLU SER LEU VAL GLU ASP LEU SEQRES 25 A 611 VAL ASN ARG SER ILE GLU PRO LEU LYS VAL ALA LEU GLN SEQRES 26 A 611 ASP ALA GLY LEU SER VAL SER ASP ILE ASP ASP VAL ILE SEQRES 27 A 611 LEU VAL GLY GLY GLN THR ARG MET PRO MET VAL GLN LYS SEQRES 28 A 611 LYS VAL ALA GLU PHE PHE GLY LYS GLU PRO ARG LYS ASP SEQRES 29 A 611 VAL ASN PRO ASP GLU ALA VAL ALA ILE GLY ALA ALA VAL SEQRES 30 A 611 GLN GLY GLY VAL LEU THR GLY ASP VAL LYS ASP VAL LEU SEQRES 31 A 611 LEU LEU ASP VAL THR PRO LEU SER LEU GLY ILE GLU THR SEQRES 32 A 611 MET GLY GLY VAL MET THR THR LEU ILE ALA LYS ASN THR SEQRES 33 A 611 THR ILE PRO THR LYS HIS SER GLN VAL PHE SER THR ALA SEQRES 34 A 611 GLU ASP ASN GLN SER ALA VAL THR ILE HIS VAL LEU GLN SEQRES 35 A 611 GLY GLU ARG LYS ARG ALA ALA ASP ASN LYS SER LEU GLY SEQRES 36 A 611 GLN PHE ASN LEU ASP GLY ILE ASN PRO ALA PRO ARG GLY SEQRES 37 A 611 MET PRO GLN ILE GLU VAL THR PHE ASP ILE ASP ALA ASP SEQRES 38 A 611 GLY ILE LEU HIS VAL SER ALA LYS ASP LYS ASN SER GLY SEQRES 39 A 611 LYS GLU GLN LYS ILE THR ILE LYS ALA SER SER GLY LEU SEQRES 40 A 611 ASN GLU ASP GLU ILE GLN LYS MET VAL ARG ASP ALA GLU SEQRES 41 A 611 ALA ASN ALA GLU ALA ASP ARG LYS CYS GLU GLU LEU VAL SEQRES 42 A 611 GLN THR ARG ASN GLN GLY ASP HIS LEU LEU HIS SER THR SEQRES 43 A 611 ARG LYS GLN VAL GLU GLU ALA GLY ASP LYS LEU PRO ALA SEQRES 44 A 611 ASP ASP LYS THR ALA ILE GLU SER ALA LEU THR ALA LEU SEQRES 45 A 611 GLU THR ALA LEU LYS GLY GLU ASP LYS ALA ALA ILE GLU SEQRES 46 A 611 ALA LYS MET GLN GLU LEU ALA GLN VAL SER GLN LYS LEU SEQRES 47 A 611 MET GLU ILE ALA GLN GLN GLN HIS HIS HIS HIS HIS HIS SEQRES 1 B 108 MET ALA LYS GLN ASP TYR TYR GLU ILE LEU GLY VAL SER SEQRES 2 B 108 LYS THR ALA GLU GLU ARG GLU ILE ARG LYS ALA TYR LYS SEQRES 3 B 108 ARG LEU ALA MET LYS TYR HIS PRO ASP ARG ASN GLN GLY SEQRES 4 B 108 ASP LYS GLU ALA GLU ALA LYS PHE LYS GLU ILE LYS GLU SEQRES 5 B 108 ALA TYR GLU VAL LEU THR ASP SER GLN LYS ARG ALA ALA SEQRES 6 B 108 TYR ASP GLN TYR GLY HIS ALA ALA PHE GLU GLN GLY GLY SEQRES 7 B 108 MET GLY GLY GLY GLY PHE GLY GLY GLY ALA ASP PHE SER SEQRES 8 B 108 ASP ILE PHE GLY ASP VAL PHE GLY ASP ILE PHE GLY GLY SEQRES 9 B 108 GLY SER SER HIS HET ATP A 700 31 HET MG A 701 1 HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE HETNAM MG MAGNESIUM ION FORMUL 3 ATP C10 H16 N5 O13 P3 FORMUL 4 MG MG 2+ FORMUL 5 HOH *4(H2 O) HELIX 1 AA1 GLY A 51 GLN A 57 1 7 HELIX 2 AA2 ASN A 61 GLN A 63 5 3 HELIX 3 AA3 ALA A 68 LEU A 72 5 5 HELIX 4 AA4 ASP A 79 MET A 89 1 11 HELIX 5 AA5 ALA A 111 GLY A 132 1 22 HELIX 6 AA6 ASN A 147 ALA A 161 1 15 HELIX 7 AA7 GLU A 171 LEU A 181 1 11 HELIX 8 AA8 GLY A 228 GLY A 249 1 22 HELIX 9 AA9 ASP A 255 SER A 274 1 20 HELIX 10 AB1 ARG A 302 SER A 316 1 15 HELIX 11 AB2 ILE A 317 GLY A 328 1 12 HELIX 12 AB3 SER A 330 ILE A 334 5 5 HELIX 13 AB4 GLY A 341 ARG A 345 5 5 HELIX 14 AB5 MET A 346 GLY A 358 1 13 HELIX 15 AB6 GLU A 369 GLY A 384 1 16 HELIX 16 AB7 MET A 404 GLY A 406 5 3 HELIX 17 AB8 ARG A 447 ASN A 451 5 5 HELIX 18 AB9 ASN A 508 GLY A 554 1 47 HELIX 19 AC1 PRO A 558 GLY A 578 1 21 HELIX 20 AC2 ASP A 580 GLN A 603 1 24 HELIX 21 AC3 ASP B 5 GLY B 11 1 7 HELIX 22 AC4 GLU B 17 HIS B 33 1 17 HELIX 23 AC5 HIS B 33 GLN B 38 1 6 HELIX 24 AC6 ASP B 40 ASP B 59 1 20 HELIX 25 AC7 ASP B 59 ALA B 65 1 7 SHEET 1 AA1 3 THR A 23 VAL A 26 0 SHEET 2 AA1 3 ASN A 13 ASP A 20 -1 N ASP A 20 O THR A 23 SHEET 3 AA1 3 THR A 36 PRO A 37 -1 O THR A 36 N SER A 14 SHEET 1 AA2 5 THR A 23 VAL A 26 0 SHEET 2 AA2 5 ASN A 13 ASP A 20 -1 N ASP A 20 O THR A 23 SHEET 3 AA2 5 ILE A 4 ASP A 8 -1 N ASP A 8 O CYS A 15 SHEET 4 AA2 5 GLU A 137 VAL A 142 1 O VAL A 139 N ILE A 7 SHEET 5 AA2 5 GLU A 164 ASN A 170 1 O ILE A 169 N VAL A 142 SHEET 1 AA3 3 THR A 48 VAL A 50 0 SHEET 2 AA3 3 ILE A 40 TYR A 42 -1 N ALA A 41 O LEU A 49 SHEET 3 AA3 3 THR A 65 LEU A 66 -1 O LEU A 66 N ILE A 40 SHEET 1 AA4 3 LYS A 92 ALA A 95 0 SHEET 2 AA4 3 ALA A 101 VAL A 105 -1 O TRP A 102 N ILE A 94 SHEET 3 AA4 3 GLN A 108 MET A 110 -1 O MET A 110 N VAL A 103 SHEET 1 AA5 5 ASP A 336 VAL A 340 0 SHEET 2 AA5 5 ASN A 187 LEU A 195 1 N TYR A 193 O VAL A 340 SHEET 3 AA5 5 PHE A 200 VAL A 210 -1 O ILE A 205 N ILE A 190 SHEET 4 AA5 5 GLU A 213 ASP A 224 -1 O GLU A 217 N GLU A 206 SHEET 5 AA5 5 VAL A 389 LEU A 392 1 O LEU A 392 N PHE A 216 SHEET 1 AA6 2 GLN A 278 ALA A 288 0 SHEET 2 AA6 2 PRO A 293 THR A 301 -1 O LYS A 294 N THR A 287 SHEET 1 AA7 5 MET A 408 ILE A 412 0 SHEET 2 AA7 5 LEU A 399 GLU A 402 -1 N LEU A 399 O ILE A 412 SHEET 3 AA7 5 VAL A 436 GLN A 442 -1 O LEU A 441 N GLY A 400 SHEET 4 AA7 5 LYS A 452 LEU A 459 -1 O LEU A 459 N VAL A 436 SHEET 5 AA7 5 THR A 500 LYS A 502 -1 O THR A 500 N ASN A 458 SHEET 1 AA8 4 THR A 420 PHE A 426 0 SHEET 2 AA8 4 ILE A 472 ILE A 478 -1 O VAL A 474 N GLN A 424 SHEET 3 AA8 4 LEU A 484 ASP A 490 -1 O SER A 487 N THR A 475 SHEET 4 AA8 4 GLU A 496 GLN A 497 -1 O GLN A 497 N ALA A 488 SSBOND 1 CYS A 47 CYS A 529 1555 1555 2.04 LINK O1G ATP A 700 MG MG A 701 1555 1555 2.27 LINK O2B ATP A 700 MG MG A 701 1555 1555 2.15 LINK MG MG A 701 O HOH A 801 1555 1555 2.18 LINK MG MG A 701 O HOH A 803 1555 1555 1.95 LINK MG MG A 701 O HOH A 804 1555 1555 1.96 CISPEP 1 ILE A 418 PRO A 419 0 0.04 SITE 1 AC1 21 GLY A 10 THR A 11 THR A 12 ASN A 13 SITE 2 AC1 21 LYS A 70 GLY A 196 GLY A 197 GLY A 198 SITE 3 AC1 21 ALA A 199 GLY A 229 GLU A 267 LYS A 270 SITE 4 AC1 21 SER A 274 GLY A 341 GLY A 342 GLN A 343 SITE 5 AC1 21 ARG A 345 MG A 701 HOH A 802 HOH A 803 SITE 6 AC1 21 HOH A 804 SITE 1 AC2 6 GLU A 171 ATP A 700 HOH A 801 HOH A 802 SITE 2 AC2 6 HOH A 803 HOH A 804 CRYST1 127.246 127.246 252.885 90.00 90.00 120.00 P 62 2 2 12 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 0.007859 0.004537 0.000000 0.00000 SCALE2 0.000000 0.009075 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003954 0.00000 ATOM 1 N GLY A 2 52.174 29.470 -32.872 1.00157.64 N ANISOU 1 N GLY A 2 14440 22187 23270 -3177 5052 -3918 N ATOM 2 CA GLY A 2 51.039 29.462 -33.777 1.00154.02 C ANISOU 2 CA GLY A 2 14753 21396 22372 -3070 5251 -3630 C ATOM 3 C GLY A 2 49.975 30.468 -33.392 1.00153.96 C ANISOU 3 C GLY A 2 15383 21081 22033 -3243 5104 -3379 C ATOM 4 O GLY A 2 50.270 31.498 -32.790 1.00162.33 O ANISOU 4 O GLY A 2 16379 22121 23176 -3619 5101 -3460 O ATOM 5 N LYS A 3 48.730 30.170 -33.746 1.00125.08 N ANISOU 5 N LYS A 3 12331 17180 18014 -2968 4986 -3091 N ATOM 6 CA LYS A 3 47.596 31.023 -33.432 1.00119.79 C ANISOU 6 CA LYS A 3 12267 16209 17040 -3043 4836 -2839 C ATOM 7 C LYS A 3 46.638 30.267 -32.523 1.00115.72 C ANISOU 7 C LYS A 3 11846 15689 16435 -2620 4262 -2683 C ATOM 8 O LYS A 3 46.527 29.040 -32.599 1.00114.18 O ANISOU 8 O LYS A 3 11502 15609 16273 -2241 4075 -2674 O ATOM 9 CB LYS A 3 46.868 31.471 -34.703 1.00119.75 C ANISOU 9 CB LYS A 3 12933 15902 16665 -3115 5212 -2618 C ATOM 10 CG LYS A 3 46.691 32.973 -34.830 1.00120.63 C ANISOU 10 CG LYS A 3 13472 15731 16632 -3532 5474 -2526 C ATOM 11 CD LYS A 3 48.033 33.682 -34.840 1.00127.80 C ANISOU 11 CD LYS A 3 13976 16758 17822 -4024 5860 -2801 C ATOM 12 CE LYS A 3 47.875 35.154 -35.177 1.00130.33 C ANISOU 12 CE LYS A 3 14816 16732 17970 -4465 6214 -2696 C ATOM 13 NZ LYS A 3 49.183 35.864 -35.180 1.00137.59 N ANISOU 13 NZ LYS A 3 15342 17758 19179 -5005 6619 -2984 N ATOM 14 N ILE A 4 45.946 31.009 -31.664 1.00112.85 N ANISOU 14 N ILE A 4 11750 15171 15957 -2699 4015 -2570 N ATOM 15 CA ILE A 4 45.041 30.441 -30.672 1.00108.80 C ANISOU 15 CA ILE A 4 11337 14648 15355 -2366 3509 -2436 C ATOM 16 C ILE A 4 43.618 30.763 -31.104 1.00105.23 C ANISOU 16 C ILE A 4 11534 13885 14566 -2250 3520 -2152 C ATOM 17 O ILE A 4 43.188 31.921 -31.041 1.00105.30 O ANISOU 17 O ILE A 4 11895 13665 14452 -2474 3636 -2068 O ATOM 18 CB ILE A 4 45.328 30.982 -29.266 1.00109.54 C ANISOU 18 CB ILE A 4 11217 14830 15573 -2527 3203 -2554 C ATOM 19 CG1 ILE A 4 46.830 30.976 -28.991 1.00114.30 C ANISOU 19 CG1 ILE A 4 11167 15739 16523 -2744 3245 -2860 C ATOM 20 CG2 ILE A 4 44.614 30.146 -28.224 1.00106.20 C ANISOU 20 CG2 ILE A 4 10814 14459 15079 -2166 2698 -2449 C ATOM 21 CD1 ILE A 4 47.188 31.258 -27.549 1.00115.45 C ANISOU 21 CD1 ILE A 4 11042 16040 16783 -2851 2843 -3000 C ATOM 22 N ILE A 5 42.882 29.743 -31.536 1.00102.50 N ANISOU 22 N ILE A 5 11338 13522 14084 -1896 3391 -2013 N ATOM 23 CA ILE A 5 41.526 29.940 -32.031 1.00 99.58 C ANISOU 23 CA ILE A 5 11521 12901 13416 -1760 3371 -1758 C ATOM 24 C ILE A 5 40.556 29.913 -30.857 1.00 96.40 C ANISOU 24 C ILE A 5 11226 12437 12963 -1594 2976 -1651 C ATOM 25 O ILE A 5 40.837 29.341 -29.804 1.00 95.91 O ANISOU 25 O ILE A 5 10857 12543 13043 -1494 2684 -1743 O ATOM 26 CB ILE A 5 41.156 28.876 -33.079 1.00 98.61 C ANISOU 26 CB ILE A 5 11518 12791 13158 -1501 3420 -1684 C ATOM 27 CG1 ILE A 5 41.046 27.504 -32.418 1.00 96.69 C ANISOU 27 CG1 ILE A 5 11002 12706 13030 -1172 3066 -1723 C ATOM 28 CG2 ILE A 5 42.196 28.841 -34.179 1.00102.24 C ANISOU 28 CG2 ILE A 5 11851 13330 13666 -1668 3847 -1824 C ATOM 29 CD1 ILE A 5 40.627 26.406 -33.360 1.00 95.83 C ANISOU 29 CD1 ILE A 5 11032 12585 12796 -924 3093 -1673 C ATOM 30 N GLY A 6 39.395 30.535 -31.037 1.00 94.60 N ANISOU 30 N GLY A 6 11448 11968 12526 -1555 2969 -1454 N ATOM 31 CA GLY A 6 38.373 30.595 -30.004 1.00 91.93 C ANISOU 31 CA GLY A 6 11241 11553 12135 -1408 2665 -1357 C ATOM 32 C GLY A 6 37.173 29.727 -30.369 1.00 89.06 C ANISOU 32 C GLY A 6 11069 11146 11623 -1088 2490 -1185 C ATOM 33 O GLY A 6 36.635 29.833 -31.473 1.00 91.29 O ANISOU 33 O GLY A 6 11634 11310 11744 -1033 2622 -1057 O ATOM 34 N ILE A 7 36.760 28.887 -29.422 1.00 87.05 N ANISOU 34 N ILE A 7 10676 10987 11411 -899 2187 -1186 N ATOM 35 CA ILE A 7 35.717 27.891 -29.659 1.00 84.69 C ANISOU 35 CA ILE A 7 10491 10675 11013 -629 2013 -1063 C ATOM 36 C ILE A 7 34.635 28.025 -28.591 1.00 82.75 C ANISOU 36 C ILE A 7 10357 10355 10728 -540 1801 -980 C ATOM 37 O ILE A 7 34.883 27.775 -27.400 1.00 82.54 O ANISOU 37 O ILE A 7 10172 10417 10773 -545 1631 -1052 O ATOM 38 CB ILE A 7 36.276 26.465 -29.683 1.00 84.66 C ANISOU 38 CB ILE A 7 10223 10842 11101 -471 1898 -1146 C ATOM 39 CG1 ILE A 7 37.385 26.351 -30.730 1.00 87.08 C ANISOU 39 CG1 ILE A 7 10389 11229 11467 -556 2159 -1261 C ATOM 40 CG2 ILE A 7 35.166 25.480 -29.990 1.00 82.60 C ANISOU 40 CG2 ILE A 7 10118 10532 10732 -243 1747 -1032 C ATOM 41 CD1 ILE A 7 37.997 24.978 -30.821 1.00 87.63 C ANISOU 41 CD1 ILE A 7 10196 11442 11659 -370 2080 -1364 C ATOM 42 N ASP A 8 33.442 28.428 -29.021 1.00 81.76 N ANISOU 42 N ASP A 8 10506 10074 10484 -455 1812 -834 N ATOM 43 CA ASP A 8 32.221 28.334 -28.233 1.00 80.06 C ANISOU 43 CA ASP A 8 10377 9801 10242 -325 1642 -755 C ATOM 44 C ASP A 8 31.650 26.938 -28.435 1.00 78.60 C ANISOU 44 C ASP A 8 10129 9702 10035 -138 1475 -714 C ATOM 45 O ASP A 8 31.091 26.635 -29.495 1.00 78.44 O ANISOU 45 O ASP A 8 10222 9651 9932 -46 1485 -638 O ATOM 46 CB ASP A 8 31.221 29.413 -28.648 1.00 80.33 C ANISOU 46 CB ASP A 8 10684 9637 10203 -294 1726 -631 C ATOM 47 CG ASP A 8 29.884 29.293 -27.932 1.00 88.93 C ANISOU 47 CG ASP A 8 11814 10681 11296 -141 1585 -567 C ATOM 48 OD1 ASP A 8 29.808 28.585 -26.908 1.00104.67 O ANISOU 48 OD1 ASP A 8 13669 12772 13330 -123 1460 -625 O ATOM 49 OD2 ASP A 8 28.907 29.923 -28.393 1.00 87.78 O ANISOU 49 OD2 ASP A 8 11840 10397 11115 -36 1604 -456 O ATOM 50 N LEU A 9 31.808 26.089 -27.424 1.00 77.93 N ANISOU 50 N LEU A 9 9892 9713 10008 -94 1317 -766 N ATOM 51 CA LEU A 9 31.329 24.709 -27.447 1.00 76.91 C ANISOU 51 CA LEU A 9 9724 9628 9871 57 1168 -735 C ATOM 52 C LEU A 9 29.968 24.682 -26.761 1.00 75.77 C ANISOU 52 C LEU A 9 9681 9418 9692 112 1080 -655 C ATOM 53 O LEU A 9 29.872 24.555 -25.541 1.00 75.60 O ANISOU 53 O LEU A 9 9636 9411 9677 90 1003 -671 O ATOM 54 CB LEU A 9 32.330 23.791 -26.758 1.00 77.49 C ANISOU 54 CB LEU A 9 9606 9812 10024 88 1053 -819 C ATOM 55 CG LEU A 9 31.930 22.330 -26.564 1.00 76.89 C ANISOU 55 CG LEU A 9 9531 9735 9949 238 901 -785 C ATOM 56 CD1 LEU A 9 31.564 21.718 -27.897 1.00 76.71 C ANISOU 56 CD1 LEU A 9 9579 9675 9894 313 962 -772 C ATOM 57 CD2 LEU A 9 33.059 21.556 -25.912 1.00 78.15 C ANISOU 57 CD2 LEU A 9 9515 9982 10196 306 775 -853 C ATOM 58 N GLY A 10 28.905 24.794 -27.555 1.00 75.41 N ANISOU 58 N GLY A 10 9741 9309 9601 180 1092 -576 N ATOM 59 CA GLY A 10 27.576 24.915 -27.003 1.00 81.78 C ANISOU 59 CA GLY A 10 10591 10066 10416 228 1044 -519 C ATOM 60 C GLY A 10 26.887 23.583 -26.773 1.00 78.90 C ANISOU 60 C GLY A 10 10178 9737 10062 283 924 -509 C ATOM 61 O GLY A 10 27.283 22.547 -27.301 1.00 74.25 O ANISOU 61 O GLY A 10 9565 9184 9464 312 866 -532 O ATOM 62 N THR A 11 25.840 23.631 -25.946 1.00 79.49 N ANISOU 62 N THR A 11 10250 9787 10167 284 918 -487 N ATOM 63 CA THR A 11 24.982 22.466 -25.774 1.00 74.03 C ANISOU 63 CA THR A 11 9524 9108 9495 295 843 -476 C ATOM 64 C THR A 11 24.280 22.116 -27.077 1.00 74.32 C ANISOU 64 C THR A 11 9542 9160 9535 350 774 -458 C ATOM 65 O THR A 11 24.119 20.937 -27.410 1.00 74.41 O ANISOU 65 O THR A 11 9550 9181 9543 338 698 -480 O ATOM 66 CB THR A 11 23.962 22.734 -24.667 1.00 74.35 C ANISOU 66 CB THR A 11 9552 9126 9574 259 908 -472 C ATOM 67 OG1 THR A 11 24.650 23.048 -23.454 1.00 74.44 O ANISOU 67 OG1 THR A 11 9627 9127 9529 192 956 -499 O ATOM 68 CG2 THR A 11 23.084 21.525 -24.436 1.00 74.66 C ANISOU 68 CG2 THR A 11 9556 9169 9642 220 871 -468 C ATOM 69 N THR A 12 23.883 23.134 -27.838 1.00 74.84 N ANISOU 69 N THR A 12 9627 9214 9593 411 786 -418 N ATOM 70 CA THR A 12 23.119 22.979 -29.067 1.00 75.67 C ANISOU 70 CA THR A 12 9734 9350 9669 475 677 -391 C ATOM 71 C THR A 12 23.919 23.320 -30.315 1.00 76.13 C ANISOU 71 C THR A 12 9929 9402 9596 501 683 -368 C ATOM 72 O THR A 12 23.904 22.558 -31.283 1.00 76.65 O ANISOU 72 O THR A 12 10042 9506 9575 502 600 -394 O ATOM 73 CB THR A 12 21.862 23.856 -29.008 1.00 76.72 C ANISOU 73 CB THR A 12 9792 9473 9885 565 652 -343 C ATOM 74 OG1 THR A 12 21.006 23.394 -27.959 1.00 76.77 O ANISOU 74 OG1 THR A 12 9652 9502 10014 519 680 -385 O ATOM 75 CG2 THR A 12 21.110 23.796 -30.318 1.00 78.14 C ANISOU 75 CG2 THR A 12 9972 9703 10015 650 480 -305 C ATOM 76 N ASN A 13 24.613 24.453 -30.327 1.00 76.31 N ANISOU 76 N ASN A 13 10042 9364 9589 499 804 -332 N ATOM 77 CA ASN A 13 25.397 24.875 -31.478 1.00 77.20 C ANISOU 77 CA ASN A 13 10313 9455 9565 488 869 -306 C ATOM 78 C ASN A 13 26.792 25.289 -31.037 1.00 76.95 C ANISOU 78 C ASN A 13 10281 9401 9554 382 1045 -359 C ATOM 79 O ASN A 13 26.971 25.871 -29.964 1.00 76.52 O ANISOU 79 O ASN A 13 10172 9312 9591 336 1105 -377 O ATOM 80 CB ASN A 13 24.728 26.038 -32.212 1.00 78.74 C ANISOU 80 CB ASN A 13 10660 9568 9688 582 845 -184 C ATOM 81 CG ASN A 13 23.284 25.757 -32.555 1.00 79.55 C ANISOU 81 CG ASN A 13 10697 9720 9809 705 632 -140 C ATOM 82 OD1 ASN A 13 22.989 24.981 -33.462 1.00 80.24 O ANISOU 82 OD1 ASN A 13 10813 9886 9788 714 492 -156 O ATOM 83 ND2 ASN A 13 22.370 26.399 -31.837 1.00 85.48 N ANISOU 83 ND2 ASN A 13 11344 10429 10704 796 609 -105 N ATOM 84 N SER A 14 27.778 24.992 -31.875 1.00 77.59 N ANISOU 84 N SER A 14 10415 9515 9552 331 1134 -404 N ATOM 85 CA SER A 14 29.154 25.391 -31.636 1.00 78.02 C ANISOU 85 CA SER A 14 10421 9577 9648 214 1311 -476 C ATOM 86 C SER A 14 29.577 26.422 -32.672 1.00 79.78 C ANISOU 86 C SER A 14 10846 9721 9746 143 1488 -421 C ATOM 87 O SER A 14 28.947 26.578 -33.721 1.00 80.74 O ANISOU 87 O SER A 14 11171 9799 9709 207 1453 -327 O ATOM 88 CB SER A 14 30.105 24.192 -31.669 1.00 77.98 C ANISOU 88 CB SER A 14 10267 9672 9691 209 1322 -597 C ATOM 89 OG SER A 14 29.918 23.370 -30.533 1.00 76.80 O ANISOU 89 OG SER A 14 9969 9559 9653 257 1178 -630 O ATOM 90 N CYS A 15 30.668 27.117 -32.369 1.00 80.60 N ANISOU 90 N CYS A 15 10906 9806 9911 -5 1674 -482 N ATOM 91 CA CYS A 15 31.069 28.267 -33.162 1.00 82.61 C ANISOU 91 CA CYS A 15 11386 9943 10062 -120 1888 -421 C ATOM 92 C CYS A 15 32.557 28.490 -32.954 1.00 83.82 C ANISOU 92 C CYS A 15 11381 10152 10315 -325 2109 -563 C ATOM 93 O CYS A 15 33.050 28.330 -31.840 1.00 83.12 O ANISOU 93 O CYS A 15 11045 10144 10395 -374 2052 -671 O ATOM 94 CB CYS A 15 30.267 29.502 -32.743 1.00 82.89 C ANISOU 94 CB CYS A 15 11592 9798 10102 -93 1870 -303 C ATOM 95 SG CYS A 15 30.409 30.919 -33.819 1.00 91.37 S ANISOU 95 SG CYS A 15 13063 10645 11008 -180 2092 -161 S ATOM 96 N VAL A 16 33.270 28.848 -34.017 1.00 86.03 N ANISOU 96 N VAL A 16 11800 10401 10487 -453 2358 -568 N ATOM 97 CA VAL A 16 34.701 29.116 -33.927 1.00 87.86 C ANISOU 97 CA VAL A 16 11845 10699 10840 -678 2609 -722 C ATOM 98 C VAL A 16 34.993 30.471 -34.553 1.00 90.45 C ANISOU 98 C VAL A 16 12465 10840 11060 -889 2895 -647 C ATOM 99 O VAL A 16 34.536 30.763 -35.664 1.00 91.69 O ANISOU 99 O VAL A 16 12978 10876 10982 -857 2981 -503 O ATOM 100 CB VAL A 16 35.547 28.009 -34.588 1.00 88.76 C ANISOU 100 CB VAL A 16 11771 10983 10972 -660 2715 -859 C ATOM 101 CG1 VAL A 16 35.138 27.789 -36.034 1.00 89.88 C ANISOU 101 CG1 VAL A 16 12239 11068 10842 -608 2819 -770 C ATOM 102 CG2 VAL A 16 37.026 28.346 -34.498 1.00 91.25 C ANISOU 102 CG2 VAL A 16 11826 11389 11455 -895 2989 -1037 C ATOM 103 N ALA A 17 35.737 31.302 -33.831 1.00 91.61 N ANISOU 103 N ALA A 17 12493 10951 11363 -1114 3028 -744 N ATOM 104 CA ALA A 17 36.163 32.601 -34.320 1.00 94.54 C ANISOU 104 CA ALA A 17 13136 11119 11668 -1372 3342 -699 C ATOM 105 C ALA A 17 37.656 32.744 -34.080 1.00 96.87 C ANISOU 105 C ALA A 17 13105 11544 12157 -1681 3591 -927 C ATOM 106 O ALA A 17 38.216 32.135 -33.164 1.00 96.03 O ANISOU 106 O ALA A 17 12568 11652 12266 -1675 3440 -1103 O ATOM 107 CB ALA A 17 35.404 33.745 -33.637 1.00 94.34 C ANISOU 107 CB ALA A 17 13352 10844 11648 -1373 3270 -591 C ATOM 108 N ILE A 18 38.306 33.550 -34.916 1.00100.26 N ANISOU 108 N ILE A 18 13741 11845 12508 -1955 3973 -922 N ATOM 109 CA ILE A 18 39.748 33.729 -34.841 1.00103.25 C ANISOU 109 CA ILE A 18 13787 12358 13087 -2289 4265 -1155 C ATOM 110 C ILE A 18 40.072 35.214 -34.921 1.00106.44 C ANISOU 110 C ILE A 18 14479 12491 13473 -2650 4576 -1131 C ATOM 111 O ILE A 18 39.204 36.059 -35.157 1.00106.49 O ANISOU 111 O ILE A 18 14981 12187 13292 -2604 4581 -914 O ATOM 112 CB ILE A 18 40.500 32.951 -35.942 1.00105.18 C ANISOU 112 CB ILE A 18 13908 12770 13286 -2317 4531 -1244 C ATOM 113 CG1 ILE A 18 40.026 33.370 -37.335 1.00106.89 C ANISOU 113 CG1 ILE A 18 14702 12764 13146 -2339 4783 -1032 C ATOM 114 CG2 ILE A 18 40.316 31.459 -35.749 1.00102.50 C ANISOU 114 CG2 ILE A 18 13256 12675 13015 -1980 4236 -1309 C ATOM 115 CD1 ILE A 18 40.935 34.366 -38.021 1.00111.58 C ANISOU 115 CD1 ILE A 18 15480 13219 13694 -2757 5300 -1069 C ATOM 116 N MET A 19 41.354 35.519 -34.730 1.00109.57 N ANISOU 116 N MET A 19 14547 13001 14083 -3011 4840 -1365 N ATOM 117 CA MET A 19 41.833 36.898 -34.703 1.00113.16 C ANISOU 117 CA MET A 19 15218 13208 14571 -3431 5164 -1397 C ATOM 118 C MET A 19 42.583 37.195 -35.996 1.00117.36 C ANISOU 118 C MET A 19 15928 13672 14990 -3722 5685 -1396 C ATOM 119 O MET A 19 43.805 37.081 -36.082 1.00120.44 O ANISOU 119 O MET A 19 15906 14267 15590 -4022 5963 -1642 O ATOM 120 CB MET A 19 42.705 37.142 -33.480 1.00114.31 C ANISOU 120 CB MET A 19 14873 13520 15039 -3693 5083 -1683 C ATOM 121 CG MET A 19 41.929 37.517 -32.245 1.00111.80 C ANISOU 121 CG MET A 19 14640 13093 14746 -3568 4721 -1654 C ATOM 122 SD MET A 19 40.974 39.027 -32.465 1.00118.71 S ANISOU 122 SD MET A 19 16272 13421 15413 -3647 4889 -1414 S ATOM 123 CE MET A 19 42.164 40.284 -32.019 1.00130.68 C ANISOU 123 CE MET A 19 17717 14803 17131 -4276 5235 -1671 C ATOM 124 N ASP A 20 41.819 37.558 -37.027 1.00128.65 N ANISOU 124 N ASP A 20 17982 14823 16077 -3620 5814 -1113 N ATOM 125 CA ASP A 20 42.370 38.419 -38.059 1.00132.30 C ANISOU 125 CA ASP A 20 18842 15051 16374 -3993 6348 -1050 C ATOM 126 C ASP A 20 42.947 39.634 -37.357 1.00134.46 C ANISOU 126 C ASP A 20 19112 15124 16852 -4424 6550 -1173 C ATOM 127 O ASP A 20 42.256 40.278 -36.563 1.00146.13 O ANISOU 127 O ASP A 20 20784 16382 18357 -4340 6307 -1091 O ATOM 128 CB ASP A 20 41.290 38.843 -39.057 1.00128.36 C ANISOU 128 CB ASP A 20 19110 14212 15448 -3789 6355 -680 C ATOM 129 CG ASP A 20 41.266 37.987 -40.302 1.00123.51 C ANISOU 129 CG ASP A 20 18642 13736 14550 -3647 6475 -605 C ATOM 130 OD1 ASP A 20 42.287 37.329 -40.590 1.00125.08 O ANISOU 130 OD1 ASP A 20 18436 14214 14875 -3817 6741 -843 O ATOM 131 OD2 ASP A 20 40.230 37.985 -41.003 1.00122.80 O ANISOU 131 OD2 ASP A 20 19072 13477 14111 -3365 6305 -319 O ATOM 132 N GLY A 21 44.224 39.909 -37.611 1.00129.99 N ANISOU 132 N GLY A 21 18289 14649 16450 -4893 6999 -1400 N ATOM 133 CA GLY A 21 44.930 40.977 -36.932 1.00133.34 C ANISOU 133 CA GLY A 21 18620 14932 17110 -5375 7208 -1583 C ATOM 134 C GLY A 21 44.088 42.212 -36.689 1.00133.69 C ANISOU 134 C GLY A 21 19324 14472 17001 -5405 7179 -1358 C ATOM 135 O GLY A 21 43.653 42.873 -37.638 1.00135.89 O ANISOU 135 O GLY A 21 20289 14371 16974 -5434 7443 -1080 O ATOM 136 N THR A 22 43.816 42.492 -35.415 1.00131.71 N ANISOU 136 N THR A 22 18893 14209 16943 -5361 6842 -1471 N ATOM 137 CA THR A 22 43.051 43.610 -34.876 1.00138.18 C ANISOU 137 CA THR A 22 20221 14580 17701 -5362 6766 -1338 C ATOM 138 C THR A 22 41.537 43.433 -35.037 1.00132.64 C ANISOU 138 C THR A 22 19959 13692 16747 -4781 6417 -999 C ATOM 139 O THR A 22 40.784 44.181 -34.414 1.00132.93 O ANISOU 139 O THR A 22 20315 13414 16780 -4671 6271 -915 O ATOM 140 CB THR A 22 43.449 44.973 -35.479 1.00153.51 C ANISOU 140 CB THR A 22 22727 16040 19558 -5843 7300 -1266 C ATOM 141 OG1 THR A 22 43.140 44.992 -36.878 1.00164.56 O ANISOU 141 OG1 THR A 22 24663 17243 20619 -5740 7563 -956 O ATOM 142 CG2 THR A 22 44.938 45.234 -35.282 1.00155.53 C ANISOU 142 CG2 THR A 22 22520 16474 20100 -6477 7669 -1631 C ATOM 143 N THR A 23 41.058 42.489 -35.844 1.00125.66 N ANISOU 143 N THR A 23 19096 12986 15663 -4415 6284 -823 N ATOM 144 CA THR A 23 39.610 42.337 -35.969 1.00122.46 C ANISOU 144 CA THR A 23 19051 12429 15049 -3887 5928 -527 C ATOM 145 C THR A 23 39.206 40.868 -35.967 1.00117.96 C ANISOU 145 C THR A 23 18074 12281 14464 -3483 5556 -540 C ATOM 146 O THR A 23 39.424 40.159 -36.956 1.00118.28 O ANISOU 146 O THR A 23 18109 12488 14345 -3430 5662 -488 O ATOM 147 CB THR A 23 39.091 43.014 -37.238 1.00125.70 C ANISOU 147 CB THR A 23 20207 12443 15111 -3829 6152 -181 C ATOM 148 OG1 THR A 23 40.043 42.857 -38.295 1.00128.79 O ANISOU 148 OG1 THR A 23 20645 12915 15374 -4148 6577 -211 O ATOM 149 CG2 THR A 23 38.842 44.491 -36.996 1.00132.35 C ANISOU 149 CG2 THR A 23 21591 12746 15950 -3995 6331 -68 C ATOM 150 N PRO A 24 38.619 40.376 -34.881 1.00114.06 N ANISOU 150 N PRO A 24 17269 11949 14119 -3211 5142 -614 N ATOM 151 CA PRO A 24 38.173 38.980 -34.852 1.00110.04 C ANISOU 151 CA PRO A 24 16420 11793 13595 -2838 4796 -615 C ATOM 152 C PRO A 24 37.018 38.742 -35.807 1.00109.00 C ANISOU 152 C PRO A 24 16702 11541 13173 -2466 4650 -313 C ATOM 153 O PRO A 24 36.181 39.619 -36.041 1.00110.11 O ANISOU 153 O PRO A 24 17330 11335 13174 -2342 4634 -87 O ATOM 154 CB PRO A 24 37.736 38.777 -33.400 1.00106.94 C ANISOU 154 CB PRO A 24 15724 11509 13401 -2685 4438 -737 C ATOM 155 CG PRO A 24 37.413 40.146 -32.922 1.00108.89 C ANISOU 155 CG PRO A 24 16342 11365 13667 -2820 4544 -692 C ATOM 156 CD PRO A 24 38.323 41.086 -33.628 1.00113.54 C ANISOU 156 CD PRO A 24 17191 11727 14223 -3249 5000 -708 C ATOM 157 N ARG A 25 36.982 37.534 -36.369 1.00113.79 N ANISOU 157 N ARG A 25 17110 12434 13692 -2279 4531 -319 N ATOM 158 CA ARG A 25 35.893 37.144 -37.251 1.00114.29 C ANISOU 158 CA ARG A 25 17501 12448 13477 -1934 4332 -72 C ATOM 159 C ARG A 25 35.523 35.689 -37.009 1.00110.70 C ANISOU 159 C ARG A 25 16648 12335 13078 -1653 3999 -159 C ATOM 160 O ARG A 25 36.381 34.853 -36.702 1.00110.31 O ANISOU 160 O ARG A 25 16154 12564 13196 -1749 4039 -382 O ATOM 161 CB ARG A 25 36.251 37.362 -38.733 1.00122.38 C ANISOU 161 CB ARG A 25 18953 13359 14186 -2072 4656 64 C ATOM 162 CG ARG A 25 36.110 38.814 -39.176 1.00135.69 C ANISOU 162 CG ARG A 25 21243 14605 15708 -2222 4897 279 C ATOM 163 CD ARG A 25 36.403 39.007 -40.651 1.00145.47 C ANISOU 163 CD ARG A 25 22978 15721 16574 -2354 5211 444 C ATOM 164 NE ARG A 25 36.407 40.425 -40.994 1.00157.32 N ANISOU 164 NE ARG A 25 25075 16765 17935 -2541 5483 647 N ATOM 165 CZ ARG A 25 36.725 40.910 -42.190 1.00168.26 C ANISOU 165 CZ ARG A 25 27014 17940 18977 -2728 5828 823 C ATOM 166 NH1 ARG A 25 37.068 40.091 -43.174 1.00168.72 N ANISOU 166 NH1 ARG A 25 27096 18223 18785 -2760 5957 800 N ATOM 167 NH2 ARG A 25 36.701 42.219 -42.400 1.00175.45 N ANISOU 167 NH2 ARG A 25 28493 18392 19780 -2890 6065 1020 N ATOM 168 N VAL A 26 34.231 35.412 -37.115 1.00100.70 N ANISOU 168 N VAL A 26 15536 11033 11693 -1304 3665 16 N ATOM 169 CA VAL A 26 33.712 34.053 -37.052 1.00 97.66 C ANISOU 169 CA VAL A 26 14870 10919 11317 -1047 3358 -34 C ATOM 170 C VAL A 26 33.850 33.417 -38.426 1.00 99.17 C ANISOU 170 C VAL A 26 15256 11192 11230 -1028 3452 15 C ATOM 171 O VAL A 26 33.689 34.079 -39.457 1.00116.52 O ANISOU 171 O VAL A 26 17927 13198 13146 -1066 3594 197 O ATOM 172 CB VAL A 26 32.247 34.060 -36.573 1.00 95.55 C ANISOU 172 CB VAL A 26 14654 10587 11063 -721 2983 105 C ATOM 173 CG1 VAL A 26 31.654 32.663 -36.608 1.00 92.94 C ANISOU 173 CG1 VAL A 26 14078 10509 10725 -496 2688 60 C ATOM 174 CG2 VAL A 26 32.155 34.641 -35.178 1.00 94.33 C ANISOU 174 CG2 VAL A 26 14319 10357 11165 -753 2934 23 C ATOM 175 N LEU A 27 34.157 32.124 -38.444 1.00 97.54 N ANISOU 175 N LEU A 27 14723 11255 11084 -967 3376 -148 N ATOM 176 CA LEU A 27 34.444 31.394 -39.671 1.00 99.15 C ANISOU 176 CA LEU A 27 15070 11558 11044 -975 3507 -171 C ATOM 177 C LEU A 27 33.273 30.491 -40.028 1.00 97.42 C ANISOU 177 C LEU A 27 14924 11422 10671 -681 3134 -92 C ATOM 178 O LEU A 27 32.780 29.743 -39.176 1.00 94.39 O ANISOU 178 O LEU A 27 14217 11159 10487 -518 2848 -165 O ATOM 179 CB LEU A 27 35.714 30.558 -39.509 1.00 99.33 C ANISOU 179 CB LEU A 27 14672 11805 11264 -1116 3729 -444 C ATOM 180 CG LEU A 27 36.854 31.253 -38.769 1.00100.52 C ANISOU 180 CG LEU A 27 14548 11957 11690 -1395 3992 -589 C ATOM 181 CD1 LEU A 27 38.064 30.340 -38.663 1.00101.21 C ANISOU 181 CD1 LEU A 27 14164 12295 11995 -1476 4165 -862 C ATOM 182 CD2 LEU A 27 37.221 32.549 -39.469 1.00104.23 C ANISOU 182 CD2 LEU A 27 15428 12192 11984 -1670 4361 -475 C ATOM 183 N GLU A 28 32.830 30.560 -41.282 1.00 99.74 N ANISOU 183 N GLU A 28 15655 11648 10596 -636 3135 51 N ATOM 184 CA GLU A 28 31.834 29.615 -41.759 1.00 98.82 C ANISOU 184 CA GLU A 28 15594 11640 10313 -408 2793 81 C ATOM 185 C GLU A 28 32.458 28.229 -41.887 1.00 98.00 C ANISOU 185 C GLU A 28 15214 11749 10274 -430 2867 -165 C ATOM 186 O GLU A 28 33.638 28.081 -42.213 1.00 99.66 O ANISOU 186 O GLU A 28 15362 12008 10496 -612 3237 -315 O ATOM 187 CB GLU A 28 31.255 30.066 -43.099 1.00102.17 C ANISOU 187 CB GLU A 28 16585 11948 10286 -364 2749 292 C ATOM 188 CG GLU A 28 30.475 31.377 -43.042 1.00103.46 C ANISOU 188 CG GLU A 28 17061 11871 10379 -261 2610 566 C ATOM 189 CD GLU A 28 29.889 31.771 -44.387 1.00107.30 C ANISOU 189 CD GLU A 28 18134 12246 10390 -180 2508 798 C ATOM 190 OE1 GLU A 28 30.218 31.112 -45.394 1.00109.16 O ANISOU 190 OE1 GLU A 28 18572 12587 10315 -264 2611 732 O ATOM 191 OE2 GLU A 28 29.098 32.738 -44.436 1.00121.23 O ANISOU 191 OE2 GLU A 28 20173 13811 12080 -20 2318 1045 O ATOM 192 N ASN A 29 31.657 27.201 -41.602 1.00 95.76 N ANISOU 192 N ASN A 29 14749 11580 10055 -242 2528 -219 N ATOM 193 CA ASN A 29 32.151 25.830 -41.693 1.00 95.17 C ANISOU 193 CA ASN A 29 14449 11660 10053 -229 2573 -447 C ATOM 194 C ASN A 29 32.145 25.353 -43.138 1.00 98.08 C ANISOU 194 C ASN A 29 15187 12050 10031 -259 2667 -479 C ATOM 195 O ASN A 29 32.033 26.163 -44.066 1.00100.88 O ANISOU 195 O ASN A 29 15971 12308 10050 -331 2769 -326 O ATOM 196 CB ASN A 29 31.339 24.878 -40.809 1.00 92.07 C ANISOU 196 CB ASN A 29 13758 11346 9878 -56 2212 -501 C ATOM 197 CG ASN A 29 29.851 24.910 -41.116 1.00 91.91 C ANISOU 197 CG ASN A 29 13928 11304 9688 85 1837 -350 C ATOM 198 OD1 ASN A 29 29.446 25.009 -42.273 1.00 94.34 O ANISOU 198 OD1 ASN A 29 14595 11597 9654 89 1785 -276 O ATOM 199 ND2 ASN A 29 29.027 24.821 -40.076 1.00 89.44 N ANISOU 199 ND2 ASN A 29 13369 11003 9611 196 1571 -313 N ATOM 200 N ALA A 30 32.270 24.039 -43.338 1.00102.32 N ANISOU 200 N ALA A 30 15599 12691 10586 -204 2640 -677 N ATOM 201 CA ALA A 30 32.288 23.505 -44.695 1.00110.84 C ANISOU 201 CA ALA A 30 17045 13792 11277 -246 2744 -750 C ATOM 202 C ALA A 30 30.995 23.827 -45.436 1.00102.07 C ANISOU 202 C ALA A 30 16336 12646 9799 -174 2394 -556 C ATOM 203 O ALA A 30 31.023 24.260 -46.594 1.00105.52 O ANISOU 203 O ALA A 30 17239 13041 9812 -255 2510 -473 O ATOM 204 CB ALA A 30 32.529 21.998 -44.660 1.00123.92 C ANISOU 204 CB ALA A 30 18495 15530 13057 -177 2740 -1009 C ATOM 205 N GLU A 31 29.853 23.645 -44.779 1.00 99.70 N ANISOU 205 N GLU A 31 15862 12370 9650 -24 1963 -479 N ATOM 206 CA GLU A 31 28.566 23.891 -45.413 1.00101.16 C ANISOU 206 CA GLU A 31 16333 12557 9546 73 1573 -315 C ATOM 207 C GLU A 31 28.244 25.371 -45.560 1.00102.56 C ANISOU 207 C GLU A 31 16770 12609 9591 109 1534 -30 C ATOM 208 O GLU A 31 27.157 25.700 -46.043 1.00104.19 O ANISOU 208 O GLU A 31 17194 12812 9581 235 1174 135 O ATOM 209 CB GLU A 31 27.444 23.207 -44.621 1.00 98.61 C ANISOU 209 CB GLU A 31 15678 12309 9478 208 1156 -349 C ATOM 210 CG GLU A 31 27.467 21.683 -44.654 1.00100.36 C ANISOU 210 CG GLU A 31 15756 12614 9762 181 1113 -604 C ATOM 211 CD GLU A 31 28.508 21.079 -43.725 1.00110.05 C ANISOU 211 CD GLU A 31 16634 13827 11352 154 1392 -772 C ATOM 212 OE1 GLU A 31 28.215 20.905 -42.522 1.00102.27 O ANISOU 212 OE1 GLU A 31 15300 12844 10716 219 1261 -763 O ATOM 213 OE2 GLU A 31 29.624 20.781 -44.199 1.00122.61 O ANISOU 213 OE2 GLU A 31 18303 15410 12874 75 1743 -913 O ATOM 214 N GLY A 32 29.142 26.265 -45.154 1.00102.38 N ANISOU 214 N GLY A 32 16724 12474 9700 7 1878 27 N ATOM 215 CA GLY A 32 28.871 27.684 -45.232 1.00103.93 C ANISOU 215 CA GLY A 32 17196 12496 9797 36 1872 293 C ATOM 216 C GLY A 32 28.077 28.258 -44.080 1.00101.42 C ANISOU 216 C GLY A 32 16596 12120 9819 198 1613 404 C ATOM 217 O GLY A 32 27.628 29.405 -44.175 1.00103.05 O ANISOU 217 O GLY A 32 17052 12158 9946 283 1540 635 O ATOM 218 N ASP A 33 27.875 27.499 -43.005 1.00 97.89 N ANISOU 218 N ASP A 33 15670 11788 9737 252 1485 250 N ATOM 219 CA ASP A 33 27.189 27.994 -41.821 1.00 95.63 C ANISOU 219 CA ASP A 33 15104 11453 9778 381 1302 320 C ATOM 220 C ASP A 33 28.217 28.557 -40.853 1.00 94.12 C ANISOU 220 C ASP A 33 14725 11181 9857 239 1625 259 C ATOM 221 O ASP A 33 29.302 27.992 -40.694 1.00 93.40 O ANISOU 221 O ASP A 33 14466 11168 9855 86 1878 80 O ATOM 222 CB ASP A 33 26.398 26.883 -41.126 1.00 93.06 C ANISOU 222 CB ASP A 33 14395 11287 9678 482 1012 190 C ATOM 223 CG ASP A 33 25.365 26.244 -42.023 1.00 94.77 C ANISOU 223 CG ASP A 33 14738 11609 9663 583 668 206 C ATOM 224 OD1 ASP A 33 24.896 26.907 -42.970 1.00 97.83 O ANISOU 224 OD1 ASP A 33 15479 11941 9752 662 530 379 O ATOM 225 OD2 ASP A 33 25.020 25.071 -41.768 1.00 93.38 O ANISOU 225 OD2 ASP A 33 14321 11563 9598 577 523 44 O ATOM 226 N ARG A 34 27.874 29.674 -40.208 1.00 94.04 N ANISOU 226 N ARG A 34 14734 11012 9985 298 1608 393 N ATOM 227 CA ARG A 34 28.762 30.224 -39.189 1.00 92.80 C ANISOU 227 CA ARG A 34 14388 10783 10087 146 1871 311 C ATOM 228 C ARG A 34 28.717 29.403 -37.908 1.00 89.41 C ANISOU 228 C ARG A 34 13492 10501 9977 172 1760 141 C ATOM 229 O ARG A 34 29.706 29.349 -37.169 1.00 88.40 O ANISOU 229 O ARG A 34 13144 10409 10034 21 1954 2 O ATOM 230 CB ARG A 34 28.390 31.674 -38.892 1.00 94.15 C ANISOU 230 CB ARG A 34 14772 10704 10295 194 1902 488 C ATOM 231 CG ARG A 34 28.324 32.564 -40.122 1.00107.44 C ANISOU 231 CG ARG A 34 16988 12192 11644 198 1983 707 C ATOM 232 CD ARG A 34 27.816 33.953 -39.774 1.00120.24 C ANISOU 232 CD ARG A 34 18832 13522 13332 303 1975 893 C ATOM 233 NE ARG A 34 28.712 34.652 -38.859 1.00125.10 N ANISOU 233 NE ARG A 34 19349 14008 14176 79 2286 790 N ATOM 234 CZ ARG A 34 29.560 35.606 -39.229 1.00128.04 C ANISOU 234 CZ ARG A 34 20045 14157 14449 -149 2630 849 C ATOM 235 NH1 ARG A 34 29.622 35.981 -40.498 1.00142.30 N ANISOU 235 NH1 ARG A 34 22333 15828 15905 -171 2725 1035 N ATOM 236 NH2 ARG A 34 30.341 36.190 -38.330 1.00114.41 N ANISOU 236 NH2 ARG A 34 18181 12336 12953 -378 2881 719 N ATOM 237 N THR A 35 27.585 28.761 -37.632 1.00 88.05 N ANISOU 237 N THR A 35 13171 10417 9866 352 1447 149 N ATOM 238 CA THR A 35 27.387 27.968 -36.428 1.00 85.25 C ANISOU 238 CA THR A 35 12440 10177 9776 379 1338 18 C ATOM 239 C THR A 35 27.173 26.515 -36.819 1.00 84.58 C ANISOU 239 C THR A 35 12245 10251 9640 408 1192 -89 C ATOM 240 O THR A 35 26.364 26.216 -37.704 1.00 85.85 O ANISOU 240 O THR A 35 12549 10446 9623 495 1001 -33 O ATOM 241 CB THR A 35 26.190 28.476 -35.630 1.00 84.63 C ANISOU 241 CB THR A 35 12265 10040 9849 533 1149 100 C ATOM 242 OG1 THR A 35 24.980 28.041 -36.261 1.00 85.46 O ANISOU 242 OG1 THR A 35 12393 10212 9865 694 867 166 O ATOM 243 CG2 THR A 35 26.202 29.992 -35.583 1.00 86.25 C ANISOU 243 CG2 THR A 35 12693 10031 10049 549 1274 232 C ATOM 244 N THR A 36 27.885 25.628 -36.164 1.00 82.99 N ANISOU 244 N THR A 36 11807 10135 9591 339 1265 -244 N ATOM 245 CA THR A 36 27.793 24.212 -36.464 1.00 82.60 C ANISOU 245 CA THR A 36 11678 10189 9518 361 1164 -361 C ATOM 246 C THR A 36 27.016 23.502 -35.375 1.00 80.69 C ANISOU 246 C THR A 36 11195 9985 9477 421 973 -396 C ATOM 247 O THR A 36 27.346 23.656 -34.193 1.00 79.29 O ANISOU 247 O THR A 36 10843 9799 9487 399 1023 -418 O ATOM 248 CB THR A 36 29.184 23.605 -36.578 1.00 82.86 C ANISOU 248 CB THR A 36 11634 10265 9585 273 1392 -511 C ATOM 249 OG1 THR A 36 29.979 24.410 -37.451 1.00 87.14 O ANISOU 249 OG1 THR A 36 12378 10765 9965 174 1641 -485 O ATOM 250 CG2 THR A 36 29.099 22.199 -37.126 1.00 83.19 C ANISOU 250 CG2 THR A 36 11681 10363 9565 310 1320 -634 C ATOM 251 N PRO A 37 25.984 22.739 -35.722 1.00 80.94 N ANISOU 251 N PRO A 37 11226 10062 9463 473 760 -407 N ATOM 252 CA PRO A 37 25.267 21.962 -34.708 1.00 79.54 C ANISOU 252 CA PRO A 37 10835 9912 9476 487 626 -452 C ATOM 253 C PRO A 37 26.213 21.057 -33.939 1.00 78.38 C ANISOU 253 C PRO A 37 10567 9759 9455 444 731 -560 C ATOM 254 O PRO A 37 27.179 20.530 -34.490 1.00 79.01 O ANISOU 254 O PRO A 37 10700 9841 9477 426 845 -648 O ATOM 255 CB PRO A 37 24.264 21.155 -35.532 1.00 80.79 C ANISOU 255 CB PRO A 37 11041 10123 9531 495 417 -489 C ATOM 256 CG PRO A 37 24.037 21.978 -36.732 1.00 82.77 C ANISOU 256 CG PRO A 37 11513 10382 9553 542 358 -397 C ATOM 257 CD PRO A 37 25.335 22.660 -37.038 1.00 82.97 C ANISOU 257 CD PRO A 37 11694 10349 9482 504 618 -373 C ATOM 258 N SER A 38 25.934 20.894 -32.647 1.00 78.18 N ANISOU 258 N SER A 38 10385 9722 9600 441 697 -552 N ATOM 259 CA SER A 38 26.758 20.064 -31.768 1.00 76.36 C ANISOU 259 CA SER A 38 10058 9476 9480 430 744 -622 C ATOM 260 C SER A 38 26.190 18.647 -31.687 1.00 76.54 C ANISOU 260 C SER A 38 10082 9465 9536 424 637 -679 C ATOM 261 O SER A 38 25.828 18.143 -30.624 1.00 77.16 O ANISOU 261 O SER A 38 10097 9507 9714 404 594 -664 O ATOM 262 CB SER A 38 26.861 20.694 -30.385 1.00 77.91 C ANISOU 262 CB SER A 38 10150 9664 9786 412 770 -577 C ATOM 263 OG SER A 38 27.316 22.033 -30.458 1.00 82.34 O ANISOU 263 OG SER A 38 10734 10225 10325 388 877 -539 O ATOM 264 N ILE A 39 26.124 18.006 -32.851 1.00 77.69 N ANISOU 264 N ILE A 39 10338 9607 9574 422 612 -751 N ATOM 265 CA ILE A 39 25.585 16.661 -32.999 1.00 78.41 C ANISOU 265 CA ILE A 39 10475 9638 9679 386 523 -833 C ATOM 266 C ILE A 39 26.659 15.777 -33.610 1.00 79.44 C ANISOU 266 C ILE A 39 10700 9708 9775 434 622 -953 C ATOM 267 O ILE A 39 27.394 16.210 -34.503 1.00 80.19 O ANISOU 267 O ILE A 39 10862 9846 9760 460 736 -992 O ATOM 268 CB ILE A 39 24.320 16.656 -33.876 1.00 79.53 C ANISOU 268 CB ILE A 39 10667 9832 9719 324 370 -845 C ATOM 269 CG1 ILE A 39 23.366 17.764 -33.435 1.00 79.04 C ANISOU 269 CG1 ILE A 39 10480 9843 9709 333 294 -729 C ATOM 270 CG2 ILE A 39 23.636 15.313 -33.806 1.00 80.44 C ANISOU 270 CG2 ILE A 39 10802 9876 9887 231 282 -941 C ATOM 271 CD1 ILE A 39 22.077 17.806 -34.222 1.00 80.65 C ANISOU 271 CD1 ILE A 39 10667 10126 9852 303 95 -738 C ATOM 272 N ILE A 40 26.752 14.538 -33.130 1.00 79.85 N ANISOU 272 N ILE A 40 10775 9642 9924 447 604 -1012 N ATOM 273 CA ILE A 40 27.823 13.626 -33.519 1.00 81.16 C ANISOU 273 CA ILE A 40 11009 9715 10113 542 709 -1133 C ATOM 274 C ILE A 40 27.206 12.272 -33.828 1.00 82.58 C ANISOU 274 C ILE A 40 11346 9743 10287 489 647 -1234 C ATOM 275 O ILE A 40 26.625 11.638 -32.943 1.00 82.42 O ANISOU 275 O ILE A 40 11333 9616 10367 442 570 -1187 O ATOM 276 CB ILE A 40 28.895 13.483 -32.426 1.00 80.84 C ANISOU 276 CB ILE A 40 10838 9638 10238 670 751 -1096 C ATOM 277 CG1 ILE A 40 29.447 14.850 -32.015 1.00 79.68 C ANISOU 277 CG1 ILE A 40 10529 9639 10107 672 800 -1016 C ATOM 278 CG2 ILE A 40 30.017 12.572 -32.902 1.00 82.74 C ANISOU 278 CG2 ILE A 40 11107 9789 10542 816 862 -1232 C ATOM 279 CD1 ILE A 40 28.623 15.567 -30.948 1.00 78.08 C ANISOU 279 CD1 ILE A 40 10269 9473 9924 594 702 -882 C ATOM 280 N ALA A 41 27.346 11.822 -35.069 1.00 84.31 N ANISOU 280 N ALA A 41 11722 9936 10374 476 703 -1381 N ATOM 281 CA ALA A 41 26.780 10.561 -35.518 1.00 86.14 C ANISOU 281 CA ALA A 41 12139 10011 10578 395 656 -1516 C ATOM 282 C ALA A 41 27.892 9.588 -35.874 1.00 88.02 C ANISOU 282 C ALA A 41 12496 10084 10866 540 819 -1667 C ATOM 283 O ALA A 41 28.931 9.987 -36.411 1.00 88.54 O ANISOU 283 O ALA A 41 12525 10220 10895 655 981 -1723 O ATOM 284 CB ALA A 41 25.870 10.767 -36.726 1.00 87.31 C ANISOU 284 CB ALA A 41 12411 10259 10503 242 554 -1597 C ATOM 285 N TYR A 42 27.664 8.311 -35.582 1.00 89.45 N ANISOU 285 N TYR A 42 12818 10028 11140 531 797 -1738 N ATOM 286 CA TYR A 42 28.598 7.244 -35.921 1.00 91.84 C ANISOU 286 CA TYR A 42 13264 10117 11513 693 947 -1897 C ATOM 287 C TYR A 42 27.908 6.305 -36.902 1.00 94.26 C ANISOU 287 C TYR A 42 13855 10274 11686 532 943 -2099 C ATOM 288 O TYR A 42 26.991 5.567 -36.525 1.00 94.88 O ANISOU 288 O TYR A 42 14047 10195 11808 375 833 -2102 O ATOM 289 CB TYR A 42 29.064 6.510 -34.668 1.00 92.08 C ANISOU 289 CB TYR A 42 13270 9941 11777 860 926 -1798 C ATOM 290 CG TYR A 42 29.861 7.389 -33.738 1.00 90.31 C ANISOU 290 CG TYR A 42 12773 9875 11664 1018 907 -1633 C ATOM 291 CD1 TYR A 42 31.139 7.808 -34.078 1.00 90.91 C ANISOU 291 CD1 TYR A 42 12680 10062 11799 1209 1045 -1699 C ATOM 292 CD2 TYR A 42 29.335 7.810 -32.527 1.00 88.42 C ANISOU 292 CD2 TYR A 42 12444 9683 11469 951 767 -1434 C ATOM 293 CE1 TYR A 42 31.871 8.615 -33.238 1.00 89.70 C ANISOU 293 CE1 TYR A 42 12262 10067 11754 1317 1011 -1575 C ATOM 294 CE2 TYR A 42 30.061 8.615 -31.676 1.00 87.15 C ANISOU 294 CE2 TYR A 42 12061 9668 11385 1071 735 -1307 C ATOM 295 CZ TYR A 42 31.328 9.016 -32.037 1.00 87.80 C ANISOU 295 CZ TYR A 42 11964 9864 11532 1247 840 -1381 C ATOM 296 OH TYR A 42 32.056 9.822 -31.195 1.00 86.93 O ANISOU 296 OH TYR A 42 11615 9910 11505 1332 790 -1281 O ATOM 297 N THR A 43 28.344 6.346 -38.157 1.00 95.97 N ANISOU 297 N THR A 43 14198 10541 11725 544 1077 -2281 N ATOM 298 CA THR A 43 27.712 5.585 -39.219 1.00 98.61 C ANISOU 298 CA THR A 43 14826 10770 11870 367 1063 -2502 C ATOM 299 C THR A 43 28.085 4.112 -39.122 1.00101.33 C ANISOU 299 C THR A 43 15391 10751 12360 455 1181 -2668 C ATOM 300 O THR A 43 28.992 3.715 -38.388 1.00101.50 O ANISOU 300 O THR A 43 15337 10614 12615 709 1288 -2615 O ATOM 301 CB THR A 43 28.116 6.129 -40.586 1.00 99.98 C ANISOU 301 CB THR A 43 15120 11110 11759 352 1191 -2641 C ATOM 302 OG1 THR A 43 29.537 6.315 -40.627 1.00100.38 O ANISOU 302 OG1 THR A 43 15070 11163 11906 598 1464 -2673 O ATOM 303 CG2 THR A 43 27.432 7.452 -40.850 1.00 98.15 C ANISOU 303 CG2 THR A 43 14779 11181 11332 221 1022 -2483 C ATOM 304 N GLN A 44 27.361 3.294 -39.885 1.00103.91 N ANISOU 304 N GLN A 44 16004 10934 12543 246 1143 -2876 N ATOM 305 CA GLN A 44 27.702 1.880 -39.977 1.00107.16 C ANISOU 305 CA GLN A 44 16696 10954 13064 315 1286 -3073 C ATOM 306 C GLN A 44 29.043 1.677 -40.665 1.00109.26 C ANISOU 306 C GLN A 44 17035 11151 13328 591 1580 -3250 C ATOM 307 O GLN A 44 29.774 0.737 -40.333 1.00111.35 O ANISOU 307 O GLN A 44 17393 11102 13811 825 1732 -3325 O ATOM 308 CB GLN A 44 26.604 1.122 -40.722 1.00111.35 C ANISOU 308 CB GLN A 44 17526 11363 13420 -21 1181 -3293 C ATOM 309 CG GLN A 44 26.712 -0.383 -40.605 1.00125.46 C ANISOU 309 CG GLN A 44 19634 12681 15352 -10 1303 -3472 C ATOM 310 CD GLN A 44 26.651 -0.844 -39.167 1.00138.13 C ANISOU 310 CD GLN A 44 21171 14052 17260 76 1260 -3246 C ATOM 311 OE1 GLN A 44 25.715 -0.516 -38.438 1.00144.30 O ANISOU 311 OE1 GLN A 44 21803 14941 18082 -134 1076 -3068 O ATOM 312 NE2 GLN A 44 27.661 -1.594 -38.741 1.00141.36 N ANISOU 312 NE2 GLN A 44 21692 14140 17880 400 1433 -3249 N ATOM 313 N ASP A 45 29.386 2.555 -41.606 1.00126.81 N ANISOU 313 N ASP A 45 19217 13652 15314 577 1677 -3313 N ATOM 314 CA ASP A 45 30.562 2.373 -42.443 1.00132.69 C ANISOU 314 CA ASP A 45 20050 14354 16013 776 2009 -3529 C ATOM 315 C ASP A 45 31.856 2.808 -41.771 1.00123.93 C ANISOU 315 C ASP A 45 18594 13311 15182 1111 2178 -3410 C ATOM 316 O ASP A 45 32.928 2.615 -42.353 1.00129.78 O ANISOU 316 O ASP A 45 19335 14016 15961 1307 2488 -3598 O ATOM 317 CB ASP A 45 30.382 3.141 -43.751 1.00144.90 C ANISOU 317 CB ASP A 45 21743 16164 17148 588 2067 -3639 C ATOM 318 CG ASP A 45 28.995 2.973 -44.336 1.00156.73 C ANISOU 318 CG ASP A 45 23500 17696 18356 242 1794 -3709 C ATOM 319 OD1 ASP A 45 28.289 3.992 -44.484 1.00154.72 O ANISOU 319 OD1 ASP A 45 23147 17731 17907 81 1571 -3545 O ATOM 320 OD2 ASP A 45 28.611 1.826 -44.645 1.00166.09 O ANISOU 320 OD2 ASP A 45 24978 18612 19518 133 1793 -3936 O ATOM 321 N GLY A 46 31.791 3.387 -40.577 1.00107.50 N ANISOU 321 N GLY A 46 16209 11340 13297 1171 1990 -3125 N ATOM 322 CA GLY A 46 32.981 3.794 -39.858 1.00106.84 C ANISOU 322 CA GLY A 46 15775 11337 13481 1465 2090 -3018 C ATOM 323 C GLY A 46 33.297 5.274 -39.909 1.00104.41 C ANISOU 323 C GLY A 46 15186 11399 13086 1406 2115 -2882 C ATOM 324 O GLY A 46 34.228 5.713 -39.224 1.00103.80 O ANISOU 324 O GLY A 46 14778 11423 13238 1603 2162 -2789 O ATOM 325 N CYS A 47 32.557 6.048 -40.698 1.00113.92 N ANISOU 325 N CYS A 47 16522 12796 13967 1142 2070 -2869 N ATOM 326 CA CYS A 47 32.729 7.489 -40.740 1.00113.34 C ANISOU 326 CA CYS A 47 16247 13026 13793 1065 2083 -2715 C ATOM 327 C CYS A 47 32.208 8.123 -39.453 1.00 98.75 C ANISOU 327 C CYS A 47 14163 11266 12093 1038 1808 -2436 C ATOM 328 O CYS A 47 31.577 7.476 -38.612 1.00 96.87 O ANISOU 328 O CYS A 47 13947 10876 11985 1039 1606 -2355 O ATOM 329 CB CYS A 47 32.002 8.082 -41.946 1.00134.41 C ANISOU 329 CB CYS A 47 19184 15835 16050 818 2072 -2756 C ATOM 330 SG CYS A 47 32.523 7.377 -43.526 1.00158.63 S ANISOU 330 SG CYS A 47 22614 18809 18848 801 2408 -3101 S ATOM 331 N THR A 48 32.473 9.418 -39.311 1.00114.39 N ANISOU 331 N THR A 48 15945 13478 14039 996 1829 -2295 N ATOM 332 CA THR A 48 31.966 10.199 -38.194 1.00110.23 C ANISOU 332 CA THR A 48 15222 13052 13608 949 1604 -2052 C ATOM 333 C THR A 48 31.382 11.489 -38.744 1.00118.68 C ANISOU 333 C THR A 48 16342 14319 14433 768 1565 -1943 C ATOM 334 O THR A 48 32.065 12.225 -39.461 1.00137.42 O ANISOU 334 O THR A 48 18718 16807 16687 747 1777 -1980 O ATOM 335 CB THR A 48 33.069 10.495 -37.181 1.00107.26 C ANISOU 335 CB THR A 48 14517 12727 13510 1128 1654 -1983 C ATOM 336 OG1 THR A 48 33.644 9.261 -36.736 1.00110.98 O ANISOU 336 OG1 THR A 48 14964 12998 14205 1346 1667 -2074 O ATOM 337 CG2 THR A 48 32.503 11.231 -35.988 1.00106.63 C ANISOU 337 CG2 THR A 48 14288 12728 13497 1065 1427 -1755 C ATOM 338 N LEU A 49 30.120 11.750 -38.428 1.00 89.85 N ANISOU 338 N LEU A 49 12736 10692 10709 641 1310 -1811 N ATOM 339 CA LEU A 49 29.427 12.936 -38.908 1.00 89.05 C ANISOU 339 CA LEU A 49 12691 10750 10393 512 1222 -1689 C ATOM 340 C LEU A 49 29.287 13.939 -37.775 1.00 86.43 C ANISOU 340 C LEU A 49 12123 10501 10216 524 1130 -1486 C ATOM 341 O LEU A 49 28.964 13.568 -36.647 1.00 85.03 O ANISOU 341 O LEU A 49 11811 10265 10233 554 1005 -1420 O ATOM 342 CB LEU A 49 28.048 12.581 -39.460 1.00 89.73 C ANISOU 342 CB LEU A 49 12965 10830 10298 374 986 -1710 C ATOM 343 CG LEU A 49 28.058 12.132 -40.919 1.00 92.71 C ANISOU 343 CG LEU A 49 13629 11124 10472 323 1054 -1937 C ATOM 344 CD1 LEU A 49 28.796 10.823 -41.064 1.00 94.89 C ANISOU 344 CD1 LEU A 49 14043 11416 10596 158 770 -1971 C ATOM 345 CD2 LEU A 49 26.635 12.009 -41.434 1.00101.20 C ANISOU 345 CD2 LEU A 49 14879 12285 11285 322 1285 -1997 C ATOM 346 N VAL A 50 29.541 15.208 -38.071 1.00 86.11 N ANISOU 346 N VAL A 50 12069 10577 10073 490 1212 -1390 N ATOM 347 CA VAL A 50 29.436 16.272 -37.084 1.00 84.03 C ANISOU 347 CA VAL A 50 11621 10375 9933 487 1153 -1220 C ATOM 348 C VAL A 50 28.654 17.421 -37.698 1.00 84.12 C ANISOU 348 C VAL A 50 11769 10455 9738 414 1076 -1092 C ATOM 349 O VAL A 50 28.981 17.884 -38.797 1.00 85.84 O ANISOU 349 O VAL A 50 12182 10703 9731 374 1204 -1107 O ATOM 350 CB VAL A 50 30.819 16.752 -36.607 1.00 84.00 C ANISOU 350 CB VAL A 50 11426 10408 10082 535 1363 -1237 C ATOM 351 CG1 VAL A 50 30.666 17.839 -35.571 1.00 82.14 C ANISOU 351 CG1 VAL A 50 11039 10219 9953 504 1293 -1087 C ATOM 352 CG2 VAL A 50 31.616 15.597 -36.035 1.00 84.54 C ANISOU 352 CG2 VAL A 50 11349 10409 10364 662 1399 -1355 C ATOM 353 N GLY A 51 27.622 17.877 -36.994 1.00 82.67 N ANISOU 353 N GLY A 51 11498 10288 9626 407 877 -965 N ATOM 354 CA GLY A 51 26.857 19.019 -37.443 1.00 83.03 C ANISOU 354 CA GLY A 51 11643 10380 9525 393 778 -826 C ATOM 355 C GLY A 51 25.648 18.653 -38.271 1.00 84.49 C ANISOU 355 C GLY A 51 11962 10602 9539 372 539 -836 C ATOM 356 O GLY A 51 24.956 17.673 -37.984 1.00 84.38 O ANISOU 356 O GLY A 51 11866 10580 9615 340 391 -915 O ATOM 357 N GLN A 52 25.402 19.442 -39.313 1.00 86.28 N ANISOU 357 N GLN A 52 12408 10866 9509 377 492 -755 N ATOM 358 CA GLN A 52 24.205 19.252 -40.126 1.00 88.23 C ANISOU 358 CA GLN A 52 12770 11180 9573 370 199 -750 C ATOM 359 C GLN A 52 24.089 17.872 -40.766 1.00 89.67 C ANISOU 359 C GLN A 52 13056 11368 9647 281 136 -951 C ATOM 360 O GLN A 52 22.956 17.369 -40.853 1.00 90.95 O ANISOU 360 O GLN A 52 13151 11586 9819 239 -139 -996 O ATOM 361 CB GLN A 52 24.138 20.358 -41.184 1.00 90.46 C ANISOU 361 CB GLN A 52 13340 11482 9548 411 163 -607 C ATOM 362 CG GLN A 52 23.740 21.718 -40.622 1.00 89.80 C ANISOU 362 CG GLN A 52 13176 11369 9576 518 115 -398 C ATOM 363 CD GLN A 52 22.264 21.793 -40.272 1.00 90.13 C ANISOU 363 CD GLN A 52 13011 11482 9751 605 -227 -342 C ATOM 364 OE1 GLN A 52 21.471 20.955 -40.702 1.00 91.47 O ANISOU 364 OE1 GLN A 52 13143 11746 9866 566 -469 -441 O ATOM 365 NE2 GLN A 52 21.889 22.800 -39.489 1.00 89.27 N ANISOU 365 NE2 GLN A 52 12756 11329 9834 714 -235 -203 N ATOM 366 N PRO A 53 25.160 17.215 -41.232 1.00 90.35 N ANISOU 366 N PRO A 53 13291 11396 9642 244 380 -1097 N ATOM 367 CA PRO A 53 24.977 15.840 -41.734 1.00 91.90 C ANISOU 367 CA PRO A 53 13596 11557 9767 163 327 -1311 C ATOM 368 C PRO A 53 24.440 14.895 -40.674 1.00 90.43 C ANISOU 368 C PRO A 53 13168 11305 9886 134 223 -1373 C ATOM 369 O PRO A 53 23.456 14.168 -40.913 1.00 91.77 O ANISOU 369 O PRO A 53 13353 11487 10029 32 0 -1469 O ATOM 370 CB PRO A 53 26.384 15.446 -42.192 1.00 92.77 C ANISOU 370 CB PRO A 53 13851 11591 9804 177 680 -1447 C ATOM 371 CG PRO A 53 27.080 16.717 -42.425 1.00 92.74 C ANISOU 371 CG PRO A 53 13909 11631 9697 210 868 -1305 C ATOM 372 CD PRO A 53 26.540 17.682 -41.436 1.00 90.41 C ANISOU 372 CD PRO A 53 13384 11366 9601 263 725 -1098 C ATOM 373 N ALA A 54 25.070 14.893 -39.497 1.00 88.07 N ANISOU 373 N ALA A 54 12658 10936 9867 203 377 -1323 N ATOM 374 CA ALA A 54 24.567 14.115 -38.372 1.00 86.82 C ANISOU 374 CA ALA A 54 12312 10701 9976 174 299 -1337 C ATOM 375 C ALA A 54 23.106 14.435 -38.097 1.00 86.82 C ANISOU 375 C ALA A 54 12169 10793 10025 101 37 -1260 C ATOM 376 O ALA A 54 22.286 13.532 -37.897 1.00 87.65 O ANISOU 376 O ALA A 54 12227 10859 10216 -17 -87 -1351 O ATOM 377 CB ALA A 54 25.417 14.385 -37.131 1.00 84.56 C ANISOU 377 CB ALA A 54 11842 10364 9924 272 459 -1247 C ATOM 378 N LYS A 55 22.760 15.723 -38.102 1.00 86.31 N ANISOU 378 N LYS A 55 12030 10840 9923 168 -35 -1102 N ATOM 379 CA LYS A 55 21.372 16.114 -37.885 1.00 86.83 C ANISOU 379 CA LYS A 55 11917 11007 10065 142 -279 -1037 C ATOM 380 C LYS A 55 20.463 15.507 -38.943 1.00 89.74 C ANISOU 380 C LYS A 55 12373 11455 10267 34 -534 -1160 C ATOM 381 O LYS A 55 19.325 15.127 -38.650 1.00 90.69 O ANISOU 381 O LYS A 55 12295 11635 10527 -62 -722 -1208 O ATOM 382 CB LYS A 55 21.251 17.637 -37.881 1.00 86.43 C ANISOU 382 CB LYS A 55 11829 11028 9983 276 -306 -850 C ATOM 383 CG LYS A 55 19.878 18.155 -37.472 1.00 87.07 C ANISOU 383 CG LYS A 55 11662 11205 10214 309 -524 -777 C ATOM 384 CD LYS A 55 19.834 19.672 -37.457 1.00 86.99 C ANISOU 384 CD LYS A 55 11657 11212 10185 477 -527 -592 C ATOM 385 CE LYS A 55 18.494 20.177 -36.962 1.00 90.80 C ANISOU 385 CE LYS A 55 11852 11778 10870 552 -712 -537 C ATOM 386 NZ LYS A 55 18.404 21.658 -37.040 1.00 97.12 N ANISOU 386 NZ LYS A 55 12698 12554 11650 749 -727 -358 N ATOM 387 N ARG A 56 20.957 15.388 -40.177 1.00 91.56 N ANISOU 387 N ARG A 56 12901 11694 10193 26 -535 -1231 N ATOM 388 CA ARG A 56 20.131 14.851 -41.251 1.00 94.80 C ANISOU 388 CA ARG A 56 13439 12194 10389 -90 -807 -1363 C ATOM 389 C ARG A 56 19.855 13.368 -41.051 1.00 95.59 C ANISOU 389 C ARG A 56 13518 12197 10605 -276 -810 -1582 C ATOM 390 O ARG A 56 18.706 12.928 -41.174 1.00 97.57 O ANISOU 390 O ARG A 56 13638 12531 10903 -419 -1069 -1674 O ATOM 391 CB ARG A 56 20.795 15.091 -42.609 1.00 96.90 C ANISOU 391 CB ARG A 56 14092 12478 10248 -67 -768 -1390 C ATOM 392 CG ARG A 56 20.800 16.543 -43.064 1.00 97.41 C ANISOU 392 CG ARG A 56 14257 12629 10126 82 -835 -1167 C ATOM 393 CD ARG A 56 21.049 16.663 -44.558 1.00100.75 C ANISOU 393 CD ARG A 56 15108 13097 10075 55 -891 -1201 C ATOM 394 NE ARG A 56 22.356 16.147 -44.957 1.00100.71 N ANISOU 394 NE ARG A 56 15360 12976 9930 3 -517 -1334 N ATOM 395 CZ ARG A 56 23.444 16.897 -45.095 1.00100.11 C ANISOU 395 CZ ARG A 56 15432 12843 9761 70 -200 -1233 C ATOM 396 NH1 ARG A 56 23.387 18.203 -44.863 1.00 99.37 N ANISOU 396 NH1 ARG A 56 15305 12768 9683 180 -216 -990 N ATOM 397 NH2 ARG A 56 24.590 16.342 -45.469 1.00100.61 N ANISOU 397 NH2 ARG A 56 15671 12821 9733 23 149 -1390 N ATOM 398 N GLN A 57 20.886 12.578 -40.736 1.00 94.48 N ANISOU 398 N GLN A 57 13498 11872 10531 -279 -528 -1673 N ATOM 399 CA GLN A 57 20.724 11.129 -40.687 1.00 95.84 C ANISOU 399 CA GLN A 57 13747 11891 10778 -444 -508 -1885 C ATOM 400 C GLN A 57 20.297 10.608 -39.317 1.00 94.32 C ANISOU 400 C GLN A 57 13312 11592 10934 -511 -463 -1849 C ATOM 401 O GLN A 57 20.389 9.400 -39.073 1.00 95.20 O ANISOU 401 O GLN A 57 13526 11506 11141 -624 -374 -1989 O ATOM 402 CB GLN A 57 22.015 10.432 -41.123 1.00 96.29 C ANISOU 402 CB GLN A 57 14086 11771 10730 -386 -230 -2019 C ATOM 403 CG GLN A 57 23.015 10.178 -40.007 1.00 93.60 C ANISOU 403 CG GLN A 57 13661 11346 10556 -190 54 -1896 C ATOM 404 CD GLN A 57 24.144 9.252 -40.412 1.00 95.94 C ANISOU 404 CD GLN A 57 13794 11480 11179 -179 128 -1857 C ATOM 405 OE1 GLN A 57 24.594 8.428 -39.620 1.00101.98 O ANISOU 405 OE1 GLN A 57 14325 12306 12118 -148 89 -1687 O ATOM 406 NE2 GLN A 57 24.605 9.381 -41.651 1.00 98.59 N ANISOU 406 NE2 GLN A 57 14290 11590 11582 -201 243 -2015 N ATOM 407 N ALA A 58 19.841 11.478 -38.418 1.00 92.41 N ANISOU 407 N ALA A 58 12789 11452 10871 -447 -500 -1667 N ATOM 408 CA ALA A 58 19.520 11.016 -37.072 1.00 91.19 C ANISOU 408 CA ALA A 58 12453 11190 11006 -517 -408 -1625 C ATOM 409 C ALA A 58 18.313 10.087 -37.058 1.00 93.66 C ANISOU 409 C ALA A 58 12682 11485 11421 -784 -548 -1773 C ATOM 410 O ALA A 58 18.227 9.204 -36.198 1.00 93.69 O ANISOU 410 O ALA A 58 12691 11304 11601 -905 -419 -1803 O ATOM 411 CB ALA A 58 19.275 12.209 -36.152 1.00 89.03 C ANISOU 411 CB ALA A 58 11919 11033 10874 -399 -391 -1423 C ATOM 412 N VAL A 59 17.379 10.261 -37.996 1.00 96.17 N ANISOU 412 N VAL A 59 12930 11988 11623 -889 -819 -1867 N ATOM 413 CA VAL A 59 16.137 9.495 -37.946 1.00 98.94 C ANISOU 413 CA VAL A 59 13116 12367 12108 -1174 -973 -2023 C ATOM 414 C VAL A 59 16.383 8.028 -38.276 1.00100.93 C ANISOU 414 C VAL A 59 13658 12376 12314 -1384 -891 -2242 C ATOM 415 O VAL A 59 15.703 7.141 -37.742 1.00102.52 O ANISOU 415 O VAL A 59 13787 12460 12704 -1641 -857 -2346 O ATOM 416 CB VAL A 59 15.090 10.128 -38.882 1.00101.61 C ANISOU 416 CB VAL A 59 13268 13000 12340 -1206 -1339 -2069 C ATOM 417 CG1 VAL A 59 15.598 10.165 -40.318 1.00103.23 C ANISOU 417 CG1 VAL A 59 13809 13251 12164 -1149 -1484 -2153 C ATOM 418 CG2 VAL A 59 13.769 9.383 -38.787 1.00104.91 C ANISOU 418 CG2 VAL A 59 13430 13487 12943 -1524 -1508 -2252 C ATOM 419 N THR A 60 17.359 7.739 -39.131 1.00101.20 N ANISOU 419 N THR A 60 14038 12307 12107 -1288 -825 -2324 N ATOM 420 CA THR A 60 17.688 6.368 -39.489 1.00103.37 C ANISOU 420 CA THR A 60 14629 12311 12334 -1446 -718 -2547 C ATOM 421 C THR A 60 18.741 5.747 -38.581 1.00101.52 C ANISOU 421 C THR A 60 14555 11764 12255 -1313 -399 -2477 C ATOM 422 O THR A 60 18.942 4.530 -38.639 1.00103.50 O ANISOU 422 O THR A 60 15061 11728 12537 -1431 -286 -2640 O ATOM 423 CB THR A 60 18.174 6.304 -40.939 1.00105.39 C ANISOU 423 CB THR A 60 15198 12607 12237 -1412 -789 -2709 C ATOM 424 OG1 THR A 60 19.143 7.335 -41.163 1.00103.04 O ANISOU 424 OG1 THR A 60 14945 12410 11796 -1117 -685 -2540 O ATOM 425 CG2 THR A 60 17.011 6.494 -41.895 1.00108.65 C ANISOU 425 CG2 THR A 60 15532 13277 12475 -1615 -1163 -2840 C ATOM 426 N ASN A 61 19.412 6.544 -37.752 1.00 98.21 N ANISOU 426 N ASN A 61 14003 11382 11930 -1067 -269 -2245 N ATOM 427 CA ASN A 61 20.438 6.053 -36.831 1.00 96.73 C ANISOU 427 CA ASN A 61 13933 10935 11885 -905 -22 -2155 C ATOM 428 C ASN A 61 20.239 6.681 -35.456 1.00 94.22 C ANISOU 428 C ASN A 61 13365 10675 11758 -849 21 -1923 C ATOM 429 O ASN A 61 21.119 7.375 -34.939 1.00 91.80 O ANISOU 429 O ASN A 61 13000 10408 11471 -613 116 -1764 O ATOM 430 CB ASN A 61 21.830 6.358 -37.379 1.00 95.83 C ANISOU 430 CB ASN A 61 13965 10809 11638 -628 115 -2153 C ATOM 431 CG ASN A 61 22.926 5.640 -36.625 1.00 95.45 C ANISOU 431 CG ASN A 61 14043 10482 11741 -443 327 -2114 C ATOM 432 OD1 ASN A 61 22.694 4.609 -35.996 1.00 96.72 O ANISOU 432 OD1 ASN A 61 14325 10380 12043 -536 374 -2139 O ATOM 433 ND2 ASN A 61 24.134 6.183 -36.687 1.00 94.11 N ANISOU 433 ND2 ASN A 61 13845 10364 11549 -179 453 -2052 N ATOM 434 N PRO A 62 19.085 6.445 -34.823 1.00 95.10 N ANISOU 434 N PRO A 62 13325 10795 12015 -1086 -30 -1916 N ATOM 435 CA PRO A 62 18.792 7.171 -33.577 1.00 93.06 C ANISOU 435 CA PRO A 62 12829 10625 11903 -1047 29 -1713 C ATOM 436 C PRO A 62 19.704 6.790 -32.428 1.00 91.78 C ANISOU 436 C PRO A 62 12820 10233 11819 -907 218 -1570 C ATOM 437 O PRO A 62 20.148 7.668 -31.680 1.00 89.44 O ANISOU 437 O PRO A 62 12403 10036 11543 -734 264 -1400 O ATOM 438 CB PRO A 62 17.331 6.795 -33.297 1.00 95.27 C ANISOU 438 CB PRO A 62 12931 10947 12323 -1373 -28 -1793 C ATOM 439 CG PRO A 62 17.167 5.465 -33.932 1.00 98.34 C ANISOU 439 CG PRO A 62 13567 11113 12683 -1594 -38 -2005 C ATOM 440 CD PRO A 62 18.031 5.472 -35.158 1.00 98.39 C ANISOU 440 CD PRO A 62 13782 11126 12475 -1423 -108 -2109 C ATOM 441 N GLN A 63 20.008 5.502 -32.272 1.00 93.64 N ANISOU 441 N GLN A 63 13338 10149 12091 -969 313 -1636 N ATOM 442 CA GLN A 63 20.794 5.039 -31.138 1.00 93.19 C ANISOU 442 CA GLN A 63 13454 9851 12103 -826 449 -1483 C ATOM 443 C GLN A 63 22.247 5.481 -31.197 1.00 91.44 C ANISOU 443 C GLN A 63 13259 9653 11831 -468 469 -1409 C ATOM 444 O GLN A 63 22.931 5.427 -30.170 1.00 90.80 O ANISOU 444 O GLN A 63 13236 9466 11799 -307 523 -1251 O ATOM 445 CB GLN A 63 20.730 3.516 -31.055 1.00 96.27 C ANISOU 445 CB GLN A 63 14181 9851 12547 -965 535 -1571 C ATOM 446 CG GLN A 63 19.330 2.967 -30.886 1.00103.11 C ANISOU 446 CG GLN A 63 15026 10659 13491 -1372 554 -1655 C ATOM 447 CD GLN A 63 19.273 1.466 -31.066 1.00114.82 C ANISOU 447 CD GLN A 63 16882 11731 15012 -1544 642 -1787 C ATOM 448 OE1 GLN A 63 19.871 0.917 -31.991 1.00116.44 O ANISOU 448 OE1 GLN A 63 17289 11795 15158 -1442 625 -1945 O ATOM 449 NE2 GLN A 63 18.556 0.790 -30.175 1.00123.25 N ANISOU 449 NE2 GLN A 63 18070 12582 16176 -1815 767 -1729 N ATOM 450 N ASN A 64 22.737 5.911 -32.360 1.00 91.07 N ANISOU 450 N ASN A 64 13172 9749 11680 -355 429 -1523 N ATOM 451 CA ASN A 64 24.140 6.271 -32.522 1.00 90.04 C ANISOU 451 CA ASN A 64 13040 9645 11526 -49 490 -1493 C ATOM 452 C ASN A 64 24.323 7.738 -32.890 1.00 87.79 C ANISOU 452 C ASN A 64 12518 9683 11153 28 451 -1435 C ATOM 453 O ASN A 64 25.414 8.135 -33.307 1.00 87.33 O ANISOU 453 O ASN A 64 12437 9687 11058 224 520 -1453 O ATOM 454 CB ASN A 64 24.800 5.375 -33.568 1.00 92.30 C ANISOU 454 CB ASN A 64 13551 9753 11767 34 563 -1693 C ATOM 455 CG ASN A 64 24.783 3.913 -33.172 1.00101.35 C ANISOU 455 CG ASN A 64 14979 10514 13017 3 622 -1742 C ATOM 456 OD1 ASN A 64 25.070 3.566 -32.026 1.00106.01 O ANISOU 456 OD1 ASN A 64 15623 10937 13719 100 642 -1583 O ATOM 457 ND2 ASN A 64 24.438 3.047 -34.118 1.00109.97 N ANISOU 457 ND2 ASN A 64 16289 11444 14051 -141 646 -1963 N ATOM 458 N THR A 65 23.283 8.550 -32.743 1.00 86.76 N ANISOU 458 N THR A 65 12211 9747 11005 -119 360 -1372 N ATOM 459 CA THR A 65 23.368 9.987 -32.977 1.00 84.91 C ANISOU 459 CA THR A 65 11788 9773 10701 -40 324 -1290 C ATOM 460 C THR A 65 23.296 10.691 -31.629 1.00 83.08 C ANISOU 460 C THR A 65 11400 9596 10572 -7 349 -1115 C ATOM 461 O THR A 65 22.229 10.755 -31.009 1.00 83.17 O ANISOU 461 O THR A 65 11317 9633 10649 -156 318 -1071 O ATOM 462 CB THR A 65 22.255 10.463 -33.903 1.00 85.69 C ANISOU 462 CB THR A 65 11812 10047 10699 -182 180 -1353 C ATOM 463 OG1 THR A 65 22.281 9.695 -35.110 1.00 87.87 O ANISOU 463 OG1 THR A 65 12282 10261 10843 -247 145 -1536 O ATOM 464 CG2 THR A 65 22.461 11.917 -34.253 1.00 84.29 C ANISOU 464 CG2 THR A 65 11515 10080 10431 -65 154 -1256 C ATOM 465 N LEU A 66 24.429 11.225 -31.190 1.00 81.82 N ANISOU 465 N LEU A 66 11203 9462 10423 172 416 -1037 N ATOM 466 CA LEU A 66 24.582 11.830 -29.877 1.00 80.45 C ANISOU 466 CA LEU A 66 10931 9325 10314 211 437 -893 C ATOM 467 C LEU A 66 24.432 13.342 -29.961 1.00 78.95 C ANISOU 467 C LEU A 66 10572 9339 10085 228 434 -833 C ATOM 468 O LEU A 66 24.982 13.985 -30.862 1.00 78.72 O ANISOU 468 O LEU A 66 10526 9402 9981 301 452 -866 O ATOM 469 CB LEU A 66 25.948 11.481 -29.284 1.00 80.57 C ANISOU 469 CB LEU A 66 10994 9248 10372 393 473 -858 C ATOM 470 CG LEU A 66 26.288 9.993 -29.230 1.00 82.53 C ANISOU 470 CG LEU A 66 11440 9246 10670 448 478 -906 C ATOM 471 CD1 LEU A 66 27.692 9.789 -28.719 1.00 83.07 C ANISOU 471 CD1 LEU A 66 11497 9261 10803 686 475 -870 C ATOM 472 CD2 LEU A 66 25.308 9.253 -28.353 1.00 83.37 C ANISOU 472 CD2 LEU A 66 11679 9194 10803 286 466 -837 C ATOM 473 N PHE A 67 23.692 13.901 -29.007 1.00 78.28 N ANISOU 473 N PHE A 67 10393 9302 10046 157 439 -747 N ATOM 474 CA PHE A 67 23.477 15.336 -28.918 1.00 77.18 C ANISOU 474 CA PHE A 67 10120 9310 9896 185 452 -688 C ATOM 475 C PHE A 67 23.358 15.713 -27.451 1.00 76.60 C ANISOU 475 C PHE A 67 10010 9226 9868 158 514 -604 C ATOM 476 O PHE A 67 23.194 14.853 -26.582 1.00 77.23 O ANISOU 476 O PHE A 67 10174 9199 9970 92 537 -580 O ATOM 477 CB PHE A 67 22.228 15.763 -29.687 1.00 77.84 C ANISOU 477 CB PHE A 67 10107 9491 9979 120 375 -714 C ATOM 478 CG PHE A 67 20.973 15.063 -29.245 1.00 79.01 C ANISOU 478 CG PHE A 67 10185 9613 10221 -35 354 -745 C ATOM 479 CD1 PHE A 67 20.124 15.650 -28.322 1.00 87.61 C ANISOU 479 CD1 PHE A 67 11129 10754 11406 -85 417 -698 C ATOM 480 CD2 PHE A 67 20.640 13.821 -29.755 1.00 80.48 C ANISOU 480 CD2 PHE A 67 10455 9715 10409 -151 302 -842 C ATOM 481 CE1 PHE A 67 18.968 15.013 -27.918 1.00 94.67 C ANISOU 481 CE1 PHE A 67 11927 11636 12406 -257 442 -743 C ATOM 482 CE2 PHE A 67 19.485 13.179 -29.353 1.00 90.59 C ANISOU 482 CE2 PHE A 67 11660 10968 11793 -342 307 -886 C ATOM 483 CZ PHE A 67 18.648 13.776 -28.434 1.00 97.01 C ANISOU 483 CZ PHE A 67 12294 11854 12713 -400 385 -835 C ATOM 484 N ALA A 68 23.434 17.017 -27.181 1.00 75.74 N ANISOU 484 N ALA A 68 9816 9208 9753 200 555 -562 N ATOM 485 CA ALA A 68 23.316 17.532 -25.819 1.00 75.45 C ANISOU 485 CA ALA A 68 9769 9169 9728 166 630 -507 C ATOM 486 C ALA A 68 24.304 16.848 -24.880 1.00 75.62 C ANISOU 486 C ALA A 68 9912 9115 9705 186 617 -475 C ATOM 487 O ALA A 68 24.009 16.613 -23.707 1.00 76.14 O ANISOU 487 O ALA A 68 10056 9134 9741 117 657 -428 O ATOM 488 CB ALA A 68 21.887 17.383 -25.296 1.00 76.29 C ANISOU 488 CB ALA A 68 9811 9274 9902 49 687 -507 C ATOM 489 N ILE A 69 25.484 16.506 -25.398 1.00 75.61 N ANISOU 489 N ILE A 69 9931 9103 9694 290 559 -501 N ATOM 490 CA ILE A 69 26.486 15.849 -24.568 1.00 76.31 C ANISOU 490 CA ILE A 69 10102 9131 9763 361 498 -468 C ATOM 491 C ILE A 69 27.007 16.805 -23.504 1.00 76.11 C ANISOU 491 C ILE A 69 10049 9185 9686 353 493 -436 C ATOM 492 O ILE A 69 27.469 16.376 -22.437 1.00 77.07 O ANISOU 492 O ILE A 69 10269 9267 9748 376 417 -382 O ATOM 493 CB ILE A 69 27.611 15.296 -25.464 1.00 76.84 C ANISOU 493 CB ILE A 69 10138 9182 9874 499 455 -533 C ATOM 494 CG1 ILE A 69 27.036 14.287 -26.453 1.00 77.43 C ANISOU 494 CG1 ILE A 69 10295 9153 9970 482 466 -588 C ATOM 495 CG2 ILE A 69 28.689 14.631 -24.648 1.00 78.10 C ANISOU 495 CG2 ILE A 69 10338 9287 10049 626 355 -499 C ATOM 496 CD1 ILE A 69 26.365 13.115 -25.787 1.00 78.53 C ANISOU 496 CD1 ILE A 69 10604 9121 10112 418 443 -539 C ATOM 497 N LYS A 70 26.917 18.111 -23.758 1.00 75.24 N ANISOU 497 N LYS A 70 9837 9171 9580 316 564 -467 N ATOM 498 CA LYS A 70 27.318 19.087 -22.755 1.00 75.32 C ANISOU 498 CA LYS A 70 9845 9238 9536 273 577 -466 C ATOM 499 C LYS A 70 26.519 18.928 -21.469 1.00 75.91 C ANISOU 499 C LYS A 70 10055 9265 9524 184 611 -414 C ATOM 500 O LYS A 70 27.013 19.269 -20.390 1.00 82.68 O ANISOU 500 O LYS A 70 10985 10149 10280 151 573 -409 O ATOM 501 CB LYS A 70 27.160 20.498 -23.318 1.00 74.62 C ANISOU 501 CB LYS A 70 9675 9201 9477 239 681 -505 C ATOM 502 CG LYS A 70 27.904 21.576 -22.560 1.00 75.01 C ANISOU 502 CG LYS A 70 9714 9297 9487 181 700 -547 C ATOM 503 CD LYS A 70 27.802 22.899 -23.291 1.00 74.67 C ANISOU 503 CD LYS A 70 9637 9251 9485 153 822 -576 C ATOM 504 CE LYS A 70 28.534 24.002 -22.564 1.00 75.40 C ANISOU 504 CE LYS A 70 9739 9361 9547 56 861 -642 C ATOM 505 NZ LYS A 70 28.311 25.316 -23.223 1.00 75.45 N ANISOU 505 NZ LYS A 70 9774 9301 9591 24 1006 -654 N ATOM 506 N ARG A 71 25.295 18.409 -21.556 1.00 76.00 N ANISOU 506 N ARG A 71 10102 9214 9560 124 688 -389 N ATOM 507 CA ARG A 71 24.467 18.172 -20.382 1.00 77.00 C ANISOU 507 CA ARG A 71 10361 9290 9607 11 781 -349 C ATOM 508 C ARG A 71 24.736 16.824 -19.727 1.00 78.35 C ANISOU 508 C ARG A 71 10734 9347 9686 2 703 -267 C ATOM 509 O ARG A 71 23.978 16.418 -18.842 1.00 79.59 O ANISOU 509 O ARG A 71 11047 9432 9759 -120 808 -219 O ATOM 510 CB ARG A 71 22.984 18.296 -20.745 1.00 77.07 C ANISOU 510 CB ARG A 71 10269 9297 9718 -71 926 -377 C ATOM 511 CG ARG A 71 22.419 19.691 -20.510 1.00 76.94 C ANISOU 511 CG ARG A 71 10154 9343 9736 -80 1060 -428 C ATOM 512 CD ARG A 71 21.280 20.016 -21.455 1.00 76.95 C ANISOU 512 CD ARG A 71 9952 9383 9901 -56 1109 -466 C ATOM 513 NE ARG A 71 20.005 19.431 -21.052 1.00 78.37 N ANISOU 513 NE ARG A 71 10075 9551 10152 -175 1234 -484 N ATOM 514 CZ ARG A 71 19.054 20.100 -20.413 1.00 79.54 C ANISOU 514 CZ ARG A 71 10136 9723 10363 -217 1424 -531 C ATOM 515 NH1 ARG A 71 19.246 21.372 -20.104 1.00 79.36 N ANISOU 515 NH1 ARG A 71 10113 9710 10328 -135 1497 -561 N ATOM 516 NH2 ARG A 71 17.916 19.501 -20.089 1.00 81.24 N ANISOU 516 NH2 ARG A 71 10260 9942 10666 -349 1564 -565 N ATOM 517 N LEU A 72 25.786 16.117 -20.149 1.00 78.52 N ANISOU 517 N LEU A 72 10771 9336 9728 135 541 -248 N ATOM 518 CA LEU A 72 26.267 14.932 -19.454 1.00 80.28 C ANISOU 518 CA LEU A 72 11214 9427 9861 187 427 -152 C ATOM 519 C LEU A 72 27.714 15.036 -19.017 1.00 81.10 C ANISOU 519 C LEU A 72 11309 9593 9913 343 222 -134 C ATOM 520 O LEU A 72 28.122 14.301 -18.113 1.00 83.08 O ANISOU 520 O LEU A 72 11772 9755 10041 401 91 -31 O ATOM 521 CB LEU A 72 26.129 13.680 -20.334 1.00 80.72 C ANISOU 521 CB LEU A 72 11312 9335 10023 238 408 -150 C ATOM 522 CG LEU A 72 24.736 13.252 -20.783 1.00 80.72 C ANISOU 522 CG LEU A 72 11324 9260 10088 66 564 -178 C ATOM 523 CD1 LEU A 72 24.826 11.957 -21.560 1.00 81.68 C ANISOU 523 CD1 LEU A 72 11538 9208 10287 110 519 -194 C ATOM 524 CD2 LEU A 72 23.811 13.091 -19.593 1.00 82.08 C ANISOU 524 CD2 LEU A 72 11676 9361 10149 -121 704 -104 C ATOM 525 N ILE A 73 28.494 15.929 -19.623 1.00 80.07 N ANISOU 525 N ILE A 73 10940 9611 9870 405 185 -231 N ATOM 526 CA ILE A 73 29.927 15.955 -19.379 1.00 81.27 C ANISOU 526 CA ILE A 73 10998 9848 10034 548 -14 -249 C ATOM 527 C ILE A 73 30.206 16.346 -17.934 1.00 82.79 C ANISOU 527 C ILE A 73 11330 10096 10029 493 -135 -201 C ATOM 528 O ILE A 73 29.557 17.234 -17.368 1.00 82.25 O ANISOU 528 O ILE A 73 11330 10070 9851 326 -11 -225 O ATOM 529 CB ILE A 73 30.606 16.903 -20.382 1.00 80.14 C ANISOU 529 CB ILE A 73 10566 9850 10032 563 36 -380 C ATOM 530 CG1 ILE A 73 32.124 16.812 -20.271 1.00 81.87 C ANISOU 530 CG1 ILE A 73 10607 10175 10324 708 -152 -429 C ATOM 531 CG2 ILE A 73 30.125 18.333 -20.191 1.00 78.96 C ANISOU 531 CG2 ILE A 73 10380 9786 9833 393 170 -433 C ATOM 532 CD1 ILE A 73 32.854 17.426 -21.443 1.00 81.33 C ANISOU 532 CD1 ILE A 73 10261 10217 10421 722 -53 -562 C ATOM 533 N GLY A 74 31.157 15.647 -17.317 1.00 85.12 N ANISOU 533 N GLY A 74 11688 10382 10270 647 -385 -135 N ATOM 534 CA GLY A 74 31.545 15.952 -15.955 1.00 87.60 C ANISOU 534 CA GLY A 74 12158 10766 10359 608 -563 -89 C ATOM 535 C GLY A 74 30.535 15.583 -14.898 1.00 93.08 C ANISOU 535 C GLY A 74 13245 11326 10795 476 -481 39 C ATOM 536 O GLY A 74 30.656 16.037 -13.760 1.00105.10 O ANISOU 536 O GLY A 74 14943 12914 12076 387 -569 56 O ATOM 537 N ARG A 75 29.541 14.769 -15.234 1.00 87.57 N ANISOU 537 N ARG A 75 12699 10443 10131 437 -301 114 N ATOM 538 CA ARG A 75 28.494 14.388 -14.302 1.00 88.78 C ANISOU 538 CA ARG A 75 13211 10459 10063 270 -150 224 C ATOM 539 C ARG A 75 28.571 12.899 -13.993 1.00 91.23 C ANISOU 539 C ARG A 75 13831 10535 10296 379 -262 403 C ATOM 540 O ARG A 75 29.200 12.122 -14.715 1.00 91.50 O ANISOU 540 O ARG A 75 13773 10487 10505 587 -401 421 O ATOM 541 CB ARG A 75 27.112 14.733 -14.860 1.00 86.73 C ANISOU 541 CB ARG A 75 12866 10172 9915 78 191 150 C ATOM 542 CG ARG A 75 26.873 16.215 -15.043 1.00 84.89 C ANISOU 542 CG ARG A 75 12403 10113 9737 -18 326 0 C ATOM 543 CD ARG A 75 25.471 16.461 -15.545 1.00 83.59 C ANISOU 543 CD ARG A 75 12145 9918 9698 -159 623 -57 C ATOM 544 NE ARG A 75 25.247 17.856 -15.900 1.00 82.02 N ANISOU 544 NE ARG A 75 11723 9848 9594 -194 740 -188 N ATOM 545 CZ ARG A 75 24.631 18.733 -15.119 1.00 82.62 C ANISOU 545 CZ ARG A 75 11868 9955 9569 -319 925 -247 C ATOM 546 NH1 ARG A 75 24.178 18.355 -13.933 1.00 84.73 N ANISOU 546 NH1 ARG A 75 12421 10159 9614 -445 1029 -190 N ATOM 547 NH2 ARG A 75 24.465 19.983 -15.524 1.00 81.46 N ANISOU 547 NH2 ARG A 75 11536 9882 9534 -317 1025 -361 N ATOM 548 N ARG A 76 27.917 12.514 -12.902 1.00 93.38 N ANISOU 548 N ARG A 76 14501 10680 10298 233 -172 533 N ATOM 549 CA ARG A 76 27.859 11.133 -12.450 1.00 96.30 C ANISOU 549 CA ARG A 76 15269 10776 10543 293 -237 733 C ATOM 550 C ARG A 76 26.598 10.465 -12.984 1.00 95.69 C ANISOU 550 C ARG A 76 15265 10503 10588 101 89 733 C ATOM 551 O ARG A 76 25.582 11.122 -13.219 1.00 93.88 O ANISOU 551 O ARG A 76 14873 10367 10431 -123 375 613 O ATOM 552 CB ARG A 76 27.879 11.069 -10.923 1.00 99.67 C ANISOU 552 CB ARG A 76 16153 11160 10557 214 -314 889 C ATOM 553 CG ARG A 76 28.954 11.932 -10.284 1.00100.53 C ANISOU 553 CG ARG A 76 16179 11511 10508 323 -626 847 C ATOM 554 CD ARG A 76 30.289 11.217 -10.269 1.00105.54 C ANISOU 554 CD ARG A 76 16811 12117 11172 669 -1070 956 C ATOM 555 NE ARG A 76 30.269 10.075 -9.360 1.00116.76 N ANISOU 555 NE ARG A 76 18781 13276 12306 742 -1201 1219 N ATOM 556 CZ ARG A 76 31.238 9.172 -9.272 1.00122.53 C ANISOU 556 CZ ARG A 76 19617 13887 13052 1077 -1571 1371 C ATOM 557 NH1 ARG A 76 32.311 9.273 -10.045 1.00130.25 N ANISOU 557 NH1 ARG A 76 20139 15009 14341 1359 -1822 1258 N ATOM 558 NH2 ARG A 76 31.133 8.165 -8.416 1.00117.88 N ANISOU 558 NH2 ARG A 76 19596 13022 12172 1136 -1673 1636 N ATOM 559 N PHE A 77 26.671 9.145 -13.177 1.00 97.61 N ANISOU 559 N PHE A 77 15749 10468 10871 194 38 858 N ATOM 560 CA PHE A 77 25.530 8.426 -13.736 1.00 97.50 C ANISOU 560 CA PHE A 77 15797 10257 10992 -16 328 835 C ATOM 561 C PHE A 77 24.325 8.476 -12.811 1.00 99.04 C ANISOU 561 C PHE A 77 16260 10389 10981 -359 646 888 C ATOM 562 O PHE A 77 23.182 8.479 -13.280 1.00 98.20 O ANISOU 562 O PHE A 77 16008 10275 11027 -606 941 779 O ATOM 563 CB PHE A 77 25.899 6.972 -14.032 1.00 99.89 C ANISOU 563 CB PHE A 77 16373 10223 11359 141 219 957 C ATOM 564 CG PHE A 77 24.733 6.132 -14.491 1.00100.58 C ANISOU 564 CG PHE A 77 16587 10071 11558 -124 513 930 C ATOM 565 CD1 PHE A 77 24.300 6.184 -15.802 1.00 98.20 C ANISOU 565 CD1 PHE A 77 15932 9834 11546 -184 613 731 C ATOM 566 CD2 PHE A 77 24.069 5.295 -13.609 1.00104.02 C ANISOU 566 CD2 PHE A 77 17511 10219 11793 -339 690 1099 C ATOM 567 CE1 PHE A 77 23.232 5.421 -16.226 1.00 99.24 C ANISOU 567 CE1 PHE A 77 16154 9768 11785 -454 853 679 C ATOM 568 CE2 PHE A 77 22.999 4.530 -14.030 1.00105.05 C ANISOU 568 CE2 PHE A 77 17733 10134 12048 -628 974 1050 C ATOM 569 CZ PHE A 77 22.581 4.594 -15.338 1.00102.66 C ANISOU 569 CZ PHE A 77 17034 9919 12055 -688 1040 829 C ATOM 570 N GLN A 78 24.553 8.512 -11.503 1.00101.69 N ANISOU 570 N GLN A 78 16979 10691 10969 -384 594 1042 N ATOM 571 CA GLN A 78 23.468 8.496 -10.536 1.00103.87 C ANISOU 571 CA GLN A 78 17569 10889 11007 -718 936 1098 C ATOM 572 C GLN A 78 22.932 9.884 -10.220 1.00102.14 C ANISOU 572 C GLN A 78 17098 10961 10750 -879 1137 928 C ATOM 573 O GLN A 78 22.006 9.999 -9.413 1.00104.07 O ANISOU 573 O GLN A 78 17556 11173 10812 -1158 1469 935 O ATOM 574 CB GLN A 78 23.921 7.809 -9.243 1.00108.27 C ANISOU 574 CB GLN A 78 18753 11238 11146 -685 806 1361 C ATOM 575 CG GLN A 78 24.006 6.291 -9.346 1.00111.22 C ANISOU 575 CG GLN A 78 19521 11213 11523 -624 756 1559 C ATOM 576 CD GLN A 78 22.661 5.647 -9.630 1.00112.04 C ANISOU 576 CD GLN A 78 19705 11111 11756 -989 1199 1520 C ATOM 577 OE1 GLN A 78 21.618 6.145 -9.205 1.00112.25 O ANISOU 577 OE1 GLN A 78 19701 11237 11714 -1322 1569 1434 O ATOM 578 NE2 GLN A 78 22.678 4.536 -10.358 1.00114.29 N ANISOU 578 NE2 GLN A 78 20074 11105 12244 -936 1172 1560 N ATOM 579 N ASP A 79 23.488 10.934 -10.823 1.00 98.97 N ANISOU 579 N ASP A 79 16268 10819 10516 -716 975 771 N ATOM 580 CA ASP A 79 22.908 12.261 -10.680 1.00 97.38 C ANISOU 580 CA ASP A 79 15814 10848 10336 -851 1190 594 C ATOM 581 C ASP A 79 21.456 12.236 -11.133 1.00 96.94 C ANISOU 581 C ASP A 79 15562 10772 10498 -1093 1586 483 C ATOM 582 O ASP A 79 21.095 11.514 -12.064 1.00 96.25 O ANISOU 582 O ASP A 79 15324 10587 10660 -1105 1605 468 O ATOM 583 CB ASP A 79 23.697 13.286 -11.495 1.00 94.13 C ANISOU 583 CB ASP A 79 14972 10663 10128 -646 972 448 C ATOM 584 CG ASP A 79 25.134 13.419 -11.037 1.00 94.94 C ANISOU 584 CG ASP A 79 15182 10836 10056 -433 585 515 C ATOM 585 OD1 ASP A 79 25.473 12.877 -9.965 1.00 98.11 O ANISOU 585 OD1 ASP A 79 16007 11137 10134 -434 464 675 O ATOM 586 OD2 ASP A 79 25.921 14.082 -11.744 1.00100.44 O ANISOU 586 OD2 ASP A 79 15537 11694 10933 -273 398 406 O ATOM 587 N GLU A 80 20.618 13.020 -10.455 1.00 97.77 N ANISOU 587 N GLU A 80 15661 10974 10513 -1289 1901 389 N ATOM 588 CA GLU A 80 19.184 12.985 -10.727 1.00 98.28 C ANISOU 588 CA GLU A 80 15515 11037 10790 -1527 2293 275 C ATOM 589 C GLU A 80 18.884 13.383 -12.166 1.00 95.15 C ANISOU 589 C GLU A 80 14576 10770 10806 -1420 2227 123 C ATOM 590 O GLU A 80 18.166 12.676 -12.888 1.00 97.64 O ANISOU 590 O GLU A 80 14733 11017 11347 -1528 2316 91 O ATOM 591 CB GLU A 80 18.455 13.905 -9.752 1.00110.61 C ANISOU 591 CB GLU A 80 17123 12701 12203 -1701 2644 171 C ATOM 592 CG GLU A 80 16.956 13.985 -9.963 1.00133.99 C ANISOU 592 CG GLU A 80 19791 15699 15420 -1928 3069 25 C ATOM 593 CD GLU A 80 16.281 14.918 -8.975 1.00155.21 C ANISOU 593 CD GLU A 80 22519 18480 17972 -2069 3450 -100 C ATOM 594 OE1 GLU A 80 16.994 15.568 -8.183 1.00162.00 O ANISOU 594 OE1 GLU A 80 23647 19378 18527 -1996 3364 -85 O ATOM 595 OE2 GLU A 80 15.035 15.001 -8.989 1.00163.22 O ANISOU 595 OE2 GLU A 80 23287 19536 19194 -2257 3839 -232 O ATOM 596 N GLU A 81 19.433 14.520 -12.600 1.00 92.55 N ANISOU 596 N GLU A 81 13983 10621 10562 -1223 2065 27 N ATOM 597 CA GLU A 81 19.218 14.985 -13.965 1.00 89.90 C ANISOU 597 CA GLU A 81 13190 10403 10563 -1103 1982 -94 C ATOM 598 C GLU A 81 19.717 13.963 -14.974 1.00 88.93 C ANISOU 598 C GLU A 81 13045 10183 10563 -1005 1742 -34 C ATOM 599 O GLU A 81 19.111 13.776 -16.034 1.00 89.70 O ANISOU 599 O GLU A 81 12864 10310 10909 -1025 1752 -117 O ATOM 600 CB GLU A 81 19.918 16.327 -14.180 1.00 91.16 C ANISOU 600 CB GLU A 81 13177 10721 10740 -916 1844 -173 C ATOM 601 CG GLU A 81 19.895 17.257 -12.975 1.00 96.14 C ANISOU 601 CG GLU A 81 13977 11401 11152 -983 2008 -218 C ATOM 602 CD GLU A 81 20.996 16.946 -11.977 1.00106.02 C ANISOU 602 CD GLU A 81 15629 12600 12054 -965 1817 -101 C ATOM 603 OE1 GLU A 81 22.005 16.326 -12.378 1.00 99.15 O ANISOU 603 OE1 GLU A 81 14805 11695 11174 -818 1504 -4 O ATOM 604 OE2 GLU A 81 20.844 17.310 -10.792 1.00120.35 O ANISOU 604 OE2 GLU A 81 17712 14413 13601 -1088 1976 -113 O ATOM 605 N VAL A 82 20.817 13.282 -14.653 1.00 89.42 N ANISOU 605 N VAL A 82 13400 10127 10447 -889 1515 101 N ATOM 606 CA VAL A 82 21.344 12.269 -15.557 1.00 88.98 C ANISOU 606 CA VAL A 82 13353 9947 10508 -772 1314 146 C ATOM 607 C VAL A 82 20.366 11.110 -15.696 1.00 90.98 C ANISOU 607 C VAL A 82 13722 10009 10838 -991 1495 164 C ATOM 608 O VAL A 82 20.178 10.581 -16.792 1.00 90.34 O ANISOU 608 O VAL A 82 13481 9885 10959 -983 1439 95 O ATOM 609 CB VAL A 82 22.729 11.799 -15.083 1.00 89.77 C ANISOU 609 CB VAL A 82 13727 9956 10425 -565 1034 285 C ATOM 610 CG1 VAL A 82 23.161 10.562 -15.850 1.00 90.28 C ANISOU 610 CG1 VAL A 82 13872 9826 10605 -448 888 335 C ATOM 611 CG2 VAL A 82 23.742 12.916 -15.262 1.00 87.77 C ANISOU 611 CG2 VAL A 82 13257 9915 10178 -369 836 218 C ATOM 612 N GLN A 83 19.723 10.701 -14.601 1.00 93.78 N ANISOU 612 N GLN A 83 14370 10240 11020 -1218 1732 244 N ATOM 613 CA GLN A 83 18.745 9.619 -14.684 1.00 96.19 C ANISOU 613 CA GLN A 83 14787 10352 11408 -1486 1951 249 C ATOM 614 C GLN A 83 17.527 10.043 -15.498 1.00 95.52 C ANISOU 614 C GLN A 83 14236 10434 11621 -1651 2129 48 C ATOM 615 O GLN A 83 17.059 9.303 -16.381 1.00 95.98 O ANISOU 615 O GLN A 83 14175 10416 11877 -1755 2119 -26 O ATOM 616 CB GLN A 83 18.334 9.184 -13.279 1.00 99.74 C ANISOU 616 CB GLN A 83 15677 10639 11581 -1719 2210 382 C ATOM 617 CG GLN A 83 19.486 8.682 -12.424 1.00101.23 C ANISOU 617 CG GLN A 83 16372 10650 11441 -1548 1991 607 C ATOM 618 CD GLN A 83 20.033 7.356 -12.909 1.00102.38 C ANISOU 618 CD GLN A 83 16767 10501 11632 -1443 1803 725 C ATOM 619 OE1 GLN A 83 19.287 6.497 -13.377 1.00103.77 O ANISOU 619 OE1 GLN A 83 16967 10495 11964 -1653 1973 688 O ATOM 620 NE2 GLN A 83 21.345 7.184 -12.807 1.00102.18 N ANISOU 620 NE2 GLN A 83 16912 10422 11488 -1116 1452 850 N ATOM 621 N ARG A 84 17.003 11.240 -15.216 1.00 94.80 N ANISOU 621 N ARG A 84 13880 10571 11571 -1665 2276 -53 N ATOM 622 CA ARG A 84 15.878 11.751 -15.992 1.00 94.52 C ANISOU 622 CA ARG A 84 13358 10716 11837 -1756 2396 -239 C ATOM 623 C ARG A 84 16.209 11.776 -17.479 1.00 92.10 C ANISOU 623 C ARG A 84 12778 10489 11729 -1572 2097 -312 C ATOM 624 O ARG A 84 15.395 11.368 -18.315 1.00 92.92 O ANISOU 624 O ARG A 84 12634 10621 12049 -1703 2107 -425 O ATOM 625 CB ARG A 84 15.488 13.147 -15.507 1.00 94.06 C ANISOU 625 CB ARG A 84 13077 10866 11795 -1700 2554 -326 C ATOM 626 CG ARG A 84 14.392 13.781 -16.345 1.00 94.03 C ANISOU 626 CG ARG A 84 12543 11060 12125 -1711 2622 -505 C ATOM 627 CD ARG A 84 14.132 15.230 -15.981 1.00 93.58 C ANISOU 627 CD ARG A 84 12276 11171 12108 -1578 2746 -590 C ATOM 628 NE ARG A 84 13.404 15.902 -17.053 1.00 93.09 N ANISOU 628 NE ARG A 84 11718 11287 12364 -1461 2663 -723 N ATOM 629 CZ ARG A 84 13.989 16.486 -18.095 1.00 90.47 C ANISOU 629 CZ ARG A 84 11251 11030 12094 -1205 2357 -717 C ATOM 630 NH1 ARG A 84 15.312 16.490 -18.198 1.00 88.06 N ANISOU 630 NH1 ARG A 84 11219 10651 11589 -1057 2137 -610 N ATOM 631 NH2 ARG A 84 13.256 17.067 -19.034 1.00 90.67 N ANISOU 631 NH2 ARG A 84 10868 11206 12378 -1096 2270 -817 N ATOM 632 N ASP A 85 17.411 12.242 -17.829 1.00 99.50 N ANISOU 632 N ASP A 85 13760 11465 12582 -1289 1834 -260 N ATOM 633 CA ASP A 85 17.828 12.221 -19.227 1.00102.29 C ANISOU 633 CA ASP A 85 13918 11874 13073 -1123 1582 -323 C ATOM 634 C ASP A 85 17.961 10.788 -19.739 1.00 90.78 C ANISOU 634 C ASP A 85 12652 10203 11638 -1204 1507 -307 C ATOM 635 O ASP A 85 17.652 10.509 -20.903 1.00 88.58 O ANISOU 635 O ASP A 85 12189 9959 11511 -1220 1406 -417 O ATOM 636 CB ASP A 85 19.145 12.987 -19.399 1.00102.98 C ANISOU 636 CB ASP A 85 14028 12036 13063 -838 1372 -277 C ATOM 637 CG ASP A 85 18.942 14.482 -19.673 1.00 92.71 C ANISOU 637 CG ASP A 85 12434 10951 11839 -732 1382 -354 C ATOM 638 OD1 ASP A 85 17.815 14.997 -19.502 1.00 91.77 O ANISOU 638 OD1 ASP A 85 12113 10923 11833 -839 1560 -429 O ATOM 639 OD2 ASP A 85 19.929 15.149 -20.056 1.00 81.64 O ANISOU 639 OD2 ASP A 85 11006 9615 10400 -536 1225 -344 O ATOM 640 N VAL A 86 18.409 9.864 -18.881 1.00 90.50 N ANISOU 640 N VAL A 86 13018 9929 11438 -1254 1550 -171 N ATOM 641 CA VAL A 86 18.552 8.462 -19.280 1.00 92.19 C ANISOU 641 CA VAL A 86 13477 9875 11674 -1322 1503 -149 C ATOM 642 C VAL A 86 17.232 7.933 -19.811 1.00 94.07 C ANISOU 642 C VAL A 86 13546 10095 12100 -1636 1659 -290 C ATOM 643 O VAL A 86 17.178 7.289 -20.866 1.00 94.34 O ANISOU 643 O VAL A 86 13533 10060 12251 -1662 1549 -393 O ATOM 644 CB VAL A 86 19.057 7.607 -18.103 1.00 94.52 C ANISOU 644 CB VAL A 86 14272 9890 11751 -1340 1555 48 C ATOM 645 CG1 VAL A 86 18.672 6.152 -18.301 1.00 97.42 C ANISOU 645 CG1 VAL A 86 14917 9932 12168 -1537 1640 61 C ATOM 646 CG2 VAL A 86 20.555 7.724 -17.953 1.00 93.31 C ANISOU 646 CG2 VAL A 86 14272 9714 11468 -987 1289 162 C ATOM 647 N SER A 87 16.142 8.210 -19.093 1.00 95.75 N ANISOU 647 N SER A 87 13650 10383 12348 -1893 1925 -320 N ATOM 648 CA SER A 87 14.843 7.734 -19.560 1.00 98.10 C ANISOU 648 CA SER A 87 13715 10698 12860 -2219 2075 -479 C ATOM 649 C SER A 87 14.428 8.390 -20.875 1.00 96.57 C ANISOU 649 C SER A 87 13039 10775 12876 -2131 1882 -660 C ATOM 650 O SER A 87 13.662 7.801 -21.647 1.00 98.37 O ANISOU 650 O SER A 87 13098 11006 13273 -2343 1861 -809 O ATOM 651 CB SER A 87 13.777 7.987 -18.498 1.00100.58 C ANISOU 651 CB SER A 87 13953 11069 13193 -2499 2435 -492 C ATOM 652 OG SER A 87 13.287 9.312 -18.589 1.00 99.23 O ANISOU 652 OG SER A 87 13341 11219 13144 -2391 2457 -592 O ATOM 653 N ILE A 88 14.930 9.591 -21.157 1.00 93.64 N ANISOU 653 N ILE A 88 12473 10622 12484 -1834 1728 -649 N ATOM 654 CA ILE A 88 14.422 10.395 -22.271 1.00 92.69 C ANISOU 654 CA ILE A 88 11918 10765 12534 -1740 1564 -789 C ATOM 655 C ILE A 88 15.214 10.169 -23.556 1.00 91.06 C ANISOU 655 C ILE A 88 11762 10545 12291 -1557 1272 -822 C ATOM 656 O ILE A 88 14.631 10.056 -24.636 1.00 91.89 O ANISOU 656 O ILE A 88 11645 10757 12512 -1620 1130 -961 O ATOM 657 CB ILE A 88 14.418 11.886 -21.877 1.00 91.02 C ANISOU 657 CB ILE A 88 11494 10766 12325 -1537 1600 -761 C ATOM 658 CG1 ILE A 88 13.468 12.129 -20.699 1.00 93.25 C ANISOU 658 CG1 ILE A 88 11684 11081 12665 -1735 1931 -778 C ATOM 659 CG2 ILE A 88 14.023 12.746 -23.054 1.00 90.24 C ANISOU 659 CG2 ILE A 88 11016 10900 12373 -1382 1394 -863 C ATOM 660 CD1 ILE A 88 13.331 13.586 -20.314 1.00 92.23 C ANISOU 660 CD1 ILE A 88 11343 11135 12565 -1546 2002 -787 C ATOM 661 N MET A 89 16.540 10.101 -23.471 1.00 89.14 N ANISOU 661 N MET A 89 11800 10184 11884 -1332 1177 -710 N ATOM 662 CA MET A 89 17.383 10.169 -24.659 1.00 87.50 C ANISOU 662 CA MET A 89 11602 10008 11638 -1120 949 -749 C ATOM 663 C MET A 89 17.221 8.935 -25.547 1.00 89.31 C ANISOU 663 C MET A 89 11951 10081 11903 -1260 876 -864 C ATOM 664 O MET A 89 16.934 7.839 -25.063 1.00 93.07 O ANISOU 664 O MET A 89 12641 10327 12396 -1469 997 -861 O ATOM 665 CB MET A 89 18.850 10.317 -24.265 1.00 85.68 C ANISOU 665 CB MET A 89 11603 9692 11261 -864 896 -623 C ATOM 666 CG MET A 89 19.183 11.609 -23.527 1.00 83.93 C ANISOU 666 CG MET A 89 11282 9625 10981 -724 932 -539 C ATOM 667 SD MET A 89 18.855 13.100 -24.485 1.00 82.29 S ANISOU 667 SD MET A 89 10723 9695 10848 -594 840 -613 S ATOM 668 CE MET A 89 19.531 14.365 -23.410 1.00 80.71 C ANISOU 668 CE MET A 89 10542 9566 10557 -451 915 -514 C ATOM 669 N PRO A 90 17.408 9.090 -26.863 1.00 88.76 N ANISOU 669 N PRO A 90 11786 10113 11824 -1163 691 -972 N ATOM 670 CA PRO A 90 17.363 7.909 -27.739 1.00 90.69 C ANISOU 670 CA PRO A 90 12194 10192 12071 -1291 624 -1108 C ATOM 671 C PRO A 90 18.574 7.010 -27.581 1.00 90.68 C ANISOU 671 C PRO A 90 12569 9901 11985 -1150 654 -1050 C ATOM 672 O PRO A 90 18.434 5.782 -27.621 1.00 93.04 O ANISOU 672 O PRO A 90 13109 9934 12309 -1311 709 -1111 O ATOM 673 CB PRO A 90 17.283 8.521 -29.146 1.00 90.17 C ANISOU 673 CB PRO A 90 11946 10350 11967 -1197 417 -1226 C ATOM 674 CG PRO A 90 17.903 9.855 -29.006 1.00 87.43 C ANISOU 674 CG PRO A 90 11479 10181 11559 -927 390 -1105 C ATOM 675 CD PRO A 90 17.543 10.339 -27.632 1.00 86.93 C ANISOU 675 CD PRO A 90 11324 10139 11567 -965 549 -984 C ATOM 676 N PHE A 91 19.759 7.582 -27.386 1.00 88.50 N ANISOU 676 N PHE A 91 12341 9659 11627 -852 622 -941 N ATOM 677 CA PHE A 91 20.953 6.775 -27.205 1.00 88.92 C ANISOU 677 CA PHE A 91 12691 9461 11635 -667 629 -888 C ATOM 678 C PHE A 91 21.050 6.273 -25.765 1.00 89.94 C ANISOU 678 C PHE A 91 13043 9383 11747 -698 733 -716 C ATOM 679 O PHE A 91 20.334 6.722 -24.866 1.00 89.87 O ANISOU 679 O PHE A 91 12955 9457 11734 -847 826 -636 O ATOM 680 CB PHE A 91 22.199 7.569 -27.585 1.00 86.79 C ANISOU 680 CB PHE A 91 12337 9332 11308 -354 551 -861 C ATOM 681 CG PHE A 91 22.309 8.901 -26.899 1.00 84.59 C ANISOU 681 CG PHE A 91 11854 9285 11002 -273 550 -746 C ATOM 682 CD1 PHE A 91 22.905 9.010 -25.655 1.00 84.31 C ANISOU 682 CD1 PHE A 91 11912 9193 10930 -175 575 -595 C ATOM 683 CD2 PHE A 91 21.839 10.049 -27.509 1.00 83.19 C ANISOU 683 CD2 PHE A 91 11422 9367 10820 -287 510 -791 C ATOM 684 CE1 PHE A 91 23.014 10.236 -25.031 1.00 82.61 C ANISOU 684 CE1 PHE A 91 11535 9176 10676 -124 581 -520 C ATOM 685 CE2 PHE A 91 21.948 11.275 -26.888 1.00 81.50 C ANISOU 685 CE2 PHE A 91 11055 9322 10590 -213 529 -700 C ATOM 686 CZ PHE A 91 22.535 11.368 -25.650 1.00 81.17 C ANISOU 686 CZ PHE A 91 11105 9222 10513 -146 574 -578 C ATOM 687 N LYS A 92 21.961 5.328 -25.551 1.00 91.29 N ANISOU 687 N LYS A 92 13516 9273 11897 -539 720 -659 N ATOM 688 CA LYS A 92 22.060 4.621 -24.281 1.00 93.17 C ANISOU 688 CA LYS A 92 14066 9247 12086 -564 792 -482 C ATOM 689 C LYS A 92 23.087 5.302 -23.387 1.00 91.84 C ANISOU 689 C LYS A 92 13889 9180 11825 -289 703 -313 C ATOM 690 O LYS A 92 24.280 5.324 -23.707 1.00 91.39 O ANISOU 690 O LYS A 92 13815 9127 11782 15 580 -314 O ATOM 691 CB LYS A 92 22.440 3.159 -24.506 1.00 96.12 C ANISOU 691 CB LYS A 92 14814 9215 12494 -521 805 -498 C ATOM 692 CG LYS A 92 22.130 2.249 -23.329 1.00 99.05 C ANISOU 692 CG LYS A 92 15579 9248 12807 -659 916 -324 C ATOM 693 CD LYS A 92 22.707 0.861 -23.541 1.00103.36 C ANISOU 693 CD LYS A 92 16532 9348 13393 -533 910 -317 C ATOM 694 CE LYS A 92 22.103 -0.137 -22.572 1.00111.63 C ANISOU 694 CE LYS A 92 18021 10011 14383 -774 1064 -167 C ATOM 695 NZ LYS A 92 22.717 -1.481 -22.719 1.00119.03 N ANISOU 695 NZ LYS A 92 19405 10459 15362 -609 1054 -137 N ATOM 696 N ILE A 93 22.622 5.846 -22.268 1.00 91.61 N ANISOU 696 N ILE A 93 13864 9239 11705 -409 775 -189 N ATOM 697 CA ILE A 93 23.491 6.383 -21.229 1.00 91.14 C ANISOU 697 CA ILE A 93 13864 9247 11516 -207 683 -28 C ATOM 698 C ILE A 93 23.703 5.297 -20.189 1.00 94.30 C ANISOU 698 C ILE A 93 14717 9313 11801 -195 689 158 C ATOM 699 O ILE A 93 22.744 4.652 -19.750 1.00 96.36 O ANISOU 699 O ILE A 93 15205 9382 12027 -475 867 201 O ATOM 700 CB ILE A 93 22.890 7.646 -20.594 1.00 89.47 C ANISOU 700 CB ILE A 93 13445 9312 11236 -341 767 -15 C ATOM 701 CG1 ILE A 93 22.563 8.673 -21.673 1.00 86.89 C ANISOU 701 CG1 ILE A 93 12718 9268 11029 -349 761 -179 C ATOM 702 CG2 ILE A 93 23.849 8.225 -19.574 1.00 89.23 C ANISOU 702 CG2 ILE A 93 13489 9363 11052 -151 648 118 C ATOM 703 CD1 ILE A 93 21.826 9.884 -21.163 1.00 85.69 C ANISOU 703 CD1 ILE A 93 12358 9347 10853 -470 868 -188 C ATOM 704 N ILE A 94 24.958 5.083 -19.802 1.00 95.14 N ANISOU 704 N ILE A 94 14954 9344 11852 130 493 271 N ATOM 705 CA ILE A 94 25.323 4.000 -18.903 1.00 98.68 C ANISOU 705 CA ILE A 94 15866 9443 12183 225 437 474 C ATOM 706 C ILE A 94 26.322 4.520 -17.883 1.00 99.08 C ANISOU 706 C ILE A 94 15959 9617 12070 474 217 632 C ATOM 707 O ILE A 94 27.003 5.523 -18.100 1.00 96.81 O ANISOU 707 O ILE A 94 15322 9641 11821 628 87 552 O ATOM 708 CB ILE A 94 25.925 2.799 -19.655 1.00100.77 C ANISOU 708 CB ILE A 94 16306 9389 12594 439 368 437 C ATOM 709 CG1 ILE A 94 27.179 3.230 -20.419 1.00 99.32 C ANISOU 709 CG1 ILE A 94 15794 9396 12546 807 179 326 C ATOM 710 CG2 ILE A 94 24.904 2.196 -20.601 1.00101.03 C ANISOU 710 CG2 ILE A 94 16357 9275 12756 149 572 266 C ATOM 711 CD1 ILE A 94 27.856 2.101 -21.166 1.00101.68 C ANISOU 711 CD1 ILE A 94 16240 9391 13005 1062 136 263 C ATOM 712 N ALA A 95 26.404 3.818 -16.758 1.00102.41 N ANISOU 712 N ALA A 95 16836 9783 12293 496 169 859 N ATOM 713 CA ALA A 95 27.411 4.125 -15.755 1.00103.78 C ANISOU 713 CA ALA A 95 17111 10041 12280 755 -104 1024 C ATOM 714 C ALA A 95 28.769 3.597 -16.192 1.00105.23 C ANISOU 714 C ALA A 95 17223 10141 12620 1205 -393 1032 C ATOM 715 O ALA A 95 28.883 2.481 -16.705 1.00107.30 O ANISOU 715 O ALA A 95 17682 10071 13016 1332 -376 1042 O ATOM 716 CB ALA A 95 27.032 3.520 -14.406 1.00107.48 C ANISOU 716 CB ALA A 95 18148 10251 12437 633 -73 1284 C ATOM 717 N ALA A 96 29.803 4.405 -15.979 1.00104.54 N ANISOU 717 N ALA A 96 16842 10349 12528 1442 -646 1009 N ATOM 718 CA ALA A 96 31.168 3.981 -16.252 1.00106.55 C ANISOU 718 CA ALA A 96 16966 10572 12946 1890 -935 1012 C ATOM 719 C ALA A 96 31.642 3.050 -15.140 1.00111.44 C ANISOU 719 C ALA A 96 18066 10899 13377 2129 -1190 1293 C ATOM 720 O ALA A 96 30.879 2.661 -14.252 1.00113.22 O ANISOU 720 O ALA A 96 18773 10912 13333 1918 -1101 1486 O ATOM 721 CB ALA A 96 32.087 5.188 -16.402 1.00104.60 C ANISOU 721 CB ALA A 96 16205 10758 12779 2015 -1106 872 C ATOM 722 N ASP A 97 32.924 2.687 -15.171 1.00114.12 N ANISOU 722 N ASP A 97 18281 11224 13854 2583 -1510 1324 N ATOM 723 CA ASP A 97 33.456 1.816 -14.129 1.00122.21 C ANISOU 723 CA ASP A 97 19760 11972 14701 2877 -1818 1611 C ATOM 724 C ASP A 97 33.532 2.540 -12.789 1.00120.34 C ANISOU 724 C ASP A 97 19669 11962 14093 2781 -2040 1771 C ATOM 725 O ASP A 97 33.237 1.950 -11.744 1.00125.50 O ANISOU 725 O ASP A 97 20904 12356 14426 2757 -2124 2044 O ATOM 726 CB ASP A 97 34.827 1.278 -14.539 1.00134.60 C ANISOU 726 CB ASP A 97 21088 13495 16558 3428 -2124 1581 C ATOM 727 CG ASP A 97 34.745 0.288 -15.690 1.00139.80 C ANISOU 727 CG ASP A 97 21782 13811 17526 3559 -1901 1461 C ATOM 728 OD1 ASP A 97 33.682 -0.345 -15.858 1.00139.52 O ANISOU 728 OD1 ASP A 97 22150 13443 17418 3276 -1607 1502 O ATOM 729 OD2 ASP A 97 35.745 0.138 -16.425 1.00143.52 O ANISOU 729 OD2 ASP A 97 21873 14344 18315 3929 -2006 1306 O ATOM 730 N ASN A 98 33.911 3.819 -12.796 1.00117.60 N ANISOU 730 N ASN A 98 18845 12078 13759 2702 -2122 1601 N ATOM 731 CA ASN A 98 34.021 4.594 -11.566 1.00118.63 C ANISOU 731 CA ASN A 98 19096 12447 13531 2589 -2331 1703 C ATOM 732 C ASN A 98 32.759 5.386 -11.245 1.00115.44 C ANISOU 732 C ASN A 98 18821 12146 12896 2082 -1967 1653 C ATOM 733 O ASN A 98 32.784 6.223 -10.337 1.00115.73 O ANISOU 733 O ASN A 98 18908 12416 12647 1938 -2071 1671 O ATOM 734 CB ASN A 98 35.226 5.541 -11.632 1.00118.37 C ANISOU 734 CB ASN A 98 18494 12844 13636 2785 -2651 1538 C ATOM 735 CG ASN A 98 35.089 6.610 -12.708 1.00113.24 C ANISOU 735 CG ASN A 98 17272 12498 13255 2574 -2374 1226 C ATOM 736 OD1 ASN A 98 34.045 6.753 -13.341 1.00109.73 O ANISOU 736 OD1 ASN A 98 16849 11982 12863 2282 -1977 1138 O ATOM 737 ND2 ASN A 98 36.157 7.374 -12.911 1.00113.22 N ANISOU 737 ND2 ASN A 98 16757 12837 13423 2718 -2595 1061 N ATOM 738 N GLY A 99 31.667 5.155 -11.968 1.00122.32 N ANISOU 738 N GLY A 99 19726 12857 13892 1813 -1549 1572 N ATOM 739 CA GLY A 99 30.409 5.809 -11.692 1.00119.71 C ANISOU 739 CA GLY A 99 19486 12606 13392 1362 -1188 1519 C ATOM 740 C GLY A 99 30.093 6.999 -12.573 1.00110.56 C ANISOU 740 C GLY A 99 17781 11775 12453 1180 -982 1240 C ATOM 741 O GLY A 99 28.950 7.473 -12.550 1.00108.53 O ANISOU 741 O GLY A 99 17541 11559 12137 835 -652 1172 O ATOM 742 N ASP A 100 31.058 7.496 -13.342 1.00103.93 N ANISOU 742 N ASP A 100 16462 11160 11865 1402 -1155 1079 N ATOM 743 CA ASP A 100 30.798 8.645 -14.197 1.00 99.71 C ANISOU 743 CA ASP A 100 15463 10907 11514 1236 -962 839 C ATOM 744 C ASP A 100 29.795 8.282 -15.287 1.00 97.42 C ANISOU 744 C ASP A 100 15116 10479 11422 1070 -636 741 C ATOM 745 O ASP A 100 29.634 7.116 -15.656 1.00 98.94 O ANISOU 745 O ASP A 100 15516 10379 11700 1147 -597 804 O ATOM 746 CB ASP A 100 32.097 9.158 -14.825 1.00 99.16 C ANISOU 746 CB ASP A 100 14925 11078 11673 1492 -1185 693 C ATOM 747 CG ASP A 100 33.035 9.798 -13.809 1.00101.20 C ANISOU 747 CG ASP A 100 15132 11561 11759 1586 -1512 726 C ATOM 748 OD1 ASP A 100 32.571 10.174 -12.711 1.00104.85 O ANISOU 748 OD1 ASP A 100 15886 12052 11902 1397 -1517 816 O ATOM 749 OD2 ASP A 100 34.240 9.934 -14.109 1.00102.27 O ANISOU 749 OD2 ASP A 100 14925 11857 12076 1835 -1758 642 O ATOM 750 N ALA A 101 29.111 9.297 -15.799 1.00 94.12 N ANISOU 750 N ALA A 101 14425 10264 11074 843 -415 582 N ATOM 751 CA ALA A 101 28.097 9.091 -16.826 1.00 92.19 C ANISOU 751 CA ALA A 101 14087 9943 10998 669 -146 475 C ATOM 752 C ALA A 101 28.753 8.982 -18.196 1.00 90.91 C ANISOU 752 C ALA A 101 13617 9825 11100 858 -193 328 C ATOM 753 O ALA A 101 29.442 9.909 -18.636 1.00 89.30 O ANISOU 753 O ALA A 101 13081 9866 10983 943 -258 213 O ATOM 754 CB ALA A 101 27.084 10.232 -16.815 1.00 89.77 C ANISOU 754 CB ALA A 101 13611 9832 10663 393 81 375 C ATOM 755 N TRP A 102 28.528 7.856 -18.870 1.00 91.95 N ANISOU 755 N TRP A 102 13885 9705 11346 897 -132 319 N ATOM 756 CA TRP A 102 29.060 7.594 -20.198 1.00 91.30 C ANISOU 756 CA TRP A 102 13584 9622 11485 1058 -132 165 C ATOM 757 C TRP A 102 27.915 7.248 -21.141 1.00 90.30 C ANISOU 757 C TRP A 102 13478 9398 11432 826 85 55 C ATOM 758 O TRP A 102 26.757 7.143 -20.736 1.00 90.36 O ANISOU 758 O TRP A 102 13637 9337 11360 555 226 99 O ATOM 759 CB TRP A 102 30.087 6.455 -20.177 1.00 94.42 C ANISOU 759 CB TRP A 102 14131 9782 11962 1389 -301 227 C ATOM 760 CG TRP A 102 31.430 6.836 -19.625 1.00 95.66 C ANISOU 760 CG TRP A 102 14117 10102 12129 1678 -562 269 C ATOM 761 CD1 TRP A 102 31.694 7.786 -18.685 1.00 95.26 C ANISOU 761 CD1 TRP A 102 13981 10287 11929 1631 -693 330 C ATOM 762 CD2 TRP A 102 32.695 6.278 -19.996 1.00 97.97 C ANISOU 762 CD2 TRP A 102 14274 10344 12606 2053 -726 227 C ATOM 763 NE1 TRP A 102 33.043 7.850 -18.439 1.00 97.24 N ANISOU 763 NE1 TRP A 102 14037 10653 12255 1934 -958 329 N ATOM 764 CE2 TRP A 102 33.681 6.935 -19.233 1.00 98.96 C ANISOU 764 CE2 TRP A 102 14198 10707 12697 2211 -979 269 C ATOM 765 CE3 TRP A 102 33.090 5.286 -20.897 1.00102.19 C ANISOU 765 CE3 TRP A 102 14831 10656 13343 2271 -675 139 C ATOM 766 CZ2 TRP A 102 35.034 6.632 -19.343 1.00101.68 C ANISOU 766 CZ2 TRP A 102 14309 11096 13229 2586 -1195 229 C ATOM 767 CZ3 TRP A 102 34.435 4.987 -21.005 1.00111.65 C ANISOU 767 CZ3 TRP A 102 15822 11876 14725 2664 -856 100 C ATOM 768 CH2 TRP A 102 35.391 5.658 -20.232 1.00107.28 C ANISOU 768 CH2 TRP A 102 15016 11585 14159 2822 -1120 147 C ATOM 769 N VAL A 103 28.247 7.068 -22.416 1.00 89.76 N ANISOU 769 N VAL A 103 13247 9339 11517 921 115 -106 N ATOM 770 CA VAL A 103 27.274 6.659 -23.420 1.00 89.38 C ANISOU 770 CA VAL A 103 13227 9205 11527 719 268 -235 C ATOM 771 C VAL A 103 27.831 5.460 -24.168 1.00 91.59 C ANISOU 771 C VAL A 103 13662 9221 11919 897 262 -315 C ATOM 772 O VAL A 103 29.048 5.306 -24.306 1.00 92.58 O ANISOU 772 O VAL A 103 13715 9337 12124 1205 167 -332 O ATOM 773 CB VAL A 103 26.927 7.797 -24.404 1.00 86.62 C ANISOU 773 CB VAL A 103 12554 9154 11205 611 332 -382 C ATOM 774 CG1 VAL A 103 26.168 8.891 -23.693 1.00 84.91 C ANISOU 774 CG1 VAL A 103 12220 9139 10904 427 373 -317 C ATOM 775 CG2 VAL A 103 28.185 8.357 -25.036 1.00 85.93 C ANISOU 775 CG2 VAL A 103 12236 9231 11181 851 274 -464 C ATOM 776 N GLU A 104 26.935 4.608 -24.656 1.00 92.76 N ANISOU 776 N GLU A 104 14009 9150 12087 697 374 -387 N ATOM 777 CA GLU A 104 27.321 3.384 -25.346 1.00 95.34 C ANISOU 777 CA GLU A 104 14550 9164 12509 828 402 -484 C ATOM 778 C GLU A 104 26.958 3.493 -26.821 1.00 94.49 C ANISOU 778 C GLU A 104 14307 9157 12439 705 491 -728 C ATOM 779 O GLU A 104 25.781 3.654 -27.165 1.00 93.79 O ANISOU 779 O GLU A 104 14190 9138 12309 387 552 -799 O ATOM 780 CB GLU A 104 26.647 2.167 -24.718 1.00 98.27 C ANISOU 780 CB GLU A 104 15344 9135 12857 675 463 -384 C ATOM 781 CG GLU A 104 26.944 0.865 -25.442 1.00101.33 C ANISOU 781 CG GLU A 104 16006 9143 13350 785 516 -502 C ATOM 782 CD GLU A 104 26.327 -0.338 -24.756 1.00104.69 C ANISOU 782 CD GLU A 104 16902 9122 13752 623 591 -383 C ATOM 783 OE1 GLU A 104 26.654 -0.592 -23.577 1.00106.25 O ANISOU 783 OE1 GLU A 104 17328 9163 13880 755 516 -139 O ATOM 784 OE2 GLU A 104 25.505 -1.026 -25.396 1.00106.10 O ANISOU 784 OE2 GLU A 104 17242 9104 13967 344 724 -534 O ATOM 785 N VAL A 105 27.966 3.391 -27.685 1.00 95.02 N ANISOU 785 N VAL A 105 14288 9235 12578 959 496 -863 N ATOM 786 CA VAL A 105 27.793 3.470 -29.131 1.00 94.75 C ANISOU 786 CA VAL A 105 14181 9290 12532 873 584 -1100 C ATOM 787 C VAL A 105 28.297 2.169 -29.737 1.00 98.08 C ANISOU 787 C VAL A 105 14867 9358 13039 1029 661 -1243 C ATOM 788 O VAL A 105 29.484 1.842 -29.610 1.00 99.61 O ANISOU 788 O VAL A 105 15051 9452 13345 1378 655 -1235 O ATOM 789 CB VAL A 105 28.538 4.670 -29.736 1.00 92.64 C ANISOU 789 CB VAL A 105 13580 9375 12244 1002 589 -1162 C ATOM 790 CG1 VAL A 105 28.105 4.880 -31.176 1.00 92.42 C ANISOU 790 CG1 VAL A 105 13529 9461 12124 847 669 -1371 C ATOM 791 CG2 VAL A 105 28.301 5.922 -28.916 1.00 89.88 C ANISOU 791 CG2 VAL A 105 13002 9310 11840 923 512 -1001 C ATOM 792 N LYS A 106 27.399 1.435 -30.398 1.00100.29 N ANISOU 792 N LYS A 106 15371 9453 13282 772 732 -1391 N ATOM 793 CA LYS A 106 27.741 0.172 -31.051 1.00105.90 C ANISOU 793 CA LYS A 106 16387 9791 14061 872 833 -1566 C ATOM 794 C LYS A 106 28.447 -0.776 -30.084 1.00105.75 C ANISOU 794 C LYS A 106 16613 9393 14176 1161 813 -1410 C ATOM 795 O LYS A 106 29.445 -1.416 -30.423 1.00108.26 O ANISOU 795 O LYS A 106 17021 9501 14613 1493 867 -1500 O ATOM 796 CB LYS A 106 28.594 0.412 -32.298 1.00111.23 C ANISOU 796 CB LYS A 106 16936 10601 14727 1059 927 -1793 C ATOM 797 CG LYS A 106 27.882 1.159 -33.412 1.00113.63 C ANISOU 797 CG LYS A 106 17114 11208 14853 780 939 -1955 C ATOM 798 CD LYS A 106 28.803 1.361 -34.605 1.00110.76 C ANISOU 798 CD LYS A 106 16690 10952 14442 963 1074 -2167 C ATOM 799 CE LYS A 106 28.047 1.903 -35.805 1.00108.66 C ANISOU 799 CE LYS A 106 16420 10922 13946 680 1070 -2333 C ATOM 800 NZ LYS A 106 27.008 0.946 -36.269 1.00110.92 N ANISOU 800 NZ LYS A 106 17006 10979 14160 384 1044 -2498 N ATOM 801 N GLY A 107 27.929 -0.856 -28.861 1.00105.61 N ANISOU 801 N GLY A 107 16713 9283 14133 1048 737 -1169 N ATOM 802 CA GLY A 107 28.500 -1.739 -27.865 1.00108.55 C ANISOU 802 CA GLY A 107 17380 9281 14582 1308 685 -976 C ATOM 803 C GLY A 107 29.801 -1.276 -27.252 1.00108.33 C ANISOU 803 C GLY A 107 17134 9401 14625 1749 536 -832 C ATOM 804 O GLY A 107 30.407 -2.030 -26.485 1.00117.46 O ANISOU 804 O GLY A 107 18528 10252 15850 2039 445 -670 O ATOM 805 N GLN A 108 30.260 -0.070 -27.566 1.00105.29 N ANISOU 805 N GLN A 108 16313 9467 14227 1807 497 -887 N ATOM 806 CA GLN A 108 31.482 0.470 -26.992 1.00105.23 C ANISOU 806 CA GLN A 108 16035 9652 14298 2172 347 -780 C ATOM 807 C GLN A 108 31.137 1.545 -25.977 1.00102.40 C ANISOU 807 C GLN A 108 15510 9598 13799 2011 219 -584 C ATOM 808 O GLN A 108 30.260 2.380 -26.215 1.00 99.35 O ANISOU 808 O GLN A 108 14990 9458 13300 1682 286 -623 O ATOM 809 CB GLN A 108 32.404 1.053 -28.064 1.00104.56 C ANISOU 809 CB GLN A 108 15578 9834 14316 2351 432 -1004 C ATOM 810 CG GLN A 108 33.370 0.053 -28.665 1.00108.44 C ANISOU 810 CG GLN A 108 16148 10049 15006 2721 515 -1159 C ATOM 811 CD GLN A 108 34.657 0.699 -29.139 1.00112.08 C ANISOU 811 CD GLN A 108 16163 10806 15616 3009 549 -1292 C ATOM 812 OE1 GLN A 108 34.950 1.848 -28.807 1.00109.66 O ANISOU 812 OE1 GLN A 108 15511 10881 15275 2961 464 -1228 O ATOM 813 NE2 GLN A 108 35.435 -0.042 -29.920 1.00121.83 N ANISOU 813 NE2 GLN A 108 17406 11854 17028 3296 699 -1497 N ATOM 814 N LYS A 109 31.822 1.512 -24.841 1.00103.82 N ANISOU 814 N LYS A 109 15713 9753 13983 2256 22 -379 N ATOM 815 CA LYS A 109 31.647 2.533 -23.823 1.00101.67 C ANISOU 815 CA LYS A 109 15304 9765 13561 2132 -105 -212 C ATOM 816 C LYS A 109 32.502 3.740 -24.174 1.00 99.60 C ANISOU 816 C LYS A 109 14554 9924 13364 2238 -151 -322 C ATOM 817 O LYS A 109 33.697 3.606 -24.453 1.00101.42 O ANISOU 817 O LYS A 109 14576 10193 13764 2573 -219 -399 O ATOM 818 CB LYS A 109 32.022 1.990 -22.447 1.00104.59 C ANISOU 818 CB LYS A 109 15949 9935 13857 2330 -321 52 C ATOM 819 CG LYS A 109 31.246 0.750 -22.028 1.00109.20 C ANISOU 819 CG LYS A 109 17079 10048 14366 2221 -253 188 C ATOM 820 CD LYS A 109 31.848 0.136 -20.773 1.00120.53 C ANISOU 820 CD LYS A 109 18826 11250 15720 2508 -496 465 C ATOM 821 CE LYS A 109 31.140 -1.151 -20.371 1.00123.82 C ANISOU 821 CE LYS A 109 19850 11139 16059 2403 -401 617 C ATOM 822 NZ LYS A 109 29.724 -0.916 -19.974 1.00119.69 N ANISOU 822 NZ LYS A 109 19516 10622 15337 1881 -199 671 N ATOM 823 N MET A 110 31.882 4.916 -24.172 1.00 96.17 N ANISOU 823 N MET A 110 13935 9794 12814 1951 -95 -337 N ATOM 824 CA MET A 110 32.520 6.151 -24.592 1.00 94.13 C ANISOU 824 CA MET A 110 13259 9908 12597 1969 -88 -448 C ATOM 825 C MET A 110 32.185 7.248 -23.596 1.00 92.14 C ANISOU 825 C MET A 110 12927 9888 12194 1791 -175 -323 C ATOM 826 O MET A 110 31.033 7.381 -23.171 1.00 90.87 O ANISOU 826 O MET A 110 12948 9687 11891 1526 -113 -241 O ATOM 827 CB MET A 110 32.056 6.576 -25.991 1.00 92.12 C ANISOU 827 CB MET A 110 12881 9767 12352 1787 126 -646 C ATOM 828 CG MET A 110 32.212 5.502 -27.053 1.00 94.16 C ANISOU 828 CG MET A 110 13277 9788 12713 1900 251 -805 C ATOM 829 SD MET A 110 32.316 6.194 -28.708 1.00 92.76 S ANISOU 829 SD MET A 110 12885 9831 12531 1801 463 -1055 S ATOM 830 CE MET A 110 33.798 7.190 -28.557 1.00 97.92 C ANISOU 830 CE MET A 110 13109 10791 13305 2015 436 -1085 C ATOM 831 N ALA A 111 33.210 8.037 -23.229 1.00 92.26 N ANISOU 831 N ALA A 111 12653 10148 12252 1928 -304 -333 N ATOM 832 CA ALA A 111 33.223 9.181 -22.332 1.00 90.93 C ANISOU 832 CA ALA A 111 12364 10224 11960 1797 -400 -264 C ATOM 833 C ALA A 111 32.875 10.452 -23.101 1.00 87.86 C ANISOU 833 C ALA A 111 11739 10077 11565 1573 -221 -392 C ATOM 834 O ALA A 111 33.319 10.631 -24.240 1.00 87.52 O ANISOU 834 O ALA A 111 11498 10110 11645 1618 -96 -545 O ATOM 835 CB ALA A 111 34.584 9.337 -21.672 1.00 93.28 C ANISOU 835 CB ALA A 111 12449 10659 12332 2051 -646 -246 C ATOM 836 N PRO A 112 32.098 11.325 -22.471 1.00 78.89 N ANISOU 836 N PRO A 112 10989 10343 8644 738 -328 -528 N ATOM 837 CA PRO A 112 31.648 12.569 -23.120 1.00 77.09 C ANISOU 837 CA PRO A 112 10558 10236 8494 627 -122 -572 C ATOM 838 C PRO A 112 32.787 13.371 -23.731 1.00 77.08 C ANISOU 838 C PRO A 112 10299 10445 8543 763 -40 -623 C ATOM 839 O PRO A 112 32.605 13.963 -24.808 1.00 76.28 O ANISOU 839 O PRO A 112 10107 10393 8483 795 100 -659 O ATOM 840 CB PRO A 112 30.975 13.330 -21.970 1.00 76.42 C ANISOU 840 CB PRO A 112 10483 10164 8390 346 -32 -534 C ATOM 841 CG PRO A 112 30.479 12.235 -21.068 1.00 77.70 C ANISOU 841 CG PRO A 112 10926 10136 8462 267 -140 -463 C ATOM 842 CD PRO A 112 31.472 11.120 -21.153 1.00 79.38 C ANISOU 842 CD PRO A 112 11253 10291 8617 519 -356 -446 C ATOM 843 N PRO A 113 33.968 13.446 -23.095 1.00 78.30 N ANISOU 843 N PRO A 113 10330 10719 8702 839 -121 -631 N ATOM 844 CA PRO A 113 35.048 14.223 -23.722 1.00 78.74 C ANISOU 844 CA PRO A 113 10094 10972 8851 937 -5 -691 C ATOM 845 C PRO A 113 35.445 13.734 -25.104 1.00 79.45 C ANISOU 845 C PRO A 113 10154 11074 8959 1181 65 -742 C ATOM 846 O PRO A 113 35.965 14.530 -25.895 1.00 80.10 O ANISOU 846 O PRO A 113 10042 11292 9098 1206 262 -776 O ATOM 847 CB PRO A 113 36.202 14.082 -22.724 1.00 80.57 C ANISOU 847 CB PRO A 113 10206 11295 9112 1002 -178 -713 C ATOM 848 CG PRO A 113 35.556 13.896 -21.449 1.00 80.37 C ANISOU 848 CG PRO A 113 10405 11158 8974 836 -310 -649 C ATOM 849 CD PRO A 113 34.343 13.067 -21.719 1.00 79.55 C ANISOU 849 CD PRO A 113 10587 10848 8789 802 -305 -593 C ATOM 850 N GLN A 114 35.224 12.456 -25.425 1.00 80.20 N ANISOU 850 N GLN A 114 10461 11018 8995 1358 -77 -750 N ATOM 851 CA GLN A 114 35.531 11.975 -26.768 1.00 81.10 C ANISOU 851 CA GLN A 114 10593 11129 9093 1605 -8 -817 C ATOM 852 C GLN A 114 34.587 12.591 -27.791 1.00 79.65 C ANISOU 852 C GLN A 114 10491 10909 8865 1519 156 -813 C ATOM 853 O GLN A 114 35.019 13.137 -28.813 1.00 80.11 O ANISOU 853 O GLN A 114 10459 11072 8908 1612 349 -848 O ATOM 854 CB GLN A 114 35.439 10.450 -26.823 1.00 82.43 C ANISOU 854 CB GLN A 114 11007 11105 9207 1809 -231 -838 C ATOM 855 CG GLN A 114 36.202 9.713 -25.733 1.00 84.52 C ANISOU 855 CG GLN A 114 11281 11342 9491 1909 -461 -827 C ATOM 856 CD GLN A 114 36.459 8.258 -26.088 1.00 89.41 C ANISOU 856 CD GLN A 114 12107 11788 10075 2200 -655 -875 C ATOM 857 OE1 GLN A 114 35.996 7.344 -25.405 1.00 90.50 O ANISOU 857 OE1 GLN A 114 12522 11708 10157 2177 -868 -816 O ATOM 858 NE2 GLN A 114 37.207 8.038 -27.165 1.00 89.45 N ANISOU 858 NE2 GLN A 114 12000 11878 10109 2477 -565 -986 N ATOM 859 N ILE A 115 33.286 12.513 -27.522 1.00 78.27 N ANISOU 859 N ILE A 115 10492 10577 8669 1344 84 -775 N ATOM 860 CA ILE A 115 32.286 13.053 -28.435 1.00 77.21 C ANISOU 860 CA ILE A 115 10439 10384 8512 1280 171 -788 C ATOM 861 C ILE A 115 32.472 14.562 -28.603 1.00 76.36 C ANISOU 861 C ILE A 115 10149 10431 8433 1155 385 -765 C ATOM 862 O ILE A 115 32.637 15.082 -29.726 1.00 76.74 O ANISOU 862 O ILE A 115 10209 10523 8425 1250 527 -782 O ATOM 863 CB ILE A 115 30.887 12.681 -27.917 1.00 76.33 C ANISOU 863 CB ILE A 115 10479 10087 8438 1094 44 -770 C ATOM 864 CG1 ILE A 115 30.803 11.167 -27.711 1.00 77.60 C ANISOU 864 CG1 ILE A 115 10841 10066 8577 1196 -159 -780 C ATOM 865 CG2 ILE A 115 29.824 13.090 -28.881 1.00 75.74 C ANISOU 865 CG2 ILE A 115 10476 9930 8370 1067 61 -813 C ATOM 866 CD1 ILE A 115 30.904 10.710 -26.280 1.00 77.96 C ANISOU 866 CD1 ILE A 115 10928 10063 8630 1066 -247 -707 C ATOM 867 N SER A 116 32.493 15.287 -27.481 1.00 82.75 N ANISOU 867 N SER A 116 10821 11310 9311 944 414 -724 N ATOM 868 CA SER A 116 32.766 16.717 -27.559 1.00 79.68 C ANISOU 868 CA SER A 116 10264 11045 8964 818 604 -707 C ATOM 869 C SER A 116 34.087 16.988 -28.267 1.00 84.36 C ANISOU 869 C SER A 116 10703 11788 9562 960 761 -724 C ATOM 870 O SER A 116 34.255 18.040 -28.895 1.00 84.70 O ANISOU 870 O SER A 116 10685 11889 9608 905 960 -705 O ATOM 871 CB SER A 116 32.766 17.329 -26.160 1.00 81.52 C ANISOU 871 CB SER A 116 10384 11329 9262 597 584 -684 C ATOM 872 OG SER A 116 31.488 17.205 -25.565 1.00 83.25 O ANISOU 872 OG SER A 116 10733 11418 9479 447 513 -674 O ATOM 873 N ALA A 117 35.022 16.038 -28.207 1.00 78.08 N ANISOU 873 N ALA A 117 9850 11043 8775 1148 688 -762 N ATOM 874 CA ALA A 117 36.279 16.194 -28.930 1.00 80.05 C ANISOU 874 CA ALA A 117 9916 11441 9057 1300 869 -803 C ATOM 875 C ALA A 117 36.089 16.037 -30.431 1.00 80.76 C ANISOU 875 C ALA A 117 10183 11486 9014 1472 1017 -819 C ATOM 876 O ALA A 117 36.847 16.620 -31.209 1.00 82.25 O ANISOU 876 O ALA A 117 10265 11788 9198 1517 1277 -826 O ATOM 877 CB ALA A 117 37.315 15.192 -28.421 1.00 81.87 C ANISOU 877 CB ALA A 117 10015 11734 9359 1488 724 -865 C ATOM 878 N GLU A 118 35.105 15.244 -30.861 1.00 80.10 N ANISOU 878 N GLU A 118 10383 11232 8818 1565 859 -832 N ATOM 879 CA GLU A 118 34.781 15.214 -32.284 1.00 80.86 C ANISOU 879 CA GLU A 118 10703 11265 8754 1718 961 -855 C ATOM 880 C GLU A 118 34.299 16.581 -32.748 1.00 80.13 C ANISOU 880 C GLU A 118 10650 11177 8621 1556 1131 -789 C ATOM 881 O GLU A 118 34.757 17.105 -33.776 1.00 81.62 O ANISOU 881 O GLU A 118 10899 11416 8698 1635 1368 -775 O ATOM 882 CB GLU A 118 33.731 14.140 -32.577 1.00 88.01 C ANISOU 882 CB GLU A 118 11897 11965 9580 1821 705 -900 C ATOM 883 CG GLU A 118 34.220 12.711 -32.398 1.00 99.68 C ANISOU 883 CG GLU A 118 13423 13390 11062 2031 542 -969 C ATOM 884 CD GLU A 118 35.364 12.355 -33.335 1.00106.76 C ANISOU 884 CD GLU A 118 14299 14390 11877 2317 715 -1045 C ATOM 885 OE1 GLU A 118 35.308 12.736 -34.526 1.00101.97 O ANISOU 885 OE1 GLU A 118 13841 13790 11114 2413 888 -1063 O ATOM 886 OE2 GLU A 118 36.325 11.700 -32.877 1.00112.84 O ANISOU 886 OE2 GLU A 118 14913 15229 12732 2456 681 -1092 O ATOM 887 N VAL A 119 33.389 17.190 -31.981 1.00 78.18 N ANISOU 887 N VAL A 119 10382 10865 8456 1330 1027 -747 N ATOM 888 CA VAL A 119 32.934 18.536 -32.342 1.00 77.68 C ANISOU 888 CA VAL A 119 10357 10785 8373 1188 1162 -690 C ATOM 889 C VAL A 119 34.114 19.503 -32.388 1.00 78.88 C ANISOU 889 C VAL A 119 10309 11091 8571 1108 1449 -644 C ATOM 890 O VAL A 119 34.297 20.262 -33.356 1.00 80.09 O ANISOU 890 O VAL A 119 10572 11239 8619 1125 1663 -597 O ATOM 891 CB VAL A 119 31.845 19.016 -31.367 1.00 75.69 C ANISOU 891 CB VAL A 119 10068 10453 8238 970 1017 -678 C ATOM 892 CG1 VAL A 119 31.665 20.512 -31.467 1.00 75.44 C ANISOU 892 CG1 VAL A 119 10011 10422 8230 816 1165 -625 C ATOM 893 CG2 VAL A 119 30.543 18.338 -31.684 1.00 75.13 C ANISOU 893 CG2 VAL A 119 10200 10210 8138 1030 791 -727 C ATOM 894 N LEU A 120 34.940 19.477 -31.340 1.00 78.93 N ANISOU 894 N LEU A 120 10031 11224 8736 1013 1451 -659 N ATOM 895 CA LEU A 120 36.121 20.329 -31.300 1.00 80.48 C ANISOU 895 CA LEU A 120 9975 11569 9036 915 1701 -641 C ATOM 896 C LEU A 120 37.002 20.106 -32.519 1.00 83.05 C ANISOU 896 C LEU A 120 10318 11968 9271 1099 1960 -653 C ATOM 897 O LEU A 120 37.546 21.061 -33.080 1.00 84.61 O ANISOU 897 O LEU A 120 10465 12213 9470 1006 2255 -603 O ATOM 898 CB LEU A 120 36.909 20.069 -30.017 1.00 80.66 C ANISOU 898 CB LEU A 120 9694 11709 9243 844 1584 -690 C ATOM 899 CG LEU A 120 36.251 20.488 -28.705 1.00 78.75 C ANISOU 899 CG LEU A 120 9425 11420 9075 631 1394 -679 C ATOM 900 CD1 LEU A 120 37.101 20.055 -27.530 1.00 79.51 C ANISOU 900 CD1 LEU A 120 9290 11621 9298 618 1238 -734 C ATOM 901 CD2 LEU A 120 36.032 21.987 -28.681 1.00 78.39 C ANISOU 901 CD2 LEU A 120 9351 11353 9080 400 1550 -632 C ATOM 902 N LYS A 121 37.144 18.852 -32.952 1.00 83.84 N ANISOU 902 N LYS A 121 10511 12063 9283 1358 1873 -720 N ATOM 903 CA LYS A 121 37.962 18.570 -34.125 1.00 86.63 C ANISOU 903 CA LYS A 121 10902 12488 9527 1563 2142 -753 C ATOM 904 C LYS A 121 37.383 19.225 -35.368 1.00 87.21 C ANISOU 904 C LYS A 121 11321 12455 9360 1577 2323 -681 C ATOM 905 O LYS A 121 38.132 19.730 -36.212 1.00 89.76 O ANISOU 905 O LYS A 121 11648 12850 9608 1597 2679 -651 O ATOM 906 CB LYS A 121 38.102 17.064 -34.334 1.00 87.41 C ANISOU 906 CB LYS A 121 11083 12565 9563 1861 1975 -857 C ATOM 907 CG LYS A 121 39.209 16.423 -33.511 1.00 88.67 C ANISOU 907 CG LYS A 121 10886 12866 9938 1941 1913 -943 C ATOM 908 CD LYS A 121 39.568 15.048 -34.048 1.00 90.47 C ANISOU 908 CD LYS A 121 11214 13074 10088 2286 1843 -1056 C ATOM 909 CE LYS A 121 38.366 14.120 -34.042 1.00 88.64 C ANISOU 909 CE LYS A 121 11345 12622 9711 2374 1508 -1060 C ATOM 910 NZ LYS A 121 38.701 12.788 -34.619 1.00 90.65 N ANISOU 910 NZ LYS A 121 11738 12823 9881 2715 1429 -1180 N ATOM 911 N LYS A 122 36.053 19.230 -35.505 1.00 85.27 N ANISOU 911 N LYS A 122 11375 12031 8993 1570 2084 -654 N ATOM 912 CA LYS A 122 35.473 19.938 -36.644 1.00 86.09 C ANISOU 912 CA LYS A 122 11831 12015 8865 1596 2199 -585 C ATOM 913 C LYS A 122 35.798 21.425 -36.587 1.00 86.63 C ANISOU 913 C LYS A 122 11813 12109 8993 1353 2461 -473 C ATOM 914 O LYS A 122 36.159 22.029 -37.607 1.00 89.00 O ANISOU 914 O LYS A 122 12308 12391 9116 1377 2757 -402 O ATOM 915 CB LYS A 122 33.962 19.723 -36.716 1.00 84.19 C ANISOU 915 CB LYS A 122 11865 11578 8546 1628 1848 -601 C ATOM 916 CG LYS A 122 33.355 20.255 -38.015 1.00 85.61 C ANISOU 916 CG LYS A 122 12464 11612 8451 1734 1887 -554 C ATOM 917 CD LYS A 122 31.867 19.977 -38.133 1.00 84.25 C ANISOU 917 CD LYS A 122 12520 11247 8245 1791 1497 -606 C ATOM 918 CE LYS A 122 31.288 20.567 -39.414 1.00 86.07 C ANISOU 918 CE LYS A 122 13187 11322 8194 1919 1484 -566 C ATOM 919 NZ LYS A 122 31.687 19.817 -40.640 1.00 88.74 N ANISOU 919 NZ LYS A 122 13853 11641 8224 2197 1562 -614 N ATOM 920 N MET A 123 35.699 22.033 -35.401 1.00 84.80 N ANISOU 920 N MET A 123 11318 11904 8997 1113 2368 -456 N ATOM 921 CA MET A 123 36.033 23.453 -35.291 1.00 85.51 C ANISOU 921 CA MET A 123 11327 11995 9169 870 2599 -362 C ATOM 922 C MET A 123 37.496 23.713 -35.642 1.00 88.54 C ANISOU 922 C MET A 123 11491 12535 9617 824 2994 -348 C ATOM 923 O MET A 123 37.809 24.637 -36.406 1.00 90.70 O ANISOU 923 O MET A 123 11902 12764 9797 733 3306 -249 O ATOM 924 CB MET A 123 35.721 23.957 -33.884 1.00 85.38 C ANISOU 924 CB MET A 123 11065 11983 9391 639 2412 -379 C ATOM 925 CG MET A 123 34.247 23.894 -33.498 1.00 93.51 C ANISOU 925 CG MET A 123 12273 12862 10397 641 2091 -397 C ATOM 926 SD MET A 123 33.190 24.944 -34.508 1.00 99.03 S ANISOU 926 SD MET A 123 13368 13341 10918 654 2097 -313 S ATOM 927 CE MET A 123 32.634 23.787 -35.756 1.00117.61 C ANISOU 927 CE MET A 123 16069 15614 13005 977 1959 -353 C ATOM 928 N LYS A 124 38.402 22.899 -35.095 1.00 89.12 N ANISOU 928 N LYS A 124 11220 12780 9859 889 2987 -447 N ATOM 929 CA LYS A 124 39.828 23.049 -35.366 1.00 92.40 C ANISOU 929 CA LYS A 124 11338 13367 10402 858 3351 -471 C ATOM 930 C LYS A 124 40.128 22.900 -36.851 1.00 95.36 C ANISOU 930 C LYS A 124 11989 13731 10512 1035 3697 -437 C ATOM 931 O LYS A 124 40.931 23.659 -37.407 1.00 98.40 O ANISOU 931 O LYS A 124 12304 14167 10916 908 4117 -378 O ATOM 932 CB LYS A 124 40.613 22.023 -34.543 1.00 92.62 C ANISOU 932 CB LYS A 124 10979 13562 10650 973 3194 -611 C ATOM 933 CG LYS A 124 42.075 21.838 -34.930 1.00 96.49 C ANISOU 933 CG LYS A 124 11125 14246 11292 1037 3536 -689 C ATOM 934 CD LYS A 124 42.731 20.737 -34.097 1.00 96.76 C ANISOU 934 CD LYS A 124 10813 14414 11537 1208 3288 -841 C ATOM 935 CE LYS A 124 44.097 20.353 -34.650 1.00101.01 C ANISOU 935 CE LYS A 124 11020 15141 12217 1357 3617 -953 C ATOM 936 NZ LYS A 124 44.017 19.891 -36.065 1.00102.84 N ANISOU 936 NZ LYS A 124 11584 15341 12149 1596 3904 -946 N ATOM 937 N LYS A 125 39.488 21.933 -37.514 1.00101.28 N ANISOU 937 N LYS A 125 13074 14403 11005 1317 3536 -477 N ATOM 938 CA LYS A 125 39.727 21.744 -38.941 1.00109.90 C ANISOU 938 CA LYS A 125 14494 15472 11790 1514 3845 -458 C ATOM 939 C LYS A 125 39.212 22.927 -39.748 1.00109.16 C ANISOU 939 C LYS A 125 14800 15215 11461 1386 4032 -297 C ATOM 940 O LYS A 125 39.830 23.321 -40.743 1.00120.48 O ANISOU 940 O LYS A 125 16401 16664 12714 1398 4464 -232 O ATOM 941 CB LYS A 125 39.077 20.450 -39.430 1.00113.56 C ANISOU 941 CB LYS A 125 15261 15858 12029 1845 3568 -555 C ATOM 942 CG LYS A 125 39.510 20.052 -40.836 1.00107.50 C ANISOU 942 CG LYS A 125 14807 15098 10939 2097 3888 -581 C ATOM 943 CD LYS A 125 38.587 19.019 -41.467 1.00100.27 C ANISOU 943 CD LYS A 125 14327 14031 9741 2397 3564 -662 C ATOM 944 CE LYS A 125 39.086 18.637 -42.848 1.00104.34 C ANISOU 944 CE LYS A 125 15180 14558 9907 2661 3898 -705 C ATOM 945 NZ LYS A 125 39.382 19.851 -43.657 1.00107.07 N ANISOU 945 NZ LYS A 125 15751 14883 10049 2517 4343 -549 N ATOM 946 N THR A 126 38.076 23.502 -39.346 1.00 96.04 N ANISOU 946 N THR A 126 13313 13386 9792 1272 3720 -231 N ATOM 947 CA THR A 126 37.597 24.710 -40.013 1.00 97.10 C ANISOU 947 CA THR A 126 13820 13341 9734 1153 3855 -77 C ATOM 948 C THR A 126 38.617 25.835 -39.891 1.00 99.47 C ANISOU 948 C THR A 126 13891 13703 10199 859 4286 21 C ATOM 949 O THR A 126 38.967 26.493 -40.883 1.00102.80 O ANISOU 949 O THR A 126 14603 14053 10405 820 4666 143 O ATOM 950 CB THR A 126 36.255 25.136 -39.423 1.00 93.80 C ANISOU 950 CB THR A 126 13526 12749 9365 1083 3427 -58 C ATOM 951 OG1 THR A 126 35.399 23.995 -39.326 1.00 91.70 O ANISOU 951 OG1 THR A 126 13347 12449 9044 1305 3029 -174 O ATOM 952 CG2 THR A 126 35.589 26.171 -40.308 1.00 95.21 C ANISOU 952 CG2 THR A 126 14192 12701 9284 1069 3475 82 C ATOM 953 N ALA A 127 39.123 26.053 -38.676 1.00 98.15 N ANISOU 953 N ALA A 127 13219 13660 10414 644 4232 -33 N ATOM 954 CA ALA A 127 40.114 27.102 -38.471 1.00100.59 C ANISOU 954 CA ALA A 127 13256 14022 10942 337 4604 32 C ATOM 955 C ALA A 127 41.375 26.845 -39.285 1.00104.96 C ANISOU 955 C ALA A 127 13681 14729 11469 379 5111 20 C ATOM 956 O ALA A 127 41.980 27.783 -39.814 1.00108.32 O ANISOU 956 O ALA A 127 14154 15115 11888 170 5548 135 O ATOM 957 CB ALA A 127 40.452 27.219 -36.988 1.00 98.63 C ANISOU 957 CB ALA A 127 12483 13889 11102 139 4391 -64 C ATOM 958 N GLU A 128 41.792 25.581 -39.393 1.00118.22 N ANISOU 958 N GLU A 128 15200 16574 13144 645 5079 -122 N ATOM 959 CA GLU A 128 42.978 25.258 -40.180 1.00116.47 C ANISOU 959 CA GLU A 128 14834 16512 12906 724 5578 -165 C ATOM 960 C GLU A 128 42.740 25.528 -41.659 1.00113.11 C ANISOU 960 C GLU A 128 15008 15948 12020 831 5923 -34 C ATOM 961 O GLU A 128 43.595 26.103 -42.344 1.00117.08 O ANISOU 961 O GLU A 128 15506 16489 12491 696 6479 40 O ATOM 962 CB GLU A 128 43.380 23.799 -39.959 1.00114.89 C ANISOU 962 CB GLU A 128 14372 16492 12791 1033 5413 -362 C ATOM 963 CG GLU A 128 43.935 23.497 -38.578 1.00108.05 C ANISOU 963 CG GLU A 128 12893 15785 12377 947 5151 -497 C ATOM 964 CD GLU A 128 44.300 22.033 -38.401 1.00108.13 C ANISOU 964 CD GLU A 128 12707 15931 12446 1283 4960 -682 C ATOM 965 OE1 GLU A 128 43.726 21.182 -39.111 1.00107.67 O ANISOU 965 OE1 GLU A 128 13044 15795 12072 1578 4860 -706 O ATOM 966 OE2 GLU A 128 45.168 21.732 -37.552 1.00108.92 O ANISOU 966 OE2 GLU A 128 12271 16200 12913 1263 4887 -811 O ATOM 967 N ASP A 129 41.578 25.115 -42.168 1.00110.71 N ANISOU 967 N ASP A 129 15236 15475 11354 1069 5599 -9 N ATOM 968 CA ASP A 129 41.241 25.355 -43.566 1.00113.56 C ANISOU 968 CA ASP A 129 16246 15675 11226 1204 5840 110 C ATOM 969 C ASP A 129 41.282 26.840 -43.888 1.00115.66 C ANISOU 969 C ASP A 129 16743 15779 11425 898 6149 325 C ATOM 970 O ASP A 129 41.850 27.251 -44.905 1.00120.21 O ANISOU 970 O ASP A 129 17603 16323 11749 866 6668 434 O ATOM 971 CB ASP A 129 39.862 24.775 -43.883 1.00110.81 C ANISOU 971 CB ASP A 129 16387 15146 10570 1478 5322 85 C ATOM 972 CG ASP A 129 39.863 23.260 -43.945 1.00110.08 C ANISOU 972 CG ASP A 129 16230 15162 10433 1812 5106 -110 C ATOM 973 OD1 ASP A 129 40.883 22.644 -43.573 1.00111.13 O ANISOU 973 OD1 ASP A 129 15898 15514 10811 1843 5295 -233 O ATOM 974 OD2 ASP A 129 38.835 22.685 -44.362 1.00108.71 O ANISOU 974 OD2 ASP A 129 16466 14839 9998 2048 4726 -152 O ATOM 975 N TYR A 130 40.693 27.668 -43.025 1.00112.72 N ANISOU 975 N TYR A 130 16272 15288 11269 667 5855 388 N ATOM 976 CA TYR A 130 40.770 29.106 -43.260 1.00114.91 C ANISOU 976 CA TYR A 130 16759 15383 11517 365 6133 587 C ATOM 977 C TYR A 130 42.211 29.599 -43.183 1.00118.79 C ANISOU 977 C TYR A 130 16819 16028 12289 71 6716 609 C ATOM 978 O TYR A 130 42.667 30.358 -44.046 1.00123.18 O ANISOU 978 O TYR A 130 17670 16478 12656 -78 7217 771 O ATOM 979 CB TYR A 130 39.893 29.863 -42.264 1.00111.12 C ANISOU 979 CB TYR A 130 16214 14753 11254 191 5693 615 C ATOM 980 CG TYR A 130 39.907 31.365 -42.468 1.00113.38 C ANISOU 980 CG TYR A 130 16750 14808 11521 -107 5928 815 C ATOM 981 CD1 TYR A 130 38.925 31.994 -43.222 1.00113.98 C ANISOU 981 CD1 TYR A 130 17493 14584 11229 -13 5792 967 C ATOM 982 CD2 TYR A 130 40.906 32.154 -41.908 1.00115.26 C ANISOU 982 CD2 TYR A 130 16565 15108 12120 -479 6260 843 C ATOM 983 CE1 TYR A 130 38.938 33.365 -43.409 1.00116.33 C ANISOU 983 CE1 TYR A 130 18062 14636 11504 -273 5991 1157 C ATOM 984 CE2 TYR A 130 40.929 33.519 -42.093 1.00117.61 C ANISOU 984 CE2 TYR A 130 17112 15163 12412 -768 6476 1026 C ATOM 985 CZ TYR A 130 39.945 34.121 -42.841 1.00118.11 C ANISOU 985 CZ TYR A 130 17871 14916 12090 -661 6346 1190 C ATOM 986 OH TYR A 130 39.974 35.485 -43.017 1.00120.72 O ANISOU 986 OH TYR A 130 18485 14972 12412 -939 6546 1380 O ATOM 987 N LEU A 131 42.945 29.178 -42.149 1.00117.62 N ANISOU 987 N LEU A 131 15972 16118 12598 -23 6656 443 N ATOM 988 CA LEU A 131 44.275 29.733 -41.911 1.00121.30 C ANISOU 988 CA LEU A 131 15933 16725 13430 -339 7135 433 C ATOM 989 C LEU A 131 45.309 29.196 -42.892 1.00126.29 C ANISOU 989 C LEU A 131 16509 17526 13951 -226 7718 395 C ATOM 990 O LEU A 131 46.287 29.889 -43.195 1.00130.91 O ANISOU 990 O LEU A 131 16900 18147 14693 -507 8280 459 O ATOM 991 CB LEU A 131 44.721 29.444 -40.477 1.00118.82 C ANISOU 991 CB LEU A 131 14902 16606 13640 -446 6824 247 C ATOM 992 CG LEU A 131 43.987 30.160 -39.343 1.00114.92 C ANISOU 992 CG LEU A 131 14346 15975 13342 -646 6364 266 C ATOM 993 CD1 LEU A 131 44.827 30.142 -38.073 1.00114.62 C ANISOU 993 CD1 LEU A 131 13591 16131 13830 -838 6239 101 C ATOM 994 CD2 LEU A 131 43.636 31.580 -39.748 1.00116.45 C ANISOU 994 CD2 LEU A 131 14942 15890 13414 -922 6558 478 C ATOM 995 N GLY A 132 45.124 27.977 -43.390 1.00125.80 N ANISOU 995 N GLY A 132 16603 17561 13635 172 7613 282 N ATOM 996 CA GLY A 132 46.112 27.370 -44.257 1.00130.61 C ANISOU 996 CA GLY A 132 17127 18348 14149 322 8154 206 C ATOM 997 C GLY A 132 47.342 26.854 -43.549 1.00132.17 C ANISOU 997 C GLY A 132 16495 18851 14875 280 8297 -9 C ATOM 998 O GLY A 132 48.315 26.484 -44.215 1.00136.95 O ANISOU 998 O GLY A 132 16921 19624 15491 361 8825 -89 O ATOM 999 N GLU A 133 47.330 26.818 -42.226 1.00135.17 N ANISOU 999 N GLU A 133 16371 19303 15685 171 7840 -114 N ATOM 1000 CA GLU A 133 48.425 26.313 -41.416 1.00135.20 C ANISOU 1000 CA GLU A 133 15584 19577 16209 157 7841 -334 C ATOM 1001 C GLU A 133 47.832 25.538 -40.258 1.00132.71 C ANISOU 1001 C GLU A 133 15094 19291 16040 335 7117 -462 C ATOM 1002 O GLU A 133 46.664 25.744 -39.894 1.00137.68 O ANISOU 1002 O GLU A 133 16097 19732 16484 326 6678 -365 O ATOM 1003 CB GLU A 133 49.314 27.457 -40.905 1.00137.10 C ANISOU 1003 CB GLU A 133 15320 19858 16912 -307 8141 -308 C ATOM 1004 CG GLU A 133 48.779 28.175 -39.678 1.00136.84 C ANISOU 1004 CG GLU A 133 15163 19708 17121 -566 7640 -274 C ATOM 1005 CD GLU A 133 49.490 29.488 -39.418 1.00146.27 C ANISOU 1005 CD GLU A 133 16046 20858 18673 -1053 7973 -207 C ATOM 1006 OE1 GLU A 133 49.220 30.462 -40.152 1.00151.33 O ANISOU 1006 OE1 GLU A 133 17138 21285 19076 -1273 8321 10 O ATOM 1007 OE2 GLU A 133 50.327 29.545 -38.493 1.00149.22 O ANISOU 1007 OE2 GLU A 133 15739 21393 19564 -1215 7874 -375 O ATOM 1008 N PRO A 134 48.591 24.620 -39.657 1.00125.27 N ANISOU 1008 N PRO A 134 13601 18571 15426 511 6973 -684 N ATOM 1009 CA PRO A 134 48.054 23.829 -38.547 1.00120.68 C ANISOU 1009 CA PRO A 134 12904 17997 14952 684 6297 -792 C ATOM 1010 C PRO A 134 47.701 24.690 -37.342 1.00117.67 C ANISOU 1010 C PRO A 134 12359 17535 14816 360 5940 -739 C ATOM 1011 O PRO A 134 48.312 25.731 -37.089 1.00119.89 O ANISOU 1011 O PRO A 134 12341 17835 15379 11 6179 -707 O ATOM 1012 CB PRO A 134 49.191 22.856 -38.217 1.00123.44 C ANISOU 1012 CB PRO A 134 12658 18597 15646 904 6305 -1035 C ATOM 1013 CG PRO A 134 50.009 22.790 -39.459 1.00128.84 C ANISOU 1013 CG PRO A 134 13320 19390 16243 990 6972 -1065 C ATOM 1014 CD PRO A 134 49.933 24.159 -40.059 1.00130.61 C ANISOU 1014 CD PRO A 134 13786 19489 16350 610 7430 -852 C ATOM 1015 N VAL A 135 46.699 24.238 -36.592 1.00112.85 N ANISOU 1015 N VAL A 135 11956 16826 14098 474 5375 -739 N ATOM 1016 CA VAL A 135 46.263 24.896 -35.367 1.00109.80 C ANISOU 1016 CA VAL A 135 11457 16363 13899 223 4992 -714 C ATOM 1017 C VAL A 135 46.463 23.927 -34.214 1.00108.18 C ANISOU 1017 C VAL A 135 10920 16274 13911 393 4515 -883 C ATOM 1018 O VAL A 135 46.024 22.773 -34.282 1.00106.50 O ANISOU 1018 O VAL A 135 10897 16053 13517 712 4266 -933 O ATOM 1019 CB VAL A 135 44.794 25.348 -35.451 1.00105.85 C ANISOU 1019 CB VAL A 135 11533 15618 13067 177 4768 -553 C ATOM 1020 CG1 VAL A 135 44.301 25.783 -34.091 1.00102.64 C ANISOU 1020 CG1 VAL A 135 11006 15152 12840 -10 4339 -569 C ATOM 1021 CG2 VAL A 135 44.647 26.483 -36.450 1.00107.83 C ANISOU 1021 CG2 VAL A 135 12117 15722 13131 -21 5192 -376 C ATOM 1022 N THR A 136 47.128 24.390 -33.159 1.00109.01 N ANISOU 1022 N THR A 136 10557 16465 14395 182 4370 -971 N ATOM 1023 CA THR A 136 47.380 23.554 -31.999 1.00108.01 C ANISOU 1023 CA THR A 136 10143 16433 14465 334 3894 -1124 C ATOM 1024 C THR A 136 46.905 24.153 -30.685 1.00105.32 C ANISOU 1024 C THR A 136 9788 16009 14221 107 3489 -1112 C ATOM 1025 O THR A 136 46.968 23.464 -29.661 1.00104.32 O ANISOU 1025 O THR A 136 9527 15925 14184 234 3057 -1216 O ATOM 1026 CB THR A 136 48.878 23.238 -31.873 1.00112.68 C ANISOU 1026 CB THR A 136 10097 17253 15463 398 4023 -1317 C ATOM 1027 OG1 THR A 136 49.089 22.377 -30.746 1.00111.92 O ANISOU 1027 OG1 THR A 136 9783 17221 15521 587 3502 -1461 O ATOM 1028 CG2 THR A 136 49.674 24.517 -31.677 1.00115.73 C ANISOU 1028 CG2 THR A 136 10081 17689 16202 3 4284 -1332 C ATOM 1029 N GLU A 137 46.430 25.397 -30.674 1.00104.40 N ANISOU 1029 N GLU A 137 9838 15759 14070 -209 3610 -992 N ATOM 1030 CA GLU A 137 46.090 26.081 -29.435 1.00102.53 C ANISOU 1030 CA GLU A 137 9564 15448 13946 -439 3274 -1006 C ATOM 1031 C GLU A 137 44.745 26.784 -29.555 1.00 99.13 C ANISOU 1031 C GLU A 137 9640 14796 13230 -560 3247 -847 C ATOM 1032 O GLU A 137 44.465 27.458 -30.553 1.00101.15 O ANISOU 1032 O GLU A 137 10142 14945 13346 -654 3590 -717 O ATOM 1033 CB GLU A 137 47.182 27.079 -29.058 1.00106.13 C ANISOU 1033 CB GLU A 137 9545 15976 14802 -752 3421 -1089 C ATOM 1034 CG GLU A 137 48.496 26.408 -28.692 1.00109.69 C ANISOU 1034 CG GLU A 137 9418 16651 15608 -630 3341 -1291 C ATOM 1035 CD GLU A 137 49.622 27.393 -28.465 1.00113.96 C ANISOU 1035 CD GLU A 137 9439 17266 16594 -956 3523 -1391 C ATOM 1036 OE1 GLU A 137 49.466 28.578 -28.830 1.00114.56 O ANISOU 1036 OE1 GLU A 137 9631 17213 16683 -1279 3819 -1279 O ATOM 1037 OE2 GLU A 137 50.667 26.977 -27.920 1.00117.01 O ANISOU 1037 OE2 GLU A 137 9300 17824 17333 -886 3354 -1589 O ATOM 1038 N ALA A 138 43.924 26.638 -28.516 1.00100.31 N ANISOU 1038 N ALA A 138 9948 14870 13294 -553 2839 -862 N ATOM 1039 CA ALA A 138 42.572 27.169 -28.535 1.00 92.78 C ANISOU 1039 CA ALA A 138 9437 13718 12097 -623 2770 -745 C ATOM 1040 C ALA A 138 42.157 27.601 -27.137 1.00 91.07 C ANISOU 1040 C ALA A 138 9205 13447 11949 -778 2431 -803 C ATOM 1041 O ALA A 138 42.671 27.104 -26.131 1.00 91.52 O ANISOU 1041 O ALA A 138 9025 13610 12138 -742 2156 -921 O ATOM 1042 CB ALA A 138 41.579 26.137 -29.080 1.00 90.28 C ANISOU 1042 CB ALA A 138 9486 13342 11474 -339 2669 -689 C ATOM 1043 N VAL A 139 41.233 28.554 -27.095 1.00 90.71 N ANISOU 1043 N VAL A 139 9435 13227 11804 -936 2450 -726 N ATOM 1044 CA VAL A 139 40.487 28.908 -25.898 1.00 87.45 C ANISOU 1044 CA VAL A 139 9131 12730 11365 -1036 2158 -771 C ATOM 1045 C VAL A 139 39.080 28.360 -26.069 1.00 89.40 C ANISOU 1045 C VAL A 139 9753 12871 11343 -867 2044 -707 C ATOM 1046 O VAL A 139 38.455 28.569 -27.115 1.00 96.64 O ANISOU 1046 O VAL A 139 10918 13681 12120 -808 2215 -607 O ATOM 1047 CB VAL A 139 40.458 30.430 -25.688 1.00 88.33 C ANISOU 1047 CB VAL A 139 9257 12706 11596 -1333 2261 -761 C ATOM 1048 CG1 VAL A 139 39.531 30.783 -24.544 1.00 86.22 C ANISOU 1048 CG1 VAL A 139 9162 12340 11257 -1399 1992 -816 C ATOM 1049 CG2 VAL A 139 41.853 30.954 -25.433 1.00 91.80 C ANISOU 1049 CG2 VAL A 139 9288 13242 12349 -1534 2348 -846 C ATOM 1050 N ILE A 140 38.582 27.654 -25.059 1.00 82.55 N ANISOU 1050 N ILE A 140 8937 12023 10405 -791 1753 -766 N ATOM 1051 CA ILE A 140 37.282 26.999 -25.138 1.00 79.98 C ANISOU 1051 CA ILE A 140 8911 11606 9871 -647 1643 -725 C ATOM 1052 C ILE A 140 36.361 27.587 -24.077 1.00 78.54 C ANISOU 1052 C ILE A 140 8858 11325 9658 -784 1498 -764 C ATOM 1053 O ILE A 140 36.791 27.894 -22.962 1.00 79.25 O ANISOU 1053 O ILE A 140 8827 11458 9826 -909 1365 -845 O ATOM 1054 CB ILE A 140 37.413 25.471 -24.971 1.00 79.60 C ANISOU 1054 CB ILE A 140 8855 11644 9747 -424 1470 -749 C ATOM 1055 CG1 ILE A 140 38.492 24.931 -25.908 1.00 81.60 C ANISOU 1055 CG1 ILE A 140 8932 12013 10061 -277 1621 -747 C ATOM 1056 CG2 ILE A 140 36.096 24.778 -25.263 1.00 77.42 C ANISOU 1056 CG2 ILE A 140 8873 11256 9289 -296 1395 -704 C ATOM 1057 CD1 ILE A 140 38.687 23.434 -25.818 1.00 81.62 C ANISOU 1057 CD1 ILE A 140 8936 12076 10000 -29 1445 -781 C ATOM 1058 N THR A 141 35.085 27.745 -24.427 1.00 76.84 N ANISOU 1058 N THR A 141 8890 10977 9330 -749 1517 -723 N ATOM 1059 CA THR A 141 34.115 28.366 -23.532 1.00 75.79 C ANISOU 1059 CA THR A 141 8872 10745 9179 -863 1432 -774 C ATOM 1060 C THR A 141 33.359 27.319 -22.716 1.00 74.47 C ANISOU 1060 C THR A 141 8801 10592 8904 -786 1261 -808 C ATOM 1061 O THR A 141 33.033 26.239 -23.215 1.00 73.77 O ANISOU 1061 O THR A 141 8784 10508 8736 -628 1221 -769 O ATOM 1062 CB THR A 141 33.117 29.224 -24.314 1.00 75.21 C ANISOU 1062 CB THR A 141 8983 10507 9087 -866 1541 -733 C ATOM 1063 OG1 THR A 141 32.215 28.377 -25.032 1.00 74.02 O ANISOU 1063 OG1 THR A 141 8982 10312 8829 -683 1502 -695 O ATOM 1064 CG2 THR A 141 33.839 30.123 -25.297 1.00 76.84 C ANISOU 1064 CG2 THR A 141 9171 10669 9357 -928 1739 -661 C ATOM 1065 N VAL A 142 33.089 27.651 -21.456 1.00 74.48 N ANISOU 1065 N VAL A 142 8825 10582 8891 -908 1170 -884 N ATOM 1066 CA VAL A 142 32.239 26.848 -20.575 1.00 73.66 C ANISOU 1066 CA VAL A 142 8856 10462 8667 -885 1065 -911 C ATOM 1067 C VAL A 142 31.268 27.778 -19.864 1.00 73.42 C ANISOU 1067 C VAL A 142 8922 10340 8635 -1011 1114 -987 C ATOM 1068 O VAL A 142 31.529 28.977 -19.719 1.00 74.14 O ANISOU 1068 O VAL A 142 8970 10394 8805 -1125 1163 -1036 O ATOM 1069 CB VAL A 142 33.056 26.060 -19.532 1.00 74.66 C ANISOU 1069 CB VAL A 142 8956 10689 8723 -877 889 -935 C ATOM 1070 CG1 VAL A 142 34.050 25.139 -20.201 1.00 75.26 C ANISOU 1070 CG1 VAL A 142 8912 10855 8830 -722 830 -886 C ATOM 1071 CG2 VAL A 142 33.734 27.016 -18.574 1.00 76.08 C ANISOU 1071 CG2 VAL A 142 9062 10901 8944 -1030 825 -1025 C ATOM 1072 N PRO A 143 30.134 27.243 -19.403 1.00 72.74 N ANISOU 1072 N PRO A 143 8961 10205 8472 -999 1116 -1007 N ATOM 1073 CA PRO A 143 29.223 28.067 -18.604 1.00 75.98 C ANISOU 1073 CA PRO A 143 9444 10543 8882 -1107 1188 -1106 C ATOM 1074 C PRO A 143 29.900 28.532 -17.328 1.00 78.67 C ANISOU 1074 C PRO A 143 9815 10932 9146 -1230 1122 -1182 C ATOM 1075 O PRO A 143 30.799 27.874 -16.801 1.00 82.44 O ANISOU 1075 O PRO A 143 10292 11496 9536 -1222 986 -1160 O ATOM 1076 CB PRO A 143 28.056 27.122 -18.303 1.00 72.97 C ANISOU 1076 CB PRO A 143 9158 10128 8440 -1079 1221 -1108 C ATOM 1077 CG PRO A 143 28.100 26.127 -19.389 1.00 71.69 C ANISOU 1077 CG PRO A 143 8971 9967 8301 -943 1170 -1014 C ATOM 1078 CD PRO A 143 29.551 25.923 -19.692 1.00 72.03 C ANISOU 1078 CD PRO A 143 8942 10103 8322 -891 1081 -953 C ATOM 1079 N ALA A 144 29.457 29.688 -16.834 1.00 74.86 N ANISOU 1079 N ALA A 144 9371 10377 8696 -1327 1194 -1287 N ATOM 1080 CA ALA A 144 30.067 30.261 -15.640 1.00 76.42 C ANISOU 1080 CA ALA A 144 9624 10599 8814 -1444 1114 -1387 C ATOM 1081 C ALA A 144 29.894 29.350 -14.433 1.00 77.17 C ANISOU 1081 C ALA A 144 9892 10746 8684 -1455 1052 -1404 C ATOM 1082 O ALA A 144 30.774 29.282 -13.569 1.00 78.62 O ANISOU 1082 O ALA A 144 10133 10984 8754 -1496 888 -1441 O ATOM 1083 CB ALA A 144 29.472 31.638 -15.357 1.00 77.07 C ANISOU 1083 CB ALA A 144 9752 10567 8964 -1525 1213 -1512 C ATOM 1084 N TYR A 145 28.769 28.640 -14.358 1.00 76.58 N ANISOU 1084 N TYR A 145 9913 10641 8542 -1423 1175 -1378 N ATOM 1085 CA TYR A 145 28.429 27.843 -13.190 1.00 77.70 C ANISOU 1085 CA TYR A 145 10275 10798 8452 -1461 1182 -1382 C ATOM 1086 C TYR A 145 28.945 26.409 -13.278 1.00 77.59 C ANISOU 1086 C TYR A 145 10316 10828 8336 -1382 1043 -1249 C ATOM 1087 O TYR A 145 28.499 25.553 -12.506 1.00 78.51 O ANISOU 1087 O TYR A 145 10646 10921 8262 -1409 1075 -1213 O ATOM 1088 CB TYR A 145 26.912 27.856 -12.983 1.00 80.46 C ANISOU 1088 CB TYR A 145 10684 11079 8809 -1501 1428 -1438 C ATOM 1089 CG TYR A 145 26.487 27.840 -11.534 1.00 84.44 C ANISOU 1089 CG TYR A 145 11438 11575 9070 -1600 1533 -1518 C ATOM 1090 CD1 TYR A 145 26.836 28.878 -10.681 1.00 81.28 C ANISOU 1090 CD1 TYR A 145 11141 11172 8570 -1661 1508 -1651 C ATOM 1091 CD2 TYR A 145 25.729 26.797 -11.022 1.00 93.15 C ANISOU 1091 CD2 TYR A 145 12700 12658 10033 -1642 1673 -1463 C ATOM 1092 CE1 TYR A 145 26.453 28.875 -9.355 1.00 84.72 C ANISOU 1092 CE1 TYR A 145 11853 11597 8739 -1738 1616 -1733 C ATOM 1093 CE2 TYR A 145 25.337 26.785 -9.694 1.00 96.40 C ANISOU 1093 CE2 TYR A 145 13386 13057 10185 -1740 1814 -1526 C ATOM 1094 CZ TYR A 145 25.703 27.828 -8.865 1.00 91.64 C ANISOU 1094 CZ TYR A 145 12903 12463 9453 -1776 1785 -1664 C ATOM 1095 OH TYR A 145 25.320 27.824 -7.543 1.00 95.98 O ANISOU 1095 OH TYR A 145 13772 12997 9701 -1860 1936 -1736 O ATOM 1096 N PHE A 146 29.872 26.130 -14.193 1.00 76.80 N ANISOU 1096 N PHE A 146 10047 10779 8356 -1284 907 -1177 N ATOM 1097 CA PHE A 146 30.447 24.795 -14.309 1.00 76.96 C ANISOU 1097 CA PHE A 146 10113 10831 8297 -1175 753 -1070 C ATOM 1098 C PHE A 146 31.205 24.424 -13.039 1.00 79.04 C ANISOU 1098 C PHE A 146 10566 11125 8341 -1186 551 -1084 C ATOM 1099 O PHE A 146 31.985 25.224 -12.513 1.00 80.24 O ANISOU 1099 O PHE A 146 10674 11323 8489 -1231 427 -1173 O ATOM 1100 CB PHE A 146 31.392 24.726 -15.509 1.00 76.21 C ANISOU 1100 CB PHE A 146 9778 10797 8381 -1058 671 -1024 C ATOM 1101 CG PHE A 146 30.861 23.929 -16.670 1.00 74.79 C ANISOU 1101 CG PHE A 146 9559 10578 8278 -946 743 -939 C ATOM 1102 CD1 PHE A 146 29.511 23.672 -16.794 1.00 74.01 C ANISOU 1102 CD1 PHE A 146 9554 10389 8178 -981 884 -932 C ATOM 1103 CD2 PHE A 146 31.720 23.427 -17.636 1.00 74.59 C ANISOU 1103 CD2 PHE A 146 9397 10607 8339 -803 666 -886 C ATOM 1104 CE1 PHE A 146 29.027 22.938 -17.863 1.00 73.02 C ANISOU 1104 CE1 PHE A 146 9398 10213 8131 -879 906 -875 C ATOM 1105 CE2 PHE A 146 31.240 22.695 -18.700 1.00 73.56 C ANISOU 1105 CE2 PHE A 146 9270 10429 8252 -688 712 -825 C ATOM 1106 CZ PHE A 146 29.894 22.450 -18.815 1.00 72.75 C ANISOU 1106 CZ PHE A 146 9275 10224 8144 -728 811 -821 C ATOM 1107 N ASN A 147 30.982 23.208 -12.546 1.00 79.80 N ANISOU 1107 N ASN A 147 10893 11176 8251 -1145 495 -997 N ATOM 1108 CA ASN A 147 31.753 22.739 -11.405 1.00 82.13 C ANISOU 1108 CA ASN A 147 11418 11478 8309 -1115 252 -992 C ATOM 1109 C ASN A 147 33.157 22.346 -11.859 1.00 82.64 C ANISOU 1109 C ASN A 147 11291 11622 8486 -953 -35 -978 C ATOM 1110 O ASN A 147 33.498 22.415 -13.040 1.00 84.50 O ANISOU 1110 O ASN A 147 11236 11909 8961 -878 3 -965 O ATOM 1111 CB ASN A 147 31.046 21.577 -10.708 1.00 83.24 C ANISOU 1111 CB ASN A 147 11922 11511 8195 -1132 298 -887 C ATOM 1112 CG ASN A 147 30.931 20.345 -11.582 1.00 86.23 C ANISOU 1112 CG ASN A 147 12270 11835 8660 -1018 276 -764 C ATOM 1113 OD1 ASN A 147 31.933 19.739 -11.961 1.00 87.09 O ANISOU 1113 OD1 ASN A 147 12300 11973 8816 -851 34 -726 O ATOM 1114 ND2 ASN A 147 29.702 19.952 -11.885 1.00 95.82 N ANISOU 1114 ND2 ASN A 147 13540 12959 9908 -1104 524 -717 N ATOM 1115 N ASP A 148 33.984 21.920 -10.903 1.00 85.07 N ANISOU 1115 N ASP A 148 11772 11936 8613 -885 -328 -988 N ATOM 1116 CA ASP A 148 35.368 21.575 -11.213 1.00 86.21 C ANISOU 1116 CA ASP A 148 11697 12163 8895 -715 -629 -1010 C ATOM 1117 C ASP A 148 35.440 20.415 -12.197 1.00 86.14 C ANISOU 1117 C ASP A 148 11611 12135 8985 -543 -627 -902 C ATOM 1118 O ASP A 148 36.153 20.484 -13.204 1.00 94.18 O ANISOU 1118 O ASP A 148 12289 13242 10254 -442 -637 -928 O ATOM 1119 CB ASP A 148 36.115 21.234 -9.923 1.00 91.54 C ANISOU 1119 CB ASP A 148 12625 12822 9334 -647 -991 -1046 C ATOM 1120 CG ASP A 148 37.548 20.800 -10.168 1.00 97.12 C ANISOU 1120 CG ASP A 148 13078 13612 10211 -444 -1341 -1092 C ATOM 1121 OD1 ASP A 148 38.460 21.624 -9.947 1.00 92.68 O ANISOU 1121 OD1 ASP A 148 12270 13143 9799 -469 -1521 -1234 O ATOM 1122 OD2 ASP A 148 37.766 19.634 -10.566 1.00108.20 O ANISOU 1122 OD2 ASP A 148 14516 14979 11617 -257 -1442 -1002 O ATOM 1123 N ALA A 149 34.703 19.337 -11.919 1.00 85.35 N ANISOU 1123 N ALA A 149 11839 11906 8684 -517 -598 -786 N ATOM 1124 CA ALA A 149 34.790 18.142 -12.753 1.00 84.89 C ANISOU 1124 CA ALA A 149 11762 11795 8696 -343 -641 -694 C ATOM 1125 C ALA A 149 34.364 18.426 -14.186 1.00 82.26 C ANISOU 1125 C ALA A 149 11143 11502 8611 -346 -390 -697 C ATOM 1126 O ALA A 149 34.931 17.867 -15.131 1.00 82.04 O ANISOU 1126 O ALA A 149 10942 11504 8726 -169 -448 -686 O ATOM 1127 CB ALA A 149 33.940 17.024 -12.157 1.00 85.71 C ANISOU 1127 CB ALA A 149 12301 11716 8548 -369 -622 -567 C ATOM 1128 N GLN A 150 33.364 19.290 -14.367 1.00 80.58 N ANISOU 1128 N GLN A 150 10896 11280 8439 -528 -118 -720 N ATOM 1129 CA GLN A 150 32.928 19.651 -15.711 1.00 78.42 C ANISOU 1129 CA GLN A 150 10393 11029 8376 -520 86 -725 C ATOM 1130 C GLN A 150 34.020 20.410 -16.454 1.00 78.38 C ANISOU 1130 C GLN A 150 10053 11158 8570 -453 62 -791 C ATOM 1131 O GLN A 150 34.316 20.114 -17.616 1.00 77.75 O ANISOU 1131 O GLN A 150 9815 11107 8620 -324 109 -772 O ATOM 1132 CB GLN A 150 31.651 20.486 -15.643 1.00 78.31 C ANISOU 1132 CB GLN A 150 10412 10966 8374 -708 340 -755 C ATOM 1133 CG GLN A 150 30.435 19.763 -15.092 1.00 88.18 C ANISOU 1133 CG GLN A 150 11929 12085 9489 -803 447 -701 C ATOM 1134 CD GLN A 150 29.252 20.695 -14.904 1.00 94.89 C ANISOU 1134 CD GLN A 150 12759 12911 10386 -976 698 -768 C ATOM 1135 OE1 GLN A 150 29.346 21.699 -14.199 1.00104.54 O ANISOU 1135 OE1 GLN A 150 13981 14179 11559 -1072 740 -847 O ATOM 1136 NE2 GLN A 150 28.133 20.371 -15.543 1.00 88.92 N ANISOU 1136 NE2 GLN A 150 11975 12072 9739 -1006 848 -756 N ATOM 1137 N ARG A 151 34.627 21.400 -15.797 1.00 79.38 N ANISOU 1137 N ARG A 151 10078 11360 8721 -550 3 -874 N ATOM 1138 CA ARG A 151 35.675 22.182 -16.444 1.00 79.83 C ANISOU 1138 CA ARG A 151 9799 11533 8999 -534 9 -939 C ATOM 1139 C ARG A 151 36.863 21.304 -16.814 1.00 81.33 C ANISOU 1139 C ARG A 151 9825 11802 9276 -324 -172 -941 C ATOM 1140 O ARG A 151 37.378 21.375 -17.937 1.00 85.72 O ANISOU 1140 O ARG A 151 10137 12426 10007 -242 -56 -944 O ATOM 1141 CB ARG A 151 36.110 23.328 -15.531 1.00 81.12 C ANISOU 1141 CB ARG A 151 9904 11737 9181 -694 -65 -1045 C ATOM 1142 CG ARG A 151 34.954 24.180 -15.037 1.00 80.08 C ANISOU 1142 CG ARG A 151 9955 11521 8951 -876 105 -1068 C ATOM 1143 CD ARG A 151 35.384 25.167 -13.972 1.00 81.78 C ANISOU 1143 CD ARG A 151 10185 11753 9136 -1013 -12 -1189 C ATOM 1144 NE ARG A 151 35.741 26.459 -14.546 1.00 81.70 N ANISOU 1144 NE ARG A 151 9926 11762 9354 -1129 104 -1257 N ATOM 1145 CZ ARG A 151 34.882 27.456 -14.721 1.00 81.75 C ANISOU 1145 CZ ARG A 151 9982 11689 9392 -1254 313 -1282 C ATOM 1146 NH1 ARG A 151 33.615 27.308 -14.363 1.00 79.54 N ANISOU 1146 NH1 ARG A 151 9941 11329 8952 -1275 439 -1265 N ATOM 1147 NH2 ARG A 151 35.289 28.600 -15.252 1.00 96.03 N ANISOU 1147 NH2 ARG A 151 11598 13486 11404 -1360 402 -1329 N ATOM 1148 N GLN A 152 37.307 20.458 -15.882 1.00 83.80 N ANISOU 1148 N GLN A 152 10286 12097 9456 -219 -454 -943 N ATOM 1149 CA GLN A 152 38.416 19.561 -16.187 1.00 84.93 C ANISOU 1149 CA GLN A 152 10272 12302 9697 20 -658 -962 C ATOM 1150 C GLN A 152 38.048 18.604 -17.308 1.00 83.70 C ANISOU 1150 C GLN A 152 10154 12094 9555 182 -533 -884 C ATOM 1151 O GLN A 152 38.881 18.289 -18.165 1.00 97.74 O ANISOU 1151 O GLN A 152 11682 13955 11498 355 -526 -921 O ATOM 1152 CB GLN A 152 38.831 18.780 -14.943 1.00 87.32 C ANISOU 1152 CB GLN A 152 10805 12552 9820 126 -1022 -968 C ATOM 1153 CG GLN A 152 40.065 17.917 -15.145 1.00 89.77 C ANISOU 1153 CG GLN A 152 10926 12922 10260 404 -1291 -1019 C ATOM 1154 CD GLN A 152 41.281 18.736 -15.522 1.00 91.35 C ANISOU 1154 CD GLN A 152 10629 13303 10778 407 -1308 -1162 C ATOM 1155 OE1 GLN A 152 41.723 19.599 -14.764 1.00 92.74 O ANISOU 1155 OE1 GLN A 152 10700 13534 11004 274 -1440 -1258 O ATOM 1156 NE2 GLN A 152 41.824 18.476 -16.703 1.00 91.95 N ANISOU 1156 NE2 GLN A 152 10399 13464 11072 549 -1158 -1185 N ATOM 1157 N ALA A 153 36.798 18.143 -17.326 1.00 82.01 N ANISOU 1157 N ALA A 153 10241 11740 9178 124 -426 -792 N ATOM 1158 CA ALA A 153 36.365 17.245 -18.388 1.00 81.01 C ANISOU 1158 CA ALA A 153 10175 11540 9064 264 -335 -734 C ATOM 1159 C ALA A 153 36.393 17.942 -19.741 1.00 79.74 C ANISOU 1159 C ALA A 153 9770 11460 9069 264 -83 -760 C ATOM 1160 O ALA A 153 36.784 17.340 -20.748 1.00 80.06 O ANISOU 1160 O ALA A 153 9729 11518 9174 454 -50 -765 O ATOM 1161 CB ALA A 153 34.969 16.710 -18.084 1.00 79.82 C ANISOU 1161 CB ALA A 153 10363 11215 8748 157 -271 -648 C ATOM 1162 N THR A 154 35.986 19.212 -19.786 1.00 78.60 N ANISOU 1162 N THR A 154 9542 11349 8976 62 99 -778 N ATOM 1163 CA THR A 154 36.053 19.962 -21.035 1.00 77.84 C ANISOU 1163 CA THR A 154 9264 11305 9008 55 334 -786 C ATOM 1164 C THR A 154 37.496 20.153 -21.475 1.00 79.78 C ANISOU 1164 C THR A 154 9195 11699 9419 152 345 -846 C ATOM 1165 O THR A 154 37.816 20.015 -22.661 1.00 80.04 O ANISOU 1165 O THR A 154 9128 11770 9515 274 503 -841 O ATOM 1166 CB THR A 154 35.354 21.314 -20.878 1.00 76.66 C ANISOU 1166 CB THR A 154 9116 11130 8880 -175 493 -794 C ATOM 1167 OG1 THR A 154 33.970 21.103 -20.584 1.00 75.19 O ANISOU 1167 OG1 THR A 154 9172 10816 8580 -248 517 -759 O ATOM 1168 CG2 THR A 154 35.458 22.121 -22.151 1.00 76.30 C ANISOU 1168 CG2 THR A 154 8941 11109 8942 -182 723 -783 C ATOM 1169 N LYS A 155 38.384 20.466 -20.530 1.00 81.53 N ANISOU 1169 N LYS A 155 9256 12004 9718 102 181 -915 N ATOM 1170 CA LYS A 155 39.800 20.581 -20.860 1.00 83.96 C ANISOU 1170 CA LYS A 155 9203 12460 10238 191 173 -998 C ATOM 1171 C LYS A 155 40.328 19.275 -21.442 1.00 85.13 C ANISOU 1171 C LYS A 155 9319 12631 10395 488 97 -1008 C ATOM 1172 O LYS A 155 41.117 19.279 -22.397 1.00 86.51 O ANISOU 1172 O LYS A 155 9239 12909 10724 598 263 -1051 O ATOM 1173 CB LYS A 155 40.583 20.985 -19.610 1.00 85.98 C ANISOU 1173 CB LYS A 155 9315 12780 10574 107 -81 -1093 C ATOM 1174 CG LYS A 155 41.961 21.569 -19.858 1.00 88.73 C ANISOU 1174 CG LYS A 155 9211 13282 11220 90 -53 -1207 C ATOM 1175 CD LYS A 155 42.472 22.259 -18.599 1.00 90.48 C ANISOU 1175 CD LYS A 155 9332 13533 11514 -61 -309 -1312 C ATOM 1176 CE LYS A 155 43.930 22.658 -18.722 1.00 93.93 C ANISOU 1176 CE LYS A 155 9270 14123 12297 -65 -352 -1455 C ATOM 1177 NZ LYS A 155 44.812 21.463 -18.811 1.00 96.26 N ANISOU 1177 NZ LYS A 155 9385 14501 12687 245 -559 -1521 N ATOM 1178 N ASP A 156 39.874 18.144 -20.897 1.00 84.84 N ANISOU 1178 N ASP A 156 9562 12484 10189 620 -131 -967 N ATOM 1179 CA ASP A 156 40.294 16.851 -21.422 1.00 86.05 C ANISOU 1179 CA ASP A 156 9736 12619 10341 918 -229 -980 C ATOM 1180 C ASP A 156 39.742 16.618 -22.821 1.00 84.70 C ANISOU 1180 C ASP A 156 9647 12405 10130 996 33 -939 C ATOM 1181 O ASP A 156 40.437 16.071 -23.683 1.00 86.21 O ANISOU 1181 O ASP A 156 9700 12657 10400 1221 99 -992 O ATOM 1182 CB ASP A 156 39.858 15.732 -20.478 1.00 87.95 C ANISOU 1182 CB ASP A 156 10319 12704 10393 1011 -534 -928 C ATOM 1183 CG ASP A 156 40.589 15.774 -19.150 1.00101.06 C ANISOU 1183 CG ASP A 156 11939 14399 12059 1013 -852 -980 C ATOM 1184 OD1 ASP A 156 41.723 16.295 -19.108 1.00104.30 O ANISOU 1184 OD1 ASP A 156 11978 14968 12684 1047 -905 -1094 O ATOM 1185 OD2 ASP A 156 40.029 15.285 -18.146 1.00107.50 O ANISOU 1185 OD2 ASP A 156 13104 15075 12664 975 -1051 -912 O ATOM 1186 N ALA A 157 38.493 17.020 -23.066 1.00 99.45 N ANISOU 1186 N ALA A 157 11743 14168 11877 830 172 -859 N ATOM 1187 CA ALA A 157 37.953 16.948 -24.420 1.00 92.48 C ANISOU 1187 CA ALA A 157 10949 13240 10949 898 390 -831 C ATOM 1188 C ALA A 157 38.787 17.779 -25.384 1.00 86.82 C ANISOU 1188 C ALA A 157 9960 12667 10359 904 662 -870 C ATOM 1189 O ALA A 157 38.982 17.395 -26.542 1.00 87.36 O ANISOU 1189 O ALA A 157 10045 12748 10401 1079 814 -884 O ATOM 1190 CB ALA A 157 36.500 17.416 -24.437 1.00 89.09 C ANISOU 1190 CB ALA A 157 10755 12681 10413 708 462 -762 C ATOM 1191 N GLY A 158 39.288 18.924 -24.922 1.00 82.84 N ANISOU 1191 N GLY A 158 9226 12262 9986 706 740 -890 N ATOM 1192 CA GLY A 158 40.163 19.723 -25.761 1.00 84.51 C ANISOU 1192 CA GLY A 158 9166 12599 10345 672 1023 -920 C ATOM 1193 C GLY A 158 41.489 19.041 -26.028 1.00 87.52 C ANISOU 1193 C GLY A 158 9255 13119 10878 894 1022 -1020 C ATOM 1194 O GLY A 158 42.056 19.170 -27.117 1.00 89.14 O ANISOU 1194 O GLY A 158 9326 13404 11139 974 1309 -1040 O ATOM 1195 N ARG A 159 42.004 18.302 -25.042 1.00 95.17 N ANISOU 1195 N ARG A 159 10134 14115 11912 1010 703 -1088 N ATOM 1196 CA ARG A 159 43.259 17.588 -25.253 1.00 96.75 C ANISOU 1196 CA ARG A 159 10033 14441 12288 1263 658 -1208 C ATOM 1197 C ARG A 159 43.078 16.421 -26.215 1.00 92.08 C ANISOU 1197 C ARG A 159 9633 13789 11566 1563 710 -1210 C ATOM 1198 O ARG A 159 43.954 16.153 -27.045 1.00 94.63 O ANISOU 1198 O ARG A 159 9726 14224 12005 1752 901 -1298 O ATOM 1199 CB ARG A 159 43.822 17.104 -23.919 1.00102.18 C ANISOU 1199 CB ARG A 159 10616 15144 13062 1337 243 -1283 C ATOM 1200 CG ARG A 159 45.100 16.294 -24.047 1.00104.59 C ANISOU 1200 CG ARG A 159 10597 15566 13577 1642 128 -1429 C ATOM 1201 CD ARG A 159 45.649 15.934 -22.682 1.00105.49 C ANISOU 1201 CD ARG A 159 10632 15679 13770 1714 -335 -1503 C ATOM 1202 NE ARG A 159 46.794 15.033 -22.770 1.00107.91 N ANISOU 1202 NE ARG A 159 10652 16070 14280 2060 -510 -1654 N ATOM 1203 CZ ARG A 159 47.456 14.566 -21.718 1.00115.44 C ANISOU 1203 CZ ARG A 159 11510 17024 15329 2213 -955 -1747 C ATOM 1204 NH1 ARG A 159 47.087 14.917 -20.494 1.00117.04 N ANISOU 1204 NH1 ARG A 159 11915 17148 15407 2037 -1252 -1696 N ATOM 1205 NH2 ARG A 159 48.485 13.750 -21.888 1.00123.53 N ANISOU 1205 NH2 ARG A 159 12252 18121 16564 2559 -1112 -1899 N ATOM 1206 N ILE A 160 41.952 15.712 -26.115 1.00 90.68 N ANISOU 1206 N ILE A 160 9870 13427 11157 1607 552 -1128 N ATOM 1207 CA ILE A 160 41.678 14.618 -27.041 1.00 89.97 C ANISOU 1207 CA ILE A 160 10005 13244 10935 1875 575 -1139 C ATOM 1208 C ILE A 160 41.519 15.149 -28.456 1.00 89.89 C ANISOU 1208 C ILE A 160 10027 13269 10856 1867 959 -1122 C ATOM 1209 O ILE A 160 41.829 14.453 -29.430 1.00 94.50 O ANISOU 1209 O ILE A 160 10658 13859 11388 2122 1075 -1183 O ATOM 1210 CB ILE A 160 40.433 13.834 -26.583 1.00 87.71 C ANISOU 1210 CB ILE A 160 10147 12732 10447 1862 326 -1054 C ATOM 1211 CG1 ILE A 160 40.627 13.306 -25.164 1.00 88.30 C ANISOU 1211 CG1 ILE A 160 10254 12754 10543 1868 -33 -1051 C ATOM 1212 CG2 ILE A 160 40.149 12.678 -27.517 1.00 88.21 C ANISOU 1212 CG2 ILE A 160 10453 12672 10390 2130 310 -1082 C ATOM 1213 CD1 ILE A 160 39.411 12.606 -24.605 1.00 86.52 C ANISOU 1213 CD1 ILE A 160 10446 12299 10129 1798 -228 -952 C ATOM 1214 N ALA A 161 41.062 16.393 -28.598 1.00 88.40 N ANISOU 1214 N ALA A 161 9842 13095 10652 1591 1159 -1044 N ATOM 1215 CA ALA A 161 40.956 17.015 -29.911 1.00 88.76 C ANISOU 1215 CA ALA A 161 9957 13159 10609 1572 1521 -1010 C ATOM 1216 C ALA A 161 42.307 17.400 -30.495 1.00 92.14 C ANISOU 1216 C ALA A 161 10023 13778 11209 1622 1839 -1085 C ATOM 1217 O ALA A 161 42.347 18.037 -31.553 1.00 93.02 O ANISOU 1217 O ALA A 161 10193 13909 11240 1576 2193 -1043 O ATOM 1218 CB ALA A 161 40.065 18.254 -29.832 1.00 86.51 C ANISOU 1218 CB ALA A 161 9804 12802 10265 1272 1612 -901 C ATOM 1219 N GLY A 162 43.408 17.047 -29.841 1.00 94.43 N ANISOU 1219 N GLY A 162 9941 14201 11736 1713 1728 -1197 N ATOM 1220 CA GLY A 162 44.709 17.471 -30.316 1.00 98.08 C ANISOU 1220 CA GLY A 162 9979 14857 12428 1727 2044 -1290 C ATOM 1221 C GLY A 162 44.987 18.936 -30.087 1.00 98.41 C ANISOU 1221 C GLY A 162 9790 14967 12634 1369 2253 -1242 C ATOM 1222 O GLY A 162 45.738 19.546 -30.853 1.00101.16 O ANISOU 1222 O GLY A 162 9910 15426 13099 1298 2656 -1263 O ATOM 1223 N LEU A 163 44.398 19.520 -29.049 1.00 95.98 N ANISOU 1223 N LEU A 163 9551 14584 12335 1135 2005 -1183 N ATOM 1224 CA LEU A 163 44.521 20.940 -28.767 1.00 96.10 C ANISOU 1224 CA LEU A 163 9410 14617 12487 786 2159 -1140 C ATOM 1225 C LEU A 163 45.159 21.147 -27.403 1.00 97.04 C ANISOU 1225 C LEU A 163 9198 14812 12862 675 1851 -1240 C ATOM 1226 O LEU A 163 44.884 20.407 -26.453 1.00 95.86 O ANISOU 1226 O LEU A 163 9151 14618 12655 789 1452 -1269 O ATOM 1227 CB LEU A 163 43.159 21.634 -28.811 1.00 92.62 C ANISOU 1227 CB LEU A 163 9386 13996 11810 599 2157 -993 C ATOM 1228 CG LEU A 163 42.669 22.070 -30.191 1.00 92.52 C ANISOU 1228 CG LEU A 163 9654 13905 11596 593 2516 -886 C ATOM 1229 CD1 LEU A 163 41.210 22.482 -30.144 1.00 89.12 C ANISOU 1229 CD1 LEU A 163 9637 13283 10942 492 2396 -773 C ATOM 1230 CD2 LEU A 163 43.525 23.212 -30.701 1.00 95.39 C ANISOU 1230 CD2 LEU A 163 9773 14342 12130 374 2915 -868 C ATOM 1231 N GLU A 164 46.022 22.151 -27.325 1.00118.02 N ANISOU 1231 N GLU A 164 11478 17567 15796 446 2036 -1293 N ATOM 1232 CA GLU A 164 46.618 22.586 -26.070 1.00125.35 C ANISOU 1232 CA GLU A 164 12095 18552 16979 292 1743 -1400 C ATOM 1233 C GLU A 164 45.761 23.725 -25.538 1.00120.74 C ANISOU 1233 C GLU A 164 11750 17831 16296 -26 1709 -1304 C ATOM 1234 O GLU A 164 45.782 24.831 -26.087 1.00130.85 O ANISOU 1234 O GLU A 164 12998 19076 17641 -273 2033 -1245 O ATOM 1235 CB GLU A 164 48.062 23.023 -26.296 1.00136.47 C ANISOU 1235 CB GLU A 164 12919 20139 18795 211 1953 -1539 C ATOM 1236 CG GLU A 164 48.842 23.383 -25.050 1.00140.64 C ANISOU 1236 CG GLU A 164 13064 20738 19636 86 1603 -1694 C ATOM 1237 CD GLU A 164 50.275 23.775 -25.373 1.00146.97 C ANISOU 1237 CD GLU A 164 13227 21718 20896 2 1832 -1853 C ATOM 1238 OE1 GLU A 164 50.652 23.744 -26.564 1.00145.35 O ANISOU 1238 OE1 GLU A 164 12898 21585 20741 42 2306 -1831 O ATOM 1239 OE2 GLU A 164 51.027 24.115 -24.438 1.00151.27 O ANISOU 1239 OE2 GLU A 164 13392 22330 21754 -107 1544 -2009 O ATOM 1240 N VAL A 165 44.991 23.453 -24.489 1.00100.25 N ANISOU 1240 N VAL A 165 9416 15141 13532 -15 1336 -1289 N ATOM 1241 CA VAL A 165 43.978 24.392 -24.016 1.00 93.18 C ANISOU 1241 CA VAL A 165 8809 14100 12494 -261 1310 -1205 C ATOM 1242 C VAL A 165 44.658 25.452 -23.158 1.00 95.19 C ANISOU 1242 C VAL A 165 8779 14388 13001 -527 1212 -1306 C ATOM 1243 O VAL A 165 45.057 25.185 -22.023 1.00103.28 O ANISOU 1243 O VAL A 165 9690 15454 14096 -500 845 -1417 O ATOM 1244 CB VAL A 165 42.874 23.679 -23.232 1.00 90.18 C ANISOU 1244 CB VAL A 165 8818 13610 11837 -157 1003 -1158 C ATOM 1245 CG1 VAL A 165 41.695 24.609 -23.039 1.00 87.58 C ANISOU 1245 CG1 VAL A 165 8789 13131 11355 -373 1071 -1073 C ATOM 1246 CG2 VAL A 165 42.448 22.423 -23.953 1.00 89.08 C ANISOU 1246 CG2 VAL A 165 8885 13445 11515 127 1020 -1101 C ATOM 1247 N LYS A 166 44.776 26.665 -23.694 1.00 96.04 N ANISOU 1247 N LYS A 166 8805 14453 13231 -787 1522 -1269 N ATOM 1248 CA LYS A 166 45.436 27.730 -22.950 1.00 98.30 C ANISOU 1248 CA LYS A 166 8820 14744 13785 -1068 1440 -1375 C ATOM 1249 C LYS A 166 44.541 28.271 -21.843 1.00 96.06 C ANISOU 1249 C LYS A 166 8839 14324 13337 -1200 1172 -1378 C ATOM 1250 O LYS A 166 45.025 28.600 -20.754 1.00 97.68 O ANISOU 1250 O LYS A 166 8887 14548 13677 -1308 880 -1513 O ATOM 1251 CB LYS A 166 45.855 28.849 -23.901 1.00100.33 C ANISOU 1251 CB LYS A 166 8924 14966 14230 -1322 1880 -1324 C ATOM 1252 CG LYS A 166 46.992 28.471 -24.832 1.00103.80 C ANISOU 1252 CG LYS A 166 8969 15566 14902 -1247 2180 -1364 C ATOM 1253 CD LYS A 166 48.215 28.039 -24.044 1.00107.17 C ANISOU 1253 CD LYS A 166 8880 16168 15671 -1191 1898 -1576 C ATOM 1254 CE LYS A 166 49.374 27.708 -24.965 1.00111.17 C ANISOU 1254 CE LYS A 166 8932 16846 16460 -1118 2233 -1644 C ATOM 1255 NZ LYS A 166 50.584 27.291 -24.207 1.00120.22 N ANISOU 1255 NZ LYS A 166 9523 18166 17991 -1040 1928 -1878 N ATOM 1256 N ARG A 167 43.236 28.362 -22.091 1.00 92.69 N ANISOU 1256 N ARG A 167 8841 13757 12621 -1183 1257 -1248 N ATOM 1257 CA ARG A 167 42.353 29.011 -21.132 1.00 90.95 C ANISOU 1257 CA ARG A 167 8891 13403 12263 -1322 1083 -1261 C ATOM 1258 C ARG A 167 40.930 28.504 -21.293 1.00 87.41 C ANISOU 1258 C ARG A 167 8861 12853 11498 -1184 1093 -1148 C ATOM 1259 O ARG A 167 40.390 28.495 -22.401 1.00 86.17 O ANISOU 1259 O ARG A 167 8848 12639 11254 -1125 1343 -1034 O ATOM 1260 CB ARG A 167 42.385 30.532 -21.306 1.00 91.98 C ANISOU 1260 CB ARG A 167 8995 13413 12541 -1622 1277 -1260 C ATOM 1261 CG ARG A 167 41.464 31.276 -20.361 1.00 90.49 C ANISOU 1261 CG ARG A 167 9089 13076 12218 -1750 1122 -1295 C ATOM 1262 CD ARG A 167 41.837 30.998 -18.921 1.00 91.55 C ANISOU 1262 CD ARG A 167 9161 13273 12349 -1746 731 -1448 C ATOM 1263 NE ARG A 167 43.250 31.262 -18.683 1.00 95.23 N ANISOU 1263 NE ARG A 167 9205 13841 13138 -1859 625 -1582 N ATOM 1264 CZ ARG A 167 43.745 32.468 -18.430 1.00 97.53 C ANISOU 1264 CZ ARG A 167 9343 14057 13658 -2134 639 -1674 C ATOM 1265 NH1 ARG A 167 42.935 33.516 -18.376 1.00 96.41 N ANISOU 1265 NH1 ARG A 167 9468 13728 13433 -2302 753 -1642 N ATOM 1266 NH2 ARG A 167 45.045 32.624 -18.224 1.00102.80 N ANISOU 1266 NH2 ARG A 167 9577 14824 14658 -2237 527 -1814 N ATOM 1267 N ILE A 168 40.335 28.093 -20.181 1.00 86.18 N ANISOU 1267 N ILE A 168 8904 12669 11172 -1139 821 -1188 N ATOM 1268 CA ILE A 168 38.911 27.803 -20.105 1.00 83.27 C ANISOU 1268 CA ILE A 168 8903 12189 10549 -1075 833 -1111 C ATOM 1269 C ILE A 168 38.232 29.092 -19.663 1.00 89.57 C ANISOU 1269 C ILE A 168 9839 12855 11337 -1286 888 -1142 C ATOM 1270 O ILE A 168 38.449 29.557 -18.543 1.00106.02 O ANISOU 1270 O ILE A 168 11918 14931 13433 -1405 708 -1249 O ATOM 1271 CB ILE A 168 38.625 26.657 -19.128 1.00 82.84 C ANISOU 1271 CB ILE A 168 9008 12160 10310 -932 559 -1131 C ATOM 1272 CG1 ILE A 168 39.346 25.376 -19.553 1.00 87.25 C ANISOU 1272 CG1 ILE A 168 9438 12822 10891 -700 474 -1113 C ATOM 1273 CG2 ILE A 168 37.148 26.415 -19.019 1.00 80.23 C ANISOU 1273 CG2 ILE A 168 9011 11711 9761 -911 610 -1064 C ATOM 1274 CD1 ILE A 168 38.662 24.613 -20.660 1.00 81.77 C ANISOU 1274 CD1 ILE A 168 8890 12087 10092 -537 640 -1004 C ATOM 1275 N ILE A 169 37.429 29.686 -20.540 1.00 81.46 N ANISOU 1275 N ILE A 169 8955 11713 10285 -1316 1116 -1060 N ATOM 1276 CA ILE A 169 36.804 30.976 -20.270 1.00 81.31 C ANISOU 1276 CA ILE A 169 9065 11545 10285 -1490 1182 -1092 C ATOM 1277 C ILE A 169 35.324 30.763 -19.991 1.00 79.07 C ANISOU 1277 C ILE A 169 9062 11168 9813 -1413 1165 -1080 C ATOM 1278 O ILE A 169 34.676 29.921 -20.623 1.00 77.54 O ANISOU 1278 O ILE A 169 8966 10976 9519 -1252 1207 -1001 O ATOM 1279 CB ILE A 169 37.016 31.969 -21.433 1.00 82.19 C ANISOU 1279 CB ILE A 169 9142 11559 10527 -1590 1439 -1016 C ATOM 1280 CG1 ILE A 169 36.484 33.358 -21.065 1.00 82.54 C ANISOU 1280 CG1 ILE A 169 9324 11421 10615 -1768 1470 -1065 C ATOM 1281 CG2 ILE A 169 36.374 31.460 -22.712 1.00 80.76 C ANISOU 1281 CG2 ILE A 169 9110 11343 10232 -1415 1601 -884 C ATOM 1282 CD1 ILE A 169 36.870 34.455 -22.046 1.00 84.18 C ANISOU 1282 CD1 ILE A 169 9520 11499 10965 -1910 1703 -990 C ATOM 1283 N ASN A 170 34.793 31.513 -19.026 1.00 79.20 N ANISOU 1283 N ASN A 170 9195 11102 9797 -1528 1104 -1176 N ATOM 1284 CA ASN A 170 33.366 31.476 -18.737 1.00 77.63 C ANISOU 1284 CA ASN A 170 9218 10811 9465 -1475 1134 -1190 C ATOM 1285 C ASN A 170 32.601 32.302 -19.767 1.00 77.01 C ANISOU 1285 C ASN A 170 9223 10583 9456 -1462 1302 -1140 C ATOM 1286 O ASN A 170 32.969 33.446 -20.054 1.00 78.21 O ANISOU 1286 O ASN A 170 9353 10636 9726 -1581 1375 -1150 O ATOM 1287 CB ASN A 170 33.090 31.990 -17.325 1.00 79.06 C ANISOU 1287 CB ASN A 170 9507 10960 9572 -1585 1035 -1329 C ATOM 1288 CG ASN A 170 33.798 31.176 -16.252 1.00 93.29 C ANISOU 1288 CG ASN A 170 11298 12887 11260 -1578 827 -1377 C ATOM 1289 OD1 ASN A 170 33.463 30.015 -16.008 1.00 97.29 O ANISOU 1289 OD1 ASN A 170 11895 13451 11619 -1465 774 -1327 O ATOM 1290 ND2 ASN A 170 34.773 31.791 -15.594 1.00103.63 N ANISOU 1290 ND2 ASN A 170 12516 14218 12642 -1700 686 -1477 N ATOM 1291 N GLU A 171 31.532 31.719 -20.313 1.00 75.48 N ANISOU 1291 N GLU A 171 9135 10353 9190 -1319 1343 -1091 N ATOM 1292 CA GLU A 171 30.806 32.319 -21.433 1.00 75.12 C ANISOU 1292 CA GLU A 171 9185 10164 9193 -1250 1448 -1036 C ATOM 1293 C GLU A 171 30.364 33.757 -21.189 1.00 76.02 C ANISOU 1293 C GLU A 171 9384 10110 9389 -1348 1490 -1112 C ATOM 1294 O GLU A 171 30.618 34.609 -22.058 1.00 76.92 O ANISOU 1294 O GLU A 171 9548 10102 9575 -1374 1573 -1046 O ATOM 1295 CB GLU A 171 29.613 31.419 -21.792 1.00 73.67 C ANISOU 1295 CB GLU A 171 9081 9968 8941 -1087 1422 -1021 C ATOM 1296 CG GLU A 171 30.017 30.037 -22.279 1.00 81.17 C ANISOU 1296 CG GLU A 171 9990 11036 9816 -970 1379 -938 C ATOM 1297 CD GLU A 171 28.842 29.089 -22.436 1.00 94.39 C ANISOU 1297 CD GLU A 171 11734 12684 11444 -849 1327 -947 C ATOM 1298 OE1 GLU A 171 27.745 29.399 -21.924 1.00109.05 O ANISOU 1298 OE1 GLU A 171 13628 14468 13338 -874 1334 -1032 O ATOM 1299 OE2 GLU A 171 29.016 28.032 -23.081 1.00 86.73 O ANISOU 1299 OE2 GLU A 171 10771 11761 10421 -729 1286 -881 O ATOM 1300 N PRO A 172 29.726 34.106 -20.065 1.00 80.93 N ANISOU 1300 N PRO A 172 10053 10701 9995 -1400 1451 -1247 N ATOM 1301 CA PRO A 172 29.325 35.509 -19.883 1.00 77.30 C ANISOU 1301 CA PRO A 172 9686 10060 9624 -1469 1486 -1335 C ATOM 1302 C PRO A 172 30.502 36.462 -19.860 1.00 79.02 C ANISOU 1302 C PRO A 172 9866 10221 9936 -1646 1496 -1329 C ATOM 1303 O PRO A 172 30.366 37.614 -20.289 1.00 80.15 O ANISOU 1303 O PRO A 172 10110 10169 10174 -1691 1548 -1329 O ATOM 1304 CB PRO A 172 28.585 35.491 -18.539 1.00 77.42 C ANISOU 1304 CB PRO A 172 9746 10097 9573 -1490 1461 -1498 C ATOM 1305 CG PRO A 172 28.185 34.081 -18.341 1.00 76.11 C ANISOU 1305 CG PRO A 172 9546 10078 9296 -1403 1445 -1463 C ATOM 1306 CD PRO A 172 29.298 33.280 -18.923 1.00 80.55 C ANISOU 1306 CD PRO A 172 10013 10759 9833 -1395 1394 -1328 C ATOM 1307 N THR A 173 31.661 36.008 -19.380 1.00 87.15 N ANISOU 1307 N THR A 173 10751 11401 10960 -1749 1435 -1329 N ATOM 1308 CA THR A 173 32.851 36.849 -19.400 1.00 81.63 C ANISOU 1308 CA THR A 173 9955 10658 10403 -1940 1442 -1336 C ATOM 1309 C THR A 173 33.305 37.117 -20.829 1.00 82.19 C ANISOU 1309 C THR A 173 10007 10659 10561 -1946 1602 -1174 C ATOM 1310 O THR A 173 33.625 38.257 -21.187 1.00 85.38 O ANISOU 1310 O THR A 173 10465 10889 11087 -2088 1687 -1155 O ATOM 1311 CB THR A 173 33.968 36.190 -18.593 1.00 82.42 C ANISOU 1311 CB THR A 173 9865 10949 10503 -2016 1304 -1391 C ATOM 1312 OG1 THR A 173 33.504 35.919 -17.268 1.00 82.22 O ANISOU 1312 OG1 THR A 173 9933 10970 10336 -2000 1161 -1527 O ATOM 1313 CG2 THR A 173 35.160 37.102 -18.504 1.00 94.15 C ANISOU 1313 CG2 THR A 173 11203 12384 12185 -2238 1290 -1437 C ATOM 1314 N ALA A 174 33.341 36.078 -21.663 1.00 82.06 N ANISOU 1314 N ALA A 174 9948 10762 10470 -1797 1656 -1054 N ATOM 1315 CA ALA A 174 33.723 36.267 -23.057 1.00 84.50 C ANISOU 1315 CA ALA A 174 10292 11007 10806 -1780 1834 -898 C ATOM 1316 C ALA A 174 32.780 37.237 -23.751 1.00 82.92 C ANISOU 1316 C ALA A 174 10363 10555 10589 -1734 1897 -848 C ATOM 1317 O ALA A 174 33.217 38.202 -24.398 1.00 85.60 O ANISOU 1317 O ALA A 174 10793 10729 11001 -1855 2033 -767 O ATOM 1318 CB ALA A 174 33.740 34.923 -23.780 1.00 81.25 C ANISOU 1318 CB ALA A 174 9840 10754 10279 -1585 1855 -807 C ATOM 1319 N ALA A 175 31.472 36.996 -23.615 1.00 80.41 N ANISOU 1319 N ALA A 175 10176 10190 10187 -1560 1797 -899 N ATOM 1320 CA ALA A 175 30.497 37.917 -24.186 1.00 80.94 C ANISOU 1320 CA ALA A 175 10484 10009 10259 -1477 1800 -883 C ATOM 1321 C ALA A 175 30.706 39.331 -23.664 1.00 82.87 C ANISOU 1321 C ALA A 175 10801 10056 10628 -1658 1815 -954 C ATOM 1322 O ALA A 175 30.492 40.308 -24.392 1.00 84.39 O ANISOU 1322 O ALA A 175 11210 10004 10849 -1657 1867 -882 O ATOM 1323 CB ALA A 175 29.081 37.441 -23.879 1.00 79.31 C ANISOU 1323 CB ALA A 175 10318 9807 10010 -1282 1674 -982 C ATOM 1324 N ALA A 176 31.140 39.460 -22.410 1.00 83.13 N ANISOU 1324 N ALA A 176 10690 10172 10724 -1810 1751 -1096 N ATOM 1325 CA ALA A 176 31.295 40.782 -21.813 1.00 85.13 C ANISOU 1325 CA ALA A 176 11023 10226 11095 -1980 1735 -1198 C ATOM 1326 C ALA A 176 32.340 41.606 -22.556 1.00 87.55 C ANISOU 1326 C ALA A 176 11361 10386 11517 -2182 1870 -1074 C ATOM 1327 O ALA A 176 32.097 42.769 -22.894 1.00 92.07 O ANISOU 1327 O ALA A 176 12151 10677 12156 -2235 1907 -1053 O ATOM 1328 CB ALA A 176 31.659 40.650 -20.335 1.00 85.25 C ANISOU 1328 CB ALA A 176 10896 10373 11121 -2099 1618 -1381 C ATOM 1329 N LEU A 177 33.516 41.023 -22.823 1.00 88.01 N ANISOU 1329 N LEU A 177 11204 10623 11613 -2297 1959 -993 N ATOM 1330 CA LEU A 177 34.552 41.773 -23.530 1.00 90.80 C ANISOU 1330 CA LEU A 177 11549 10850 12101 -2522 2143 -877 C ATOM 1331 C LEU A 177 34.232 41.929 -25.007 1.00 91.31 C ANISOU 1331 C LEU A 177 11871 10762 12059 -2413 2323 -666 C ATOM 1332 O LEU A 177 34.578 42.960 -25.604 1.00 93.96 O ANISOU 1332 O LEU A 177 12382 10852 12468 -2574 2473 -564 O ATOM 1333 CB LEU A 177 35.928 41.123 -23.344 1.00 91.71 C ANISOU 1333 CB LEU A 177 11306 11210 12329 -2674 2197 -884 C ATOM 1334 CG LEU A 177 36.358 39.763 -23.901 1.00 90.47 C ANISOU 1334 CG LEU A 177 10963 11325 12086 -2527 2267 -798 C ATOM 1335 CD1 LEU A 177 36.522 39.789 -25.398 1.00 91.50 C ANISOU 1335 CD1 LEU A 177 11236 11381 12149 -2488 2538 -591 C ATOM 1336 CD2 LEU A 177 37.674 39.389 -23.288 1.00 91.97 C ANISOU 1336 CD2 LEU A 177 10768 11719 12456 -2690 2231 -889 C ATOM 1337 N ALA A 178 33.595 40.923 -25.613 1.00 89.14 N ANISOU 1337 N ALA A 178 11652 10613 11605 -2149 2303 -598 N ATOM 1338 CA ALA A 178 33.122 41.104 -26.979 1.00 89.79 C ANISOU 1338 CA ALA A 178 12048 10525 11543 -2003 2412 -419 C ATOM 1339 C ALA A 178 32.251 42.346 -27.073 1.00 91.01 C ANISOU 1339 C ALA A 178 12530 10336 11713 -1973 2336 -426 C ATOM 1340 O ALA A 178 32.356 43.127 -28.026 1.00 93.37 O ANISOU 1340 O ALA A 178 13124 10385 11968 -2013 2467 -268 O ATOM 1341 CB ALA A 178 32.359 39.864 -27.440 1.00 87.28 C ANISOU 1341 CB ALA A 178 11750 10368 11043 -1703 2318 -400 C ATOM 1342 N TYR A 179 31.405 42.556 -26.064 1.00 89.77 N ANISOU 1342 N TYR A 179 12341 10154 11615 -1902 2132 -612 N ATOM 1343 CA TYR A 179 30.617 43.780 -25.978 1.00 91.22 C ANISOU 1343 CA TYR A 179 12794 10011 11854 -1865 2042 -665 C ATOM 1344 C TYR A 179 31.481 44.982 -25.625 1.00 94.08 C ANISOU 1344 C TYR A 179 13200 10167 12379 -2174 2132 -673 C ATOM 1345 O TYR A 179 31.159 46.114 -26.007 1.00 96.32 O ANISOU 1345 O TYR A 179 13795 10108 12695 -2186 2130 -626 O ATOM 1346 CB TYR A 179 29.508 43.590 -24.943 1.00 89.40 C ANISOU 1346 CB TYR A 179 12474 9842 11651 -1701 1841 -889 C ATOM 1347 CG TYR A 179 28.838 44.855 -24.455 1.00 91.07 C ANISOU 1347 CG TYR A 179 12875 9759 11970 -1687 1743 -1022 C ATOM 1348 CD1 TYR A 179 27.810 45.443 -25.179 1.00 92.07 C ANISOU 1348 CD1 TYR A 179 13286 9620 12077 -1456 1650 -993 C ATOM 1349 CD2 TYR A 179 29.207 45.437 -23.250 1.00 91.91 C ANISOU 1349 CD2 TYR A 179 12883 9845 12192 -1877 1715 -1197 C ATOM 1350 CE1 TYR A 179 27.185 46.586 -24.728 1.00 93.86 C ANISOU 1350 CE1 TYR A 179 13680 9565 12415 -1410 1549 -1132 C ATOM 1351 CE2 TYR A 179 28.588 46.580 -22.791 1.00 93.65 C ANISOU 1351 CE2 TYR A 179 13288 9787 12506 -1845 1626 -1340 C ATOM 1352 CZ TYR A 179 27.578 47.149 -23.533 1.00 94.60 C ANISOU 1352 CZ TYR A 179 13676 9644 12623 -1607 1552 -1307 C ATOM 1353 OH TYR A 179 26.958 48.288 -23.078 1.00 96.60 O ANISOU 1353 OH TYR A 179 14113 9607 12985 -1546 1454 -1465 O ATOM 1354 N GLY A 180 32.591 44.759 -24.921 1.00 94.38 N ANISOU 1354 N GLY A 180 12938 10390 12533 -2424 2191 -735 N ATOM 1355 CA GLY A 180 33.343 45.865 -24.361 1.00 97.17 C ANISOU 1355 CA GLY A 180 13280 10557 13082 -2730 2219 -803 C ATOM 1356 C GLY A 180 34.353 46.496 -25.293 1.00101.64 C ANISOU 1356 C GLY A 180 13934 10950 13733 -2985 2472 -607 C ATOM 1357 O GLY A 180 34.791 47.620 -25.034 1.00112.09 O ANISOU 1357 O GLY A 180 15345 12015 15229 -3239 2502 -637 O ATOM 1358 N LEU A 181 34.736 45.807 -26.372 1.00100.31 N ANISOU 1358 N LEU A 181 13760 10905 13449 -2934 2673 -411 N ATOM 1359 CA LEU A 181 35.748 46.370 -27.264 1.00103.87 C ANISOU 1359 CA LEU A 181 14288 11206 13973 -3199 2982 -219 C ATOM 1360 C LEU A 181 35.264 47.641 -27.959 1.00112.99 C ANISOU 1360 C LEU A 181 15943 11907 15083 -3227 3041 -80 C ATOM 1361 O LEU A 181 36.075 48.518 -28.279 1.00115.07 O ANISOU 1361 O LEU A 181 16295 11942 15482 -3544 3260 24 O ATOM 1362 CB LEU A 181 36.179 45.333 -28.300 1.00103.42 C ANISOU 1362 CB LEU A 181 14160 11377 13757 -3097 3206 -50 C ATOM 1363 CG LEU A 181 37.010 44.166 -27.768 1.00101.95 C ANISOU 1363 CG LEU A 181 13471 11604 13662 -3127 3210 -157 C ATOM 1364 CD1 LEU A 181 37.910 43.639 -28.870 1.00111.63 C ANISOU 1364 CD1 LEU A 181 14621 12955 14838 -3179 3556 18 C ATOM 1365 CD2 LEU A 181 37.829 44.564 -26.543 1.00103.17 C ANISOU 1365 CD2 LEU A 181 13269 11814 14117 -3416 3108 -351 C ATOM 1366 N ASP A 182 33.956 47.761 -28.199 1.00137.22 N ANISOU 1366 N ASP A 182 19338 14821 17977 -2904 2843 -81 N ATOM 1367 CA ASP A 182 33.427 48.963 -28.839 1.00152.75 C ANISOU 1367 CA ASP A 182 21815 16330 19893 -2880 2842 41 C ATOM 1368 C ASP A 182 33.547 50.179 -27.924 1.00155.20 C ANISOU 1368 C ASP A 182 22162 16364 20443 -3108 2745 -105 C ATOM 1369 O ASP A 182 33.874 51.281 -28.383 1.00163.45 O ANISOU 1369 O ASP A 182 23527 17029 21548 -3312 2874 26 O ATOM 1370 CB ASP A 182 31.969 48.731 -29.249 1.00162.05 C ANISOU 1370 CB ASP A 182 23271 17433 20866 -2441 2596 32 C ATOM 1371 CG ASP A 182 31.429 49.814 -30.176 1.00175.92 C ANISOU 1371 CG ASP A 182 25610 18717 22513 -2346 2576 201 C ATOM 1372 OD1 ASP A 182 31.542 51.015 -29.850 1.00185.17 O ANISOU 1372 OD1 ASP A 182 26975 19548 23834 -2523 2563 178 O ATOM 1373 OD2 ASP A 182 30.877 49.459 -31.240 1.00176.57 O ANISOU 1373 OD2 ASP A 182 25987 18752 22350 -2080 2549 353 O ATOM 1374 N LYS A 183 33.307 49.996 -26.628 1.00131.45 N ANISOU 1374 N LYS A 183 18861 13526 17560 -3084 2527 -376 N ATOM 1375 CA LYS A 183 33.176 51.121 -25.713 1.00123.84 C ANISOU 1375 CA LYS A 183 17986 12287 16780 -3218 2378 -559 C ATOM 1376 C LYS A 183 34.513 51.815 -25.471 1.00136.25 C ANISOU 1376 C LYS A 183 19435 13739 18593 -3683 2542 -545 C ATOM 1377 O LYS A 183 35.583 51.208 -25.558 1.00134.61 O ANISOU 1377 O LYS A 183 18891 13790 18464 -3899 2720 -493 O ATOM 1378 CB LYS A 183 32.584 50.648 -24.387 1.00111.30 C ANISOU 1378 CB LYS A 183 16135 10939 15215 -3061 2130 -856 C ATOM 1379 CG LYS A 183 31.293 49.864 -24.555 1.00106.09 C ANISOU 1379 CG LYS A 183 15511 10431 14367 -2640 1993 -891 C ATOM 1380 CD LYS A 183 30.242 50.694 -25.272 1.00105.31 C ANISOU 1380 CD LYS A 183 15853 9951 14209 -2397 1902 -826 C ATOM 1381 CE LYS A 183 29.136 49.817 -25.833 1.00102.76 C ANISOU 1381 CE LYS A 183 15551 9779 13715 -2004 1796 -799 C ATOM 1382 NZ LYS A 183 29.648 48.883 -26.874 1.00101.81 N ANISOU 1382 NZ LYS A 183 15392 9857 13433 -2002 1958 -566 N ATOM 1383 N GLY A 184 34.437 53.105 -25.162 1.00133.72 N ANISOU 1383 N GLY A 184 19379 13012 18417 -3833 2471 -610 N ATOM 1384 CA GLY A 184 35.603 53.910 -24.863 1.00141.02 C ANISOU 1384 CA GLY A 184 20211 13757 19614 -4293 2587 -630 C ATOM 1385 C GLY A 184 35.896 53.972 -23.381 1.00143.49 C ANISOU 1385 C GLY A 184 20205 14203 20111 -4420 2355 -956 C ATOM 1386 O GLY A 184 35.409 53.162 -22.590 1.00142.36 O ANISOU 1386 O GLY A 184 19846 14381 19865 -4186 2165 -1141 O ATOM 1387 N THR A 185 36.703 54.962 -23.004 1.00153.14 N ANISOU 1387 N THR A 185 21429 15155 21602 -4807 2368 -1029 N ATOM 1388 CA THR A 185 37.127 55.090 -21.616 1.00149.25 C ANISOU 1388 CA THR A 185 20657 14762 21290 -4966 2127 -1348 C ATOM 1389 C THR A 185 35.944 55.446 -20.725 1.00150.46 C ANISOU 1389 C THR A 185 21045 14802 21321 -4664 1837 -1591 C ATOM 1390 O THR A 185 35.150 56.334 -21.051 1.00158.43 O ANISOU 1390 O THR A 185 22484 15421 22291 -4532 1805 -1558 O ATOM 1391 CB THR A 185 38.220 56.150 -21.486 1.00145.77 C ANISOU 1391 CB THR A 185 20189 14007 21190 -5461 2192 -1378 C ATOM 1392 OG1 THR A 185 37.646 57.457 -21.605 1.00145.68 O ANISOU 1392 OG1 THR A 185 20679 13459 21213 -5480 2138 -1375 O ATOM 1393 CG2 THR A 185 39.273 55.965 -22.570 1.00143.59 C ANISOU 1393 CG2 THR A 185 19746 13768 21042 -5762 2568 -1103 C ATOM 1394 N GLY A 186 35.830 54.753 -19.603 1.00162.15 N ANISOU 1394 N GLY A 186 22258 16614 22737 -4544 1632 -1839 N ATOM 1395 CA GLY A 186 34.741 54.992 -18.680 1.00154.82 C ANISOU 1395 CA GLY A 186 21516 15628 21680 -4263 1405 -2091 C ATOM 1396 C GLY A 186 34.515 53.792 -17.789 1.00148.83 C ANISOU 1396 C GLY A 186 20468 15336 20747 -4066 1283 -2252 C ATOM 1397 O GLY A 186 35.177 52.761 -17.905 1.00151.26 O ANISOU 1397 O GLY A 186 20443 15998 21032 -4123 1342 -2164 O ATOM 1398 N ASN A 187 33.551 53.956 -16.889 1.00125.62 N ANISOU 1398 N ASN A 187 17679 12372 17679 -3826 1123 -2492 N ATOM 1399 CA ASN A 187 33.186 52.937 -15.917 1.00124.51 C ANISOU 1399 CA ASN A 187 17354 12616 17339 -3634 1019 -2662 C ATOM 1400 C ASN A 187 31.741 52.526 -16.150 1.00119.31 C ANISOU 1400 C ASN A 187 16824 12019 16489 -3230 1076 -2648 C ATOM 1401 O ASN A 187 30.854 53.382 -16.219 1.00119.78 O ANISOU 1401 O ASN A 187 17164 11778 16569 -3066 1055 -2731 O ATOM 1402 CB ASN A 187 33.370 53.454 -14.487 1.00131.68 C ANISOU 1402 CB ASN A 187 18317 13464 18250 -3731 799 -2999 C ATOM 1403 CG ASN A 187 32.593 52.643 -13.464 1.00132.77 C ANISOU 1403 CG ASN A 187 18431 13897 18119 -3463 726 -3189 C ATOM 1404 OD1 ASN A 187 33.073 51.624 -12.969 1.00131.51 O ANISOU 1404 OD1 ASN A 187 18040 14084 17845 -3487 669 -3200 O ATOM 1405 ND2 ASN A 187 31.389 53.100 -13.135 1.00134.43 N ANISOU 1405 ND2 ASN A 187 18889 13958 18231 -3204 738 -3343 N ATOM 1406 N ARG A 188 31.509 51.221 -16.276 1.00137.69 N ANISOU 1406 N ARG A 188 18936 14722 18656 -3069 1136 -2556 N ATOM 1407 CA ARG A 188 30.162 50.694 -16.424 1.00126.52 C ANISOU 1407 CA ARG A 188 17575 13406 17090 -2710 1182 -2565 C ATOM 1408 C ARG A 188 30.000 49.478 -15.530 1.00122.20 C ANISOU 1408 C ARG A 188 16821 13256 16355 -2617 1158 -2669 C ATOM 1409 O ARG A 188 30.976 48.849 -15.113 1.00132.81 O ANISOU 1409 O ARG A 188 17968 14825 17668 -2792 1106 -2657 O ATOM 1410 CB ARG A 188 29.850 50.299 -17.872 1.00119.75 C ANISOU 1410 CB ARG A 188 16730 12542 16227 -2575 1307 -2280 C ATOM 1411 CG ARG A 188 30.019 51.408 -18.880 1.00123.42 C ANISOU 1411 CG ARG A 188 17456 12608 16829 -2662 1352 -2124 C ATOM 1412 CD ARG A 188 30.211 50.838 -20.270 1.00122.53 C ANISOU 1412 CD ARG A 188 17334 12557 16666 -2618 1489 -1813 C ATOM 1413 NE ARG A 188 30.846 51.796 -21.169 1.00131.20 N ANISOU 1413 NE ARG A 188 18696 13285 17868 -2782 1574 -1625 N ATOM 1414 CZ ARG A 188 32.158 51.998 -21.239 1.00133.14 C ANISOU 1414 CZ ARG A 188 18883 13455 18251 -3151 1673 -1541 C ATOM 1415 NH1 ARG A 188 32.984 51.311 -20.459 1.00132.42 N ANISOU 1415 NH1 ARG A 188 18455 13638 18222 -3368 1655 -1647 N ATOM 1416 NH2 ARG A 188 32.648 52.893 -22.088 1.00133.20 N ANISOU 1416 NH2 ARG A 188 19172 13098 18340 -3305 1787 -1354 N ATOM 1417 N THR A 189 28.747 49.150 -15.243 1.00 99.96 N ANISOU 1417 N THR A 189 14049 10509 13423 -2336 1195 -2774 N ATOM 1418 CA THR A 189 28.408 47.889 -14.605 1.00 97.64 C ANISOU 1418 CA THR A 189 13590 10571 12938 -2227 1225 -2818 C ATOM 1419 C THR A 189 27.304 47.238 -15.424 1.00 95.44 C ANISOU 1419 C THR A 189 13256 10368 12638 -1960 1329 -2703 C ATOM 1420 O THR A 189 26.305 47.888 -15.761 1.00104.20 O ANISOU 1420 O THR A 189 14491 11268 13832 -1767 1348 -2769 O ATOM 1421 CB THR A 189 27.974 48.084 -13.152 1.00 98.96 C ANISOU 1421 CB THR A 189 13859 10770 12971 -2187 1187 -3115 C ATOM 1422 OG1 THR A 189 28.854 49.017 -12.512 1.00101.77 O ANISOU 1422 OG1 THR A 189 14333 10950 13385 -2410 1047 -3257 O ATOM 1423 CG2 THR A 189 28.046 46.763 -12.412 1.00 97.19 C ANISOU 1423 CG2 THR A 189 13500 10904 12523 -2171 1204 -3123 C ATOM 1424 N ILE A 190 27.505 45.966 -15.773 1.00 92.93 N ANISOU 1424 N ILE A 190 12748 10333 12228 -1942 1371 -2542 N ATOM 1425 CA ILE A 190 26.620 45.259 -16.687 1.00 90.95 C ANISOU 1425 CA ILE A 190 12429 10154 11975 -1721 1438 -2413 C ATOM 1426 C ILE A 190 26.195 43.928 -16.083 1.00 88.97 C ANISOU 1426 C ILE A 190 12020 10214 11570 -1644 1488 -2447 C ATOM 1427 O ILE A 190 26.928 43.298 -15.310 1.00 88.59 O ANISOU 1427 O ILE A 190 11902 10362 11394 -1780 1462 -2461 O ATOM 1428 CB ILE A 190 27.268 45.027 -18.072 1.00 90.14 C ANISOU 1428 CB ILE A 190 12299 10029 11920 -1763 1452 -2136 C ATOM 1429 CG1 ILE A 190 28.382 43.980 -17.991 1.00 88.77 C ANISOU 1429 CG1 ILE A 190 11932 10133 11663 -1918 1461 -2017 C ATOM 1430 CG2 ILE A 190 27.789 46.331 -18.649 1.00 92.56 C ANISOU 1430 CG2 ILE A 190 12797 10010 12363 -1886 1437 -2075 C ATOM 1431 CD1 ILE A 190 28.897 43.532 -19.342 1.00 87.92 C ANISOU 1431 CD1 ILE A 190 11779 10055 11571 -1917 1522 -1762 C ATOM 1432 N ALA A 191 24.989 43.507 -16.458 1.00 88.05 N ANISOU 1432 N ALA A 191 11853 10123 11479 -1424 1546 -2461 N ATOM 1433 CA ALA A 191 24.438 42.198 -16.150 1.00 86.31 C ANISOU 1433 CA ALA A 191 11483 10159 11153 -1349 1617 -2457 C ATOM 1434 C ALA A 191 24.355 41.408 -17.446 1.00 84.45 C ANISOU 1434 C ALA A 191 11153 9981 10955 -1252 1593 -2243 C ATOM 1435 O ALA A 191 23.690 41.832 -18.398 1.00 84.79 O ANISOU 1435 O ALA A 191 11235 9859 11121 -1091 1556 -2209 O ATOM 1436 CB ALA A 191 23.057 42.316 -15.510 1.00 87.30 C ANISOU 1436 CB ALA A 191 11588 10267 11315 -1189 1720 -2678 C ATOM 1437 N VAL A 192 25.036 40.273 -17.480 1.00 82.80 N ANISOU 1437 N VAL A 192 10842 9989 10628 -1332 1591 -2108 N ATOM 1438 CA VAL A 192 25.045 39.385 -18.632 1.00 81.13 C ANISOU 1438 CA VAL A 192 10556 9852 10418 -1242 1569 -1919 C ATOM 1439 C VAL A 192 24.109 38.228 -18.326 1.00 80.97 C ANISOU 1439 C VAL A 192 10418 9992 10356 -1143 1615 -1965 C ATOM 1440 O VAL A 192 24.333 37.474 -17.367 1.00 86.39 O ANISOU 1440 O VAL A 192 11064 10847 10911 -1234 1659 -1999 O ATOM 1441 CB VAL A 192 26.464 38.892 -18.943 1.00 80.43 C ANISOU 1441 CB VAL A 192 10424 9883 10254 -1385 1544 -1750 C ATOM 1442 CG1 VAL A 192 26.449 37.934 -20.115 1.00 78.94 C ANISOU 1442 CG1 VAL A 192 10182 9770 10040 -1271 1536 -1574 C ATOM 1443 CG2 VAL A 192 27.364 40.075 -19.232 1.00 82.06 C ANISOU 1443 CG2 VAL A 192 10721 9917 10542 -1522 1533 -1713 C ATOM 1444 N TYR A 193 23.054 38.103 -19.134 1.00 79.85 N ANISOU 1444 N TYR A 193 10233 9777 10329 -960 1593 -1969 N ATOM 1445 CA TYR A 193 22.006 37.103 -18.953 1.00 79.31 C ANISOU 1445 CA TYR A 193 10023 9820 10291 -872 1639 -2033 C ATOM 1446 C TYR A 193 22.118 36.108 -20.103 1.00 77.82 C ANISOU 1446 C TYR A 193 9794 9689 10087 -793 1548 -1860 C ATOM 1447 O TYR A 193 21.699 36.397 -21.226 1.00 78.08 O ANISOU 1447 O TYR A 193 9863 9591 10215 -638 1442 -1817 O ATOM 1448 CB TYR A 193 20.635 37.773 -18.914 1.00 80.92 C ANISOU 1448 CB TYR A 193 10167 9889 10689 -715 1659 -2226 C ATOM 1449 CG TYR A 193 19.469 36.841 -18.688 1.00 81.02 C ANISOU 1449 CG TYR A 193 9983 10004 10797 -649 1735 -2325 C ATOM 1450 CD1 TYR A 193 18.890 36.151 -19.743 1.00 80.45 C ANISOU 1450 CD1 TYR A 193 9808 9924 10836 -517 1616 -2263 C ATOM 1451 CD2 TYR A 193 18.929 36.673 -17.422 1.00 82.10 C ANISOU 1451 CD2 TYR A 193 10049 10232 10915 -729 1933 -2492 C ATOM 1452 CE1 TYR A 193 17.822 35.309 -19.540 1.00 80.93 C ANISOU 1452 CE1 TYR A 193 9661 10062 11028 -486 1682 -2366 C ATOM 1453 CE2 TYR A 193 17.857 35.836 -17.211 1.00 82.67 C ANISOU 1453 CE2 TYR A 193 9926 10386 11099 -704 2046 -2582 C ATOM 1454 CZ TYR A 193 17.312 35.155 -18.273 1.00 82.07 C ANISOU 1454 CZ TYR A 193 9711 10297 11176 -592 1914 -2521 C ATOM 1455 OH TYR A 193 16.246 34.318 -18.072 1.00 82.98 O ANISOU 1455 OH TYR A 193 9604 10481 11445 -595 2022 -2621 O ATOM 1456 N ASP A 194 22.679 34.938 -19.818 1.00 76.55 N ANISOU 1456 N ASP A 194 9588 9707 9792 -882 1571 -1768 N ATOM 1457 CA ASP A 194 22.973 33.927 -20.828 1.00 75.27 C ANISOU 1457 CA ASP A 194 9409 9605 9584 -816 1489 -1610 C ATOM 1458 C ASP A 194 22.005 32.768 -20.637 1.00 74.92 C ANISOU 1458 C ASP A 194 9247 9638 9580 -775 1505 -1661 C ATOM 1459 O ASP A 194 22.065 32.065 -19.626 1.00 78.17 O ANISOU 1459 O ASP A 194 9631 10167 9902 -891 1596 -1686 O ATOM 1460 CB ASP A 194 24.426 33.460 -20.715 1.00 85.58 C ANISOU 1460 CB ASP A 194 10747 11035 10734 -932 1487 -1474 C ATOM 1461 CG ASP A 194 24.887 32.636 -21.913 1.00 96.94 C ANISOU 1461 CG ASP A 194 12197 12512 12124 -839 1418 -1316 C ATOM 1462 OD1 ASP A 194 24.036 32.079 -22.639 1.00 94.88 O ANISOU 1462 OD1 ASP A 194 11925 12214 11913 -702 1354 -1314 O ATOM 1463 OD2 ASP A 194 26.114 32.541 -22.126 1.00110.91 O ANISOU 1463 OD2 ASP A 194 13978 14349 13815 -900 1426 -1209 O ATOM 1464 N LEU A 195 21.117 32.569 -21.606 1.00 75.09 N ANISOU 1464 N LEU A 195 9218 9578 9736 -618 1406 -1678 N ATOM 1465 CA LEU A 195 20.174 31.453 -21.591 1.00 75.11 C ANISOU 1465 CA LEU A 195 9084 9628 9826 -592 1399 -1731 C ATOM 1466 C LEU A 195 20.306 30.719 -22.923 1.00 74.37 C ANISOU 1466 C LEU A 195 9037 9510 9712 -462 1224 -1613 C ATOM 1467 O LEU A 195 19.717 31.131 -23.926 1.00 75.10 O ANISOU 1467 O LEU A 195 9147 9474 9912 -293 1076 -1642 O ATOM 1468 CB LEU A 195 18.752 31.943 -21.353 1.00 76.80 C ANISOU 1468 CB LEU A 195 9139 9760 10283 -521 1432 -1935 C ATOM 1469 CG LEU A 195 17.673 30.876 -21.163 1.00 77.49 C ANISOU 1469 CG LEU A 195 9028 9890 10523 -542 1472 -2027 C ATOM 1470 CD1 LEU A 195 18.050 29.961 -20.022 1.00 77.08 C ANISOU 1470 CD1 LEU A 195 9001 9977 10309 -749 1663 -1980 C ATOM 1471 CD2 LEU A 195 16.330 31.531 -20.901 1.00 79.68 C ANISOU 1471 CD2 LEU A 195 9098 10093 11084 -467 1527 -2258 C ATOM 1472 N GLY A 196 21.074 29.641 -22.939 1.00 73.24 N ANISOU 1472 N GLY A 196 8938 9474 9417 -520 1224 -1490 N ATOM 1473 CA GLY A 196 21.361 28.912 -24.147 1.00 72.69 C ANISOU 1473 CA GLY A 196 8946 9388 9286 -396 1078 -1384 C ATOM 1474 C GLY A 196 20.481 27.699 -24.333 1.00 72.89 C ANISOU 1474 C GLY A 196 8880 9409 9407 -365 996 -1435 C ATOM 1475 O GLY A 196 19.330 27.657 -23.883 1.00 73.91 O ANISOU 1475 O GLY A 196 8851 9503 9728 -397 1023 -1576 O ATOM 1476 N GLY A 197 21.026 26.701 -25.028 1.00 72.25 N ANISOU 1476 N GLY A 197 8889 9353 9208 -304 902 -1331 N ATOM 1477 CA GLY A 197 20.279 25.481 -25.254 1.00 72.62 C ANISOU 1477 CA GLY A 197 8877 9371 9344 -287 802 -1375 C ATOM 1478 C GLY A 197 20.274 24.534 -24.081 1.00 72.53 C ANISOU 1478 C GLY A 197 8808 9433 9315 -472 933 -1370 C ATOM 1479 O GLY A 197 19.390 23.678 -23.994 1.00 73.37 O ANISOU 1479 O GLY A 197 8827 9491 9561 -520 904 -1437 O ATOM 1480 N GLY A 198 21.229 24.676 -23.171 1.00 72.55 N ANISOU 1480 N GLY A 198 8874 9538 9155 -582 1067 -1294 N ATOM 1481 CA GLY A 198 21.294 23.774 -22.043 1.00 77.42 C ANISOU 1481 CA GLY A 198 9511 10205 9700 -741 1172 -1269 C ATOM 1482 C GLY A 198 21.564 24.429 -20.704 1.00 84.28 C ANISOU 1482 C GLY A 198 10395 11146 10481 -888 1348 -1292 C ATOM 1483 O GLY A 198 21.140 23.911 -19.665 1.00 96.73 O ANISOU 1483 O GLY A 198 11991 12733 12030 -1034 1479 -1314 O ATOM 1484 N ALA A 199 22.268 25.558 -20.703 1.00 71.99 N ANISOU 1484 N ALA A 199 8857 9626 8868 -860 1357 -1287 N ATOM 1485 CA ALA A 199 22.736 26.178 -19.476 1.00 72.41 C ANISOU 1485 CA ALA A 199 8960 9743 8808 -986 1475 -1313 C ATOM 1486 C ALA A 199 22.225 27.606 -19.363 1.00 72.99 C ANISOU 1486 C ALA A 199 8967 9766 8999 -984 1551 -1437 C ATOM 1487 O ALA A 199 21.910 28.257 -20.361 1.00 72.84 O ANISOU 1487 O ALA A 199 8896 9668 9112 -864 1477 -1461 O ATOM 1488 CB ALA A 199 24.265 26.173 -19.405 1.00 71.80 C ANISOU 1488 CB ALA A 199 8969 9751 8562 -980 1393 -1206 C ATOM 1489 N PHE A 200 22.163 28.083 -18.121 1.00 73.94 N ANISOU 1489 N PHE A 200 9128 9917 9047 -1106 1689 -1518 N ATOM 1490 CA PHE A 200 21.823 29.462 -17.800 1.00 74.78 C ANISOU 1490 CA PHE A 200 9207 9972 9235 -1109 1767 -1651 C ATOM 1491 C PHE A 200 22.880 30.039 -16.875 1.00 75.10 C ANISOU 1491 C PHE A 200 9376 10066 9094 -1208 1777 -1649 C ATOM 1492 O PHE A 200 23.260 29.403 -15.889 1.00 75.58 O ANISOU 1492 O PHE A 200 9547 10204 8967 -1308 1812 -1623 O ATOM 1493 CB PHE A 200 20.459 29.568 -17.126 1.00 76.38 C ANISOU 1493 CB PHE A 200 9316 10143 9561 -1150 1952 -1816 C ATOM 1494 CG PHE A 200 20.220 30.892 -16.465 1.00 77.65 C ANISOU 1494 CG PHE A 200 9490 10261 9752 -1161 2059 -1973 C ATOM 1495 CD1 PHE A 200 20.037 32.029 -17.222 1.00 77.74 C ANISOU 1495 CD1 PHE A 200 9448 10161 9929 -1034 1970 -2035 C ATOM 1496 CD2 PHE A 200 20.180 31.000 -15.090 1.00 79.07 C ANISOU 1496 CD2 PHE A 200 9776 10492 9774 -1287 2241 -2059 C ATOM 1497 CE1 PHE A 200 19.818 33.243 -16.624 1.00 79.13 C ANISOU 1497 CE1 PHE A 200 9654 10269 10141 -1032 2054 -2189 C ATOM 1498 CE2 PHE A 200 19.959 32.215 -14.489 1.00 80.47 C ANISOU 1498 CE2 PHE A 200 9986 10618 9972 -1282 2334 -2224 C ATOM 1499 CZ PHE A 200 19.777 33.338 -15.258 1.00 80.46 C ANISOU 1499 CZ PHE A 200 9908 10498 10164 -1153 2237 -2293 C ATOM 1500 N ASP A 201 23.340 31.244 -17.190 1.00 75.18 N ANISOU 1500 N ASP A 201 9392 10015 9158 -1183 1727 -1678 N ATOM 1501 CA ASP A 201 24.295 31.975 -16.376 1.00 75.88 C ANISOU 1501 CA ASP A 201 9578 10126 9127 -1285 1709 -1711 C ATOM 1502 C ASP A 201 23.839 33.416 -16.249 1.00 77.02 C ANISOU 1502 C ASP A 201 9733 10144 9387 -1275 1764 -1857 C ATOM 1503 O ASP A 201 23.225 33.973 -17.161 1.00 76.95 O ANISOU 1503 O ASP A 201 9662 10020 9554 -1163 1750 -1876 O ATOM 1504 CB ASP A 201 25.705 31.957 -16.974 1.00 75.15 C ANISOU 1504 CB ASP A 201 9479 10074 9001 -1295 1567 -1577 C ATOM 1505 CG ASP A 201 26.388 30.622 -16.823 1.00 85.10 C ANISOU 1505 CG ASP A 201 10749 11460 10124 -1300 1489 -1463 C ATOM 1506 OD1 ASP A 201 26.130 29.927 -15.820 1.00 81.13 O ANISOU 1506 OD1 ASP A 201 10337 11011 9479 -1353 1523 -1489 O ATOM 1507 OD2 ASP A 201 27.186 30.269 -17.714 1.00 99.71 O ANISOU 1507 OD2 ASP A 201 12538 13346 12002 -1243 1404 -1347 O ATOM 1508 N ILE A 202 24.141 34.009 -15.102 1.00 78.35 N ANISOU 1508 N ILE A 202 10009 10318 9444 -1376 1804 -1969 N ATOM 1509 CA ILE A 202 24.016 35.442 -14.889 1.00 79.70 C ANISOU 1509 CA ILE A 202 10229 10352 9700 -1380 1822 -2112 C ATOM 1510 C ILE A 202 25.316 35.924 -14.272 1.00 80.44 C ANISOU 1510 C ILE A 202 10425 10463 9676 -1513 1711 -2116 C ATOM 1511 O ILE A 202 25.807 35.326 -13.306 1.00 80.93 O ANISOU 1511 O ILE A 202 10573 10639 9538 -1596 1682 -2124 O ATOM 1512 CB ILE A 202 22.823 35.798 -13.986 1.00 81.37 C ANISOU 1512 CB ILE A 202 10471 10529 9918 -1357 2004 -2318 C ATOM 1513 CG1 ILE A 202 22.919 37.257 -13.545 1.00 83.10 C ANISOU 1513 CG1 ILE A 202 10793 10606 10176 -1370 2000 -2483 C ATOM 1514 CG2 ILE A 202 22.755 34.867 -12.792 1.00 82.06 C ANISOU 1514 CG2 ILE A 202 10657 10754 9768 -1452 2117 -2340 C ATOM 1515 CD1 ILE A 202 22.754 38.241 -14.677 1.00 83.03 C ANISOU 1515 CD1 ILE A 202 10736 10412 10399 -1263 1915 -2470 C ATOM 1516 N SER A 203 25.883 36.985 -14.835 1.00 80.85 N ANISOU 1516 N SER A 203 10477 10387 9855 -1538 1634 -2110 N ATOM 1517 CA SER A 203 27.115 37.529 -14.284 1.00 82.00 C ANISOU 1517 CA SER A 203 10679 10529 9949 -1687 1516 -2138 C ATOM 1518 C SER A 203 27.016 39.042 -14.193 1.00 83.73 C ANISOU 1518 C SER A 203 10988 10538 10288 -1724 1516 -2275 C ATOM 1519 O SER A 203 26.625 39.697 -15.160 1.00 83.62 O ANISOU 1519 O SER A 203 10962 10368 10442 -1651 1545 -2234 O ATOM 1520 CB SER A 203 28.325 37.121 -15.124 1.00 90.44 C ANISOU 1520 CB SER A 203 11626 11666 11072 -1737 1412 -1958 C ATOM 1521 OG SER A 203 28.654 35.762 -14.902 1.00 98.32 O ANISOU 1521 OG SER A 203 12575 12852 11933 -1714 1366 -1869 O ATOM 1522 N ILE A 204 27.363 39.586 -13.029 1.00 85.59 N ANISOU 1522 N ILE A 204 11348 10752 10422 -1827 1465 -2439 N ATOM 1523 CA ILE A 204 27.498 41.023 -12.833 1.00 87.63 C ANISOU 1523 CA ILE A 204 11714 10794 10787 -1892 1426 -2582 C ATOM 1524 C ILE A 204 28.974 41.364 -12.950 1.00 88.48 C ANISOU 1524 C ILE A 204 11770 10885 10964 -2079 1261 -2524 C ATOM 1525 O ILE A 204 29.793 40.890 -12.148 1.00 89.13 O ANISOU 1525 O ILE A 204 11846 11103 10917 -2176 1130 -2559 O ATOM 1526 CB ILE A 204 26.939 41.468 -11.474 1.00 89.65 C ANISOU 1526 CB ILE A 204 12156 11017 10890 -1886 1470 -2833 C ATOM 1527 CG1 ILE A 204 25.512 40.961 -11.291 1.00 89.17 C ANISOU 1527 CG1 ILE A 204 12090 11014 10776 -1721 1680 -2895 C ATOM 1528 CG2 ILE A 204 26.983 42.980 -11.364 1.00 91.88 C ANISOU 1528 CG2 ILE A 204 12565 11041 11305 -1927 1424 -2993 C ATOM 1529 CD1 ILE A 204 24.560 41.444 -12.347 1.00 88.64 C ANISOU 1529 CD1 ILE A 204 11928 10801 10949 -1566 1762 -2878 C ATOM 1530 N ILE A 205 29.304 42.188 -13.944 1.00 88.86 N ANISOU 1530 N ILE A 205 11786 10756 11221 -2130 1264 -2439 N ATOM 1531 CA ILE A 205 30.681 42.487 -14.317 1.00 89.86 C ANISOU 1531 CA ILE A 205 11805 10860 11478 -2326 1167 -2355 C ATOM 1532 C ILE A 205 30.844 43.997 -14.406 1.00 92.28 C ANISOU 1532 C ILE A 205 12239 10869 11956 -2449 1148 -2445 C ATOM 1533 O ILE A 205 29.974 44.691 -14.946 1.00 92.42 O ANISOU 1533 O ILE A 205 12390 10682 12046 -2339 1236 -2445 O ATOM 1534 CB ILE A 205 31.055 41.829 -15.662 1.00 88.19 C ANISOU 1534 CB ILE A 205 11432 10728 11347 -2293 1247 -2105 C ATOM 1535 CG1 ILE A 205 30.859 40.314 -15.598 1.00 85.95 C ANISOU 1535 CG1 ILE A 205 11045 10708 10902 -2162 1252 -2023 C ATOM 1536 CG2 ILE A 205 32.483 42.168 -16.055 1.00 89.75 C ANISOU 1536 CG2 ILE A 205 11484 10908 11708 -2511 1204 -2030 C ATOM 1537 CD1 ILE A 205 31.025 39.623 -16.931 1.00 84.34 C ANISOU 1537 CD1 ILE A 205 10724 10573 10748 -2083 1337 -1804 C ATOM 1538 N GLU A 206 31.957 44.508 -13.883 1.00 94.50 N ANISOU 1538 N GLU A 206 12480 11107 12317 -2672 1010 -2530 N ATOM 1539 CA GLU A 206 32.279 45.926 -13.960 1.00 97.23 C ANISOU 1539 CA GLU A 206 12942 11147 12853 -2838 976 -2612 C ATOM 1540 C GLU A 206 33.396 46.134 -14.973 1.00 98.12 C ANISOU 1540 C GLU A 206 12886 11207 13188 -3042 1023 -2426 C ATOM 1541 O GLU A 206 34.379 45.385 -14.983 1.00 97.96 O ANISOU 1541 O GLU A 206 12620 11403 13199 -3141 972 -2362 O ATOM 1542 CB GLU A 206 32.692 46.479 -12.593 1.00 99.81 C ANISOU 1542 CB GLU A 206 13365 11423 13135 -2969 780 -2878 C ATOM 1543 CG GLU A 206 32.810 47.999 -12.552 1.00102.87 C ANISOU 1543 CG GLU A 206 13928 11449 13707 -3118 735 -3004 C ATOM 1544 CD GLU A 206 33.383 48.512 -11.246 1.00108.38 C ANISOU 1544 CD GLU A 206 14714 12095 14372 -3269 501 -3278 C ATOM 1545 OE1 GLU A 206 33.248 47.812 -10.223 1.00115.15 O ANISOU 1545 OE1 GLU A 206 15607 13162 14982 -3177 400 -3407 O ATOM 1546 OE2 GLU A 206 33.974 49.612 -11.241 1.00119.03 O ANISOU 1546 OE2 GLU A 206 16118 13176 15930 -3486 409 -3365 O ATOM 1547 N ILE A 207 33.239 47.147 -15.821 1.00 99.40 N ANISOU 1547 N ILE A 207 13190 11073 13505 -3098 1129 -2342 N ATOM 1548 CA ILE A 207 34.188 47.452 -16.885 1.00100.74 C ANISOU 1548 CA ILE A 207 13255 11149 13873 -3303 1246 -2145 C ATOM 1549 C ILE A 207 34.676 48.874 -16.651 1.00104.46 C ANISOU 1549 C ILE A 207 13857 11280 14553 -3562 1192 -2252 C ATOM 1550 O ILE A 207 33.974 49.842 -16.964 1.00105.53 O ANISOU 1550 O ILE A 207 14280 11096 14720 -3509 1234 -2255 O ATOM 1551 CB ILE A 207 33.571 47.306 -18.278 1.00 99.28 C ANISOU 1551 CB ILE A 207 13184 10891 13648 -3137 1443 -1900 C ATOM 1552 CG1 ILE A 207 32.992 45.906 -18.463 1.00 95.79 C ANISOU 1552 CG1 ILE A 207 12628 10759 13009 -2878 1469 -1824 C ATOM 1553 CG2 ILE A 207 34.607 47.597 -19.347 1.00101.15 C ANISOU 1553 CG2 ILE A 207 13344 11036 14051 -3365 1613 -1691 C ATOM 1554 CD1 ILE A 207 32.234 45.730 -19.758 1.00 94.47 C ANISOU 1554 CD1 ILE A 207 12602 10515 12776 -2674 1605 -1623 C ATOM 1555 N ASP A 208 35.874 49.006 -16.099 1.00106.74 N ANISOU 1555 N ASP A 208 13935 11617 15003 -3839 1076 -2351 N ATOM 1556 CA ASP A 208 36.503 50.299 -15.892 1.00120.35 C ANISOU 1556 CA ASP A 208 15737 13018 16972 -4140 1014 -2456 C ATOM 1557 C ASP A 208 37.709 50.413 -16.813 1.00120.36 C ANISOU 1557 C ASP A 208 15500 12994 17238 -4439 1182 -2271 C ATOM 1558 O ASP A 208 38.338 49.411 -17.161 1.00111.64 O ANISOU 1558 O ASP A 208 14083 12193 16143 -4437 1254 -2162 O ATOM 1559 CB ASP A 208 36.927 50.482 -14.428 1.00133.67 C ANISOU 1559 CB ASP A 208 17375 14748 18666 -4247 714 -2767 C ATOM 1560 CG ASP A 208 37.172 51.941 -14.057 1.00147.38 C ANISOU 1560 CG ASP A 208 19308 16083 20606 -4491 609 -2936 C ATOM 1561 OD1 ASP A 208 37.292 52.789 -14.967 1.00161.09 O ANISOU 1561 OD1 ASP A 208 21159 17513 22534 -4649 778 -2787 O ATOM 1562 OD2 ASP A 208 37.251 52.240 -12.846 1.00142.72 O ANISOU 1562 OD2 ASP A 208 18790 15466 19971 -4525 350 -3219 O ATOM 1563 N GLU A 209 38.018 51.642 -17.214 1.00152.94 N ANISOU 1563 N GLU A 209 19783 16742 21585 -4695 1263 -2240 N ATOM 1564 CA GLU A 209 39.131 51.929 -18.109 1.00157.49 C ANISOU 1564 CA GLU A 209 20170 17234 22436 -5026 1484 -2063 C ATOM 1565 C GLU A 209 40.118 52.839 -17.393 1.00157.51 C ANISOU 1565 C GLU A 209 20042 17042 22765 -5419 1324 -2268 C ATOM 1566 O GLU A 209 39.789 53.985 -17.069 1.00159.74 O ANISOU 1566 O GLU A 209 20632 16946 23115 -5518 1232 -2381 O ATOM 1567 CB GLU A 209 38.636 52.583 -19.397 1.00160.42 C ANISOU 1567 CB GLU A 209 20888 17286 22779 -5012 1768 -1794 C ATOM 1568 CG GLU A 209 39.747 53.105 -20.287 1.00163.75 C ANISOU 1568 CG GLU A 209 21200 17539 23479 -5403 2047 -1611 C ATOM 1569 CD GLU A 209 40.269 52.055 -21.235 1.00161.79 C ANISOU 1569 CD GLU A 209 20681 17606 23186 -5367 2321 -1387 C ATOM 1570 OE1 GLU A 209 39.967 50.866 -21.024 1.00160.31 O ANISOU 1570 OE1 GLU A 209 20317 17793 22800 -5077 2232 -1414 O ATOM 1571 OE2 GLU A 209 40.975 52.422 -22.196 1.00162.19 O ANISOU 1571 OE2 GLU A 209 20715 17516 23392 -5629 2642 -1185 O ATOM 1572 N VAL A 210 41.325 52.332 -17.156 1.00149.65 N ANISOU 1572 N VAL A 210 18583 16289 21989 -5636 1273 -2332 N ATOM 1573 CA VAL A 210 42.365 53.065 -16.443 1.00149.83 C ANISOU 1573 CA VAL A 210 18395 16171 22365 -6020 1076 -2556 C ATOM 1574 C VAL A 210 43.647 52.978 -17.262 1.00144.22 C ANISOU 1574 C VAL A 210 17258 15524 22015 -6362 1335 -2415 C ATOM 1575 O VAL A 210 44.201 51.886 -17.442 1.00136.78 O ANISOU 1575 O VAL A 210 15922 14963 21086 -6282 1383 -2369 O ATOM 1576 CB VAL A 210 42.583 52.527 -15.022 1.00153.17 C ANISOU 1576 CB VAL A 210 18635 16845 22717 -5924 645 -2871 C ATOM 1577 CG1 VAL A 210 41.333 52.733 -14.189 1.00158.99 C ANISOU 1577 CG1 VAL A 210 19136 17426 23846 -6326 402 -3118 C ATOM 1578 CG2 VAL A 210 42.967 51.050 -15.062 1.00154.14 C ANISOU 1578 CG2 VAL A 210 19193 16905 22469 -5596 455 -3013 C ATOM 1579 N ASP A 211 44.112 54.125 -17.761 1.00137.16 N ANISOU 1579 N ASP A 211 16449 14245 21420 -6744 1520 -2350 N ATOM 1580 CA ASP A 211 45.362 54.225 -18.518 1.00141.16 C ANISOU 1580 CA ASP A 211 16554 14758 22321 -7140 1820 -2232 C ATOM 1581 C ASP A 211 45.342 53.334 -19.760 1.00147.22 C ANISOU 1581 C ASP A 211 17238 15767 22932 -6976 2238 -1915 C ATOM 1582 O ASP A 211 46.268 52.560 -20.012 1.00150.74 O ANISOU 1582 O ASP A 211 17183 16529 23560 -7055 2362 -1902 O ATOM 1583 CB ASP A 211 46.568 53.900 -17.633 1.00144.69 C ANISOU 1583 CB ASP A 211 16408 15444 23125 -7361 1531 -2516 C ATOM 1584 CG ASP A 211 46.858 54.983 -16.611 1.00150.12 C ANISOU 1584 CG ASP A 211 17156 15818 24066 -7648 1172 -2818 C ATOM 1585 OD1 ASP A 211 46.524 56.159 -16.871 1.00152.27 O ANISOU 1585 OD1 ASP A 211 17823 15631 24403 -7845 1283 -2763 O ATOM 1586 OD2 ASP A 211 47.428 54.659 -15.549 1.00151.65 O ANISOU 1586 OD2 ASP A 211 17026 16206 24388 -7668 758 -3118 O ATOM 1587 N GLY A 212 44.272 53.455 -20.543 1.00152.84 N ANISOU 1587 N GLY A 212 18450 16316 23304 -6729 2438 -1676 N ATOM 1588 CA GLY A 212 44.149 52.687 -21.772 1.00149.66 C ANISOU 1588 CA GLY A 212 18066 16094 22703 -6553 2816 -1377 C ATOM 1589 C GLY A 212 44.146 51.189 -21.566 1.00135.39 C ANISOU 1589 C GLY A 212 15930 14795 20718 -6220 2710 -1421 C ATOM 1590 O GLY A 212 44.523 50.438 -22.474 1.00135.66 O ANISOU 1590 O GLY A 212 15783 15046 20714 -6165 3016 -1238 O ATOM 1591 N GLU A 213 43.733 50.731 -20.389 1.00142.90 N ANISOU 1591 N GLU A 213 16826 15926 21543 -5995 2290 -1661 N ATOM 1592 CA GLU A 213 43.757 49.312 -20.044 1.00139.77 C ANISOU 1592 CA GLU A 213 16141 15983 20983 -5693 2141 -1720 C ATOM 1593 C GLU A 213 42.392 48.935 -19.474 1.00133.66 C ANISOU 1593 C GLU A 213 15729 15251 19807 -5292 1902 -1774 C ATOM 1594 O GLU A 213 42.093 49.229 -18.313 1.00142.28 O ANISOU 1594 O GLU A 213 16908 16292 20862 -5264 1567 -2010 O ATOM 1595 CB GLU A 213 44.888 49.009 -19.064 1.00143.49 C ANISOU 1595 CB GLU A 213 16094 16670 21756 -5868 1855 -1985 C ATOM 1596 CG GLU A 213 46.284 49.199 -19.660 1.00153.52 C ANISOU 1596 CG GLU A 213 16891 17965 23474 -6248 2116 -1951 C ATOM 1597 CD GLU A 213 47.397 49.018 -18.639 1.00161.99 C ANISOU 1597 CD GLU A 213 17431 19216 24901 -6424 1766 -2252 C ATOM 1598 OE1 GLU A 213 47.099 49.022 -17.428 1.00171.38 O ANISOU 1598 OE1 GLU A 213 18712 20421 25983 -6313 1308 -2490 O ATOM 1599 OE2 GLU A 213 48.570 48.871 -19.047 1.00159.76 O ANISOU 1599 OE2 GLU A 213 16640 19057 25003 -6667 1946 -2262 O ATOM 1600 N LYS A 214 41.568 48.296 -20.304 1.00108.71 N ANISOU 1600 N LYS A 214 11484 14256 15563 -4272 3208 -1685 N ATOM 1601 CA LYS A 214 40.259 47.829 -19.870 1.00106.10 C ANISOU 1601 CA LYS A 214 11410 13797 15105 -4090 3145 -1736 C ATOM 1602 C LYS A 214 40.406 46.807 -18.751 1.00105.67 C ANISOU 1602 C LYS A 214 11281 13923 14948 -3995 2939 -1808 C ATOM 1603 O LYS A 214 41.183 45.856 -18.861 1.00106.17 O ANISOU 1603 O LYS A 214 11123 14192 15026 -3879 2880 -1749 O ATOM 1604 CB LYS A 214 39.505 47.203 -21.046 1.00104.07 C ANISOU 1604 CB LYS A 214 11278 13485 14778 -3854 3283 -1612 C ATOM 1605 CG LYS A 214 39.147 48.153 -22.178 1.00109.24 C ANISOU 1605 CG LYS A 214 12060 13950 15499 -3950 3452 -1497 C ATOM 1606 CD LYS A 214 37.739 48.709 -22.015 1.00107.47 C ANISOU 1606 CD LYS A 214 12125 13426 15285 -3917 3435 -1525 C ATOM 1607 CE LYS A 214 37.424 49.744 -23.087 1.00103.96 C ANISOU 1607 CE LYS A 214 11795 12758 14947 -4039 3549 -1374 C ATOM 1608 NZ LYS A 214 37.788 49.281 -24.460 1.00104.19 N ANISOU 1608 NZ LYS A 214 11770 12933 14883 -3993 3688 -1186 N ATOM 1609 N THR A 215 39.660 47.004 -17.670 1.00105.10 N ANISOU 1609 N THR A 215 11383 13769 14780 -4056 2825 -1937 N ATOM 1610 CA THR A 215 39.586 46.032 -16.588 1.00104.71 C ANISOU 1610 CA THR A 215 11323 13881 14582 -3994 2617 -1976 C ATOM 1611 C THR A 215 38.167 45.489 -16.553 1.00102.07 C ANISOU 1611 C THR A 215 11246 13427 14108 -3804 2643 -1990 C ATOM 1612 O THR A 215 37.221 46.229 -16.264 1.00101.55 O ANISOU 1612 O THR A 215 11386 13179 14021 -3881 2710 -2112 O ATOM 1613 CB THR A 215 39.973 46.650 -15.247 1.00106.81 C ANISOU 1613 CB THR A 215 11566 14219 14798 -4279 2456 -2127 C ATOM 1614 OG1 THR A 215 41.298 47.183 -15.337 1.00115.48 O ANISOU 1614 OG1 THR A 215 12411 15421 16044 -4463 2429 -2107 O ATOM 1615 CG2 THR A 215 39.939 45.594 -14.150 1.00106.81 C ANISOU 1615 CG2 THR A 215 11559 14413 14612 -4248 2212 -2122 C ATOM 1616 N PHE A 216 38.021 44.204 -16.870 1.00100.64 N ANISOU 1616 N PHE A 216 11038 13335 13865 -3557 2595 -1877 N ATOM 1617 CA PHE A 216 36.743 43.502 -16.771 1.00 98.28 C ANISOU 1617 CA PHE A 216 10959 12957 13426 -3380 2589 -1874 C ATOM 1618 C PHE A 216 36.767 42.690 -15.483 1.00 98.73 C ANISOU 1618 C PHE A 216 11012 13178 13325 -3419 2349 -1892 C ATOM 1619 O PHE A 216 37.335 41.598 -15.444 1.00 99.03 O ANISOU 1619 O PHE A 216 10904 13353 13371 -3292 2202 -1773 O ATOM 1620 CB PHE A 216 36.515 42.590 -17.972 1.00 96.64 C ANISOU 1620 CB PHE A 216 10745 12727 13246 -3102 2684 -1740 C ATOM 1621 CG PHE A 216 36.423 43.309 -19.285 1.00 96.40 C ANISOU 1621 CG PHE A 216 10746 12564 13318 -3088 2907 -1691 C ATOM 1622 CD1 PHE A 216 37.567 43.681 -19.969 1.00 98.19 C ANISOU 1622 CD1 PHE A 216 10764 12875 13668 -3170 2994 -1642 C ATOM 1623 CD2 PHE A 216 35.192 43.583 -19.855 1.00 94.66 C ANISOU 1623 CD2 PHE A 216 10756 12146 13067 -3008 3019 -1677 C ATOM 1624 CE1 PHE A 216 37.485 44.330 -21.184 1.00 98.32 C ANISOU 1624 CE1 PHE A 216 10824 12792 13741 -3198 3190 -1570 C ATOM 1625 CE2 PHE A 216 35.105 44.233 -21.070 1.00 94.80 C ANISOU 1625 CE2 PHE A 216 10812 12045 13162 -3022 3186 -1592 C ATOM 1626 CZ PHE A 216 36.253 44.607 -21.735 1.00 96.65 C ANISOU 1626 CZ PHE A 216 10861 12378 13485 -3129 3273 -1531 C ATOM 1627 N GLU A 217 36.150 43.211 -14.429 1.00 99.11 N ANISOU 1627 N GLU A 217 11215 13209 13235 -3607 2305 -2041 N ATOM 1628 CA GLU A 217 36.112 42.525 -13.144 1.00 99.94 C ANISOU 1628 CA GLU A 217 11347 13493 13133 -3710 2075 -2050 C ATOM 1629 C GLU A 217 34.739 41.901 -12.954 1.00 97.93 C ANISOU 1629 C GLU A 217 11319 13176 12714 -3591 2104 -2063 C ATOM 1630 O GLU A 217 33.723 42.602 -13.006 1.00 97.05 O ANISOU 1630 O GLU A 217 11379 12907 12589 -3620 2277 -2212 O ATOM 1631 CB GLU A 217 36.432 43.467 -11.985 1.00102.35 C ANISOU 1631 CB GLU A 217 11662 13882 13343 -4055 2003 -2233 C ATOM 1632 CG GLU A 217 36.421 42.752 -10.641 1.00103.65 C ANISOU 1632 CG GLU A 217 11868 14272 13241 -4212 1748 -2221 C ATOM 1633 CD GLU A 217 36.850 43.631 -9.484 1.00106.49 C ANISOU 1633 CD GLU A 217 12230 14761 13472 -4588 1660 -2409 C ATOM 1634 OE1 GLU A 217 36.900 44.865 -9.656 1.00107.20 O ANISOU 1634 OE1 GLU A 217 12331 14716 13683 -4719 1831 -2598 O ATOM 1635 OE2 GLU A 217 37.137 43.081 -8.398 1.00114.67 O ANISOU 1635 OE2 GLU A 217 13261 16027 14283 -4769 1407 -2362 O ATOM 1636 N VAL A 218 34.713 40.589 -12.742 1.00 97.45 N ANISOU 1636 N VAL A 218 11243 13225 12560 -3458 1928 -1906 N ATOM 1637 CA VAL A 218 33.467 39.880 -12.476 1.00 95.83 C ANISOU 1637 CA VAL A 218 11240 12987 12184 -3371 1927 -1896 C ATOM 1638 C VAL A 218 33.094 40.131 -11.020 1.00 97.41 C ANISOU 1638 C VAL A 218 11560 13331 12122 -3669 1827 -2030 C ATOM 1639 O VAL A 218 33.787 39.681 -10.106 1.00 99.42 O ANISOU 1639 O VAL A 218 11741 13789 12245 -3833 1576 -1949 O ATOM 1640 CB VAL A 218 33.591 38.381 -12.763 1.00 95.11 C ANISOU 1640 CB VAL A 218 11092 12939 12105 -3142 1762 -1674 C ATOM 1641 CG1 VAL A 218 32.323 37.669 -12.332 1.00 93.82 C ANISOU 1641 CG1 VAL A 218 11142 12761 11744 -3108 1737 -1657 C ATOM 1642 CG2 VAL A 218 33.849 38.151 -14.236 1.00 93.75 C ANISOU 1642 CG2 VAL A 218 10821 12636 12163 -2864 1907 -1597 C ATOM 1643 N LEU A 219 32.002 40.861 -10.803 1.00 96.85 N ANISOU 1643 N LEU A 219 11663 13159 11978 -3754 2021 -2241 N ATOM 1644 CA LEU A 219 31.557 41.125 -9.440 1.00 98.63 C ANISOU 1644 CA LEU A 219 12007 13537 11931 -4057 1978 -2423 C ATOM 1645 C LEU A 219 30.841 39.921 -8.849 1.00 98.22 C ANISOU 1645 C LEU A 219 12074 13617 11627 -4049 1846 -2303 C ATOM 1646 O LEU A 219 31.084 39.562 -7.691 1.00100.34 O ANISOU 1646 O LEU A 219 12373 14124 11630 -4304 1647 -2281 O ATOM 1647 CB LEU A 219 30.654 42.358 -9.409 1.00 98.66 C ANISOU 1647 CB LEU A 219 12121 13370 11994 -4147 2252 -2734 C ATOM 1648 CG LEU A 219 31.296 43.632 -9.959 1.00 99.41 C ANISOU 1648 CG LEU A 219 12116 13298 12355 -4186 2374 -2847 C ATOM 1649 CD1 LEU A 219 30.396 44.836 -9.738 1.00100.12 C ANISOU 1649 CD1 LEU A 219 12308 13200 12531 -4299 2608 -3174 C ATOM 1650 CD2 LEU A 219 32.663 43.855 -9.331 1.00101.91 C ANISOU 1650 CD2 LEU A 219 12292 13808 12619 -4419 2187 -2829 C ATOM 1651 N ALA A 220 29.969 39.275 -9.622 1.00105.60 N ANISOU 1651 N ALA A 220 13083 14410 12632 -3782 1936 -2209 N ATOM 1652 CA ALA A 220 29.290 38.096 -9.100 1.00 98.71 C ANISOU 1652 CA ALA A 220 12321 13646 11537 -3781 1803 -2076 C ATOM 1653 C ALA A 220 28.848 37.211 -10.252 1.00 92.85 C ANISOU 1653 C ALA A 220 11585 12732 10961 -3428 1833 -1893 C ATOM 1654 O ALA A 220 28.744 37.654 -11.396 1.00 92.04 O ANISOU 1654 O ALA A 220 11447 12431 11094 -3217 2011 -1923 O ATOM 1655 CB ALA A 220 28.089 38.480 -8.229 1.00102.52 C ANISOU 1655 CB ALA A 220 12975 14195 11782 -3999 1953 -2314 C ATOM 1656 N THR A 221 28.590 35.947 -9.936 1.00 92.78 N ANISOU 1656 N THR A 221 11629 12802 10820 -3388 1644 -1697 N ATOM 1657 CA THR A 221 28.071 35.036 -10.940 1.00 90.54 C ANISOU 1657 CA THR A 221 11372 12357 10672 -3078 1666 -1548 C ATOM 1658 C THR A 221 27.205 33.983 -10.274 1.00 90.66 C ANISOU 1658 C THR A 221 11528 12452 10465 -3142 1540 -1436 C ATOM 1659 O THR A 221 27.453 33.578 -9.135 1.00 92.79 O ANISOU 1659 O THR A 221 11828 12921 10507 -3386 1326 -1351 O ATOM 1660 CB THR A 221 29.187 34.361 -11.736 1.00 90.47 C ANISOU 1660 CB THR A 221 11186 12293 10894 -2849 1522 -1354 C ATOM 1661 OG1 THR A 221 28.601 33.483 -12.701 1.00 88.51 O ANISOU 1661 OG1 THR A 221 10982 11890 10757 -2568 1563 -1252 O ATOM 1662 CG2 THR A 221 30.089 33.557 -10.819 1.00 92.86 C ANISOU 1662 CG2 THR A 221 11398 12764 11120 -2973 1180 -1164 C ATOM 1663 N ASN A 222 26.182 33.551 -11.001 1.00 88.92 N ANISOU 1663 N ASN A 222 11399 12081 10305 -2944 1664 -1422 N ATOM 1664 CA ASN A 222 25.301 32.491 -10.534 1.00 88.54 C ANISOU 1664 CA ASN A 222 11481 12079 10079 -2983 1557 -1299 C ATOM 1665 C ASN A 222 24.670 31.855 -11.762 1.00 86.14 C ANISOU 1665 C ASN A 222 11206 11561 9962 -2665 1637 -1224 C ATOM 1666 O ASN A 222 24.861 32.322 -12.886 1.00 84.70 O ANISOU 1666 O ASN A 222 10957 11224 10000 -2455 1786 -1282 O ATOM 1667 CB ASN A 222 24.247 33.031 -9.565 1.00 89.37 C ANISOU 1667 CB ASN A 222 11720 12316 9921 -3262 1703 -1497 C ATOM 1668 CG ASN A 222 23.989 32.091 -8.414 1.00 96.84 C ANISOU 1668 CG ASN A 222 12767 13468 10559 -3510 1487 -1343 C ATOM 1669 OD1 ASN A 222 23.182 31.170 -8.520 1.00 96.35 O ANISOU 1669 OD1 ASN A 222 12796 13365 10448 -3447 1446 -1216 O ATOM 1670 ND2 ASN A 222 24.683 32.310 -7.305 1.00106.88 N ANISOU 1670 ND2 ASN A 222 14029 14969 11611 -3817 1332 -1339 N ATOM 1671 N GLY A 223 23.929 30.775 -11.547 1.00 85.97 N ANISOU 1671 N GLY A 223 11288 11539 9837 -2656 1528 -1086 N ATOM 1672 CA GLY A 223 23.209 30.177 -12.656 1.00 83.88 C ANISOU 1672 CA GLY A 223 11068 11080 9723 -2387 1606 -1038 C ATOM 1673 C GLY A 223 22.835 28.733 -12.372 1.00 84.32 C ANISOU 1673 C GLY A 223 11203 11128 9707 -2374 1385 -818 C ATOM 1674 O GLY A 223 22.866 28.279 -11.230 1.00 97.40 O ANISOU 1674 O GLY A 223 12911 12943 11154 -2612 1198 -706 O ATOM 1675 N ASP A 224 22.473 28.041 -13.452 1.00 83.19 N ANISOU 1675 N ASP A 224 11076 10797 9735 -2110 1406 -758 N ATOM 1676 CA ASP A 224 22.039 26.648 -13.416 1.00 83.02 C ANISOU 1676 CA ASP A 224 11132 10704 9709 -2055 1213 -563 C ATOM 1677 C ASP A 224 22.565 25.976 -14.673 1.00 86.73 C ANISOU 1677 C ASP A 224 11521 10973 10458 -1732 1178 -511 C ATOM 1678 O ASP A 224 22.217 26.389 -15.783 1.00 83.02 O ANISOU 1678 O ASP A 224 11054 10395 10094 -1560 1388 -636 O ATOM 1679 CB ASP A 224 20.513 26.554 -13.345 1.00 82.03 C ANISOU 1679 CB ASP A 224 11154 10571 9444 -2128 1346 -617 C ATOM 1680 CG ASP A 224 20.015 25.143 -13.094 1.00 82.72 C ANISOU 1680 CG ASP A 224 11336 10607 9488 -2144 1132 -402 C ATOM 1681 OD1 ASP A 224 20.821 24.192 -13.164 1.00 83.79 O ANISOU 1681 OD1 ASP A 224 11422 10657 9756 -2042 882 -216 O ATOM 1682 OD2 ASP A 224 18.804 24.986 -12.831 1.00 82.42 O ANISOU 1682 OD2 ASP A 224 11408 10600 9307 -2259 1212 -424 O ATOM 1683 N THR A 225 23.396 24.949 -14.506 1.00 83.81 N ANISOU 1683 N THR A 225 11076 10553 10216 -1661 910 -332 N ATOM 1684 CA THR A 225 24.046 24.300 -15.639 1.00 83.66 C ANISOU 1684 CA THR A 225 10945 10352 10491 -1361 886 -328 C ATOM 1685 C THR A 225 23.153 23.291 -16.348 1.00 82.78 C ANISOU 1685 C THR A 225 10945 10059 10447 -1206 880 -292 C ATOM 1686 O THR A 225 23.603 22.666 -17.314 1.00 82.90 O ANISOU 1686 O THR A 225 10882 9918 10697 -964 874 -321 O ATOM 1687 CB THR A 225 25.328 23.604 -15.181 1.00 86.19 C ANISOU 1687 CB THR A 225 11099 10658 10991 -1325 594 -172 C ATOM 1688 OG1 THR A 225 24.998 22.476 -14.364 1.00 87.78 O ANISOU 1688 OG1 THR A 225 11385 10818 11150 -1424 295 60 O ATOM 1689 CG2 THR A 225 26.173 24.549 -14.369 1.00 87.35 C ANISOU 1689 CG2 THR A 225 11142 11001 11047 -1517 563 -189 C ATOM 1690 N HIS A 226 21.913 23.110 -15.903 1.00 82.14 N ANISOU 1690 N HIS A 226 11036 10002 10172 -1350 890 -250 N ATOM 1691 CA HIS A 226 20.985 22.161 -16.508 1.00 81.43 C ANISOU 1691 CA HIS A 226 11059 9748 10133 -1237 872 -211 C ATOM 1692 C HIS A 226 19.621 22.809 -16.694 1.00 79.58 C ANISOU 1692 C HIS A 226 10951 9560 9725 -1322 1101 -327 C ATOM 1693 O HIS A 226 18.575 22.232 -16.388 1.00 79.54 O ANISOU 1693 O HIS A 226 11068 9537 9618 -1417 1054 -254 O ATOM 1694 CB HIS A 226 20.883 20.895 -15.666 1.00 83.39 C ANISOU 1694 CB HIS A 226 11366 9943 10376 -1336 556 31 C ATOM 1695 CG HIS A 226 20.379 19.704 -16.419 1.00 83.32 C ANISOU 1695 CG HIS A 226 11423 9703 10534 -1162 475 81 C ATOM 1696 ND1 HIS A 226 19.051 19.541 -16.753 1.00 85.62 N ANISOU 1696 ND1 HIS A 226 11860 9954 10716 -1194 589 44 N ATOM 1697 CD2 HIS A 226 21.023 18.610 -16.887 1.00 84.74 C ANISOU 1697 CD2 HIS A 226 11529 9666 11001 -959 288 149 C ATOM 1698 CE1 HIS A 226 18.901 18.399 -17.399 1.00 89.94 C ANISOU 1698 CE1 HIS A 226 12440 10280 11454 -1032 471 92 C ATOM 1699 NE2 HIS A 226 20.082 17.815 -17.495 1.00 86.90 N ANISOU 1699 NE2 HIS A 226 11925 9775 11318 -882 294 145 N ATOM 1700 N LEU A 227 19.631 24.039 -17.202 1.00 78.26 N ANISOU 1700 N LEU A 227 10742 9445 9549 -1293 1344 -504 N ATOM 1701 CA LEU A 227 18.416 24.778 -17.523 1.00 76.73 C ANISOU 1701 CA LEU A 227 10627 9258 9269 -1334 1560 -627 C ATOM 1702 C LEU A 227 18.645 25.509 -18.836 1.00 75.46 C ANISOU 1702 C LEU A 227 10416 9014 9240 -1151 1745 -752 C ATOM 1703 O LEU A 227 19.546 26.350 -18.925 1.00 75.64 O ANISOU 1703 O LEU A 227 10341 9091 9309 -1146 1821 -820 O ATOM 1704 CB LEU A 227 18.058 25.767 -16.413 1.00 77.16 C ANISOU 1704 CB LEU A 227 10686 9488 9144 -1586 1656 -709 C ATOM 1705 CG LEU A 227 16.951 26.764 -16.753 1.00 75.97 C ANISOU 1705 CG LEU A 227 10559 9323 8983 -1606 1897 -876 C ATOM 1706 CD1 LEU A 227 15.609 26.070 -16.804 1.00 75.60 C ANISOU 1706 CD1 LEU A 227 10606 9229 8888 -1629 1892 -835 C ATOM 1707 CD2 LEU A 227 16.929 27.898 -15.750 1.00 76.80 C ANISOU 1707 CD2 LEU A 227 10626 9581 8973 -1825 2019 -1020 C ATOM 1708 N GLY A 228 17.849 25.194 -19.848 1.00 74.41 N ANISOU 1708 N GLY A 228 10354 8763 9156 -1026 1807 -771 N ATOM 1709 CA GLY A 228 18.046 25.812 -21.139 1.00 73.58 C ANISOU 1709 CA GLY A 228 10222 8595 9139 -885 1958 -859 C ATOM 1710 C GLY A 228 16.905 25.518 -22.082 1.00 72.64 C ANISOU 1710 C GLY A 228 10205 8372 9025 -809 2003 -865 C ATOM 1711 O GLY A 228 15.821 25.111 -21.661 1.00 72.43 O ANISOU 1711 O GLY A 228 10253 8327 8939 -881 1956 -827 O ATOM 1712 N GLY A 229 17.176 25.723 -23.374 1.00 72.35 N ANISOU 1712 N GLY A 229 10165 8280 9043 -684 2091 -911 N ATOM 1713 CA GLY A 229 16.137 25.546 -24.377 1.00 71.70 C ANISOU 1713 CA GLY A 229 10181 8113 8948 -631 2122 -911 C ATOM 1714 C GLY A 229 15.600 24.130 -24.434 1.00 71.94 C ANISOU 1714 C GLY A 229 10295 8060 8977 -582 1983 -864 C ATOM 1715 O GLY A 229 14.405 23.918 -24.659 1.00 71.46 O ANISOU 1715 O GLY A 229 10317 7948 8885 -609 1964 -839 O ATOM 1716 N GLU A 230 16.474 23.142 -24.218 1.00 72.92 N ANISOU 1716 N GLU A 230 10387 8155 9166 -512 1871 -847 N ATOM 1717 CA GLU A 230 16.057 21.745 -24.250 1.00 73.52 C ANISOU 1717 CA GLU A 230 10539 8113 9283 -464 1717 -799 C ATOM 1718 C GLU A 230 14.870 21.484 -23.337 1.00 73.21 C ANISOU 1718 C GLU A 230 10576 8077 9164 -609 1631 -700 C ATOM 1719 O GLU A 230 14.021 20.639 -23.645 1.00 73.29 O ANISOU 1719 O GLU A 230 10678 7990 9178 -601 1552 -668 O ATOM 1720 CB GLU A 230 17.224 20.843 -23.851 1.00 75.05 C ANISOU 1720 CB GLU A 230 10650 8253 9611 -383 1577 -774 C ATOM 1721 CG GLU A 230 18.370 20.811 -24.840 1.00 75.87 C ANISOU 1721 CG GLU A 230 10657 8340 9832 -224 1668 -905 C ATOM 1722 CD GLU A 230 18.067 19.964 -26.062 1.00 87.14 C ANISOU 1722 CD GLU A 230 12158 9645 11306 -103 1690 -1010 C ATOM 1723 OE1 GLU A 230 17.393 18.920 -25.919 1.00 93.46 O ANISOU 1723 OE1 GLU A 230 13048 10312 12148 -96 1544 -959 O ATOM 1724 OE2 GLU A 230 18.498 20.352 -27.170 1.00 91.23 O ANISOU 1724 OE2 GLU A 230 12649 10209 11803 -39 1856 -1146 O ATOM 1725 N ASP A 231 14.786 22.201 -22.218 1.00 73.09 N ANISOU 1725 N ASP A 231 10520 8184 9068 -761 1655 -668 N ATOM 1726 CA ASP A 231 13.708 21.964 -21.269 1.00 73.22 C ANISOU 1726 CA ASP A 231 10592 8242 8985 -933 1603 -596 C ATOM 1727 C ASP A 231 12.423 22.666 -21.689 1.00 72.23 C ANISOU 1727 C ASP A 231 10489 8123 8832 -970 1740 -662 C ATOM 1728 O ASP A 231 11.330 22.134 -21.459 1.00 75.34 O ANISOU 1728 O ASP A 231 10937 8497 9190 -1053 1695 -616 O ATOM 1729 CB ASP A 231 14.153 22.393 -19.872 1.00 73.99 C ANISOU 1729 CB ASP A 231 10638 8492 8984 -1109 1581 -560 C ATOM 1730 CG ASP A 231 15.473 21.751 -19.465 1.00 75.27 C ANISOU 1730 CG ASP A 231 10752 8641 9204 -1071 1409 -469 C ATOM 1731 OD1 ASP A 231 15.517 20.513 -19.291 1.00 88.79 O ANISOU 1731 OD1 ASP A 231 12512 10254 10970 -1055 1209 -341 O ATOM 1732 OD2 ASP A 231 16.474 22.484 -19.334 1.00 75.41 O ANISOU 1732 OD2 ASP A 231 10675 8735 9243 -1055 1460 -522 O ATOM 1733 N PHE A 232 12.527 23.848 -22.306 1.00 71.49 N ANISOU 1733 N PHE A 232 10343 8045 8776 -917 1893 -756 N ATOM 1734 CA PHE A 232 11.372 24.432 -22.986 1.00 70.87 C ANISOU 1734 CA PHE A 232 10273 7920 8733 -909 1980 -796 C ATOM 1735 C PHE A 232 10.795 23.438 -23.987 1.00 70.80 C ANISOU 1735 C PHE A 232 10357 7801 8741 -822 1885 -749 C ATOM 1736 O PHE A 232 9.595 23.113 -23.958 1.00 74.61 O ANISOU 1736 O PHE A 232 10869 8254 9224 -881 1851 -722 O ATOM 1737 CB PHE A 232 11.773 25.728 -23.699 1.00 70.46 C ANISOU 1737 CB PHE A 232 10163 7863 8746 -849 2109 -861 C ATOM 1738 CG PHE A 232 12.165 26.858 -22.775 1.00 70.68 C ANISOU 1738 CG PHE A 232 10096 7974 8783 -946 2216 -935 C ATOM 1739 CD1 PHE A 232 13.290 26.771 -21.977 1.00 71.14 C ANISOU 1739 CD1 PHE A 232 10121 8123 8786 -992 2191 -940 C ATOM 1740 CD2 PHE A 232 11.429 28.030 -22.743 1.00 70.70 C ANISOU 1740 CD2 PHE A 232 10035 7950 8877 -990 2329 -1008 C ATOM 1741 CE1 PHE A 232 13.654 27.811 -21.144 1.00 71.54 C ANISOU 1741 CE1 PHE A 232 10093 8257 8832 -1101 2285 -1025 C ATOM 1742 CE2 PHE A 232 11.792 29.071 -21.912 1.00 71.17 C ANISOU 1742 CE2 PHE A 232 10009 8069 8963 -1084 2435 -1111 C ATOM 1743 CZ PHE A 232 12.906 28.959 -21.114 1.00 71.55 C ANISOU 1743 CZ PHE A 232 10042 8227 8917 -1148 2417 -1124 C ATOM 1744 N ASP A 233 11.657 22.930 -24.871 1.00 70.97 N ANISOU 1744 N ASP A 233 10416 7767 8781 -694 1849 -759 N ATOM 1745 CA ASP A 233 11.269 21.871 -25.794 1.00 71.28 C ANISOU 1745 CA ASP A 233 10552 7702 8829 -621 1758 -751 C ATOM 1746 C ASP A 233 10.567 20.738 -25.062 1.00 71.77 C ANISOU 1746 C ASP A 233 10669 7711 8890 -697 1616 -674 C ATOM 1747 O ASP A 233 9.511 20.270 -25.495 1.00 71.81 O ANISOU 1747 O ASP A 233 10738 7655 8892 -722 1563 -653 O ATOM 1748 CB ASP A 233 12.504 21.346 -26.528 1.00 71.95 C ANISOU 1748 CB ASP A 233 10642 7749 8948 -488 1753 -815 C ATOM 1749 CG ASP A 233 13.173 22.403 -27.376 1.00 71.77 C ANISOU 1749 CG ASP A 233 10574 7794 8900 -443 1901 -881 C ATOM 1750 OD1 ASP A 233 12.699 23.557 -27.373 1.00 72.66 O ANISOU 1750 OD1 ASP A 233 10660 7956 8993 -508 1982 -857 O ATOM 1751 OD2 ASP A 233 14.181 22.081 -28.040 1.00 72.55 O ANISOU 1751 OD2 ASP A 233 10656 7892 9018 -351 1939 -961 O ATOM 1752 N SER A 234 11.134 20.293 -23.937 1.00 72.39 N ANISOU 1752 N SER A 234 10721 7817 8965 -755 1537 -612 N ATOM 1753 CA SER A 234 10.567 19.147 -23.232 1.00 73.25 C ANISOU 1753 CA SER A 234 10894 7869 9067 -853 1377 -503 C ATOM 1754 C SER A 234 9.160 19.442 -22.742 1.00 72.99 C ANISOU 1754 C SER A 234 10864 7906 8961 -1016 1422 -474 C ATOM 1755 O SER A 234 8.280 18.577 -22.807 1.00 73.48 O ANISOU 1755 O SER A 234 10993 7896 9029 -1074 1325 -414 O ATOM 1756 CB SER A 234 11.464 18.741 -22.066 1.00 74.30 C ANISOU 1756 CB SER A 234 10997 8038 9196 -919 1262 -406 C ATOM 1757 OG SER A 234 10.999 17.546 -21.465 1.00 75.51 O ANISOU 1757 OG SER A 234 11226 8113 9352 -1022 1074 -265 O ATOM 1758 N ARG A 235 8.928 20.661 -22.252 1.00 72.46 N ANISOU 1758 N ARG A 235 10711 7972 8848 -1094 1575 -535 N ATOM 1759 CA ARG A 235 7.585 21.041 -21.826 1.00 72.53 C ANISOU 1759 CA ARG A 235 10679 8047 8830 -1235 1652 -554 C ATOM 1760 C ARG A 235 6.605 20.968 -22.988 1.00 72.12 C ANISOU 1760 C ARG A 235 10647 7894 8860 -1157 1645 -572 C ATOM 1761 O ARG A 235 5.531 20.359 -22.878 1.00 72.63 O ANISOU 1761 O ARG A 235 10731 7940 8926 -1249 1589 -527 O ATOM 1762 CB ARG A 235 7.600 22.446 -21.225 1.00 72.33 C ANISOU 1762 CB ARG A 235 10538 8148 8795 -1302 1834 -665 C ATOM 1763 CG ARG A 235 8.420 22.578 -19.951 1.00 73.05 C ANISOU 1763 CG ARG A 235 10610 8377 8769 -1435 1842 -658 C ATOM 1764 CD ARG A 235 7.916 21.639 -18.883 1.00 74.35 C ANISOU 1764 CD ARG A 235 10824 8624 8802 -1647 1748 -554 C ATOM 1765 NE ARG A 235 8.735 21.701 -17.680 1.00 82.81 N ANISOU 1765 NE ARG A 235 11894 9841 9728 -1804 1717 -516 N ATOM 1766 CZ ARG A 235 8.584 22.615 -16.731 1.00 78.91 C ANISOU 1766 CZ ARG A 235 11329 9529 9126 -1981 1872 -634 C ATOM 1767 NH1 ARG A 235 7.646 23.543 -16.855 1.00 75.82 N ANISOU 1767 NH1 ARG A 235 10843 9166 8802 -1996 2076 -808 N ATOM 1768 NH2 ARG A 235 9.368 22.604 -15.663 1.00 80.16 N ANISOU 1768 NH2 ARG A 235 11502 9833 9122 -2148 1816 -587 N ATOM 1769 N LEU A 236 6.967 21.565 -24.127 1.00 71.43 N ANISOU 1769 N LEU A 236 10560 7751 8831 -1007 1688 -624 N ATOM 1770 CA LEU A 236 6.054 21.523 -25.268 1.00 71.35 C ANISOU 1770 CA LEU A 236 10577 7660 8874 -958 1652 -620 C ATOM 1771 C LEU A 236 5.806 20.089 -25.729 1.00 71.91 C ANISOU 1771 C LEU A 236 10768 7630 8923 -948 1495 -569 C ATOM 1772 O LEU A 236 4.676 19.724 -26.077 1.00 72.26 O ANISOU 1772 O LEU A 236 10829 7634 8994 -1001 1431 -540 O ATOM 1773 CB LEU A 236 6.595 22.373 -26.412 1.00 70.92 C ANISOU 1773 CB LEU A 236 10523 7581 8842 -837 1708 -658 C ATOM 1774 CG LEU A 236 5.644 22.499 -27.597 1.00 71.15 C ANISOU 1774 CG LEU A 236 10580 7549 8907 -817 1651 -629 C ATOM 1775 CD1 LEU A 236 4.266 22.921 -27.132 1.00 71.45 C ANISOU 1775 CD1 LEU A 236 10507 7591 9051 -906 1659 -612 C ATOM 1776 CD2 LEU A 236 6.179 23.494 -28.601 1.00 71.07 C ANISOU 1776 CD2 LEU A 236 10568 7539 8896 -747 1704 -633 C ATOM 1777 N ILE A 237 6.847 19.260 -25.720 1.00 72.24 N ANISOU 1777 N ILE A 237 10883 7618 8948 -882 1423 -565 N ATOM 1778 CA ILE A 237 6.691 17.854 -26.081 1.00 73.13 C ANISOU 1778 CA ILE A 237 11104 7597 9083 -869 1267 -536 C ATOM 1779 C ILE A 237 5.666 17.193 -25.175 1.00 73.76 C ANISOU 1779 C ILE A 237 11193 7675 9157 -1037 1180 -434 C ATOM 1780 O ILE A 237 4.709 16.570 -25.642 1.00 74.25 O ANISOU 1780 O ILE A 237 11307 7664 9239 -1084 1096 -413 O ATOM 1781 CB ILE A 237 8.045 17.129 -26.009 1.00 73.79 C ANISOU 1781 CB ILE A 237 11220 7603 9213 -764 1204 -555 C ATOM 1782 CG1 ILE A 237 9.007 17.666 -27.064 1.00 73.53 C ANISOU 1782 CG1 ILE A 237 11174 7584 9180 -612 1309 -680 C ATOM 1783 CG2 ILE A 237 7.852 15.642 -26.168 1.00 75.09 C ANISOU 1783 CG2 ILE A 237 11485 7594 9453 -761 1028 -525 C ATOM 1784 CD1 ILE A 237 10.429 17.199 -26.867 1.00 74.31 C ANISOU 1784 CD1 ILE A 237 11240 7635 9361 -503 1284 -721 C ATOM 1785 N ASN A 238 5.850 17.329 -23.859 1.00 74.00 N ANISOU 1785 N ASN A 238 11172 7802 9141 -1158 1198 -368 N ATOM 1786 CA ASN A 238 4.936 16.687 -22.921 1.00 78.12 C ANISOU 1786 CA ASN A 238 11705 8356 9621 -1362 1128 -261 C ATOM 1787 C ASN A 238 3.504 17.137 -23.156 1.00 76.37 C ANISOU 1787 C ASN A 238 11415 8190 9413 -1447 1207 -297 C ATOM 1788 O ASN A 238 2.571 16.327 -23.081 1.00 79.59 O ANISOU 1788 O ASN A 238 11857 8555 9830 -1565 1116 -228 O ATOM 1789 CB ASN A 238 5.366 16.975 -21.485 1.00 87.14 C ANISOU 1789 CB ASN A 238 12800 9649 10660 -1516 1165 -200 C ATOM 1790 CG ASN A 238 6.714 16.369 -21.150 1.00 93.49 C ANISOU 1790 CG ASN A 238 13657 10384 11480 -1454 1029 -121 C ATOM 1791 OD1 ASN A 238 7.121 15.367 -21.739 1.00 94.69 O ANISOU 1791 OD1 ASN A 238 13888 10349 11741 -1341 874 -85 O ATOM 1792 ND2 ASN A 238 7.417 16.976 -20.200 1.00 93.78 N ANISOU 1792 ND2 ASN A 238 13639 10566 11429 -1530 1080 -107 N ATOM 1793 N TYR A 239 3.306 18.419 -23.467 1.00 73.96 N ANISOU 1793 N TYR A 239 11001 7962 9139 -1388 1363 -398 N ATOM 1794 CA TYR A 239 1.952 18.870 -23.771 1.00 74.14 C ANISOU 1794 CA TYR A 239 10926 8008 9236 -1442 1416 -432 C ATOM 1795 C TYR A 239 1.411 18.183 -25.014 1.00 74.31 C ANISOU 1795 C TYR A 239 11031 7894 9310 -1375 1275 -403 C ATOM 1796 O TYR A 239 0.257 17.737 -25.034 1.00 75.11 O ANISOU 1796 O TYR A 239 11102 7984 9451 -1482 1218 -367 O ATOM 1797 CB TYR A 239 1.913 20.383 -23.949 1.00 73.52 C ANISOU 1797 CB TYR A 239 10709 7987 9237 -1370 1576 -535 C ATOM 1798 CG TYR A 239 0.583 20.886 -24.455 1.00 73.98 C ANISOU 1798 CG TYR A 239 10644 8026 9438 -1383 1594 -561 C ATOM 1799 CD1 TYR A 239 -0.532 20.899 -23.632 1.00 75.05 C ANISOU 1799 CD1 TYR A 239 10645 8247 9624 -1542 1665 -591 C ATOM 1800 CD2 TYR A 239 0.442 21.345 -25.755 1.00 73.67 C ANISOU 1800 CD2 TYR A 239 10612 7894 9486 -1251 1532 -550 C ATOM 1801 CE1 TYR A 239 -1.748 21.357 -24.086 1.00 75.77 C ANISOU 1801 CE1 TYR A 239 10585 8310 9895 -1542 1672 -619 C ATOM 1802 CE2 TYR A 239 -0.770 21.805 -26.218 1.00 74.41 C ANISOU 1802 CE2 TYR A 239 10576 7957 9739 -1264 1508 -546 C ATOM 1803 CZ TYR A 239 -1.860 21.809 -25.378 1.00 75.44 C ANISOU 1803 CZ TYR A 239 10547 8153 9963 -1396 1576 -586 C ATOM 1804 OH TYR A 239 -3.072 22.265 -25.830 1.00 79.65 O ANISOU 1804 OH TYR A 239 10914 8645 10702 -1397 1544 -588 O ATOM 1805 N LEU A 240 2.230 18.079 -26.060 1.00 73.82 N ANISOU 1805 N LEU A 240 11069 7743 9237 -1217 1223 -431 N ATOM 1806 CA LEU A 240 1.754 17.461 -27.293 1.00 74.28 C ANISOU 1806 CA LEU A 240 11219 7693 9310 -1176 1097 -432 C ATOM 1807 C LEU A 240 1.415 15.993 -27.083 1.00 75.34 C ANISOU 1807 C LEU A 240 11456 7725 9443 -1265 945 -377 C ATOM 1808 O LEU A 240 0.424 15.496 -27.628 1.00 76.07 O ANISOU 1808 O LEU A 240 11574 7764 9566 -1330 844 -357 O ATOM 1809 CB LEU A 240 2.797 17.621 -28.393 1.00 73.94 C ANISOU 1809 CB LEU A 240 11265 7608 9220 -1021 1104 -503 C ATOM 1810 CG LEU A 240 3.071 19.062 -28.814 1.00 73.19 C ANISOU 1810 CG LEU A 240 11087 7594 9129 -953 1226 -530 C ATOM 1811 CD1 LEU A 240 4.189 19.111 -29.830 1.00 73.19 C ANISOU 1811 CD1 LEU A 240 11180 7579 9048 -837 1249 -597 C ATOM 1812 CD2 LEU A 240 1.815 19.689 -29.378 1.00 73.55 C ANISOU 1812 CD2 LEU A 240 11056 7647 9242 -1001 1189 -486 C ATOM 1813 N VAL A 241 2.228 15.284 -26.300 1.00 75.67 N ANISOU 1813 N VAL A 241 11556 7725 9469 -1277 904 -337 N ATOM 1814 CA VAL A 241 1.962 13.880 -26.017 1.00 77.00 C ANISOU 1814 CA VAL A 241 11825 7763 9669 -1371 735 -257 C ATOM 1815 C VAL A 241 0.677 13.732 -25.218 1.00 77.70 C ANISOU 1815 C VAL A 241 11844 7929 9748 -1592 725 -160 C ATOM 1816 O VAL A 241 -0.156 12.868 -25.510 1.00 78.75 O ANISOU 1816 O VAL A 241 12031 7969 9921 -1685 600 -116 O ATOM 1817 CB VAL A 241 3.154 13.248 -25.280 1.00 77.54 C ANISOU 1817 CB VAL A 241 11947 7759 9756 -1339 667 -202 C ATOM 1818 CG1 VAL A 241 2.817 11.842 -24.863 1.00 79.26 C ANISOU 1818 CG1 VAL A 241 12260 7819 10035 -1462 469 -81 C ATOM 1819 CG2 VAL A 241 4.381 13.248 -26.160 1.00 77.29 C ANISOU 1819 CG2 VAL A 241 11959 7638 9770 -1120 680 -327 C ATOM 1820 N GLU A 242 0.497 14.565 -24.193 1.00 77.38 N ANISOU 1820 N GLU A 242 11678 8068 9655 -1693 869 -142 N ATOM 1821 CA GLU A 242 -0.712 14.465 -23.386 1.00 83.42 C ANISOU 1821 CA GLU A 242 12352 8940 10401 -1923 901 -82 C ATOM 1822 C GLU A 242 -1.952 14.750 -24.219 1.00 78.51 C ANISOU 1822 C GLU A 242 11641 8314 9874 -1925 908 -134 C ATOM 1823 O GLU A 242 -2.976 14.072 -24.071 1.00 82.64 O ANISOU 1823 O GLU A 242 12148 8829 10425 -2089 836 -71 O ATOM 1824 CB GLU A 242 -0.628 15.411 -22.190 1.00106.12 C ANISOU 1824 CB GLU A 242 15098 12028 13195 -2032 1091 -112 C ATOM 1825 CG GLU A 242 0.403 14.991 -21.155 1.00129.87 C ANISOU 1825 CG GLU A 242 18190 15071 16082 -2112 1045 -15 C ATOM 1826 CD GLU A 242 0.268 13.531 -20.756 1.00149.94 C ANISOU 1826 CD GLU A 242 20863 17507 18600 -2270 836 167 C ATOM 1827 OE1 GLU A 242 -0.875 13.067 -20.553 1.00157.27 O ANISOU 1827 OE1 GLU A 242 21765 18465 19524 -2459 817 222 O ATOM 1828 OE2 GLU A 242 1.306 12.845 -20.652 1.00156.41 O ANISOU 1828 OE2 GLU A 242 21799 18198 19430 -2206 681 260 O ATOM 1829 N GLU A 243 -1.877 15.735 -25.114 1.00 77.48 N ANISOU 1829 N GLU A 243 11450 8186 9802 -1758 973 -229 N ATOM 1830 CA GLU A 243 -3.028 16.023 -25.958 1.00 77.89 C ANISOU 1830 CA GLU A 243 11411 8223 9960 -1760 934 -248 C ATOM 1831 C GLU A 243 -3.270 14.912 -26.970 1.00 78.56 C ANISOU 1831 C GLU A 243 11651 8157 10044 -1755 729 -213 C ATOM 1832 O GLU A 243 -4.425 14.604 -27.280 1.00 79.60 O ANISOU 1832 O GLU A 243 11724 8276 10244 -1859 645 -183 O ATOM 1833 CB GLU A 243 -2.847 17.369 -26.656 1.00 76.98 C ANISOU 1833 CB GLU A 243 11203 8134 9913 -1601 1020 -320 C ATOM 1834 CG GLU A 243 -3.178 18.562 -25.776 1.00 84.76 C ANISOU 1834 CG GLU A 243 11971 9246 10986 -1635 1215 -386 C ATOM 1835 CD GLU A 243 -4.628 18.568 -25.339 1.00 95.19 C ANISOU 1835 CD GLU A 243 13101 10631 12436 -1787 1246 -393 C ATOM 1836 OE1 GLU A 243 -5.487 18.146 -26.140 1.00100.49 O ANISOU 1836 OE1 GLU A 243 13762 11234 13187 -1806 1100 -342 O ATOM 1837 OE2 GLU A 243 -4.908 18.983 -24.194 1.00 95.69 O ANISOU 1837 OE2 GLU A 243 13018 10825 12515 -1902 1421 -463 O ATOM 1838 N PHE A 244 -2.207 14.287 -27.479 1.00 78.27 N ANISOU 1838 N PHE A 244 11796 8003 9942 -1644 651 -236 N ATOM 1839 CA PHE A 244 -2.392 13.222 -28.461 1.00 79.24 C ANISOU 1839 CA PHE A 244 12070 7972 10067 -1644 473 -250 C ATOM 1840 C PHE A 244 -2.981 11.976 -27.815 1.00 80.66 C ANISOU 1840 C PHE A 244 12299 8065 10282 -1822 349 -159 C ATOM 1841 O PHE A 244 -3.893 11.354 -28.367 1.00 81.80 O ANISOU 1841 O PHE A 244 12472 8141 10467 -1917 219 -146 O ATOM 1842 CB PHE A 244 -1.072 12.888 -29.152 1.00 78.98 C ANISOU 1842 CB PHE A 244 12191 7834 9983 -1476 454 -344 C ATOM 1843 CG PHE A 244 -1.220 11.932 -30.306 1.00 80.23 C ANISOU 1843 CG PHE A 244 12502 7847 10135 -1469 304 -422 C ATOM 1844 CD1 PHE A 244 -1.115 10.567 -30.117 1.00 81.59 C ANISOU 1844 CD1 PHE A 244 12793 7836 10371 -1520 169 -421 C ATOM 1845 CD2 PHE A 244 -1.466 12.403 -31.583 1.00 80.37 C ANISOU 1845 CD2 PHE A 244 12549 7906 10082 -1430 287 -497 C ATOM 1846 CE1 PHE A 244 -1.250 9.697 -31.179 1.00 83.01 C ANISOU 1846 CE1 PHE A 244 13113 7872 10556 -1520 42 -532 C ATOM 1847 CE2 PHE A 244 -1.600 11.534 -32.644 1.00 81.82 C ANISOU 1847 CE2 PHE A 244 12882 7980 10226 -1452 159 -596 C ATOM 1848 CZ PHE A 244 -1.492 10.182 -32.442 1.00 83.12 C ANISOU 1848 CZ PHE A 244 13159 7958 10466 -1492 48 -634 C ATOM 1849 N LYS A 245 -2.459 11.583 -26.653 1.00 82.76 N ANISOU 1849 N LYS A 245 12582 8333 10529 -1889 368 -80 N ATOM 1850 CA LYS A 245 -3.063 10.484 -25.909 1.00 86.73 C ANISOU 1850 CA LYS A 245 13126 8772 11058 -2103 248 50 C ATOM 1851 C LYS A 245 -4.483 10.826 -25.483 1.00 87.74 C ANISOU 1851 C LYS A 245 13086 9053 11197 -2302 312 96 C ATOM 1852 O LYS A 245 -5.326 9.935 -25.341 1.00 86.02 O ANISOU 1852 O LYS A 245 12889 8777 11015 -2488 195 181 O ATOM 1853 CB LYS A 245 -2.204 10.145 -24.690 1.00 92.86 C ANISOU 1853 CB LYS A 245 13944 9550 11787 -2163 246 161 C ATOM 1854 CG LYS A 245 -2.564 8.835 -24.018 1.00103.31 C ANISOU 1854 CG LYS A 245 15360 10753 13141 -2379 67 332 C ATOM 1855 CD LYS A 245 -1.932 8.707 -22.643 1.00108.94 C ANISOU 1855 CD LYS A 245 16084 11538 13770 -2508 65 490 C ATOM 1856 CE LYS A 245 -2.072 7.284 -22.125 1.00111.75 C ANISOU 1856 CE LYS A 245 16569 11709 14184 -2702 -172 694 C ATOM 1857 NZ LYS A 245 -3.441 6.739 -22.369 1.00111.82 N ANISOU 1857 NZ LYS A 245 16564 11697 14225 -2898 -227 731 N ATOM 1858 N LYS A 246 -4.766 12.113 -25.290 1.00 90.51 N ANISOU 1858 N LYS A 246 13256 9590 11545 -2267 497 30 N ATOM 1859 CA LYS A 246 -6.093 12.535 -24.861 1.00 94.82 C ANISOU 1859 CA LYS A 246 13593 10285 12149 -2436 588 35 C ATOM 1860 C LYS A 246 -7.105 12.439 -25.996 1.00104.63 C ANISOU 1860 C LYS A 246 14786 11461 13507 -2423 468 12 C ATOM 1861 O LYS A 246 -8.260 12.061 -25.773 1.00110.15 O ANISOU 1861 O LYS A 246 15377 12202 14273 -2611 434 58 O ATOM 1862 CB LYS A 246 -6.013 13.961 -24.320 1.00 89.76 C ANISOU 1862 CB LYS A 246 12759 9825 11519 -2380 823 -61 C ATOM 1863 CG LYS A 246 -7.272 14.503 -23.675 1.00 86.32 C ANISOU 1863 CG LYS A 246 12065 9560 11173 -2547 971 -104 C ATOM 1864 CD LYS A 246 -6.921 15.735 -22.851 1.00 85.41 C ANISOU 1864 CD LYS A 246 11798 9608 11046 -2517 1220 -222 C ATOM 1865 CE LYS A 246 -8.133 16.592 -22.531 1.00 90.02 C ANISOU 1865 CE LYS A 246 12074 10326 11805 -2595 1393 -341 C ATOM 1866 NZ LYS A 246 -7.749 17.749 -21.674 1.00 91.46 N ANISOU 1866 NZ LYS A 246 12118 10652 11982 -2578 1647 -494 N ATOM 1867 N ASP A 247 -6.691 12.771 -27.218 1.00 90.73 N ANISOU 1867 N ASP A 247 13103 9614 11758 -2228 396 -53 N ATOM 1868 CA ASP A 247 -7.619 12.848 -28.341 1.00 93.90 C ANISOU 1868 CA ASP A 247 13454 9980 12245 -2225 268 -64 C ATOM 1869 C ASP A 247 -7.679 11.566 -29.161 1.00 89.92 C ANISOU 1869 C ASP A 247 13156 9306 11703 -2274 48 -52 C ATOM 1870 O ASP A 247 -8.738 11.240 -29.710 1.00 92.97 O ANISOU 1870 O ASP A 247 13493 9674 12158 -2384 -86 -28 O ATOM 1871 CB ASP A 247 -7.250 14.010 -29.263 1.00103.68 C ANISOU 1871 CB ASP A 247 14657 11242 13496 -2031 299 -123 C ATOM 1872 CG ASP A 247 -7.483 15.367 -28.616 1.00110.86 C ANISOU 1872 CG ASP A 247 15321 12284 14517 -1989 489 -149 C ATOM 1873 OD1 ASP A 247 -8.336 15.470 -27.715 1.00112.05 O ANISOU 1873 OD1 ASP A 247 15277 12528 14768 -2125 582 -146 O ATOM 1874 OD2 ASP A 247 -6.806 16.337 -29.030 1.00113.93 O ANISOU 1874 OD2 ASP A 247 15707 12681 14900 -1829 551 -186 O ATOM 1875 N GLN A 248 -6.568 10.835 -29.271 1.00 84.26 N ANISOU 1875 N GLN A 248 12656 8456 10901 -2195 3 -85 N ATOM 1876 CA GLN A 248 -6.497 9.635 -30.094 1.00 85.50 C ANISOU 1876 CA GLN A 248 13015 8424 11048 -2219 -188 -126 C ATOM 1877 C GLN A 248 -6.309 8.350 -29.302 1.00 86.66 C ANISOU 1877 C GLN A 248 13275 8418 11234 -2340 -277 -54 C ATOM 1878 O GLN A 248 -6.393 7.268 -29.895 1.00 88.12 O ANISOU 1878 O GLN A 248 13613 8413 11456 -2385 -447 -93 O ATOM 1879 CB GLN A 248 -5.353 9.755 -31.114 1.00 84.86 C ANISOU 1879 CB GLN A 248 13092 8274 10877 -2018 -184 -266 C ATOM 1880 CG GLN A 248 -5.431 10.985 -32.000 1.00 88.13 C ANISOU 1880 CG GLN A 248 13431 8825 11230 -1919 -126 -308 C ATOM 1881 CD GLN A 248 -6.355 10.798 -33.184 1.00103.90 C ANISOU 1881 CD GLN A 248 15461 10814 13205 -2008 -298 -325 C ATOM 1882 OE1 GLN A 248 -7.575 10.903 -33.059 1.00113.63 O ANISOU 1882 OE1 GLN A 248 16548 12097 14530 -2140 -374 -235 O ATOM 1883 NE2 GLN A 248 -5.776 10.514 -34.345 1.00108.26 N ANISOU 1883 NE2 GLN A 248 16193 11312 13627 -1950 -358 -452 N ATOM 1884 N GLY A 249 -6.040 8.430 -28.000 1.00 87.12 N ANISOU 1884 N GLY A 249 13272 8544 11286 -2406 -180 52 N ATOM 1885 CA GLY A 249 -5.932 7.240 -27.180 1.00 87.83 C ANISOU 1885 CA GLY A 249 13465 8494 11414 -2560 -296 176 C ATOM 1886 C GLY A 249 -4.619 6.501 -27.267 1.00 88.07 C ANISOU 1886 C GLY A 249 13678 8302 11481 -2416 -386 146 C ATOM 1887 O GLY A 249 -4.555 5.335 -26.869 1.00 89.83 O ANISOU 1887 O GLY A 249 14012 8328 11791 -2527 -550 246 O ATOM 1888 N ILE A 250 -3.564 7.140 -27.761 1.00 86.61 N ANISOU 1888 N ILE A 250 13514 8135 11259 -2177 -289 14 N ATOM 1889 CA ILE A 250 -2.266 6.504 -27.950 1.00 88.49 C ANISOU 1889 CA ILE A 250 13886 8166 11570 -2010 -355 -57 C ATOM 1890 C ILE A 250 -1.224 7.273 -27.151 1.00 92.07 C ANISOU 1890 C ILE A 250 14270 8742 11971 -1902 -219 -17 C ATOM 1891 O ILE A 250 -1.059 8.484 -27.341 1.00 83.96 O ANISOU 1891 O ILE A 250 13143 7912 10845 -1805 -44 -88 O ATOM 1892 CB ILE A 250 -1.870 6.451 -29.432 1.00 87.12 C ANISOU 1892 CB ILE A 250 13805 7899 11396 -1833 -360 -292 C ATOM 1893 CG1 ILE A 250 -2.806 5.524 -30.207 1.00 92.13 C ANISOU 1893 CG1 ILE A 250 14536 8386 12084 -1958 -527 -345 C ATOM 1894 CG2 ILE A 250 -0.423 6.012 -29.574 1.00 87.55 C ANISOU 1894 CG2 ILE A 250 13941 7781 11545 -1633 -366 -407 C ATOM 1895 CD1 ILE A 250 -2.433 5.362 -31.662 1.00 93.32 C ANISOU 1895 CD1 ILE A 250 14800 8457 12200 -1831 -535 -599 C ATOM 1896 N ASP A 251 -0.516 6.572 -26.267 1.00105.63 N ANISOU 1896 N ASP A 251 16037 10330 13767 -1928 -321 107 N ATOM 1897 CA ASP A 251 0.673 7.130 -25.631 1.00 99.23 C ANISOU 1897 CA ASP A 251 15179 9593 12930 -1808 -238 130 C ATOM 1898 C ASP A 251 1.801 7.094 -26.650 1.00 85.55 C ANISOU 1898 C ASP A 251 13492 7727 11286 -1535 -215 -81 C ATOM 1899 O ASP A 251 2.300 6.020 -26.998 1.00 87.71 O ANISOU 1899 O ASP A 251 13861 7728 11738 -1457 -366 -136 O ATOM 1900 CB ASP A 251 1.048 6.353 -24.372 1.00104.39 C ANISOU 1900 CB ASP A 251 15869 10151 13643 -1947 -396 362 C ATOM 1901 CG ASP A 251 2.198 6.993 -23.604 1.00104.33 C ANISOU 1901 CG ASP A 251 15798 10258 13587 -1863 -326 409 C ATOM 1902 OD1 ASP A 251 3.154 7.488 -24.237 1.00106.95 O ANISOU 1902 OD1 ASP A 251 16100 10579 13956 -1621 -234 240 O ATOM 1903 OD2 ASP A 251 2.148 7.005 -22.358 1.00102.69 O ANISOU 1903 OD2 ASP A 251 15567 10164 13286 -2063 -363 617 O ATOM 1904 N LEU A 252 2.211 8.266 -27.117 1.00 83.69 N ANISOU 1904 N LEU A 252 13181 7677 10940 -1398 -21 -209 N ATOM 1905 CA LEU A 252 3.209 8.369 -28.170 1.00 83.59 C ANISOU 1905 CA LEU A 252 13198 7595 10967 -1171 45 -427 C ATOM 1906 C LEU A 252 4.638 8.203 -27.661 1.00 84.01 C ANISOU 1906 C LEU A 252 13218 7564 11138 -1025 34 -429 C ATOM 1907 O LEU A 252 5.564 8.178 -28.476 1.00 84.36 O ANISOU 1907 O LEU A 252 13266 7541 11245 -837 97 -627 O ATOM 1908 CB LEU A 252 3.061 9.718 -28.883 1.00 81.73 C ANISOU 1908 CB LEU A 252 12896 7594 10563 -1113 241 -529 C ATOM 1909 CG LEU A 252 3.315 9.780 -30.390 1.00 82.07 C ANISOU 1909 CG LEU A 252 13008 7616 10558 -996 295 -752 C ATOM 1910 CD1 LEU A 252 2.455 8.767 -31.111 1.00 83.73 C ANISOU 1910 CD1 LEU A 252 13337 7674 10804 -1087 148 -814 C ATOM 1911 CD2 LEU A 252 3.036 11.172 -30.929 1.00 80.48 C ANISOU 1911 CD2 LEU A 252 12739 7648 10191 -990 447 -769 C ATOM 1912 N ARG A 253 4.848 8.075 -26.348 1.00100.05 N ANISOU 1912 N ARG A 253 15210 9608 13197 -1122 -48 -216 N ATOM 1913 CA ARG A 253 6.208 8.073 -25.814 1.00104.10 C ANISOU 1913 CA ARG A 253 15664 10072 13816 -994 -73 -192 C ATOM 1914 C ARG A 253 6.950 6.767 -26.060 1.00105.71 C ANISOU 1914 C ARG A 253 15918 9937 14309 -868 -265 -240 C ATOM 1915 O ARG A 253 8.139 6.686 -25.739 1.00105.91 O ANISOU 1915 O ARG A 253 15871 9889 14481 -732 -305 -241 O ATOM 1916 CB ARG A 253 6.182 8.384 -24.315 1.00101.49 C ANISOU 1916 CB ARG A 253 15283 9888 13392 -1173 -117 63 C ATOM 1917 CG ARG A 253 5.551 9.723 -23.997 1.00 93.94 C ANISOU 1917 CG ARG A 253 14249 9252 12193 -1281 96 65 C ATOM 1918 CD ARG A 253 5.497 10.024 -22.512 1.00 95.71 C ANISOU 1918 CD ARG A 253 14428 9646 12291 -1491 79 272 C ATOM 1919 NE ARG A 253 5.045 11.394 -22.286 1.00109.67 N ANISOU 1919 NE ARG A 253 16098 11699 13873 -1553 316 204 N ATOM 1920 CZ ARG A 253 4.815 11.926 -21.091 1.00122.31 C ANISOU 1920 CZ ARG A 253 17642 13512 15317 -1756 380 309 C ATOM 1921 NH1 ARG A 253 4.991 11.201 -19.996 1.00143.06 N ANISOU 1921 NH1 ARG A 253 20319 16129 17909 -1945 212 521 N ATOM 1922 NH2 ARG A 253 4.406 13.185 -20.993 1.00109.97 N ANISOU 1922 NH2 ARG A 253 15975 12170 13638 -1785 607 198 N ATOM 1923 N ASN A 254 6.291 5.757 -26.622 1.00107.63 N ANISOU 1923 N ASN A 254 16268 9961 14665 -908 -391 -292 N ATOM 1924 CA ASN A 254 6.940 4.482 -26.898 1.00109.60 C ANISOU 1924 CA ASN A 254 16558 9843 15240 -783 -576 -371 C ATOM 1925 C ASN A 254 7.683 4.490 -28.227 1.00120.15 C ANISOU 1925 C ASN A 254 17878 11110 16665 -543 -429 -737 C ATOM 1926 O ASN A 254 8.817 4.005 -28.304 1.00126.69 O ANISOU 1926 O ASN A 254 18638 11742 17758 -354 -474 -850 O ATOM 1927 CB ASN A 254 5.909 3.354 -26.880 1.00 99.82 C ANISOU 1927 CB ASN A 254 15447 8378 14102 -952 -782 -276 C ATOM 1928 CG ASN A 254 5.071 3.363 -25.622 1.00101.73 C ANISOU 1928 CG ASN A 254 15707 8733 14214 -1235 -895 74 C ATOM 1929 OD1 ASN A 254 5.505 3.845 -24.577 1.00103.13 O ANISOU 1929 OD1 ASN A 254 15814 9058 14312 -1294 -900 271 O ATOM 1930 ND2 ASN A 254 3.858 2.831 -25.716 1.00103.12 N ANISOU 1930 ND2 ASN A 254 15971 8856 14352 -1433 -980 144 N ATOM 1931 N ASP A 255 7.063 5.023 -29.270 1.00108.61 N ANISOU 1931 N ASP A 255 16467 9813 14989 -563 -258 -923 N ATOM 1932 CA ASP A 255 7.657 5.114 -30.599 1.00104.31 C ANISOU 1932 CA ASP A 255 15925 9267 14442 -396 -92 -1275 C ATOM 1933 C ASP A 255 8.826 6.090 -30.587 1.00 94.25 C ANISOU 1933 C ASP A 255 14514 8181 13115 -242 101 -1348 C ATOM 1934 O ASP A 255 8.596 7.305 -30.545 1.00 94.05 O ANISOU 1934 O ASP A 255 14453 8451 12830 -300 252 -1274 O ATOM 1935 CB ASP A 255 6.589 5.563 -31.605 1.00104.21 C ANISOU 1935 CB ASP A 255 16009 9430 14155 -515 8 -1378 C ATOM 1936 CG ASP A 255 7.043 5.440 -33.053 1.00112.07 C ANISOU 1936 CG ASP A 255 17053 10418 15110 -409 150 -1746 C ATOM 1937 OD1 ASP A 255 8.261 5.384 -33.316 1.00119.15 O ANISOU 1937 OD1 ASP A 255 17871 11266 16137 -229 257 -1944 O ATOM 1938 OD2 ASP A 255 6.163 5.413 -33.940 1.00110.48 O ANISOU 1938 OD2 ASP A 255 16962 10280 14735 -526 157 -1843 O ATOM 1939 N PRO A 256 10.079 5.627 -30.632 1.00 92.07 N ANISOU 1939 N PRO A 256 14143 7736 13102 -48 100 -1496 N ATOM 1940 CA PRO A 256 11.196 6.583 -30.580 1.00 91.04 C ANISOU 1940 CA PRO A 256 13865 7801 12925 80 283 -1554 C ATOM 1941 C PRO A 256 11.315 7.430 -31.834 1.00 96.42 C ANISOU 1941 C PRO A 256 14558 8723 13356 107 557 -1809 C ATOM 1942 O PRO A 256 11.687 8.609 -31.748 1.00107.11 O ANISOU 1942 O PRO A 256 15834 10337 14528 108 718 -1760 O ATOM 1943 CB PRO A 256 12.415 5.676 -30.377 1.00 93.89 C ANISOU 1943 CB PRO A 256 14105 7876 13693 279 182 -1663 C ATOM 1944 CG PRO A 256 12.030 4.399 -30.999 1.00 96.57 C ANISOU 1944 CG PRO A 256 14546 7901 14245 301 65 -1843 C ATOM 1945 CD PRO A 256 10.548 4.241 -30.795 1.00 95.43 C ANISOU 1945 CD PRO A 256 14574 7777 13909 71 -60 -1641 C ATOM 1946 N LEU A 257 11.017 6.858 -33.001 1.00114.34 N ANISOU 1946 N LEU A 257 16930 10913 15602 108 606 -2078 N ATOM 1947 CA LEU A 257 10.994 7.643 -34.230 1.00103.78 C ANISOU 1947 CA LEU A 257 15635 9829 13967 74 841 -2286 C ATOM 1948 C LEU A 257 9.990 8.785 -34.118 1.00 90.23 C ANISOU 1948 C LEU A 257 13975 8380 11928 -97 866 -2047 C ATOM 1949 O LEU A 257 10.311 9.949 -34.400 1.00 92.66 O ANISOU 1949 O LEU A 257 14232 8940 12034 -106 1038 -2036 O ATOM 1950 CB LEU A 257 10.663 6.728 -35.411 1.00108.74 C ANISOU 1950 CB LEU A 257 16393 10327 14597 50 850 -2595 C ATOM 1951 CG LEU A 257 10.679 7.252 -36.848 1.00112.55 C ANISOU 1951 CG LEU A 257 16951 11050 14764 -19 1073 -2861 C ATOM 1952 CD1 LEU A 257 11.023 6.121 -37.804 1.00118.55 C ANISOU 1952 CD1 LEU A 257 17765 11621 15658 35 1122 -3274 C ATOM 1953 CD2 LEU A 257 9.340 7.863 -37.231 1.00110.93 C ANISOU 1953 CD2 LEU A 257 16889 11035 14226 -234 1017 -2685 C ATOM 1954 N ALA A 258 8.769 8.466 -33.685 1.00 87.88 N ANISOU 1954 N ALA A 258 13765 8016 11608 -237 690 -1853 N ATOM 1955 CA ALA A 258 7.749 9.493 -33.515 1.00 85.53 C ANISOU 1955 CA ALA A 258 13485 7941 11072 -388 702 -1638 C ATOM 1956 C ALA A 258 8.201 10.562 -32.533 1.00 83.42 C ANISOU 1956 C ALA A 258 13084 7832 10778 -362 779 -1449 C ATOM 1957 O ALA A 258 7.905 11.747 -32.716 1.00 81.77 O ANISOU 1957 O ALA A 258 12847 7842 10380 -418 888 -1378 O ATOM 1958 CB ALA A 258 6.439 8.863 -33.048 1.00 85.58 C ANISOU 1958 CB ALA A 258 13566 7835 11114 -539 503 -1467 C ATOM 1959 N MET A 259 8.919 10.165 -31.482 1.00 83.70 N ANISOU 1959 N MET A 259 13037 7751 11015 -287 706 -1362 N ATOM 1960 CA MET A 259 9.396 11.147 -30.515 1.00 81.99 C ANISOU 1960 CA MET A 259 12699 7692 10762 -283 772 -1201 C ATOM 1961 C MET A 259 10.463 12.043 -31.124 1.00 81.62 C ANISOU 1961 C MET A 259 12569 7801 10643 -172 981 -1351 C ATOM 1962 O MET A 259 10.558 13.227 -30.782 1.00 89.53 O ANISOU 1962 O MET A 259 13500 8995 11521 -207 1087 -1254 O ATOM 1963 CB MET A 259 9.931 10.446 -29.270 1.00 82.84 C ANISOU 1963 CB MET A 259 12748 7645 11084 -258 610 -1054 C ATOM 1964 CG MET A 259 8.854 9.808 -28.410 1.00 85.79 C ANISOU 1964 CG MET A 259 13193 7927 11478 -428 416 -834 C ATOM 1965 SD MET A 259 7.599 10.979 -27.859 1.00 84.07 S ANISOU 1965 SD MET A 259 12961 7979 11003 -631 501 -659 S ATOM 1966 CE MET A 259 8.530 11.944 -26.677 1.00 94.74 C ANISOU 1966 CE MET A 259 14178 9502 12317 -625 579 -544 C ATOM 1967 N GLN A 260 11.281 11.496 -32.024 1.00 83.49 N ANISOU 1967 N GLN A 260 12803 7955 10963 -49 1052 -1602 N ATOM 1968 CA GLN A 260 12.249 12.328 -32.729 1.00 83.49 C ANISOU 1968 CA GLN A 260 12725 8130 10867 24 1273 -1760 C ATOM 1969 C GLN A 260 11.544 13.366 -33.591 1.00 82.30 C ANISOU 1969 C GLN A 260 12654 8199 10415 -101 1390 -1744 C ATOM 1970 O GLN A 260 11.816 14.573 -33.487 1.00 80.89 O ANISOU 1970 O GLN A 260 12410 8206 10119 -127 1507 -1658 O ATOM 1971 CB GLN A 260 13.173 11.458 -33.581 1.00 87.55 C ANISOU 1971 CB GLN A 260 13213 8523 11530 159 1349 -2074 C ATOM 1972 CG GLN A 260 14.259 10.728 -32.805 1.00103.94 C ANISOU 1972 CG GLN A 260 15138 10401 13954 326 1267 -2104 C ATOM 1973 CD GLN A 260 15.315 10.134 -33.717 1.00117.06 C ANISOU 1973 CD GLN A 260 16715 11983 15781 477 1410 -2464 C ATOM 1974 OE1 GLN A 260 15.052 9.855 -34.886 1.00108.98 O ANISOU 1974 OE1 GLN A 260 15792 10985 14631 442 1523 -2712 O ATOM 1975 NE2 GLN A 260 16.521 9.950 -33.190 1.00131.99 N ANISOU 1975 NE2 GLN A 260 18408 13789 17954 636 1409 -2508 N ATOM 1976 N ARG A 261 10.622 12.912 -34.449 1.00 93.76 N ANISOU 1976 N ARG A 261 14249 9621 11755 -190 1337 -1812 N ATOM 1977 CA ARG A 261 9.848 13.850 -35.256 1.00 88.13 C ANISOU 1977 CA ARG A 261 13612 9099 10773 -326 1389 -1752 C ATOM 1978 C ARG A 261 9.151 14.880 -34.382 1.00 80.84 C ANISOU 1978 C ARG A 261 12628 8264 9822 -396 1346 -1479 C ATOM 1979 O ARG A 261 9.023 16.049 -34.768 1.00 80.15 O ANISOU 1979 O ARG A 261 12524 8341 9586 -456 1430 -1403 O ATOM 1980 CB ARG A 261 8.819 13.097 -36.100 1.00 90.13 C ANISOU 1980 CB ARG A 261 14022 9288 10937 -431 1277 -1826 C ATOM 1981 CG ARG A 261 9.401 12.068 -37.057 1.00102.32 C ANISOU 1981 CG ARG A 261 15639 10744 12496 -384 1335 -2148 C ATOM 1982 CD ARG A 261 8.291 11.285 -37.741 1.00104.88 C ANISOU 1982 CD ARG A 261 16124 10988 12740 -511 1193 -2208 C ATOM 1983 NE ARG A 261 7.382 12.158 -38.474 1.00107.61 N ANISOU 1983 NE ARG A 261 16549 11536 12802 -683 1171 -2082 N ATOM 1984 CZ ARG A 261 6.240 11.756 -39.018 1.00108.48 C ANISOU 1984 CZ ARG A 261 16781 11623 12812 -828 1019 -2060 C ATOM 1985 NH1 ARG A 261 5.863 10.489 -38.906 1.00106.15 N ANISOU 1985 NH1 ARG A 261 16554 11111 12669 -827 892 -2169 N ATOM 1986 NH2 ARG A 261 5.473 12.620 -39.667 1.00109.52 N ANISOU 1986 NH2 ARG A 261 16962 11937 12712 -979 974 -1917 N ATOM 1987 N LEU A 262 8.729 14.471 -33.187 1.00 79.17 N ANISOU 1987 N LEU A 262 12378 7942 9763 -401 1221 -1336 N ATOM 1988 CA LEU A 262 7.970 15.346 -32.306 1.00 77.37 C ANISOU 1988 CA LEU A 262 12083 7796 9517 -485 1197 -1122 C ATOM 1989 C LEU A 262 8.849 16.386 -31.627 1.00 76.20 C ANISOU 1989 C LEU A 262 11809 7762 9381 -436 1323 -1072 C ATOM 1990 O LEU A 262 8.391 17.505 -31.377 1.00 74.98 O ANISOU 1990 O LEU A 262 11599 7719 9173 -498 1375 -966 O ATOM 1991 CB LEU A 262 7.232 14.516 -31.257 1.00 77.36 C ANISOU 1991 CB LEU A 262 12088 7671 9636 -548 1040 -1000 C ATOM 1992 CG LEU A 262 6.155 15.249 -30.464 1.00 76.07 C ANISOU 1992 CG LEU A 262 11859 7598 9445 -672 1025 -824 C ATOM 1993 CD1 LEU A 262 5.252 15.991 -31.417 1.00 75.84 C ANISOU 1993 CD1 LEU A 262 11847 7655 9312 -732 1043 -815 C ATOM 1994 CD2 LEU A 262 5.342 14.286 -29.620 1.00 76.60 C ANISOU 1994 CD2 LEU A 262 11951 7560 9594 -777 875 -718 C ATOM 1995 N LYS A 263 10.100 16.045 -31.307 1.00 77.45 N ANISOU 1995 N LYS A 263 11908 7882 9639 -326 1365 -1154 N ATOM 1996 CA LYS A 263 11.003 17.059 -30.770 1.00 75.90 C ANISOU 1996 CA LYS A 263 11590 7804 9443 -291 1484 -1121 C ATOM 1997 C LYS A 263 11.393 18.057 -31.847 1.00 76.86 C ANISOU 1997 C LYS A 263 11709 8067 9426 -291 1646 -1198 C ATOM 1998 O LYS A 263 11.441 19.267 -31.592 1.00 90.59 O ANISOU 1998 O LYS A 263 13383 9919 11118 -333 1727 -1112 O ATOM 1999 CB LYS A 263 12.253 16.414 -30.169 1.00 76.85 C ANISOU 1999 CB LYS A 263 11625 7846 9728 -178 1461 -1176 C ATOM 2000 CG LYS A 263 13.215 17.427 -29.543 1.00 76.11 C ANISOU 2000 CG LYS A 263 11396 7880 9641 -158 1564 -1139 C ATOM 2001 CD LYS A 263 14.591 16.847 -29.252 1.00 80.44 C ANISOU 2001 CD LYS A 263 11833 8363 10367 -30 1549 -1220 C ATOM 2002 CE LYS A 263 15.575 17.936 -28.839 1.00 80.24 C ANISOU 2002 CE LYS A 263 11671 8488 10330 -24 1666 -1204 C ATOM 2003 NZ LYS A 263 15.246 18.546 -27.518 1.00 75.90 N ANISOU 2003 NZ LYS A 263 11089 8004 9744 -137 1602 -1025 N ATOM 2004 N GLU A 264 11.676 17.567 -33.057 1.00 77.35 N ANISOU 2004 N GLU A 264 11846 8127 9418 -263 1695 -1363 N ATOM 2005 CA GLU A 264 11.958 18.478 -34.162 1.00 77.74 C ANISOU 2005 CA GLU A 264 11917 8335 9286 -314 1838 -1412 C ATOM 2006 C GLU A 264 10.806 19.454 -34.364 1.00 76.71 C ANISOU 2006 C GLU A 264 11832 8269 9044 -439 1788 -1232 C ATOM 2007 O GLU A 264 11.000 20.679 -34.370 1.00 85.95 O ANISOU 2007 O GLU A 264 12946 9540 10171 -479 1866 -1140 O ATOM 2008 CB GLU A 264 12.226 17.682 -35.441 1.00 79.91 C ANISOU 2008 CB GLU A 264 12288 8614 9460 -312 1892 -1633 C ATOM 2009 CG GLU A 264 12.518 18.533 -36.670 1.00 89.93 C ANISOU 2009 CG GLU A 264 13605 10078 10486 -414 2038 -1679 C ATOM 2010 CD GLU A 264 12.811 17.699 -37.910 1.00106.21 C ANISOU 2010 CD GLU A 264 15765 12176 12413 -442 2118 -1940 C ATOM 2011 OE1 GLU A 264 12.033 16.767 -38.208 1.00111.49 O ANISOU 2011 OE1 GLU A 264 16546 12738 13076 -466 1997 -2006 O ATOM 2012 OE2 GLU A 264 13.827 17.972 -38.585 1.00110.26 O ANISOU 2012 OE2 GLU A 264 16238 12831 12824 -454 2313 -2097 O ATOM 2013 N ALA A 265 9.588 18.924 -34.499 1.00 76.76 N ANISOU 2013 N ALA A 265 11925 8201 9039 -500 1643 -1178 N ATOM 2014 CA ALA A 265 8.426 19.781 -34.699 1.00 76.15 C ANISOU 2014 CA ALA A 265 11861 8164 8910 -607 1569 -1009 C ATOM 2015 C ALA A 265 8.218 20.716 -33.519 1.00 74.55 C ANISOU 2015 C ALA A 265 11524 7963 8840 -601 1588 -874 C ATOM 2016 O ALA A 265 7.802 21.867 -33.694 1.00 74.24 O ANISOU 2016 O ALA A 265 11439 7970 8798 -654 1599 -762 O ATOM 2017 CB ALA A 265 7.182 18.928 -34.920 1.00 76.66 C ANISOU 2017 CB ALA A 265 12011 8141 8975 -671 1402 -985 C ATOM 2018 N ALA A 266 8.512 20.240 -32.308 1.00 73.86 N ANISOU 2018 N ALA A 266 11369 7819 8874 -549 1585 -885 N ATOM 2019 CA ALA A 266 8.274 21.040 -31.112 1.00 72.68 C ANISOU 2019 CA ALA A 266 11100 7691 8822 -574 1614 -792 C ATOM 2020 C ALA A 266 9.198 22.246 -31.064 1.00 72.28 C ANISOU 2020 C ALA A 266 10969 7726 8767 -552 1751 -794 C ATOM 2021 O ALA A 266 8.740 23.380 -30.888 1.00 71.83 O ANISOU 2021 O ALA A 266 10842 7691 8757 -598 1784 -721 O ATOM 2022 CB ALA A 266 8.444 20.180 -29.862 1.00 72.47 C ANISOU 2022 CB ALA A 266 11045 7613 8878 -565 1563 -790 C ATOM 2023 N GLU A 267 10.508 22.026 -31.205 1.00 72.68 N ANISOU 2023 N GLU A 267 11010 7812 8793 -482 1831 -887 N ATOM 2024 CA GLU A 267 11.428 23.158 -31.221 1.00 72.50 C ANISOU 2024 CA GLU A 267 10908 7877 8764 -479 1962 -889 C ATOM 2025 C GLU A 267 11.109 24.105 -32.368 1.00 72.99 C ANISOU 2025 C GLU A 267 11013 7985 8733 -545 1995 -828 C ATOM 2026 O GLU A 267 11.152 25.333 -32.204 1.00 72.67 O ANISOU 2026 O GLU A 267 10906 7967 8739 -586 2047 -753 O ATOM 2027 CB GLU A 267 12.873 22.676 -31.318 1.00 73.25 C ANISOU 2027 CB GLU A 267 10965 8007 8859 -396 2042 -1010 C ATOM 2028 CG GLU A 267 13.883 23.807 -31.344 1.00 76.30 C ANISOU 2028 CG GLU A 267 11258 8493 9238 -409 2180 -1014 C ATOM 2029 CD GLU A 267 15.323 23.329 -31.377 1.00 89.35 C ANISOU 2029 CD GLU A 267 12832 10189 10928 -325 2261 -1142 C ATOM 2030 OE1 GLU A 267 15.558 22.106 -31.467 1.00 92.27 O ANISOU 2030 OE1 GLU A 267 13218 10492 11348 -240 2210 -1241 O ATOM 2031 OE2 GLU A 267 16.225 24.188 -31.310 1.00 97.79 O ANISOU 2031 OE2 GLU A 267 13805 11345 12004 -342 2373 -1149 O ATOM 2032 N LYS A 268 10.773 23.551 -33.538 1.00 74.04 N ANISOU 2032 N LYS A 268 11265 8127 8739 -573 1949 -853 N ATOM 2033 CA LYS A 268 10.384 24.404 -34.653 1.00 74.88 C ANISOU 2033 CA LYS A 268 11432 8288 8732 -672 1936 -754 C ATOM 2034 C LYS A 268 9.203 25.285 -34.276 1.00 74.28 C ANISOU 2034 C LYS A 268 11300 8137 8786 -718 1836 -591 C ATOM 2035 O LYS A 268 9.161 26.467 -34.633 1.00 74.69 O ANISOU 2035 O LYS A 268 11321 8196 8860 -776 1843 -474 O ATOM 2036 CB LYS A 268 10.050 23.555 -35.878 1.00 76.35 C ANISOU 2036 CB LYS A 268 11766 8506 8736 -726 1876 -812 C ATOM 2037 CG LYS A 268 9.831 24.362 -37.155 1.00 81.57 C ANISOU 2037 CG LYS A 268 12513 9262 9218 -867 1852 -698 C ATOM 2038 CD LYS A 268 9.670 23.460 -38.378 1.00 86.74 C ANISOU 2038 CD LYS A 268 13329 9990 9639 -950 1816 -798 C ATOM 2039 CE LYS A 268 8.271 22.859 -38.477 1.00 84.10 C ANISOU 2039 CE LYS A 268 13060 9565 9331 -985 1612 -734 C ATOM 2040 NZ LYS A 268 7.261 23.861 -38.921 1.00 81.90 N ANISOU 2040 NZ LYS A 268 12783 9280 9054 -1100 1453 -486 N ATOM 2041 N ALA A 269 8.245 24.736 -33.528 1.00 73.58 N ANISOU 2041 N ALA A 269 11181 7966 8809 -697 1744 -584 N ATOM 2042 CA ALA A 269 7.065 25.513 -33.166 1.00 73.37 C ANISOU 2042 CA ALA A 269 11067 7868 8943 -734 1666 -467 C ATOM 2043 C ALA A 269 7.397 26.581 -32.136 1.00 72.64 C ANISOU 2043 C ALA A 269 10831 7758 9010 -713 1773 -470 C ATOM 2044 O ALA A 269 6.852 27.688 -32.191 1.00 73.04 O ANISOU 2044 O ALA A 269 10799 7748 9204 -741 1750 -382 O ATOM 2045 CB ALA A 269 5.965 24.596 -32.643 1.00 73.12 C ANISOU 2045 CB ALA A 269 11027 7777 8977 -740 1564 -478 C ATOM 2046 N LYS A 270 8.265 26.261 -31.176 1.00 71.83 N ANISOU 2046 N LYS A 270 10692 7696 8905 -672 1873 -573 N ATOM 2047 CA LYS A 270 8.715 27.260 -30.212 1.00 71.37 C ANISOU 2047 CA LYS A 270 10512 7643 8963 -675 1980 -600 C ATOM 2048 C LYS A 270 9.354 28.446 -30.924 1.00 71.96 C ANISOU 2048 C LYS A 270 10574 7722 9046 -696 2037 -543 C ATOM 2049 O LYS A 270 8.923 29.601 -30.773 1.00 72.31 O ANISOU 2049 O LYS A 270 10531 7690 9253 -724 2043 -490 O ATOM 2050 CB LYS A 270 9.700 26.617 -29.232 1.00 70.78 C ANISOU 2050 CB LYS A 270 10420 7633 8841 -647 2045 -697 C ATOM 2051 CG LYS A 270 10.275 27.551 -28.176 1.00 70.50 C ANISOU 2051 CG LYS A 270 10270 7628 8887 -676 2150 -745 C ATOM 2052 CD LYS A 270 11.398 26.877 -27.397 1.00 70.29 C ANISOU 2052 CD LYS A 270 10235 7678 8795 -657 2173 -808 C ATOM 2053 CE LYS A 270 12.579 26.568 -28.302 1.00 70.71 C ANISOU 2053 CE LYS A 270 10327 7769 8772 -590 2201 -827 C ATOM 2054 NZ LYS A 270 13.702 25.932 -27.560 1.00 70.86 N ANISOU 2054 NZ LYS A 270 10300 7839 8785 -555 2200 -881 N ATOM 2055 N ILE A 271 10.380 28.164 -31.732 1.00 72.39 N ANISOU 2055 N ILE A 271 10708 7858 8940 -690 2081 -558 N ATOM 2056 CA ILE A 271 11.071 29.220 -32.465 1.00 73.24 C ANISOU 2056 CA ILE A 271 10815 7995 9018 -744 2141 -489 C ATOM 2057 C ILE A 271 10.092 29.997 -33.333 1.00 74.27 C ANISOU 2057 C ILE A 271 10976 8045 9200 -814 2024 -320 C ATOM 2058 O ILE A 271 10.162 31.228 -33.422 1.00 74.93 O ANISOU 2058 O ILE A 271 11002 8064 9403 -861 2030 -224 O ATOM 2059 CB ILE A 271 12.223 28.626 -33.295 1.00 73.95 C ANISOU 2059 CB ILE A 271 10981 8213 8903 -746 2222 -557 C ATOM 2060 CG1 ILE A 271 13.263 27.997 -32.370 1.00 73.27 C ANISOU 2060 CG1 ILE A 271 10822 8177 8841 -665 2313 -704 C ATOM 2061 CG2 ILE A 271 12.864 29.693 -34.157 1.00 75.18 C ANISOU 2061 CG2 ILE A 271 11149 8425 8991 -845 2286 -465 C ATOM 2062 CD1 ILE A 271 14.479 27.464 -33.083 1.00 74.28 C ANISOU 2062 CD1 ILE A 271 10968 8419 8835 -647 2417 -809 C ATOM 2063 N GLU A 272 9.150 29.295 -33.967 1.00 74.68 N ANISOU 2063 N GLU A 272 11110 8083 9182 -827 1893 -271 N ATOM 2064 CA GLU A 272 8.143 29.981 -34.768 1.00 75.94 C ANISOU 2064 CA GLU A 272 11285 8160 9410 -898 1736 -85 C ATOM 2065 C GLU A 272 7.269 30.886 -33.915 1.00 75.79 C ANISOU 2065 C GLU A 272 11101 7980 9716 -863 1695 -46 C ATOM 2066 O GLU A 272 6.781 31.912 -34.400 1.00 77.12 O ANISOU 2066 O GLU A 272 11225 8038 10038 -908 1590 116 O ATOM 2067 CB GLU A 272 7.280 28.967 -35.516 1.00 76.50 C ANISOU 2067 CB GLU A 272 11464 8255 9346 -928 1592 -57 C ATOM 2068 CG GLU A 272 7.933 28.375 -36.754 1.00 79.81 C ANISOU 2068 CG GLU A 272 12055 8821 9446 -1011 1605 -71 C ATOM 2069 CD GLU A 272 7.033 27.378 -37.456 1.00 92.35 C ANISOU 2069 CD GLU A 272 13756 10427 10905 -1057 1455 -67 C ATOM 2070 OE1 GLU A 272 5.951 27.075 -36.911 1.00 98.26 O ANISOU 2070 OE1 GLU A 272 14439 11074 11822 -1013 1345 -49 O ATOM 2071 OE2 GLU A 272 7.405 26.901 -38.550 1.00 96.53 O ANISOU 2071 OE2 GLU A 272 14435 11081 11160 -1152 1456 -95 O ATOM 2072 N LEU A 273 7.053 30.524 -32.652 1.00 74.54 N ANISOU 2072 N LEU A 273 10844 7804 9673 -794 1773 -194 N ATOM 2073 CA LEU A 273 6.238 31.323 -31.751 1.00 74.68 C ANISOU 2073 CA LEU A 273 10688 7692 9993 -770 1781 -223 C ATOM 2074 C LEU A 273 7.010 32.465 -31.117 1.00 74.73 C ANISOU 2074 C LEU A 273 10602 7654 10138 -771 1911 -280 C ATOM 2075 O LEU A 273 6.402 33.312 -30.456 1.00 75.31 O ANISOU 2075 O LEU A 273 10522 7600 10491 -757 1933 -327 O ATOM 2076 CB LEU A 273 5.633 30.443 -30.657 1.00 73.73 C ANISOU 2076 CB LEU A 273 10509 7605 9898 -742 1824 -365 C ATOM 2077 CG LEU A 273 4.498 29.535 -31.127 1.00 74.04 C ANISOU 2077 CG LEU A 273 10586 7636 9911 -753 1677 -307 C ATOM 2078 CD1 LEU A 273 4.092 28.576 -30.030 1.00 73.22 C ANISOU 2078 CD1 LEU A 273 10445 7587 9788 -757 1732 -434 C ATOM 2079 CD2 LEU A 273 3.309 30.361 -31.581 1.00 75.53 C ANISOU 2079 CD2 LEU A 273 10654 7682 10360 -758 1544 -189 C ATOM 2080 N SER A 274 8.328 32.515 -31.294 1.00 74.39 N ANISOU 2080 N SER A 274 10632 7709 9923 -792 2004 -296 N ATOM 2081 CA SER A 274 9.035 33.718 -30.876 1.00 74.80 C ANISOU 2081 CA SER A 274 10601 7703 10117 -816 2100 -320 C ATOM 2082 C SER A 274 8.663 34.941 -31.705 1.00 76.56 C ANISOU 2082 C SER A 274 10796 7761 10530 -862 1994 -136 C ATOM 2083 O SER A 274 8.936 36.062 -31.271 1.00 77.25 O ANISOU 2083 O SER A 274 10787 7732 10831 -879 2048 -159 O ATOM 2084 CB SER A 274 10.542 33.502 -30.940 1.00 74.31 C ANISOU 2084 CB SER A 274 10603 7789 9843 -840 2215 -368 C ATOM 2085 OG SER A 274 10.967 32.682 -29.870 1.00 75.48 O ANISOU 2085 OG SER A 274 10726 8040 9913 -800 2301 -533 O ATOM 2086 N SER A 275 8.054 34.767 -32.882 1.00 77.57 N ANISOU 2086 N SER A 275 11011 7869 10593 -897 1826 54 N ATOM 2087 CA SER A 275 7.711 35.903 -33.730 1.00 79.65 C ANISOU 2087 CA SER A 275 11260 7971 11032 -963 1676 283 C ATOM 2088 C SER A 275 6.299 35.862 -34.297 1.00 80.89 C ANISOU 2088 C SER A 275 11385 8006 11344 -953 1452 436 C ATOM 2089 O SER A 275 5.839 36.884 -34.815 1.00 82.93 O ANISOU 2089 O SER A 275 11586 8076 11846 -991 1292 634 O ATOM 2090 CB SER A 275 8.710 36.037 -34.891 1.00 80.59 C ANISOU 2090 CB SER A 275 11539 8215 10868 -1090 1667 444 C ATOM 2091 OG SER A 275 8.780 34.847 -35.654 1.00 80.27 O ANISOU 2091 OG SER A 275 11651 8366 10480 -1123 1645 446 O ATOM 2092 N ALA A 276 5.602 34.735 -34.221 1.00 79.99 N ANISOU 2092 N ALA A 276 11297 7977 11121 -912 1416 365 N ATOM 2093 CA ALA A 276 4.201 34.639 -34.605 1.00 81.18 C ANISOU 2093 CA ALA A 276 11381 8016 11447 -899 1207 483 C ATOM 2094 C ALA A 276 3.328 34.543 -33.360 1.00 80.54 C ANISOU 2094 C ALA A 276 11098 7849 11656 -796 1285 284 C ATOM 2095 O ALA A 276 3.814 34.355 -32.245 1.00 79.08 O ANISOU 2095 O ALA A 276 10866 7729 11452 -756 1494 60 O ATOM 2096 CB ALA A 276 3.965 33.431 -35.516 1.00 81.07 C ANISOU 2096 CB ALA A 276 11542 8164 11097 -960 1096 550 C ATOM 2097 N GLN A 277 2.016 34.664 -33.564 1.00 81.95 N ANISOU 2097 N GLN A 277 11147 7895 12095 -772 1112 369 N ATOM 2098 CA GLN A 277 1.057 34.605 -32.469 1.00 81.91 C ANISOU 2098 CA GLN A 277 10921 7818 12382 -694 1193 176 C ATOM 2099 C GLN A 277 0.368 33.253 -32.332 1.00 80.97 C ANISOU 2099 C GLN A 277 10837 7838 12089 -705 1172 110 C ATOM 2100 O GLN A 277 -0.286 33.017 -31.314 1.00 80.75 O ANISOU 2100 O GLN A 277 10649 7812 12219 -673 1286 -75 O ATOM 2101 CB GLN A 277 -0.004 35.696 -32.637 1.00 84.50 C ANISOU 2101 CB GLN A 277 11016 7881 13211 -645 1033 276 C ATOM 2102 CG GLN A 277 0.523 37.103 -32.430 1.00 85.72 C ANISOU 2102 CG GLN A 277 11077 7838 13654 -620 1081 277 C ATOM 2103 CD GLN A 277 0.928 37.369 -30.995 1.00 84.73 C ANISOU 2103 CD GLN A 277 10835 7730 13628 -577 1379 -55 C ATOM 2104 OE1 GLN A 277 0.223 36.991 -30.061 1.00 89.16 O ANISOU 2104 OE1 GLN A 277 11244 8329 14303 -542 1507 -281 O ATOM 2105 NE2 GLN A 277 2.072 38.017 -30.812 1.00 84.34 N ANISOU 2105 NE2 GLN A 277 10858 7673 13515 -606 1494 -88 N ATOM 2106 N GLN A 278 0.495 32.369 -33.320 1.00 80.68 N ANISOU 2106 N GLN A 278 11004 7920 11731 -767 1039 245 N ATOM 2107 CA GLN A 278 -0.087 31.034 -33.273 1.00 79.95 C ANISOU 2107 CA GLN A 278 10969 7942 11465 -791 1004 189 C ATOM 2108 C GLN A 278 0.492 30.207 -34.411 1.00 79.73 C ANISOU 2108 C GLN A 278 11204 8047 11042 -867 907 294 C ATOM 2109 O GLN A 278 0.593 30.689 -35.540 1.00 81.16 O ANISOU 2109 O GLN A 278 11473 8207 11156 -931 749 492 O ATOM 2110 CB GLN A 278 -1.616 31.079 -33.387 1.00 81.61 C ANISOU 2110 CB GLN A 278 10993 8043 11973 -786 831 257 C ATOM 2111 CG GLN A 278 -2.254 29.717 -33.566 1.00 81.24 C ANISOU 2111 CG GLN A 278 11024 8105 11738 -840 749 243 C ATOM 2112 CD GLN A 278 -3.740 29.793 -33.848 1.00 83.21 C ANISOU 2112 CD GLN A 278 11082 8254 12278 -851 545 340 C ATOM 2113 OE1 GLN A 278 -4.505 30.366 -33.075 1.00 84.10 O ANISOU 2113 OE1 GLN A 278 10925 8264 12765 -794 605 250 O ATOM 2114 NE2 GLN A 278 -4.156 29.215 -34.968 1.00 84.17 N ANISOU 2114 NE2 GLN A 278 11332 8413 12237 -933 304 511 N ATOM 2115 N THR A 279 0.867 28.967 -34.108 1.00 78.27 N ANISOU 2115 N THR A 279 11143 7994 10601 -873 999 157 N ATOM 2116 CA THR A 279 1.359 28.042 -35.121 1.00 78.33 C ANISOU 2116 CA THR A 279 11384 8120 10259 -938 933 190 C ATOM 2117 C THR A 279 0.644 26.710 -34.952 1.00 78.02 C ANISOU 2117 C THR A 279 11382 8116 10146 -958 874 112 C ATOM 2118 O THR A 279 -0.093 26.497 -33.989 1.00 77.59 O ANISOU 2118 O THR A 279 11183 8019 10279 -930 909 40 O ATOM 2119 CB THR A 279 2.878 27.856 -35.035 1.00 77.21 C ANISOU 2119 CB THR A 279 11368 8083 9884 -918 1119 80 C ATOM 2120 OG1 THR A 279 3.339 27.114 -36.169 1.00 77.89 O ANISOU 2120 OG1 THR A 279 11660 8280 9657 -990 1067 91 O ATOM 2121 CG2 THR A 279 3.241 27.102 -33.779 1.00 75.51 C ANISOU 2121 CG2 THR A 279 11117 7901 9673 -851 1278 -111 C ATOM 2122 N ASP A 280 0.857 25.809 -35.904 1.00 80.91 N ANISOU 2122 N ASP A 280 11945 8562 10233 -1024 792 116 N ATOM 2123 CA ASP A 280 0.265 24.480 -35.862 1.00 83.20 C ANISOU 2123 CA ASP A 280 12300 8869 10444 -1057 722 40 C ATOM 2124 C ASP A 280 1.370 23.438 -35.886 1.00 77.70 C ANISOU 2124 C ASP A 280 11777 8245 9503 -1036 842 -123 C ATOM 2125 O ASP A 280 2.249 23.482 -36.754 1.00 78.28 O ANISOU 2125 O ASP A 280 11987 8394 9361 -1062 879 -143 O ATOM 2126 CB ASP A 280 -0.692 24.256 -37.037 1.00100.94 C ANISOU 2126 CB ASP A 280 14612 11118 12623 -1170 473 175 C ATOM 2127 CG ASP A 280 -1.946 25.095 -36.940 1.00114.51 C ANISOU 2127 CG ASP A 280 16119 12737 14654 -1178 317 333 C ATOM 2128 OD1 ASP A 280 -2.263 25.559 -35.829 1.00111.23 O ANISOU 2128 OD1 ASP A 280 15499 12251 14515 -1097 424 282 O ATOM 2129 OD2 ASP A 280 -2.619 25.286 -37.975 1.00128.65 O ANISOU 2129 OD2 ASP A 280 17938 14523 16421 -1274 83 502 O ATOM 2130 N VAL A 281 1.331 22.513 -34.933 1.00 76.72 N ANISOU 2130 N VAL A 281 11633 8093 9424 -998 903 -239 N ATOM 2131 CA VAL A 281 2.159 21.315 -34.990 1.00 76.51 C ANISOU 2131 CA VAL A 281 11756 8084 9232 -974 957 -385 C ATOM 2132 C VAL A 281 1.399 20.302 -35.833 1.00 77.86 C ANISOU 2132 C VAL A 281 12049 8235 9300 -1063 789 -397 C ATOM 2133 O VAL A 281 0.368 19.771 -35.408 1.00 78.00 O ANISOU 2133 O VAL A 281 12013 8194 9430 -1108 687 -366 O ATOM 2134 CB VAL A 281 2.477 20.761 -33.598 1.00 75.27 C ANISOU 2134 CB VAL A 281 11534 7889 9177 -916 1055 -465 C ATOM 2135 CG1 VAL A 281 3.381 19.562 -33.725 1.00 75.48 C ANISOU 2135 CG1 VAL A 281 11696 7893 9090 -875 1080 -600 C ATOM 2136 CG2 VAL A 281 3.133 21.824 -32.738 1.00 74.18 C ANISOU 2136 CG2 VAL A 281 11270 7784 9131 -856 1209 -459 C ATOM 2137 N ASN A 282 1.908 20.041 -37.034 1.00 79.10 N ANISOU 2137 N ASN A 282 12367 8454 9233 -1109 770 -455 N ATOM 2138 CA ASN A 282 1.209 19.277 -38.063 1.00 80.86 C ANISOU 2138 CA ASN A 282 12724 8684 9314 -1229 602 -471 C ATOM 2139 C ASN A 282 2.100 18.110 -38.466 1.00 82.32 C ANISOU 2139 C ASN A 282 13071 8867 9340 -1210 681 -703 C ATOM 2140 O ASN A 282 3.016 18.275 -39.275 1.00 94.68 O ANISOU 2140 O ASN A 282 14732 10532 10710 -1224 783 -799 O ATOM 2141 CB ASN A 282 0.883 20.171 -39.253 1.00 82.40 C ANISOU 2141 CB ASN A 282 12965 8976 9367 -1347 487 -323 C ATOM 2142 CG ASN A 282 -0.101 19.544 -40.204 1.00 84.60 C ANISOU 2142 CG ASN A 282 13350 9271 9522 -1501 266 -293 C ATOM 2143 OD1 ASN A 282 -0.296 18.331 -40.208 1.00 92.29 O ANISOU 2143 OD1 ASN A 282 14411 10195 10459 -1523 232 -440 O ATOM 2144 ND2 ASN A 282 -0.732 20.373 -41.026 1.00 86.52 N ANISOU 2144 ND2 ASN A 282 13587 9574 9712 -1619 93 -90 N ATOM 2145 N LEU A 283 1.839 16.935 -37.903 1.00 81.50 N ANISOU 2145 N LEU A 283 12986 8642 9336 -1185 639 -798 N ATOM 2146 CA LEU A 283 2.606 15.729 -38.214 1.00 82.55 C ANISOU 2146 CA LEU A 283 13251 8715 9400 -1150 692 -1034 C ATOM 2147 C LEU A 283 1.689 14.660 -38.785 1.00 84.23 C ANISOU 2147 C LEU A 283 13581 8853 9571 -1268 517 -1097 C ATOM 2148 O LEU A 283 0.943 14.005 -38.033 1.00 83.88 O ANISOU 2148 O LEU A 283 13493 8680 9696 -1281 411 -1042 O ATOM 2149 CB LEU A 283 3.334 15.210 -36.977 1.00 81.33 C ANISOU 2149 CB LEU A 283 13020 8441 9439 -1008 785 -1093 C ATOM 2150 CG LEU A 283 4.499 16.105 -36.554 1.00 80.12 C ANISOU 2150 CG LEU A 283 12775 8369 9300 -897 970 -1090 C ATOM 2151 CD1 LEU A 283 5.272 15.502 -35.396 1.00 79.38 C ANISOU 2151 CD1 LEU A 283 12613 8163 9385 -774 1025 -1142 C ATOM 2152 CD2 LEU A 283 5.418 16.356 -37.737 1.00 81.45 C ANISOU 2152 CD2 LEU A 283 13029 8658 9262 -904 1091 -1237 C ATOM 2153 N PRO A 284 1.687 14.470 -40.099 1.00 86.31 N ANISOU 2153 N PRO A 284 13994 9203 9596 -1382 479 -1207 N ATOM 2154 CA PRO A 284 0.913 13.383 -40.698 1.00 88.24 C ANISOU 2154 CA PRO A 284 14367 9376 9786 -1508 317 -1310 C ATOM 2155 C PRO A 284 1.633 12.054 -40.561 1.00 89.23 C ANISOU 2155 C PRO A 284 14574 9336 9993 -1426 388 -1588 C ATOM 2156 O PRO A 284 2.861 11.993 -40.475 1.00 89.19 O ANISOU 2156 O PRO A 284 14559 9326 10003 -1296 574 -1751 O ATOM 2157 CB PRO A 284 0.808 13.794 -42.173 1.00 90.40 C ANISOU 2157 CB PRO A 284 14777 9839 9732 -1681 271 -1338 C ATOM 2158 CG PRO A 284 1.206 15.229 -42.212 1.00 89.33 C ANISOU 2158 CG PRO A 284 14556 9854 9533 -1657 356 -1154 C ATOM 2159 CD PRO A 284 2.197 15.396 -41.116 1.00 87.20 C ANISOU 2159 CD PRO A 284 14162 9511 9457 -1451 555 -1197 C ATOM 2160 N TYR A 285 0.837 10.981 -40.555 1.00 99.46 N ANISOU 2160 N TYR A 285 15937 10483 11372 -1505 226 -1639 N ATOM 2161 CA TYR A 285 1.332 9.615 -40.406 1.00106.24 C ANISOU 2161 CA TYR A 285 16871 11122 12372 -1439 240 -1887 C ATOM 2162 C TYR A 285 2.333 9.525 -39.258 1.00 96.75 C ANISOU 2162 C TYR A 285 15553 9798 11409 -1233 366 -1883 C ATOM 2163 O TYR A 285 3.387 8.891 -39.385 1.00100.36 O ANISOU 2163 O TYR A 285 16038 10150 11944 -1116 476 -2126 O ATOM 2164 CB TYR A 285 1.947 9.117 -41.716 1.00121.94 C ANISOU 2164 CB TYR A 285 19022 13162 14148 -1493 327 -2224 C ATOM 2165 CG TYR A 285 0.963 9.044 -42.872 1.00128.33 C ANISOU 2165 CG TYR A 285 19974 14091 14694 -1734 173 -2243 C ATOM 2166 CD1 TYR A 285 1.349 9.386 -44.161 1.00132.34 C ANISOU 2166 CD1 TYR A 285 20608 14819 14857 -1860 262 -2410 C ATOM 2167 CD2 TYR A 285 -0.343 8.623 -42.679 1.00126.96 C ANISOU 2167 CD2 TYR A 285 19808 13827 14605 -1861 -67 -2093 C ATOM 2168 CE1 TYR A 285 0.454 9.321 -45.215 1.00132.01 C ANISOU 2168 CE1 TYR A 285 20706 14904 14548 -2109 93 -2409 C ATOM 2169 CE2 TYR A 285 -1.246 8.559 -43.726 1.00124.83 C ANISOU 2169 CE2 TYR A 285 19658 13671 14102 -2092 -236 -2097 C ATOM 2170 CZ TYR A 285 -0.840 8.908 -44.993 1.00124.18 C ANISOU 2170 CZ TYR A 285 19711 13807 13664 -2218 -166 -2250 C ATOM 2171 OH TYR A 285 -1.741 8.839 -46.033 1.00117.79 O ANISOU 2171 OH TYR A 285 19031 13126 12597 -2477 -361 -2238 O ATOM 2172 N ILE A 286 2.008 10.163 -38.133 1.00 87.90 N ANISOU 2172 N ILE A 286 14289 8695 10413 -1197 346 -1616 N ATOM 2173 CA ILE A 286 2.934 10.193 -37.007 1.00 86.55 C ANISOU 2173 CA ILE A 286 14008 8445 10431 -1035 445 -1579 C ATOM 2174 C ILE A 286 3.158 8.790 -36.466 1.00 87.87 C ANISOU 2174 C ILE A 286 14214 8336 10835 -985 351 -1671 C ATOM 2175 O ILE A 286 4.283 8.412 -36.117 1.00 90.30 O ANISOU 2175 O ILE A 286 14487 8533 11290 -834 427 -1784 O ATOM 2176 CB ILE A 286 2.416 11.148 -35.916 1.00 84.15 C ANISOU 2176 CB ILE A 286 13556 8235 10184 -1049 442 -1296 C ATOM 2177 CG1 ILE A 286 3.319 11.076 -34.685 1.00 83.10 C ANISOU 2177 CG1 ILE A 286 13325 8027 10222 -922 513 -1248 C ATOM 2178 CG2 ILE A 286 0.963 10.844 -35.563 1.00 84.22 C ANISOU 2178 CG2 ILE A 286 13548 8200 10251 -1200 268 -1135 C ATOM 2179 CD1 ILE A 286 4.723 11.567 -34.941 1.00 82.91 C ANISOU 2179 CD1 ILE A 286 13268 8075 10161 -776 692 -1381 C ATOM 2180 N THR A 287 2.100 7.988 -36.415 1.00 88.83 N ANISOU 2180 N THR A 287 14402 8330 11019 -1115 168 -1619 N ATOM 2181 CA THR A 287 2.195 6.638 -35.887 1.00 93.02 C ANISOU 2181 CA THR A 287 14978 8567 11798 -1096 42 -1668 C ATOM 2182 C THR A 287 1.105 5.799 -36.533 1.00102.31 C ANISOU 2182 C THR A 287 16279 9639 12955 -1266 -129 -1730 C ATOM 2183 O THR A 287 0.148 6.327 -37.108 1.00100.99 O ANISOU 2183 O THR A 287 16129 9642 12601 -1408 -174 -1661 O ATOM 2184 CB THR A 287 2.074 6.627 -34.361 1.00 88.99 C ANISOU 2184 CB THR A 287 14360 7994 11458 -1098 -24 -1395 C ATOM 2185 OG1 THR A 287 2.424 5.335 -33.855 1.00 90.83 O ANISOU 2185 OG1 THR A 287 14639 7922 11952 -1064 -157 -1425 O ATOM 2186 CG2 THR A 287 0.657 6.954 -33.940 1.00 88.07 C ANISOU 2186 CG2 THR A 287 14201 7982 11278 -1287 -119 -1163 C ATOM 2187 N ALA A 288 1.272 4.480 -36.442 1.00 94.45 N ANISOU 2187 N ALA A 288 15363 8346 12179 -1253 -243 -1857 N ATOM 2188 CA ALA A 288 0.374 3.517 -37.074 1.00 96.75 C ANISOU 2188 CA ALA A 288 15785 8488 12486 -1413 -410 -1962 C ATOM 2189 C ALA A 288 -0.357 2.731 -35.995 1.00 97.03 C ANISOU 2189 C ALA A 288 15803 8315 12749 -1520 -609 -1726 C ATOM 2190 O ALA A 288 0.260 1.962 -35.251 1.00 97.93 O ANISOU 2190 O ALA A 288 15909 8173 13126 -1433 -671 -1703 O ATOM 2191 CB ALA A 288 1.138 2.576 -38.006 1.00 99.76 C ANISOU 2191 CB ALA A 288 16286 8672 12946 -1335 -375 -2356 C ATOM 2192 N ASP A 289 -1.665 2.936 -35.907 1.00100.52 N ANISOU 2192 N ASP A 289 16227 8868 13096 -1719 -717 -1538 N ATOM 2193 CA ASP A 289 -2.505 2.108 -35.064 1.00 97.51 C ANISOU 2193 CA ASP A 289 15844 8309 12896 -1878 -906 -1339 C ATOM 2194 C ASP A 289 -2.773 0.784 -35.770 1.00100.59 C ANISOU 2194 C ASP A 289 16394 8412 13413 -1966 -1071 -1547 C ATOM 2195 O ASP A 289 -2.489 0.616 -36.957 1.00102.06 O ANISOU 2195 O ASP A 289 16688 8590 13501 -1931 -1029 -1851 O ATOM 2196 CB ASP A 289 -3.815 2.831 -34.748 1.00103.49 C ANISOU 2196 CB ASP A 289 16490 9304 13528 -2062 -939 -1094 C ATOM 2197 CG ASP A 289 -4.599 2.174 -33.630 1.00110.35 C ANISOU 2197 CG ASP A 289 17314 10056 14559 -2241 -1080 -847 C ATOM 2198 OD1 ASP A 289 -3.991 1.441 -32.823 1.00122.92 O ANISOU 2198 OD1 ASP A 289 18939 11428 16336 -2205 -1135 -779 O ATOM 2199 OD2 ASP A 289 -5.826 2.404 -33.556 1.00103.09 O ANISOU 2199 OD2 ASP A 289 16314 9269 13586 -2430 -1141 -709 O ATOM 2200 N ALA A 290 -3.321 -0.172 -35.023 1.00101.96 N ANISOU 2200 N ALA A 290 16590 8349 13801 -2101 -1257 -1387 N ATOM 2201 CA ALA A 290 -3.746 -1.419 -35.649 1.00105.17 C ANISOU 2201 CA ALA A 290 17144 8468 14346 -2220 -1437 -1564 C ATOM 2202 C ALA A 290 -4.832 -1.170 -36.685 1.00105.67 C ANISOU 2202 C ALA A 290 17252 8718 14179 -2403 -1484 -1651 C ATOM 2203 O ALA A 290 -4.879 -1.841 -37.722 1.00108.18 O ANISOU 2203 O ALA A 290 17714 8905 14484 -2451 -1547 -1941 O ATOM 2204 CB ALA A 290 -4.241 -2.397 -34.589 1.00106.56 C ANISOU 2204 CB ALA A 290 17327 8376 14785 -2373 -1645 -1314 C ATOM 2205 N THR A 291 -5.721 -0.212 -36.421 1.00103.61 N ANISOU 2205 N THR A 291 16861 8761 13747 -2513 -1463 -1411 N ATOM 2206 CA THR A 291 -6.804 0.062 -37.357 1.00104.30 C ANISOU 2206 CA THR A 291 16961 9025 13644 -2693 -1548 -1447 C ATOM 2207 C THR A 291 -6.311 0.853 -38.561 1.00103.97 C ANISOU 2207 C THR A 291 16973 9200 13331 -2598 -1423 -1665 C ATOM 2208 O THR A 291 -6.712 0.580 -39.697 1.00106.02 O ANISOU 2208 O THR A 291 17352 9487 13443 -2724 -1512 -1856 O ATOM 2209 CB THR A 291 -7.928 0.814 -36.651 1.00102.66 C ANISOU 2209 CB THR A 291 16557 9045 13404 -2833 -1574 -1124 C ATOM 2210 OG1 THR A 291 -7.370 1.842 -35.823 1.00 99.84 O ANISOU 2210 OG1 THR A 291 16054 8861 13018 -2676 -1385 -970 O ATOM 2211 CG2 THR A 291 -8.735 -0.138 -35.795 1.00104.08 C ANISOU 2211 CG2 THR A 291 16715 9037 13792 -3036 -1736 -943 C ATOM 2212 N GLY A 292 -5.454 1.838 -38.335 1.00101.65 N ANISOU 2212 N GLY A 292 16598 9075 12951 -2406 -1224 -1633 N ATOM 2213 CA GLY A 292 -4.921 2.635 -39.410 1.00101.44 C ANISOU 2213 CA GLY A 292 16619 9265 12658 -2334 -1095 -1807 C ATOM 2214 C GLY A 292 -3.988 3.704 -38.887 1.00 98.74 C ANISOU 2214 C GLY A 292 16159 9078 12279 -2129 -882 -1717 C ATOM 2215 O GLY A 292 -3.927 3.969 -37.682 1.00103.04 O ANISOU 2215 O GLY A 292 16571 9607 12974 -2063 -844 -1498 O ATOM 2216 N PRO A 293 -3.241 4.342 -39.785 1.00 98.74 N ANISOU 2216 N PRO A 293 16211 9245 12060 -2049 -738 -1889 N ATOM 2217 CA PRO A 293 -2.287 5.367 -39.355 1.00 96.39 C ANISOU 2217 CA PRO A 293 15805 9090 11727 -1862 -533 -1820 C ATOM 2218 C PRO A 293 -2.995 6.539 -38.698 1.00 93.91 C ANISOU 2218 C PRO A 293 15316 8973 11393 -1891 -536 -1496 C ATOM 2219 O PRO A 293 -4.166 6.820 -38.960 1.00 94.20 O ANISOU 2219 O PRO A 293 15311 9107 11373 -2050 -676 -1356 O ATOM 2220 CB PRO A 293 -1.608 5.787 -40.659 1.00 97.54 C ANISOU 2220 CB PRO A 293 16058 9407 11597 -1852 -407 -2062 C ATOM 2221 CG PRO A 293 -2.613 5.473 -41.709 1.00 99.77 C ANISOU 2221 CG PRO A 293 16464 9750 11696 -2082 -580 -2126 C ATOM 2222 CD PRO A 293 -3.333 4.246 -41.248 1.00101.06 C ANISOU 2222 CD PRO A 293 16662 9645 12092 -2169 -763 -2129 C ATOM 2223 N LYS A 294 -2.265 7.227 -37.827 1.00103.98 N ANISOU 2223 N LYS A 294 16471 10298 12739 -1735 -383 -1392 N ATOM 2224 CA LYS A 294 -2.816 8.338 -37.071 1.00 97.96 C ANISOU 2224 CA LYS A 294 15527 9697 11998 -1743 -351 -1128 C ATOM 2225 C LYS A 294 -2.109 9.634 -37.447 1.00 94.44 C ANISOU 2225 C LYS A 294 15030 9452 11401 -1635 -189 -1123 C ATOM 2226 O LYS A 294 -1.056 9.641 -38.088 1.00 97.88 O ANISOU 2226 O LYS A 294 15558 9908 11723 -1545 -74 -1308 O ATOM 2227 CB LYS A 294 -2.714 8.072 -35.566 1.00 97.61 C ANISOU 2227 CB LYS A 294 15377 9550 12162 -1702 -324 -984 C ATOM 2228 CG LYS A 294 -3.537 6.873 -35.110 1.00102.70 C ANISOU 2228 CG LYS A 294 16059 10008 12956 -1850 -499 -929 C ATOM 2229 CD LYS A 294 -4.993 7.022 -35.527 1.00109.53 C ANISOU 2229 CD LYS A 294 16871 10964 13782 -2040 -638 -830 C ATOM 2230 CE LYS A 294 -5.835 5.844 -35.066 1.00115.34 C ANISOU 2230 CE LYS A 294 17635 11524 14666 -2214 -808 -767 C ATOM 2231 NZ LYS A 294 -7.250 5.971 -35.508 1.00120.23 N ANISOU 2231 NZ LYS A 294 18180 12237 15265 -2404 -950 -680 N ATOM 2232 N HIS A 295 -2.711 10.744 -37.031 1.00 86.73 N ANISOU 2232 N HIS A 295 13892 8617 10444 -1653 -176 -915 N ATOM 2233 CA HIS A 295 -2.280 12.072 -37.435 1.00 85.74 C ANISOU 2233 CA HIS A 295 13709 8668 10200 -1587 -66 -865 C ATOM 2234 C HIS A 295 -2.271 13.005 -36.241 1.00 83.64 C ANISOU 2234 C HIS A 295 13246 8453 10079 -1508 45 -705 C ATOM 2235 O HIS A 295 -3.005 12.806 -35.272 1.00 83.22 O ANISOU 2235 O HIS A 295 13079 8358 10183 -1559 8 -600 O ATOM 2236 CB HIS A 295 -3.197 12.658 -38.499 1.00 86.93 C ANISOU 2236 CB HIS A 295 13866 8941 10222 -1721 -212 -777 C ATOM 2237 CG HIS A 295 -3.209 11.877 -39.767 1.00 90.43 C ANISOU 2237 CG HIS A 295 14514 9382 10462 -1836 -316 -945 C ATOM 2238 ND1 HIS A 295 -2.074 11.305 -40.293 1.00 90.18 N ANISOU 2238 ND1 HIS A 295 14643 9323 10299 -1779 -195 -1195 N ATOM 2239 CD2 HIS A 295 -4.216 11.565 -40.615 1.00102.07 C ANISOU 2239 CD2 HIS A 295 16054 10885 11844 -2018 -527 -921 C ATOM 2240 CE1 HIS A 295 -2.380 10.682 -41.416 1.00 95.93 C ANISOU 2240 CE1 HIS A 295 15536 10069 10844 -1927 -307 -1340 C ATOM 2241 NE2 HIS A 295 -3.674 10.822 -41.633 1.00104.14 N ANISOU 2241 NE2 HIS A 295 16531 11145 11891 -2081 -521 -1166 N ATOM 2242 N MET A 296 -1.457 14.048 -36.337 1.00 82.58 N ANISOU 2242 N MET A 296 13072 8423 9880 -1406 187 -698 N ATOM 2243 CA MET A 296 -1.462 15.113 -35.349 1.00 80.86 C ANISOU 2243 CA MET A 296 12669 8268 9788 -1343 297 -571 C ATOM 2244 C MET A 296 -1.600 16.451 -36.056 1.00 80.86 C ANISOU 2244 C MET A 296 12606 8384 9732 -1343 300 -476 C ATOM 2245 O MET A 296 -0.908 16.710 -37.045 1.00 81.47 O ANISOU 2245 O MET A 296 12800 8526 9630 -1333 325 -532 O ATOM 2246 CB MET A 296 -0.198 15.097 -34.493 1.00 79.60 C ANISOU 2246 CB MET A 296 12500 8086 9657 -1214 468 -639 C ATOM 2247 CG MET A 296 -0.358 15.875 -33.201 1.00 78.16 C ANISOU 2247 CG MET A 296 12135 7950 9611 -1194 566 -532 C ATOM 2248 SD MET A 296 1.100 15.798 -32.164 1.00 77.01 S ANISOU 2248 SD MET A 296 11984 7792 9484 -1076 723 -591 S ATOM 2249 CE MET A 296 2.335 16.223 -33.370 1.00 77.21 C ANISOU 2249 CE MET A 296 12107 7866 9362 -967 811 -713 C ATOM 2250 N ASN A 297 -2.507 17.285 -35.556 1.00 80.50 N ANISOU 2250 N ASN A 297 12370 8362 9855 -1365 271 -334 N ATOM 2251 CA ASN A 297 -2.656 18.658 -36.033 1.00 80.63 C ANISOU 2251 CA ASN A 297 12290 8444 9904 -1349 259 -215 C ATOM 2252 C ASN A 297 -3.179 19.462 -34.847 1.00 79.73 C ANISOU 2252 C ASN A 297 11929 8316 10047 -1307 346 -151 C ATOM 2253 O ASN A 297 -4.382 19.450 -34.573 1.00 80.47 O ANISOU 2253 O ASN A 297 11874 8388 10314 -1372 252 -86 O ATOM 2254 CB ASN A 297 -3.594 18.737 -37.230 1.00 96.13 C ANISOU 2254 CB ASN A 297 14286 10429 11810 -1470 29 -109 C ATOM 2255 CG ASN A 297 -3.567 20.095 -37.907 1.00105.73 C ANISOU 2255 CG ASN A 297 15445 11695 13033 -1467 -22 42 C ATOM 2256 OD1 ASN A 297 -3.013 21.057 -37.378 1.00104.47 O ANISOU 2256 OD1 ASN A 297 15184 11534 12975 -1369 121 66 O ATOM 2257 ND2 ASN A 297 -4.173 20.178 -39.086 1.00114.62 N ANISOU 2257 ND2 ASN A 297 16638 12859 14051 -1593 -245 156 N ATOM 2258 N ILE A 298 -2.274 20.141 -34.147 1.00 78.38 N ANISOU 2258 N ILE A 298 11708 8166 9905 -1208 533 -191 N ATOM 2259 CA ILE A 298 -2.592 20.815 -32.894 1.00 77.64 C ANISOU 2259 CA ILE A 298 11401 8074 10025 -1179 661 -192 C ATOM 2260 C ILE A 298 -2.268 22.296 -33.026 1.00 77.50 C ANISOU 2260 C ILE A 298 11276 8059 10111 -1106 729 -142 C ATOM 2261 O ILE A 298 -1.148 22.660 -33.404 1.00 76.94 O ANISOU 2261 O ILE A 298 11312 8015 9905 -1050 800 -159 O ATOM 2262 CB ILE A 298 -1.818 20.201 -31.716 1.00 76.43 C ANISOU 2262 CB ILE A 298 11283 7939 9819 -1159 816 -292 C ATOM 2263 CG1 ILE A 298 -2.050 18.694 -31.662 1.00 76.89 C ANISOU 2263 CG1 ILE A 298 11468 7955 9793 -1234 719 -319 C ATOM 2264 CG2 ILE A 298 -2.229 20.853 -30.414 1.00 76.10 C ANISOU 2264 CG2 ILE A 298 11030 7933 9951 -1176 955 -315 C ATOM 2265 CD1 ILE A 298 -1.426 18.020 -30.463 1.00 76.20 C ANISOU 2265 CD1 ILE A 298 11406 7866 9679 -1242 816 -367 C ATOM 2266 N LYS A 299 -3.244 23.145 -32.716 1.00 78.26 N ANISOU 2266 N LYS A 299 11147 8117 10471 -1109 708 -89 N ATOM 2267 CA LYS A 299 -2.994 24.575 -32.632 1.00 78.35 C ANISOU 2267 CA LYS A 299 11026 8089 10655 -1035 779 -58 C ATOM 2268 C LYS A 299 -2.245 24.889 -31.349 1.00 77.03 C ANISOU 2268 C LYS A 299 10797 7958 10512 -989 1022 -198 C ATOM 2269 O LYS A 299 -2.523 24.315 -30.294 1.00 76.66 O ANISOU 2269 O LYS A 299 10690 7958 10480 -1035 1122 -295 O ATOM 2270 CB LYS A 299 -4.302 25.361 -32.670 1.00 80.03 C ANISOU 2270 CB LYS A 299 10985 8216 11208 -1039 674 17 C ATOM 2271 CG LYS A 299 -5.012 25.321 -34.000 1.00 81.74 C ANISOU 2271 CG LYS A 299 11241 8392 11425 -1092 393 198 C ATOM 2272 CD LYS A 299 -6.347 26.027 -33.909 1.00 83.66 C ANISOU 2272 CD LYS A 299 11187 8534 12068 -1083 277 269 C ATOM 2273 CE LYS A 299 -7.239 25.370 -32.867 1.00 83.73 C ANISOU 2273 CE LYS A 299 11020 8577 12216 -1124 376 133 C ATOM 2274 NZ LYS A 299 -7.600 23.977 -33.253 1.00 83.75 N ANISOU 2274 NZ LYS A 299 11180 8648 11992 -1237 251 154 N ATOM 2275 N VAL A 300 -1.279 25.794 -31.446 1.00 76.53 N ANISOU 2275 N VAL A 300 10758 7885 10436 -925 1110 -199 N ATOM 2276 CA VAL A 300 -0.559 26.300 -30.286 1.00 75.58 C ANISOU 2276 CA VAL A 300 10565 7797 10355 -892 1325 -327 C ATOM 2277 C VAL A 300 -0.494 27.810 -30.407 1.00 76.29 C ANISOU 2277 C VAL A 300 10518 7795 10675 -837 1358 -300 C ATOM 2278 O VAL A 300 0.075 28.331 -31.373 1.00 76.56 O ANISOU 2278 O VAL A 300 10646 7793 10650 -815 1281 -186 O ATOM 2279 CB VAL A 300 0.858 25.719 -30.172 1.00 74.23 C ANISOU 2279 CB VAL A 300 10581 7707 9915 -873 1410 -379 C ATOM 2280 CG1 VAL A 300 1.544 26.282 -28.952 1.00 73.52 C ANISOU 2280 CG1 VAL A 300 10407 7660 9866 -863 1603 -497 C ATOM 2281 CG2 VAL A 300 0.811 24.211 -30.110 1.00 73.90 C ANISOU 2281 CG2 VAL A 300 10674 7708 9697 -917 1349 -398 C ATOM 2282 N THR A 301 -1.077 28.508 -29.445 1.00 76.91 N ANISOU 2282 N THR A 301 10373 7831 11018 -831 1474 -412 N ATOM 2283 CA THR A 301 -0.939 29.951 -29.369 1.00 77.77 C ANISOU 2283 CA THR A 301 10337 7821 11389 -773 1530 -429 C ATOM 2284 C THR A 301 0.350 30.302 -28.642 1.00 76.58 C ANISOU 2284 C THR A 301 10251 7736 11110 -768 1720 -546 C ATOM 2285 O THR A 301 0.959 29.466 -27.973 1.00 75.31 O ANISOU 2285 O THR A 301 10194 7714 10707 -811 1818 -631 O ATOM 2286 CB THR A 301 -2.126 30.570 -28.639 1.00 79.38 C ANISOU 2286 CB THR A 301 10249 7940 11973 -765 1593 -549 C ATOM 2287 OG1 THR A 301 -2.137 30.099 -27.289 1.00 78.84 O ANISOU 2287 OG1 THR A 301 10125 8008 11821 -835 1807 -760 O ATOM 2288 CG2 THR A 301 -3.418 30.158 -29.295 1.00 80.71 C ANISOU 2288 CG2 THR A 301 10327 8055 12286 -776 1396 -433 C ATOM 2289 N ARG A 302 0.770 31.559 -28.788 1.00 77.24 N ANISOU 2289 N ARG A 302 10267 7706 11376 -725 1751 -536 N ATOM 2290 CA ARG A 302 1.911 32.027 -28.012 1.00 76.44 C ANISOU 2290 CA ARG A 302 10189 7657 11197 -733 1933 -666 C ATOM 2291 C ARG A 302 1.605 31.971 -26.522 1.00 76.52 C ANISOU 2291 C ARG A 302 10063 7747 11265 -786 2130 -905 C ATOM 2292 O ARG A 302 2.467 31.607 -25.710 1.00 75.50 O ANISOU 2292 O ARG A 302 10012 7758 10915 -841 2254 -1006 O ATOM 2293 CB ARG A 302 2.295 33.447 -28.430 1.00 77.52 C ANISOU 2293 CB ARG A 302 10262 7629 11562 -693 1920 -611 C ATOM 2294 CG ARG A 302 3.482 34.013 -27.661 1.00 76.91 C ANISOU 2294 CG ARG A 302 10200 7598 11424 -715 2100 -748 C ATOM 2295 CD ARG A 302 3.874 35.403 -28.130 1.00 78.17 C ANISOU 2295 CD ARG A 302 10307 7574 11820 -692 2072 -676 C ATOM 2296 NE ARG A 302 4.467 35.394 -29.463 1.00 78.12 N ANISOU 2296 NE ARG A 302 10469 7565 11650 -703 1921 -426 N ATOM 2297 CZ ARG A 302 4.978 36.466 -30.058 1.00 79.26 C ANISOU 2297 CZ ARG A 302 10619 7577 11918 -719 1870 -299 C ATOM 2298 NH1 ARG A 302 4.974 37.637 -29.436 1.00 80.45 N ANISOU 2298 NH1 ARG A 302 10615 7558 12396 -705 1948 -407 N ATOM 2299 NH2 ARG A 302 5.494 36.370 -31.273 1.00 79.46 N ANISOU 2299 NH2 ARG A 302 10808 7645 11739 -767 1746 -73 N ATOM 2300 N ALA A 303 0.371 32.304 -26.146 1.00 78.04 N ANISOU 2300 N ALA A 303 10041 7865 11747 -787 2157 -1000 N ATOM 2301 CA ALA A 303 0.004 32.262 -24.738 1.00 78.60 C ANISOU 2301 CA ALA A 303 9972 8042 11849 -873 2370 -1252 C ATOM 2302 C ALA A 303 0.151 30.857 -24.170 1.00 77.37 C ANISOU 2302 C ALA A 303 9959 8102 11337 -981 2393 -1251 C ATOM 2303 O ALA A 303 0.603 30.684 -23.034 1.00 77.20 O ANISOU 2303 O ALA A 303 9951 8231 11152 -1088 2551 -1398 O ATOM 2304 CB ALA A 303 -1.421 32.773 -24.555 1.00 80.80 C ANISOU 2304 CB ALA A 303 9971 8207 12520 -854 2398 -1363 C ATOM 2305 N LYS A 304 -0.205 29.837 -24.952 1.00 76.76 N ANISOU 2305 N LYS A 304 9996 8035 11135 -970 2218 -1077 N ATOM 2306 CA LYS A 304 -0.095 28.466 -24.465 1.00 75.90 C ANISOU 2306 CA LYS A 304 10022 8085 10730 -1070 2209 -1056 C ATOM 2307 C LYS A 304 1.351 28.111 -24.149 1.00 74.51 C ANISOU 2307 C LYS A 304 10031 8003 10276 -1084 2238 -1041 C ATOM 2308 O LYS A 304 1.647 27.536 -23.096 1.00 74.40 O ANISOU 2308 O LYS A 304 10055 8131 10083 -1200 2319 -1106 O ATOM 2309 CB LYS A 304 -0.675 27.498 -25.494 1.00 75.70 C ANISOU 2309 CB LYS A 304 10095 8018 10649 -1047 2001 -882 C ATOM 2310 CG LYS A 304 -0.839 26.085 -24.975 1.00 75.35 C ANISOU 2310 CG LYS A 304 10156 8093 10382 -1161 1974 -861 C ATOM 2311 CD LYS A 304 -1.897 26.044 -23.890 1.00 76.73 C ANISOU 2311 CD LYS A 304 10142 8357 10653 -1298 2107 -991 C ATOM 2312 CE LYS A 304 -1.852 24.751 -23.097 1.00 80.91 C ANISOU 2312 CE LYS A 304 10788 9026 10928 -1458 2105 -963 C ATOM 2313 NZ LYS A 304 -2.966 24.679 -22.110 1.00 88.12 N ANISOU 2313 NZ LYS A 304 11516 10057 11911 -1630 2243 -1082 N ATOM 2314 N LEU A 305 2.270 28.453 -25.053 1.00 73.72 N ANISOU 2314 N LEU A 305 10039 7832 10140 -980 2167 -945 N ATOM 2315 CA LEU A 305 3.683 28.170 -24.824 1.00 72.66 C ANISOU 2315 CA LEU A 305 10043 7777 9786 -978 2194 -939 C ATOM 2316 C LEU A 305 4.194 28.922 -23.605 1.00 72.98 C ANISOU 2316 C LEU A 305 9995 7896 9839 -1052 2367 -1098 C ATOM 2317 O LEU A 305 4.885 28.352 -22.747 1.00 72.66 O ANISOU 2317 O LEU A 305 10020 7985 9602 -1135 2401 -1127 O ATOM 2318 CB LEU A 305 4.494 28.543 -26.064 1.00 72.18 C ANISOU 2318 CB LEU A 305 10079 7640 9707 -873 2117 -829 C ATOM 2319 CG LEU A 305 6.008 28.409 -25.931 1.00 71.38 C ANISOU 2319 CG LEU A 305 10077 7613 9431 -856 2160 -838 C ATOM 2320 CD1 LEU A 305 6.367 26.966 -25.695 1.00 70.85 C ANISOU 2320 CD1 LEU A 305 10129 7624 9168 -873 2091 -810 C ATOM 2321 CD2 LEU A 305 6.717 28.928 -27.163 1.00 71.34 C ANISOU 2321 CD2 LEU A 305 10138 7553 9417 -783 2120 -748 C ATOM 2322 N GLU A 306 3.859 30.212 -23.513 1.00 73.91 N ANISOU 2322 N GLU A 306 9960 7925 10200 -1033 2464 -1202 N ATOM 2323 CA GLU A 306 4.275 31.003 -22.362 1.00 74.58 C ANISOU 2323 CA GLU A 306 9953 8075 10309 -1119 2641 -1395 C ATOM 2324 C GLU A 306 3.804 30.358 -21.066 1.00 75.24 C ANISOU 2324 C GLU A 306 10001 8338 10248 -1287 2742 -1519 C ATOM 2325 O GLU A 306 4.563 30.249 -20.097 1.00 75.30 O ANISOU 2325 O GLU A 306 10055 8494 10061 -1405 2816 -1593 O ATOM 2326 CB GLU A 306 3.747 32.433 -22.493 1.00 75.97 C ANISOU 2326 CB GLU A 306 9945 8083 10837 -1067 2722 -1511 C ATOM 2327 CG GLU A 306 4.479 33.279 -23.528 1.00 75.71 C ANISOU 2327 CG GLU A 306 9956 7893 10918 -957 2642 -1388 C ATOM 2328 CD GLU A 306 3.830 34.634 -23.756 1.00 77.47 C ANISOU 2328 CD GLU A 306 9993 7894 11547 -899 2669 -1459 C ATOM 2329 OE1 GLU A 306 2.660 34.809 -23.365 1.00 78.86 O ANISOU 2329 OE1 GLU A 306 9993 8017 11952 -905 2724 -1585 O ATOM 2330 OE2 GLU A 306 4.487 35.529 -24.326 1.00 77.73 O ANISOU 2330 OE2 GLU A 306 10043 7795 11694 -852 2633 -1387 O ATOM 2331 N SER A 307 2.556 29.889 -21.043 1.00 75.96 N ANISOU 2331 N SER A 307 10014 8432 10416 -1322 2733 -1526 N ATOM 2332 CA SER A 307 2.063 29.204 -19.857 1.00 76.86 C ANISOU 2332 CA SER A 307 10104 8738 10362 -1518 2829 -1621 C ATOM 2333 C SER A 307 2.841 27.922 -19.606 1.00 75.84 C ANISOU 2333 C SER A 307 10182 8731 9905 -1592 2704 -1457 C ATOM 2334 O SER A 307 3.089 27.554 -18.454 1.00 76.57 O ANISOU 2334 O SER A 307 10305 9005 9783 -1781 2770 -1509 O ATOM 2335 CB SER A 307 0.573 28.910 -20.001 1.00 77.96 C ANISOU 2335 CB SER A 307 10106 8851 10664 -1542 2834 -1643 C ATOM 2336 OG SER A 307 0.349 27.865 -20.923 1.00 76.93 O ANISOU 2336 OG SER A 307 10101 8661 10467 -1475 2626 -1420 O ATOM 2337 N LEU A 308 3.255 27.240 -20.672 1.00 74.48 N ANISOU 2337 N LEU A 308 10150 8456 9694 -1456 2517 -1262 N ATOM 2338 CA LEU A 308 3.944 25.968 -20.506 1.00 73.87 C ANISOU 2338 CA LEU A 308 10246 8444 9377 -1499 2380 -1115 C ATOM 2339 C LEU A 308 5.363 26.125 -19.977 1.00 73.53 C ANISOU 2339 C LEU A 308 10270 8475 9192 -1517 2388 -1117 C ATOM 2340 O LEU A 308 5.878 25.192 -19.352 1.00 73.74 O ANISOU 2340 O LEU A 308 10395 8591 9033 -1614 2297 -1026 O ATOM 2341 CB LEU A 308 3.964 25.208 -21.831 1.00 72.91 C ANISOU 2341 CB LEU A 308 10238 8183 9279 -1348 2200 -958 C ATOM 2342 CG LEU A 308 2.637 24.580 -22.262 1.00 73.39 C ANISOU 2342 CG LEU A 308 10277 8194 9414 -1372 2127 -906 C ATOM 2343 CD1 LEU A 308 2.644 24.257 -23.740 1.00 72.70 C ANISOU 2343 CD1 LEU A 308 10281 7965 9376 -1218 1976 -798 C ATOM 2344 CD2 LEU A 308 2.379 23.324 -21.463 1.00 74.00 C ANISOU 2344 CD2 LEU A 308 10429 8361 9327 -1534 2063 -837 C ATOM 2345 N VAL A 309 6.013 27.267 -20.208 1.00 73.23 N ANISOU 2345 N VAL A 309 10177 8395 9254 -1435 2472 -1203 N ATOM 2346 CA VAL A 309 7.399 27.439 -19.787 1.00 73.01 C ANISOU 2346 CA VAL A 309 10196 8435 9108 -1450 2468 -1201 C ATOM 2347 C VAL A 309 7.572 28.556 -18.761 1.00 74.03 C ANISOU 2347 C VAL A 309 10221 8663 9244 -1580 2641 -1393 C ATOM 2348 O VAL A 309 8.708 28.919 -18.434 1.00 74.00 O ANISOU 2348 O VAL A 309 10235 8713 9171 -1599 2645 -1411 O ATOM 2349 CB VAL A 309 8.326 27.676 -20.994 1.00 71.93 C ANISOU 2349 CB VAL A 309 10108 8178 9043 -1260 2402 -1123 C ATOM 2350 CG1 VAL A 309 8.204 26.537 -21.981 1.00 71.28 C ANISOU 2350 CG1 VAL A 309 10136 8015 8934 -1152 2250 -978 C ATOM 2351 CG2 VAL A 309 8.002 28.998 -21.658 1.00 71.98 C ANISOU 2351 CG2 VAL A 309 10020 8068 9261 -1180 2498 -1198 C ATOM 2352 N GLU A 310 6.473 29.102 -18.228 1.00 75.19 N ANISOU 2352 N GLU A 310 10247 8840 9483 -1678 2789 -1558 N ATOM 2353 CA GLU A 310 6.588 30.251 -17.333 1.00 76.50 C ANISOU 2353 CA GLU A 310 10302 9077 9690 -1796 2979 -1795 C ATOM 2354 C GLU A 310 7.409 29.922 -16.093 1.00 77.32 C ANISOU 2354 C GLU A 310 10474 9404 9499 -2010 2982 -1818 C ATOM 2355 O GLU A 310 8.265 30.713 -15.684 1.00 77.73 O ANISOU 2355 O GLU A 310 10506 9496 9533 -2055 3044 -1924 O ATOM 2356 CB GLU A 310 5.209 30.764 -16.923 1.00 78.08 C ANISOU 2356 CB GLU A 310 10336 9278 10055 -1871 3155 -2003 C ATOM 2357 CG GLU A 310 5.285 31.946 -15.956 1.00 87.66 C ANISOU 2357 CG GLU A 310 11424 10558 11326 -2003 3377 -2306 C ATOM 2358 CD GLU A 310 3.936 32.567 -15.650 1.00 96.51 C ANISOU 2358 CD GLU A 310 12336 11645 12691 -2044 3576 -2561 C ATOM 2359 OE1 GLU A 310 2.962 31.813 -15.448 1.00 94.23 O ANISOU 2359 OE1 GLU A 310 12013 11445 12346 -2125 3592 -2543 O ATOM 2360 OE2 GLU A 310 3.852 33.814 -15.614 1.00104.23 O ANISOU 2360 OE2 GLU A 310 13167 12492 13943 -1994 3717 -2785 O ATOM 2361 N ASP A 311 7.158 28.767 -15.473 1.00 77.81 N ANISOU 2361 N ASP A 311 10619 9615 9329 -2164 2899 -1705 N ATOM 2362 CA ASP A 311 7.895 28.423 -14.261 1.00 84.00 C ANISOU 2362 CA ASP A 311 11475 10623 9818 -2401 2864 -1688 C ATOM 2363 C ASP A 311 9.376 28.236 -14.551 1.00 78.04 C ANISOU 2363 C ASP A 311 10803 9830 9018 -2299 2691 -1531 C ATOM 2364 O ASP A 311 10.220 28.510 -13.687 1.00 79.07 O ANISOU 2364 O ASP A 311 10946 10108 8988 -2455 2685 -1570 O ATOM 2365 CB ASP A 311 7.306 27.167 -13.625 1.00 96.22 C ANISOU 2365 CB ASP A 311 13106 12313 11142 -2596 2772 -1545 C ATOM 2366 CG ASP A 311 7.700 25.902 -14.356 1.00100.00 C ANISOU 2366 CG ASP A 311 13712 12666 11619 -2452 2508 -1249 C ATOM 2367 OD1 ASP A 311 7.151 25.643 -15.449 1.00 98.35 O ANISOU 2367 OD1 ASP A 311 13497 12275 11597 -2251 2470 -1195 O ATOM 2368 OD2 ASP A 311 8.560 25.166 -13.829 1.00105.06 O ANISOU 2368 OD2 ASP A 311 14453 13384 12081 -2548 2329 -1077 O ATOM 2369 N LEU A 312 9.708 27.778 -15.761 1.00 76.34 N ANISOU 2369 N LEU A 312 10632 9429 8943 -2051 2555 -1369 N ATOM 2370 CA LEU A 312 11.105 27.710 -16.167 1.00 75.61 C ANISOU 2370 CA LEU A 312 10576 9290 8862 -1929 2431 -1262 C ATOM 2371 C LEU A 312 11.708 29.100 -16.276 1.00 75.57 C ANISOU 2371 C LEU A 312 10483 9259 8970 -1893 2568 -1425 C ATOM 2372 O LEU A 312 12.832 29.330 -15.817 1.00 76.05 O ANISOU 2372 O LEU A 312 10539 9402 8954 -1952 2525 -1421 O ATOM 2373 CB LEU A 312 11.233 26.966 -17.494 1.00 74.17 C ANISOU 2373 CB LEU A 312 10449 8928 8804 -1687 2303 -1107 C ATOM 2374 CG LEU A 312 11.057 25.449 -17.464 1.00 84.54 C ANISOU 2374 CG LEU A 312 11863 10226 10033 -1697 2112 -921 C ATOM 2375 CD1 LEU A 312 11.185 24.877 -18.866 1.00 84.75 C ANISOU 2375 CD1 LEU A 312 11935 10068 10199 -1456 2025 -837 C ATOM 2376 CD2 LEU A 312 12.077 24.825 -16.530 1.00 98.83 C ANISOU 2376 CD2 LEU A 312 13709 12144 11696 -1817 1952 -802 C ATOM 2377 N VAL A 313 10.982 30.042 -16.879 1.00 75.24 N ANISOU 2377 N VAL A 313 10364 9090 9134 -1802 2715 -1557 N ATOM 2378 CA VAL A 313 11.499 31.406 -16.958 1.00 75.53 C ANISOU 2378 CA VAL A 313 10317 9070 9310 -1783 2837 -1707 C ATOM 2379 C VAL A 313 11.707 31.977 -15.561 1.00 77.27 C ANISOU 2379 C VAL A 313 10496 9469 9395 -2027 2946 -1901 C ATOM 2380 O VAL A 313 12.727 32.620 -15.282 1.00 77.70 O ANISOU 2380 O VAL A 313 10530 9560 9434 -2075 2957 -1957 O ATOM 2381 CB VAL A 313 10.562 32.292 -17.798 1.00 75.35 C ANISOU 2381 CB VAL A 313 10211 8850 9570 -1655 2943 -1793 C ATOM 2382 CG1 VAL A 313 11.082 33.710 -17.841 1.00 75.99 C ANISOU 2382 CG1 VAL A 313 10208 8840 9826 -1650 3052 -1936 C ATOM 2383 CG2 VAL A 313 10.441 31.745 -19.203 1.00 73.91 C ANISOU 2383 CG2 VAL A 313 10089 8523 9472 -1451 2818 -1593 C ATOM 2384 N ASN A 314 10.754 31.738 -14.657 1.00 78.54 N ANISOU 2384 N ASN A 314 10642 9763 9438 -2209 3034 -2014 N ATOM 2385 CA ASN A 314 10.873 32.247 -13.297 1.00 80.64 C ANISOU 2385 CA ASN A 314 10878 10235 9527 -2485 3159 -2228 C ATOM 2386 C ASN A 314 12.030 31.600 -12.556 1.00 81.16 C ANISOU 2386 C ASN A 314 11040 10493 9302 -2640 2987 -2079 C ATOM 2387 O ASN A 314 12.628 32.228 -11.678 1.00 82.68 O ANISOU 2387 O ASN A 314 11216 10830 9369 -2833 3044 -2226 O ATOM 2388 CB ASN A 314 9.569 32.021 -12.535 1.00 82.19 C ANISOU 2388 CB ASN A 314 11035 10562 9631 -2669 3304 -2378 C ATOM 2389 CG ASN A 314 8.429 32.860 -13.070 1.00 84.34 C ANISOU 2389 CG ASN A 314 11158 10649 10237 -2540 3491 -2582 C ATOM 2390 OD1 ASN A 314 8.645 33.922 -13.651 1.00 93.36 O ANISOU 2390 OD1 ASN A 314 12219 11595 11657 -2391 3553 -2685 O ATOM 2391 ND2 ASN A 314 7.205 32.386 -12.877 1.00 90.58 N ANISOU 2391 ND2 ASN A 314 11901 11493 11024 -2605 3568 -2628 N ATOM 2392 N ARG A 315 12.360 30.351 -12.893 1.00 80.19 N ANISOU 2392 N ARG A 315 11012 10365 9092 -2564 2764 -1793 N ATOM 2393 CA ARG A 315 13.514 29.703 -12.278 1.00 80.91 C ANISOU 2393 CA ARG A 315 11171 10596 8976 -2678 2555 -1618 C ATOM 2394 C ARG A 315 14.806 30.474 -12.528 1.00 80.66 C ANISOU 2394 C ARG A 315 11083 10521 9042 -2598 2532 -1649 C ATOM 2395 O ARG A 315 15.759 30.342 -11.752 1.00 81.93 O ANISOU 2395 O ARG A 315 11259 10836 9036 -2756 2404 -1587 O ATOM 2396 CB ARG A 315 13.640 28.267 -12.793 1.00 80.02 C ANISOU 2396 CB ARG A 315 11142 10405 8858 -2550 2316 -1320 C ATOM 2397 CG ARG A 315 14.747 27.453 -12.135 1.00 81.20 C ANISOU 2397 CG ARG A 315 11343 10666 8844 -2659 2056 -1104 C ATOM 2398 CD ARG A 315 14.913 26.084 -12.769 1.00 80.52 C ANISOU 2398 CD ARG A 315 11316 10436 8842 -2488 1822 -838 C ATOM 2399 NE ARG A 315 13.798 25.196 -12.459 1.00 81.21 N ANISOU 2399 NE ARG A 315 11489 10551 8816 -2606 1784 -745 N ATOM 2400 CZ ARG A 315 13.721 23.932 -12.859 1.00 91.41 C ANISOU 2400 CZ ARG A 315 12849 11714 10168 -2508 1580 -524 C ATOM 2401 NH1 ARG A 315 14.697 23.405 -13.590 1.00 83.48 N ANISOU 2401 NH1 ARG A 315 11826 10545 9348 -2275 1411 -401 N ATOM 2402 NH2 ARG A 315 12.670 23.196 -12.528 1.00106.39 N ANISOU 2402 NH2 ARG A 315 14822 13643 11957 -2649 1555 -444 N ATOM 2403 N SER A 316 14.855 31.291 -13.576 1.00 82.93 N ANISOU 2403 N SER A 316 11304 10611 9593 -2379 2641 -1729 N ATOM 2404 CA SER A 316 16.052 32.051 -13.898 1.00 81.79 C ANISOU 2404 CA SER A 316 11101 10421 9555 -2313 2633 -1753 C ATOM 2405 C SER A 316 16.129 33.387 -13.174 1.00 88.31 C ANISOU 2405 C SER A 316 11861 11305 10387 -2489 2807 -2023 C ATOM 2406 O SER A 316 17.189 34.020 -13.190 1.00100.56 O ANISOU 2406 O SER A 316 13365 12856 11985 -2501 2788 -2049 O ATOM 2407 CB SER A 316 16.128 32.296 -15.405 1.00 77.38 C ANISOU 2407 CB SER A 316 10515 9632 9255 -2030 2658 -1687 C ATOM 2408 OG SER A 316 15.095 33.173 -15.814 1.00 78.15 O ANISOU 2408 OG SER A 316 10573 9591 9529 -1981 2833 -1841 O ATOM 2409 N ILE A 317 15.044 33.837 -12.547 1.00 81.74 N ANISOU 2409 N ILE A 317 11013 10520 9526 -2631 2984 -2243 N ATOM 2410 CA ILE A 317 15.059 35.155 -11.922 1.00 83.43 C ANISOU 2410 CA ILE A 317 11153 10753 9795 -2784 3173 -2552 C ATOM 2411 C ILE A 317 15.705 35.099 -10.545 1.00 85.61 C ANISOU 2411 C ILE A 317 11466 11315 9748 -3106 3130 -2629 C ATOM 2412 O ILE A 317 16.358 36.056 -10.117 1.00 95.47 O ANISOU 2412 O ILE A 317 12669 12594 11009 -3227 3195 -2809 O ATOM 2413 CB ILE A 317 13.630 35.724 -11.870 1.00 84.15 C ANISOU 2413 CB ILE A 317 11174 10753 10045 -2787 3402 -2801 C ATOM 2414 CG1 ILE A 317 13.036 35.795 -13.276 1.00 82.24 C ANISOU 2414 CG1 ILE A 317 10895 10226 10125 -2480 3396 -2685 C ATOM 2415 CG2 ILE A 317 13.624 37.098 -11.247 1.00 86.25 C ANISOU 2415 CG2 ILE A 317 11349 11001 10421 -2930 3609 -3160 C ATOM 2416 CD1 ILE A 317 13.866 36.587 -14.250 1.00 81.33 C ANISOU 2416 CD1 ILE A 317 10748 9904 10250 -2306 3360 -2619 C ATOM 2417 N GLU A 318 15.540 33.989 -9.833 1.00111.26 N ANISOU 2417 N GLU A 318 14802 14774 12696 -3270 3002 -2481 N ATOM 2418 CA GLU A 318 16.162 33.836 -8.517 1.00115.01 C ANISOU 2418 CA GLU A 318 15331 15547 12822 -3611 2913 -2499 C ATOM 2419 C GLU A 318 17.670 34.059 -8.534 1.00107.60 C ANISOU 2419 C GLU A 318 14368 14624 11890 -3604 2735 -2387 C ATOM 2420 O GLU A 318 18.173 34.814 -7.681 1.00117.80 O ANISOU 2420 O GLU A 318 15644 16069 13045 -3851 2783 -2578 O ATOM 2421 CB GLU A 318 15.816 32.448 -7.958 1.00130.64 C ANISOU 2421 CB GLU A 318 17419 17707 14511 -3758 2736 -2253 C ATOM 2422 CG GLU A 318 14.332 32.132 -7.963 1.00149.47 C ANISOU 2422 CG GLU A 318 19815 20089 16887 -3777 2903 -2340 C ATOM 2423 CD GLU A 318 13.555 32.974 -6.973 1.00169.11 C ANISOU 2423 CD GLU A 318 22263 22760 19231 -4069 3192 -2726 C ATOM 2424 OE1 GLU A 318 14.115 33.311 -5.909 1.00170.32 O ANISOU 2424 OE1 GLU A 318 22450 23158 19107 -4382 3191 -2844 O ATOM 2425 OE2 GLU A 318 12.384 33.300 -7.258 1.00180.96 O ANISOU 2425 OE2 GLU A 318 23687 24163 20905 -3992 3421 -2926 O ATOM 2426 N PRO A 319 18.443 33.466 -9.450 1.00 87.01 N ANISOU 2426 N PRO A 319 11745 11876 9441 -3348 2541 -2111 N ATOM 2427 CA PRO A 319 19.887 33.741 -9.453 1.00 87.47 C ANISOU 2427 CA PRO A 319 11741 11959 9535 -3349 2392 -2032 C ATOM 2428 C PRO A 319 20.224 35.185 -9.766 1.00 87.54 C ANISOU 2428 C PRO A 319 11661 11852 9747 -3321 2581 -2280 C ATOM 2429 O PRO A 319 21.337 35.623 -9.454 1.00 97.69 O ANISOU 2429 O PRO A 319 12893 13213 11013 -3422 2495 -2287 O ATOM 2430 CB PRO A 319 20.426 32.787 -10.529 1.00 86.33 C ANISOU 2430 CB PRO A 319 11575 11658 9569 -3044 2207 -1735 C ATOM 2431 CG PRO A 319 19.383 31.736 -10.663 1.00 84.77 C ANISOU 2431 CG PRO A 319 11468 11433 9309 -2986 2173 -1610 C ATOM 2432 CD PRO A 319 18.096 32.452 -10.461 1.00 84.86 C ANISOU 2432 CD PRO A 319 11500 11437 9307 -3072 2441 -1871 C ATOM 2433 N LEU A 320 19.309 35.940 -10.376 1.00 86.62 N ANISOU 2433 N LEU A 320 11520 11541 9850 -3192 2814 -2468 N ATOM 2434 CA LEU A 320 19.529 37.375 -10.510 1.00 87.30 C ANISOU 2434 CA LEU A 320 11529 11503 10140 -3212 2987 -2719 C ATOM 2435 C LEU A 320 19.563 38.036 -9.140 1.00 90.16 C ANISOU 2435 C LEU A 320 11898 12071 10289 -3562 3078 -3008 C ATOM 2436 O LEU A 320 20.489 38.791 -8.822 1.00 91.46 O ANISOU 2436 O LEU A 320 12017 12270 10463 -3688 3063 -3109 O ATOM 2437 CB LEU A 320 18.443 38.011 -11.376 1.00 86.23 C ANISOU 2437 CB LEU A 320 11358 11099 10308 -3014 3185 -2845 C ATOM 2438 CG LEU A 320 18.137 37.456 -12.766 1.00 83.71 C ANISOU 2438 CG LEU A 320 11047 10578 10182 -2698 3127 -2602 C ATOM 2439 CD1 LEU A 320 17.349 38.486 -13.545 1.00 83.45 C ANISOU 2439 CD1 LEU A 320 10955 10269 10484 -2556 3297 -2740 C ATOM 2440 CD2 LEU A 320 19.398 37.093 -13.510 1.00 82.63 C ANISOU 2440 CD2 LEU A 320 10894 10421 10079 -2565 2962 -2357 C ATOM 2441 N LYS A 321 18.557 37.754 -8.311 1.00 91.43 N ANISOU 2441 N LYS A 321 12112 12386 10241 -3746 3182 -3155 N ATOM 2442 CA LYS A 321 18.539 38.278 -6.951 1.00 94.57 C ANISOU 2442 CA LYS A 321 12531 13031 10372 -4124 3285 -3451 C ATOM 2443 C LYS A 321 19.789 37.858 -6.189 1.00 95.98 C ANISOU 2443 C LYS A 321 12755 13467 10246 -4353 3030 -3281 C ATOM 2444 O LYS A 321 20.453 38.689 -5.558 1.00 98.05 O ANISOU 2444 O LYS A 321 12993 13825 10438 -4571 3057 -3482 O ATOM 2445 CB LYS A 321 17.281 37.802 -6.224 1.00 95.82 C ANISOU 2445 CB LYS A 321 12742 13361 10305 -4300 3424 -3585 C ATOM 2446 CG LYS A 321 15.974 38.172 -6.913 1.00 94.81 C ANISOU 2446 CG LYS A 321 12538 12990 10496 -4082 3663 -3757 C ATOM 2447 CD LYS A 321 14.773 37.733 -6.087 1.00 96.55 C ANISOU 2447 CD LYS A 321 12784 13420 10481 -4300 3823 -3924 C ATOM 2448 CE LYS A 321 13.466 38.197 -6.709 1.00 96.04 C ANISOU 2448 CE LYS A 321 12603 13112 10778 -4092 4066 -4130 C ATOM 2449 NZ LYS A 321 12.289 37.844 -5.865 1.00 98.89 N ANISOU 2449 NZ LYS A 321 12953 13695 10925 -4324 4261 -4338 N ATOM 2450 N VAL A 322 20.135 36.570 -6.248 1.00 95.11 N ANISOU 2450 N VAL A 322 12702 13455 9981 -4308 2761 -2906 N ATOM 2451 CA VAL A 322 21.295 36.096 -5.496 1.00 96.83 C ANISOU 2451 CA VAL A 322 12945 13907 9938 -4525 2474 -2709 C ATOM 2452 C VAL A 322 22.568 36.786 -5.972 1.00 96.53 C ANISOU 2452 C VAL A 322 12796 13757 10123 -4419 2395 -2690 C ATOM 2453 O VAL A 322 23.409 37.200 -5.165 1.00 98.86 O ANISOU 2453 O VAL A 322 13077 14237 10249 -4685 2297 -2758 O ATOM 2454 CB VAL A 322 21.411 34.566 -5.598 1.00 96.06 C ANISOU 2454 CB VAL A 322 12906 13862 9730 -4445 2181 -2293 C ATOM 2455 CG1 VAL A 322 22.657 34.089 -4.885 1.00 98.09 C ANISOU 2455 CG1 VAL A 322 13159 14321 9790 -4641 1843 -2058 C ATOM 2456 CG2 VAL A 322 20.179 33.908 -5.008 1.00 96.83 C ANISOU 2456 CG2 VAL A 322 13118 14101 9571 -4615 2253 -2306 C ATOM 2457 N ALA A 323 22.727 36.927 -7.289 1.00 93.90 N ANISOU 2457 N ALA A 323 12384 13138 10156 -4056 2437 -2599 N ATOM 2458 CA ALA A 323 23.941 37.530 -7.827 1.00 93.69 C ANISOU 2458 CA ALA A 323 12242 13012 10345 -3959 2373 -2560 C ATOM 2459 C ALA A 323 24.041 39.003 -7.461 1.00 95.32 C ANISOU 2459 C ALA A 323 12410 13186 10619 -4135 2573 -2913 C ATOM 2460 O ALA A 323 25.123 39.488 -7.111 1.00 96.85 O ANISOU 2460 O ALA A 323 12540 13466 10793 -4283 2473 -2936 O ATOM 2461 CB ALA A 323 23.988 37.352 -9.341 1.00 90.84 C ANISOU 2461 CB ALA A 323 11819 12375 10321 -3567 2404 -2397 C ATOM 2462 N LEU A 324 22.930 39.737 -7.550 1.00 95.23 N ANISOU 2462 N LEU A 324 12424 13036 10724 -4118 2848 -3196 N ATOM 2463 CA LEU A 324 22.946 41.134 -7.134 1.00 97.23 C ANISOU 2463 CA LEU A 324 12639 13229 11075 -4292 3043 -3568 C ATOM 2464 C LEU A 324 23.264 41.257 -5.653 1.00100.53 C ANISOU 2464 C LEU A 324 13109 13976 11113 -4715 2999 -3757 C ATOM 2465 O LEU A 324 23.923 42.212 -5.228 1.00102.55 O ANISOU 2465 O LEU A 324 13322 14251 11389 -4905 3032 -3970 O ATOM 2466 CB LEU A 324 21.608 41.795 -7.452 1.00 96.95 C ANISOU 2466 CB LEU A 324 12597 12969 11270 -4184 3330 -3841 C ATOM 2467 CG LEU A 324 21.362 42.071 -8.933 1.00 94.40 C ANISOU 2467 CG LEU A 324 12215 12289 11362 -3815 3381 -3702 C ATOM 2468 CD1 LEU A 324 20.045 42.788 -9.139 1.00 94.74 C ANISOU 2468 CD1 LEU A 324 12229 12103 11664 -3732 3631 -3975 C ATOM 2469 CD2 LEU A 324 22.500 42.896 -9.479 1.00 94.52 C ANISOU 2469 CD2 LEU A 324 12155 12162 11596 -3778 3330 -3659 C ATOM 2470 N GLN A 325 22.803 40.298 -4.850 1.00101.38 N ANISOU 2470 N GLN A 325 13314 14351 10856 -4894 2917 -3676 N ATOM 2471 CA GLN A 325 23.139 40.307 -3.432 1.00104.85 C ANISOU 2471 CA GLN A 325 13822 15148 10867 -5339 2840 -3807 C ATOM 2472 C GLN A 325 24.634 40.105 -3.224 1.00105.71 C ANISOU 2472 C GLN A 325 13889 15389 10887 -5438 2521 -3560 C ATOM 2473 O GLN A 325 25.276 40.853 -2.479 1.00108.40 O ANISOU 2473 O GLN A 325 14217 15872 11096 -5732 2507 -3763 O ATOM 2474 CB GLN A 325 22.341 39.231 -2.696 1.00105.68 C ANISOU 2474 CB GLN A 325 14049 15515 10589 -5520 2791 -3702 C ATOM 2475 CG GLN A 325 22.641 39.143 -1.211 1.00110.27 C ANISOU 2475 CG GLN A 325 14727 16511 10661 -6029 2691 -3797 C ATOM 2476 CD GLN A 325 21.777 38.121 -0.497 1.00124.87 C ANISOU 2476 CD GLN A 325 16705 18623 12118 -6243 2662 -3688 C ATOM 2477 OE1 GLN A 325 20.920 37.481 -1.106 1.00127.84 O ANISOU 2477 OE1 GLN A 325 17090 18860 12624 -6002 2726 -3558 O ATOM 2478 NE2 GLN A 325 21.999 37.966 0.804 1.00132.32 N ANISOU 2478 NE2 GLN A 325 17752 19959 12562 -6726 2558 -3733 N ATOM 2479 N ASP A 326 25.210 39.097 -3.884 1.00103.71 N ANISOU 2479 N ASP A 326 13595 15082 10726 -5196 2260 -3137 N ATOM 2480 CA ASP A 326 26.634 38.827 -3.715 1.00104.75 C ANISOU 2480 CA ASP A 326 13646 15329 10825 -5263 1941 -2890 C ATOM 2481 C ASP A 326 27.482 39.986 -4.222 1.00104.76 C ANISOU 2481 C ASP A 326 13517 15166 11122 -5199 2023 -3043 C ATOM 2482 O ASP A 326 28.533 40.296 -3.647 1.00107.02 O ANISOU 2482 O ASP A 326 13742 15609 11310 -5424 1850 -3038 O ATOM 2483 CB ASP A 326 27.013 37.533 -4.433 1.00102.73 C ANISOU 2483 CB ASP A 326 13342 14997 10693 -4969 1684 -2451 C ATOM 2484 CG ASP A 326 26.317 36.317 -3.853 1.00103.23 C ANISOU 2484 CG ASP A 326 13536 15223 10464 -5070 1541 -2249 C ATOM 2485 OD1 ASP A 326 25.849 36.390 -2.698 1.00107.31 O ANISOU 2485 OD1 ASP A 326 14173 16002 10598 -5448 1563 -2389 O ATOM 2486 OD2 ASP A 326 26.239 35.285 -4.553 1.00104.30 O ANISOU 2486 OD2 ASP A 326 13657 15228 10746 -4791 1410 -1957 O ATOM 2487 N ALA A 327 27.044 40.639 -5.298 1.00102.50 N ANISOU 2487 N ALA A 327 13184 14564 11197 -4912 2268 -3162 N ATOM 2488 CA ALA A 327 27.777 41.789 -5.805 1.00102.72 C ANISOU 2488 CA ALA A 327 13100 14417 11514 -4874 2355 -3298 C ATOM 2489 C ALA A 327 27.591 43.021 -4.939 1.00105.52 C ANISOU 2489 C ALA A 327 13489 14815 11790 -5193 2536 -3726 C ATOM 2490 O ALA A 327 28.292 44.015 -5.150 1.00106.41 O ANISOU 2490 O ALA A 327 13516 14808 12108 -5237 2577 -3852 O ATOM 2491 CB ALA A 327 27.350 42.104 -7.237 1.00 99.82 C ANISOU 2491 CB ALA A 327 12686 13698 11545 -4498 2535 -3258 C ATOM 2492 N GLY A 328 26.666 42.987 -3.986 1.00110.33 N ANISOU 2492 N GLY A 328 16731 12682 12509 -4311 953 -4454 N ATOM 2493 CA GLY A 328 26.423 44.144 -3.151 1.00113.90 C ANISOU 2493 CA GLY A 328 17330 13051 12898 -4533 1220 -4877 C ATOM 2494 C GLY A 328 25.790 45.302 -3.884 1.00113.58 C ANISOU 2494 C GLY A 328 17123 12710 13322 -4295 1641 -5036 C ATOM 2495 O GLY A 328 25.991 46.456 -3.499 1.00116.54 O ANISOU 2495 O GLY A 328 17529 12887 13865 -4415 1776 -5371 O ATOM 2496 N LEU A 329 25.028 45.025 -4.934 1.00110.43 N ANISOU 2496 N LEU A 329 16555 12243 13159 -3969 1810 -4799 N ATOM 2497 CA LEU A 329 24.441 46.060 -5.765 1.00110.24 C ANISOU 2497 CA LEU A 329 16365 11892 13629 -3730 2118 -4861 C ATOM 2498 C LEU A 329 22.923 45.995 -5.693 1.00110.35 C ANISOU 2498 C LEU A 329 16384 11925 13619 -3591 2449 -4994 C ATOM 2499 O LEU A 329 22.335 45.022 -5.218 1.00109.81 O ANISOU 2499 O LEU A 329 16419 12156 13147 -3663 2453 -4951 O ATOM 2500 CB LEU A 329 24.907 45.918 -7.218 1.00107.00 C ANISOU 2500 CB LEU A 329 15718 11369 13568 -3480 2011 -4449 C ATOM 2501 CG LEU A 329 26.405 46.044 -7.492 1.00107.16 C ANISOU 2501 CG LEU A 329 15636 11385 13695 -3598 1735 -4329 C ATOM 2502 CD1 LEU A 329 26.690 45.823 -8.965 1.00104.41 C ANISOU 2502 CD1 LEU A 329 15036 11018 13617 -3378 1707 -3958 C ATOM 2503 CD2 LEU A 329 26.920 47.402 -7.050 1.00110.72 C ANISOU 2503 CD2 LEU A 329 16127 11566 14377 -3795 1789 -4617 C ATOM 2504 N SER A 330 22.296 47.063 -6.165 1.00111.55 N ANISOU 2504 N SER A 330 16409 11736 14238 -3409 2703 -5156 N ATOM 2505 CA SER A 330 20.861 47.117 -6.382 1.00111.68 C ANISOU 2505 CA SER A 330 16330 11695 14410 -3195 3000 -5261 C ATOM 2506 C SER A 330 20.584 47.126 -7.877 1.00108.62 C ANISOU 2506 C SER A 330 15741 11079 14450 -2863 2963 -4841 C ATOM 2507 O SER A 330 21.485 47.322 -8.695 1.00107.18 O ANISOU 2507 O SER A 330 15496 10766 14462 -2832 2769 -4544 O ATOM 2508 CB SER A 330 20.248 48.353 -5.717 1.00116.41 C ANISOU 2508 CB SER A 330 16912 12042 15275 -3225 3286 -5834 C ATOM 2509 OG SER A 330 18.925 48.564 -6.180 1.00116.76 O ANISOU 2509 OG SER A 330 16773 11931 15661 -2946 3536 -5919 O ATOM 2510 N VAL A 331 19.313 46.910 -8.227 1.00108.04 N ANISOU 2510 N VAL A 331 15559 10989 14502 -2645 3155 -4827 N ATOM 2511 CA VAL A 331 18.915 46.891 -9.632 1.00105.54 C ANISOU 2511 CA VAL A 331 15071 10471 14557 -2348 3103 -4426 C ATOM 2512 C VAL A 331 19.275 48.202 -10.319 1.00107.37 C ANISOU 2512 C VAL A 331 15223 10229 15345 -2279 3050 -4389 C ATOM 2513 O VAL A 331 19.647 48.215 -11.500 1.00109.54 O ANISOU 2513 O VAL A 331 15423 10394 15802 -2187 2892 -3960 O ATOM 2514 CB VAL A 331 17.409 46.579 -9.742 1.00114.24 C ANISOU 2514 CB VAL A 331 16055 11601 15750 -2144 3316 -4493 C ATOM 2515 CG1 VAL A 331 16.852 47.053 -11.070 1.00121.86 C ANISOU 2515 CG1 VAL A 331 16842 12213 17248 -1846 3272 -4202 C ATOM 2516 CG2 VAL A 331 17.168 45.091 -9.572 1.00115.07 C ANISOU 2516 CG2 VAL A 331 16227 12150 15345 -2196 3262 -4283 C ATOM 2517 N SER A 332 19.198 49.317 -9.594 1.00111.55 N ANISOU 2517 N SER A 332 15774 10476 16134 -2358 3164 -4838 N ATOM 2518 CA SER A 332 19.491 50.621 -10.168 1.00114.08 C ANISOU 2518 CA SER A 332 16036 10275 17033 -2320 3067 -4812 C ATOM 2519 C SER A 332 20.980 50.866 -10.375 1.00113.69 C ANISOU 2519 C SER A 332 16066 10223 16909 -2556 2845 -4596 C ATOM 2520 O SER A 332 21.338 51.827 -11.061 1.00115.44 O ANISOU 2520 O SER A 332 16246 10048 17569 -2575 2718 -4429 O ATOM 2521 CB SER A 332 18.911 51.722 -9.281 1.00119.25 C ANISOU 2521 CB SER A 332 16670 10599 18041 -2312 3240 -5432 C ATOM 2522 OG SER A 332 19.449 51.651 -7.974 1.00121.01 O ANISOU 2522 OG SER A 332 17048 11085 17846 -2588 3325 -5864 O ATOM 2523 N ASP A 333 21.850 50.035 -9.800 1.00111.93 N ANISOU 2523 N ASP A 333 15942 10418 16169 -2755 2769 -4588 N ATOM 2524 CA ASP A 333 23.285 50.177 -10.019 1.00115.94 C ANISOU 2524 CA ASP A 333 16463 10966 16624 -2971 2554 -4399 C ATOM 2525 C ASP A 333 23.747 49.570 -11.336 1.00113.44 C ANISOU 2525 C ASP A 333 16016 10800 16284 -2896 2421 -3861 C ATOM 2526 O ASP A 333 24.870 49.850 -11.766 1.00124.84 O ANISOU 2526 O ASP A 333 17402 12248 17783 -3069 2279 -3684 O ATOM 2527 CB ASP A 333 24.067 49.533 -8.873 1.00128.26 C ANISOU 2527 CB ASP A 333 18154 12888 17690 -3210 2465 -4618 C ATOM 2528 CG ASP A 333 23.617 50.020 -7.515 1.00145.09 C ANISOU 2528 CG ASP A 333 20437 14977 19713 -3344 2618 -5178 C ATOM 2529 OD1 ASP A 333 22.868 51.014 -7.463 1.00149.05 O ANISOU 2529 OD1 ASP A 333 20904 15115 20614 -3244 2789 -5459 O ATOM 2530 OD2 ASP A 333 24.012 49.411 -6.499 1.00155.48 O ANISOU 2530 OD2 ASP A 333 21901 16622 20552 -3561 2549 -5352 O ATOM 2531 N ILE A 334 22.919 48.750 -11.975 1.00105.56 N ANISOU 2531 N ILE A 334 14958 9953 15197 -2666 2475 -3628 N ATOM 2532 CA ILE A 334 23.283 48.086 -13.222 1.00102.70 C ANISOU 2532 CA ILE A 334 14473 9786 14764 -2594 2369 -3175 C ATOM 2533 C ILE A 334 23.154 49.093 -14.359 1.00104.30 C ANISOU 2533 C ILE A 334 14603 9633 15392 -2583 2351 -2891 C ATOM 2534 O ILE A 334 22.050 49.534 -14.685 1.00105.17 O ANISOU 2534 O ILE A 334 14711 9448 15799 -2406 2413 -2855 O ATOM 2535 CB ILE A 334 22.408 46.854 -13.470 1.00 99.49 C ANISOU 2535 CB ILE A 334 14045 9645 14111 -2368 2406 -3046 C ATOM 2536 CG1 ILE A 334 22.593 45.845 -12.337 1.00 98.52 C ANISOU 2536 CG1 ILE A 334 14024 9853 13554 -2444 2357 -3263 C ATOM 2537 CG2 ILE A 334 22.742 46.219 -14.803 1.00 97.07 C ANISOU 2537 CG2 ILE A 334 13606 9531 13744 -2288 2308 -2637 C ATOM 2538 CD1 ILE A 334 24.021 45.371 -12.168 1.00 98.11 C ANISOU 2538 CD1 ILE A 334 13946 10040 13292 -2619 2137 -3229 C ATOM 2539 N ASP A 335 24.284 49.459 -14.969 1.00107.79 N ANISOU 2539 N ASP A 335 14977 10104 15873 -2799 2243 -2678 N ATOM 2540 CA ASP A 335 24.238 50.439 -16.049 1.00111.86 C ANISOU 2540 CA ASP A 335 15460 10295 16746 -2882 2185 -2347 C ATOM 2541 C ASP A 335 23.707 49.821 -17.340 1.00107.69 C ANISOU 2541 C ASP A 335 14856 9935 16125 -2741 2177 -1933 C ATOM 2542 O ASP A 335 22.964 50.473 -18.082 1.00106.82 O ANISOU 2542 O ASP A 335 14771 9489 16325 -2687 2124 -1685 O ATOM 2543 CB ASP A 335 25.618 51.065 -16.267 1.00113.54 C ANISOU 2543 CB ASP A 335 15619 10522 16999 -3232 2091 -2247 C ATOM 2544 CG ASP A 335 25.912 52.206 -15.289 1.00117.28 C ANISOU 2544 CG ASP A 335 16196 10594 17770 -3398 2048 -2572 C ATOM 2545 OD1 ASP A 335 25.244 53.261 -15.367 1.00118.67 O ANISOU 2545 OD1 ASP A 335 16449 10249 18393 -3368 2007 -2579 O ATOM 2546 OD2 ASP A 335 26.828 52.056 -14.454 1.00120.53 O ANISOU 2546 OD2 ASP A 335 16605 11192 17999 -3559 2022 -2831 O ATOM 2547 N ASP A 336 24.060 48.567 -17.629 1.00102.01 N ANISOU 2547 N ASP A 336 14046 9709 15006 -2679 2192 -1864 N ATOM 2548 CA ASP A 336 23.564 47.925 -18.843 1.00100.20 C ANISOU 2548 CA ASP A 336 13748 9669 14653 -2552 2185 -1519 C ATOM 2549 C ASP A 336 23.265 46.457 -18.585 1.00 96.53 C ANISOU 2549 C ASP A 336 13246 9581 13849 -2322 2207 -1637 C ATOM 2550 O ASP A 336 23.912 45.816 -17.757 1.00106.82 O ANISOU 2550 O ASP A 336 14532 11114 14941 -2346 2179 -1886 O ATOM 2551 CB ASP A 336 24.563 48.055 -19.998 1.00101.38 C ANISOU 2551 CB ASP A 336 13777 10055 14688 -2816 2151 -1208 C ATOM 2552 CG ASP A 336 24.319 49.288 -20.840 1.00104.83 C ANISOU 2552 CG ASP A 336 14284 10117 15430 -3010 2077 -853 C ATOM 2553 OD1 ASP A 336 23.152 49.729 -20.925 1.00105.49 O ANISOU 2553 OD1 ASP A 336 14473 9806 15803 -2834 2020 -762 O ATOM 2554 OD2 ASP A 336 25.293 49.813 -21.419 1.00107.30 O ANISOU 2554 OD2 ASP A 336 14534 10525 15711 -3355 2053 -660 O ATOM 2555 N VAL A 337 22.271 45.931 -19.301 1.00 94.91 N ANISOU 2555 N VAL A 337 13037 9410 13615 -2114 2211 -1437 N ATOM 2556 CA VAL A 337 21.923 44.514 -19.257 1.00 91.70 C ANISOU 2556 CA VAL A 337 12595 9332 12915 -1908 2193 -1486 C ATOM 2557 C VAL A 337 21.925 43.994 -20.686 1.00 90.86 C ANISOU 2557 C VAL A 337 12389 9465 12669 -1876 2153 -1172 C ATOM 2558 O VAL A 337 21.390 44.652 -21.585 1.00 92.27 O ANISOU 2558 O VAL A 337 12594 9457 13009 -1907 2144 -884 O ATOM 2559 CB VAL A 337 20.558 44.275 -18.578 1.00 90.79 C ANISOU 2559 CB VAL A 337 12570 9048 12876 -1688 2250 -1615 C ATOM 2560 CG1 VAL A 337 19.474 45.129 -19.219 1.00 92.38 C ANISOU 2560 CG1 VAL A 337 12785 8883 13434 -1591 2271 -1423 C ATOM 2561 CG2 VAL A 337 20.183 42.803 -18.627 1.00 87.80 C ANISOU 2561 CG2 VAL A 337 12167 8987 12205 -1515 2193 -1602 C ATOM 2562 N ILE A 338 22.552 42.837 -20.908 1.00 89.11 N ANISOU 2562 N ILE A 338 12051 9648 12161 -1831 2101 -1241 N ATOM 2563 CA ILE A 338 22.671 42.271 -22.247 1.00 88.78 C ANISOU 2563 CA ILE A 338 11889 9903 11939 -1820 2085 -1034 C ATOM 2564 C ILE A 338 22.234 40.813 -22.237 1.00 86.04 C ANISOU 2564 C ILE A 338 11507 9780 11403 -1561 1994 -1130 C ATOM 2565 O ILE A 338 22.487 40.074 -21.278 1.00 84.79 O ANISOU 2565 O ILE A 338 11350 9685 11179 -1475 1905 -1372 O ATOM 2566 CB ILE A 338 24.101 42.390 -22.813 1.00 90.64 C ANISOU 2566 CB ILE A 338 11936 10456 12048 -2070 2120 -1063 C ATOM 2567 CG1 ILE A 338 25.113 41.689 -21.909 1.00 90.02 C ANISOU 2567 CG1 ILE A 338 11730 10574 11900 -2046 2046 -1415 C ATOM 2568 CG2 ILE A 338 24.468 43.842 -23.017 1.00 93.80 C ANISOU 2568 CG2 ILE A 338 12383 10628 12628 -2379 2184 -884 C ATOM 2569 CD1 ILE A 338 26.519 41.704 -22.464 1.00 92.18 C ANISOU 2569 CD1 ILE A 338 11738 11200 12088 -2265 2088 -1510 C ATOM 2570 N LEU A 339 21.582 40.405 -23.320 1.00 85.49 N ANISOU 2570 N LEU A 339 11422 9817 11245 -1464 1978 -921 N ATOM 2571 CA LEU A 339 21.043 39.064 -23.464 1.00 83.23 C ANISOU 2571 CA LEU A 339 11111 9701 10811 -1224 1869 -978 C ATOM 2572 C LEU A 339 21.930 38.249 -24.392 1.00 83.64 C ANISOU 2572 C LEU A 339 10963 10174 10644 -1238 1832 -1067 C ATOM 2573 O LEU A 339 22.359 38.729 -25.444 1.00 85.64 O ANISOU 2573 O LEU A 339 11133 10611 10797 -1424 1930 -932 O ATOM 2574 CB LEU A 339 19.614 39.117 -24.007 1.00 82.62 C ANISOU 2574 CB LEU A 339 11139 9444 10808 -1089 1856 -724 C ATOM 2575 CG LEU A 339 18.641 39.935 -23.154 1.00 82.88 C ANISOU 2575 CG LEU A 339 11304 9069 11119 -1045 1912 -701 C ATOM 2576 CD1 LEU A 339 17.270 39.971 -23.787 1.00 82.78 C ANISOU 2576 CD1 LEU A 339 11331 8888 11234 -900 1871 -464 C ATOM 2577 CD2 LEU A 339 18.562 39.356 -21.757 1.00 81.51 C ANISOU 2577 CD2 LEU A 339 11180 8877 10915 -970 1903 -982 C ATOM 2578 N VAL A 340 22.212 37.017 -23.988 1.00 82.29 N ANISOU 2578 N VAL A 340 10709 10156 10403 -1064 1678 -1311 N ATOM 2579 CA VAL A 340 23.084 36.117 -24.730 1.00 83.10 C ANISOU 2579 CA VAL A 340 10569 10637 10368 -1021 1617 -1518 C ATOM 2580 C VAL A 340 22.419 34.752 -24.774 1.00 81.30 C ANISOU 2580 C VAL A 340 10359 10431 10101 -747 1404 -1593 C ATOM 2581 O VAL A 340 21.800 34.325 -23.795 1.00 79.62 O ANISOU 2581 O VAL A 340 10299 9986 9965 -631 1257 -1586 O ATOM 2582 CB VAL A 340 24.480 36.023 -24.083 1.00 84.39 C ANISOU 2582 CB VAL A 340 10540 10926 10598 -1099 1561 -1827 C ATOM 2583 CG1 VAL A 340 25.336 34.979 -24.785 1.00 85.68 C ANISOU 2583 CG1 VAL A 340 10391 11465 10699 -996 1474 -2133 C ATOM 2584 CG2 VAL A 340 25.162 37.369 -24.110 1.00 86.49 C ANISOU 2584 CG2 VAL A 340 10777 11180 10905 -1402 1764 -1746 C ATOM 2585 N GLY A 341 22.543 34.066 -25.908 1.00 82.08 N ANISOU 2585 N GLY A 341 10302 10822 10062 -675 1388 -1674 N ATOM 2586 CA GLY A 341 21.934 32.760 -26.062 1.00 80.79 C ANISOU 2586 CA GLY A 341 10148 10665 9886 -420 1160 -1758 C ATOM 2587 C GLY A 341 20.679 32.801 -26.903 1.00 80.04 C ANISOU 2587 C GLY A 341 10197 10528 9686 -381 1201 -1470 C ATOM 2588 O GLY A 341 19.921 33.774 -26.843 1.00 79.65 O ANISOU 2588 O GLY A 341 10318 10270 9677 -483 1327 -1164 O ATOM 2589 N GLY A 342 20.448 31.757 -27.699 1.00 80.21 N ANISOU 2589 N GLY A 342 10139 10729 9610 -227 1068 -1586 N ATOM 2590 CA GLY A 342 19.300 31.770 -28.587 1.00 79.89 C ANISOU 2590 CA GLY A 342 10223 10676 9454 -207 1077 -1316 C ATOM 2591 C GLY A 342 17.983 31.837 -27.840 1.00 77.65 C ANISOU 2591 C GLY A 342 10159 10016 9328 -114 988 -1051 C ATOM 2592 O GLY A 342 17.036 32.483 -28.293 1.00 77.66 O ANISOU 2592 O GLY A 342 10277 9898 9334 -165 1057 -743 O ATOM 2593 N GLN A 343 17.908 31.189 -26.676 1.00 76.21 N ANISOU 2593 N GLN A 343 10022 9649 9283 -1 822 -1168 N ATOM 2594 CA GLN A 343 16.643 31.132 -25.956 1.00 74.62 C ANISOU 2594 CA GLN A 343 9994 9166 9192 51 765 -963 C ATOM 2595 C GLN A 343 16.196 32.501 -25.459 1.00 74.71 C ANISOU 2595 C GLN A 343 10103 8967 9315 -82 999 -770 C ATOM 2596 O GLN A 343 15.004 32.692 -25.202 1.00 74.14 O ANISOU 2596 O GLN A 343 10117 8699 9352 -45 1022 -598 O ATOM 2597 CB GLN A 343 16.746 30.150 -24.793 1.00 73.80 C ANISOU 2597 CB GLN A 343 9937 8952 9149 115 527 -1109 C ATOM 2598 CG GLN A 343 15.414 29.784 -24.157 1.00 72.69 C ANISOU 2598 CG GLN A 343 9946 8612 9062 135 450 -927 C ATOM 2599 CD GLN A 343 14.424 29.199 -25.144 1.00 72.38 C ANISOU 2599 CD GLN A 343 9898 8594 9010 258 349 -789 C ATOM 2600 OE1 GLN A 343 14.511 28.028 -25.507 1.00 74.55 O ANISOU 2600 OE1 GLN A 343 10136 8930 9259 374 80 -895 O ATOM 2601 NE2 GLN A 343 13.466 30.010 -25.573 1.00 72.37 N ANISOU 2601 NE2 GLN A 343 9922 8514 9062 237 526 -562 N ATOM 2602 N THR A 344 17.114 33.460 -25.319 1.00 75.80 N ANISOU 2602 N THR A 344 10204 9132 9465 -234 1164 -824 N ATOM 2603 CA THR A 344 16.704 34.807 -24.940 1.00 76.45 C ANISOU 2603 CA THR A 344 10370 8971 9705 -350 1353 -667 C ATOM 2604 C THR A 344 15.991 35.537 -26.066 1.00 77.60 C ANISOU 2604 C THR A 344 10536 9050 9897 -382 1405 -371 C ATOM 2605 O THR A 344 15.505 36.649 -25.845 1.00 78.60 O ANISOU 2605 O THR A 344 10722 8907 10236 -444 1503 -227 O ATOM 2606 CB THR A 344 17.908 35.631 -24.487 1.00 77.64 C ANISOU 2606 CB THR A 344 10484 9140 9874 -527 1476 -797 C ATOM 2607 OG1 THR A 344 18.783 35.851 -25.597 1.00 79.20 O ANISOU 2607 OG1 THR A 344 10561 9594 9936 -644 1528 -776 O ATOM 2608 CG2 THR A 344 18.670 34.914 -23.397 1.00 76.97 C ANISOU 2608 CG2 THR A 344 10381 9113 9751 -512 1362 -1069 C ATOM 2609 N ARG A 345 15.920 34.955 -27.262 1.00 77.95 N ANISOU 2609 N ARG A 345 10536 9320 9760 -351 1313 -287 N ATOM 2610 CA ARG A 345 15.134 35.561 -28.325 1.00 79.36 C ANISOU 2610 CA ARG A 345 10768 9429 9958 -404 1292 41 C ATOM 2611 C ARG A 345 13.641 35.482 -28.052 1.00 78.53 C ANISOU 2611 C ARG A 345 10717 9038 10083 -239 1202 193 C ATOM 2612 O ARG A 345 12.870 36.168 -28.728 1.00 80.04 O ANISOU 2612 O ARG A 345 10946 9061 10404 -267 1147 480 O ATOM 2613 CB ARG A 345 15.438 34.896 -29.670 1.00 80.38 C ANISOU 2613 CB ARG A 345 10845 9927 9770 -448 1217 58 C ATOM 2614 CG ARG A 345 16.866 35.085 -30.167 1.00 82.23 C ANISOU 2614 CG ARG A 345 10970 10513 9762 -658 1350 -96 C ATOM 2615 CD ARG A 345 17.116 34.330 -31.467 1.00 83.76 C ANISOU 2615 CD ARG A 345 11084 11133 9610 -705 1310 -171 C ATOM 2616 NE ARG A 345 18.499 34.454 -31.924 1.00 86.08 N ANISOU 2616 NE ARG A 345 11211 11830 9666 -921 1481 -392 N ATOM 2617 CZ ARG A 345 18.944 35.446 -32.689 1.00105.28 C ANISOU 2617 CZ ARG A 345 13662 14433 11907 -1271 1624 -172 C ATOM 2618 NH1 ARG A 345 18.115 36.402 -33.085 1.00118.36 N ANISOU 2618 NH1 ARG A 345 15519 15835 13616 -1422 1558 298 N ATOM 2619 NH2 ARG A 345 20.217 35.484 -33.058 1.00125.40 N ANISOU 2619 NH2 ARG A 345 16014 17399 14232 -1488 1809 -418 N ATOM 2620 N MET A 346 13.218 34.667 -27.098 1.00 76.65 N ANISOU 2620 N MET A 346 10473 8746 9906 -95 1165 19 N ATOM 2621 CA MET A 346 11.797 34.530 -26.824 1.00 76.26 C ANISOU 2621 CA MET A 346 10428 8481 10064 32 1110 130 C ATOM 2622 C MET A 346 11.274 35.823 -26.216 1.00 77.62 C ANISOU 2622 C MET A 346 10596 8326 10570 2 1257 181 C ATOM 2623 O MET A 346 11.873 36.341 -25.271 1.00 77.75 O ANISOU 2623 O MET A 346 10630 8275 10637 -78 1408 -3 O ATOM 2624 CB MET A 346 11.532 33.364 -25.882 1.00 74.51 C ANISOU 2624 CB MET A 346 10210 8311 9789 115 1042 -54 C ATOM 2625 CG MET A 346 10.058 33.094 -25.647 1.00 74.44 C ANISOU 2625 CG MET A 346 10170 8151 9962 208 1001 47 C ATOM 2626 SD MET A 346 9.752 32.028 -24.232 1.00 73.32 S ANISOU 2626 SD MET A 346 10062 8047 9750 177 975 -135 S ATOM 2627 CE MET A 346 7.970 32.034 -24.220 1.00 74.17 C ANISOU 2627 CE MET A 346 10063 8009 10109 245 996 3 C ATOM 2628 N PRO A 347 10.172 36.369 -26.723 1.00 79.05 N ANISOU 2628 N PRO A 347 10740 8281 11014 70 1192 398 N ATOM 2629 CA PRO A 347 9.667 37.640 -26.184 1.00 81.07 C ANISOU 2629 CA PRO A 347 10950 8174 11679 76 1299 392 C ATOM 2630 C PRO A 347 9.444 37.628 -24.684 1.00 80.63 C ANISOU 2630 C PRO A 347 10848 8051 11736 101 1504 64 C ATOM 2631 O PRO A 347 9.721 38.628 -24.009 1.00 82.10 O ANISOU 2631 O PRO A 347 11030 8040 12124 43 1652 -86 O ATOM 2632 CB PRO A 347 8.354 37.826 -26.948 1.00 82.63 C ANISOU 2632 CB PRO A 347 11070 8165 12162 199 1122 643 C ATOM 2633 CG PRO A 347 8.560 37.102 -28.211 1.00 82.07 C ANISOU 2633 CG PRO A 347 11071 8351 11761 160 922 876 C ATOM 2634 CD PRO A 347 9.387 35.906 -27.873 1.00 79.43 C ANISOU 2634 CD PRO A 347 10775 8374 11030 142 981 648 C ATOM 2635 N MET A 348 8.956 36.517 -24.140 1.00 79.05 N ANISOU 2635 N MET A 348 10623 8020 11392 151 1505 -52 N ATOM 2636 CA MET A 348 8.662 36.480 -22.716 1.00 79.29 C ANISOU 2636 CA MET A 348 10623 8043 11460 104 1706 -343 C ATOM 2637 C MET A 348 9.925 36.634 -21.879 1.00 78.80 C ANISOU 2637 C MET A 348 10678 8081 11181 -51 1810 -548 C ATOM 2638 O MET A 348 9.914 37.320 -20.853 1.00 80.22 O ANISOU 2638 O MET A 348 10849 8158 11471 -129 2009 -788 O ATOM 2639 CB MET A 348 7.949 35.184 -22.368 1.00 78.09 C ANISOU 2639 CB MET A 348 10451 8080 11141 115 1643 -358 C ATOM 2640 CG MET A 348 7.751 35.011 -20.892 1.00 89.44 C ANISOU 2640 CG MET A 348 11894 9600 12490 -27 1842 -630 C ATOM 2641 SD MET A 348 6.993 33.443 -20.493 1.00 89.53 S ANISOU 2641 SD MET A 348 11915 9838 12263 -103 1721 -577 S ATOM 2642 CE MET A 348 7.034 33.546 -18.715 1.00 97.95 C ANISOU 2642 CE MET A 348 13038 11037 13140 -379 1987 -889 C ATOM 2643 N VAL A 349 11.024 36.005 -22.297 1.00 77.20 N ANISOU 2643 N VAL A 349 10565 8083 10685 -99 1672 -493 N ATOM 2644 CA VAL A 349 12.271 36.131 -21.547 1.00 77.02 C ANISOU 2644 CA VAL A 349 10623 8149 10491 -242 1724 -683 C ATOM 2645 C VAL A 349 12.734 37.580 -21.526 1.00 78.85 C ANISOU 2645 C VAL A 349 10850 8172 10937 -316 1869 -722 C ATOM 2646 O VAL A 349 13.107 38.118 -20.474 1.00 79.79 O ANISOU 2646 O VAL A 349 11010 8226 11080 -428 2006 -951 O ATOM 2647 CB VAL A 349 13.344 35.203 -22.141 1.00 75.58 C ANISOU 2647 CB VAL A 349 10465 8213 10039 -244 1529 -651 C ATOM 2648 CG1 VAL A 349 14.670 35.431 -21.459 1.00 75.84 C ANISOU 2648 CG1 VAL A 349 10537 8317 9961 -382 1555 -841 C ATOM 2649 CG2 VAL A 349 12.919 33.759 -21.994 1.00 74.23 C ANISOU 2649 CG2 VAL A 349 10316 8180 9709 -178 1336 -646 C ATOM 2650 N GLN A 350 12.708 38.238 -22.685 1.00 79.79 N ANISOU 2650 N GLN A 350 10935 8176 11206 -284 1812 -487 N ATOM 2651 CA GLN A 350 13.096 39.641 -22.747 1.00 82.06 C ANISOU 2651 CA GLN A 350 11231 8209 11739 -380 1889 -466 C ATOM 2652 C GLN A 350 12.196 40.496 -21.869 1.00 84.06 C ANISOU 2652 C GLN A 350 11433 8139 12367 -322 2030 -655 C ATOM 2653 O GLN A 350 12.662 41.443 -21.226 1.00 87.80 O ANISOU 2653 O GLN A 350 11931 8431 12997 -420 2139 -836 O ATOM 2654 CB GLN A 350 13.059 40.134 -24.193 1.00 83.34 C ANISOU 2654 CB GLN A 350 11390 8296 11979 -402 1748 -109 C ATOM 2655 CG GLN A 350 13.991 39.389 -25.130 1.00 82.22 C ANISOU 2655 CG GLN A 350 11266 8526 11448 -492 1660 11 C ATOM 2656 CD GLN A 350 13.916 39.893 -26.558 1.00 84.92 C ANISOU 2656 CD GLN A 350 11631 8853 11783 -592 1533 376 C ATOM 2657 OE1 GLN A 350 12.925 40.500 -26.964 1.00 89.03 O ANISOU 2657 OE1 GLN A 350 12159 9075 12593 -533 1425 600 O ATOM 2658 NE2 GLN A 350 14.969 39.644 -27.330 1.00 88.60 N ANISOU 2658 NE2 GLN A 350 12095 9654 11917 -765 1531 430 N ATOM 2659 N LYS A 351 10.903 40.174 -21.817 1.00 88.20 N ANISOU 2659 N LYS A 351 11860 8596 13056 -168 2036 -659 N ATOM 2660 CA LYS A 351 9.987 40.978 -21.017 1.00 88.48 C ANISOU 2660 CA LYS A 351 11777 8351 13489 -96 2197 -914 C ATOM 2661 C LYS A 351 10.244 40.792 -19.527 1.00 86.87 C ANISOU 2661 C LYS A 351 11611 8305 13090 -221 2428 -1316 C ATOM 2662 O LYS A 351 10.314 41.768 -18.775 1.00 89.93 O ANISOU 2662 O LYS A 351 11974 8491 13702 -268 2585 -1604 O ATOM 2663 CB LYS A 351 8.541 40.634 -21.360 1.00 97.85 C ANISOU 2663 CB LYS A 351 12797 9469 14911 88 2152 -838 C ATOM 2664 CG LYS A 351 7.528 41.477 -20.609 1.00107.01 C ANISOU 2664 CG LYS A 351 13756 10349 16552 190 2329 -1163 C ATOM 2665 CD LYS A 351 6.103 41.171 -21.038 1.00110.44 C ANISOU 2665 CD LYS A 351 13970 10709 17281 378 2261 -1086 C ATOM 2666 CE LYS A 351 5.108 42.024 -20.267 1.00111.95 C ANISOU 2666 CE LYS A 351 13890 10640 18008 496 2461 -1497 C ATOM 2667 NZ LYS A 351 3.700 41.771 -20.679 1.00112.12 N ANISOU 2667 NZ LYS A 351 13635 10581 18384 688 2388 -1451 N ATOM 2668 N LYS A 352 10.388 39.543 -19.082 1.00 84.60 N ANISOU 2668 N LYS A 352 11397 8365 12381 -298 2418 -1338 N ATOM 2669 CA LYS A 352 10.619 39.292 -17.664 1.00 85.09 C ANISOU 2669 CA LYS A 352 11534 8607 12188 -481 2588 -1663 C ATOM 2670 C LYS A 352 11.943 39.883 -17.204 1.00 85.44 C ANISOU 2670 C LYS A 352 11710 8631 12124 -637 2599 -1793 C ATOM 2671 O LYS A 352 12.021 40.468 -16.120 1.00 87.55 O ANISOU 2671 O LYS A 352 12004 8862 12398 -768 2785 -2126 O ATOM 2672 CB LYS A 352 10.577 37.794 -17.379 1.00 82.96 C ANISOU 2672 CB LYS A 352 11350 8670 11503 -564 2473 -1574 C ATOM 2673 CG LYS A 352 9.187 37.187 -17.428 1.00 83.30 C ANISOU 2673 CG LYS A 352 11263 8773 11614 -491 2515 -1531 C ATOM 2674 CD LYS A 352 8.710 36.790 -16.039 1.00 84.95 C ANISOU 2674 CD LYS A 352 11497 9203 11579 -722 2711 -1798 C ATOM 2675 CE LYS A 352 7.315 36.182 -16.075 1.00 85.73 C ANISOU 2675 CE LYS A 352 11430 9397 11745 -693 2776 -1760 C ATOM 2676 NZ LYS A 352 6.852 35.782 -14.715 1.00 87.98 N ANISOU 2676 NZ LYS A 352 11740 9964 11724 -1000 2994 -2010 N ATOM 2677 N VAL A 353 12.998 39.737 -18.008 1.00 83.79 N ANISOU 2677 N VAL A 353 11564 8468 11805 -646 2413 -1566 N ATOM 2678 CA VAL A 353 14.284 40.329 -17.643 1.00 84.40 C ANISOU 2678 CA VAL A 353 11726 8527 11816 -805 2413 -1679 C ATOM 2679 C VAL A 353 14.172 41.846 -17.604 1.00 87.30 C ANISOU 2679 C VAL A 353 12049 8531 12590 -808 2537 -1796 C ATOM 2680 O VAL A 353 14.585 42.499 -16.634 1.00 89.13 O ANISOU 2680 O VAL A 353 12335 8685 12846 -945 2654 -2093 O ATOM 2681 CB VAL A 353 15.384 39.872 -18.618 1.00 82.64 C ANISOU 2681 CB VAL A 353 11512 8463 11425 -818 2217 -1440 C ATOM 2682 CG1 VAL A 353 16.665 40.630 -18.352 1.00 83.80 C ANISOU 2682 CG1 VAL A 353 11694 8570 11574 -991 2228 -1545 C ATOM 2683 CG2 VAL A 353 15.617 38.381 -18.498 1.00 80.41 C ANISOU 2683 CG2 VAL A 353 11264 8486 10803 -804 2050 -1409 C ATOM 2684 N ALA A 354 13.596 42.425 -18.658 1.00 88.16 N ANISOU 2684 N ALA A 354 12070 8389 13040 -668 2472 -1561 N ATOM 2685 CA ALA A 354 13.465 43.874 -18.738 1.00 91.45 C ANISOU 2685 CA ALA A 354 12445 8377 13924 -660 2499 -1622 C ATOM 2686 C ALA A 354 12.659 44.430 -17.576 1.00 94.13 C ANISOU 2686 C ALA A 354 12706 8540 14518 -615 2714 -2070 C ATOM 2687 O ALA A 354 12.938 45.535 -17.099 1.00 97.03 O ANISOU 2687 O ALA A 354 13078 8619 15168 -675 2773 -2308 O ATOM 2688 CB ALA A 354 12.817 44.269 -20.063 1.00 92.36 C ANISOU 2688 CB ALA A 354 12487 8241 14364 -525 2320 -1248 C ATOM 2689 N GLU A 355 11.664 43.683 -17.105 1.00 93.65 N ANISOU 2689 N GLU A 355 12559 8663 14358 -530 2839 -2218 N ATOM 2690 CA GLU A 355 10.856 44.156 -15.992 1.00 96.78 C ANISOU 2690 CA GLU A 355 12840 8980 14952 -518 3099 -2705 C ATOM 2691 C GLU A 355 11.536 43.921 -14.653 1.00 97.04 C ANISOU 2691 C GLU A 355 13019 9296 14555 -776 3270 -3052 C ATOM 2692 O GLU A 355 11.301 44.683 -13.711 1.00100.48 O ANISOU 2692 O GLU A 355 13404 9625 15148 -836 3485 -3515 O ATOM 2693 CB GLU A 355 9.483 43.490 -16.019 1.00 96.87 C ANISOU 2693 CB GLU A 355 12667 9113 15025 -376 3191 -2735 C ATOM 2694 CG GLU A 355 8.609 43.950 -17.167 1.00106.79 C ANISOU 2694 CG GLU A 355 13738 10015 16820 -111 3021 -2487 C ATOM 2695 CD GLU A 355 7.175 43.505 -17.004 1.00125.29 C ANISOU 2695 CD GLU A 355 15833 12438 19334 29 3149 -2636 C ATOM 2696 OE1 GLU A 355 6.864 42.890 -15.962 1.00135.22 O ANISOU 2696 OE1 GLU A 355 17066 14042 20268 -114 3406 -2943 O ATOM 2697 OE2 GLU A 355 6.358 43.771 -17.910 1.00128.85 O ANISOU 2697 OE2 GLU A 355 16109 12615 20233 251 2977 -2433 O ATOM 2698 N PHE A 356 12.373 42.887 -14.540 1.00 93.96 N ANISOU 2698 N PHE A 356 12804 9254 13642 -934 3151 -2861 N ATOM 2699 CA PHE A 356 13.198 42.760 -13.345 1.00 94.58 C ANISOU 2699 CA PHE A 356 13052 9550 13333 -1206 3216 -3126 C ATOM 2700 C PHE A 356 14.129 43.954 -13.210 1.00 96.48 C ANISOU 2700 C PHE A 356 13345 9521 13792 -1282 3204 -3277 C ATOM 2701 O PHE A 356 14.224 44.561 -12.138 1.00 99.39 O ANISOU 2701 O PHE A 356 13759 9866 14141 -1434 3372 -3699 O ATOM 2702 CB PHE A 356 14.003 41.460 -13.372 1.00 91.34 C ANISOU 2702 CB PHE A 356 12797 9480 12427 -1329 2991 -2858 C ATOM 2703 CG PHE A 356 14.924 41.288 -12.183 1.00 92.24 C ANISOU 2703 CG PHE A 356 13100 9795 12152 -1624 2965 -3071 C ATOM 2704 CD1 PHE A 356 14.517 40.572 -11.072 1.00 93.33 C ANISOU 2704 CD1 PHE A 356 13346 10228 11885 -1848 3039 -3236 C ATOM 2705 CD2 PHE A 356 16.197 41.837 -12.179 1.00 92.41 C ANISOU 2705 CD2 PHE A 356 13193 9724 12195 -1716 2845 -3085 C ATOM 2706 CE1 PHE A 356 15.355 40.411 -9.985 1.00 94.62 C ANISOU 2706 CE1 PHE A 356 13711 10575 11665 -2155 2960 -3394 C ATOM 2707 CE2 PHE A 356 17.035 41.681 -11.092 1.00 93.53 C ANISOU 2707 CE2 PHE A 356 13504 10038 11997 -1991 2775 -3271 C ATOM 2708 CZ PHE A 356 16.614 40.966 -9.997 1.00 94.66 C ANISOU 2708 CZ PHE A 356 13778 10459 11728 -2209 2816 -3417 C ATOM 2709 N PHE A 357 14.836 44.304 -14.287 1.00 95.25 N ANISOU 2709 N PHE A 357 13187 9181 13823 -1213 3006 -2945 N ATOM 2710 CA PHE A 357 15.765 45.421 -14.186 1.00 97.29 C ANISOU 2710 CA PHE A 357 13496 9183 14286 -1331 2969 -3047 C ATOM 2711 C PHE A 357 15.102 46.772 -14.417 1.00100.89 C ANISOU 2711 C PHE A 357 13838 9140 15357 -1199 3026 -3189 C ATOM 2712 O PHE A 357 15.769 47.801 -14.249 1.00103.31 O ANISOU 2712 O PHE A 357 14188 9168 15896 -1307 2987 -3311 O ATOM 2713 CB PHE A 357 16.917 45.249 -15.173 1.00 95.19 C ANISOU 2713 CB PHE A 357 13267 8980 13923 -1392 2747 -2650 C ATOM 2714 CG PHE A 357 17.818 44.092 -14.862 1.00 92.60 C ANISOU 2714 CG PHE A 357 13020 9066 13098 -1519 2640 -2595 C ATOM 2715 CD1 PHE A 357 18.906 44.248 -14.024 1.00 93.50 C ANISOU 2715 CD1 PHE A 357 13229 9269 13029 -1742 2598 -2794 C ATOM 2716 CD2 PHE A 357 17.576 42.848 -15.407 1.00 89.67 C ANISOU 2716 CD2 PHE A 357 12623 8963 12486 -1410 2536 -2354 C ATOM 2717 CE1 PHE A 357 19.732 43.187 -13.739 1.00 91.66 C ANISOU 2717 CE1 PHE A 357 13048 9368 12413 -1840 2431 -2742 C ATOM 2718 CE2 PHE A 357 18.401 41.784 -15.123 1.00 87.88 C ANISOU 2718 CE2 PHE A 357 12451 9051 11888 -1500 2376 -2324 C ATOM 2719 CZ PHE A 357 19.480 41.955 -14.288 1.00 88.95 C ANISOU 2719 CZ PHE A 357 12666 9254 11876 -1709 2311 -2513 C ATOM 2720 N GLY A 358 13.816 46.795 -14.767 1.00101.73 N ANISOU 2720 N GLY A 358 13784 9099 15768 -971 3084 -3191 N ATOM 2721 CA GLY A 358 13.167 48.044 -15.125 1.00105.53 C ANISOU 2721 CA GLY A 358 14127 9041 16930 -805 3046 -3285 C ATOM 2722 C GLY A 358 13.868 48.782 -16.240 1.00105.97 C ANISOU 2722 C GLY A 358 14244 8763 17256 -844 2764 -2853 C ATOM 2723 O GLY A 358 13.855 50.017 -16.265 1.00114.36 O ANISOU 2723 O GLY A 358 15276 9331 18844 -829 2675 -2966 O ATOM 2724 N LYS A 359 14.496 48.054 -17.160 1.00102.56 N ANISOU 2724 N LYS A 359 13896 8600 16474 -920 2614 -2374 N ATOM 2725 CA LYS A 359 15.351 48.654 -18.172 1.00103.18 C ANISOU 2725 CA LYS A 359 14048 8500 16655 -1066 2388 -1961 C ATOM 2726 C LYS A 359 15.365 47.771 -19.412 1.00100.22 C ANISOU 2726 C LYS A 359 13676 8410 15992 -1044 2254 -1466 C ATOM 2727 O LYS A 359 15.254 46.547 -19.319 1.00 96.88 O ANISOU 2727 O LYS A 359 13243 8407 15159 -982 2329 -1472 O ATOM 2728 CB LYS A 359 16.774 48.848 -17.633 1.00103.08 C ANISOU 2728 CB LYS A 359 14150 8635 16381 -1342 2416 -2077 C ATOM 2729 CG LYS A 359 17.697 49.688 -18.485 1.00108.96 C ANISOU 2729 CG LYS A 359 14951 9173 17277 -1564 2224 -1730 C ATOM 2730 CD LYS A 359 18.753 50.339 -17.608 1.00113.36 C ANISOU 2730 CD LYS A 359 15578 9659 17834 -1797 2264 -2019 C ATOM 2731 CE LYS A 359 19.341 49.333 -16.634 1.00112.77 C ANISOU 2731 CE LYS A 359 15534 10073 17241 -1854 2414 -2310 C ATOM 2732 NZ LYS A 359 20.082 50.004 -15.540 1.00118.82 N ANISOU 2732 NZ LYS A 359 16372 10727 18046 -2045 2457 -2693 N ATOM 2733 N GLU A 360 15.506 48.396 -20.572 1.00101.90 N ANISOU 2733 N GLU A 360 13915 8391 16411 -1125 2034 -1039 N ATOM 2734 CA GLU A 360 15.477 47.606 -21.800 1.00 99.76 C ANISOU 2734 CA GLU A 360 13651 8413 15839 -1133 1915 -596 C ATOM 2735 C GLU A 360 16.873 47.098 -22.141 1.00 97.94 C ANISOU 2735 C GLU A 360 13474 8626 15115 -1386 1944 -471 C ATOM 2736 O GLU A 360 17.818 47.895 -22.193 1.00100.04 O ANISOU 2736 O GLU A 360 13787 8787 15437 -1639 1909 -413 O ATOM 2737 CB GLU A 360 14.933 48.435 -22.956 1.00115.98 C ANISOU 2737 CB GLU A 360 15722 10070 18275 -1151 1640 -158 C ATOM 2738 CG GLU A 360 13.417 48.439 -23.050 1.00129.77 C ANISOU 2738 CG GLU A 360 17354 11527 20424 -843 1552 -174 C ATOM 2739 CD GLU A 360 12.877 47.157 -23.649 1.00138.74 C ANISOU 2739 CD GLU A 360 18452 13070 21193 -714 1554 -1 C ATOM 2740 OE1 GLU A 360 13.666 46.418 -24.275 1.00144.31 O ANISOU 2740 OE1 GLU A 360 19233 14213 21385 -874 1560 211 O ATOM 2741 OE2 GLU A 360 11.667 46.886 -23.494 1.00139.63 O ANISOU 2741 OE2 GLU A 360 18437 13068 21549 -456 1551 -108 O ATOM 2742 N PRO A 361 17.041 45.798 -22.379 1.00 94.53 N ANISOU 2742 N PRO A 361 13009 8673 14234 -1327 1994 -452 N ATOM 2743 CA PRO A 361 18.363 45.285 -22.748 1.00 93.39 C ANISOU 2743 CA PRO A 361 12849 8953 13680 -1534 2015 -398 C ATOM 2744 C PRO A 361 18.837 45.873 -24.068 1.00 95.76 C ANISOU 2744 C PRO A 361 13167 9270 13949 -1787 1904 18 C ATOM 2745 O PRO A 361 18.051 46.353 -24.886 1.00 97.58 O ANISOU 2745 O PRO A 361 13446 9252 14377 -1777 1757 347 O ATOM 2746 CB PRO A 361 18.140 43.774 -22.862 1.00 89.91 C ANISOU 2746 CB PRO A 361 12354 8925 12881 -1355 2030 -459 C ATOM 2747 CG PRO A 361 16.934 43.505 -22.048 1.00 88.95 C ANISOU 2747 CG PRO A 361 12244 8627 12926 -1114 2073 -646 C ATOM 2748 CD PRO A 361 16.061 44.716 -22.202 1.00 91.92 C ANISOU 2748 CD PRO A 361 12631 8511 13784 -1070 2030 -541 C ATOM 2749 N ARG A 362 20.153 45.839 -24.261 1.00 96.22 N ANISOU 2749 N ARG A 362 13174 9637 13748 -2047 1962 6 N ATOM 2750 CA ARG A 362 20.764 46.365 -25.474 1.00 99.03 C ANISOU 2750 CA ARG A 362 13533 10115 13979 -2384 1903 379 C ATOM 2751 C ARG A 362 20.256 45.607 -26.698 1.00 98.36 C ANISOU 2751 C ARG A 362 13437 10327 13606 -2342 1844 650 C ATOM 2752 O ARG A 362 19.775 44.476 -26.604 1.00100.25 O ANISOU 2752 O ARG A 362 13625 10783 13682 -2065 1871 489 O ATOM 2753 CB ARG A 362 22.287 46.260 -25.382 1.00 99.58 C ANISOU 2753 CB ARG A 362 13478 10568 13791 -2655 2026 222 C ATOM 2754 CG ARG A 362 22.880 46.879 -24.124 1.00100.15 C ANISOU 2754 CG ARG A 362 13558 10399 14096 -2707 2067 -79 C ATOM 2755 CD ARG A 362 23.246 48.337 -24.348 1.00104.44 C ANISOU 2755 CD ARG A 362 14185 10580 14917 -3049 1986 162 C ATOM 2756 NE ARG A 362 24.255 48.485 -25.394 1.00106.90 N ANISOU 2756 NE ARG A 362 14407 11264 14948 -3458 2020 425 N ATOM 2757 CZ ARG A 362 24.783 49.645 -25.773 1.00111.14 C ANISOU 2757 CZ ARG A 362 15002 11600 15628 -3868 1943 703 C ATOM 2758 NH1 ARG A 362 24.403 50.775 -25.191 1.00113.36 N ANISOU 2758 NH1 ARG A 362 15434 11250 16387 -3883 1792 740 N ATOM 2759 NH2 ARG A 362 25.697 49.674 -26.734 1.00113.64 N ANISOU 2759 NH2 ARG A 362 15212 12352 15614 -4283 2016 925 N ATOM 2760 N LYS A 363 20.363 46.247 -27.866 1.00116.61 N ANISOU 2760 N LYS A 363 15815 12647 15843 -2656 1739 1081 N ATOM 2761 CA LYS A 363 19.911 45.642 -29.111 1.00126.43 C ANISOU 2761 CA LYS A 363 17077 14191 16771 -2688 1665 1362 C ATOM 2762 C LYS A 363 21.024 45.394 -30.120 1.00137.46 C ANISOU 2762 C LYS A 363 18385 16182 17664 -3079 1784 1459 C ATOM 2763 O LYS A 363 20.762 44.791 -31.167 1.00147.75 O ANISOU 2763 O LYS A 363 19690 17830 18618 -3135 1757 1622 O ATOM 2764 CB LYS A 363 18.828 46.511 -29.767 1.00128.34 C ANISOU 2764 CB LYS A 363 17494 13957 17311 -2737 1382 1835 C ATOM 2765 CG LYS A 363 17.605 46.737 -28.899 1.00130.86 C ANISOU 2765 CG LYS A 363 17838 13717 18165 -2334 1274 1700 C ATOM 2766 CD LYS A 363 16.396 46.974 -29.779 1.00142.08 C ANISOU 2766 CD LYS A 363 19354 14856 19775 -2272 978 2113 C ATOM 2767 CE LYS A 363 16.145 45.770 -30.684 1.00150.22 C ANISOU 2767 CE LYS A 363 20361 16398 20316 -2224 989 2200 C ATOM 2768 NZ LYS A 363 15.034 46.005 -31.650 1.00159.45 N ANISOU 2768 NZ LYS A 363 21637 17328 21620 -2220 658 2649 N ATOM 2769 N ASP A 364 22.255 45.810 -29.828 1.00115.76 N ANISOU 2769 N ASP A 364 15535 13594 14855 -3359 1928 1324 N ATOM 2770 CA ASP A 364 23.369 45.687 -30.759 1.00118.88 C ANISOU 2770 CA ASP A 364 15793 14585 14793 -3783 2083 1378 C ATOM 2771 C ASP A 364 24.281 44.511 -30.425 1.00120.09 C ANISOU 2771 C ASP A 364 15655 15275 14698 -3625 2305 843 C ATOM 2772 O ASP A 364 25.478 44.545 -30.729 1.00129.86 O ANISOU 2772 O ASP A 364 16687 16951 15703 -3946 2482 712 O ATOM 2773 CB ASP A 364 24.161 46.992 -30.787 1.00123.15 C ANISOU 2773 CB ASP A 364 16378 14962 15450 -4268 2074 1621 C ATOM 2774 CG ASP A 364 24.576 47.443 -29.406 1.00120.31 C ANISOU 2774 CG ASP A 364 15981 14236 15495 -4127 2098 1309 C ATOM 2775 OD1 ASP A 364 24.082 46.858 -28.418 1.00115.44 O ANISOU 2775 OD1 ASP A 364 15352 13436 15076 -3669 2098 966 O ATOM 2776 OD2 ASP A 364 25.389 48.387 -29.308 1.00122.80 O ANISOU 2776 OD2 ASP A 364 16290 14460 15907 -4511 2108 1415 O ATOM 2777 N VAL A 365 23.734 43.465 -29.812 1.00121.92 N ANISOU 2777 N VAL A 365 15849 15474 15001 -3150 2274 532 N ATOM 2778 CA VAL A 365 24.495 42.284 -29.426 1.00113.20 C ANISOU 2778 CA VAL A 365 14484 14775 13751 -2947 2384 33 C ATOM 2779 C VAL A 365 23.941 41.088 -30.185 1.00117.80 C ANISOU 2779 C VAL A 365 15021 15670 14069 -2726 2355 -44 C ATOM 2780 O VAL A 365 22.733 40.834 -30.150 1.00122.05 O ANISOU 2780 O VAL A 365 15737 15926 14710 -2468 2207 111 O ATOM 2781 CB VAL A 365 24.431 42.041 -27.908 1.00 97.56 C ANISOU 2781 CB VAL A 365 12517 12460 12091 -2621 2316 -275 C ATOM 2782 CG1 VAL A 365 25.370 40.913 -27.514 1.00100.38 C ANISOU 2782 CG1 VAL A 365 12602 13193 12345 -2466 2350 -749 C ATOM 2783 CG2 VAL A 365 24.764 43.316 -27.153 1.00 98.02 C ANISOU 2783 CG2 VAL A 365 12672 12134 12438 -2825 2318 -190 C ATOM 2784 N ASN A 366 24.820 40.367 -30.876 1.00120.05 N ANISOU 2784 N ASN A 366 15043 16539 14032 -2832 2495 -315 N ATOM 2785 CA ASN A 366 24.435 39.117 -31.514 1.00119.01 C ANISOU 2785 CA ASN A 366 14827 16719 13673 -2594 2460 -509 C ATOM 2786 C ASN A 366 24.591 37.986 -30.506 1.00126.05 C ANISOU 2786 C ASN A 366 15578 17540 14776 -2159 2354 -965 C ATOM 2787 O ASN A 366 25.717 37.558 -30.225 1.00135.35 O ANISOU 2787 O ASN A 366 16466 18991 15971 -2154 2421 -1370 O ATOM 2788 CB ASN A 366 25.282 38.848 -32.758 1.00120.41 C ANISOU 2788 CB ASN A 366 14763 17578 13410 -2914 2666 -657 C ATOM 2789 CG ASN A 366 24.869 39.700 -33.940 1.00131.96 C ANISOU 2789 CG ASN A 366 16430 19154 14554 -3357 2701 -140 C ATOM 2790 OD1 ASN A 366 23.734 40.171 -34.013 1.00144.04 O ANISOU 2790 OD1 ASN A 366 18270 20256 16201 -3309 2504 300 O ATOM 2791 ND2 ASN A 366 25.789 39.900 -34.878 1.00131.10 N ANISOU 2791 ND2 ASN A 366 16134 19635 14042 -3815 2935 -193 N ATOM 2792 N PRO A 367 23.493 37.480 -29.939 1.00124.54 N ANISOU 2792 N PRO A 367 15572 16986 14761 -1813 2162 -905 N ATOM 2793 CA PRO A 367 23.617 36.416 -28.930 1.00123.21 C ANISOU 2793 CA PRO A 367 15315 16723 14778 -1461 2008 -1271 C ATOM 2794 C PRO A 367 24.213 35.132 -29.471 1.00139.54 C ANISOU 2794 C PRO A 367 17105 19206 16707 -1308 1966 -1688 C ATOM 2795 O PRO A 367 24.732 34.330 -28.684 1.00141.83 O ANISOU 2795 O PRO A 367 17249 19462 17179 -1088 1812 -2034 O ATOM 2796 CB PRO A 367 22.171 36.206 -28.465 1.00103.21 C ANISOU 2796 CB PRO A 367 13048 13780 12388 -1214 1843 -1047 C ATOM 2797 CG PRO A 367 21.350 36.647 -29.618 1.00102.51 C ANISOU 2797 CG PRO A 367 13091 13723 12137 -1342 1876 -683 C ATOM 2798 CD PRO A 367 22.087 37.793 -30.236 1.00114.18 C ANISOU 2798 CD PRO A 367 14537 15356 13488 -1747 2053 -500 C ATOM 2799 N ASP A 368 24.174 34.916 -30.785 1.00146.50 N ANISOU 2799 N ASP A 368 17904 20476 17283 -1429 2072 -1684 N ATOM 2800 CA ASP A 368 24.692 33.672 -31.341 1.00145.86 C ANISOU 2800 CA ASP A 368 17535 20790 17096 -1260 2037 -2159 C ATOM 2801 C ASP A 368 26.195 33.728 -31.592 1.00139.65 C ANISOU 2801 C ASP A 368 16350 20458 16252 -1448 2237 -2570 C ATOM 2802 O ASP A 368 26.843 32.677 -31.652 1.00147.25 O ANISOU 2802 O ASP A 368 16993 21654 17300 -1231 2161 -3094 O ATOM 2803 CB ASP A 368 23.963 33.330 -32.641 1.00151.31 C ANISOU 2803 CB ASP A 368 18302 21738 17453 -1309 2066 -2044 C ATOM 2804 CG ASP A 368 22.527 32.898 -32.408 1.00150.23 C ANISOU 2804 CG ASP A 368 18459 21195 17427 -1041 1816 -1774 C ATOM 2805 OD1 ASP A 368 22.307 31.730 -32.028 1.00139.01 O ANISOU 2805 OD1 ASP A 368 16981 19670 16165 -702 1592 -2047 O ATOM 2806 OD2 ASP A 368 21.616 33.724 -32.620 1.00159.56 O ANISOU 2806 OD2 ASP A 368 19911 22152 18563 -1179 1821 -1288 O ATOM 2807 N GLU A 369 26.771 34.926 -31.733 1.00113.63 N ANISOU 2807 N GLU A 369 13041 17279 12852 -1849 2471 -2364 N ATOM 2808 CA GLU A 369 28.164 35.065 -32.140 1.00106.71 C ANISOU 2808 CA GLU A 369 11758 16918 11869 -2110 2715 -2729 C ATOM 2809 C GLU A 369 29.050 35.789 -31.135 1.00108.34 C ANISOU 2809 C GLU A 369 11863 16949 12351 -2231 2736 -2761 C ATOM 2810 O GLU A 369 30.258 35.885 -31.368 1.00107.64 O ANISOU 2810 O GLU A 369 11389 17276 12232 -2439 2924 -3094 O ATOM 2811 CB GLU A 369 28.247 35.794 -33.489 1.00110.25 C ANISOU 2811 CB GLU A 369 12216 17837 11836 -2613 3016 -2487 C ATOM 2812 CG GLU A 369 27.648 35.025 -34.659 1.00115.90 C ANISOU 2812 CG GLU A 369 12947 18897 12191 -2572 3038 -2570 C ATOM 2813 CD GLU A 369 27.650 35.824 -35.951 1.00123.05 C ANISOU 2813 CD GLU A 369 13938 20256 12559 -3145 3294 -2239 C ATOM 2814 OE1 GLU A 369 28.313 36.883 -35.996 1.00123.89 O ANISOU 2814 OE1 GLU A 369 14012 20483 12577 -3593 3482 -2022 O ATOM 2815 OE2 GLU A 369 26.984 35.395 -36.918 1.00126.84 O ANISOU 2815 OE2 GLU A 369 14533 20966 12693 -3180 3282 -2174 O ATOM 2816 N ALA A 370 28.504 36.285 -30.024 1.00 93.28 N ANISOU 2816 N ALA A 370 13247 11778 10416 -2782 630 -1187 N ATOM 2817 CA ALA A 370 29.299 37.124 -29.132 1.00 84.01 C ANISOU 2817 CA ALA A 370 11804 10743 9372 -2877 833 -1173 C ATOM 2818 C ALA A 370 30.269 36.304 -28.285 1.00 83.13 C ANISOU 2818 C ALA A 370 11495 10846 9244 -2782 1023 -1283 C ATOM 2819 O ALA A 370 31.408 36.731 -28.049 1.00 83.65 O ANISOU 2819 O ALA A 370 11408 11096 9278 -2833 1231 -1263 O ATOM 2820 CB ALA A 370 28.379 37.952 -28.241 1.00 82.69 C ANISOU 2820 CB ALA A 370 11482 10410 9527 -2968 704 -1154 C ATOM 2821 N VAL A 371 29.837 35.134 -27.814 1.00 95.98 N ANISOU 2821 N VAL A 371 13108 12442 10918 -2649 941 -1383 N ATOM 2822 CA VAL A 371 30.696 34.319 -26.959 1.00 92.10 C ANISOU 2822 CA VAL A 371 12433 12137 10424 -2546 1096 -1475 C ATOM 2823 C VAL A 371 31.974 33.942 -27.698 1.00 94.13 C ANISOU 2823 C VAL A 371 12744 12596 10427 -2470 1313 -1474 C ATOM 2824 O VAL A 371 33.087 34.103 -27.179 1.00 93.58 O ANISOU 2824 O VAL A 371 12457 12727 10373 -2479 1504 -1474 O ATOM 2825 CB VAL A 371 29.936 33.075 -26.469 1.00 91.16 C ANISOU 2825 CB VAL A 371 12327 11915 10396 -2414 961 -1554 C ATOM 2826 CG1 VAL A 371 30.832 32.211 -25.603 1.00 92.16 C ANISOU 2826 CG1 VAL A 371 12280 12224 10511 -2295 1110 -1633 C ATOM 2827 CG2 VAL A 371 28.690 33.487 -25.708 1.00 92.54 C ANISOU 2827 CG2 VAL A 371 12411 11903 10849 -2479 798 -1525 C ATOM 2828 N ALA A 372 31.834 33.466 -28.937 1.00102.51 N ANISOU 2828 N ALA A 372 14098 13601 11250 -2389 1285 -1468 N ATOM 2829 CA ALA A 372 32.988 32.979 -29.685 1.00103.79 C ANISOU 2829 CA ALA A 372 14344 13947 11146 -2267 1526 -1473 C ATOM 2830 C ALA A 372 33.998 34.089 -29.939 1.00100.33 C ANISOU 2830 C ALA A 372 13774 13675 10672 -2391 1763 -1344 C ATOM 2831 O ALA A 372 35.202 33.910 -29.722 1.00100.25 O ANISOU 2831 O ALA A 372 13567 13882 10643 -2338 2009 -1334 O ATOM 2832 CB ALA A 372 32.532 32.359 -31.004 1.00112.74 C ANISOU 2832 CB ALA A 372 15885 14957 11994 -2154 1430 -1500 C ATOM 2833 N ILE A 373 33.529 35.243 -30.411 1.00 98.57 N ANISOU 2833 N ILE A 373 13643 13343 10466 -2558 1685 -1227 N ATOM 2834 CA ILE A 373 34.445 36.346 -30.679 1.00100.25 C ANISOU 2834 CA ILE A 373 13733 13682 10676 -2700 1898 -1078 C ATOM 2835 C ILE A 373 35.126 36.788 -29.390 1.00100.21 C ANISOU 2835 C ILE A 373 13332 13794 10949 -2803 1967 -1094 C ATOM 2836 O ILE A 373 36.318 37.127 -29.384 1.00102.60 O ANISOU 2836 O ILE A 373 13431 14281 11270 -2852 2196 -1013 O ATOM 2837 CB ILE A 373 33.701 37.501 -31.378 1.00101.66 C ANISOU 2837 CB ILE A 373 14101 13681 10845 -2861 1765 -942 C ATOM 2838 CG1 ILE A 373 34.609 38.708 -31.564 1.00112.43 C ANISOU 2838 CG1 ILE A 373 15317 15142 12258 -3036 1971 -768 C ATOM 2839 CG2 ILE A 373 32.470 37.912 -30.615 1.00 98.82 C ANISOU 2839 CG2 ILE A 373 13693 13102 10751 -2949 1472 -989 C ATOM 2840 CD1 ILE A 373 33.901 39.881 -32.204 1.00124.67 C ANISOU 2840 CD1 ILE A 373 17051 16500 13819 -3195 1836 -618 C ATOM 2841 N GLY A 374 34.396 36.748 -28.271 1.00 97.15 N ANISOU 2841 N GLY A 374 12830 13300 10782 -2827 1768 -1196 N ATOM 2842 CA GLY A 374 35.033 36.985 -26.985 1.00 90.40 C ANISOU 2842 CA GLY A 374 11652 12557 10140 -2888 1803 -1244 C ATOM 2843 C GLY A 374 36.170 36.017 -26.709 1.00 89.34 C ANISOU 2843 C GLY A 374 11344 12654 9949 -2745 1980 -1291 C ATOM 2844 O GLY A 374 37.241 36.417 -26.241 1.00 88.82 O ANISOU 2844 O GLY A 374 11010 12747 9991 -2821 2098 -1250 O ATOM 2845 N ALA A 375 35.955 34.730 -27.001 1.00 86.07 N ANISOU 2845 N ALA A 375 11072 12245 9387 -2536 1982 -1373 N ATOM 2846 CA ALA A 375 37.014 33.743 -26.807 1.00 86.96 C ANISOU 2846 CA ALA A 375 11036 12559 9447 -2366 2156 -1415 C ATOM 2847 C ALA A 375 38.223 34.049 -27.680 1.00 94.96 C ANISOU 2847 C ALA A 375 11978 13753 10348 -2367 2443 -1292 C ATOM 2848 O ALA A 375 39.369 33.979 -27.216 1.00106.24 O ANISOU 2848 O ALA A 375 13106 15378 11883 -2352 2597 -1260 O ATOM 2849 CB ALA A 375 36.490 32.340 -27.104 1.00 86.55 C ANISOU 2849 CB ALA A 375 11203 12431 9252 -2140 2097 -1525 C ATOM 2850 N ALA A 376 37.985 34.381 -28.952 1.00 91.40 N ANISOU 2850 N ALA A 376 11799 13241 9688 -2380 2521 -1208 N ATOM 2851 CA ALA A 376 39.082 34.742 -29.845 1.00 94.55 C ANISOU 2851 CA ALA A 376 12150 13808 9965 -2380 2837 -1057 C ATOM 2852 C ALA A 376 39.896 35.893 -29.275 1.00 95.27 C ANISOU 2852 C ALA A 376 11878 14001 10319 -2610 2911 -925 C ATOM 2853 O ALA A 376 41.133 35.845 -29.242 1.00 97.38 O ANISOU 2853 O ALA A 376 11866 14475 10660 -2588 3153 -837 O ATOM 2854 CB ALA A 376 38.532 35.105 -31.222 1.00 96.12 C ANISOU 2854 CB ALA A 376 12742 13895 9886 -2387 2866 -970 C ATOM 2855 N VAL A 377 39.213 36.937 -28.806 1.00 93.80 N ANISOU 2855 N VAL A 377 11682 13656 10301 -2831 2694 -908 N ATOM 2856 CA VAL A 377 39.920 38.071 -28.221 1.00 94.65 C ANISOU 2856 CA VAL A 377 11476 13813 10675 -3068 2711 -805 C ATOM 2857 C VAL A 377 40.737 37.630 -27.012 1.00 94.27 C ANISOU 2857 C VAL A 377 11069 13918 10831 -3037 2689 -888 C ATOM 2858 O VAL A 377 41.880 38.064 -26.834 1.00 96.40 O ANISOU 2858 O VAL A 377 11024 14336 11270 -3141 2820 -777 O ATOM 2859 CB VAL A 377 38.934 39.193 -27.857 1.00 93.14 C ANISOU 2859 CB VAL A 377 11381 13387 10622 -3275 2457 -810 C ATOM 2860 CG1 VAL A 377 39.660 40.320 -27.151 1.00 94.18 C ANISOU 2860 CG1 VAL A 377 11210 13535 11040 -3518 2432 -737 C ATOM 2861 CG2 VAL A 377 38.239 39.701 -29.107 1.00 94.07 C ANISOU 2861 CG2 VAL A 377 11829 13360 10553 -3314 2471 -691 C ATOM 2862 N GLN A 378 40.173 36.763 -26.165 1.00 92.94 N ANISOU 2862 N GLN A 378 10937 13713 10663 -2898 2514 -1066 N ATOM 2863 CA GLN A 378 40.937 36.256 -25.024 1.00 91.84 C ANISOU 2863 CA GLN A 378 10492 13721 10682 -2844 2477 -1137 C ATOM 2864 C GLN A 378 42.222 35.573 -25.482 1.00 94.28 C ANISOU 2864 C GLN A 378 10594 14264 10964 -2700 2751 -1054 C ATOM 2865 O GLN A 378 43.299 35.798 -24.912 1.00101.01 O ANISOU 2865 O GLN A 378 11087 15267 12023 -2770 2789 -993 O ATOM 2866 CB GLN A 378 40.087 35.294 -24.199 1.00 94.99 C ANISOU 2866 CB GLN A 378 11010 14041 11042 -2683 2288 -1311 C ATOM 2867 CG GLN A 378 40.843 34.632 -23.057 1.00109.17 C ANISOU 2867 CG GLN A 378 12535 15988 12956 -2592 2242 -1376 C ATOM 2868 CD GLN A 378 41.211 35.607 -21.962 1.00121.55 C ANISOU 2868 CD GLN A 378 13880 17565 14740 -2798 2076 -1383 C ATOM 2869 OE1 GLN A 378 40.361 36.338 -21.460 1.00130.88 O ANISOU 2869 OE1 GLN A 378 15186 18579 15964 -2923 1900 -1443 O ATOM 2870 NE2 GLN A 378 42.483 35.630 -21.590 1.00124.83 N ANISOU 2870 NE2 GLN A 378 13966 18164 15300 -2827 2123 -1325 N ATOM 2871 N GLY A 379 42.129 34.734 -26.517 1.00 95.04 N ANISOU 2871 N GLY A 379 10913 14384 10814 -2489 2939 -1051 N ATOM 2872 CA GLY A 379 43.339 34.168 -27.094 1.00 98.03 C ANISOU 2872 CA GLY A 379 11119 14976 11152 -2329 3258 -957 C ATOM 2873 C GLY A 379 44.328 35.237 -27.511 1.00101.04 C ANISOU 2873 C GLY A 379 11236 15474 11680 -2522 3466 -738 C ATOM 2874 O GLY A 379 45.536 35.107 -27.288 1.00103.40 O ANISOU 2874 O GLY A 379 11162 15968 12159 -2495 3634 -642 O ATOM 2875 N GLY A 380 43.826 36.324 -28.101 1.00101.21 N ANISOU 2875 N GLY A 380 11428 15367 11660 -2727 3447 -638 N ATOM 2876 CA GLY A 380 44.694 37.447 -28.417 1.00104.11 C ANISOU 2876 CA GLY A 380 11539 15808 12212 -2954 3613 -410 C ATOM 2877 C GLY A 380 45.389 38.016 -27.195 1.00104.34 C ANISOU 2877 C GLY A 380 11135 15885 12623 -3155 3438 -400 C ATOM 2878 O GLY A 380 46.558 38.402 -27.257 1.00107.48 O ANISOU 2878 O GLY A 380 11164 16432 13243 -3254 3614 -221 O ATOM 2879 N VAL A 381 44.675 38.090 -26.068 1.00107.20 N ANISOU 2879 N VAL A 381 11542 16118 13073 -3219 3084 -585 N ATOM 2880 CA VAL A 381 45.293 38.562 -24.833 1.00106.31 C ANISOU 2880 CA VAL A 381 11078 16038 13276 -3389 2869 -612 C ATOM 2881 C VAL A 381 46.408 37.622 -24.418 1.00103.32 C ANISOU 2881 C VAL A 381 10357 15894 13008 -3221 2969 -600 C ATOM 2882 O VAL A 381 47.463 38.054 -23.939 1.00105.78 O ANISOU 2882 O VAL A 381 10268 16312 13613 -3364 2941 -497 O ATOM 2883 CB VAL A 381 44.242 38.699 -23.716 1.00108.37 C ANISOU 2883 CB VAL A 381 11519 16119 13539 -3431 2506 -827 C ATOM 2884 CG1 VAL A 381 44.825 39.451 -22.532 1.00107.83 C ANISOU 2884 CG1 VAL A 381 11165 16042 13761 -3644 2259 -855 C ATOM 2885 CG2 VAL A 381 42.992 39.375 -24.227 1.00111.68 C ANISOU 2885 CG2 VAL A 381 12303 16303 13827 -3517 2433 -846 C ATOM 2886 N LEU A 382 46.191 36.320 -24.594 1.00102.23 N ANISOU 2886 N LEU A 382 10364 15821 12657 -2915 3067 -701 N ATOM 2887 CA LEU A 382 47.203 35.358 -24.182 1.00103.80 C ANISOU 2887 CA LEU A 382 10250 16225 12963 -2722 3154 -693 C ATOM 2888 C LEU A 382 48.444 35.448 -25.057 1.00107.97 C ANISOU 2888 C LEU A 382 10476 16945 13603 -2698 3528 -462 C ATOM 2889 O LEU A 382 49.567 35.307 -24.560 1.00110.39 O ANISOU 2889 O LEU A 382 10344 17417 14183 -2695 3551 -374 O ATOM 2890 CB LEU A 382 46.621 33.951 -24.204 1.00101.81 C ANISOU 2890 CB LEU A 382 10259 15960 12465 -2399 3168 -855 C ATOM 2891 CG LEU A 382 45.399 33.770 -23.303 1.00 98.02 C ANISOU 2891 CG LEU A 382 10042 15299 11902 -2408 2831 -1053 C ATOM 2892 CD1 LEU A 382 45.066 32.302 -23.148 1.00 96.72 C ANISOU 2892 CD1 LEU A 382 10032 15136 11581 -2100 2831 -1181 C ATOM 2893 CD2 LEU A 382 45.634 34.412 -21.948 1.00104.18 C ANISOU 2893 CD2 LEU A 382 10589 16076 12920 -2601 2532 -1092 C ATOM 2894 N THR A 383 48.271 35.684 -26.360 1.00117.97 N ANISOU 2894 N THR A 383 11964 18193 14667 -2673 3827 -346 N ATOM 2895 CA THR A 383 49.434 35.825 -27.233 1.00126.63 C ANISOU 2895 CA THR A 383 12783 19475 15856 -2643 4239 -97 C ATOM 2896 C THR A 383 50.113 37.178 -27.047 1.00127.95 C ANISOU 2896 C THR A 383 12588 19649 16380 -3002 4204 115 C ATOM 2897 O THR A 383 51.335 37.249 -26.876 1.00130.93 O ANISOU 2897 O THR A 383 12478 20198 17073 -3041 4340 288 O ATOM 2898 CB THR A 383 49.032 35.633 -28.695 1.00132.42 C ANISOU 2898 CB THR A 383 13919 20187 16210 -2484 4579 -36 C ATOM 2899 OG1 THR A 383 47.881 36.435 -28.990 1.00133.83 O ANISOU 2899 OG1 THR A 383 14483 20144 16222 -2671 4391 -76 O ATOM 2900 CG2 THR A 383 48.720 34.174 -28.971 1.00132.20 C ANISOU 2900 CG2 THR A 383 14166 20181 15882 -2099 4672 -216 C ATOM 2901 N GLY A 384 49.339 38.259 -27.083 1.00122.05 N ANISOU 2901 N GLY A 384 12058 18700 15614 -3268 4014 114 N ATOM 2902 CA GLY A 384 49.889 39.587 -26.907 1.00121.16 C ANISOU 2902 CA GLY A 384 11649 18541 15845 -3627 3944 302 C ATOM 2903 C GLY A 384 49.372 40.591 -27.914 1.00118.20 C ANISOU 2903 C GLY A 384 11548 18020 15343 -3801 4076 457 C ATOM 2904 O GLY A 384 49.629 41.792 -27.788 1.00119.36 O ANISOU 2904 O GLY A 384 11523 18065 15763 -4124 3980 603 O ATOM 2905 N ASP A 385 48.630 40.115 -28.916 1.00122.77 N ANISOU 2905 N ASP A 385 12571 18569 15508 -3594 4271 426 N ATOM 2906 CA ASP A 385 48.140 41.003 -29.965 1.00135.07 C ANISOU 2906 CA ASP A 385 14422 19995 16902 -3729 4403 593 C ATOM 2907 C ASP A 385 47.141 42.029 -29.446 1.00132.60 C ANISOU 2907 C ASP A 385 14304 19405 16672 -3991 4008 499 C ATOM 2908 O ASP A 385 46.960 43.073 -30.080 1.00136.69 O ANISOU 2908 O ASP A 385 14935 19796 17207 -4195 4061 683 O ATOM 2909 CB ASP A 385 47.519 40.186 -31.097 1.00149.24 C ANISOU 2909 CB ASP A 385 16690 21807 18207 -3431 4634 549 C ATOM 2910 CG ASP A 385 48.550 39.375 -31.862 1.00169.72 C ANISOU 2910 CG ASP A 385 19143 24656 20688 -3171 5113 688 C ATOM 2911 OD1 ASP A 385 49.758 39.660 -31.724 1.00171.00 O ANISOU 2911 OD1 ASP A 385 18818 24981 21175 -3262 5324 897 O ATOM 2912 OD2 ASP A 385 48.152 38.456 -32.609 1.00184.11 O ANISOU 2912 OD2 ASP A 385 21341 26505 22108 -2870 5275 591 O ATOM 2913 N VAL A 386 46.486 41.762 -28.322 1.00129.92 N ANISOU 2913 N VAL A 386 14018 18965 16380 -3976 3633 229 N ATOM 2914 CA VAL A 386 45.712 42.772 -27.610 1.00123.60 C ANISOU 2914 CA VAL A 386 13321 17912 15728 -4218 3266 132 C ATOM 2915 C VAL A 386 46.287 42.884 -26.207 1.00127.99 C ANISOU 2915 C VAL A 386 13524 18496 16612 -4335 2996 15 C ATOM 2916 O VAL A 386 46.289 41.906 -25.449 1.00125.71 O ANISOU 2916 O VAL A 386 13183 18306 16275 -4144 2889 -170 O ATOM 2917 CB VAL A 386 44.208 42.453 -27.584 1.00113.89 C ANISOU 2917 CB VAL A 386 12548 16500 14223 -4085 3062 -80 C ATOM 2918 CG1 VAL A 386 43.568 42.832 -28.911 1.00116.01 C ANISOU 2918 CG1 VAL A 386 13176 16662 14238 -4081 3215 64 C ATOM 2919 CG2 VAL A 386 43.968 40.993 -27.275 1.00110.22 C ANISOU 2919 CG2 VAL A 386 12164 16154 13561 -3775 3058 -278 C ATOM 2920 N LYS A 387 46.803 44.068 -25.878 1.00123.82 N ANISOU 2920 N LYS A 387 12763 17868 16413 -4650 2874 133 N ATOM 2921 CA LYS A 387 47.428 44.332 -24.591 1.00128.99 C ANISOU 2921 CA LYS A 387 13093 18524 17392 -4802 2577 36 C ATOM 2922 C LYS A 387 46.601 45.248 -23.702 1.00134.57 C ANISOU 2922 C LYS A 387 14000 18949 18180 -4984 2184 -148 C ATOM 2923 O LYS A 387 46.999 45.506 -22.563 1.00143.75 O ANISOU 2923 O LYS A 387 14976 20080 19563 -5103 1888 -269 O ATOM 2924 CB LYS A 387 48.817 44.959 -24.787 1.00130.14 C ANISOU 2924 CB LYS A 387 12763 18767 17918 -5037 2701 309 C ATOM 2925 CG LYS A 387 49.852 44.057 -25.435 1.00129.45 C ANISOU 2925 CG LYS A 387 12372 18981 17833 -4849 3092 495 C ATOM 2926 CD LYS A 387 51.241 44.689 -25.383 1.00133.62 C ANISOU 2926 CD LYS A 387 12348 19595 18826 -5101 3157 762 C ATOM 2927 CE LYS A 387 52.305 43.771 -25.971 1.00135.26 C ANISOU 2927 CE LYS A 387 12210 20111 19072 -4886 3572 955 C ATOM 2928 NZ LYS A 387 52.166 43.626 -27.445 1.00137.81 N ANISOU 2928 NZ LYS A 387 12750 20505 19105 -4739 4070 1158 N ATOM 2929 N ASP A 388 45.475 45.754 -24.185 1.00134.19 N ANISOU 2929 N ASP A 388 14334 18691 17963 -4998 2165 -174 N ATOM 2930 CA ASP A 388 44.720 46.771 -23.470 1.00132.49 C ANISOU 2930 CA ASP A 388 14303 18184 17854 -5172 1842 -316 C ATOM 2931 C ASP A 388 43.613 46.204 -22.590 1.00123.98 C ANISOU 2931 C ASP A 388 13500 17029 16576 -4970 1630 -614 C ATOM 2932 O ASP A 388 42.842 46.981 -22.018 1.00123.52 O ANISOU 2932 O ASP A 388 13640 16724 16567 -5060 1398 -747 O ATOM 2933 CB ASP A 388 44.119 47.758 -24.472 1.00145.73 C ANISOU 2933 CB ASP A 388 16216 19648 19509 -5310 1931 -149 C ATOM 2934 CG ASP A 388 43.220 47.079 -25.487 1.00159.40 C ANISOU 2934 CG ASP A 388 18274 21411 20878 -5072 2135 -123 C ATOM 2935 OD1 ASP A 388 43.304 45.840 -25.620 1.00170.76 O ANISOU 2935 OD1 ASP A 388 19710 23064 22107 -4819 2277 -184 O ATOM 2936 OD2 ASP A 388 42.431 47.781 -26.151 1.00159.48 O ANISOU 2936 OD2 ASP A 388 18554 21219 20821 -5136 2131 -41 O ATOM 2937 N VAL A 389 43.506 44.885 -22.456 1.00115.27 N ANISOU 2937 N VAL A 389 12415 16118 15263 -4695 1714 -713 N ATOM 2938 CA VAL A 389 42.379 44.274 -21.764 1.00112.13 C ANISOU 2938 CA VAL A 389 12285 15648 14672 -4493 1565 -949 C ATOM 2939 C VAL A 389 42.892 43.263 -20.748 1.00119.45 C ANISOU 2939 C VAL A 389 13039 16764 15583 -4339 1477 -1087 C ATOM 2940 O VAL A 389 43.810 42.488 -21.039 1.00129.15 O ANISOU 2940 O VAL A 389 14031 18223 16817 -4246 1640 -994 O ATOM 2941 CB VAL A 389 41.406 43.610 -22.755 1.00101.96 C ANISOU 2941 CB VAL A 389 11287 14344 13108 -4291 1739 -923 C ATOM 2942 CG1 VAL A 389 40.608 44.677 -23.486 1.00100.14 C ANISOU 2942 CG1 VAL A 389 11292 13872 12886 -4430 1726 -830 C ATOM 2943 CG2 VAL A 389 42.166 42.747 -23.741 1.00 99.61 C ANISOU 2943 CG2 VAL A 389 10875 14282 12690 -4162 2038 -772 C ATOM 2944 N LEU A 390 42.303 43.282 -19.553 1.00110.54 N ANISOU 2944 N LEU A 390 12037 15533 14431 -4297 1229 -1298 N ATOM 2945 CA LEU A 390 42.554 42.289 -18.520 1.00107.72 C ANISOU 2945 CA LEU A 390 11597 15326 14004 -4122 1123 -1436 C ATOM 2946 C LEU A 390 41.223 41.797 -17.983 1.00 94.99 C ANISOU 2946 C LEU A 390 10299 13603 12190 -3929 1059 -1605 C ATOM 2947 O LEU A 390 40.285 42.582 -17.803 1.00 93.18 O ANISOU 2947 O LEU A 390 10295 13149 11959 -3992 968 -1677 O ATOM 2948 CB LEU A 390 43.388 42.845 -17.364 1.00118.32 C ANISOU 2948 CB LEU A 390 12746 16672 15537 -4282 847 -1515 C ATOM 2949 CG LEU A 390 43.717 41.793 -16.302 1.00119.67 C ANISOU 2949 CG LEU A 390 12838 17011 15621 -4093 723 -1635 C ATOM 2950 CD1 LEU A 390 44.432 40.626 -16.964 1.00116.40 C ANISOU 2950 CD1 LEU A 390 12196 16849 15180 -3924 956 -1501 C ATOM 2951 CD2 LEU A 390 44.544 42.372 -15.168 1.00128.53 C ANISOU 2951 CD2 LEU A 390 13797 18126 16913 -4258 400 -1717 C ATOM 2952 N LEU A 391 41.148 40.498 -17.719 1.00 96.52 N ANISOU 2952 N LEU A 391 10493 13944 12236 -3689 1115 -1653 N ATOM 2953 CA LEU A 391 39.928 39.866 -17.244 1.00 91.23 C ANISOU 2953 CA LEU A 391 10079 13186 11397 -3496 1086 -1774 C ATOM 2954 C LEU A 391 40.173 39.254 -15.874 1.00101.98 C ANISOU 2954 C LEU A 391 11397 14641 12710 -3379 930 -1899 C ATOM 2955 O LEU A 391 41.087 38.440 -15.708 1.00110.14 O ANISOU 2955 O LEU A 391 12226 15874 13747 -3292 946 -1864 O ATOM 2956 CB LEU A 391 39.449 38.794 -18.221 1.00 88.14 C ANISOU 2956 CB LEU A 391 9782 12844 10862 -3306 1285 -1708 C ATOM 2957 CG LEU A 391 38.668 39.265 -19.446 1.00 95.75 C ANISOU 2957 CG LEU A 391 10931 13658 11790 -3361 1392 -1621 C ATOM 2958 CD1 LEU A 391 39.531 40.081 -20.401 1.00107.80 C ANISOU 2958 CD1 LEU A 391 12326 15223 13409 -3549 1503 -1466 C ATOM 2959 CD2 LEU A 391 38.081 38.063 -20.147 1.00 90.43 C ANISOU 2959 CD2 LEU A 391 10399 13008 10952 -3148 1510 -1607 C ATOM 2960 N LEU A 392 39.349 39.645 -14.905 1.00 96.89 N ANISOU 2960 N LEU A 392 10954 13848 12011 -3361 791 -2035 N ATOM 2961 CA LEU A 392 39.402 39.138 -13.536 1.00 93.68 C ANISOU 2961 CA LEU A 392 10586 13504 11504 -3235 644 -2156 C ATOM 2962 C LEU A 392 38.130 38.336 -13.297 1.00 88.92 C ANISOU 2962 C LEU A 392 10203 12831 10750 -3016 741 -2191 C ATOM 2963 O LEU A 392 37.071 38.911 -13.023 1.00 86.30 O ANISOU 2963 O LEU A 392 10080 12312 10398 -3014 737 -2254 O ATOM 2964 CB LEU A 392 39.524 40.276 -12.522 1.00 95.23 C ANISOU 2964 CB LEU A 392 10865 13580 11740 -3380 413 -2289 C ATOM 2965 CG LEU A 392 40.885 40.939 -12.301 1.00100.04 C ANISOU 2965 CG LEU A 392 11238 14258 12514 -3593 218 -2282 C ATOM 2966 CD1 LEU A 392 41.342 41.704 -13.530 1.00101.99 C ANISOU 2966 CD1 LEU A 392 11320 14464 12968 -3810 318 -2137 C ATOM 2967 CD2 LEU A 392 40.827 41.860 -11.097 1.00108.89 C ANISOU 2967 CD2 LEU A 392 12529 15232 13610 -3682 -54 -2462 C ATOM 2968 N ASP A 393 38.231 37.019 -13.408 1.00 87.57 N ANISOU 2968 N ASP A 393 9974 12797 10501 -2832 832 -2138 N ATOM 2969 CA ASP A 393 37.103 36.134 -13.176 1.00 96.23 C ANISOU 2969 CA ASP A 393 11242 13828 11492 -2634 915 -2144 C ATOM 2970 C ASP A 393 37.166 35.586 -11.758 1.00102.53 C ANISOU 2970 C ASP A 393 12090 14697 12170 -2496 815 -2212 C ATOM 2971 O ASP A 393 38.163 35.733 -11.047 1.00111.17 O ANISOU 2971 O ASP A 393 13078 15912 13248 -2535 664 -2255 O ATOM 2972 CB ASP A 393 37.086 34.993 -14.196 1.00102.42 C ANISOU 2972 CB ASP A 393 11975 14676 12263 -2513 1063 -2046 C ATOM 2973 CG ASP A 393 35.705 34.752 -14.782 1.00102.70 C ANISOU 2973 CG ASP A 393 12195 14532 12294 -2451 1151 -2016 C ATOM 2974 OD1 ASP A 393 34.703 35.033 -14.092 1.00 96.94 O ANISOU 2974 OD1 ASP A 393 11604 13665 11562 -2421 1126 -2057 O ATOM 2975 OD2 ASP A 393 35.623 34.282 -15.936 1.00107.02 O ANISOU 2975 OD2 ASP A 393 12751 15070 12844 -2426 1243 -1949 O ATOM 2976 N VAL A 394 36.073 34.948 -11.351 1.00 89.45 N ANISOU 2976 N VAL A 394 10595 12958 10434 -2333 894 -2207 N ATOM 2977 CA VAL A 394 35.912 34.448 -9.997 1.00 92.38 C ANISOU 2977 CA VAL A 394 11069 13372 10662 -2183 839 -2248 C ATOM 2978 C VAL A 394 35.506 32.985 -10.066 1.00 93.15 C ANISOU 2978 C VAL A 394 11164 13504 10725 -1987 949 -2149 C ATOM 2979 O VAL A 394 35.146 32.468 -11.122 1.00 86.45 O ANISOU 2979 O VAL A 394 10279 12605 9963 -1970 1054 -2076 O ATOM 2980 CB VAL A 394 34.869 35.255 -9.200 1.00 96.64 C ANISOU 2980 CB VAL A 394 11835 13743 11140 -2171 853 -2329 C ATOM 2981 CG1 VAL A 394 35.236 36.728 -9.176 1.00100.73 C ANISOU 2981 CG1 VAL A 394 12381 14183 11709 -2368 729 -2439 C ATOM 2982 CG2 VAL A 394 33.488 35.059 -9.799 1.00 95.51 C ANISOU 2982 CG2 VAL A 394 11772 13431 11085 -2112 1027 -2253 C ATOM 2983 N THR A 395 35.576 32.319 -8.922 1.00115.48 N ANISOU 2983 N THR A 395 14053 16405 13418 -1838 907 -2146 N ATOM 2984 CA THR A 395 35.012 30.982 -8.999 1.00110.96 C ANISOU 2984 CA THR A 395 13499 15815 12845 -1663 1021 -2037 C ATOM 2985 C THR A 395 33.558 31.003 -8.539 1.00 99.53 C ANISOU 2985 C THR A 395 12230 14198 11389 -1589 1145 -2001 C ATOM 2986 O THR A 395 33.207 31.743 -7.618 1.00 90.84 O ANISOU 2986 O THR A 395 11268 13059 10187 -1585 1139 -2066 O ATOM 2987 CB THR A 395 35.816 29.994 -8.149 1.00106.51 C ANISOU 2987 CB THR A 395 12888 15413 12169 -1515 938 -1998 C ATOM 2988 OG1 THR A 395 35.220 28.695 -8.218 1.00113.57 O ANISOU 2988 OG1 THR A 395 13812 16255 13083 -1350 1046 -1881 O ATOM 2989 CG2 THR A 395 35.879 30.438 -6.703 1.00 92.34 C ANISOU 2989 CG2 THR A 395 11240 13660 10184 -1475 832 -2060 C ATOM 2990 N PRO A 396 32.673 30.234 -9.176 1.00 88.51 N ANISOU 2990 N PRO A 396 10834 12685 10111 -1528 1260 -1898 N ATOM 2991 CA PRO A 396 31.242 30.361 -8.868 1.00 87.52 C ANISOU 2991 CA PRO A 396 10821 12382 10050 -1481 1388 -1839 C ATOM 2992 C PRO A 396 30.794 29.614 -7.627 1.00 87.80 C ANISOU 2992 C PRO A 396 10950 12431 9980 -1304 1472 -1753 C ATOM 2993 O PRO A 396 29.723 29.934 -7.093 1.00 91.88 O ANISOU 2993 O PRO A 396 11561 12829 10519 -1254 1605 -1710 O ATOM 2994 CB PRO A 396 30.572 29.780 -10.120 1.00 88.38 C ANISOU 2994 CB PRO A 396 10870 12354 10355 -1507 1427 -1754 C ATOM 2995 CG PRO A 396 31.547 28.756 -10.587 1.00 89.02 C ANISOU 2995 CG PRO A 396 10865 12555 10405 -1457 1366 -1739 C ATOM 2996 CD PRO A 396 32.914 29.312 -10.300 1.00 87.48 C ANISOU 2996 CD PRO A 396 10601 12555 10082 -1511 1271 -1838 C ATOM 2997 N LEU A 397 31.568 28.650 -7.144 1.00 81.33 N ANISOU 2997 N LEU A 397 10103 11747 9050 -1199 1415 -1711 N ATOM 2998 CA LEU A 397 31.134 27.766 -6.075 1.00 82.66 C ANISOU 2998 CA LEU A 397 10362 11919 9124 -1023 1503 -1586 C ATOM 2999 C LEU A 397 32.113 27.815 -4.915 1.00 82.75 C ANISOU 2999 C LEU A 397 10456 12113 8871 -947 1388 -1640 C ATOM 3000 O LEU A 397 33.328 27.874 -5.120 1.00 85.81 O ANISOU 3000 O LEU A 397 10745 12642 9218 -999 1214 -1720 O ATOM 3001 CB LEU A 397 31.010 26.325 -6.574 1.00 87.68 C ANISOU 3001 CB LEU A 397 10914 12506 9897 -941 1526 -1443 C ATOM 3002 CG LEU A 397 30.041 26.094 -7.731 1.00 91.96 C ANISOU 3002 CG LEU A 397 11392 12847 10700 -1011 1587 -1384 C ATOM 3003 CD1 LEU A 397 30.261 24.720 -8.339 1.00 93.11 C ANISOU 3003 CD1 LEU A 397 11474 12950 10952 -943 1542 -1300 C ATOM 3004 CD2 LEU A 397 28.607 26.244 -7.260 1.00 99.76 C ANISOU 3004 CD2 LEU A 397 12436 13671 11797 -979 1753 -1266 C ATOM 3005 N SER A 398 31.577 27.781 -3.699 1.00 84.25 N ANISOU 3005 N SER A 398 10826 12298 8885 -818 1486 -1585 N ATOM 3006 CA SER A 398 32.414 27.702 -2.512 1.00 86.41 C ANISOU 3006 CA SER A 398 11228 12735 8871 -721 1356 -1619 C ATOM 3007 C SER A 398 33.104 26.349 -2.444 1.00 86.77 C ANISOU 3007 C SER A 398 11178 12876 8915 -612 1275 -1491 C ATOM 3008 O SER A 398 32.485 25.307 -2.675 1.00 86.16 O ANISOU 3008 O SER A 398 11059 12706 8971 -528 1408 -1323 O ATOM 3009 CB SER A 398 31.578 27.920 -1.254 1.00 88.26 C ANISOU 3009 CB SER A 398 11722 12931 8882 -578 1520 -1572 C ATOM 3010 OG SER A 398 30.903 29.161 -1.305 1.00 92.90 O ANISOU 3010 OG SER A 398 12404 13410 9485 -650 1614 -1693 O ATOM 3011 N LEU A 399 34.394 26.366 -2.124 1.00 88.03 N ANISOU 3011 N LEU A 399 11293 13205 8949 -614 1040 -1565 N ATOM 3012 CA LEU A 399 35.190 25.153 -1.989 1.00 91.59 C ANISOU 3012 CA LEU A 399 11645 13757 9397 -493 935 -1452 C ATOM 3013 C LEU A 399 35.455 24.911 -0.513 1.00 99.26 C ANISOU 3013 C LEU A 399 12824 14831 10057 -340 842 -1396 C ATOM 3014 O LEU A 399 36.031 25.770 0.160 1.00110.00 O ANISOU 3014 O LEU A 399 14292 16289 11214 -383 660 -1532 O ATOM 3015 CB LEU A 399 36.511 25.269 -2.745 1.00 98.87 C ANISOU 3015 CB LEU A 399 12324 14802 10442 -588 734 -1544 C ATOM 3016 CG LEU A 399 37.440 24.059 -2.604 1.00104.72 C ANISOU 3016 CG LEU A 399 12939 15650 11202 -442 617 -1434 C ATOM 3017 CD1 LEU A 399 37.146 23.034 -3.690 1.00108.96 C ANISOU 3017 CD1 LEU A 399 13346 16076 11977 -392 762 -1342 C ATOM 3018 CD2 LEU A 399 38.906 24.471 -2.622 1.00104.97 C ANISOU 3018 CD2 LEU A 399 12779 15861 11245 -507 359 -1526 C ATOM 3019 N GLY A 400 35.053 23.743 -0.017 1.00105.99 N ANISOU 3019 N GLY A 400 13750 15653 10870 -167 949 -1194 N ATOM 3020 CA GLY A 400 35.235 23.439 1.386 1.00108.68 C ANISOU 3020 CA GLY A 400 14323 16086 10886 -3 882 -1108 C ATOM 3021 C GLY A 400 35.542 21.973 1.600 1.00111.79 C ANISOU 3021 C GLY A 400 14664 16496 11314 162 858 -894 C ATOM 3022 O GLY A 400 35.659 21.195 0.652 1.00114.16 O ANISOU 3022 O GLY A 400 14751 16729 11896 153 884 -834 O ATOM 3023 N ILE A 401 35.676 21.604 2.871 1.00 98.68 N ANISOU 3023 N ILE A 401 13231 14915 9347 325 800 -780 N ATOM 3024 CA ILE A 401 35.956 20.236 3.275 1.00100.10 C ANISOU 3024 CA ILE A 401 13409 15105 9519 502 766 -550 C ATOM 3025 C ILE A 401 34.856 19.779 4.220 1.00101.64 C ANISOU 3025 C ILE A 401 13874 15216 9528 647 1029 -329 C ATOM 3026 O ILE A 401 34.183 20.585 4.865 1.00102.52 O ANISOU 3026 O ILE A 401 14218 15327 9409 652 1174 -375 O ATOM 3027 CB ILE A 401 37.335 20.099 3.947 1.00102.67 C ANISOU 3027 CB ILE A 401 13738 15621 9653 580 404 -576 C ATOM 3028 CG1 ILE A 401 37.420 21.032 5.157 1.00105.29 C ANISOU 3028 CG1 ILE A 401 14386 16060 9558 602 277 -676 C ATOM 3029 CG2 ILE A 401 38.436 20.403 2.953 1.00102.18 C ANISOU 3029 CG2 ILE A 401 13346 15636 9843 449 186 -743 C ATOM 3030 CD1 ILE A 401 38.765 21.033 5.841 1.00110.13 C ANISOU 3030 CD1 ILE A 401 15010 16853 9982 653 -141 -719 C ATOM 3031 N GLU A 402 34.674 18.464 4.293 1.00102.23 N ANISOU 3031 N GLU A 402 13917 15208 9717 774 1108 -76 N ATOM 3032 CA GLU A 402 33.691 17.878 5.191 1.00104.12 C ANISOU 3032 CA GLU A 402 14383 15364 9815 917 1371 193 C ATOM 3033 C GLU A 402 34.315 17.682 6.562 1.00107.81 C ANISOU 3033 C GLU A 402 15128 15991 9843 1097 1212 289 C ATOM 3034 O GLU A 402 35.407 17.116 6.675 1.00108.91 O ANISOU 3034 O GLU A 402 15198 16225 9959 1166 919 309 O ATOM 3035 CB GLU A 402 33.184 16.543 4.651 1.00103.44 C ANISOU 3035 CB GLU A 402 14145 15084 10074 957 1512 439 C ATOM 3036 CG GLU A 402 32.304 15.795 5.633 1.00105.98 C ANISOU 3036 CG GLU A 402 14672 15319 10275 1109 1769 772 C ATOM 3037 CD GLU A 402 31.909 14.420 5.140 1.00105.76 C ANISOU 3037 CD GLU A 402 14495 15076 10613 1138 1853 1023 C ATOM 3038 OE1 GLU A 402 32.628 13.868 4.284 1.00107.37 O ANISOU 3038 OE1 GLU A 402 14498 15237 11061 1109 1647 942 O ATOM 3039 OE2 GLU A 402 30.876 13.892 5.604 1.00107.20 O ANISOU 3039 OE2 GLU A 402 14762 15119 10851 1192 2134 1304 O ATOM 3040 N THR A 403 33.629 18.152 7.596 1.00113.16 N ANISOU 3040 N THR A 403 16128 16695 10170 1186 1403 349 N ATOM 3041 CA THR A 403 34.087 18.017 8.969 1.00121.40 C ANISOU 3041 CA THR A 403 17515 17883 10728 1373 1273 446 C ATOM 3042 C THR A 403 33.140 17.105 9.740 1.00134.52 C ANISOU 3042 C THR A 403 19376 19454 12283 1550 1613 816 C ATOM 3043 O THR A 403 32.227 16.497 9.175 1.00137.60 O ANISOU 3043 O THR A 403 19591 19662 13030 1513 1905 1001 O ATOM 3044 CB THR A 403 34.204 19.386 9.640 1.00115.47 C ANISOU 3044 CB THR A 403 17049 17251 9572 1356 1188 190 C ATOM 3045 OG1 THR A 403 32.938 20.054 9.590 1.00114.70 O ANISOU 3045 OG1 THR A 403 17045 17045 9491 1328 1588 170 O ATOM 3046 CG2 THR A 403 35.248 20.230 8.929 1.00113.73 C ANISOU 3046 CG2 THR A 403 16615 17114 9483 1169 817 -140 C ATOM 3047 N MET A 404 33.366 17.021 11.049 1.00138.38 N ANISOU 3047 N MET A 404 20240 20064 12273 1738 1562 932 N ATOM 3048 CA MET A 404 32.606 16.098 11.881 1.00140.32 C ANISOU 3048 CA MET A 404 20698 20243 12374 1925 1873 1322 C ATOM 3049 C MET A 404 31.119 16.419 11.828 1.00132.01 C ANISOU 3049 C MET A 404 19669 19054 11433 1908 2394 1431 C ATOM 3050 O MET A 404 30.713 17.584 11.838 1.00128.95 O ANISOU 3050 O MET A 404 19379 18696 10921 1856 2514 1203 O ATOM 3051 CB MET A 404 33.103 16.153 13.323 1.00152.76 C ANISOU 3051 CB MET A 404 22736 21992 13315 2137 1726 1394 C ATOM 3052 CG MET A 404 32.319 15.274 14.282 1.00161.35 C ANISOU 3052 CG MET A 404 24094 23028 14185 2347 2081 1820 C ATOM 3053 SD MET A 404 32.904 15.440 15.975 1.00166.07 S ANISOU 3053 SD MET A 404 25306 23837 13955 2608 1893 1882 S ATOM 3054 CE MET A 404 31.783 14.335 16.827 1.00176.41 C ANISOU 3054 CE MET A 404 26844 25045 15139 2825 2430 2440 C ATOM 3055 N GLY A 405 30.304 15.368 11.763 1.00135.38 N ANISOU 3055 N GLY A 405 19988 19317 12133 1952 2696 1792 N ATOM 3056 CA GLY A 405 28.866 15.506 11.737 1.00133.65 C ANISOU 3056 CA GLY A 405 19737 18954 12091 1942 3199 1968 C ATOM 3057 C GLY A 405 28.258 15.671 10.363 1.00129.05 C ANISOU 3057 C GLY A 405 18739 18188 12106 1717 3278 1861 C ATOM 3058 O GLY A 405 27.030 15.774 10.259 1.00127.66 O ANISOU 3058 O GLY A 405 18478 17875 12152 1693 3673 2018 O ATOM 3059 N GLY A 406 29.069 15.694 9.308 1.00129.47 N ANISOU 3059 N GLY A 406 18531 18236 12428 1559 2920 1612 N ATOM 3060 CA GLY A 406 28.573 15.926 7.970 1.00124.81 C ANISOU 3060 CA GLY A 406 17593 17484 12346 1349 2953 1479 C ATOM 3061 C GLY A 406 28.472 17.381 7.571 1.00121.11 C ANISOU 3061 C GLY A 406 17113 17079 11824 1232 2944 1136 C ATOM 3062 O GLY A 406 28.116 17.668 6.422 1.00115.66 O ANISOU 3062 O GLY A 406 16151 16266 11530 1054 2940 1009 O ATOM 3063 N VAL A 407 28.765 18.308 8.483 1.00113.40 N ANISOU 3063 N VAL A 407 16448 16275 10365 1328 2927 983 N ATOM 3064 CA VAL A 407 28.751 19.725 8.152 1.00112.70 C ANISOU 3064 CA VAL A 407 16376 16229 10214 1219 2887 644 C ATOM 3065 C VAL A 407 29.929 20.043 7.240 1.00112.31 C ANISOU 3065 C VAL A 407 16126 16249 10297 1051 2457 348 C ATOM 3066 O VAL A 407 30.982 19.394 7.296 1.00117.07 O ANISOU 3066 O VAL A 407 16696 16942 10842 1081 2157 360 O ATOM 3067 CB VAL A 407 28.785 20.568 9.441 1.00113.96 C ANISOU 3067 CB VAL A 407 16972 16530 9796 1385 2962 555 C ATOM 3068 CG1 VAL A 407 28.697 22.056 9.136 1.00112.76 C ANISOU 3068 CG1 VAL A 407 16861 16384 9597 1280 2933 207 C ATOM 3069 CG2 VAL A 407 27.656 20.155 10.367 1.00117.18 C ANISOU 3069 CG2 VAL A 407 17582 16884 10056 1582 3436 888 C ATOM 3070 N MET A 408 29.750 21.037 6.378 1.00116.03 N ANISOU 3070 N MET A 408 16447 16672 10967 880 2439 102 N ATOM 3071 CA MET A 408 30.792 21.470 5.464 1.00114.09 C ANISOU 3071 CA MET A 408 16003 16487 10858 711 2085 -168 C ATOM 3072 C MET A 408 31.419 22.767 5.961 1.00112.12 C ANISOU 3072 C MET A 408 15960 16372 10270 681 1891 -459 C ATOM 3073 O MET A 408 30.743 23.628 6.529 1.00110.03 O ANISOU 3073 O MET A 408 15924 16082 9799 730 2085 -529 O ATOM 3074 CB MET A 408 30.231 21.659 4.054 1.00115.17 C ANISOU 3074 CB MET A 408 15830 16466 11465 523 2164 -232 C ATOM 3075 CG MET A 408 31.276 21.966 3.007 1.00121.12 C ANISOU 3075 CG MET A 408 16363 17275 12384 359 1851 -463 C ATOM 3076 SD MET A 408 30.548 22.027 1.369 1.00126.68 S ANISOU 3076 SD MET A 408 16762 17780 13589 169 1951 -499 S ATOM 3077 CE MET A 408 31.829 22.877 0.452 1.00128.20 C ANISOU 3077 CE MET A 408 16801 18093 13817 -5 1633 -806 C ATOM 3078 N THR A 409 32.725 22.893 5.738 1.00109.33 N ANISOU 3078 N THR A 409 15517 16144 9881 604 1504 -626 N ATOM 3079 CA THR A 409 33.521 24.022 6.202 1.00110.90 C ANISOU 3079 CA THR A 409 15883 16461 9794 551 1227 -896 C ATOM 3080 C THR A 409 34.187 24.680 5.004 1.00106.45 C ANISOU 3080 C THR A 409 15014 15895 9539 317 1015 -1117 C ATOM 3081 O THR A 409 34.954 24.032 4.285 1.00102.44 O ANISOU 3081 O THR A 409 14224 15428 9268 261 847 -1082 O ATOM 3082 CB THR A 409 34.568 23.562 7.216 1.00116.17 C ANISOU 3082 CB THR A 409 16730 17293 10115 681 916 -856 C ATOM 3083 OG1 THR A 409 33.910 23.082 8.395 1.00112.50 O ANISOU 3083 OG1 THR A 409 16611 16833 9300 907 1134 -651 O ATOM 3084 CG2 THR A 409 35.506 24.702 7.580 1.00124.10 C ANISOU 3084 CG2 THR A 409 17862 18401 10890 588 547 -1147 C ATOM 3085 N THR A 410 33.906 25.965 4.802 1.00104.02 N ANISOU 3085 N THR A 410 14769 15532 9221 195 1037 -1336 N ATOM 3086 CA THR A 410 34.368 26.674 3.616 1.00 99.38 C ANISOU 3086 CA THR A 410 13904 14917 8938 -35 897 -1517 C ATOM 3087 C THR A 410 35.822 27.104 3.768 1.00100.81 C ANISOU 3087 C THR A 410 14029 15244 9031 -130 473 -1682 C ATOM 3088 O THR A 410 36.192 27.745 4.756 1.00103.65 O ANISOU 3088 O THR A 410 14659 15662 9062 -97 279 -1810 O ATOM 3089 CB THR A 410 33.489 27.895 3.351 1.00100.89 C ANISOU 3089 CB THR A 410 14185 14971 9176 -128 1077 -1667 C ATOM 3090 OG1 THR A 410 32.191 27.466 2.923 1.00104.85 O ANISOU 3090 OG1 THR A 410 14622 15329 9888 -78 1444 -1496 O ATOM 3091 CG2 THR A 410 34.100 28.770 2.275 1.00 96.68 C ANISOU 3091 CG2 THR A 410 13418 14420 8895 -370 890 -1859 C ATOM 3092 N LEU A 411 36.643 26.746 2.782 1.00 99.47 N ANISOU 3092 N LEU A 411 13509 15124 9162 -244 327 -1676 N ATOM 3093 CA LEU A 411 38.017 27.217 2.670 1.00100.64 C ANISOU 3093 CA LEU A 411 13495 15396 9349 -373 -47 -1813 C ATOM 3094 C LEU A 411 38.157 28.384 1.707 1.00104.37 C ANISOU 3094 C LEU A 411 13799 15805 10053 -616 -78 -1994 C ATOM 3095 O LEU A 411 38.915 29.319 1.978 1.00114.15 O ANISOU 3095 O LEU A 411 15055 17086 11231 -746 -360 -2161 O ATOM 3096 CB LEU A 411 38.930 26.078 2.216 1.00100.13 C ANISOU 3096 CB LEU A 411 13129 15437 9480 -320 -166 -1671 C ATOM 3097 CG LEU A 411 38.836 24.805 3.049 1.00101.66 C ANISOU 3097 CG LEU A 411 13455 15674 9497 -80 -140 -1458 C ATOM 3098 CD1 LEU A 411 39.756 23.754 2.483 1.00101.48 C ANISOU 3098 CD1 LEU A 411 13115 15729 9714 -27 -254 -1338 C ATOM 3099 CD2 LEU A 411 39.183 25.094 4.496 1.00106.47 C ANISOU 3099 CD2 LEU A 411 14387 16376 9692 17 -381 -1495 C ATOM 3100 N ILE A 412 37.450 28.343 0.578 1.00 97.96 N ANISOU 3100 N ILE A 412 12830 14881 9511 -686 184 -1956 N ATOM 3101 CA ILE A 412 37.431 29.433 -0.391 1.00 94.20 C ANISOU 3101 CA ILE A 412 12221 14324 9247 -906 195 -2097 C ATOM 3102 C ILE A 412 35.978 29.688 -0.766 1.00 92.21 C ANISOU 3102 C ILE A 412 12085 13892 9060 -894 519 -2073 C ATOM 3103 O ILE A 412 35.315 28.806 -1.324 1.00 90.40 O ANISOU 3103 O ILE A 412 11767 13602 8979 -822 733 -1922 O ATOM 3104 CB ILE A 412 38.261 29.121 -1.647 1.00 92.76 C ANISOU 3104 CB ILE A 412 11666 14203 9377 -1020 145 -2061 C ATOM 3105 CG1 ILE A 412 39.688 28.729 -1.259 1.00 95.04 C ANISOU 3105 CG1 ILE A 412 11786 14674 9651 -1000 -155 -2044 C ATOM 3106 CG2 ILE A 412 38.274 30.321 -2.576 1.00 91.67 C ANISOU 3106 CG2 ILE A 412 11420 13984 9425 -1250 153 -2187 C ATOM 3107 CD1 ILE A 412 40.565 28.358 -2.432 1.00101.30 C ANISOU 3107 CD1 ILE A 412 12202 15542 10745 -1072 -164 -1991 C ATOM 3108 N ALA A 413 35.482 30.882 -0.459 1.00 98.31 N ANISOU 3108 N ALA A 413 13050 14563 9741 -963 541 -2220 N ATOM 3109 CA ALA A 413 34.078 31.188 -0.671 1.00 98.96 C ANISOU 3109 CA ALA A 413 13243 14471 9886 -928 845 -2191 C ATOM 3110 C ALA A 413 33.805 31.511 -2.135 1.00 94.03 C ANISOU 3110 C ALA A 413 12381 13745 9600 -1096 928 -2189 C ATOM 3111 O ALA A 413 34.706 31.852 -2.905 1.00100.24 O ANISOU 3111 O ALA A 413 12972 14584 10529 -1261 760 -2254 O ATOM 3112 CB ALA A 413 33.640 32.358 0.208 1.00109.27 C ANISOU 3112 CB ALA A 413 14860 15690 10966 -907 852 -2355 C ATOM 3113 N LYS A 414 32.532 31.398 -2.510 1.00 87.41 N ANISOU 3113 N LYS A 414 11562 12756 8893 -1050 1191 -2097 N ATOM 3114 CA LYS A 414 32.119 31.697 -3.871 1.00 85.13 C ANISOU 3114 CA LYS A 414 11094 12351 8900 -1193 1260 -2084 C ATOM 3115 C LYS A 414 32.393 33.157 -4.203 1.00 85.41 C ANISOU 3115 C LYS A 414 11152 12322 8977 -1373 1149 -2260 C ATOM 3116 O LYS A 414 32.467 34.015 -3.321 1.00 87.31 O ANISOU 3116 O LYS A 414 11593 12543 9038 -1363 1082 -2396 O ATOM 3117 CB LYS A 414 30.634 31.390 -4.059 1.00 84.16 C ANISOU 3117 CB LYS A 414 10997 12061 8919 -1108 1526 -1949 C ATOM 3118 CG LYS A 414 29.710 32.182 -3.150 1.00 90.02 C ANISOU 3118 CG LYS A 414 11961 12698 9543 -1014 1688 -1992 C ATOM 3119 CD LYS A 414 28.264 32.100 -3.615 1.00 93.20 C ANISOU 3119 CD LYS A 414 12304 12915 10193 -976 1936 -1855 C ATOM 3120 CE LYS A 414 27.339 32.893 -2.706 1.00 97.86 C ANISOU 3120 CE LYS A 414 13098 13401 10682 -850 2142 -1887 C ATOM 3121 NZ LYS A 414 25.969 33.033 -3.274 1.00 99.44 N ANISOU 3121 NZ LYS A 414 13187 13407 11190 -838 2358 -1760 N ATOM 3122 N ASN A 415 32.555 33.426 -5.498 1.00 85.39 N ANISOU 3122 N ASN A 415 10964 12277 9205 -1534 1124 -2256 N ATOM 3123 CA ASN A 415 32.838 34.753 -6.035 1.00 92.50 C ANISOU 3123 CA ASN A 415 11848 13100 10197 -1729 1025 -2382 C ATOM 3124 C ASN A 415 34.199 35.291 -5.600 1.00 96.31 C ANISOU 3124 C ASN A 415 12306 13707 10581 -1840 768 -2507 C ATOM 3125 O ASN A 415 34.406 36.508 -5.583 1.00107.03 O ANISOU 3125 O ASN A 415 13725 14979 11964 -1984 658 -2636 O ATOM 3126 CB ASN A 415 31.725 35.746 -5.670 1.00 96.91 C ANISOU 3126 CB ASN A 415 12602 13464 10757 -1705 1145 -2449 C ATOM 3127 CG ASN A 415 30.352 35.275 -6.124 1.00 94.16 C ANISOU 3127 CG ASN A 415 12230 12980 10567 -1610 1382 -2304 C ATOM 3128 OD1 ASN A 415 30.144 34.960 -7.297 1.00 91.67 O ANISOU 3128 OD1 ASN A 415 11755 12622 10455 -1688 1403 -2212 O ATOM 3129 ND2 ASN A 415 29.409 35.216 -5.191 1.00 98.28 N ANISOU 3129 ND2 ASN A 415 12913 13431 10999 -1437 1557 -2275 N ATOM 3130 N THR A 416 35.138 34.413 -5.251 1.00 93.37 N ANISOU 3130 N THR A 416 11834 13521 10124 -1781 650 -2464 N ATOM 3131 CA THR A 416 36.509 34.825 -4.976 1.00 91.23 C ANISOU 3131 CA THR A 416 11464 13374 9827 -1902 377 -2550 C ATOM 3132 C THR A 416 37.268 34.980 -6.287 1.00 92.64 C ANISOU 3132 C THR A 416 11349 13598 10253 -2080 355 -2500 C ATOM 3133 O THR A 416 37.221 34.094 -7.145 1.00 98.41 O ANISOU 3133 O THR A 416 11929 14376 11085 -2025 494 -2378 O ATOM 3134 CB THR A 416 37.213 33.802 -4.083 1.00 93.36 C ANISOU 3134 CB THR A 416 11721 13822 9927 -1751 252 -2502 C ATOM 3135 OG1 THR A 416 36.598 33.774 -2.790 1.00 95.34 O ANISOU 3135 OG1 THR A 416 12283 14040 9902 -1589 266 -2548 O ATOM 3136 CG2 THR A 416 38.686 34.148 -3.931 1.00102.84 C ANISOU 3136 CG2 THR A 416 12747 15156 11170 -1887 -54 -2561 C ATOM 3137 N THR A 417 37.966 36.103 -6.444 1.00 93.90 N ANISOU 3137 N THR A 417 11442 13730 10505 -2289 185 -2591 N ATOM 3138 CA THR A 417 38.715 36.348 -7.670 1.00 90.70 C ANISOU 3138 CA THR A 417 10759 13369 10333 -2465 192 -2521 C ATOM 3139 C THR A 417 39.806 35.300 -7.846 1.00 89.39 C ANISOU 3139 C THR A 417 10328 13421 10213 -2399 150 -2418 C ATOM 3140 O THR A 417 40.499 34.936 -6.894 1.00 93.65 O ANISOU 3140 O THR A 417 10843 14080 10658 -2333 -42 -2442 O ATOM 3141 CB THR A 417 39.323 37.748 -7.647 1.00101.94 C ANISOU 3141 CB THR A 417 12152 14714 11867 -2711 -4 -2619 C ATOM 3142 OG1 THR A 417 38.277 38.719 -7.557 1.00103.56 O ANISOU 3142 OG1 THR A 417 12608 14693 12046 -2752 54 -2714 O ATOM 3143 CG2 THR A 417 40.125 38.005 -8.907 1.00111.92 C ANISOU 3143 CG2 THR A 417 13116 16032 13378 -2893 39 -2510 C ATOM 3144 N ILE A 418 39.948 34.809 -9.072 1.00 88.08 N ANISOU 3144 N ILE A 418 9981 13300 10186 -2401 327 -2303 N ATOM 3145 CA ILE A 418 40.915 33.763 -9.375 1.00 88.69 C ANISOU 3145 CA ILE A 418 9808 13566 10323 -2303 342 -2201 C ATOM 3146 C ILE A 418 41.959 34.290 -10.358 1.00 89.97 C ANISOU 3146 C ILE A 418 9679 13805 10701 -2479 357 -2136 C ATOM 3147 O ILE A 418 41.681 35.232 -11.100 1.00 96.40 O ANISOU 3147 O ILE A 418 10518 14508 11603 -2650 428 -2139 O ATOM 3148 CB ILE A 418 40.212 32.508 -9.925 1.00 86.55 C ANISOU 3148 CB ILE A 418 9599 13282 10004 -2098 562 -2118 C ATOM 3149 CG1 ILE A 418 39.491 32.827 -11.236 1.00 84.77 C ANISOU 3149 CG1 ILE A 418 9424 12928 9856 -2173 759 -2087 C ATOM 3150 CG2 ILE A 418 39.245 31.957 -8.897 1.00 85.75 C ANISOU 3150 CG2 ILE A 418 9746 13111 9725 -1931 560 -2142 C ATOM 3151 CD1 ILE A 418 38.811 31.637 -11.867 1.00 83.05 C ANISOU 3151 CD1 ILE A 418 9279 12667 9608 -1995 930 -2019 C ATOM 3152 N PRO A 419 43.166 33.690 -10.376 1.00 98.46 N ANISOU 3152 N PRO A 419 10466 15068 11875 -2432 303 -2057 N ATOM 3153 CA PRO A 419 43.668 32.565 -9.575 1.00 98.62 C ANISOU 3153 CA PRO A 419 10416 15229 11827 -2228 201 -2028 C ATOM 3154 C PRO A 419 43.794 32.908 -8.100 1.00102.33 C ANISOU 3154 C PRO A 419 11008 15701 12172 -2245 -107 -2125 C ATOM 3155 O PRO A 419 43.985 34.073 -7.761 1.00 99.38 O ANISOU 3155 O PRO A 419 10660 15261 11839 -2449 -290 -2211 O ATOM 3156 CB PRO A 419 45.049 32.286 -10.181 1.00101.49 C ANISOU 3156 CB PRO A 419 10379 15771 12412 -2244 220 -1911 C ATOM 3157 CG PRO A 419 45.016 32.916 -11.528 1.00104.33 C ANISOU 3157 CG PRO A 419 10659 16083 12900 -2388 446 -1858 C ATOM 3158 CD PRO A 419 44.163 34.128 -11.366 1.00103.04 C ANISOU 3158 CD PRO A 419 10737 15732 12681 -2582 376 -1960 C ATOM 3159 N THR A 420 43.676 31.907 -7.233 1.00104.58 N ANISOU 3159 N THR A 420 11396 16046 12294 -2029 -171 -2110 N ATOM 3160 CA THR A 420 43.749 32.149 -5.801 1.00110.26 C ANISOU 3160 CA THR A 420 12292 16772 12831 -2012 -459 -2198 C ATOM 3161 C THR A 420 44.346 30.927 -5.125 1.00106.75 C ANISOU 3161 C THR A 420 11764 16478 12320 -1795 -571 -2109 C ATOM 3162 O THR A 420 44.349 29.824 -5.677 1.00 96.70 O ANISOU 3162 O THR A 420 10382 15256 11103 -1625 -381 -1996 O ATOM 3163 CB THR A 420 42.373 32.475 -5.205 1.00109.91 C ANISOU 3163 CB THR A 420 12657 16560 12544 -1962 -378 -2297 C ATOM 3164 OG1 THR A 420 42.531 32.915 -3.851 1.00111.27 O ANISOU 3164 OG1 THR A 420 13035 16732 12511 -1961 -662 -2405 O ATOM 3165 CG2 THR A 420 41.475 31.254 -5.227 1.00107.58 C ANISOU 3165 CG2 THR A 420 12499 16243 12133 -1723 -143 -2205 C ATOM 3166 N LYS A 421 44.860 31.144 -3.917 1.00122.23 N ANISOU 3166 N LYS A 421 13795 18493 14156 -1799 -904 -2164 N ATOM 3167 CA LYS A 421 45.505 30.097 -3.142 1.00128.59 C ANISOU 3167 CA LYS A 421 14532 19439 14889 -1603 -1079 -2073 C ATOM 3168 C LYS A 421 45.022 30.195 -1.704 1.00122.92 C ANISOU 3168 C LYS A 421 14204 18681 13818 -1517 -1282 -2157 C ATOM 3169 O LYS A 421 44.764 31.289 -1.198 1.00125.98 O ANISOU 3169 O LYS A 421 14810 18975 14082 -1660 -1429 -2310 O ATOM 3170 CB LYS A 421 47.036 30.217 -3.209 1.00141.37 C ANISOU 3170 CB LYS A 421 15734 21210 16771 -1700 -1350 -2015 C ATOM 3171 CG LYS A 421 47.773 28.892 -3.187 1.00149.30 C ANISOU 3171 CG LYS A 421 16494 22365 17869 -1474 -1362 -1853 C ATOM 3172 CD LYS A 421 49.289 29.073 -3.150 1.00154.01 C ANISOU 3172 CD LYS A 421 16649 23111 18757 -1568 -1653 -1782 C ATOM 3173 CE LYS A 421 49.852 29.498 -4.495 1.00151.26 C ANISOU 3173 CE LYS A 421 15910 22795 18765 -1720 -1435 -1721 C ATOM 3174 NZ LYS A 421 51.326 29.319 -4.555 1.00153.16 N ANISOU 3174 NZ LYS A 421 15650 23201 19342 -1736 -1630 -1588 N ATOM 3175 N HIS A 422 44.884 29.042 -1.053 1.00116.22 N ANISOU 3175 N HIS A 422 13469 17894 12798 -1271 -1277 -2053 N ATOM 3176 CA HIS A 422 44.521 29.020 0.360 1.00117.36 C ANISOU 3176 CA HIS A 422 13995 18026 12571 -1156 -1461 -2101 C ATOM 3177 C HIS A 422 45.175 27.825 1.035 1.00118.91 C ANISOU 3177 C HIS A 422 14127 18358 12694 -940 -1633 -1950 C ATOM 3178 O HIS A 422 44.964 26.685 0.616 1.00120.10 O ANISOU 3178 O HIS A 422 14185 18523 12923 -765 -1407 -1799 O ATOM 3179 CB HIS A 422 43.004 28.960 0.548 1.00113.51 C ANISOU 3179 CB HIS A 422 13884 17394 11852 -1053 -1139 -2119 C ATOM 3180 CG HIS A 422 42.578 28.938 1.981 1.00115.44 C ANISOU 3180 CG HIS A 422 14548 17629 11686 -910 -1261 -2152 C ATOM 3181 ND1 HIS A 422 42.436 27.770 2.697 1.00114.90 N ANISOU 3181 ND1 HIS A 422 14611 17621 11423 -666 -1235 -1994 N ATOM 3182 CD2 HIS A 422 42.276 29.943 2.835 1.00119.64 C ANISOU 3182 CD2 HIS A 422 15421 18091 11947 -964 -1402 -2323 C ATOM 3183 CE1 HIS A 422 42.057 28.055 3.929 1.00119.14 C ANISOU 3183 CE1 HIS A 422 15558 18142 11569 -574 -1338 -2053 C ATOM 3184 NE2 HIS A 422 41.953 29.367 4.039 1.00123.71 N ANISOU 3184 NE2 HIS A 422 16280 18641 12085 -743 -1440 -2265 N ATOM 3185 N SER A 423 45.952 28.087 2.081 1.00115.66 N ANISOU 3185 N SER A 423 13782 18029 12136 -950 -2054 -1992 N ATOM 3186 CA SER A 423 46.669 27.050 2.807 1.00118.33 C ANISOU 3186 CA SER A 423 14062 18497 12402 -752 -2288 -1844 C ATOM 3187 C SER A 423 46.067 26.859 4.192 1.00122.81 C ANISOU 3187 C SER A 423 15132 19042 12487 -585 -2396 -1853 C ATOM 3188 O SER A 423 45.588 27.811 4.816 1.00126.75 O ANISOU 3188 O SER A 423 15981 19463 12717 -667 -2478 -2023 O ATOM 3189 CB SER A 423 48.154 27.394 2.936 1.00121.20 C ANISOU 3189 CB SER A 423 14073 18985 12994 -879 -2739 -1849 C ATOM 3190 OG SER A 423 48.740 27.593 1.664 1.00123.55 O ANISOU 3190 OG SER A 423 13897 19312 13735 -1025 -2601 -1817 O ATOM 3191 N GLN A 424 46.097 25.616 4.670 1.00116.52 N ANISOU 3191 N GLN A 424 14387 18309 11578 -337 -2382 -1663 N ATOM 3192 CA GLN A 424 45.608 25.309 6.005 1.00118.71 C ANISOU 3192 CA GLN A 424 15138 18584 11384 -152 -2473 -1624 C ATOM 3193 C GLN A 424 46.412 24.153 6.579 1.00121.42 C ANISOU 3193 C GLN A 424 15383 19048 11703 54 -2721 -1419 C ATOM 3194 O GLN A 424 46.841 23.254 5.851 1.00120.33 O ANISOU 3194 O GLN A 424 14881 18948 11891 132 -2618 -1267 O ATOM 3195 CB GLN A 424 44.112 24.972 6.000 1.00115.95 C ANISOU 3195 CB GLN A 424 15103 18107 10844 -29 -1992 -1567 C ATOM 3196 CG GLN A 424 43.552 24.667 7.375 1.00118.49 C ANISOU 3196 CG GLN A 424 15927 18430 10664 176 -2017 -1500 C ATOM 3197 CD GLN A 424 42.055 24.857 7.455 1.00121.36 C ANISOU 3197 CD GLN A 424 16617 18656 10838 231 -1565 -1506 C ATOM 3198 OE1 GLN A 424 41.483 25.685 6.748 1.00116.21 O ANISOU 3198 OE1 GLN A 424 15916 17902 10336 72 -1357 -1650 O ATOM 3199 NE2 GLN A 424 41.408 24.087 8.324 1.00132.04 N ANISOU 3199 NE2 GLN A 424 18295 20002 11874 460 -1405 -1327 N ATOM 3200 N VAL A 425 46.612 24.188 7.895 1.00127.73 N ANISOU 3200 N VAL A 425 16533 19900 12100 155 -3055 -1418 N ATOM 3201 CA VAL A 425 47.417 23.201 8.603 1.00130.08 C ANISOU 3201 CA VAL A 425 16787 20310 12326 351 -3371 -1224 C ATOM 3202 C VAL A 425 46.513 22.090 9.110 1.00129.52 C ANISOU 3202 C VAL A 425 17034 20195 11982 620 -3066 -1009 C ATOM 3203 O VAL A 425 45.489 22.349 9.754 1.00128.00 O ANISOU 3203 O VAL A 425 17307 19932 11394 681 -2863 -1042 O ATOM 3204 CB VAL A 425 48.199 23.845 9.758 1.00136.59 C ANISOU 3204 CB VAL A 425 17830 21213 12855 308 -3962 -1330 C ATOM 3205 CG1 VAL A 425 48.936 22.782 10.550 1.00141.85 C ANISOU 3205 CG1 VAL A 425 18495 21990 13413 534 -4294 -1105 C ATOM 3206 CG2 VAL A 425 49.167 24.878 9.215 1.00143.42 C ANISOU 3206 CG2 VAL A 425 18314 22105 14073 21 -4288 -1508 C ATOM 3207 N PHE A 426 46.895 20.854 8.816 1.00133.31 N ANISOU 3207 N PHE A 426 17256 20705 12691 786 -3021 -780 N ATOM 3208 CA PHE A 426 46.201 19.671 9.290 1.00131.29 C ANISOU 3208 CA PHE A 426 17248 20395 12241 1040 -2783 -534 C ATOM 3209 C PHE A 426 47.158 18.832 10.122 1.00134.39 C ANISOU 3209 C PHE A 426 17629 20894 12539 1236 -3193 -339 C ATOM 3210 O PHE A 426 48.383 18.919 9.973 1.00145.42 O ANISOU 3210 O PHE A 426 18672 22396 14184 1186 -3585 -361 O ATOM 3211 CB PHE A 426 45.651 18.835 8.129 1.00132.18 C ANISOU 3211 CB PHE A 426 17098 20393 12733 1081 -2329 -421 C ATOM 3212 CG PHE A 426 44.552 19.512 7.362 1.00137.21 C ANISOU 3212 CG PHE A 426 17787 20906 13440 920 -1915 -568 C ATOM 3213 CD1 PHE A 426 44.846 20.482 6.422 1.00141.76 C ANISOU 3213 CD1 PHE A 426 18087 21490 14284 685 -1917 -784 C ATOM 3214 CD2 PHE A 426 43.225 19.178 7.585 1.00136.62 C ANISOU 3214 CD2 PHE A 426 18025 20703 13182 1005 -1526 -468 C ATOM 3215 CE1 PHE A 426 43.840 21.112 5.715 1.00136.96 C ANISOU 3215 CE1 PHE A 426 17533 20762 13742 544 -1562 -907 C ATOM 3216 CE2 PHE A 426 42.211 19.806 6.879 1.00132.43 C ANISOU 3216 CE2 PHE A 426 17517 20054 12747 862 -1170 -590 C ATOM 3217 CZ PHE A 426 42.520 20.774 5.942 1.00131.38 C ANISOU 3217 CZ PHE A 426 17127 19929 12864 635 -1199 -814 C ATOM 3218 N SER A 427 46.583 18.007 10.994 1.00146.37 N ANISOU 3218 N SER A 427 19522 22378 13714 1461 -3095 -124 N ATOM 3219 CA SER A 427 47.367 17.190 11.906 1.00142.79 C ANISOU 3219 CA SER A 427 19141 22012 13102 1671 -3481 89 C ATOM 3220 C SER A 427 46.649 15.869 12.146 1.00137.91 C ANISOU 3220 C SER A 427 18702 21293 12405 1915 -3161 398 C ATOM 3221 O SER A 427 45.527 15.650 11.685 1.00134.64 O ANISOU 3221 O SER A 427 18373 20743 12042 1907 -2664 437 O ATOM 3222 CB SER A 427 47.612 17.921 13.229 1.00152.34 C ANISOU 3222 CB SER A 427 20799 23316 13768 1676 -3904 -2 C ATOM 3223 OG SER A 427 48.611 17.268 13.991 1.00159.43 O ANISOU 3223 OG SER A 427 21683 24315 14579 1841 -4392 177 O ATOM 3224 N THR A 428 47.317 14.984 12.878 1.00141.71 N ANISOU 3224 N THR A 428 19229 21829 12784 2126 -3472 632 N ATOM 3225 CA THR A 428 46.715 13.719 13.259 1.00142.34 C ANISOU 3225 CA THR A 428 19516 21805 12763 2365 -3225 957 C ATOM 3226 C THR A 428 45.737 13.922 14.413 1.00144.26 C ANISOU 3226 C THR A 428 20386 22036 12389 2449 -3070 1039 C ATOM 3227 O THR A 428 45.799 14.907 15.153 1.00155.11 O ANISOU 3227 O THR A 428 22079 23509 13347 2384 -3294 863 O ATOM 3228 CB THR A 428 47.791 12.703 13.652 1.00146.07 C ANISOU 3228 CB THR A 428 19826 22331 13345 2577 -3621 1197 C ATOM 3229 OG1 THR A 428 48.647 13.275 14.647 1.00150.63 O ANISOU 3229 OG1 THR A 428 20571 23073 13589 2583 -4191 1139 O ATOM 3230 CG2 THR A 428 48.626 12.321 12.445 1.00144.22 C ANISOU 3230 CG2 THR A 428 18967 22081 13749 2547 -3653 1158 C ATOM 3231 N ALA A 429 44.812 12.972 14.551 1.00159.24 N ANISOU 3231 N ALA A 429 22466 23799 14239 2599 -2669 1314 N ATOM 3232 CA ALA A 429 43.838 12.990 15.633 1.00159.11 C ANISOU 3232 CA ALA A 429 23024 23765 13667 2717 -2440 1463 C ATOM 3233 C ALA A 429 44.020 11.850 16.624 1.00157.66 C ANISOU 3233 C ALA A 429 23108 23580 13216 2989 -2573 1843 C ATOM 3234 O ALA A 429 43.462 11.915 17.727 1.00153.41 O ANISOU 3234 O ALA A 429 23097 23073 12118 3117 -2485 1979 O ATOM 3235 CB ALA A 429 42.411 12.950 15.065 1.00155.50 C ANISOU 3235 CB ALA A 429 22597 23138 13346 2648 -1800 1499 C ATOM 3236 N GLU A 430 44.787 10.821 16.271 1.00176.31 N ANISOU 3236 N GLU A 430 25137 25904 15951 3096 -2772 2024 N ATOM 3237 CA GLU A 430 45.007 9.675 17.139 1.00184.34 C ANISOU 3237 CA GLU A 430 26372 26896 16771 3359 -2915 2407 C ATOM 3238 C GLU A 430 46.487 9.319 17.137 1.00187.12 C ANISOU 3238 C GLU A 430 26411 27346 17341 3442 -3501 2425 C ATOM 3239 O GLU A 430 47.234 9.674 16.220 1.00185.72 O ANISOU 3239 O GLU A 430 25748 27209 17608 3307 -3670 2197 O ATOM 3240 CB GLU A 430 44.167 8.470 16.701 1.00190.51 C ANISOU 3240 CB GLU A 430 27082 27446 17857 3452 -2445 2712 C ATOM 3241 CG GLU A 430 44.378 8.076 15.250 1.00197.20 C ANISOU 3241 CG GLU A 430 27364 28160 19403 3352 -2320 2602 C ATOM 3242 CD GLU A 430 43.413 7.005 14.784 1.00206.90 C ANISOU 3242 CD GLU A 430 28562 29124 20925 3406 -1858 2857 C ATOM 3243 OE1 GLU A 430 42.728 6.407 15.637 1.00215.49 O ANISOU 3243 OE1 GLU A 430 30019 30134 21723 3543 -1671 3182 O ATOM 3244 OE2 GLU A 430 43.337 6.765 13.561 1.00205.73 O ANISOU 3244 OE2 GLU A 430 28033 28838 21296 3309 -1685 2738 O ATOM 3245 N ASP A 431 46.898 8.610 18.186 1.00186.59 N ANISOU 3245 N ASP A 431 26622 27316 16956 3674 -3802 2720 N ATOM 3246 CA ASP A 431 48.285 8.188 18.321 1.00188.35 C ANISOU 3246 CA ASP A 431 26566 27626 17371 3789 -4386 2792 C ATOM 3247 C ASP A 431 48.695 7.286 17.162 1.00194.85 C ANISOU 3247 C ASP A 431 26812 28313 18909 3829 -4271 2861 C ATOM 3248 O ASP A 431 47.970 6.356 16.795 1.00198.31 O ANISOU 3248 O ASP A 431 27251 28549 19548 3915 -3854 3070 O ATOM 3249 CB ASP A 431 48.479 7.464 19.654 1.00183.85 C ANISOU 3249 CB ASP A 431 26449 27089 16319 4055 -4672 3149 C ATOM 3250 CG ASP A 431 47.440 6.385 19.888 1.00181.33 C ANISOU 3250 CG ASP A 431 26402 26578 15919 4218 -4181 3523 C ATOM 3251 OD1 ASP A 431 46.435 6.355 19.148 1.00173.93 O ANISOU 3251 OD1 ASP A 431 25377 25494 15214 4103 -3619 3478 O ATOM 3252 OD2 ASP A 431 47.622 5.575 20.820 1.00189.19 O ANISOU 3252 OD2 ASP A 431 27698 27561 16623 4454 -4371 3875 O ATOM 3253 N ASN A 432 49.863 7.574 16.585 1.00188.81 N ANISOU 3253 N ASN A 432 25555 27647 18536 3769 -4640 2684 N ATOM 3254 CA ASN A 432 50.423 6.788 15.484 1.00174.13 C ANISOU 3254 CA ASN A 432 23135 25680 17345 3836 -4564 2721 C ATOM 3255 C ASN A 432 49.438 6.673 14.323 1.00156.17 C ANISOU 3255 C ASN A 432 20725 23222 15389 3714 -3950 2611 C ATOM 3256 O ASN A 432 49.267 5.606 13.729 1.00154.91 O ANISOU 3256 O ASN A 432 20402 22868 15591 3845 -3710 2773 O ATOM 3257 CB ASN A 432 50.861 5.402 15.966 1.00177.46 C ANISOU 3257 CB ASN A 432 23573 26003 17851 4148 -4745 3108 C ATOM 3258 CG ASN A 432 51.847 5.467 17.117 1.00183.19 C ANISOU 3258 CG ASN A 432 24436 26902 18265 4281 -5396 3240 C ATOM 3259 OD1 ASN A 432 52.581 6.444 17.267 1.00187.14 O ANISOU 3259 OD1 ASN A 432 24806 27595 18704 4142 -5799 3015 O ATOM 3260 ND2 ASN A 432 51.870 4.422 17.938 1.00183.30 N ANISOU 3260 ND2 ASN A 432 24718 26836 18090 4546 -5526 3617 N ATOM 3261 N GLN A 433 48.771 7.781 14.005 1.00152.62 N ANISOU 3261 N GLN A 433 20363 22820 14806 3464 -3714 2331 N ATOM 3262 CA GLN A 433 47.865 7.803 12.863 1.00147.45 C ANISOU 3262 CA GLN A 433 19565 22003 14456 3324 -3183 2201 C ATOM 3263 C GLN A 433 48.674 7.695 11.576 1.00149.77 C ANISOU 3263 C GLN A 433 19281 22283 15343 3287 -3201 2040 C ATOM 3264 O GLN A 433 49.537 8.536 11.302 1.00146.90 O ANISOU 3264 O GLN A 433 18629 22090 15096 3163 -3469 1822 O ATOM 3265 CB GLN A 433 47.016 9.074 12.875 1.00144.82 C ANISOU 3265 CB GLN A 433 19459 21730 13834 3078 -2965 1946 C ATOM 3266 CG GLN A 433 45.817 9.024 11.940 1.00140.09 C ANISOU 3266 CG GLN A 433 18832 20943 13454 2955 -2404 1882 C ATOM 3267 CD GLN A 433 44.822 10.138 12.200 1.00138.33 C ANISOU 3267 CD GLN A 433 18918 20757 12886 2771 -2165 1710 C ATOM 3268 OE1 GLN A 433 45.043 10.999 13.051 1.00140.56 O ANISOU 3268 OE1 GLN A 433 19454 21201 12752 2732 -2411 1607 O ATOM 3269 NE2 GLN A 433 43.715 10.123 11.469 1.00134.61 N ANISOU 3269 NE2 GLN A 433 18432 20119 12594 2664 -1698 1677 N ATOM 3270 N SER A 434 48.399 6.644 10.796 1.00143.82 N ANISOU 3270 N SER A 434 18368 21313 14964 3401 -2913 2157 N ATOM 3271 CA SER A 434 49.201 6.352 9.613 1.00148.48 C ANISOU 3271 CA SER A 434 18450 21872 16093 3436 -2906 2040 C ATOM 3272 C SER A 434 49.055 7.430 8.554 1.00158.05 C ANISOU 3272 C SER A 434 19434 23146 17472 3170 -2704 1698 C ATOM 3273 O SER A 434 49.983 7.660 7.771 1.00162.80 O ANISOU 3273 O SER A 434 19604 23833 18418 3152 -2800 1554 O ATOM 3274 CB SER A 434 48.793 5.003 9.021 1.00142.43 C ANISOU 3274 CB SER A 434 17653 20821 15644 3617 -2621 2216 C ATOM 3275 OG SER A 434 47.459 5.039 8.564 1.00144.48 O ANISOU 3275 OG SER A 434 18288 20958 15650 3779 -2630 2542 O ATOM 3276 N ALA A 435 47.912 8.108 8.525 1.00154.22 N ANISOU 3276 N ALA A 435 19223 22620 16753 2971 -2416 1581 N ATOM 3277 CA ALA A 435 47.493 8.849 7.346 1.00147.71 C ANISOU 3277 CA ALA A 435 18221 21766 16136 2747 -2122 1305 C ATOM 3278 C ALA A 435 46.290 9.701 7.717 1.00142.67 C ANISOU 3278 C ALA A 435 17943 21118 15146 2553 -1905 1218 C ATOM 3279 O ALA A 435 45.581 9.412 8.686 1.00144.09 O ANISOU 3279 O ALA A 435 18508 21249 14991 2627 -1851 1407 O ATOM 3280 CB ALA A 435 47.156 7.896 6.196 1.00144.42 C ANISOU 3280 CB ALA A 435 17640 21113 16120 2829 -1799 1329 C ATOM 3281 N VAL A 436 46.069 10.763 6.944 1.00149.40 N ANISOU 3281 N VAL A 436 18670 22017 16078 2316 -1766 943 N ATOM 3282 CA VAL A 436 44.859 11.554 7.133 1.00145.33 C ANISOU 3282 CA VAL A 436 18460 21460 15298 2143 -1511 851 C ATOM 3283 C VAL A 436 44.148 11.685 5.794 1.00141.03 C ANISOU 3283 C VAL A 436 17756 20764 15064 1998 -1145 704 C ATOM 3284 O VAL A 436 44.783 11.719 4.737 1.00139.45 O ANISOU 3284 O VAL A 436 17211 20575 15198 1959 -1149 568 O ATOM 3285 CB VAL A 436 45.139 12.943 7.751 1.00148.20 C ANISOU 3285 CB VAL A 436 18940 22023 15348 1981 -1745 654 C ATOM 3286 CG1 VAL A 436 45.822 12.799 9.101 1.00152.85 C ANISOU 3286 CG1 VAL A 436 19734 22749 15592 2128 -2151 794 C ATOM 3287 CG2 VAL A 436 45.950 13.807 6.801 1.00150.74 C ANISOU 3287 CG2 VAL A 436 18868 22448 15958 1799 -1860 395 C ATOM 3288 N THR A 437 42.816 11.738 5.843 1.00144.63 N ANISOU 3288 N THR A 437 18468 21076 15410 1929 -824 746 N ATOM 3289 CA THR A 437 41.973 11.776 4.653 1.00138.49 C ANISOU 3289 CA THR A 437 17589 20122 14910 1797 -494 640 C ATOM 3290 C THR A 437 41.071 12.998 4.717 1.00129.18 C ANISOU 3290 C THR A 437 16574 18968 13540 1590 -324 484 C ATOM 3291 O THR A 437 40.355 13.191 5.705 1.00129.50 O ANISOU 3291 O THR A 437 16928 19012 13265 1614 -242 592 O ATOM 3292 CB THR A 437 41.123 10.507 4.534 1.00143.73 C ANISOU 3292 CB THR A 437 18357 20525 15729 1916 -263 877 C ATOM 3293 OG1 THR A 437 41.909 9.449 3.973 1.00155.97 O ANISOU 3293 OG1 THR A 437 19690 21994 17579 2078 -364 940 O ATOM 3294 CG2 THR A 437 39.895 10.750 3.669 1.00130.84 C ANISOU 3294 CG2 THR A 437 16742 18706 14267 1747 66 796 C ATOM 3295 N ILE A 438 41.096 13.813 3.662 1.00120.86 N ANISOU 3295 N ILE A 438 15319 17926 12675 1404 -254 241 N ATOM 3296 CA ILE A 438 40.344 15.063 3.600 1.00116.25 C ANISOU 3296 CA ILE A 438 14853 17360 11956 1203 -117 68 C ATOM 3297 C ILE A 438 39.294 14.944 2.505 1.00112.68 C ANISOU 3297 C ILE A 438 14343 16701 11771 1098 200 36 C ATOM 3298 O ILE A 438 39.605 14.538 1.383 1.00117.70 O ANISOU 3298 O ILE A 438 14747 17263 12711 1084 226 -27 O ATOM 3299 CB ILE A 438 41.273 16.259 3.333 1.00116.43 C ANISOU 3299 CB ILE A 438 14702 17568 11969 1049 -341 -183 C ATOM 3300 CG1 ILE A 438 42.458 16.238 4.296 1.00121.55 C ANISOU 3300 CG1 ILE A 438 15347 18405 12432 1152 -725 -144 C ATOM 3301 CG2 ILE A 438 40.516 17.552 3.468 1.00116.72 C ANISOU 3301 CG2 ILE A 438 14913 17608 11827 868 -230 -349 C ATOM 3302 CD1 ILE A 438 43.326 17.475 4.224 1.00128.03 C ANISOU 3302 CD1 ILE A 438 16019 19392 13235 979 -986 -370 C ATOM 3303 N HIS A 439 38.056 15.309 2.821 1.00110.12 N ANISOU 3303 N HIS A 439 14229 16279 11332 1033 435 79 N ATOM 3304 CA HIS A 439 36.953 15.248 1.866 1.00102.06 C ANISOU 3304 CA HIS A 439 13159 15050 10569 922 706 67 C ATOM 3305 C HIS A 439 36.719 16.651 1.318 1.00100.81 C ANISOU 3305 C HIS A 439 12956 14944 10404 715 750 -181 C ATOM 3306 O HIS A 439 36.283 17.544 2.052 1.00104.15 O ANISOU 3306 O HIS A 439 13564 15430 10579 669 799 -226 O ATOM 3307 CB HIS A 439 35.694 14.699 2.532 1.00101.41 C ANISOU 3307 CB HIS A 439 13289 14808 10435 987 952 314 C ATOM 3308 CG HIS A 439 34.650 14.226 1.569 1.00 99.71 C ANISOU 3308 CG HIS A 439 12984 14336 10565 904 1168 370 C ATOM 3309 ND1 HIS A 439 33.375 13.886 1.963 1.00 99.91 N ANISOU 3309 ND1 HIS A 439 13131 14192 10640 910 1419 586 N ATOM 3310 CD2 HIS A 439 34.694 14.024 0.231 1.00101.59 C ANISOU 3310 CD2 HIS A 439 13029 14452 11119 816 1155 245 C ATOM 3311 CE1 HIS A 439 32.676 13.500 0.911 1.00 98.15 C ANISOU 3311 CE1 HIS A 439 12776 13743 10774 811 1516 589 C ATOM 3312 NE2 HIS A 439 33.454 13.574 -0.153 1.00 96.78 N ANISOU 3312 NE2 HIS A 439 12437 13593 10743 758 1353 374 N ATOM 3313 N VAL A 440 37.012 16.849 0.035 1.00 97.19 N ANISOU 3313 N VAL A 440 12273 14451 10202 602 740 -340 N ATOM 3314 CA VAL A 440 36.931 18.161 -0.599 1.00 95.80 C ANISOU 3314 CA VAL A 440 12031 14321 10046 402 758 -565 C ATOM 3315 C VAL A 440 35.710 18.198 -1.506 1.00 92.08 C ANISOU 3315 C VAL A 440 11557 13639 9791 295 990 -567 C ATOM 3316 O VAL A 440 35.512 17.298 -2.339 1.00 97.09 O ANISOU 3316 O VAL A 440 12104 14121 10666 326 1044 -510 O ATOM 3317 CB VAL A 440 38.206 18.492 -1.391 1.00 95.89 C ANISOU 3317 CB VAL A 440 11791 14468 10174 342 579 -729 C ATOM 3318 CG1 VAL A 440 38.039 19.813 -2.116 1.00 92.33 C ANISOU 3318 CG1 VAL A 440 11279 14033 9768 124 620 -931 C ATOM 3319 CG2 VAL A 440 39.396 18.551 -0.461 1.00110.48 C ANISOU 3319 CG2 VAL A 440 13612 16522 11844 427 309 -721 C ATOM 3320 N LEU A 441 34.910 19.256 -1.359 1.00 91.22 N ANISOU 3320 N LEU A 441 11548 13508 9603 173 1105 -643 N ATOM 3321 CA LEU A 441 33.638 19.394 -2.050 1.00 89.40 C ANISOU 3321 CA LEU A 441 11320 13077 9573 74 1311 -621 C ATOM 3322 C LEU A 441 33.431 20.841 -2.483 1.00 88.57 C ANISOU 3322 C LEU A 441 11200 13001 9450 -103 1329 -819 C ATOM 3323 O LEU A 441 34.080 21.766 -1.984 1.00 90.48 O ANISOU 3323 O LEU A 441 11486 13400 9490 -143 1212 -953 O ATOM 3324 CB LEU A 441 32.457 18.963 -1.168 1.00 90.54 C ANISOU 3324 CB LEU A 441 11625 13099 9675 159 1517 -400 C ATOM 3325 CG LEU A 441 32.513 17.657 -0.376 1.00 92.63 C ANISOU 3325 CG LEU A 441 11968 13332 9896 342 1530 -153 C ATOM 3326 CD1 LEU A 441 33.013 17.893 1.041 1.00 98.24 C ANISOU 3326 CD1 LEU A 441 12873 14231 10222 468 1469 -107 C ATOM 3327 CD2 LEU A 441 31.147 17.005 -0.355 1.00 92.81 C ANISOU 3327 CD2 LEU A 441 12018 13122 10125 351 1765 76 C ATOM 3328 N GLN A 442 32.492 21.017 -3.412 1.00 87.91 N ANISOU 3328 N GLN A 442 11064 12744 9595 -212 1455 -830 N ATOM 3329 CA GLN A 442 32.061 22.318 -3.905 1.00 84.86 C ANISOU 3329 CA GLN A 442 10670 12332 9239 -374 1498 -981 C ATOM 3330 C GLN A 442 30.561 22.468 -3.708 1.00 84.69 C ANISOU 3330 C GLN A 442 10722 12134 9323 -384 1714 -864 C ATOM 3331 O GLN A 442 29.799 21.535 -3.977 1.00 88.11 O ANISOU 3331 O GLN A 442 11116 12399 9963 -349 1804 -698 O ATOM 3332 CB GLN A 442 32.377 22.491 -5.390 1.00 83.05 C ANISOU 3332 CB GLN A 442 10287 12059 9208 -503 1427 -1103 C ATOM 3333 CG GLN A 442 33.802 22.865 -5.717 1.00 85.19 C ANISOU 3333 CG GLN A 442 10448 12518 9401 -542 1259 -1249 C ATOM 3334 CD GLN A 442 34.012 23.037 -7.207 1.00 97.35 C ANISOU 3334 CD GLN A 442 11866 14009 11115 -653 1247 -1345 C ATOM 3335 OE1 GLN A 442 33.564 22.215 -8.006 1.00 87.31 O ANISOU 3335 OE1 GLN A 442 10583 12590 10002 -622 1292 -1289 O ATOM 3336 NE2 GLN A 442 34.685 24.116 -7.591 1.00114.01 N ANISOU 3336 NE2 GLN A 442 13901 16229 13188 -784 1180 -1484 N ATOM 3337 N GLY A 443 30.139 23.640 -3.265 1.00 95.63 N ANISOU 3337 N GLY A 443 12201 13538 10595 -432 1792 -948 N ATOM 3338 CA GLY A 443 28.723 23.920 -3.126 1.00 96.11 C ANISOU 3338 CA GLY A 443 12297 13434 10786 -434 2018 -841 C ATOM 3339 C GLY A 443 28.466 24.888 -1.990 1.00 99.84 C ANISOU 3339 C GLY A 443 12960 13975 10998 -369 2136 -891 C ATOM 3340 O GLY A 443 29.375 25.325 -1.290 1.00104.72 O ANISOU 3340 O GLY A 443 13708 14759 11322 -333 2009 -1016 O ATOM 3341 N GLU A 444 27.183 25.212 -1.821 1.00 87.01 N ANISOU 3341 N GLU A 444 11355 12208 9498 -346 2378 -790 N ATOM 3342 CA GLU A 444 26.749 26.169 -0.813 1.00 88.81 C ANISOU 3342 CA GLU A 444 11782 12463 9499 -259 2547 -839 C ATOM 3343 C GLU A 444 25.931 25.551 0.309 1.00 91.79 C ANISOU 3343 C GLU A 444 12280 12815 9782 -65 2835 -595 C ATOM 3344 O GLU A 444 25.728 26.210 1.333 1.00101.96 O ANISOU 3344 O GLU A 444 13797 14157 10786 59 2987 -635 O ATOM 3345 CB GLU A 444 25.924 27.286 -1.466 1.00 95.77 C ANISOU 3345 CB GLU A 444 12596 13202 10588 -363 2636 -931 C ATOM 3346 CG GLU A 444 26.665 28.031 -2.554 1.00107.64 C ANISOU 3346 CG GLU A 444 14005 14723 12170 -556 2384 -1152 C ATOM 3347 CD GLU A 444 27.882 28.750 -2.024 1.00118.99 C ANISOU 3347 CD GLU A 444 15595 16332 13286 -575 2189 -1370 C ATOM 3348 OE1 GLU A 444 27.817 29.273 -0.890 1.00140.05 O ANISOU 3348 OE1 GLU A 444 18493 19046 15675 -459 2270 -1425 O ATOM 3349 OE2 GLU A 444 28.905 28.782 -2.737 1.00105.21 O ANISOU 3349 OE2 GLU A 444 13742 14668 11567 -701 1954 -1483 O ATOM 3350 N ARG A 445 25.466 24.317 0.147 1.00 91.32 N ANISOU 3350 N ARG A 445 12089 12664 9945 -33 2919 -343 N ATOM 3351 CA ARG A 445 24.636 23.677 1.155 1.00 93.90 C ANISOU 3351 CA ARG A 445 12498 12950 10230 138 3222 -62 C ATOM 3352 C ARG A 445 25.432 23.442 2.438 1.00 96.28 C ANISOU 3352 C ARG A 445 13080 13443 10057 310 3201 -53 C ATOM 3353 O ARG A 445 26.665 23.408 2.440 1.00 95.78 O ANISOU 3353 O ARG A 445 13079 13526 9786 286 2906 -215 O ATOM 3354 CB ARG A 445 24.089 22.357 0.618 1.00 93.54 C ANISOU 3354 CB ARG A 445 12236 12741 10563 103 3254 204 C ATOM 3355 CG ARG A 445 23.430 22.472 -0.745 1.00 91.35 C ANISOU 3355 CG ARG A 445 11698 12268 10742 -80 3183 181 C ATOM 3356 CD ARG A 445 22.130 23.240 -0.664 1.00 93.07 C ANISOU 3356 CD ARG A 445 11844 12360 11160 -75 3456 264 C ATOM 3357 NE ARG A 445 21.161 22.570 0.194 1.00104.82 N ANISOU 3357 NE ARG A 445 13311 13768 12750 59 3787 600 N ATOM 3358 CZ ARG A 445 20.359 21.593 -0.212 1.00106.38 C ANISOU 3358 CZ ARG A 445 13284 13767 13368 3 3839 869 C ATOM 3359 NH1 ARG A 445 20.412 21.171 -1.468 1.00 98.70 N ANISOU 3359 NH1 ARG A 445 12128 12653 12720 -174 3560 813 N ATOM 3360 NH2 ARG A 445 19.505 21.040 0.638 1.00114.35 N ANISOU 3360 NH2 ARG A 445 14265 14711 14473 124 4169 1198 N ATOM 3361 N LYS A 446 24.708 23.279 3.547 1.00101.47 N ANISOU 3361 N LYS A 446 13907 14101 10547 493 3521 153 N ATOM 3362 CA LYS A 446 25.350 23.128 4.847 1.00108.71 C ANISOU 3362 CA LYS A 446 15149 15194 10962 678 3517 172 C ATOM 3363 C LYS A 446 25.736 21.692 5.167 1.00106.28 C ANISOU 3363 C LYS A 446 14829 14912 10642 754 3457 424 C ATOM 3364 O LYS A 446 26.577 21.474 6.046 1.00110.19 O ANISOU 3364 O LYS A 446 15566 15568 10734 877 3322 412 O ATOM 3365 CB LYS A 446 24.442 23.670 5.956 1.00122.05 C ANISOU 3365 CB LYS A 446 17089 16884 12400 873 3915 272 C ATOM 3366 CG LYS A 446 24.874 25.029 6.487 1.00132.39 C ANISOU 3366 CG LYS A 446 18698 18299 13307 921 3839 -51 C ATOM 3367 CD LYS A 446 23.871 25.587 7.482 1.00140.24 C ANISOU 3367 CD LYS A 446 19944 19265 14076 1137 4279 36 C ATOM 3368 CE LYS A 446 22.591 26.026 6.789 1.00135.61 C ANISOU 3368 CE LYS A 446 19088 18486 13952 1082 4580 115 C ATOM 3369 NZ LYS A 446 21.607 26.616 7.741 1.00132.81 N ANISOU 3369 NZ LYS A 446 18958 18101 13401 1318 5049 199 N ATOM 3370 N ARG A 447 25.153 20.713 4.484 1.00101.98 N ANISOU 3370 N ARG A 447 14020 14198 10531 683 3526 652 N ATOM 3371 CA ARG A 447 25.515 19.316 4.664 1.00102.84 C ANISOU 3371 CA ARG A 447 14100 14286 10688 742 3447 887 C ATOM 3372 C ARG A 447 26.473 18.890 3.562 1.00101.31 C ANISOU 3372 C ARG A 447 13716 14082 10695 603 3069 721 C ATOM 3373 O ARG A 447 26.273 19.226 2.392 1.00103.09 O ANISOU 3373 O ARG A 447 13729 14202 11238 434 2981 577 O ATOM 3374 CB ARG A 447 24.275 18.421 4.647 1.00112.62 C ANISOU 3374 CB ARG A 447 15179 15310 12300 755 3752 1260 C ATOM 3375 CG ARG A 447 23.269 18.719 5.744 1.00130.55 C ANISOU 3375 CG ARG A 447 17607 17586 14408 917 4195 1485 C ATOM 3376 CD ARG A 447 23.752 18.211 7.090 1.00143.35 C ANISOU 3376 CD ARG A 447 19554 19361 15550 1136 4271 1653 C ATOM 3377 NE ARG A 447 23.864 16.756 7.105 1.00149.40 N ANISOU 3377 NE ARG A 447 20232 20030 16504 1152 4220 1954 N ATOM 3378 CZ ARG A 447 24.345 16.055 8.125 1.00153.60 C ANISOU 3378 CZ ARG A 447 21009 20662 16690 1327 4229 2149 C ATOM 3379 NH1 ARG A 447 24.765 16.676 9.219 1.00154.05 N ANISOU 3379 NH1 ARG A 447 21432 20931 16168 1501 4274 2064 N ATOM 3380 NH2 ARG A 447 24.410 14.732 8.050 1.00156.19 N ANISOU 3380 NH2 ARG A 447 21236 20863 17245 1330 4174 2427 N ATOM 3381 N ALA A 448 27.514 18.145 3.942 1.00112.08 N ANISOU 3381 N ALA A 448 15164 15555 11865 691 2854 750 N ATOM 3382 CA ALA A 448 28.467 17.667 2.947 1.00107.09 C ANISOU 3382 CA ALA A 448 14353 14919 11420 599 2533 610 C ATOM 3383 C ALA A 448 27.779 16.804 1.902 1.00112.40 C ANISOU 3383 C ALA A 448 14790 15337 12581 499 2572 742 C ATOM 3384 O ALA A 448 28.107 16.874 0.713 1.00112.73 O ANISOU 3384 O ALA A 448 14663 15321 12848 368 2390 558 O ATOM 3385 CB ALA A 448 29.596 16.893 3.623 1.00106.13 C ANISOU 3385 CB ALA A 448 14345 14933 11047 743 2325 675 C ATOM 3386 N ALA A 449 26.806 15.996 2.321 1.00117.27 N ANISOU 3386 N ALA A 449 15401 15789 13369 555 2805 1065 N ATOM 3387 CA ALA A 449 26.111 15.133 1.377 1.00121.23 C ANISOU 3387 CA ALA A 449 15690 16014 14358 447 2805 1200 C ATOM 3388 C ALA A 449 25.276 15.917 0.376 1.00113.84 C ANISOU 3388 C ALA A 449 14583 14953 13720 268 2847 1070 C ATOM 3389 O ALA A 449 24.948 15.383 -0.689 1.00106.24 O ANISOU 3389 O ALA A 449 13452 13778 13134 147 2730 1071 O ATOM 3390 CB ALA A 449 25.222 14.143 2.126 1.00132.06 C ANISOU 3390 CB ALA A 449 17076 17225 15874 531 3052 1607 C ATOM 3391 N ASP A 450 24.920 17.159 0.691 1.00110.36 N ANISOU 3391 N ASP A 450 14198 14620 13114 256 2996 955 N ATOM 3392 CA ASP A 450 24.121 17.989 -0.198 1.00110.09 C ANISOU 3392 CA ASP A 450 14007 14470 13352 101 3034 843 C ATOM 3393 C ASP A 450 24.966 18.792 -1.177 1.00 95.62 C ANISOU 3393 C ASP A 450 12146 12731 11454 -17 2766 488 C ATOM 3394 O ASP A 450 24.443 19.708 -1.816 1.00 91.78 O ANISOU 3394 O ASP A 450 11576 12189 11107 -133 2785 364 O ATOM 3395 CB ASP A 450 23.239 18.942 0.612 1.00120.03 C ANISOU 3395 CB ASP A 450 15336 15770 14501 166 3356 911 C ATOM 3396 CG ASP A 450 22.211 18.217 1.451 1.00119.65 C ANISOU 3396 CG ASP A 450 15269 15606 14587 270 3686 1298 C ATOM 3397 OD1 ASP A 450 21.799 17.108 1.054 1.00129.51 O ANISOU 3397 OD1 ASP A 450 16359 16655 16196 213 3654 1520 O ATOM 3398 OD2 ASP A 450 21.812 18.760 2.504 1.00106.63 O ANISOU 3398 OD2 ASP A 450 13773 14056 12686 413 3984 1385 O ATOM 3399 N ASN A 451 26.251 18.477 -1.312 1.00 97.31 N ANISOU 3399 N ASN A 451 12413 13081 11477 13 2529 343 N ATOM 3400 CA ASN A 451 27.145 19.215 -2.193 1.00 97.47 C ANISOU 3400 CA ASN A 451 12394 13208 11433 -91 2304 37 C ATOM 3401 C ASN A 451 27.825 18.253 -3.160 1.00102.18 C ANISOU 3401 C ASN A 451 12894 13735 12194 -116 2088 -7 C ATOM 3402 O ASN A 451 27.639 17.034 -3.101 1.00117.73 O ANISOU 3402 O ASN A 451 14847 15568 14320 -50 2087 182 O ATOM 3403 CB ASN A 451 28.181 20.009 -1.390 1.00 95.41 C ANISOU 3403 CB ASN A 451 12282 13210 10759 -26 2226 -130 C ATOM 3404 CG ASN A 451 27.599 21.260 -0.770 1.00 97.67 C ANISOU 3404 CG ASN A 451 12684 13546 10882 -30 2395 -197 C ATOM 3405 OD1 ASN A 451 26.804 21.964 -1.393 1.00 94.25 O ANISOU 3405 OD1 ASN A 451 12165 12997 10648 -140 2481 -250 O ATOM 3406 ND2 ASN A 451 27.987 21.542 0.467 1.00105.90 N ANISOU 3406 ND2 ASN A 451 13938 14749 11552 101 2433 -197 N ATOM 3407 N LYS A 452 28.613 18.820 -4.068 1.00 98.76 N ANISOU 3407 N LYS A 452 12406 13386 11731 -205 1916 -254 N ATOM 3408 CA LYS A 452 29.314 18.050 -5.085 1.00 95.53 C ANISOU 3408 CA LYS A 452 11923 12926 11448 -211 1739 -332 C ATOM 3409 C LYS A 452 30.687 17.660 -4.556 1.00 95.96 C ANISOU 3409 C LYS A 452 12003 13182 11275 -77 1618 -372 C ATOM 3410 O LYS A 452 31.543 18.525 -4.341 1.00100.22 O ANISOU 3410 O LYS A 452 12543 13935 11601 -95 1543 -530 O ATOM 3411 CB LYS A 452 29.445 18.855 -6.377 1.00 98.21 C ANISOU 3411 CB LYS A 452 12191 13255 11869 -362 1650 -551 C ATOM 3412 CG LYS A 452 30.404 18.256 -7.394 1.00102.06 C ANISOU 3412 CG LYS A 452 12633 13748 12396 -340 1496 -673 C ATOM 3413 CD LYS A 452 29.915 16.915 -7.903 1.00106.60 C ANISOU 3413 CD LYS A 452 13219 14070 13213 -291 1457 -556 C ATOM 3414 CE LYS A 452 30.847 16.369 -8.971 1.00107.68 C ANISOU 3414 CE LYS A 452 13347 14201 13365 -242 1329 -703 C ATOM 3415 NZ LYS A 452 30.327 15.113 -9.576 1.00111.95 N ANISOU 3415 NZ LYS A 452 13940 14453 14143 -203 1261 -628 N ATOM 3416 N SER A 453 30.894 16.363 -4.348 1.00 87.55 N ANISOU 3416 N SER A 453 10950 12034 10282 52 1582 -222 N ATOM 3417 CA SER A 453 32.174 15.887 -3.848 1.00 88.81 C ANISOU 3417 CA SER A 453 11115 12366 10264 199 1453 -231 C ATOM 3418 C SER A 453 33.227 15.944 -4.943 1.00 88.46 C ANISOU 3418 C SER A 453 10951 12392 10268 182 1310 -438 C ATOM 3419 O SER A 453 33.055 15.364 -6.019 1.00 98.59 O ANISOU 3419 O SER A 453 12197 13500 11761 164 1290 -478 O ATOM 3420 CB SER A 453 32.045 14.461 -3.321 1.00 94.85 C ANISOU 3420 CB SER A 453 11932 12993 11115 353 1461 10 C ATOM 3421 OG SER A 453 33.320 13.884 -3.092 1.00 98.38 O ANISOU 3421 OG SER A 453 12353 13571 11457 505 1307 -7 O ATOM 3422 N LEU A 454 34.318 16.657 -4.673 1.00 88.09 N ANISOU 3422 N LEU A 454 10849 12594 10028 188 1210 -567 N ATOM 3423 CA LEU A 454 35.480 16.600 -5.549 1.00 87.92 C ANISOU 3423 CA LEU A 454 10683 12669 10054 210 1101 -715 C ATOM 3424 C LEU A 454 36.351 15.392 -5.255 1.00 89.84 C ANISOU 3424 C LEU A 454 10884 12931 10320 419 1008 -617 C ATOM 3425 O LEU A 454 36.978 14.852 -6.173 1.00 89.96 O ANISOU 3425 O LEU A 454 10805 12912 10465 488 979 -690 O ATOM 3426 CB LEU A 454 36.305 17.885 -5.438 1.00 87.71 C ANISOU 3426 CB LEU A 454 10569 12884 9873 108 1023 -875 C ATOM 3427 CG LEU A 454 35.598 19.143 -5.939 1.00 85.87 C ANISOU 3427 CG LEU A 454 10360 12621 9645 -98 1101 -998 C ATOM 3428 CD1 LEU A 454 36.603 20.241 -6.249 1.00 85.77 C ANISOU 3428 CD1 LEU A 454 10218 12805 9566 -208 1009 -1166 C ATOM 3429 CD2 LEU A 454 34.737 18.838 -7.160 1.00 93.78 C ANISOU 3429 CD2 LEU A 454 11375 13400 10857 -165 1195 -1015 C ATOM 3430 N GLY A 455 36.402 14.950 -4.009 1.00108.60 N ANISOU 3430 N GLY A 455 13344 15355 12565 537 968 -449 N ATOM 3431 CA GLY A 455 36.983 13.648 -3.732 1.00123.28 C ANISOU 3431 CA GLY A 455 15190 17165 14486 746 890 -311 C ATOM 3432 C GLY A 455 37.655 13.587 -2.378 1.00141.19 C ANISOU 3432 C GLY A 455 17499 19619 16528 870 761 -192 C ATOM 3433 O GLY A 455 37.697 14.558 -1.624 1.00153.23 O ANISOU 3433 O GLY A 455 19084 21312 17825 795 722 -232 O ATOM 3434 N GLN A 456 38.193 12.402 -2.082 1.00114.33 N ANISOU 3434 N GLN A 456 14085 16168 13188 1072 677 -45 N ATOM 3435 CA GLN A 456 38.858 12.132 -0.815 1.00112.40 C ANISOU 3435 CA GLN A 456 13893 16073 12739 1221 520 103 C ATOM 3436 C GLN A 456 40.357 12.031 -1.052 1.00109.63 C ANISOU 3436 C GLN A 456 13316 15895 12442 1330 319 19 C ATOM 3437 O GLN A 456 40.826 11.127 -1.754 1.00107.82 O ANISOU 3437 O GLN A 456 12968 15564 12436 1464 317 27 O ATOM 3438 CB GLN A 456 38.317 10.861 -0.167 1.00116.68 C ANISOU 3438 CB GLN A 456 14592 16424 13317 1378 568 381 C ATOM 3439 CG GLN A 456 36.958 11.056 0.481 1.00121.69 C ANISOU 3439 CG GLN A 456 15438 16953 13845 1292 761 528 C ATOM 3440 CD GLN A 456 36.434 9.796 1.129 1.00133.17 C ANISOU 3440 CD GLN A 456 17031 18210 15356 1435 825 840 C ATOM 3441 OE1 GLN A 456 36.942 8.702 0.882 1.00137.14 O ANISOU 3441 OE1 GLN A 456 17478 18594 16036 1583 732 925 O ATOM 3442 NE2 GLN A 456 35.414 9.940 1.968 1.00138.42 N ANISOU 3442 NE2 GLN A 456 17880 18832 15882 1402 1000 1024 N ATOM 3443 N PHE A 457 41.098 12.957 -0.462 1.00117.21 N ANISOU 3443 N PHE A 457 14216 17104 13213 1276 148 -60 N ATOM 3444 CA PHE A 457 42.533 13.074 -0.651 1.00123.48 C ANISOU 3444 CA PHE A 457 14742 18087 14086 1341 -56 -135 C ATOM 3445 C PHE A 457 43.220 12.438 0.551 1.00132.83 C ANISOU 3445 C PHE A 457 15967 19364 15138 1537 -296 54 C ATOM 3446 O PHE A 457 43.048 12.893 1.688 1.00135.50 O ANISOU 3446 O PHE A 457 16501 19801 15182 1511 -416 114 O ATOM 3447 CB PHE A 457 42.934 14.541 -0.813 1.00118.53 C ANISOU 3447 CB PHE A 457 14001 17653 13383 1129 -132 -338 C ATOM 3448 CG PHE A 457 42.337 15.210 -2.029 1.00109.40 C ANISOU 3448 CG PHE A 457 12800 16412 12354 940 86 -512 C ATOM 3449 CD1 PHE A 457 40.968 15.392 -2.146 1.00104.16 C ANISOU 3449 CD1 PHE A 457 12356 15580 11639 835 286 -513 C ATOM 3450 CD2 PHE A 457 43.152 15.679 -3.046 1.00111.57 C ANISOU 3450 CD2 PHE A 457 12805 16780 12805 872 91 -656 C ATOM 3451 CE1 PHE A 457 40.425 16.006 -3.256 1.00102.73 C ANISOU 3451 CE1 PHE A 457 12140 15317 11574 668 450 -662 C ATOM 3452 CE2 PHE A 457 42.613 16.299 -4.156 1.00110.97 C ANISOU 3452 CE2 PHE A 457 12717 16629 12816 706 281 -800 C ATOM 3453 CZ PHE A 457 41.249 16.462 -4.261 1.00106.23 C ANISOU 3453 CZ PHE A 457 12352 15855 12156 604 442 -807 C ATOM 3454 N ASN A 458 43.981 11.381 0.295 1.00138.33 N ANISOU 3454 N ASN A 458 16503 20019 16038 1747 -365 149 N ATOM 3455 CA ASN A 458 44.624 10.584 1.327 1.00137.63 C ANISOU 3455 CA ASN A 458 16442 19979 15871 1966 -595 360 C ATOM 3456 C ASN A 458 46.110 10.910 1.356 1.00138.63 C ANISOU 3456 C ASN A 458 16245 20336 16090 2019 -868 304 C ATOM 3457 O ASN A 458 46.804 10.779 0.338 1.00140.83 O ANISOU 3457 O ASN A 458 16226 20628 16656 2062 -809 209 O ATOM 3458 CB ASN A 458 44.393 9.095 1.083 1.00142.46 C ANISOU 3458 CB ASN A 458 17103 20345 16679 2184 -493 534 C ATOM 3459 CG ASN A 458 42.921 8.745 1.029 1.00149.95 C ANISOU 3459 CG ASN A 458 18330 21044 17598 2111 -241 613 C ATOM 3460 OD1 ASN A 458 42.080 9.486 1.536 1.00152.70 O ANISOU 3460 OD1 ASN A 458 18871 21426 17722 1951 -160 608 O ATOM 3461 ND2 ASN A 458 42.598 7.615 0.408 1.00154.28 N ANISOU 3461 ND2 ASN A 458 18896 21329 18395 2231 -119 688 N ATOM 3462 N LEU A 459 46.576 11.361 2.521 1.00150.84 N ANISOU 3462 N LEU A 459 17860 22061 17393 2014 -1165 366 N ATOM 3463 CA LEU A 459 47.986 11.583 2.814 1.00153.11 C ANISOU 3463 CA LEU A 459 17850 22559 17766 2073 -1507 367 C ATOM 3464 C LEU A 459 48.446 10.402 3.654 1.00160.23 C ANISOU 3464 C LEU A 459 18802 23430 18650 2354 -1715 626 C ATOM 3465 O LEU A 459 48.227 10.367 4.871 1.00166.86 O ANISOU 3465 O LEU A 459 19928 24308 19162 2396 -1904 762 O ATOM 3466 CB LEU A 459 48.192 12.898 3.552 1.00146.44 C ANISOU 3466 CB LEU A 459 17074 21908 16660 1868 -1758 250 C ATOM 3467 CG LEU A 459 47.530 14.126 2.941 1.00138.38 C ANISOU 3467 CG LEU A 459 16100 20887 15592 1584 -1559 16 C ATOM 3468 CD1 LEU A 459 47.810 15.328 3.814 1.00135.55 C ANISOU 3468 CD1 LEU A 459 15845 20690 14967 1415 -1860 -90 C ATOM 3469 CD2 LEU A 459 48.055 14.341 1.540 1.00139.61 C ANISOU 3469 CD2 LEU A 459 15871 21056 16120 1512 -1399 -118 C ATOM 3470 N ASP A 460 49.046 9.422 2.984 1.00145.96 N ANISOU 3470 N ASP A 460 16740 21539 17179 2562 -1660 697 N ATOM 3471 CA ASP A 460 49.606 8.244 3.619 1.00150.80 C ANISOU 3471 CA ASP A 460 17340 22102 17854 2854 -1856 945 C ATOM 3472 C ASP A 460 51.052 8.520 4.016 1.00150.86 C ANISOU 3472 C ASP A 460 17002 22342 17974 2924 -2250 976 C ATOM 3473 O ASP A 460 51.592 9.605 3.782 1.00147.19 O ANISOU 3473 O ASP A 460 16307 22063 17555 2733 -2360 809 O ATOM 3474 CB ASP A 460 49.512 7.043 2.681 1.00156.20 C ANISOU 3474 CB ASP A 460 17938 22548 18865 3059 -1599 993 C ATOM 3475 CG ASP A 460 50.118 7.328 1.319 1.00165.22 C ANISOU 3475 CG ASP A 460 18709 23728 20339 3036 -1425 789 C ATOM 3476 OD1 ASP A 460 49.954 8.459 0.820 1.00169.30 O ANISOU 3476 OD1 ASP A 460 19159 24358 20809 2782 -1328 585 O ATOM 3477 OD2 ASP A 460 50.763 6.420 0.751 1.00169.06 O ANISOU 3477 OD2 ASP A 460 18983 24125 21127 3283 -1372 839 O ATOM 3478 N GLY A 461 51.687 7.521 4.619 1.00142.66 N ANISOU 3478 N GLY A 461 15914 21280 17012 3198 -2480 1208 N ATOM 3479 CA GLY A 461 53.084 7.649 4.990 1.00148.58 C ANISOU 3479 CA GLY A 461 16297 22230 17927 3292 -2880 1273 C ATOM 3480 C GLY A 461 53.361 8.713 6.031 1.00150.77 C ANISOU 3480 C GLY A 461 16671 22724 17890 3106 -3282 1238 C ATOM 3481 O GLY A 461 54.346 9.451 5.911 1.00157.01 O ANISOU 3481 O GLY A 461 17093 23702 18860 3004 -3532 1150 O ATOM 3482 N ILE A 462 52.506 8.826 7.041 1.00177.76 N ANISOU 3482 N ILE A 462 20584 26111 20845 3056 -3343 1305 N ATOM 3483 CA ILE A 462 52.767 9.671 8.201 1.00178.40 C ANISOU 3483 CA ILE A 462 20856 26371 20558 2939 -3768 1292 C ATOM 3484 C ILE A 462 53.396 8.775 9.255 1.00184.06 C ANISOU 3484 C ILE A 462 21646 27108 21179 3208 -4164 1578 C ATOM 3485 O ILE A 462 52.719 7.912 9.823 1.00187.37 O ANISOU 3485 O ILE A 462 22432 27388 21371 3375 -4058 1786 O ATOM 3486 CB ILE A 462 51.489 10.333 8.731 1.00174.93 C ANISOU 3486 CB ILE A 462 20943 25890 19631 2763 -3588 1201 C ATOM 3487 CG1 ILE A 462 50.703 10.965 7.586 1.00169.39 C ANISOU 3487 CG1 ILE A 462 20183 25111 19067 2543 -3136 964 C ATOM 3488 CG2 ILE A 462 51.834 11.372 9.771 1.00176.53 C ANISOU 3488 CG2 ILE A 462 21335 26274 19465 2625 -4023 1116 C ATOM 3489 CD1 ILE A 462 51.513 11.912 6.765 1.00167.90 C ANISOU 3489 CD1 ILE A 462 19558 25057 19181 2352 -3217 743 C ATOM 3490 N ASN A 463 54.691 8.958 9.507 1.00164.24 N ANISOU 3490 N ASN A 463 18775 24763 18867 3250 -4625 1613 N ATOM 3491 CA ASN A 463 55.372 8.108 10.469 1.00171.78 C ANISOU 3491 CA ASN A 463 19762 25739 19767 3516 -5045 1896 C ATOM 3492 C ASN A 463 54.696 8.240 11.835 1.00174.67 C ANISOU 3492 C ASN A 463 20759 26117 19492 3513 -5243 1997 C ATOM 3493 O ASN A 463 54.064 9.259 12.126 1.00173.20 O ANISOU 3493 O ASN A 463 20881 25987 18940 3281 -5200 1806 O ATOM 3494 CB ASN A 463 56.866 8.450 10.554 1.00178.07 C ANISOU 3494 CB ASN A 463 20044 26724 20890 3523 -5556 1906 C ATOM 3495 CG ASN A 463 57.137 9.909 10.917 1.00180.81 C ANISOU 3495 CG ASN A 463 20396 27251 21052 3206 -5889 1683 C ATOM 3496 OD1 ASN A 463 56.468 10.497 11.767 1.00181.51 O ANISOU 3496 OD1 ASN A 463 21000 27359 20607 3081 -6003 1613 O ATOM 3497 ND2 ASN A 463 58.148 10.490 10.281 1.00182.31 N ANISOU 3497 ND2 ASN A 463 20009 27563 21696 3085 -6047 1580 N ATOM 3498 N PRO A 464 54.769 7.206 12.675 1.00178.35 N ANISOU 3498 N PRO A 464 21451 26518 19797 3783 -5428 2302 N ATOM 3499 CA PRO A 464 54.048 7.252 13.955 1.00179.96 C ANISOU 3499 CA PRO A 464 22301 26725 19353 3809 -5543 2428 C ATOM 3500 C PRO A 464 54.458 8.446 14.802 1.00183.11 C ANISOU 3500 C PRO A 464 22873 27329 19373 3632 -6029 2269 C ATOM 3501 O PRO A 464 55.605 8.899 14.771 1.00183.53 O ANISOU 3501 O PRO A 464 22536 27524 19672 3574 -6487 2194 O ATOM 3502 CB PRO A 464 54.434 5.927 14.624 1.00184.53 C ANISOU 3502 CB PRO A 464 22958 27220 19934 4148 -5764 2807 C ATOM 3503 CG PRO A 464 54.742 5.020 13.485 1.00182.52 C ANISOU 3503 CG PRO A 464 22232 26815 20302 4294 -5485 2860 C ATOM 3504 CD PRO A 464 55.394 5.887 12.445 1.00180.60 C ANISOU 3504 CD PRO A 464 21451 26693 20476 4097 -5467 2560 C ATOM 3505 N ALA A 465 53.496 8.952 15.559 1.00178.35 N ANISOU 3505 N ALA A 465 22862 26726 18178 3548 -5919 2220 N ATOM 3506 CA ALA A 465 53.659 10.169 16.339 1.00182.04 C ANISOU 3506 CA ALA A 465 23607 27348 18213 3368 -6307 2018 C ATOM 3507 C ALA A 465 52.482 10.268 17.308 1.00180.22 C ANISOU 3507 C ALA A 465 24118 27075 17283 3410 -6095 2079 C ATOM 3508 O ALA A 465 51.470 9.584 17.122 1.00183.15 O ANISOU 3508 O ALA A 465 24683 27298 17610 3504 -5568 2231 O ATOM 3509 CB ALA A 465 53.715 11.414 15.433 1.00179.27 C ANISOU 3509 CB ALA A 465 22946 27050 18117 3045 -6195 1646 C ATOM 3510 N PRO A 466 52.597 11.087 18.351 1.00173.12 N ANISOU 3510 N PRO A 466 23644 26293 15840 3353 -6495 1974 N ATOM 3511 CA PRO A 466 51.442 11.322 19.220 1.00173.54 C ANISOU 3511 CA PRO A 466 24414 26315 15208 3393 -6227 1997 C ATOM 3512 C PRO A 466 50.338 12.042 18.468 1.00170.17 C ANISOU 3512 C PRO A 466 24021 25810 14827 3186 -5624 1752 C ATOM 3513 O PRO A 466 50.561 12.677 17.434 1.00173.90 O ANISOU 3513 O PRO A 466 24048 26284 15743 2966 -5539 1498 O ATOM 3514 CB PRO A 466 52.010 12.194 20.343 1.00178.75 C ANISOU 3514 CB PRO A 466 25456 27121 15339 3354 -6860 1860 C ATOM 3515 CG PRO A 466 53.211 12.842 19.742 1.00179.06 C ANISOU 3515 CG PRO A 466 24908 27249 15876 3155 -7331 1639 C ATOM 3516 CD PRO A 466 53.790 11.807 18.825 1.00177.45 C ANISOU 3516 CD PRO A 466 24060 26998 16366 3261 -7225 1840 C ATOM 3517 N ARG A 467 49.127 11.931 19.002 1.00193.18 N ANISOU 3517 N ARG A 467 27468 28651 17281 3267 -5193 1854 N ATOM 3518 CA ARG A 467 47.985 12.560 18.355 1.00187.16 C ANISOU 3518 CA ARG A 467 26755 27801 16556 3096 -4607 1658 C ATOM 3519 C ARG A 467 48.133 14.078 18.356 1.00184.43 C ANISOU 3519 C ARG A 467 26483 27544 16050 2854 -4809 1256 C ATOM 3520 O ARG A 467 48.334 14.699 19.405 1.00186.86 O ANISOU 3520 O ARG A 467 27242 27943 15813 2880 -5175 1166 O ATOM 3521 CB ARG A 467 46.681 12.148 19.044 1.00191.56 C ANISOU 3521 CB ARG A 467 27865 28270 16648 3248 -4119 1881 C ATOM 3522 CG ARG A 467 46.591 12.458 20.528 1.00205.78 C ANISOU 3522 CG ARG A 467 30352 30172 17663 3394 -4363 1944 C ATOM 3523 CD ARG A 467 45.222 12.082 21.083 1.00211.62 C ANISOU 3523 CD ARG A 467 31585 30822 18000 3538 -3768 2179 C ATOM 3524 NE ARG A 467 44.137 12.731 20.349 1.00209.11 N ANISOU 3524 NE ARG A 467 31194 30411 17846 3364 -3195 1984 N ATOM 3525 CZ ARG A 467 43.615 13.910 20.671 1.00205.96 C ANISOU 3525 CZ ARG A 467 31133 30055 17066 3273 -3082 1710 C ATOM 3526 NH1 ARG A 467 44.076 14.574 21.720 1.00202.84 N ANISOU 3526 NH1 ARG A 467 31205 29786 16078 3336 -3509 1579 N ATOM 3527 NH2 ARG A 467 42.633 14.426 19.945 1.00204.85 N ANISOU 3527 NH2 ARG A 467 30879 29817 17138 3127 -2562 1563 N ATOM 3528 N GLY A 468 48.054 14.672 17.166 1.00157.58 N ANISOU 3528 N GLY A 468 22650 24100 13122 2622 -4587 1012 N ATOM 3529 CA GLY A 468 48.035 16.108 17.023 1.00156.65 C ANISOU 3529 CA GLY A 468 22584 24022 12915 2375 -4685 640 C ATOM 3530 C GLY A 468 49.387 16.775 16.865 1.00158.69 C ANISOU 3530 C GLY A 468 22482 24390 13423 2211 -5306 445 C ATOM 3531 O GLY A 468 49.432 17.982 16.602 1.00158.05 O ANISOU 3531 O GLY A 468 22373 24317 13364 1974 -5392 133 O ATOM 3532 N MET A 469 50.491 16.033 17.011 1.00161.72 N ANISOU 3532 N MET A 469 22570 24847 14029 2327 -5742 632 N ATOM 3533 CA MET A 469 51.814 16.672 16.948 1.00164.44 C ANISOU 3533 CA MET A 469 22549 25298 14633 2169 -6372 477 C ATOM 3534 C MET A 469 52.192 17.095 15.538 1.00160.38 C ANISOU 3534 C MET A 469 21371 24769 14796 1939 -6201 314 C ATOM 3535 O MET A 469 52.501 18.284 15.334 1.00160.38 O ANISOU 3535 O MET A 469 21271 24794 14871 1680 -6410 36 O ATOM 3536 CB MET A 469 52.869 15.755 17.570 1.00170.48 C ANISOU 3536 CB MET A 469 23186 26146 15444 2379 -6900 748 C ATOM 3537 CG MET A 469 54.280 16.330 17.492 1.00177.37 C ANISOU 3537 CG MET A 469 23605 27125 16664 2220 -7570 633 C ATOM 3538 SD MET A 469 54.345 18.051 18.030 1.00185.09 S ANISOU 3538 SD MET A 469 24921 28127 17278 1921 -7980 232 S ATOM 3539 CE MET A 469 56.052 18.466 17.681 1.00190.66 C ANISOU 3539 CE MET A 469 24899 28931 18612 1727 -8702 182 C ATOM 3540 N PRO A 470 52.200 16.220 14.524 1.00157.13 N ANISOU 3540 N PRO A 470 20509 24308 14886 2015 -5834 465 N ATOM 3541 CA PRO A 470 52.716 16.633 13.214 1.00154.15 C ANISOU 3541 CA PRO A 470 19505 23938 15129 1815 -5718 320 C ATOM 3542 C PRO A 470 51.885 17.753 12.606 1.00150.04 C ANISOU 3542 C PRO A 470 19085 23351 14573 1558 -5358 35 C ATOM 3543 O PRO A 470 50.695 17.900 12.890 1.00148.08 O ANISOU 3543 O PRO A 470 19305 23017 13941 1579 -5000 -7 O ATOM 3544 CB PRO A 470 52.629 15.355 12.374 1.00151.68 C ANISOU 3544 CB PRO A 470 18864 23550 15216 2008 -5322 542 C ATOM 3545 CG PRO A 470 51.557 14.569 13.009 1.00151.24 C ANISOU 3545 CG PRO A 470 19326 23395 14745 2212 -5023 726 C ATOM 3546 CD PRO A 470 51.672 14.843 14.478 1.00156.06 C ANISOU 3546 CD PRO A 470 20442 24084 14768 2282 -5472 764 C ATOM 3547 N GLN A 471 52.537 18.552 11.764 1.00150.45 N ANISOU 3547 N GLN A 471 18675 23441 15050 1318 -5453 -143 N ATOM 3548 CA GLN A 471 51.900 19.673 11.084 1.00150.89 C ANISOU 3548 CA GLN A 471 18755 23429 15146 1056 -5157 -408 C ATOM 3549 C GLN A 471 52.140 19.523 9.590 1.00150.89 C ANISOU 3549 C GLN A 471 18174 23411 15745 970 -4812 -410 C ATOM 3550 O GLN A 471 53.290 19.578 9.139 1.00155.98 O ANISOU 3550 O GLN A 471 18298 24144 16822 906 -5068 -384 O ATOM 3551 CB GLN A 471 52.449 21.013 11.585 1.00151.47 C ANISOU 3551 CB GLN A 471 18907 23547 15098 810 -5650 -647 C ATOM 3552 CG GLN A 471 52.300 21.250 13.084 1.00155.39 C ANISOU 3552 CG GLN A 471 20024 24060 14957 898 -6049 -681 C ATOM 3553 CD GLN A 471 50.853 21.392 13.523 1.00154.02 C ANISOU 3553 CD GLN A 471 20480 23787 14255 980 -5610 -743 C ATOM 3554 OE1 GLN A 471 50.280 22.481 13.479 1.00152.77 O ANISOU 3554 OE1 GLN A 471 20558 23555 13932 804 -5498 -994 O ATOM 3555 NE2 GLN A 471 50.257 20.288 13.957 1.00154.21 N ANISOU 3555 NE2 GLN A 471 20766 23796 14031 1253 -5354 -500 N ATOM 3556 N ILE A 472 51.066 19.327 8.828 1.00141.84 N ANISOU 3556 N ILE A 472 17117 22150 14627 976 -4234 -432 N ATOM 3557 CA ILE A 472 51.141 19.211 7.376 1.00133.56 C ANISOU 3557 CA ILE A 472 15609 21066 14072 902 -3867 -454 C ATOM 3558 C ILE A 472 50.315 20.334 6.771 1.00130.01 C ANISOU 3558 C ILE A 472 15279 20535 13585 652 -3574 -688 C ATOM 3559 O ILE A 472 49.097 20.397 6.980 1.00127.74 O ANISOU 3559 O ILE A 472 15405 20140 12990 674 -3270 -725 O ATOM 3560 CB ILE A 472 50.645 17.848 6.876 1.00131.40 C ANISOU 3560 CB ILE A 472 15305 20700 13920 1145 -3468 -258 C ATOM 3561 CG1 ILE A 472 51.414 16.718 7.554 1.00136.47 C ANISOU 3561 CG1 ILE A 472 15870 21400 14582 1414 -3765 -12 C ATOM 3562 CG2 ILE A 472 50.795 17.755 5.367 1.00128.32 C ANISOU 3562 CG2 ILE A 472 14478 20273 14004 1082 -3122 -305 C ATOM 3563 CD1 ILE A 472 51.049 15.362 7.025 1.00137.31 C ANISOU 3563 CD1 ILE A 472 15917 21389 14864 1653 -3412 177 C ATOM 3564 N GLU A 473 50.972 21.213 6.022 1.00140.02 N ANISOU 3564 N GLU A 473 16171 21847 15183 420 -3656 -824 N ATOM 3565 CA GLU A 473 50.292 22.309 5.352 1.00137.91 C ANISOU 3565 CA GLU A 473 15971 21495 14933 175 -3398 -1032 C ATOM 3566 C GLU A 473 49.771 21.836 4.003 1.00139.60 C ANISOU 3566 C GLU A 473 15977 21632 15432 201 -2874 -996 C ATOM 3567 O GLU A 473 50.535 21.316 3.180 1.00143.69 O ANISOU 3567 O GLU A 473 16055 22206 16337 254 -2809 -904 O ATOM 3568 CB GLU A 473 51.228 23.501 5.169 1.00138.30 C ANISOU 3568 CB GLU A 473 15727 21608 15213 -102 -3735 -1176 C ATOM 3569 CG GLU A 473 50.516 24.775 4.766 1.00138.36 C ANISOU 3569 CG GLU A 473 15903 21509 15158 -359 -3563 -1401 C ATOM 3570 CD GLU A 473 51.477 25.851 4.327 1.00144.26 C ANISOU 3570 CD GLU A 473 16272 22296 16245 -646 -3830 -1504 C ATOM 3571 OE1 GLU A 473 52.439 25.523 3.603 1.00151.62 O ANISOU 3571 OE1 GLU A 473 16674 23322 17612 -656 -3843 -1383 O ATOM 3572 OE2 GLU A 473 51.277 27.021 4.709 1.00143.79 O ANISOU 3572 OE2 GLU A 473 16442 22163 16029 -856 -4017 -1698 O ATOM 3573 N VAL A 474 48.471 22.009 3.788 1.00130.11 N ANISOU 3573 N VAL A 474 15102 20297 14039 176 -2505 -1067 N ATOM 3574 CA VAL A 474 47.821 21.678 2.528 1.00118.19 C ANISOU 3574 CA VAL A 474 13468 18685 12753 174 -2038 -1060 C ATOM 3575 C VAL A 474 47.464 22.975 1.821 1.00116.42 C ANISOU 3575 C VAL A 474 13220 18408 12605 -101 -1908 -1257 C ATOM 3576 O VAL A 474 46.948 23.915 2.440 1.00116.53 O ANISOU 3576 O VAL A 474 13538 18378 12361 -226 -1996 -1393 O ATOM 3577 CB VAL A 474 46.574 20.801 2.743 1.00113.01 C ANISOU 3577 CB VAL A 474 13160 17894 11885 353 -1723 -956 C ATOM 3578 CG1 VAL A 474 45.912 20.493 1.415 1.00109.26 C ANISOU 3578 CG1 VAL A 474 12566 17296 11653 332 -1301 -965 C ATOM 3579 CG2 VAL A 474 46.956 19.519 3.453 1.00115.43 C ANISOU 3579 CG2 VAL A 474 13495 18236 12125 623 -1861 -740 C ATOM 3580 N THR A 475 47.744 23.021 0.523 1.00111.12 N ANISOU 3580 N THR A 475 12208 17734 12280 -180 -1691 -1268 N ATOM 3581 CA THR A 475 47.574 24.208 -0.301 1.00109.40 C ANISOU 3581 CA THR A 475 11902 17472 12192 -441 -1571 -1421 C ATOM 3582 C THR A 475 46.557 23.917 -1.393 1.00105.50 C ANISOU 3582 C THR A 475 11476 16845 11764 -422 -1123 -1425 C ATOM 3583 O THR A 475 46.714 22.956 -2.160 1.00108.63 O ANISOU 3583 O THR A 475 11695 17237 12344 -276 -926 -1325 O ATOM 3584 CB THR A 475 48.905 24.645 -0.910 1.00112.76 C ANISOU 3584 CB THR A 475 11845 18022 12976 -574 -1730 -1413 C ATOM 3585 OG1 THR A 475 49.770 25.121 0.128 1.00121.59 O ANISOU 3585 OG1 THR A 475 12915 19238 14045 -645 -2205 -1432 O ATOM 3586 CG2 THR A 475 48.688 25.748 -1.919 1.00109.53 C ANISOU 3586 CG2 THR A 475 11340 17554 12724 -829 -1542 -1530 C ATOM 3587 N PHE A 476 45.525 24.755 -1.456 1.00111.16 N ANISOU 3587 N PHE A 476 12457 17441 12336 -564 -982 -1545 N ATOM 3588 CA PHE A 476 44.447 24.663 -2.431 1.00107.02 C ANISOU 3588 CA PHE A 476 12028 16772 11864 -581 -608 -1561 C ATOM 3589 C PHE A 476 44.620 25.786 -3.445 1.00109.94 C ANISOU 3589 C PHE A 476 12224 17126 12423 -825 -533 -1673 C ATOM 3590 O PHE A 476 44.541 26.969 -3.089 1.00115.12 O ANISOU 3590 O PHE A 476 12977 17758 13004 -1013 -668 -1794 O ATOM 3591 CB PHE A 476 43.084 24.766 -1.747 1.00103.52 C ANISOU 3591 CB PHE A 476 11994 16193 11144 -545 -487 -1584 C ATOM 3592 CG PHE A 476 42.868 23.748 -0.667 1.00103.93 C ANISOU 3592 CG PHE A 476 12250 16257 10982 -316 -544 -1452 C ATOM 3593 CD1 PHE A 476 43.379 23.946 0.605 1.00108.03 C ANISOU 3593 CD1 PHE A 476 12907 16875 11263 -274 -853 -1457 C ATOM 3594 CD2 PHE A 476 42.142 22.597 -0.917 1.00101.44 C ANISOU 3594 CD2 PHE A 476 12007 15838 10697 -148 -306 -1314 C ATOM 3595 CE1 PHE A 476 43.180 23.011 1.599 1.00107.58 C ANISOU 3595 CE1 PHE A 476 13061 16831 10984 -56 -898 -1312 C ATOM 3596 CE2 PHE A 476 41.937 21.661 0.076 1.00102.53 C ANISOU 3596 CE2 PHE A 476 12332 15974 10651 55 -347 -1162 C ATOM 3597 CZ PHE A 476 42.458 21.868 1.334 1.00104.99 C ANISOU 3597 CZ PHE A 476 12786 16402 10706 107 -631 -1154 C ATOM 3598 N ASP A 477 44.853 25.416 -4.701 1.00113.92 N ANISOU 3598 N ASP A 477 12496 17630 13158 -813 -318 -1629 N ATOM 3599 CA ASP A 477 45.052 26.362 -5.786 1.00114.36 C ANISOU 3599 CA ASP A 477 12382 17677 13395 -1023 -206 -1695 C ATOM 3600 C ASP A 477 43.852 26.351 -6.719 1.00109.34 C ANISOU 3600 C ASP A 477 11931 16875 12739 -1041 101 -1724 C ATOM 3601 O ASP A 477 43.299 25.293 -7.022 1.00107.97 O ANISOU 3601 O ASP A 477 11850 16628 12544 -865 268 -1660 O ATOM 3602 CB ASP A 477 46.314 26.026 -6.585 1.00124.49 C ANISOU 3602 CB ASP A 477 13254 19098 14948 -992 -177 -1613 C ATOM 3603 CG ASP A 477 47.585 26.375 -5.843 1.00129.83 C ANISOU 3603 CG ASP A 477 13664 19932 15734 -1053 -511 -1584 C ATOM 3604 OD1 ASP A 477 48.107 27.484 -6.066 1.00131.89 O ANISOU 3604 OD1 ASP A 477 13753 20225 16136 -1289 -612 -1629 O ATOM 3605 OD2 ASP A 477 48.064 25.540 -5.047 1.00133.26 O ANISOU 3605 OD2 ASP A 477 14055 20446 16131 -871 -690 -1506 O ATOM 3606 N ILE A 478 43.455 27.530 -7.177 1.00107.27 N ANISOU 3606 N ILE A 478 11721 16539 12498 -1258 150 -1814 N ATOM 3607 CA ILE A 478 42.489 27.667 -8.256 1.00101.68 C ANISOU 3607 CA ILE A 478 11130 15686 11819 -1305 409 -1833 C ATOM 3608 C ILE A 478 43.154 28.509 -9.331 1.00110.88 C ANISOU 3608 C ILE A 478 12071 16895 13163 -1489 472 -1845 C ATOM 3609 O ILE A 478 43.386 29.709 -9.133 1.00116.82 O ANISOU 3609 O ILE A 478 12791 17645 13951 -1698 347 -1907 O ATOM 3610 CB ILE A 478 41.171 28.294 -7.789 1.00 93.42 C ANISOU 3610 CB ILE A 478 10396 14475 10624 -1374 436 -1905 C ATOM 3611 CG1 ILE A 478 40.512 27.420 -6.726 1.00 88.40 C ANISOU 3611 CG1 ILE A 478 9973 13802 9813 -1181 419 -1857 C ATOM 3612 CG2 ILE A 478 40.234 28.465 -8.965 1.00 89.03 C ANISOU 3612 CG2 ILE A 478 9924 13769 10136 -1433 662 -1910 C ATOM 3613 CD1 ILE A 478 39.128 27.877 -6.337 1.00 87.00 C ANISOU 3613 CD1 ILE A 478 10080 13460 9515 -1206 518 -1896 C ATOM 3614 N ASP A 479 43.480 27.883 -10.458 1.00104.57 N ANISOU 3614 N ASP A 479 11132 16126 12472 -1404 670 -1781 N ATOM 3615 CA ASP A 479 44.178 28.562 -11.539 1.00106.56 C ANISOU 3615 CA ASP A 479 11165 16439 12883 -1546 782 -1756 C ATOM 3616 C ASP A 479 43.205 29.471 -12.288 1.00 96.75 C ANISOU 3616 C ASP A 479 10120 15039 11603 -1717 901 -1808 C ATOM 3617 O ASP A 479 42.042 29.631 -11.907 1.00 87.40 O ANISOU 3617 O ASP A 479 9206 13705 10298 -1729 880 -1868 O ATOM 3618 CB ASP A 479 44.847 27.544 -12.461 1.00112.16 C ANISOU 3618 CB ASP A 479 11699 17236 13681 -1358 982 -1673 C ATOM 3619 CG ASP A 479 43.902 26.442 -12.904 1.00110.10 C ANISOU 3619 CG ASP A 479 11690 16839 13303 -1159 1136 -1684 C ATOM 3620 OD1 ASP A 479 42.680 26.693 -12.989 1.00103.87 O ANISOU 3620 OD1 ASP A 479 11174 15881 12409 -1225 1158 -1738 O ATOM 3621 OD2 ASP A 479 44.382 25.321 -13.171 1.00114.96 O ANISOU 3621 OD2 ASP A 479 12223 17502 13953 -937 1223 -1637 O ATOM 3622 N ALA A 480 43.679 30.078 -13.377 1.00 89.96 N ANISOU 3622 N ALA A 480 9116 14209 10856 -1842 1039 -1767 N ATOM 3623 CA ALA A 480 42.832 30.972 -14.154 1.00 90.38 C ANISOU 3623 CA ALA A 480 9348 14112 10880 -2004 1137 -1795 C ATOM 3624 C ALA A 480 41.712 30.233 -14.871 1.00 91.24 C ANISOU 3624 C ALA A 480 9716 14080 10871 -1869 1293 -1806 C ATOM 3625 O ALA A 480 40.719 30.860 -15.252 1.00 95.13 O ANISOU 3625 O ALA A 480 10408 14414 11323 -1976 1317 -1837 O ATOM 3626 CB ALA A 480 43.675 31.745 -15.162 1.00 99.83 C ANISOU 3626 CB ALA A 480 10330 15383 12218 -2162 1260 -1715 C ATOM 3627 N ASP A 481 41.851 28.922 -15.073 1.00113.11 N ANISOU 3627 N ASP A 481 12485 16887 13604 -1639 1379 -1780 N ATOM 3628 CA ASP A 481 40.771 28.140 -15.660 1.00106.38 C ANISOU 3628 CA ASP A 481 11890 15873 12659 -1516 1472 -1799 C ATOM 3629 C ASP A 481 39.627 27.907 -14.686 1.00 99.05 C ANISOU 3629 C ASP A 481 11158 14805 11673 -1486 1352 -1834 C ATOM 3630 O ASP A 481 38.552 27.476 -15.112 1.00100.16 O ANISOU 3630 O ASP A 481 11501 14774 11779 -1439 1395 -1839 O ATOM 3631 CB ASP A 481 41.295 26.787 -16.155 1.00113.43 C ANISOU 3631 CB ASP A 481 12740 16818 13541 -1271 1589 -1771 C ATOM 3632 CG ASP A 481 42.241 26.915 -17.338 1.00125.53 C ANISOU 3632 CG ASP A 481 14130 18463 15102 -1256 1786 -1729 C ATOM 3633 OD1 ASP A 481 42.203 27.954 -18.027 1.00124.22 O ANISOU 3633 OD1 ASP A 481 13971 18288 14938 -1439 1854 -1713 O ATOM 3634 OD2 ASP A 481 43.020 25.969 -17.585 1.00138.29 O ANISOU 3634 OD2 ASP A 481 15632 20172 16740 -1049 1892 -1702 O ATOM 3635 N GLY A 482 39.829 28.181 -13.402 1.00 87.93 N ANISOU 3635 N GLY A 482 9696 13459 10253 -1510 1202 -1848 N ATOM 3636 CA GLY A 482 38.860 27.845 -12.381 1.00 89.69 C ANISOU 3636 CA GLY A 482 10099 13579 10401 -1441 1129 -1857 C ATOM 3637 C GLY A 482 38.949 26.427 -11.865 1.00 90.25 C ANISOU 3637 C GLY A 482 10178 13670 10441 -1214 1120 -1800 C ATOM 3638 O GLY A 482 38.006 25.961 -11.215 1.00 81.83 O ANISOU 3638 O GLY A 482 9276 12490 9326 -1139 1111 -1773 O ATOM 3639 N ILE A 483 40.053 25.731 -12.121 1.00 94.51 N ANISOU 3639 N ILE A 483 10538 14345 11027 -1095 1134 -1767 N ATOM 3640 CA ILE A 483 40.201 24.318 -11.792 1.00 92.60 C ANISOU 3640 CA ILE A 483 10302 14101 10780 -861 1133 -1706 C ATOM 3641 C ILE A 483 41.082 24.186 -10.558 1.00 97.96 C ANISOU 3641 C ILE A 483 10843 14943 11434 -795 966 -1669 C ATOM 3642 O ILE A 483 42.030 24.958 -10.369 1.00 99.41 O ANISOU 3642 O ILE A 483 10833 15279 11660 -901 871 -1688 O ATOM 3643 CB ILE A 483 40.781 23.540 -12.991 1.00 88.28 C ANISOU 3643 CB ILE A 483 9676 13567 10301 -730 1275 -1698 C ATOM 3644 CG1 ILE A 483 39.796 23.568 -14.163 1.00 86.26 C ANISOU 3644 CG1 ILE A 483 9624 13124 10029 -780 1395 -1740 C ATOM 3645 CG2 ILE A 483 41.116 22.103 -12.617 1.00 86.54 C ANISOU 3645 CG2 ILE A 483 9439 13342 10102 -475 1260 -1639 C ATOM 3646 CD1 ILE A 483 40.260 22.798 -15.377 1.00 85.95 C ANISOU 3646 CD1 ILE A 483 9588 13068 9999 -633 1540 -1755 C ATOM 3647 N LEU A 484 40.762 23.211 -9.709 1.00117.22 N ANISOU 3647 N LEU A 484 13385 17338 13813 -628 912 -1603 N ATOM 3648 CA LEU A 484 41.466 23.033 -8.448 1.00112.16 C ANISOU 3648 CA LEU A 484 12671 16834 13109 -551 724 -1555 C ATOM 3649 C LEU A 484 42.742 22.223 -8.632 1.00109.28 C ANISOU 3649 C LEU A 484 12057 16606 12859 -387 689 -1495 C ATOM 3650 O LEU A 484 42.795 21.288 -9.435 1.00108.15 O ANISOU 3650 O LEU A 484 11894 16399 12800 -237 828 -1467 O ATOM 3651 CB LEU A 484 40.556 22.343 -7.432 1.00104.93 C ANISOU 3651 CB LEU A 484 11989 15814 12067 -433 700 -1479 C ATOM 3652 CG LEU A 484 41.117 22.069 -6.035 1.00 97.09 C ANISOU 3652 CG LEU A 484 11001 14942 10946 -329 500 -1412 C ATOM 3653 CD1 LEU A 484 41.455 23.369 -5.336 1.00 96.20 C ANISOU 3653 CD1 LEU A 484 10892 14938 10723 -498 328 -1504 C ATOM 3654 CD2 LEU A 484 40.132 21.269 -5.208 1.00 93.02 C ANISOU 3654 CD2 LEU A 484 10731 14302 10310 -196 546 -1302 C ATOM 3655 N HIS A 485 43.773 22.598 -7.875 1.00107.71 N ANISOU 3655 N HIS A 485 11670 16583 12670 -410 487 -1478 N ATOM 3656 CA HIS A 485 45.018 21.844 -7.783 1.00109.97 C ANISOU 3656 CA HIS A 485 11688 17010 13085 -239 407 -1396 C ATOM 3657 C HIS A 485 45.444 21.826 -6.323 1.00112.75 C ANISOU 3657 C HIS A 485 12044 17462 13333 -200 111 -1344 C ATOM 3658 O HIS A 485 45.755 22.875 -5.749 1.00109.94 O ANISOU 3658 O HIS A 485 11651 17190 12930 -377 -83 -1401 O ATOM 3659 CB HIS A 485 46.115 22.457 -8.657 1.00108.52 C ANISOU 3659 CB HIS A 485 11167 16965 13100 -333 461 -1411 C ATOM 3660 CG HIS A 485 45.720 22.637 -10.088 1.00108.73 C ANISOU 3660 CG HIS A 485 11230 16907 13176 -385 746 -1463 C ATOM 3661 ND1 HIS A 485 45.610 21.584 -10.969 1.00117.20 N ANISOU 3661 ND1 HIS A 485 12349 17897 14286 -182 956 -1446 N ATOM 3662 CD2 HIS A 485 45.416 23.752 -10.793 1.00113.44 C ANISOU 3662 CD2 HIS A 485 11851 17477 13776 -612 841 -1531 C ATOM 3663 CE1 HIS A 485 45.251 22.041 -12.155 1.00124.61 C ANISOU 3663 CE1 HIS A 485 13353 18771 15223 -279 1161 -1506 C ATOM 3664 NE2 HIS A 485 45.128 23.354 -12.076 1.00122.33 N ANISOU 3664 NE2 HIS A 485 13043 18519 14920 -540 1100 -1546 N ATOM 3665 N VAL A 486 45.450 20.642 -5.723 1.00107.68 N ANISOU 3665 N VAL A 486 11470 16796 12647 32 59 -1236 N ATOM 3666 CA VAL A 486 45.762 20.473 -4.310 1.00109.99 C ANISOU 3666 CA VAL A 486 11827 17169 12795 105 -223 -1165 C ATOM 3667 C VAL A 486 47.171 19.915 -4.193 1.00115.48 C ANISOU 3667 C VAL A 486 12183 18020 13674 251 -392 -1071 C ATOM 3668 O VAL A 486 47.461 18.829 -4.709 1.00115.20 O ANISOU 3668 O VAL A 486 12038 17950 13783 464 -265 -990 O ATOM 3669 CB VAL A 486 44.752 19.547 -3.619 1.00108.34 C ANISOU 3669 CB VAL A 486 11941 16818 12404 263 -169 -1072 C ATOM 3670 CG1 VAL A 486 45.064 19.450 -2.138 1.00110.87 C ANISOU 3670 CG1 VAL A 486 12374 17231 12520 340 -456 -991 C ATOM 3671 CG2 VAL A 486 43.340 20.051 -3.850 1.00106.86 C ANISOU 3671 CG2 VAL A 486 12032 16470 12102 130 31 -1143 C ATOM 3672 N SER A 487 48.045 20.647 -3.509 1.00136.75 N ANISOU 3672 N SER A 487 14711 20869 16380 143 -694 -1081 N ATOM 3673 CA SER A 487 49.386 20.163 -3.215 1.00144.40 C ANISOU 3673 CA SER A 487 15337 21990 17540 278 -917 -969 C ATOM 3674 C SER A 487 49.596 20.176 -1.710 1.00149.37 C ANISOU 3674 C SER A 487 16113 22684 17957 310 -1309 -918 C ATOM 3675 O SER A 487 48.985 20.970 -0.997 1.00154.63 O ANISOU 3675 O SER A 487 17070 23319 18362 160 -1430 -1010 O ATOM 3676 CB SER A 487 50.461 21.011 -3.906 1.00148.50 C ANISOU 3676 CB SER A 487 15430 22645 18348 111 -952 -1000 C ATOM 3677 OG SER A 487 50.486 22.329 -3.389 1.00147.86 O ANISOU 3677 OG SER A 487 15394 22602 18183 -166 -1187 -1103 O ATOM 3678 N ALA A 488 50.453 19.286 -1.224 1.00148.52 N ANISOU 3678 N ALA A 488 15826 22658 17948 524 -1507 -770 N ATOM 3679 CA ALA A 488 50.698 19.171 0.206 1.00154.99 C ANISOU 3679 CA ALA A 488 16806 23539 18544 588 -1904 -698 C ATOM 3680 C ALA A 488 52.182 19.335 0.493 1.00159.48 C ANISOU 3680 C ALA A 488 16949 24283 19363 584 -2278 -629 C ATOM 3681 O ALA A 488 53.028 19.189 -0.393 1.00160.02 O ANISOU 3681 O ALA A 488 16575 24420 19805 615 -2173 -583 O ATOM 3682 CB ALA A 488 50.201 17.830 0.760 1.00159.86 C ANISOU 3682 CB ALA A 488 17676 24063 19003 873 -1849 -542 C ATOM 3683 N LYS A 489 52.492 19.642 1.751 1.00154.34 N ANISOU 3683 N LYS A 489 16439 23700 18503 554 -2721 -614 N ATOM 3684 CA LYS A 489 53.882 19.809 2.149 1.00161.85 C ANISOU 3684 CA LYS A 489 16993 24807 19696 537 -3156 -537 C ATOM 3685 C LYS A 489 53.984 19.687 3.660 1.00164.06 C ANISOU 3685 C LYS A 489 17574 25122 19640 610 -3630 -483 C ATOM 3686 O LYS A 489 53.082 20.106 4.389 1.00164.61 O ANISOU 3686 O LYS A 489 18141 25123 19282 546 -3664 -582 O ATOM 3687 CB LYS A 489 54.432 21.162 1.679 1.00166.36 C ANISOU 3687 CB LYS A 489 17274 25441 20494 213 -3265 -668 C ATOM 3688 CG LYS A 489 55.915 21.361 1.934 1.00173.66 C ANISOU 3688 CG LYS A 489 17695 26517 21772 166 -3698 -568 C ATOM 3689 CD LYS A 489 56.435 22.572 1.182 1.00175.24 C ANISOU 3689 CD LYS A 489 17536 26755 22293 -151 -3687 -658 C ATOM 3690 CE LYS A 489 56.234 22.409 -0.317 1.00172.37 C ANISOU 3690 CE LYS A 489 16947 26366 22180 -129 -3104 -649 C ATOM 3691 NZ LYS A 489 56.737 23.583 -1.082 1.00171.95 N ANISOU 3691 NZ LYS A 489 16546 26348 22438 -435 -3058 -703 N ATOM 3692 N ASP A 490 55.085 19.100 4.121 1.00154.24 N ANISOU 3692 N ASP A 490 16032 23985 18586 763 -3987 -317 N ATOM 3693 CA ASP A 490 55.364 19.050 5.550 1.00159.08 C ANISOU 3693 CA ASP A 490 16900 24649 18894 822 -4517 -259 C ATOM 3694 C ASP A 490 55.682 20.455 6.045 1.00163.65 C ANISOU 3694 C ASP A 490 17523 25272 19384 510 -4924 -438 C ATOM 3695 O ASP A 490 56.613 21.098 5.550 1.00172.40 O ANISOU 3695 O ASP A 490 18150 26456 20899 324 -5091 -464 O ATOM 3696 CB ASP A 490 56.521 18.097 5.839 1.00162.51 C ANISOU 3696 CB ASP A 490 16956 25180 19609 1059 -4825 -25 C ATOM 3697 CG ASP A 490 56.808 17.962 7.323 1.00165.67 C ANISOU 3697 CG ASP A 490 17650 25630 19668 1144 -5400 57 C ATOM 3698 OD1 ASP A 490 55.909 18.268 8.134 1.00166.55 O ANISOU 3698 OD1 ASP A 490 18349 25680 19253 1109 -5439 -34 O ATOM 3699 OD2 ASP A 490 57.930 17.545 7.680 1.00166.71 O ANISOU 3699 OD2 ASP A 490 17429 25860 20052 1258 -5810 221 O ATOM 3700 N LYS A 491 54.907 20.928 7.024 1.00155.80 N ANISOU 3700 N LYS A 491 17111 24220 17866 458 -5074 -557 N ATOM 3701 CA LYS A 491 54.987 22.324 7.446 1.00154.99 C ANISOU 3701 CA LYS A 491 17157 24108 17624 160 -5402 -776 C ATOM 3702 C LYS A 491 56.386 22.685 7.931 1.00156.54 C ANISOU 3702 C LYS A 491 16987 24414 18076 54 -6054 -736 C ATOM 3703 O LYS A 491 57.005 23.634 7.437 1.00158.66 O ANISOU 3703 O LYS A 491 16894 24697 18691 -221 -6201 -832 O ATOM 3704 CB LYS A 491 53.953 22.593 8.539 1.00155.87 C ANISOU 3704 CB LYS A 491 18000 24140 17085 200 -5453 -890 C ATOM 3705 CG LYS A 491 54.026 23.981 9.151 1.00159.58 C ANISOU 3705 CG LYS A 491 18722 24574 17339 -64 -5845 -1136 C ATOM 3706 CD LYS A 491 53.663 25.055 8.140 1.00156.64 C ANISOU 3706 CD LYS A 491 18202 24115 17199 -347 -5541 -1329 C ATOM 3707 CE LYS A 491 53.599 26.431 8.787 1.00160.41 C ANISOU 3707 CE LYS A 491 19007 24512 17429 -595 -5906 -1590 C ATOM 3708 NZ LYS A 491 53.250 27.486 7.795 1.00156.05 N ANISOU 3708 NZ LYS A 491 18311 23859 17123 -869 -5615 -1760 N ATOM 3709 N ASN A 492 56.903 21.932 8.901 1.00164.05 N ANISOU 3709 N ASN A 492 18016 25434 18881 264 -6468 -575 N ATOM 3710 CA ASN A 492 58.159 22.312 9.540 1.00170.55 C ANISOU 3710 CA ASN A 492 18562 26347 19891 159 -7179 -541 C ATOM 3711 C ASN A 492 59.344 22.114 8.602 1.00168.42 C ANISOU 3711 C ASN A 492 17466 26173 20351 120 -7188 -387 C ATOM 3712 O ASN A 492 60.132 23.040 8.377 1.00168.73 O ANISOU 3712 O ASN A 492 17122 26240 20748 -158 -7490 -453 O ATOM 3713 CB ASN A 492 58.349 21.513 10.829 1.00176.95 C ANISOU 3713 CB ASN A 492 19707 27202 20323 417 -7620 -391 C ATOM 3714 CG ASN A 492 57.237 21.755 11.831 1.00173.49 C ANISOU 3714 CG ASN A 492 20100 26682 19138 467 -7614 -529 C ATOM 3715 OD1 ASN A 492 56.725 22.868 11.950 1.00166.75 O ANISOU 3715 OD1 ASN A 492 19560 25750 18047 241 -7619 -784 O ATOM 3716 ND2 ASN A 492 56.856 20.710 12.556 1.00175.77 N ANISOU 3716 ND2 ASN A 492 20751 26978 19054 775 -7584 -349 N ATOM 3717 N SER A 493 59.484 20.915 8.039 1.00178.01 N ANISOU 3717 N SER A 493 18398 27428 21810 401 -6846 -174 N ATOM 3718 CA SER A 493 60.664 20.606 7.238 1.00181.60 C ANISOU 3718 CA SER A 493 18075 27983 22942 431 -6846 -1 C ATOM 3719 C SER A 493 60.594 21.247 5.859 1.00179.13 C ANISOU 3719 C SER A 493 17402 27654 23003 225 -6346 -95 C ATOM 3720 O SER A 493 61.566 21.855 5.397 1.00181.21 O ANISOU 3720 O SER A 493 17097 27989 23764 31 -6510 -59 O ATOM 3721 CB SER A 493 60.825 19.091 7.108 1.00184.20 C ANISOU 3721 CB SER A 493 18262 28337 23388 832 -6638 244 C ATOM 3722 OG SER A 493 59.732 18.523 6.407 1.00181.37 O ANISOU 3722 OG SER A 493 18181 27876 22854 971 -5970 207 O ATOM 3723 N GLY A 494 59.453 21.128 5.190 1.00178.74 N ANISOU 3723 N GLY A 494 17673 27508 22731 261 -5744 -199 N ATOM 3724 CA GLY A 494 59.331 21.498 3.800 1.00174.92 C ANISOU 3724 CA GLY A 494 16883 27007 22570 137 -5213 -253 C ATOM 3725 C GLY A 494 59.331 20.321 2.851 1.00174.50 C ANISOU 3725 C GLY A 494 16591 26959 22751 437 -4697 -106 C ATOM 3726 O GLY A 494 59.114 20.516 1.648 1.00176.68 O ANISOU 3726 O GLY A 494 16693 27212 23226 375 -4204 -154 O ATOM 3727 N LYS A 495 59.577 19.112 3.356 1.00170.17 N ANISOU 3727 N LYS A 495 16053 26430 22176 765 -4808 71 N ATOM 3728 CA LYS A 495 59.491 17.921 2.525 1.00167.94 C ANISOU 3728 CA LYS A 495 15627 26111 22074 1077 -4331 191 C ATOM 3729 C LYS A 495 58.082 17.771 1.969 1.00161.91 C ANISOU 3729 C LYS A 495 15347 25194 20978 1087 -3803 52 C ATOM 3730 O LYS A 495 57.097 17.856 2.707 1.00158.35 O ANISOU 3730 O LYS A 495 15453 24655 20059 1054 -3861 -30 O ATOM 3731 CB LYS A 495 59.882 16.679 3.327 1.00171.49 C ANISOU 3731 CB LYS A 495 16094 26570 22496 1422 -4593 401 C ATOM 3732 CG LYS A 495 59.241 15.394 2.817 1.00168.69 C ANISOU 3732 CG LYS A 495 15926 26088 22081 1746 -4121 472 C ATOM 3733 CD LYS A 495 59.840 14.148 3.448 1.00168.80 C ANISOU 3733 CD LYS A 495 15837 26106 22193 2101 -4366 712 C ATOM 3734 CE LYS A 495 61.114 13.726 2.733 1.00169.77 C ANISOU 3734 CE LYS A 495 15259 26323 22922 2275 -4316 861 C ATOM 3735 NZ LYS A 495 61.383 12.272 2.903 1.00170.08 N ANISOU 3735 NZ LYS A 495 15256 26292 23076 2694 -4294 1068 N ATOM 3736 N GLU A 496 57.994 17.554 0.660 1.00176.50 N ANISOU 3736 N GLU A 496 16981 27009 23073 1138 -3287 32 N ATOM 3737 CA GLU A 496 56.706 17.407 0.003 1.00170.79 C ANISOU 3737 CA GLU A 496 16667 26131 22095 1139 -2804 -95 C ATOM 3738 C GLU A 496 55.950 16.204 0.563 1.00159.60 C ANISOU 3738 C GLU A 496 15665 24584 20392 1416 -2748 -13 C ATOM 3739 O GLU A 496 56.521 15.308 1.191 1.00153.67 O ANISOU 3739 O GLU A 496 14823 23860 19707 1662 -2985 161 O ATOM 3740 CB GLU A 496 56.899 17.259 -1.505 1.00180.56 C ANISOU 3740 CB GLU A 496 17590 27360 23656 1189 -2305 -111 C ATOM 3741 CG GLU A 496 57.770 18.341 -2.126 1.00190.66 C ANISOU 3741 CG GLU A 496 18389 28773 25278 944 -2318 -133 C ATOM 3742 CD GLU A 496 58.302 17.951 -3.490 1.00195.70 C ANISOU 3742 CD GLU A 496 18634 29444 26280 1091 -1859 -76 C ATOM 3743 OE1 GLU A 496 58.414 16.737 -3.761 1.00202.43 O ANISOU 3743 OE1 GLU A 496 19457 30248 27211 1432 -1666 14 O ATOM 3744 OE2 GLU A 496 58.608 18.856 -4.293 1.00191.39 O ANISOU 3744 OE2 GLU A 496 17826 28961 25931 875 -1682 -118 O ATOM 3745 N GLN A 497 54.640 16.195 0.329 1.00130.69 N ANISOU 3745 N GLN A 497 12452 20771 16434 1367 -2435 -124 N ATOM 3746 CA GLN A 497 53.767 15.119 0.781 1.00132.41 C ANISOU 3746 CA GLN A 497 13078 20835 16396 1588 -2329 -40 C ATOM 3747 C GLN A 497 52.935 14.638 -0.398 1.00130.68 C ANISOU 3747 C GLN A 497 12970 20448 16234 1648 -1816 -108 C ATOM 3748 O GLN A 497 52.189 15.422 -0.995 1.00130.08 O ANISOU 3748 O GLN A 497 13036 20323 16067 1429 -1585 -269 O ATOM 3749 CB GLN A 497 52.867 15.588 1.927 1.00130.15 C ANISOU 3749 CB GLN A 497 13295 20513 15643 1464 -2518 -83 C ATOM 3750 CG GLN A 497 51.641 14.722 2.167 1.00125.34 C ANISOU 3750 CG GLN A 497 13137 19717 14768 1611 -2272 -18 C ATOM 3751 CD GLN A 497 51.980 13.301 2.572 1.00127.76 C ANISOU 3751 CD GLN A 497 13431 19967 15145 1941 -2352 209 C ATOM 3752 OE1 GLN A 497 52.363 12.475 1.743 1.00127.90 O ANISOU 3752 OE1 GLN A 497 13197 19922 15476 2125 -2158 265 O ATOM 3753 NE2 GLN A 497 51.830 13.008 3.852 1.00129.93 N ANISOU 3753 NE2 GLN A 497 14003 20251 15113 2031 -2631 342 N ATOM 3754 N LYS A 498 53.061 13.357 -0.731 1.00151.12 N ANISOU 3754 N LYS A 498 15507 22934 18976 1946 -1663 10 N ATOM 3755 CA LYS A 498 52.329 12.793 -1.854 1.00145.05 C ANISOU 3755 CA LYS A 498 14863 21982 18269 2024 -1223 -60 C ATOM 3756 C LYS A 498 50.862 12.590 -1.494 1.00141.13 C ANISOU 3756 C LYS A 498 14877 21294 17451 1967 -1104 -81 C ATOM 3757 O LYS A 498 50.517 12.238 -0.362 1.00144.45 O ANISOU 3757 O LYS A 498 15555 21684 17645 2029 -1305 41 O ATOM 3758 CB LYS A 498 52.960 11.473 -2.297 1.00145.89 C ANISOU 3758 CB LYS A 498 14772 22010 18649 2376 -1117 61 C ATOM 3759 CG LYS A 498 54.299 11.659 -2.989 1.00147.73 C ANISOU 3759 CG LYS A 498 14466 22409 19254 2450 -1090 70 C ATOM 3760 CD LYS A 498 54.953 10.335 -3.333 1.00152.60 C ANISOU 3760 CD LYS A 498 14895 22944 20141 2837 -990 194 C ATOM 3761 CE LYS A 498 56.295 10.566 -4.004 1.00157.74 C ANISOU 3761 CE LYS A 498 14976 23776 21182 2923 -925 223 C ATOM 3762 NZ LYS A 498 57.039 9.300 -4.234 1.00164.03 N ANISOU 3762 NZ LYS A 498 15557 24503 22264 3334 -850 355 N ATOM 3763 N ILE A 499 49.999 12.816 -2.479 1.00127.04 N ANISOU 3763 N ILE A 499 13234 19381 15655 1852 -770 -221 N ATOM 3764 CA ILE A 499 48.555 12.847 -2.290 1.00124.21 C ANISOU 3764 CA ILE A 499 13301 18847 15046 1744 -630 -254 C ATOM 3765 C ILE A 499 47.927 11.783 -3.176 1.00124.30 C ANISOU 3765 C ILE A 499 13438 18612 15178 1899 -343 -250 C ATOM 3766 O ILE A 499 48.233 11.710 -4.371 1.00126.53 O ANISOU 3766 O ILE A 499 13554 18866 15656 1935 -138 -353 O ATOM 3767 CB ILE A 499 47.981 14.235 -2.626 1.00123.16 C ANISOU 3767 CB ILE A 499 13240 18764 14792 1425 -543 -433 C ATOM 3768 CG1 ILE A 499 48.673 15.316 -1.792 1.00123.81 C ANISOU 3768 CG1 ILE A 499 13200 19065 14779 1264 -858 -461 C ATOM 3769 CG2 ILE A 499 46.479 14.254 -2.426 1.00124.14 C ANISOU 3769 CG2 ILE A 499 13765 18706 14697 1332 -388 -449 C ATOM 3770 CD1 ILE A 499 48.189 16.716 -2.082 1.00124.36 C ANISOU 3770 CD1 ILE A 499 13336 19167 14749 957 -796 -637 C ATOM 3771 N THR A 500 47.048 10.965 -2.600 1.00127.17 N ANISOU 3771 N THR A 500 14110 18787 15424 1989 -330 -127 N ATOM 3772 CA THR A 500 46.317 9.953 -3.355 1.00126.74 C ANISOU 3772 CA THR A 500 14219 18452 15487 2106 -101 -120 C ATOM 3773 C THR A 500 44.851 10.355 -3.422 1.00121.94 C ANISOU 3773 C THR A 500 13914 17691 14726 1894 51 -169 C ATOM 3774 O THR A 500 44.195 10.485 -2.386 1.00122.45 O ANISOU 3774 O THR A 500 14189 17749 14588 1831 -23 -56 O ATOM 3775 CB THR A 500 46.460 8.571 -2.718 1.00131.89 C ANISOU 3775 CB THR A 500 14953 18959 16200 2383 -200 93 C ATOM 3776 OG1 THR A 500 47.838 8.316 -2.425 1.00137.26 O ANISOU 3776 OG1 THR A 500 15334 19809 17008 2576 -394 167 O ATOM 3777 CG2 THR A 500 45.949 7.496 -3.668 1.00132.43 C ANISOU 3777 CG2 THR A 500 15141 18721 16457 2521 7 70 C ATOM 3778 N ILE A 501 44.333 10.541 -4.631 1.00126.51 N ANISOU 3778 N ILE A 501 14520 18148 15401 1796 265 -326 N ATOM 3779 CA ILE A 501 42.961 10.994 -4.826 1.00126.51 C ANISOU 3779 CA ILE A 501 14759 18003 15307 1586 399 -378 C ATOM 3780 C ILE A 501 42.075 9.781 -5.072 1.00128.94 C ANISOU 3780 C ILE A 501 15276 17986 15729 1692 493 -284 C ATOM 3781 O ILE A 501 42.254 9.059 -6.060 1.00137.14 O ANISOU 3781 O ILE A 501 16295 18866 16945 1815 575 -356 O ATOM 3782 CB ILE A 501 42.858 11.995 -5.984 1.00128.95 C ANISOU 3782 CB ILE A 501 14990 18361 15646 1393 538 -593 C ATOM 3783 CG1 ILE A 501 43.831 13.153 -5.762 1.00135.44 C ANISOU 3783 CG1 ILE A 501 15574 19482 16405 1283 431 -667 C ATOM 3784 CG2 ILE A 501 41.441 12.515 -6.099 1.00125.56 C ANISOU 3784 CG2 ILE A 501 14785 17786 15134 1179 645 -628 C ATOM 3785 CD1 ILE A 501 43.770 14.209 -6.838 1.00140.16 C ANISOU 3785 CD1 ILE A 501 16093 20134 17028 1082 568 -849 C ATOM 3786 N LYS A 502 41.116 9.562 -4.177 1.00119.45 N ANISOU 3786 N LYS A 502 14281 16673 14429 1645 486 -121 N ATOM 3787 CA LYS A 502 40.177 8.458 -4.275 1.00121.80 C ANISOU 3787 CA LYS A 502 14769 16646 14864 1707 559 7 C ATOM 3788 C LYS A 502 38.752 8.993 -4.333 1.00120.83 C ANISOU 3788 C LYS A 502 14804 16396 14709 1477 686 9 C ATOM 3789 O LYS A 502 38.476 10.134 -3.941 1.00121.98 O ANISOU 3789 O LYS A 502 14953 16715 14679 1309 711 -40 O ATOM 3790 CB LYS A 502 40.323 7.494 -3.088 1.00126.84 C ANISOU 3790 CB LYS A 502 15491 17235 15468 1894 452 276 C ATOM 3791 CG LYS A 502 41.710 6.893 -2.931 1.00130.18 C ANISOU 3791 CG LYS A 502 15745 17769 15950 2146 300 310 C ATOM 3792 CD LYS A 502 42.105 6.093 -4.161 1.00137.99 C ANISOU 3792 CD LYS A 502 16661 18572 17198 2295 364 188 C ATOM 3793 CE LYS A 502 41.138 4.947 -4.419 1.00141.52 C ANISOU 3793 CE LYS A 502 17328 18625 17818 2344 428 290 C ATOM 3794 NZ LYS A 502 41.471 4.229 -5.680 1.00141.71 N ANISOU 3794 NZ LYS A 502 17339 18445 18060 2490 484 126 N ATOM 3795 N ALA A 503 37.848 8.143 -4.828 1.00120.56 N ANISOU 3795 N ALA A 503 14898 16039 14872 1475 755 70 N ATOM 3796 CA ALA A 503 36.425 8.466 -4.947 1.00124.36 C ANISOU 3796 CA ALA A 503 15497 16349 15406 1270 866 107 C ATOM 3797 C ALA A 503 36.202 9.731 -5.770 1.00122.12 C ANISOU 3797 C ALA A 503 15155 16177 15069 1065 927 -124 C ATOM 3798 O ALA A 503 35.268 10.495 -5.519 1.00120.08 O ANISOU 3798 O ALA A 503 14944 15922 14760 889 1010 -99 O ATOM 3799 CB ALA A 503 35.766 8.596 -3.570 1.00130.21 C ANISOU 3799 CB ALA A 503 16336 17134 16004 1238 917 352 C ATOM 3800 N SER A 504 37.057 9.960 -6.758 1.00120.04 N ANISOU 3800 N SER A 504 14787 16001 14822 1098 903 -335 N ATOM 3801 CA SER A 504 36.997 11.158 -7.574 1.00112.71 C ANISOU 3801 CA SER A 504 13800 15190 13834 916 957 -541 C ATOM 3802 C SER A 504 36.325 10.850 -8.908 1.00111.05 C ANISOU 3802 C SER A 504 13687 14719 13788 853 994 -660 C ATOM 3803 O SER A 504 35.946 9.714 -9.201 1.00116.81 O ANISOU 3803 O SER A 504 14528 15170 14685 946 961 -602 O ATOM 3804 CB SER A 504 38.401 11.728 -7.776 1.00114.49 C ANISOU 3804 CB SER A 504 13837 15704 13961 978 921 -673 C ATOM 3805 OG SER A 504 39.296 10.725 -8.223 1.00118.41 O ANISOU 3805 OG SER A 504 14274 16152 14565 1207 896 -689 O ATOM 3806 N SER A 505 36.176 11.884 -9.727 1.00103.66 N ANISOU 3806 N SER A 505 12727 13859 12800 689 1040 -828 N ATOM 3807 CA SER A 505 35.583 11.757 -11.048 1.00101.77 C ANISOU 3807 CA SER A 505 12602 13399 12668 619 1048 -960 C ATOM 3808 C SER A 505 36.582 12.173 -12.120 1.00101.78 C ANISOU 3808 C SER A 505 12542 13548 12583 666 1096 -1162 C ATOM 3809 O SER A 505 37.608 12.798 -11.837 1.00109.78 O ANISOU 3809 O SER A 505 13381 14846 13484 695 1130 -1193 O ATOM 3810 CB SER A 505 34.310 12.605 -11.159 1.00105.27 C ANISOU 3810 CB SER A 505 13099 13758 13141 375 1068 -950 C ATOM 3811 OG SER A 505 33.813 12.605 -12.486 1.00107.34 O ANISOU 3811 OG SER A 505 13473 13830 13480 297 1036 -1088 O ATOM 3812 N GLY A 506 36.277 11.799 -13.356 1.00106.67 N ANISOU 3812 N GLY A 506 13311 13961 13258 677 1093 -1290 N ATOM 3813 CA GLY A 506 37.030 12.232 -14.518 1.00109.76 C ANISOU 3813 CA GLY A 506 13693 14463 13546 713 1177 -1475 C ATOM 3814 C GLY A 506 37.919 11.132 -15.075 1.00116.76 C ANISOU 3814 C GLY A 506 14627 15277 14459 993 1213 -1546 C ATOM 3815 O GLY A 506 38.035 10.036 -14.526 1.00125.22 O ANISOU 3815 O GLY A 506 15724 16215 15640 1163 1154 -1454 O ATOM 3816 N LEU A 507 38.543 11.456 -16.203 1.00 97.14 N ANISOU 3816 N LEU A 507 12165 12875 11870 1048 1327 -1706 N ATOM 3817 CA LEU A 507 39.515 10.589 -16.848 1.00 97.20 C ANISOU 3817 CA LEU A 507 12205 12854 11872 1339 1422 -1797 C ATOM 3818 C LEU A 507 40.890 10.877 -16.277 1.00 99.04 C ANISOU 3818 C LEU A 507 12111 13419 12100 1465 1528 -1732 C ATOM 3819 O LEU A 507 41.158 11.980 -15.799 1.00110.87 O ANISOU 3819 O LEU A 507 13396 15180 13550 1294 1544 -1680 O ATOM 3820 CB LEU A 507 39.542 10.811 -18.359 1.00100.60 C ANISOU 3820 CB LEU A 507 12835 13224 12165 1360 1530 -1989 C ATOM 3821 CG LEU A 507 38.196 10.926 -19.062 1.00101.12 C ANISOU 3821 CG LEU A 507 13199 13015 12206 1169 1396 -2065 C ATOM 3822 CD1 LEU A 507 38.367 11.681 -20.362 1.00101.17 C ANISOU 3822 CD1 LEU A 507 13331 13099 12010 1126 1517 -2217 C ATOM 3823 CD2 LEU A 507 37.625 9.546 -19.316 1.00101.38 C ANISOU 3823 CD2 LEU A 507 13509 12657 12353 1308 1249 -2110 C ATOM 3824 N ASN A 508 41.765 9.880 -16.340 1.00107.59 N ANISOU 3824 N ASN A 508 13152 14473 13254 1766 1584 -1736 N ATOM 3825 CA ASN A 508 43.152 10.017 -15.916 1.00117.09 C ANISOU 3825 CA ASN A 508 14019 15970 14499 1924 1676 -1669 C ATOM 3826 C ASN A 508 44.072 9.960 -17.132 1.00126.55 C ANISOU 3826 C ASN A 508 15192 17243 15650 2126 1917 -1801 C ATOM 3827 O ASN A 508 43.618 9.900 -18.280 1.00138.11 O ANISOU 3827 O ASN A 508 16934 18545 16999 2131 2007 -1954 O ATOM 3828 CB ASN A 508 43.503 8.953 -14.881 1.00114.72 C ANISOU 3828 CB ASN A 508 13640 15604 14345 2132 1555 -1526 C ATOM 3829 CG ASN A 508 43.140 7.551 -15.339 1.00106.00 C ANISOU 3829 CG ASN A 508 12819 14134 13321 2359 1532 -1582 C ATOM 3830 OD1 ASN A 508 43.818 6.956 -16.175 1.00107.06 O ANISOU 3830 OD1 ASN A 508 12999 14208 13469 2621 1674 -1694 O ATOM 3831 ND2 ASN A 508 42.068 7.009 -14.771 1.00113.47 N ANISOU 3831 ND2 ASN A 508 13958 14823 14332 2264 1359 -1496 N ATOM 3832 N GLU A 509 45.380 9.946 -16.871 1.00148.71 N ANISOU 3832 N GLU A 509 21585 20193 14725 5662 -4416 -1020 N ATOM 3833 CA GLU A 509 46.357 10.062 -17.950 1.00147.08 C ANISOU 3833 CA GLU A 509 20894 19898 15093 5303 -4578 -918 C ATOM 3834 C GLU A 509 46.272 8.889 -18.918 1.00143.87 C ANISOU 3834 C GLU A 509 20224 19520 14922 5121 -3968 -644 C ATOM 3835 O GLU A 509 46.371 9.074 -20.136 1.00140.98 O ANISOU 3835 O GLU A 509 19491 19097 14978 4770 -3840 -603 O ATOM 3836 CB GLU A 509 47.768 10.182 -17.371 1.00150.74 C ANISOU 3836 CB GLU A 509 21274 20349 15651 5417 -5186 -891 C ATOM 3837 CG GLU A 509 48.880 10.268 -18.413 1.00149.78 C ANISOU 3837 CG GLU A 509 20614 20180 16117 5068 -5360 -757 C ATOM 3838 CD GLU A 509 48.804 11.520 -19.270 1.00148.26 C ANISOU 3838 CD GLU A 509 20178 19868 16284 4694 -5607 -910 C ATOM 3839 OE1 GLU A 509 48.175 12.512 -18.842 1.00149.02 O ANISOU 3839 OE1 GLU A 509 20546 19887 16190 4748 -5870 -1170 O ATOM 3840 OE2 GLU A 509 49.376 11.507 -20.380 1.00146.50 O ANISOU 3840 OE2 GLU A 509 19503 19632 16529 4357 -5538 -767 O ATOM 3841 N ASP A 510 46.082 7.676 -18.402 1.00144.56 N ANISOU 3841 N ASP A 510 20512 19684 14731 5361 -3597 -453 N ATOM 3842 CA ASP A 510 46.005 6.503 -19.268 1.00141.94 C ANISOU 3842 CA ASP A 510 19974 19348 14607 5218 -3049 -202 C ATOM 3843 C ASP A 510 44.829 6.608 -20.233 1.00138.02 C ANISOU 3843 C ASP A 510 19395 18817 14228 4953 -2571 -245 C ATOM 3844 O ASP A 510 45.002 6.566 -21.463 1.00135.20 O ANISOU 3844 O ASP A 510 18682 18405 14281 4645 -2412 -187 O ATOM 3845 CB ASP A 510 45.902 5.244 -18.410 1.00143.89 C ANISOU 3845 CB ASP A 510 20528 19654 14491 5539 -2773 2 C ATOM 3846 CG ASP A 510 47.051 5.118 -17.432 1.00147.97 C ANISOU 3846 CG ASP A 510 21147 20205 14871 5829 -3260 41 C ATOM 3847 OD1 ASP A 510 48.162 5.593 -17.753 1.00148.72 O ANISOU 3847 OD1 ASP A 510 20929 20277 15301 5718 -3702 7 O ATOM 3848 OD2 ASP A 510 46.845 4.544 -16.343 1.00150.66 O ANISOU 3848 OD2 ASP A 510 21873 20602 14767 6165 -3205 116 O ATOM 3849 N GLU A 511 43.617 6.744 -19.684 1.00138.05 N ANISOU 3849 N GLU A 511 19721 18867 13864 5083 -2337 -347 N ATOM 3850 CA GLU A 511 42.433 6.964 -20.508 1.00134.73 C ANISOU 3850 CA GLU A 511 19231 18423 13536 4853 -1935 -422 C ATOM 3851 C GLU A 511 42.674 8.071 -21.524 1.00132.62 C ANISOU 3851 C GLU A 511 18652 18065 13674 4530 -2206 -586 C ATOM 3852 O GLU A 511 42.362 7.919 -22.711 1.00129.38 O ANISOU 3852 O GLU A 511 17984 17600 13574 4240 -1901 -536 O ATOM 3853 CB GLU A 511 41.235 7.303 -19.620 1.00135.99 C ANISOU 3853 CB GLU A 511 19760 18678 13231 5075 -1803 -569 C ATOM 3854 CG GLU A 511 40.692 6.139 -18.804 1.00137.65 C ANISOU 3854 CG GLU A 511 20262 18990 13049 5327 -1380 -362 C ATOM 3855 CD GLU A 511 39.953 6.601 -17.562 1.00140.64 C ANISOU 3855 CD GLU A 511 21036 19513 12888 5660 -1438 -507 C ATOM 3856 OE1 GLU A 511 40.471 7.499 -16.866 1.00143.12 O ANISOU 3856 OE1 GLU A 511 21491 19842 13047 5849 -1976 -708 O ATOM 3857 OE2 GLU A 511 38.854 6.076 -17.284 1.00140.77 O ANISOU 3857 OE2 GLU A 511 21219 19634 12635 5735 -953 -419 O ATOM 3858 N ILE A 512 43.261 9.184 -21.076 1.00134.71 N ANISOU 3858 N ILE A 512 18942 18299 13942 4573 -2802 -774 N ATOM 3859 CA ILE A 512 43.506 10.309 -21.975 1.00133.23 C ANISOU 3859 CA ILE A 512 18483 18006 14134 4256 -3106 -915 C ATOM 3860 C ILE A 512 44.355 9.868 -23.161 1.00131.31 C ANISOU 3860 C ILE A 512 17799 17728 14364 3958 -3000 -711 C ATOM 3861 O ILE A 512 43.969 10.057 -24.319 1.00128.27 O ANISOU 3861 O ILE A 512 17189 17292 14257 3664 -2767 -708 O ATOM 3862 CB ILE A 512 44.158 11.480 -21.218 1.00136.50 C ANISOU 3862 CB ILE A 512 19005 18365 14494 4356 -3824 -1121 C ATOM 3863 CG1 ILE A 512 43.120 12.208 -20.363 1.00137.84 C ANISOU 3863 CG1 ILE A 512 19580 18551 14242 4601 -3922 -1392 C ATOM 3864 CG2 ILE A 512 44.786 12.452 -22.193 1.00135.57 C ANISOU 3864 CG2 ILE A 512 18537 18120 14853 3985 -4179 -1169 C ATOM 3865 CD1 ILE A 512 43.687 13.368 -19.559 1.00141.41 C ANISOU 3865 CD1 ILE A 512 20203 18923 14604 4738 -4660 -1630 C ATOM 3866 N GLN A 513 45.512 9.256 -22.894 1.00133.24 N ANISOU 3866 N GLN A 513 17918 18016 14692 4053 -3161 -538 N ATOM 3867 CA GLN A 513 46.411 8.865 -23.979 1.00131.99 C ANISOU 3867 CA GLN A 513 17320 17861 14969 3811 -3084 -349 C ATOM 3868 C GLN A 513 45.715 7.937 -24.965 1.00128.55 C ANISOU 3868 C GLN A 513 16791 17426 14628 3684 -2440 -217 C ATOM 3869 O GLN A 513 45.729 8.179 -26.183 1.00126.15 O ANISOU 3869 O GLN A 513 16185 17089 14656 3384 -2307 -192 O ATOM 3870 CB GLN A 513 47.664 8.202 -23.409 1.00134.96 C ANISOU 3870 CB GLN A 513 17609 18307 15361 4007 -3314 -186 C ATOM 3871 CG GLN A 513 48.568 9.147 -22.637 1.00138.53 C ANISOU 3871 CG GLN A 513 18055 18748 15830 4071 -4017 -301 C ATOM 3872 CD GLN A 513 49.842 8.475 -22.167 1.00141.52 C ANISOU 3872 CD GLN A 513 18296 19207 16267 4254 -4248 -134 C ATOM 3873 OE1 GLN A 513 49.884 7.258 -21.997 1.00141.54 O ANISOU 3873 OE1 GLN A 513 18377 19268 16135 4456 -3907 34 O ATOM 3874 NE2 GLN A 513 50.890 9.265 -21.963 1.00144.28 N ANISOU 3874 NE2 GLN A 513 18437 19552 16833 4180 -4848 -177 N ATOM 3875 N LYS A 514 45.084 6.875 -24.454 1.00128.53 N ANISOU 3875 N LYS A 514 17055 17450 14329 3906 -2044 -127 N ATOM 3876 CA LYS A 514 44.399 5.944 -25.345 1.00125.63 C ANISOU 3876 CA LYS A 514 16624 17055 14054 3789 -1461 -6 C ATOM 3877 C LYS A 514 43.376 6.664 -26.212 1.00122.60 C ANISOU 3877 C LYS A 514 16179 16614 13788 3523 -1284 -157 C ATOM 3878 O LYS A 514 43.310 6.443 -27.427 1.00120.07 O ANISOU 3878 O LYS A 514 15608 16256 13757 3287 -1029 -97 O ATOM 3879 CB LYS A 514 43.722 4.838 -24.541 1.00126.50 C ANISOU 3879 CB LYS A 514 17077 17181 13806 4046 -1101 105 C ATOM 3880 CG LYS A 514 42.687 4.071 -25.342 1.00123.68 C ANISOU 3880 CG LYS A 514 16722 16765 13506 3904 -526 178 C ATOM 3881 CD LYS A 514 41.959 3.044 -24.498 1.00124.97 C ANISOU 3881 CD LYS A 514 17227 16935 13319 4124 -184 308 C ATOM 3882 CE LYS A 514 40.771 2.469 -25.253 1.00122.39 C ANISOU 3882 CE LYS A 514 16904 16540 13057 3946 342 348 C ATOM 3883 NZ LYS A 514 41.167 1.977 -26.602 1.00120.06 N ANISOU 3883 NZ LYS A 514 16308 16155 13156 3732 511 427 N ATOM 3884 N MET A 515 42.588 7.553 -25.610 1.00123.03 N ANISOU 3884 N MET A 515 16465 16667 13614 3578 -1436 -365 N ATOM 3885 CA MET A 515 41.540 8.216 -26.374 1.00120.37 C ANISOU 3885 CA MET A 515 16093 16277 13365 3361 -1269 -520 C ATOM 3886 C MET A 515 42.115 9.231 -27.353 1.00119.27 C ANISOU 3886 C MET A 515 15646 16070 13603 3062 -1575 -589 C ATOM 3887 O MET A 515 41.473 9.546 -28.361 1.00120.44 O ANISOU 3887 O MET A 515 15672 16161 13928 2827 -1380 -647 O ATOM 3888 CB MET A 515 40.541 8.868 -25.423 1.00121.53 C ANISOU 3888 CB MET A 515 16575 16458 13143 3547 -1346 -730 C ATOM 3889 CG MET A 515 39.819 7.857 -24.543 1.00122.65 C ANISOU 3889 CG MET A 515 17007 16689 12905 3811 -964 -631 C ATOM 3890 SD MET A 515 38.675 8.599 -23.370 1.00124.64 S ANISOU 3890 SD MET A 515 17638 17041 12677 4080 -1024 -866 S ATOM 3891 CE MET A 515 38.163 7.148 -22.453 1.00126.37 C ANISOU 3891 CE MET A 515 18123 17378 12513 4344 -540 -627 C ATOM 3892 N VAL A 516 43.315 9.746 -27.086 1.00121.48 N ANISOU 3892 N VAL A 516 15790 16352 14014 3056 -2059 -570 N ATOM 3893 CA VAL A 516 43.989 10.575 -28.077 1.00120.81 C ANISOU 3893 CA VAL A 516 15366 16215 14323 2739 -2317 -565 C ATOM 3894 C VAL A 516 44.354 9.738 -29.294 1.00118.75 C ANISOU 3894 C VAL A 516 14783 15990 14349 2562 -1935 -355 C ATOM 3895 O VAL A 516 44.084 10.124 -30.441 1.00116.52 O ANISOU 3895 O VAL A 516 14308 15662 14302 2290 -1805 -364 O ATOM 3896 CB VAL A 516 45.225 11.257 -27.464 1.00124.15 C ANISOU 3896 CB VAL A 516 15694 16639 14838 2765 -2932 -569 C ATOM 3897 CG1 VAL A 516 46.021 11.980 -28.541 1.00123.84 C ANISOU 3897 CG1 VAL A 516 15250 16565 15238 2407 -3156 -494 C ATOM 3898 CG2 VAL A 516 44.809 12.233 -26.379 1.00126.23 C ANISOU 3898 CG2 VAL A 516 16296 16839 14828 2930 -3354 -819 C ATOM 3899 N ARG A 517 44.947 8.564 -29.063 1.00119.65 N ANISOU 3899 N ARG A 517 14855 16181 14427 2737 -1751 -171 N ATOM 3900 CA ARG A 517 45.293 7.697 -30.185 1.00118.04 C ANISOU 3900 CA ARG A 517 14374 16012 14463 2624 -1386 11 C ATOM 3901 C ARG A 517 44.055 7.324 -30.991 1.00114.80 C ANISOU 3901 C ARG A 517 14048 15534 14035 2513 -899 -32 C ATOM 3902 O ARG A 517 44.055 7.406 -32.227 1.00112.86 O ANISOU 3902 O ARG A 517 13564 15277 14041 2284 -730 4 O ATOM 3903 CB ARG A 517 46.012 6.445 -29.685 1.00119.80 C ANISOU 3903 CB ARG A 517 14608 16305 14605 2886 -1274 192 C ATOM 3904 CG ARG A 517 47.393 6.723 -29.118 1.00123.07 C ANISOU 3904 CG ARG A 517 14843 16804 15112 2973 -1745 262 C ATOM 3905 CD ARG A 517 48.221 5.455 -29.026 1.00124.51 C ANISOU 3905 CD ARG A 517 14930 17066 15312 3191 -1595 461 C ATOM 3906 NE ARG A 517 47.720 4.544 -28.004 1.00125.39 N ANISOU 3906 NE ARG A 517 15433 17139 15070 3498 -1429 485 N ATOM 3907 CZ ARG A 517 48.126 4.556 -26.739 1.00128.37 C ANISOU 3907 CZ ARG A 517 16014 17544 15216 3751 -1751 475 C ATOM 3908 NH1 ARG A 517 49.038 5.434 -26.347 1.00130.72 N ANISOU 3908 NH1 ARG A 517 16153 17894 15619 3729 -2281 424 N ATOM 3909 NH2 ARG A 517 47.622 3.693 -25.869 1.00129.25 N ANISOU 3909 NH2 ARG A 517 16492 17625 14992 4019 -1557 524 N ATOM 3910 N ASP A 518 42.980 6.926 -30.304 1.00114.42 N ANISOU 3910 N ASP A 518 14336 15451 13688 2673 -674 -106 N ATOM 3911 CA ASP A 518 41.746 6.594 -31.007 1.00111.67 C ANISOU 3911 CA ASP A 518 14060 15038 13331 2561 -237 -154 C ATOM 3912 C ASP A 518 41.196 7.794 -31.763 1.00109.85 C ANISOU 3912 C ASP A 518 13738 14754 13247 2305 -353 -326 C ATOM 3913 O ASP A 518 40.626 7.635 -32.848 1.00107.43 O ANISOU 3913 O ASP A 518 13328 14399 13092 2125 -63 -332 O ATOM 3914 CB ASP A 518 40.704 6.055 -30.027 1.00112.20 C ANISOU 3914 CB ASP A 518 14478 15103 13049 2769 -6 -187 C ATOM 3915 CG ASP A 518 41.162 4.786 -29.331 1.00114.05 C ANISOU 3915 CG ASP A 518 14837 15363 13133 3012 140 9 C ATOM 3916 OD1 ASP A 518 42.253 4.282 -29.670 1.00114.72 O ANISOU 3916 OD1 ASP A 518 14729 15464 13396 3032 78 152 O ATOM 3917 OD2 ASP A 518 40.429 4.286 -28.451 1.00115.05 O ANISOU 3917 OD2 ASP A 518 15252 15499 12961 3188 323 29 O ATOM 3918 N ALA A 519 41.363 9.000 -31.217 1.00111.19 N ANISOU 3918 N ALA A 519 13959 14915 13372 2295 -798 -472 N ATOM 3919 CA ALA A 519 40.920 10.190 -31.934 1.00109.80 C ANISOU 3919 CA ALA A 519 13708 14663 13348 2054 -959 -628 C ATOM 3920 C ALA A 519 41.694 10.366 -33.230 1.00108.79 C ANISOU 3920 C ALA A 519 13224 14529 13584 1778 -975 -503 C ATOM 3921 O ALA A 519 41.116 10.718 -34.266 1.00112.11 O ANISOU 3921 O ALA A 519 13561 14890 14147 1567 -826 -554 O ATOM 3922 CB ALA A 519 41.073 11.425 -31.054 1.00111.97 C ANISOU 3922 CB ALA A 519 14125 14903 13514 2114 -1491 -804 C ATOM 3923 N GLU A 520 43.006 10.124 -33.192 1.00110.58 N ANISOU 3923 N GLU A 520 13229 14831 13955 1788 -1151 -333 N ATOM 3924 CA GLU A 520 43.805 10.207 -34.410 1.00110.08 C ANISOU 3924 CA GLU A 520 12796 14810 14220 1549 -1123 -181 C ATOM 3925 C GLU A 520 43.363 9.166 -35.430 1.00107.71 C ANISOU 3925 C GLU A 520 12429 14524 13972 1525 -591 -96 C ATOM 3926 O GLU A 520 43.198 9.472 -36.618 1.00106.08 O ANISOU 3926 O GLU A 520 12058 14299 13950 1301 -464 -83 O ATOM 3927 CB GLU A 520 45.284 10.036 -34.079 1.00112.87 C ANISOU 3927 CB GLU A 520 12906 15277 14702 1605 -1388 -9 C ATOM 3928 CG GLU A 520 45.878 11.189 -33.300 1.00126.96 C ANISOU 3928 CG GLU A 520 14690 17030 16519 1560 -1981 -81 C ATOM 3929 CD GLU A 520 47.312 10.933 -32.890 1.00146.16 C ANISOU 3929 CD GLU A 520 16874 19584 19077 1635 -2247 89 C ATOM 3930 OE1 GLU A 520 47.589 9.854 -32.325 1.00157.39 O ANISOU 3930 OE1 GLU A 520 18363 21084 20354 1905 -2084 169 O ATOM 3931 OE2 GLU A 520 48.163 11.809 -33.142 1.00150.63 O ANISOU 3931 OE2 GLU A 520 17171 20165 19898 1418 -2628 152 O ATOM 3932 N ALA A 521 43.163 7.925 -34.981 1.00107.72 N ANISOU 3932 N ALA A 521 12577 14545 13807 1759 -291 -36 N ATOM 3933 CA ALA A 521 42.696 6.881 -35.889 1.00105.77 C ANISOU 3933 CA ALA A 521 12309 14275 13605 1752 185 29 C ATOM 3934 C ALA A 521 41.374 7.271 -36.542 1.00103.18 C ANISOU 3934 C ALA A 521 12095 13842 13266 1589 380 -127 C ATOM 3935 O ALA A 521 41.212 7.155 -37.765 1.00101.52 O ANISOU 3935 O ALA A 521 11741 13612 13218 1433 591 -106 O ATOM 3936 CB ALA A 521 42.558 5.558 -35.138 1.00106.55 C ANISOU 3936 CB ALA A 521 12611 14365 13507 2024 428 107 C ATOM 3937 N ASN A 522 40.416 7.742 -35.737 1.00103.03 N ANISOU 3937 N ASN A 522 12334 13766 13045 1644 306 -291 N ATOM 3938 CA ASN A 522 39.160 8.236 -36.288 1.00100.89 C ANISOU 3938 CA ASN A 522 12155 13410 12769 1503 442 -458 C ATOM 3939 C ASN A 522 39.393 9.376 -37.268 1.00100.09 C ANISOU 3939 C ASN A 522 11861 13279 12889 1242 222 -507 C ATOM 3940 O ASN A 522 38.641 9.524 -38.236 1.00105.23 O ANISOU 3940 O ASN A 522 12491 13867 13626 1089 405 -577 O ATOM 3941 CB ASN A 522 38.229 8.685 -35.158 1.00101.52 C ANISOU 3941 CB ASN A 522 12515 13474 12583 1639 346 -628 C ATOM 3942 CG ASN A 522 37.637 7.518 -34.378 1.00102.02 C ANISOU 3942 CG ASN A 522 12787 13559 12417 1853 671 -571 C ATOM 3943 OD1 ASN A 522 37.930 7.329 -33.197 1.00104.12 O ANISOU 3943 OD1 ASN A 522 13206 13883 12471 2066 551 -537 O ATOM 3944 ND2 ASN A 522 36.785 6.739 -35.035 1.00100.34 N ANISOU 3944 ND2 ASN A 522 12588 13291 12244 1789 1071 -554 N ATOM 3945 N ALA A 523 40.431 10.181 -37.046 1.00101.85 N ANISOU 3945 N ALA A 523 11944 13540 13215 1178 -179 -458 N ATOM 3946 CA ALA A 523 40.719 11.273 -37.970 1.00101.53 C ANISOU 3946 CA ALA A 523 11716 13462 13398 904 -402 -463 C ATOM 3947 C ALA A 523 41.155 10.743 -39.330 1.00100.47 C ANISOU 3947 C ALA A 523 11322 13385 13467 763 -121 -300 C ATOM 3948 O ALA A 523 40.673 11.208 -40.372 1.00 98.93 O ANISOU 3948 O ALA A 523 11078 13133 13378 569 -42 -341 O ATOM 3949 CB ALA A 523 41.784 12.196 -37.384 1.00104.14 C ANISOU 3949 CB ALA A 523 11941 13812 13816 850 -912 -422 C ATOM 3950 N GLU A 524 42.069 9.767 -39.346 1.00116.80 N ANISOU 3950 N GLU A 524 13233 15570 15576 881 27 -118 N ATOM 3951 CA GLU A 524 42.468 9.185 -40.625 1.00114.07 C ANISOU 3951 CA GLU A 524 12657 15298 15387 802 318 24 C ATOM 3952 C GLU A 524 41.284 8.515 -41.309 1.00106.08 C ANISOU 3952 C GLU A 524 11809 14191 14304 817 717 -77 C ATOM 3953 O GLU A 524 41.100 8.646 -42.528 1.00110.34 O ANISOU 3953 O GLU A 524 12244 14724 14956 664 868 -66 O ATOM 3954 CB GLU A 524 43.613 8.190 -40.427 1.00117.11 C ANISOU 3954 CB GLU A 524 12866 15827 15804 985 403 212 C ATOM 3955 CG GLU A 524 44.259 7.703 -41.724 1.00120.56 C ANISOU 3955 CG GLU A 524 13022 16385 16401 933 652 368 C ATOM 3956 CD GLU A 524 45.027 8.793 -42.456 1.00129.77 C ANISOU 3956 CD GLU A 524 13876 17653 17777 669 427 481 C ATOM 3957 OE1 GLU A 524 45.395 9.801 -41.816 1.00130.63 O ANISOU 3957 OE1 GLU A 524 13941 17747 17944 550 23 479 O ATOM 3958 OE2 GLU A 524 45.264 8.641 -43.673 1.00135.50 O ANISOU 3958 OE2 GLU A 524 14410 18468 18605 581 649 579 O ATOM 3959 N ALA A 525 40.450 7.815 -40.536 1.00 97.71 N ANISOU 3959 N ALA A 525 11010 13057 13057 993 881 -170 N ATOM 3960 CA ALA A 525 39.268 7.186 -41.114 1.00 95.65 C ANISOU 3960 CA ALA A 525 10899 12693 12751 987 1232 -266 C ATOM 3961 C ALA A 525 38.357 8.221 -41.761 1.00 94.01 C ANISOU 3961 C ALA A 525 10728 12401 12590 780 1159 -428 C ATOM 3962 O ALA A 525 37.826 8.002 -42.858 1.00 92.48 O ANISOU 3962 O ALA A 525 10511 12156 12470 683 1380 -462 O ATOM 3963 CB ALA A 525 38.518 6.397 -40.043 1.00 95.83 C ANISOU 3963 CB ALA A 525 11182 12659 12570 1181 1383 -315 C ATOM 3964 N ASP A 526 38.170 9.366 -41.099 1.00 94.51 N ANISOU 3964 N ASP A 526 10864 12441 12605 728 828 -538 N ATOM 3965 CA ASP A 526 37.309 10.404 -41.655 1.00 93.23 C ANISOU 3965 CA ASP A 526 10756 12185 12482 555 719 -702 C ATOM 3966 C ASP A 526 37.927 11.032 -42.897 1.00 93.05 C ANISOU 3966 C ASP A 526 10515 12175 12665 327 629 -608 C ATOM 3967 O ASP A 526 37.203 11.413 -43.828 1.00 91.59 O ANISOU 3967 O ASP A 526 10353 11913 12533 189 702 -696 O ATOM 3968 CB ASP A 526 37.010 11.468 -40.598 1.00 94.23 C ANISOU 3968 CB ASP A 526 11036 12272 12495 592 357 -855 C ATOM 3969 CG ASP A 526 35.878 11.062 -39.663 1.00100.91 C ANISOU 3969 CG ASP A 526 12128 13102 13113 784 512 -1005 C ATOM 3970 OD1 ASP A 526 34.701 11.227 -40.047 1.00110.24 O ANISOU 3970 OD1 ASP A 526 13399 14219 14269 742 650 -1159 O ATOM 3971 OD2 ASP A 526 36.158 10.582 -38.545 1.00100.72 O ANISOU 3971 OD2 ASP A 526 12199 13140 12931 980 497 -962 O ATOM 3972 N ARG A 527 39.256 11.143 -42.940 1.00 94.76 N ANISOU 3972 N ARG A 527 10511 12498 12995 284 474 -418 N ATOM 3973 CA ARG A 527 39.906 11.556 -44.179 1.00 94.95 C ANISOU 3973 CA ARG A 527 10296 12577 13204 76 466 -276 C ATOM 3974 C ARG A 527 39.565 10.597 -45.308 1.00 93.47 C ANISOU 3974 C ARG A 527 10079 12411 13025 105 887 -247 C ATOM 3975 O ARG A 527 39.223 11.022 -46.419 1.00 92.54 O ANISOU 3975 O ARG A 527 9929 12258 12975 -55 947 -262 O ATOM 3976 CB ARG A 527 41.417 11.635 -43.990 1.00104.88 C ANISOU 3976 CB ARG A 527 11279 13988 14584 52 284 -52 C ATOM 3977 CG ARG A 527 41.883 12.850 -43.226 1.00114.71 C ANISOU 3977 CG ARG A 527 12504 15191 15889 -65 -209 -60 C ATOM 3978 CD ARG A 527 43.400 12.909 -43.178 1.00121.05 C ANISOU 3978 CD ARG A 527 12980 16158 16855 -123 -383 184 C ATOM 3979 NE ARG A 527 43.869 13.918 -42.235 1.00133.80 N ANISOU 3979 NE ARG A 527 14602 17713 18522 -199 -889 162 N ATOM 3980 CZ ARG A 527 43.971 13.718 -40.926 1.00152.42 C ANISOU 3980 CZ ARG A 527 17105 20057 20750 7 -1074 77 C ATOM 3981 NH1 ARG A 527 44.406 14.688 -40.134 1.00162.36 N ANISOU 3981 NH1 ARG A 527 18382 21246 22059 -64 -1570 43 N ATOM 3982 NH2 ARG A 527 43.631 12.545 -40.409 1.00159.00 N ANISOU 3982 NH2 ARG A 527 18082 20934 21399 285 -775 30 N ATOM 3983 N LYS A 528 39.642 9.292 -45.037 1.00 93.44 N ANISOU 3983 N LYS A 528 10111 12449 12945 319 1165 -209 N ATOM 3984 CA LYS A 528 39.296 8.321 -46.069 1.00 92.31 C ANISOU 3984 CA LYS A 528 9975 12295 12805 370 1537 -205 C ATOM 3985 C LYS A 528 37.840 8.468 -46.499 1.00 90.20 C ANISOU 3985 C LYS A 528 9915 11866 12490 298 1648 -409 C ATOM 3986 O LYS A 528 37.518 8.316 -47.684 1.00 89.27 O ANISOU 3986 O LYS A 528 9779 11723 12418 228 1822 -430 O ATOM 3987 CB LYS A 528 39.578 6.905 -45.574 1.00 92.94 C ANISOU 3987 CB LYS A 528 10101 12401 12811 621 1769 -141 C ATOM 3988 CG LYS A 528 41.027 6.679 -45.183 1.00105.85 C ANISOU 3988 CG LYS A 528 11516 14208 14496 725 1664 55 C ATOM 3989 CD LYS A 528 41.339 5.212 -44.954 1.00110.54 C ANISOU 3989 CD LYS A 528 12155 14817 15029 988 1914 123 C ATOM 3990 CE LYS A 528 42.830 5.023 -44.753 1.00113.81 C ANISOU 3990 CE LYS A 528 12304 15427 15512 1099 1812 318 C ATOM 3991 NZ LYS A 528 43.584 5.586 -45.909 1.00116.98 N ANISOU 3991 NZ LYS A 528 12401 15992 16053 954 1807 436 N ATOM 3992 N CYS A 529 36.945 8.776 -45.555 1.00 89.64 N ANISOU 3992 N CYS A 529 10038 11700 12323 327 1546 -566 N ATOM 3993 CA CYS A 529 35.545 8.995 -45.915 1.00 87.93 C ANISOU 3993 CA CYS A 529 9983 11352 12074 261 1629 -766 C ATOM 3994 C CYS A 529 35.400 10.178 -46.866 1.00 87.37 C ANISOU 3994 C CYS A 529 9855 11245 12096 50 1448 -815 C ATOM 3995 O CYS A 529 34.698 10.094 -47.884 1.00 86.14 O ANISOU 3995 O CYS A 529 9736 11020 11972 -22 1596 -895 O ATOM 3996 CB CYS A 529 34.702 9.211 -44.658 1.00 93.43 C ANISOU 3996 CB CYS A 529 10865 12000 12635 351 1540 -912 C ATOM 3997 SG CYS A 529 34.522 7.756 -43.615 1.00109.70 S ANISOU 3997 SG CYS A 529 13049 14072 14560 582 1807 -856 S ATOM 3998 N GLU A 530 36.063 11.293 -46.547 1.00 88.50 N ANISOU 3998 N GLU A 530 9920 11419 12286 -55 1106 -763 N ATOM 3999 CA GLU A 530 36.062 12.447 -47.442 1.00 88.41 C ANISOU 3999 CA GLU A 530 9856 11361 12376 -275 905 -766 C ATOM 4000 C GLU A 530 36.553 12.059 -48.833 1.00 88.31 C ANISOU 4000 C GLU A 530 9688 11422 12445 -356 1123 -616 C ATOM 4001 O GLU A 530 35.951 12.441 -49.851 1.00 89.42 O ANISOU 4001 O GLU A 530 9876 11491 12610 -471 1160 -681 O ATOM 4002 CB GLU A 530 36.933 13.551 -46.838 1.00 90.24 C ANISOU 4002 CB GLU A 530 10005 11611 12673 -381 494 -682 C ATOM 4003 CG GLU A 530 36.685 14.955 -47.366 1.00 91.56 C ANISOU 4003 CG GLU A 530 10206 11661 12923 -602 183 -733 C ATOM 4004 CD GLU A 530 37.395 16.018 -46.538 1.00105.26 C ANISOU 4004 CD GLU A 530 11913 13362 14718 -688 -275 -691 C ATOM 4005 OE1 GLU A 530 37.724 15.737 -45.367 1.00111.21 O ANISOU 4005 OE1 GLU A 530 12696 14160 15400 -534 -368 -709 O ATOM 4006 OE2 GLU A 530 37.631 17.130 -47.056 1.00110.49 O ANISOU 4006 OE2 GLU A 530 12540 13942 15500 -911 -559 -636 O ATOM 4007 N GLU A 531 37.637 11.277 -48.889 1.00 97.95 N ANISOU 4007 N GLU A 531 10730 12795 13693 -272 1269 -421 N ATOM 4008 CA GLU A 531 38.127 10.750 -50.159 1.00 98.14 C ANISOU 4008 CA GLU A 531 10610 12922 13756 -283 1519 -286 C ATOM 4009 C GLU A 531 37.027 10.020 -50.919 1.00 87.94 C ANISOU 4009 C GLU A 531 9492 11522 12399 -213 1800 -446 C ATOM 4010 O GLU A 531 36.826 10.252 -52.115 1.00 87.61 O ANISOU 4010 O GLU A 531 9440 11474 12372 -306 1876 -444 O ATOM 4011 CB GLU A 531 39.308 9.808 -49.925 1.00112.14 C ANISOU 4011 CB GLU A 531 12195 14872 15539 -121 1664 -98 C ATOM 4012 CG GLU A 531 40.543 10.445 -49.320 1.00127.42 C ANISOU 4012 CG GLU A 531 13902 16944 17568 -195 1393 90 C ATOM 4013 CD GLU A 531 41.655 9.434 -49.094 1.00143.09 C ANISOU 4013 CD GLU A 531 15693 19113 19560 0 1548 258 C ATOM 4014 OE1 GLU A 531 41.531 8.296 -49.593 1.00150.60 O ANISOU 4014 OE1 GLU A 531 16686 20087 20447 183 1871 242 O ATOM 4015 OE2 GLU A 531 42.648 9.773 -48.416 1.00147.38 O ANISOU 4015 OE2 GLU A 531 16050 19769 20179 -19 1325 398 O ATOM 4016 N LEU A 532 36.307 9.123 -50.238 1.00 87.06 N ANISOU 4016 N LEU A 532 9541 11322 12215 -52 1948 -578 N ATOM 4017 CA LEU A 532 35.257 8.363 -50.912 1.00 85.70 C ANISOU 4017 CA LEU A 532 9523 11031 12010 2 2194 -727 C ATOM 4018 C LEU A 532 34.179 9.281 -51.469 1.00 84.45 C ANISOU 4018 C LEU A 532 9473 10749 11863 -154 2075 -898 C ATOM 4019 O LEU A 532 33.653 9.040 -52.562 1.00 83.78 O ANISOU 4019 O LEU A 532 9442 10607 11782 -178 2211 -969 O ATOM 4020 CB LEU A 532 34.644 7.339 -49.960 1.00 85.35 C ANISOU 4020 CB LEU A 532 9623 10902 11905 161 2342 -811 C ATOM 4021 CG LEU A 532 33.398 6.602 -50.463 1.00 84.19 C ANISOU 4021 CG LEU A 532 9638 10599 11751 183 2551 -978 C ATOM 4022 CD1 LEU A 532 33.668 5.901 -51.782 1.00 85.45 C ANISOU 4022 CD1 LEU A 532 9774 10757 11935 227 2746 -944 C ATOM 4023 CD2 LEU A 532 32.914 5.605 -49.429 1.00 84.38 C ANISOU 4023 CD2 LEU A 532 9782 10551 11727 314 2691 -1004 C ATOM 4024 N VAL A 533 33.827 10.334 -50.733 1.00 84.30 N ANISOU 4024 N VAL A 533 9502 10685 11844 -241 1803 -980 N ATOM 4025 CA VAL A 533 32.837 11.278 -51.248 1.00 83.36 C ANISOU 4025 CA VAL A 533 9488 10448 11739 -370 1655 -1148 C ATOM 4026 C VAL A 533 33.331 11.904 -52.546 1.00 83.77 C ANISOU 4026 C VAL A 533 9454 10529 11844 -522 1599 -1037 C ATOM 4027 O VAL A 533 32.627 11.907 -53.569 1.00 82.99 O ANISOU 4027 O VAL A 533 9434 10356 11740 -562 1680 -1134 O ATOM 4028 CB VAL A 533 32.508 12.344 -50.189 1.00 83.60 C ANISOU 4028 CB VAL A 533 9589 10427 11748 -403 1341 -1254 C ATOM 4029 CG1 VAL A 533 31.644 13.429 -50.788 1.00 82.99 C ANISOU 4029 CG1 VAL A 533 9610 10229 11695 -527 1145 -1411 C ATOM 4030 CG2 VAL A 533 31.802 11.704 -49.010 1.00 83.31 C ANISOU 4030 CG2 VAL A 533 9658 10374 11620 -238 1444 -1377 C ATOM 4031 N GLN A 534 34.563 12.421 -52.534 1.00 85.26 N ANISOU 4031 N GLN A 534 9474 10837 12084 -609 1460 -820 N ATOM 4032 CA GLN A 534 35.083 13.066 -53.737 1.00 86.09 C ANISOU 4032 CA GLN A 534 9482 10994 12233 -772 1414 -671 C ATOM 4033 C GLN A 534 35.159 12.087 -54.907 1.00 85.97 C ANISOU 4033 C GLN A 534 9442 11055 12169 -680 1752 -625 C ATOM 4034 O GLN A 534 34.787 12.427 -56.038 1.00 85.80 O ANISOU 4034 O GLN A 534 9479 10997 12125 -760 1777 -646 O ATOM 4035 CB GLN A 534 36.452 13.677 -53.454 1.00 88.15 C ANISOU 4035 CB GLN A 534 9522 11393 12578 -890 1228 -413 C ATOM 4036 CG GLN A 534 36.726 14.938 -54.252 1.00103.57 C ANISOU 4036 CG GLN A 534 11426 13325 14601 -1142 1001 -287 C ATOM 4037 CD GLN A 534 38.166 15.396 -54.150 1.00126.51 C ANISOU 4037 CD GLN A 534 14058 16394 17615 -1282 865 16 C ATOM 4038 OE1 GLN A 534 38.956 14.833 -53.392 1.00134.83 O ANISOU 4038 OE1 GLN A 534 14961 17575 18694 -1177 905 108 O ATOM 4039 NE2 GLN A 534 38.517 16.420 -54.920 1.00136.04 N ANISOU 4039 NE2 GLN A 534 15196 17599 18895 -1526 697 185 N ATOM 4040 N THR A 535 35.625 10.863 -54.651 1.00 86.26 N ANISOU 4040 N THR A 535 9415 11184 12174 -491 1998 -573 N ATOM 4041 CA THR A 535 35.687 9.854 -55.704 1.00 86.41 C ANISOU 4041 CA THR A 535 9441 11257 12132 -359 2303 -559 C ATOM 4042 C THR A 535 34.305 9.563 -56.271 1.00 84.81 C ANISOU 4042 C THR A 535 9467 10866 11891 -336 2382 -806 C ATOM 4043 O THR A 535 34.151 9.391 -57.485 1.00 84.99 O ANISOU 4043 O THR A 535 9536 10893 11862 -322 2503 -822 O ATOM 4044 CB THR A 535 36.326 8.574 -55.167 1.00 87.09 C ANISOU 4044 CB THR A 535 9461 11431 12199 -137 2512 -492 C ATOM 4045 OG1 THR A 535 37.686 8.836 -54.807 1.00 88.91 O ANISOU 4045 OG1 THR A 535 9443 11866 12474 -151 2441 -252 O ATOM 4046 CG2 THR A 535 36.289 7.479 -56.214 1.00 87.40 C ANISOU 4046 CG2 THR A 535 9554 11486 12167 34 2803 -522 C ATOM 4047 N ARG A 536 33.287 9.506 -55.409 1.00 83.50 N ANISOU 4047 N ARG A 536 9439 10545 11742 -325 2313 -999 N ATOM 4048 CA ARG A 536 31.923 9.310 -55.892 1.00 82.22 C ANISOU 4048 CA ARG A 536 9459 10211 11572 -325 2358 -1234 C ATOM 4049 C ARG A 536 31.507 10.446 -56.816 1.00 82.01 C ANISOU 4049 C ARG A 536 9481 10135 11544 -482 2181 -1284 C ATOM 4050 O ARG A 536 30.855 10.217 -57.845 1.00 81.67 O ANISOU 4050 O ARG A 536 9544 10015 11472 -469 2260 -1397 O ATOM 4051 CB ARG A 536 30.957 9.186 -54.711 1.00 81.29 C ANISOU 4051 CB ARG A 536 9431 9979 11474 -298 2310 -1400 C ATOM 4052 CG ARG A 536 29.510 8.929 -55.114 1.00 80.27 C ANISOU 4052 CG ARG A 536 9447 9687 11363 -303 2360 -1638 C ATOM 4053 CD ARG A 536 28.592 8.689 -53.919 1.00 79.79 C ANISOU 4053 CD ARG A 536 9439 9560 11318 -265 2367 -1769 C ATOM 4054 NE ARG A 536 28.876 7.429 -53.240 1.00 80.29 N ANISOU 4054 NE ARG A 536 9500 9634 11372 -140 2581 -1689 N ATOM 4055 CZ ARG A 536 29.426 7.338 -52.036 1.00 80.82 C ANISOU 4055 CZ ARG A 536 9526 9781 11400 -75 2564 -1583 C ATOM 4056 NH1 ARG A 536 29.743 8.440 -51.372 1.00 80.95 N ANISOU 4056 NH1 ARG A 536 9499 9871 11387 -124 2332 -1561 N ATOM 4057 NH2 ARG A 536 29.653 6.150 -51.495 1.00 81.43 N ANISOU 4057 NH2 ARG A 536 9626 9849 11466 44 2757 -1503 N ATOM 4058 N ASN A 537 31.895 11.680 -56.480 1.00 82.45 N ANISOU 4058 N ASN A 537 9475 10220 11631 -628 1919 -1199 N ATOM 4059 CA ASN A 537 31.607 12.796 -57.376 1.00 82.60 C ANISOU 4059 CA ASN A 537 9553 10181 11651 -785 1731 -1211 C ATOM 4060 C ASN A 537 32.291 12.609 -58.726 1.00 83.71 C ANISOU 4060 C ASN A 537 9637 10436 11732 -796 1885 -1041 C ATOM 4061 O ASN A 537 31.666 12.780 -59.782 1.00 83.52 O ANISOU 4061 O ASN A 537 9737 10339 11657 -818 1893 -1130 O ATOM 4062 CB ASN A 537 32.026 14.116 -56.732 1.00 83.31 C ANISOU 4062 CB ASN A 537 9594 10261 11800 -944 1397 -1124 C ATOM 4063 CG ASN A 537 30.937 14.710 -55.869 1.00 82.34 C ANISOU 4063 CG ASN A 537 9610 9980 11695 -940 1177 -1368 C ATOM 4064 OD1 ASN A 537 30.091 15.466 -56.348 1.00 81.96 O ANISOU 4064 OD1 ASN A 537 9691 9803 11649 -1006 1011 -1512 O ATOM 4065 ND2 ASN A 537 30.949 14.370 -54.588 1.00 82.15 N ANISOU 4065 ND2 ASN A 537 9565 9978 11670 -841 1176 -1416 N ATOM 4066 N GLN A 538 33.579 12.249 -58.714 1.00 85.12 N ANISOU 4066 N GLN A 538 9625 10811 11904 -764 2012 -796 N ATOM 4067 CA GLN A 538 34.279 11.998 -59.972 1.00 86.56 C ANISOU 4067 CA GLN A 538 9734 11152 12004 -736 2200 -625 C ATOM 4068 C GLN A 538 33.564 10.936 -60.793 1.00 85.94 C ANISOU 4068 C GLN A 538 9817 11006 11830 -552 2435 -805 C ATOM 4069 O GLN A 538 33.430 11.068 -62.015 1.00 86.59 O ANISOU 4069 O GLN A 538 9976 11107 11816 -552 2493 -797 O ATOM 4070 CB GLN A 538 35.721 11.575 -59.704 1.00 88.32 C ANISOU 4070 CB GLN A 538 9701 11618 12239 -675 2334 -361 C ATOM 4071 CG GLN A 538 36.541 12.610 -58.967 1.00105.77 C ANISOU 4071 CG GLN A 538 11726 13900 14561 -872 2081 -161 C ATOM 4072 CD GLN A 538 37.918 12.101 -58.606 1.00131.25 C ANISOU 4072 CD GLN A 538 14676 17373 17820 -793 2205 80 C ATOM 4073 OE1 GLN A 538 38.504 11.293 -59.327 1.00134.87 O ANISOU 4073 OE1 GLN A 538 15035 18012 18196 -636 2484 182 O ATOM 4074 NE2 GLN A 538 38.440 12.562 -57.477 1.00144.42 N ANISOU 4074 NE2 GLN A 538 16221 19052 19601 -881 1985 159 N ATOM 4075 N GLY A 539 33.082 9.884 -60.133 1.00 84.91 N ANISOU 4075 N GLY A 539 9755 10785 11723 -397 2554 -967 N ATOM 4076 CA GLY A 539 32.371 8.836 -60.845 1.00 84.56 C ANISOU 4076 CA GLY A 539 9874 10637 11618 -236 2738 -1149 C ATOM 4077 C GLY A 539 31.104 9.337 -61.507 1.00 83.59 C ANISOU 4077 C GLY A 539 9940 10332 11488 -319 2606 -1364 C ATOM 4078 O GLY A 539 30.832 9.025 -62.669 1.00 84.12 O ANISOU 4078 O GLY A 539 10123 10374 11463 -246 2690 -1433 O ATOM 4079 N ASP A 540 30.306 10.121 -60.777 1.00 82.37 N ANISOU 4079 N ASP A 540 9824 10051 11420 -451 2386 -1485 N ATOM 4080 CA ASP A 540 29.094 10.667 -61.382 1.00 81.63 C ANISOU 4080 CA ASP A 540 9893 9794 11330 -520 2236 -1696 C ATOM 4081 C ASP A 540 29.424 11.551 -62.579 1.00 82.66 C ANISOU 4081 C ASP A 540 10059 9978 11369 -609 2145 -1583 C ATOM 4082 O ASP A 540 28.768 11.463 -63.627 1.00 82.79 O ANISOU 4082 O ASP A 540 10226 9913 11317 -572 2148 -1711 O ATOM 4083 CB ASP A 540 28.285 11.440 -60.343 1.00 84.99 C ANISOU 4083 CB ASP A 540 10332 10110 11851 -617 2011 -1833 C ATOM 4084 CG ASP A 540 27.452 10.533 -59.460 1.00 95.27 C ANISOU 4084 CG ASP A 540 11656 11321 13222 -526 2115 -2009 C ATOM 4085 OD1 ASP A 540 27.120 9.413 -59.901 1.00 97.91 O ANISOU 4085 OD1 ASP A 540 12050 11598 13555 -423 2303 -2090 O ATOM 4086 OD2 ASP A 540 27.123 10.940 -58.328 1.00100.48 O ANISOU 4086 OD2 ASP A 540 12282 11963 13932 -557 2003 -2062 O ATOM 4087 N HIS A 541 30.448 12.401 -62.446 1.00 83.66 N ANISOU 4087 N HIS A 541 10051 10241 11494 -734 2054 -1331 N ATOM 4088 CA HIS A 541 30.875 13.216 -63.579 1.00 85.09 C ANISOU 4088 CA HIS A 541 10252 10494 11583 -838 1991 -1165 C ATOM 4089 C HIS A 541 31.246 12.349 -64.775 1.00 86.30 C ANISOU 4089 C HIS A 541 10439 10770 11582 -676 2262 -1110 C ATOM 4090 O HIS A 541 30.865 12.652 -65.911 1.00 86.96 O ANISOU 4090 O HIS A 541 10669 10821 11552 -678 2236 -1144 O ATOM 4091 CB HIS A 541 32.054 14.103 -63.181 1.00 86.43 C ANISOU 4091 CB HIS A 541 10229 10808 11803 -1009 1878 -861 C ATOM 4092 CG HIS A 541 31.653 15.407 -62.566 1.00 91.17 C ANISOU 4092 CG HIS A 541 10878 11256 12507 -1203 1519 -898 C ATOM 4093 ND1 HIS A 541 32.320 15.957 -61.492 1.00101.99 N ANISOU 4093 ND1 HIS A 541 12104 12658 13989 -1315 1351 -770 N ATOM 4094 CD2 HIS A 541 30.667 16.279 -62.883 1.00 87.52 C ANISOU 4094 CD2 HIS A 541 10603 10601 12050 -1287 1272 -1058 C ATOM 4095 CE1 HIS A 541 31.756 17.106 -61.168 1.00 97.21 C ANISOU 4095 CE1 HIS A 541 11611 11877 13449 -1453 1014 -858 C ATOM 4096 NE2 HIS A 541 30.751 17.325 -61.996 1.00 89.38 N ANISOU 4096 NE2 HIS A 541 10816 10749 12395 -1435 964 -1031 N ATOM 4097 N LEU A 542 31.982 11.259 -64.538 1.00 86.82 N ANISOU 4097 N LEU A 542 10388 10975 11625 -510 2513 -1036 N ATOM 4098 CA LEU A 542 32.366 10.378 -65.637 1.00 88.27 C ANISOU 4098 CA LEU A 542 10616 11281 11644 -308 2770 -1005 C ATOM 4099 C LEU A 542 31.144 9.737 -66.282 1.00 87.48 C ANISOU 4099 C LEU A 542 10773 10972 11495 -182 2777 -1314 C ATOM 4100 O LEU A 542 31.072 9.625 -67.511 1.00 88.72 O ANISOU 4100 O LEU A 542 11061 11163 11487 -87 2846 -1334 O ATOM 4101 CB LEU A 542 33.340 9.308 -65.144 1.00 89.07 C ANISOU 4101 CB LEU A 542 10552 11544 11745 -126 3007 -896 C ATOM 4102 CG LEU A 542 33.916 8.372 -66.210 1.00 91.05 C ANISOU 4102 CG LEU A 542 10828 11956 11809 131 3281 -852 C ATOM 4103 CD1 LEU A 542 34.664 9.173 -67.253 1.00 93.23 C ANISOU 4103 CD1 LEU A 542 11021 12468 11935 65 3327 -599 C ATOM 4104 CD2 LEU A 542 34.829 7.321 -65.598 1.00 91.86 C ANISOU 4104 CD2 LEU A 542 10775 12196 11932 330 3482 -766 C ATOM 4105 N LEU A 543 30.174 9.307 -65.468 1.00 85.70 N ANISOU 4105 N LEU A 543 10618 10537 11407 -179 2703 -1551 N ATOM 4106 CA LEU A 543 28.929 8.766 -66.006 1.00 85.11 C ANISOU 4106 CA LEU A 543 10759 10247 11333 -101 2669 -1846 C ATOM 4107 C LEU A 543 28.273 9.756 -66.954 1.00 85.29 C ANISOU 4107 C LEU A 543 10924 10198 11283 -200 2475 -1917 C ATOM 4108 O LEU A 543 27.924 9.416 -68.093 1.00 86.23 O ANISOU 4108 O LEU A 543 11214 10275 11273 -85 2507 -2025 O ATOM 4109 CB LEU A 543 27.965 8.419 -64.869 1.00 83.40 C ANISOU 4109 CB LEU A 543 10545 9843 11301 -146 2595 -2043 C ATOM 4110 CG LEU A 543 28.075 7.077 -64.150 1.00 83.33 C ANISOU 4110 CG LEU A 543 10507 9792 11362 -10 2779 -2080 C ATOM 4111 CD1 LEU A 543 26.954 6.942 -63.143 1.00 81.94 C ANISOU 4111 CD1 LEU A 543 10339 9439 11354 -93 2690 -2260 C ATOM 4112 CD2 LEU A 543 28.014 5.940 -65.138 1.00 84.57 C ANISOU 4112 CD2 LEU A 543 10815 9887 11429 189 2924 -2185 C ATOM 4113 N HIS A 544 28.097 10.993 -66.492 1.00 84.59 N ANISOU 4113 N HIS A 544 10787 10083 11270 -400 2252 -1865 N ATOM 4114 CA HIS A 544 27.431 11.995 -67.314 1.00 84.84 C ANISOU 4114 CA HIS A 544 10970 10020 11245 -495 2032 -1934 C ATOM 4115 C HIS A 544 28.203 12.246 -68.602 1.00 86.91 C ANISOU 4115 C HIS A 544 11286 10440 11295 -461 2121 -1729 C ATOM 4116 O HIS A 544 27.629 12.229 -69.700 1.00 87.64 O ANISOU 4116 O HIS A 544 11577 10463 11260 -386 2081 -1850 O ATOM 4117 CB HIS A 544 27.265 13.287 -66.520 1.00 84.09 C ANISOU 4117 CB HIS A 544 10815 9867 11267 -698 1764 -1891 C ATOM 4118 CG HIS A 544 26.475 14.333 -67.238 1.00 84.34 C ANISOU 4118 CG HIS A 544 11019 9762 11263 -786 1499 -1987 C ATOM 4119 ND1 HIS A 544 25.219 14.093 -67.752 1.00 83.86 N ANISOU 4119 ND1 HIS A 544 11126 9531 11206 -706 1408 -2281 N ATOM 4120 CD2 HIS A 544 26.760 15.622 -67.529 1.00 85.25 C ANISOU 4120 CD2 HIS A 544 11169 9875 11346 -947 1285 -1825 C ATOM 4121 CE1 HIS A 544 24.765 15.190 -68.329 1.00 84.39 C ANISOU 4121 CE1 HIS A 544 11328 9504 11232 -793 1153 -2304 C ATOM 4122 NE2 HIS A 544 25.681 16.133 -68.208 1.00 85.24 N ANISOU 4122 NE2 HIS A 544 11371 9701 11316 -943 1073 -2026 N ATOM 4123 N SER A 545 29.514 12.468 -68.486 1.00 88.14 N ANISOU 4123 N SER A 545 11259 10824 11404 -508 2246 -1411 N ATOM 4124 CA SER A 545 30.344 12.710 -69.661 1.00 90.54 C ANISOU 4124 CA SER A 545 11572 11332 11496 -480 2372 -1168 C ATOM 4125 C SER A 545 30.205 11.589 -70.682 1.00 91.59 C ANISOU 4125 C SER A 545 11858 11502 11439 -205 2586 -1302 C ATOM 4126 O SER A 545 30.008 11.838 -71.877 1.00 93.04 O ANISOU 4126 O SER A 545 12220 11704 11428 -149 2575 -1302 O ATOM 4127 CB SER A 545 31.803 12.872 -69.241 1.00 91.89 C ANISOU 4127 CB SER A 545 11461 11772 11681 -549 2516 -813 C ATOM 4128 OG SER A 545 32.662 12.827 -70.364 1.00 94.57 O ANISOU 4128 OG SER A 545 11770 12363 11800 -469 2721 -574 O ATOM 4129 N THR A 546 30.289 10.340 -70.223 1.00 91.08 N ANISOU 4129 N THR A 546 11752 11432 11421 -20 2764 -1423 N ATOM 4130 CA THR A 546 30.272 9.214 -71.150 1.00 92.45 C ANISOU 4130 CA THR A 546 12080 11631 11415 266 2954 -1550 C ATOM 4131 C THR A 546 28.916 9.075 -71.831 1.00 91.94 C ANISOU 4131 C THR A 546 12302 11307 11326 317 2782 -1875 C ATOM 4132 O THR A 546 28.847 8.878 -73.049 1.00 93.72 O ANISOU 4132 O THR A 546 12717 11567 11326 478 2826 -1925 O ATOM 4133 CB THR A 546 30.651 7.930 -70.418 1.00 92.16 C ANISOU 4133 CB THR A 546 11950 11604 11461 441 3142 -1606 C ATOM 4134 OG1 THR A 546 32.006 8.033 -69.964 1.00 93.16 O ANISOU 4134 OG1 THR A 546 11808 12010 11580 433 3307 -1296 O ATOM 4135 CG2 THR A 546 30.539 6.740 -71.340 1.00 93.71 C ANISOU 4135 CG2 THR A 546 12345 11773 11488 750 3290 -1780 C ATOM 4136 N ARG A 547 27.822 9.184 -71.070 1.00 89.79 N ANISOU 4136 N ARG A 547 12057 10785 11274 191 2580 -2100 N ATOM 4137 CA ARG A 547 26.506 9.078 -71.698 1.00 89.53 C ANISOU 4137 CA ARG A 547 12259 10512 11246 228 2396 -2409 C ATOM 4138 C ARG A 547 26.299 10.183 -72.728 1.00 90.57 C ANISOU 4138 C ARG A 547 12536 10662 11213 160 2231 -2356 C ATOM 4139 O ARG A 547 25.814 9.927 -73.842 1.00 91.86 O ANISOU 4139 O ARG A 547 12930 10759 11214 304 2186 -2509 O ATOM 4140 CB ARG A 547 25.405 9.107 -70.639 1.00 87.34 C ANISOU 4140 CB ARG A 547 11932 10011 11243 91 2222 -2625 C ATOM 4141 CG ARG A 547 25.406 7.901 -69.702 1.00 86.60 C ANISOU 4141 CG ARG A 547 11744 9856 11305 163 2373 -2700 C ATOM 4142 CD ARG A 547 24.101 7.789 -68.914 1.00 85.06 C ANISOU 4142 CD ARG A 547 11535 9435 11349 56 2217 -2945 C ATOM 4143 NE ARG A 547 24.099 6.647 -68.000 1.00 96.53 N ANISOU 4143 NE ARG A 547 12907 10825 12947 104 2366 -2981 N ATOM 4144 CZ ARG A 547 23.697 5.422 -68.327 1.00112.31 C ANISOU 4144 CZ ARG A 547 15023 12670 14979 234 2430 -3146 C ATOM 4145 NH1 ARG A 547 23.258 5.169 -69.553 1.00110.62 N ANISOU 4145 NH1 ARG A 547 15015 12357 14659 345 2349 -3313 N ATOM 4146 NH2 ARG A 547 23.736 4.447 -67.429 1.00124.61 N ANISOU 4146 NH2 ARG A 547 16512 14160 16675 255 2555 -3143 N ATOM 4147 N LYS A 548 26.680 11.416 -72.382 1.00 90.27 N ANISOU 4147 N LYS A 548 12386 10704 11210 -53 2122 -2136 N ATOM 4148 CA LYS A 548 26.601 12.512 -73.345 1.00 91.60 C ANISOU 4148 CA LYS A 548 12698 10889 11216 -133 1965 -2032 C ATOM 4149 C LYS A 548 27.386 12.187 -74.611 1.00 94.31 C ANISOU 4149 C LYS A 548 13143 11444 11246 46 2179 -1868 C ATOM 4150 O LYS A 548 26.879 12.339 -75.730 1.00 95.65 O ANISOU 4150 O LYS A 548 13559 11558 11225 140 2089 -1966 O ATOM 4151 CB LYS A 548 27.122 13.802 -72.711 1.00 91.32 C ANISOU 4151 CB LYS A 548 12510 10912 11277 -395 1832 -1770 C ATOM 4152 CG LYS A 548 26.045 14.811 -72.343 1.00 90.02 C ANISOU 4152 CG LYS A 548 12433 10507 11263 -555 1477 -1939 C ATOM 4153 CD LYS A 548 26.603 15.917 -71.452 1.00 89.68 C ANISOU 4153 CD LYS A 548 12229 10492 11355 -794 1334 -1713 C ATOM 4154 CE LYS A 548 27.793 16.617 -72.089 1.00 92.04 C ANISOU 4154 CE LYS A 548 12480 10990 11500 -910 1403 -1310 C ATOM 4155 NZ LYS A 548 28.385 17.641 -71.180 1.00 91.99 N ANISOU 4155 NZ LYS A 548 12309 10987 11656 -1159 1237 -1088 N ATOM 4156 N GLN A 549 28.627 11.718 -74.450 1.00 95.38 N ANISOU 4156 N GLN A 549 13090 11839 11312 117 2465 -1621 N ATOM 4157 CA GLN A 549 29.456 11.412 -75.612 1.00 98.34 C ANISOU 4157 CA GLN A 549 13526 12469 11368 314 2704 -1444 C ATOM 4158 C GLN A 549 28.840 10.311 -76.463 1.00 99.18 C ANISOU 4158 C GLN A 549 13897 12475 11312 624 2754 -1752 C ATOM 4159 O GLN A 549 28.948 10.335 -77.694 1.00101.61 O ANISOU 4159 O GLN A 549 14400 12888 11319 787 2812 -1721 O ATOM 4160 CB GLN A 549 30.858 11.015 -75.164 1.00 99.39 C ANISOU 4160 CB GLN A 549 13368 12906 11489 360 3001 -1154 C ATOM 4161 CG GLN A 549 31.673 12.163 -74.609 1.00 99.63 C ANISOU 4161 CG GLN A 549 13142 13086 11625 63 2959 -790 C ATOM 4162 CD GLN A 549 33.041 11.724 -74.161 1.00110.87 C ANISOU 4162 CD GLN A 549 14251 14817 13056 117 3238 -516 C ATOM 4163 OE1 GLN A 549 33.300 10.534 -74.000 1.00114.77 O ANISOU 4163 OE1 GLN A 549 14515 15502 13591 -92 3254 -169 O ATOM 4164 NE2 GLN A 549 33.932 12.686 -73.957 1.00115.91 N ANISOU 4164 NE2 GLN A 549 14877 15498 13667 396 3442 -669 N ATOM 4165 N VAL A 550 28.187 9.338 -75.828 1.00 97.47 N ANISOU 4165 N VAL A 550 13702 12048 11286 707 2720 -2047 N ATOM 4166 CA VAL A 550 27.502 8.296 -76.585 1.00 98.39 C ANISOU 4166 CA VAL A 550 14082 12008 11292 973 2704 -2365 C ATOM 4167 C VAL A 550 26.392 8.901 -77.432 1.00 98.65 C ANISOU 4167 C VAL A 550 14381 11851 11252 939 2423 -2561 C ATOM 4168 O VAL A 550 26.275 8.608 -78.628 1.00100.90 O ANISOU 4168 O VAL A 550 14919 12155 11263 1161 2430 -2656 O ATOM 4169 CB VAL A 550 26.964 7.207 -75.643 1.00 96.63 C ANISOU 4169 CB VAL A 550 13813 11564 11338 1008 2691 -2614 C ATOM 4170 CG1 VAL A 550 26.041 6.273 -76.395 1.00 97.59 C ANISOU 4170 CG1 VAL A 550 14223 11450 11407 1218 2582 -2969 C ATOM 4171 CG2 VAL A 550 28.110 6.430 -75.028 1.00 97.03 C ANISOU 4171 CG2 VAL A 550 13666 11804 11399 1126 2976 -2441 C ATOM 4172 N GLU A 551 25.560 9.755 -76.829 1.00 96.59 N ANISOU 4172 N GLU A 551 14074 11406 11218 684 2162 -2634 N ATOM 4173 CA GLU A 551 24.477 10.346 -77.611 1.00 96.96 C ANISOU 4173 CA GLU A 551 14365 11267 11207 665 1871 -2831 C ATOM 4174 C GLU A 551 25.020 11.179 -78.765 1.00 99.41 C ANISOU 4174 C GLU A 551 14825 11760 11184 699 1889 -2595 C ATOM 4175 O GLU A 551 24.468 11.153 -79.872 1.00101.09 O ANISOU 4175 O GLU A 551 15322 11899 11186 851 1767 -2749 O ATOM 4176 CB GLU A 551 23.562 11.197 -76.730 1.00 94.60 C ANISOU 4176 CB GLU A 551 13970 10771 11201 407 1593 -2934 C ATOM 4177 CG GLU A 551 22.351 11.747 -77.485 1.00 99.42 C ANISOU 4177 CG GLU A 551 14820 11174 11781 409 1266 -3174 C ATOM 4178 CD GLU A 551 21.380 12.523 -76.606 1.00113.88 C ANISOU 4178 CD GLU A 551 16548 12819 13902 201 991 -3313 C ATOM 4179 OE1 GLU A 551 21.619 12.643 -75.386 1.00121.02 O ANISOU 4179 OE1 GLU A 551 17210 13751 15020 56 1052 -3229 O ATOM 4180 OE2 GLU A 551 20.366 13.017 -77.145 1.00116.50 O ANISOU 4180 OE2 GLU A 551 17047 12983 14233 205 705 -3515 O ATOM 4181 N GLU A 552 26.106 11.919 -78.530 1.00 99.92 N ANISOU 4181 N GLU A 552 14704 12066 11194 554 2036 -2208 N ATOM 4182 CA GLU A 552 26.698 12.700 -79.612 1.00102.66 C ANISOU 4182 CA GLU A 552 15172 12612 11224 563 2086 -1927 C ATOM 4183 C GLU A 552 27.233 11.794 -80.713 1.00107.33 C ANISOU 4183 C GLU A 552 15918 13404 11458 903 2344 -1923 C ATOM 4184 O GLU A 552 27.145 12.127 -81.901 1.00116.00 O ANISOU 4184 O GLU A 552 17267 14564 12243 1021 2312 -1882 O ATOM 4185 CB GLU A 552 27.813 13.597 -79.073 1.00110.42 C ANISOU 4185 CB GLU A 552 15881 13815 12258 314 2198 -1491 C ATOM 4186 CG GLU A 552 27.336 14.746 -78.198 1.00122.17 C ANISOU 4186 CG GLU A 552 17284 15109 14028 -10 1895 -1464 C ATOM 4187 CD GLU A 552 28.484 15.599 -77.679 1.00135.99 C ANISOU 4187 CD GLU A 552 18772 17056 15841 -261 1975 -1034 C ATOM 4188 OE1 GLU A 552 29.655 15.245 -77.933 1.00139.83 O ANISOU 4188 OE1 GLU A 552 19100 17853 16178 -191 2288 -752 O ATOM 4189 OE2 GLU A 552 28.215 16.623 -77.015 1.00141.70 O ANISOU 4189 OE2 GLU A 552 19446 17625 16770 -521 1711 -983 O ATOM 4190 N ALA A 553 27.783 10.638 -80.339 1.00105.51 N ANISOU 4190 N ALA A 553 15560 13274 11254 1088 2593 -1973 N ATOM 4191 CA ALA A 553 28.326 9.723 -81.336 1.00108.49 C ANISOU 4191 CA ALA A 553 16089 13846 11286 1456 2838 -1992 C ATOM 4192 C ALA A 553 27.220 9.077 -82.158 1.00109.17 C ANISOU 4192 C ALA A 553 16544 13676 11259 1692 2637 -2406 C ATOM 4193 O ALA A 553 27.359 8.920 -83.376 1.00112.20 O ANISOU 4193 O ALA A 553 17183 14182 11267 1953 2700 -2416 O ATOM 4194 CB ALA A 553 29.178 8.653 -80.660 1.00108.35 C ANISOU 4194 CB ALA A 553 15847 13973 11349 1606 3122 -1956 C ATOM 4195 N GLY A 554 26.129 8.676 -81.513 1.00107.02 N ANISOU 4195 N GLY A 554 15853 13923 10886 498 1452 -1 N ATOM 4196 CA GLY A 554 25.001 8.140 -82.254 1.00112.29 C ANISOU 4196 CA GLY A 554 16696 14625 11343 630 1201 -130 C ATOM 4197 C GLY A 554 25.332 6.821 -82.922 1.00117.82 C ANISOU 4197 C GLY A 554 17495 15536 11737 782 1235 -362 C ATOM 4198 O GLY A 554 26.054 5.980 -82.378 1.00120.71 O ANISOU 4198 O GLY A 554 17757 15929 12180 792 1352 -547 O ATOM 4199 N ASP A 555 24.797 6.638 -84.133 1.00131.08 N ANISOU 4199 N ASP A 555 19387 17356 13061 922 1104 -367 N ATOM 4200 CA ASP A 555 24.993 5.390 -84.865 1.00126.48 C ANISOU 4200 CA ASP A 555 18919 16971 12168 1100 1088 -626 C ATOM 4201 C ASP A 555 26.453 5.145 -85.219 1.00115.68 C ANISOU 4201 C ASP A 555 17507 15857 10587 1144 1427 -612 C ATOM 4202 O ASP A 555 26.816 4.013 -85.558 1.00119.08 O ANISOU 4202 O ASP A 555 17973 16430 10842 1298 1437 -889 O ATOM 4203 CB ASP A 555 24.157 5.388 -86.145 1.00136.08 C ANISOU 4203 CB ASP A 555 20385 18306 13015 1251 872 -621 C ATOM 4204 CG ASP A 555 22.668 5.439 -85.871 1.00142.52 C ANISOU 4204 CG ASP A 555 21214 18891 14045 1240 505 -710 C ATOM 4205 OD1 ASP A 555 22.280 5.919 -84.786 1.00147.14 O ANISOU 4205 OD1 ASP A 555 21624 19247 15035 1090 464 -666 O ATOM 4206 OD2 ASP A 555 21.887 5.001 -86.745 1.00143.87 O ANISOU 4206 OD2 ASP A 555 21559 19125 13980 1389 255 -842 O ATOM 4207 N LYS A 556 27.296 6.170 -85.150 1.00115.54 N ANISOU 4207 N LYS A 556 17400 15897 10604 1013 1693 -315 N ATOM 4208 CA LYS A 556 28.680 6.070 -85.606 1.00117.85 C ANISOU 4208 CA LYS A 556 17622 16475 10680 1038 2044 -274 C ATOM 4209 C LYS A 556 29.582 5.497 -84.517 1.00115.65 C ANISOU 4209 C LYS A 556 17094 16126 10723 1000 2178 -465 C ATOM 4210 O LYS A 556 30.669 5.999 -84.235 1.00121.92 O ANISOU 4210 O LYS A 556 17708 16992 11624 895 2454 -328 O ATOM 4211 CB LYS A 556 29.159 7.441 -86.067 1.00120.22 C ANISOU 4211 CB LYS A 556 17934 16860 10882 885 2262 155 C ATOM 4212 CG LYS A 556 28.076 8.281 -86.747 1.00122.43 C ANISOU 4212 CG LYS A 556 18453 17059 11008 874 2037 403 C ATOM 4213 CD LYS A 556 27.455 7.574 -87.953 1.00134.49 C ANISOU 4213 CD LYS A 556 20246 18796 12058 1095 1874 253 C ATOM 4214 CE LYS A 556 26.172 8.261 -88.398 1.00139.85 C ANISOU 4214 CE LYS A 556 21140 19315 12680 1109 1542 420 C ATOM 4215 NZ LYS A 556 25.181 8.366 -87.287 1.00138.47 N ANISOU 4215 NZ LYS A 556 20841 18774 12999 1045 1256 304 N ATOM 4216 N LEU A 557 29.113 4.422 -83.897 1.00113.20 N ANISOU 4216 N LEU A 557 16775 15658 10577 1080 1959 -782 N ATOM 4217 CA LEU A 557 29.824 3.749 -82.823 1.00111.05 C ANISOU 4217 CA LEU A 557 16314 15276 10603 1064 2007 -982 C ATOM 4218 C LEU A 557 29.568 2.253 -82.920 1.00111.06 C ANISOU 4218 C LEU A 557 16404 15264 10529 1248 1808 -1358 C ATOM 4219 O LEU A 557 28.407 1.827 -82.975 1.00110.31 O ANISOU 4219 O LEU A 557 16449 15028 10436 1273 1525 -1462 O ATOM 4220 CB LEU A 557 29.378 4.277 -81.460 1.00107.50 C ANISOU 4220 CB LEU A 557 15747 14509 10591 875 1898 -893 C ATOM 4221 CG LEU A 557 30.175 3.768 -80.258 1.00105.47 C ANISOU 4221 CG LEU A 557 15305 14128 10639 836 1947 -1043 C ATOM 4222 CD1 LEU A 557 31.575 4.366 -80.250 1.00106.78 C ANISOU 4222 CD1 LEU A 557 15282 14445 10846 790 2256 -915 C ATOM 4223 CD2 LEU A 557 29.444 4.072 -78.960 1.00102.22 C ANISOU 4223 CD2 LEU A 557 14836 13419 10584 678 1781 -1013 C ATOM 4224 N PRO A 558 30.615 1.435 -82.940 1.00112.16 N ANISOU 4224 N PRO A 558 16457 15533 10628 1379 1930 -1580 N ATOM 4225 CA PRO A 558 30.430 -0.012 -83.107 1.00112.74 C ANISOU 4225 CA PRO A 558 16631 15572 10634 1576 1713 -1953 C ATOM 4226 C PRO A 558 29.478 -0.594 -82.073 1.00109.70 C ANISOU 4226 C PRO A 558 16286 14823 10570 1480 1399 -2055 C ATOM 4227 O PRO A 558 29.582 -0.311 -80.878 1.00107.04 O ANISOU 4227 O PRO A 558 15824 14282 10566 1315 1408 -1963 O ATOM 4228 CB PRO A 558 31.847 -0.563 -82.940 1.00113.97 C ANISOU 4228 CB PRO A 558 16615 15863 10825 1695 1904 -2140 C ATOM 4229 CG PRO A 558 32.735 0.568 -83.339 1.00115.63 C ANISOU 4229 CG PRO A 558 16678 16336 10920 1613 2276 -1872 C ATOM 4230 CD PRO A 558 32.034 1.819 -82.909 1.00113.52 C ANISOU 4230 CD PRO A 558 16422 15898 10810 1366 2265 -1509 C ATOM 4231 N ALA A 559 28.535 -1.415 -82.546 1.00110.41 N ANISOU 4231 N ALA A 559 16553 14846 10553 1577 1120 -2249 N ATOM 4232 CA ALA A 559 27.522 -1.976 -81.657 1.00108.10 C ANISOU 4232 CA ALA A 559 16298 14227 10549 1454 830 -2327 C ATOM 4233 C ALA A 559 28.159 -2.754 -80.516 1.00106.62 C ANISOU 4233 C ALA A 559 16023 13839 10649 1419 793 -2460 C ATOM 4234 O ALA A 559 27.664 -2.730 -79.383 1.00104.15 O ANISOU 4234 O ALA A 559 15667 13280 10626 1227 696 -2384 O ATOM 4235 CB ALA A 559 26.568 -2.869 -82.448 1.00109.83 C ANISOU 4235 CB ALA A 559 16704 14414 10613 1579 531 -2555 C ATOM 4236 N ASP A 560 29.262 -3.450 -80.799 1.00108.42 N ANISOU 4236 N ASP A 560 16225 14179 10792 1613 864 -2666 N ATOM 4237 CA ASP A 560 30.014 -4.108 -79.737 1.00107.40 C ANISOU 4237 CA ASP A 560 16011 13862 10933 1604 822 -2780 C ATOM 4238 C ASP A 560 30.544 -3.094 -78.732 1.00105.12 C ANISOU 4238 C ASP A 560 15539 13540 10863 1418 1030 -2529 C ATOM 4239 O ASP A 560 30.427 -3.294 -77.515 1.00107.07 O ANISOU 4239 O ASP A 560 15762 13535 11385 1278 920 -2498 O ATOM 4240 CB ASP A 560 31.161 -4.917 -80.337 1.00110.25 C ANISOU 4240 CB ASP A 560 16344 14387 11158 1883 870 -3067 C ATOM 4241 CG ASP A 560 30.682 -6.161 -81.050 1.00112.47 C ANISOU 4241 CG ASP A 560 16815 14609 11309 2081 580 -3387 C ATOM 4242 OD1 ASP A 560 29.464 -6.279 -81.293 1.00112.10 O ANISOU 4242 OD1 ASP A 560 16917 14449 11228 2001 375 -3363 O ATOM 4243 OD2 ASP A 560 31.529 -7.021 -81.367 1.00114.83 O ANISOU 4243 OD2 ASP A 560 17102 14970 11559 2325 542 -3685 O ATOM 4244 N ASP A 561 31.126 -1.997 -79.222 1.00114.56 N ANISOU 4244 N ASP A 561 16612 14982 11932 1407 1324 -2343 N ATOM 4245 CA ASP A 561 31.619 -0.960 -78.323 1.00109.31 C ANISOU 4245 CA ASP A 561 15768 14273 11492 1228 1502 -2111 C ATOM 4246 C ASP A 561 30.487 -0.377 -77.489 1.00103.57 C ANISOU 4246 C ASP A 561 15076 13322 10952 1004 1379 -1928 C ATOM 4247 O ASP A 561 30.617 -0.230 -76.271 1.00 99.20 O ANISOU 4247 O ASP A 561 14441 12587 10662 874 1351 -1880 O ATOM 4248 CB ASP A 561 32.327 0.141 -79.111 1.00113.96 C ANISOU 4248 CB ASP A 561 16236 15150 11914 1226 1822 -1916 C ATOM 4249 CG ASP A 561 33.767 -0.206 -79.430 1.00122.03 C ANISOU 4249 CG ASP A 561 17098 16389 12880 1384 2025 -2070 C ATOM 4250 OD1 ASP A 561 34.247 -1.251 -78.943 1.00128.89 O ANISOU 4250 OD1 ASP A 561 17944 17153 13876 1510 1891 -2334 O ATOM 4251 OD2 ASP A 561 34.425 0.572 -80.154 1.00126.39 O ANISOU 4251 OD2 ASP A 561 17539 17213 13270 1377 2314 -1924 O ATOM 4252 N LYS A 562 29.362 -0.049 -78.128 1.00101.38 N ANISOU 4252 N LYS A 562 14916 13068 10537 970 1294 -1846 N ATOM 4253 CA LYS A 562 28.220 0.479 -77.386 1.00 99.19 C ANISOU 4253 CA LYS A 562 14642 12604 10442 778 1172 -1716 C ATOM 4254 C LYS A 562 27.787 -0.487 -76.290 1.00 97.65 C ANISOU 4254 C LYS A 562 14482 12164 10458 694 969 -1856 C ATOM 4255 O LYS A 562 27.602 -0.089 -75.135 1.00 95.70 O ANISOU 4255 O LYS A 562 14154 11776 10431 529 972 -1763 O ATOM 4256 CB LYS A 562 27.060 0.765 -78.339 1.00100.16 C ANISOU 4256 CB LYS A 562 14885 12787 10384 797 1059 -1669 C ATOM 4257 CG LYS A 562 25.858 1.423 -77.677 1.00 98.37 C ANISOU 4257 CG LYS A 562 14621 12404 10350 621 945 -1553 C ATOM 4258 CD LYS A 562 24.635 1.406 -78.581 1.00101.72 C ANISOU 4258 CD LYS A 562 15162 12858 10628 666 756 -1582 C ATOM 4259 CE LYS A 562 23.451 2.105 -77.927 1.00102.22 C ANISOU 4259 CE LYS A 562 15144 12787 10908 508 649 -1497 C ATOM 4260 NZ LYS A 562 23.682 3.569 -77.790 1.00104.19 N ANISOU 4260 NZ LYS A 562 15299 13063 11227 451 796 -1257 N ATOM 4261 N THR A 563 27.639 -1.768 -76.633 1.00 98.86 N ANISOU 4261 N THR A 563 14764 12260 10536 805 784 -2079 N ATOM 4262 CA THR A 563 27.237 -2.766 -75.647 1.00 97.97 C ANISOU 4262 CA THR A 563 14714 11893 10615 705 574 -2186 C ATOM 4263 C THR A 563 28.197 -2.787 -74.465 1.00 96.79 C ANISOU 4263 C THR A 563 14480 11642 10655 652 645 -2155 C ATOM 4264 O THR A 563 27.784 -2.649 -73.303 1.00 95.13 O ANISOU 4264 O THR A 563 14247 11277 10622 463 604 -2063 O ATOM 4265 CB THR A 563 27.166 -4.145 -76.304 1.00100.03 C ANISOU 4265 CB THR A 563 15133 12094 10780 862 353 -2442 C ATOM 4266 OG1 THR A 563 26.133 -4.153 -77.292 1.00101.16 O ANISOU 4266 OG1 THR A 563 15363 12304 10769 894 239 -2483 O ATOM 4267 CG2 THR A 563 26.874 -5.213 -75.271 1.00 99.58 C ANISOU 4267 CG2 THR A 563 15161 11741 10934 742 127 -2521 C ATOM 4268 N ALA A 564 29.492 -2.936 -74.746 1.00 97.92 N ANISOU 4268 N ALA A 564 14563 11890 10752 824 754 -2242 N ATOM 4269 CA ALA A 564 30.464 -3.052 -73.666 1.00 97.21 C ANISOU 4269 CA ALA A 564 14391 11693 10850 807 776 -2250 C ATOM 4270 C ALA A 564 30.502 -1.791 -72.809 1.00 95.23 C ANISOU 4270 C ALA A 564 13997 11447 10740 630 935 -2028 C ATOM 4271 O ALA A 564 30.566 -1.871 -71.575 1.00 93.98 O ANISOU 4271 O ALA A 564 13833 11123 10753 514 864 -1995 O ATOM 4272 CB ALA A 564 31.841 -3.367 -74.242 1.00 99.21 C ANISOU 4272 CB ALA A 564 14558 12095 11041 1041 875 -2410 C ATOM 4273 N ILE A 565 30.442 -0.616 -73.441 1.00 95.21 N ANISOU 4273 N ILE A 565 13893 11623 10661 608 1130 -1875 N ATOM 4274 CA ILE A 565 30.444 0.631 -72.680 1.00 93.64 C ANISOU 4274 CA ILE A 565 13560 11403 10618 452 1251 -1682 C ATOM 4275 C ILE A 565 29.226 0.694 -71.769 1.00 91.93 C ANISOU 4275 C ILE A 565 13400 11024 10504 272 1116 -1632 C ATOM 4276 O ILE A 565 29.329 1.093 -70.607 1.00 90.65 O ANISOU 4276 O ILE A 565 13172 10765 10506 158 1122 -1578 O ATOM 4277 CB ILE A 565 30.506 1.857 -73.614 1.00 94.41 C ANISOU 4277 CB ILE A 565 13569 11684 10618 453 1447 -1508 C ATOM 4278 CG1 ILE A 565 31.815 1.905 -74.404 1.00 96.48 C ANISOU 4278 CG1 ILE A 565 13732 12145 10780 591 1640 -1532 C ATOM 4279 CG2 ILE A 565 30.382 3.140 -72.810 1.00 92.98 C ANISOU 4279 CG2 ILE A 565 13265 11432 10634 293 1518 -1328 C ATOM 4280 CD1 ILE A 565 31.851 3.008 -75.457 1.00 97.91 C ANISOU 4280 CD1 ILE A 565 13870 12519 10813 574 1836 -1328 C ATOM 4281 N GLU A 566 28.054 0.295 -72.274 1.00 92.17 N ANISOU 4281 N GLU A 566 13543 11040 10438 246 994 -1664 N ATOM 4282 CA GLU A 566 26.845 0.398 -71.460 1.00 90.97 C ANISOU 4282 CA GLU A 566 13401 10775 10388 63 897 -1625 C ATOM 4283 C GLU A 566 26.901 -0.549 -70.270 1.00 90.51 C ANISOU 4283 C GLU A 566 13415 10545 10430 -33 777 -1692 C ATOM 4284 O GLU A 566 26.505 -0.184 -69.153 1.00 89.44 O ANISOU 4284 O GLU A 566 13233 10347 10404 -191 788 -1629 O ATOM 4285 CB GLU A 566 25.601 0.135 -72.310 1.00101.28 C ANISOU 4285 CB GLU A 566 14783 12106 11592 58 777 -1664 C ATOM 4286 CG GLU A 566 25.392 1.183 -73.401 1.00112.88 C ANISOU 4286 CG GLU A 566 16210 13730 12950 137 864 -1563 C ATOM 4287 CD GLU A 566 23.941 1.354 -73.816 1.00119.36 C ANISOU 4287 CD GLU A 566 17047 14548 13755 83 731 -1569 C ATOM 4288 OE1 GLU A 566 23.242 0.338 -74.011 1.00123.66 O ANISOU 4288 OE1 GLU A 566 17681 15032 14271 69 560 -1702 O ATOM 4289 OE2 GLU A 566 23.501 2.516 -73.951 1.00119.46 O ANISOU 4289 OE2 GLU A 566 16976 14606 13807 58 778 -1449 O ATOM 4290 N SER A 567 27.404 -1.766 -70.485 1.00 91.63 N ANISOU 4290 N SER A 567 13681 10608 10527 67 652 -1824 N ATOM 4291 CA SER A 567 27.603 -2.675 -69.363 1.00 91.62 C ANISOU 4291 CA SER A 567 13780 10414 10618 -15 514 -1860 C ATOM 4292 C SER A 567 28.550 -2.072 -68.334 1.00 90.70 C ANISOU 4292 C SER A 567 13570 10287 10606 -30 608 -1797 C ATOM 4293 O SER A 567 28.283 -2.121 -67.125 1.00 90.09 O ANISOU 4293 O SER A 567 13528 10106 10595 -186 561 -1737 O ATOM 4294 CB SER A 567 28.133 -4.013 -69.865 1.00 93.88 C ANISOU 4294 CB SER A 567 14212 10596 10863 141 336 -2030 C ATOM 4295 OG SER A 567 27.265 -4.555 -70.844 1.00106.45 O ANISOU 4295 OG SER A 567 15890 12193 12362 166 225 -2113 O ATOM 4296 N ALA A 568 29.655 -1.481 -68.796 1.00 90.90 N ANISOU 4296 N ALA A 568 13468 10429 10638 123 743 -1809 N ATOM 4297 CA ALA A 568 30.588 -0.857 -67.865 1.00 90.27 C ANISOU 4297 CA ALA A 568 13275 10335 10688 113 814 -1766 C ATOM 4298 C ALA A 568 29.933 0.292 -67.112 1.00 88.82 C ANISOU 4298 C ALA A 568 13000 10173 10575 -56 904 -1633 C ATOM 4299 O ALA A 568 30.176 0.478 -65.914 1.00 88.28 O ANISOU 4299 O ALA A 568 12921 10026 10594 -133 872 -1614 O ATOM 4300 CB ALA A 568 31.828 -0.367 -68.607 1.00 91.78 C ANISOU 4300 CB ALA A 568 13306 10670 10897 281 966 -1798 C ATOM 4301 N LEU A 569 29.101 1.074 -67.802 1.00 88.47 N ANISOU 4301 N LEU A 569 12894 10231 10488 -98 997 -1558 N ATOM 4302 CA LEU A 569 28.377 2.164 -67.161 1.00 87.42 C ANISOU 4302 CA LEU A 569 12666 10113 10437 -232 1057 -1469 C ATOM 4303 C LEU A 569 27.521 1.645 -66.023 1.00 87.03 C ANISOU 4303 C LEU A 569 12701 9977 10389 -392 959 -1490 C ATOM 4304 O LEU A 569 27.589 2.154 -64.901 1.00 90.35 O ANISOU 4304 O LEU A 569 13071 10376 10882 -472 980 -1473 O ATOM 4305 CB LEU A 569 27.494 2.894 -68.173 1.00 87.54 C ANISOU 4305 CB LEU A 569 12633 10225 10403 -231 1112 -1404 C ATOM 4306 CG LEU A 569 28.094 3.899 -69.150 1.00 88.11 C ANISOU 4306 CG LEU A 569 12605 10399 10473 -136 1244 -1307 C ATOM 4307 CD1 LEU A 569 26.981 4.668 -69.836 1.00 88.29 C ANISOU 4307 CD1 LEU A 569 12611 10471 10464 -163 1237 -1231 C ATOM 4308 CD2 LEU A 569 29.028 4.847 -68.441 1.00 87.76 C ANISOU 4308 CD2 LEU A 569 12418 10328 10599 -156 1335 -1249 C ATOM 4309 N THR A 570 26.691 0.638 -66.302 1.00 87.60 N ANISOU 4309 N THR A 570 12900 10007 10377 -449 853 -1529 N ATOM 4310 CA THR A 570 25.817 0.106 -65.263 1.00 87.72 C ANISOU 4310 CA THR A 570 12989 9956 10384 -642 784 -1522 C ATOM 4311 C THR A 570 26.625 -0.422 -64.084 1.00 87.92 C ANISOU 4311 C THR A 570 13117 9871 10417 -674 718 -1517 C ATOM 4312 O THR A 570 26.303 -0.132 -62.922 1.00 87.78 O ANISOU 4312 O THR A 570 13092 9863 10398 -810 746 -1480 O ATOM 4313 CB THR A 570 24.918 -0.979 -65.850 1.00 88.73 C ANISOU 4313 CB THR A 570 13234 10028 10452 -707 661 -1561 C ATOM 4314 OG1 THR A 570 24.043 -0.385 -66.816 1.00 88.69 O ANISOU 4314 OG1 THR A 570 13126 10133 10440 -685 701 -1571 O ATOM 4315 CG2 THR A 570 24.085 -1.636 -64.769 1.00 89.38 C ANISOU 4315 CG2 THR A 570 13395 10039 10527 -945 603 -1527 C ATOM 4316 N ALA A 571 27.696 -1.173 -64.361 1.00 88.53 N ANISOU 4316 N ALA A 571 13289 9853 10494 -531 621 -1568 N ATOM 4317 CA ALA A 571 28.563 -1.623 -63.276 1.00 88.96 C ANISOU 4317 CA ALA A 571 13443 9788 10570 -526 520 -1570 C ATOM 4318 C ALA A 571 29.059 -0.450 -62.441 1.00 88.11 C ANISOU 4318 C ALA A 571 13194 9753 10531 -527 625 -1544 C ATOM 4319 O ALA A 571 29.065 -0.513 -61.203 1.00 88.36 O ANISOU 4319 O ALA A 571 13303 9738 10534 -626 572 -1515 O ATOM 4320 CB ALA A 571 29.743 -2.411 -63.837 1.00 89.92 C ANISOU 4320 CB ALA A 571 13625 9818 10721 -319 403 -1670 C ATOM 4321 N LEU A 572 29.461 0.639 -63.100 1.00 87.40 N ANISOU 4321 N LEU A 572 12909 9774 10525 -425 764 -1550 N ATOM 4322 CA LEU A 572 29.957 1.800 -62.367 1.00 86.85 C ANISOU 4322 CA LEU A 572 12694 9744 10560 -424 838 -1539 C ATOM 4323 C LEU A 572 28.861 2.439 -61.528 1.00 86.40 C ANISOU 4323 C LEU A 572 12610 9744 10474 -583 888 -1510 C ATOM 4324 O LEU A 572 29.104 2.823 -60.383 1.00 86.49 O ANISOU 4324 O LEU A 572 12615 9745 10502 -621 866 -1530 O ATOM 4325 CB LEU A 572 30.544 2.834 -63.321 1.00 86.60 C ANISOU 4325 CB LEU A 572 12465 9799 10641 -315 972 -1521 C ATOM 4326 CG LEU A 572 30.941 4.139 -62.624 1.00 86.26 C ANISOU 4326 CG LEU A 572 12258 9766 10749 -332 1029 -1509 C ATOM 4327 CD1 LEU A 572 32.058 3.882 -61.634 1.00 86.77 C ANISOU 4327 CD1 LEU A 572 12336 9746 10885 -281 923 -1577 C ATOM 4328 CD2 LEU A 572 31.347 5.209 -63.616 1.00 86.38 C ANISOU 4328 CD2 LEU A 572 12093 9845 10881 -275 1162 -1445 C ATOM 4329 N GLU A 573 27.660 2.587 -62.089 1.00 86.18 N ANISOU 4329 N GLU A 573 12551 9790 10404 -661 949 -1486 N ATOM 4330 CA GLU A 573 26.542 3.126 -61.323 1.00 86.15 C ANISOU 4330 CA GLU A 573 12489 9866 10377 -802 1003 -1495 C ATOM 4331 C GLU A 573 26.318 2.315 -60.055 1.00 86.97 C ANISOU 4331 C GLU A 573 12748 9942 10356 -945 942 -1489 C ATOM 4332 O GLU A 573 26.144 2.876 -58.962 1.00 87.24 O ANISOU 4332 O GLU A 573 12744 10041 10362 -1009 981 -1519 O ATOM 4333 CB GLU A 573 25.285 3.135 -62.193 1.00 86.20 C ANISOU 4333 CB GLU A 573 12444 9944 10364 -857 1040 -1490 C ATOM 4334 CG GLU A 573 24.350 4.317 -61.985 1.00102.02 C ANISOU 4334 CG GLU A 573 14266 12057 12441 -896 1122 -1529 C ATOM 4335 CD GLU A 573 23.371 4.493 -63.140 1.00118.48 C ANISOU 4335 CD GLU A 573 16278 14191 14548 -880 1122 -1529 C ATOM 4336 OE1 GLU A 573 23.444 3.708 -64.109 1.00121.19 O ANISOU 4336 OE1 GLU A 573 16721 14494 14833 -840 1065 -1500 O ATOM 4337 OE2 GLU A 573 22.532 5.417 -63.084 1.00124.37 O ANISOU 4337 OE2 GLU A 573 16869 15013 15374 -890 1156 -1578 O ATOM 4338 N THR A 574 26.358 0.987 -60.180 1.00 87.71 N ANISOU 4338 N THR A 574 13033 9931 10362 -993 833 -1450 N ATOM 4339 CA THR A 574 26.199 0.134 -59.008 1.00 88.95 C ANISOU 4339 CA THR A 574 13380 10031 10386 -1147 755 -1400 C ATOM 4340 C THR A 574 27.310 0.388 -57.997 1.00 89.14 C ANISOU 4340 C THR A 574 13459 10008 10402 -1068 688 -1416 C ATOM 4341 O THR A 574 27.054 0.491 -56.792 1.00 89.99 O ANISOU 4341 O THR A 574 13632 10171 10391 -1184 700 -1397 O ATOM 4342 CB THR A 574 26.168 -1.334 -59.425 1.00 89.98 C ANISOU 4342 CB THR A 574 13721 10000 10469 -1193 602 -1351 C ATOM 4343 OG1 THR A 574 25.473 -1.456 -60.669 1.00 89.67 O ANISOU 4343 OG1 THR A 574 13605 9987 10479 -1179 630 -1379 O ATOM 4344 CG2 THR A 574 25.440 -2.160 -58.386 1.00 91.69 C ANISOU 4344 CG2 THR A 574 14118 10181 10540 -1445 559 -1251 C ATOM 4345 N ALA A 575 28.554 0.514 -58.469 1.00 88.64 N ANISOU 4345 N ALA A 575 13356 9863 10461 -868 621 -1463 N ATOM 4346 CA ALA A 575 29.651 0.776 -57.540 1.00 89.03 C ANISOU 4346 CA ALA A 575 13430 9859 10538 -779 529 -1502 C ATOM 4347 C ALA A 575 29.490 2.130 -56.859 1.00 88.58 C ANISOU 4347 C ALA A 575 13205 9930 10520 -792 638 -1555 C ATOM 4348 O ALA A 575 29.834 2.287 -55.682 1.00 89.39 O ANISOU 4348 O ALA A 575 13377 10031 10554 -805 566 -1583 O ATOM 4349 CB ALA A 575 30.992 0.701 -58.265 1.00 88.87 C ANISOU 4349 CB ALA A 575 13338 9751 10678 -566 456 -1565 C ATOM 4350 N LEU A 576 28.967 3.119 -57.586 1.00 87.57 N ANISOU 4350 N LEU A 576 12868 9902 10500 -777 785 -1578 N ATOM 4351 CA LEU A 576 28.755 4.447 -57.028 1.00 87.37 C ANISOU 4351 CA LEU A 576 12676 9971 10550 -772 862 -1651 C ATOM 4352 C LEU A 576 27.660 4.446 -55.977 1.00 88.25 C ANISOU 4352 C LEU A 576 12841 10208 10480 -927 914 -1676 C ATOM 4353 O LEU A 576 27.662 5.301 -55.085 1.00 88.73 O ANISOU 4353 O LEU A 576 12828 10342 10542 -911 928 -1772 O ATOM 4354 CB LEU A 576 28.405 5.437 -58.139 1.00 86.46 C ANISOU 4354 CB LEU A 576 12352 9899 10600 -718 972 -1652 C ATOM 4355 CG LEU A 576 29.539 5.875 -59.061 1.00 86.04 C ANISOU 4355 CG LEU A 576 12187 9770 10735 -578 971 -1628 C ATOM 4356 CD1 LEU A 576 29.002 6.758 -60.165 1.00 85.58 C ANISOU 4356 CD1 LEU A 576 11979 9754 10782 -559 1073 -1583 C ATOM 4357 CD2 LEU A 576 30.592 6.612 -58.268 1.00 86.45 C ANISOU 4357 CD2 LEU A 576 12152 9765 10929 -507 906 -1698 C ATOM 4358 N LYS A 577 26.708 3.517 -56.067 1.00 88.78 N ANISOU 4358 N LYS A 577 13022 10315 10395 -1081 948 -1603 N ATOM 4359 CA LYS A 577 25.717 3.440 -55.002 1.00 90.14 C ANISOU 4359 CA LYS A 577 13237 10639 10374 -1256 1026 -1616 C ATOM 4360 C LYS A 577 26.295 2.873 -53.710 1.00 91.62 C ANISOU 4360 C LYS A 577 13648 10796 10365 -1305 925 -1581 C ATOM 4361 O LYS A 577 25.710 3.080 -52.644 1.00 93.06 O ANISOU 4361 O LYS A 577 13854 11140 10363 -1416 1001 -1615 O ATOM 4362 CB LYS A 577 24.517 2.618 -55.463 1.00 90.70 C ANISOU 4362 CB LYS A 577 13339 10759 10363 -1439 1096 -1540 C ATOM 4363 CG LYS A 577 23.596 3.398 -56.382 1.00 89.91 C ANISOU 4363 CG LYS A 577 12995 10759 10409 -1413 1206 -1613 C ATOM 4364 CD LYS A 577 22.505 2.535 -56.981 1.00 91.02 C ANISOU 4364 CD LYS A 577 13151 10922 10511 -1575 1236 -1553 C ATOM 4365 CE LYS A 577 21.534 3.379 -57.792 1.00107.99 C ANISOU 4365 CE LYS A 577 15047 13180 12802 -1534 1317 -1647 C ATOM 4366 NZ LYS A 577 22.236 4.242 -58.787 1.00115.06 N ANISOU 4366 NZ LYS A 577 15853 13988 13877 -1308 1268 -1671 N ATOM 4367 N GLY A 578 27.433 2.191 -53.771 1.00 91.59 N ANISOU 4367 N GLY A 578 13807 10604 10388 -1211 748 -1526 N ATOM 4368 CA GLY A 578 28.041 1.580 -52.607 1.00 93.24 C ANISOU 4368 CA GLY A 578 14262 10750 10415 -1237 597 -1481 C ATOM 4369 C GLY A 578 28.908 2.537 -51.819 1.00 93.39 C ANISOU 4369 C GLY A 578 14213 10793 10480 -1086 528 -1612 C ATOM 4370 O GLY A 578 28.854 3.757 -51.991 1.00 93.73 O ANISOU 4370 O GLY A 578 14013 10922 10677 -998 621 -1741 O ATOM 4371 N GLU A 579 29.722 1.962 -50.935 1.00 94.86 N ANISOU 4371 N GLU A 579 14625 10877 10539 -1052 330 -1582 N ATOM 4372 CA GLU A 579 30.640 2.703 -50.074 1.00 95.49 C ANISOU 4372 CA GLU A 579 14680 10954 10648 -904 203 -1715 C ATOM 4373 C GLU A 579 32.027 2.070 -50.098 1.00 95.92 C ANISOU 4373 C GLU A 579 14851 10781 10813 -745 -64 -1710 C ATOM 4374 O GLU A 579 32.696 1.956 -49.067 1.00 97.60 O ANISOU 4374 O GLU A 579 15223 10947 10912 -683 -262 -1745 O ATOM 4375 CB GLU A 579 30.122 2.776 -48.638 1.00 98.54 C ANISOU 4375 CB GLU A 579 15235 11508 10699 -1017 216 -1724 C ATOM 4376 CG GLU A 579 28.642 3.124 -48.489 1.00106.34 C ANISOU 4376 CG GLU A 579 16130 12751 11524 -1201 486 -1727 C ATOM 4377 CD GLU A 579 28.367 4.615 -48.551 1.00110.76 C ANISOU 4377 CD GLU A 579 16380 13455 12251 -1094 612 -1944 C ATOM 4378 OE1 GLU A 579 29.243 5.406 -48.141 1.00105.42 O ANISOU 4378 OE1 GLU A 579 15633 12728 11694 -920 481 -2095 O ATOM 4379 OE2 GLU A 579 27.268 4.993 -49.009 1.00119.97 O ANISOU 4379 OE2 GLU A 579 17368 14767 13448 -1181 818 -1973 O ATOM 4380 N ASP A 580 32.482 1.643 -51.277 1.00114.11 N ANISOU 4380 N ASP A 580 17073 12951 13333 -662 -85 -1686 N ATOM 4381 CA ASP A 580 33.798 1.029 -51.446 1.00113.68 C ANISOU 4381 CA ASP A 580 17074 12696 13423 -486 -326 -1719 C ATOM 4382 C ASP A 580 34.557 1.810 -52.509 1.00110.29 C ANISOU 4382 C ASP A 580 16314 12258 13333 -326 -250 -1832 C ATOM 4383 O ASP A 580 34.258 1.691 -53.701 1.00114.08 O ANISOU 4383 O ASP A 580 16682 12753 13908 -333 -108 -1795 O ATOM 4384 CB ASP A 580 33.677 -0.446 -51.833 1.00113.88 C ANISOU 4384 CB ASP A 580 17343 12565 13360 -533 -445 -1590 C ATOM 4385 CG ASP A 580 35.028 -1.112 -52.038 1.00113.11 C ANISOU 4385 CG ASP A 580 17285 12259 13431 -318 -714 -1663 C ATOM 4386 OD1 ASP A 580 36.044 -0.577 -51.544 1.00113.24 O ANISOU 4386 OD1 ASP A 580 17203 12250 13572 -164 -846 -1790 O ATOM 4387 OD2 ASP A 580 35.074 -2.179 -52.687 1.00111.44 O ANISOU 4387 OD2 ASP A 580 17192 11905 13243 -295 -809 -1617 O ATOM 4388 N LYS A 581 35.544 2.599 -52.076 1.00 94.21 N ANISOU 4388 N LYS A 581 14126 10200 11471 -192 -349 -1966 N ATOM 4389 CA LYS A 581 36.292 3.435 -53.010 1.00 93.27 C ANISOU 4389 CA LYS A 581 13676 10080 11683 -79 -259 -2052 C ATOM 4390 C LYS A 581 37.036 2.594 -54.038 1.00 93.36 C ANISOU 4390 C LYS A 581 13643 10001 11828 36 -299 -2051 C ATOM 4391 O LYS A 581 37.103 2.957 -55.219 1.00 92.38 O ANISOU 4391 O LYS A 581 13306 9935 11860 57 -117 -2042 O ATOM 4392 CB LYS A 581 37.266 4.323 -52.241 1.00 94.26 C ANISOU 4392 CB LYS A 581 13655 10171 11989 28 -400 -2202 C ATOM 4393 CG LYS A 581 38.083 5.269 -53.100 1.00 93.82 C ANISOU 4393 CG LYS A 581 13240 10108 12298 106 -307 -2273 C ATOM 4394 CD LYS A 581 39.185 5.914 -52.275 1.00 98.61 C ANISOU 4394 CD LYS A 581 13715 10639 13113 213 -511 -2435 C ATOM 4395 CE LYS A 581 39.872 7.044 -53.023 1.00102.83 C ANISOU 4395 CE LYS A 581 13874 11168 14027 233 -397 -2484 C ATOM 4396 NZ LYS A 581 40.930 7.685 -52.191 1.00109.68 N ANISOU 4396 NZ LYS A 581 14594 11947 15133 324 -619 -2658 N ATOM 4397 N ALA A 582 37.594 1.461 -53.609 1.00102.28 N ANISOU 4397 N ALA A 582 14982 10992 12886 118 -546 -2065 N ATOM 4398 CA ALA A 582 38.371 0.622 -54.516 1.00106.13 C ANISOU 4398 CA ALA A 582 15420 11391 13512 267 -618 -2117 C ATOM 4399 C ALA A 582 37.514 0.109 -55.665 1.00 94.48 C ANISOU 4399 C ALA A 582 13981 9965 11952 194 -437 -2024 C ATOM 4400 O ALA A 582 37.925 0.152 -56.829 1.00 93.97 O ANISOU 4400 O ALA A 582 13717 9951 12035 290 -316 -2077 O ATOM 4401 CB ALA A 582 38.989 -0.544 -53.747 1.00118.28 C ANISOU 4401 CB ALA A 582 17222 12739 14982 373 -966 -2150 C ATOM 4402 N ALA A 583 36.314 -0.384 -55.355 1.00 93.97 N ANISOU 4402 N ALA A 583 14163 9898 11641 20 -416 -1891 N ATOM 4403 CA ALA A 583 35.435 -0.884 -56.405 1.00 93.12 C ANISOU 4403 CA ALA A 583 14093 9826 11464 -55 -276 -1817 C ATOM 4404 C ALA A 583 35.038 0.226 -57.366 1.00 91.42 C ANISOU 4404 C ALA A 583 13603 9787 11344 -83 10 -1814 C ATOM 4405 O ALA A 583 34.963 0.009 -58.581 1.00 91.02 O ANISOU 4405 O ALA A 583 13472 9777 11334 -32 113 -1821 O ATOM 4406 CB ALA A 583 34.196 -1.529 -55.790 1.00 96.37 C ANISOU 4406 CB ALA A 583 14785 10210 11621 -271 -301 -1672 C ATOM 4407 N ILE A 584 34.786 1.426 -56.841 1.00 90.69 N ANISOU 4407 N ILE A 584 13380 9794 11285 -154 121 -1809 N ATOM 4408 CA ILE A 584 34.409 2.545 -57.699 1.00 89.41 C ANISOU 4408 CA ILE A 584 12979 9762 11231 -181 354 -1789 C ATOM 4409 C ILE A 584 35.546 2.885 -58.650 1.00 89.66 C ANISOU 4409 C ILE A 584 12778 9807 11483 -33 412 -1847 C ATOM 4410 O ILE A 584 35.343 3.035 -59.860 1.00 89.20 O ANISOU 4410 O ILE A 584 12618 9830 11444 -21 571 -1805 O ATOM 4411 CB ILE A 584 33.996 3.761 -56.853 1.00 89.03 C ANISOU 4411 CB ILE A 584 12841 9782 11206 -262 411 -1804 C ATOM 4412 CG1 ILE A 584 32.737 3.440 -56.050 1.00 89.09 C ANISOU 4412 CG1 ILE A 584 13042 9841 10966 -422 418 -1752 C ATOM 4413 CG2 ILE A 584 33.759 4.962 -57.743 1.00 88.11 C ANISOU 4413 CG2 ILE A 584 12482 9748 11249 -269 601 -1780 C ATOM 4414 CD1 ILE A 584 32.124 4.637 -55.364 1.00 88.90 C ANISOU 4414 CD1 ILE A 584 12910 9923 10945 -486 503 -1801 C ATOM 4415 N GLU A 585 36.765 2.999 -58.119 1.00 90.73 N ANISOU 4415 N GLU A 585 12821 9877 11776 78 283 -1947 N ATOM 4416 CA GLU A 585 37.902 3.322 -58.972 1.00 91.46 C ANISOU 4416 CA GLU A 585 12651 10007 12093 200 360 -2010 C ATOM 4417 C GLU A 585 38.131 2.238 -60.014 1.00 92.06 C ANISOU 4417 C GLU A 585 12769 10100 12108 309 374 -2042 C ATOM 4418 O GLU A 585 38.382 2.537 -61.188 1.00 92.23 O ANISOU 4418 O GLU A 585 12612 10243 12190 347 564 -2029 O ATOM 4419 CB GLU A 585 39.149 3.540 -58.120 1.00 92.85 C ANISOU 4419 CB GLU A 585 12708 10102 12469 301 184 -2140 C ATOM 4420 CG GLU A 585 39.030 4.746 -57.207 1.00100.09 C ANISOU 4420 CG GLU A 585 13545 11008 13478 217 169 -2143 C ATOM 4421 CD GLU A 585 40.358 5.191 -56.629 1.00112.90 C ANISOU 4421 CD GLU A 585 14967 12563 15368 316 20 -2283 C ATOM 4422 OE1 GLU A 585 41.053 4.358 -56.011 1.00114.88 O ANISOU 4422 OE1 GLU A 585 15315 12721 15613 438 -218 -2390 O ATOM 4423 OE2 GLU A 585 40.711 6.378 -56.803 1.00118.63 O ANISOU 4423 OE2 GLU A 585 15435 13310 16328 272 120 -2286 O ATOM 4424 N ALA A 586 38.024 0.971 -59.612 1.00 92.67 N ANISOU 4424 N ALA A 586 13097 10059 12057 358 166 -2082 N ATOM 4425 CA ALA A 586 38.167 -0.117 -60.571 1.00 93.49 C ANISOU 4425 CA ALA A 586 13262 10152 12106 478 139 -2144 C ATOM 4426 C ALA A 586 37.154 0.016 -61.701 1.00 92.39 C ANISOU 4426 C ALA A 586 13131 10138 11836 395 352 -2050 C ATOM 4427 O ALA A 586 37.516 -0.009 -62.885 1.00 98.99 O ANISOU 4427 O ALA A 586 13827 11092 12692 497 490 -2098 O ATOM 4428 CB ALA A 586 38.016 -1.460 -59.858 1.00 94.46 C ANISOU 4428 CB ALA A 586 13701 10075 12116 507 -155 -2170 C ATOM 4429 N LYS A 587 35.877 0.187 -61.353 1.00 91.09 N ANISOU 4429 N LYS A 587 13117 9966 11526 215 383 -1924 N ATOM 4430 CA LYS A 587 34.845 0.290 -62.378 1.00 90.24 C ANISOU 4430 CA LYS A 587 13022 9962 11304 143 542 -1847 C ATOM 4431 C LYS A 587 35.068 1.499 -63.280 1.00 89.86 C ANISOU 4431 C LYS A 587 12721 10079 11343 156 781 -1801 C ATOM 4432 O LYS A 587 34.812 1.429 -64.491 1.00 90.05 O ANISOU 4432 O LYS A 587 12717 10209 11290 196 900 -1784 O ATOM 4433 CB LYS A 587 33.465 0.333 -61.723 1.00 89.24 C ANISOU 4433 CB LYS A 587 13054 9811 11044 -57 531 -1741 C ATOM 4434 CG LYS A 587 33.082 -0.970 -61.027 1.00 90.07 C ANISOU 4434 CG LYS A 587 13437 9756 11027 -117 318 -1737 C ATOM 4435 CD LYS A 587 32.880 -2.096 -62.033 1.00 90.86 C ANISOU 4435 CD LYS A 587 13652 9800 11069 -48 243 -1784 C ATOM 4436 CE LYS A 587 32.791 -3.460 -61.364 1.00 92.26 C ANISOU 4436 CE LYS A 587 14113 9759 11184 -84 -21 -1783 C ATOM 4437 NZ LYS A 587 34.137 -4.004 -61.027 1.00 97.17 N ANISOU 4437 NZ LYS A 587 14762 10251 11908 113 -218 -1898 N ATOM 4438 N MET A 588 35.561 2.607 -62.720 1.00 89.65 N ANISOU 4438 N MET A 588 12522 10067 11475 122 837 -1778 N ATOM 4439 CA MET A 588 35.900 3.760 -63.548 1.00 89.80 C ANISOU 4439 CA MET A 588 12306 10206 11609 116 1044 -1709 C ATOM 4440 C MET A 588 36.980 3.405 -64.560 1.00 91.40 C ANISOU 4440 C MET A 588 12367 10508 11852 260 1135 -1776 C ATOM 4441 O MET A 588 36.854 3.706 -65.753 1.00 91.85 O ANISOU 4441 O MET A 588 12355 10706 11838 267 1316 -1704 O ATOM 4442 CB MET A 588 36.358 4.927 -62.675 1.00 89.74 C ANISOU 4442 CB MET A 588 12137 10151 11809 56 1040 -1696 C ATOM 4443 CG MET A 588 35.289 5.497 -61.764 1.00 88.53 C ANISOU 4443 CG MET A 588 12078 9946 11613 -71 989 -1654 C ATOM 4444 SD MET A 588 35.870 6.926 -60.835 1.00 88.87 S ANISOU 4444 SD MET A 588 11924 9926 11917 -110 960 -1680 S ATOM 4445 CE MET A 588 35.776 8.212 -62.070 1.00 89.13 C ANISOU 4445 CE MET A 588 11756 10021 12089 -168 1169 -1529 C ATOM 4446 N GLN A 589 38.052 2.757 -64.097 1.00 92.58 N ANISOU 4446 N GLN A 589 12472 10600 12106 386 1006 -1925 N ATOM 4447 CA GLN A 589 39.138 2.384 -64.998 1.00 95.23 C ANISOU 4447 CA GLN A 589 12632 11056 12494 544 1096 -2036 C ATOM 4448 C GLN A 589 38.632 1.490 -66.122 1.00 94.94 C ANISOU 4448 C GLN A 589 12732 11109 12233 630 1140 -2071 C ATOM 4449 O GLN A 589 38.912 1.737 -67.303 1.00 96.11 O ANISOU 4449 O GLN A 589 12746 11452 12319 678 1353 -2056 O ATOM 4450 CB GLN A 589 40.250 1.686 -64.219 1.00111.66 C ANISOU 4450 CB GLN A 589 14665 13032 14731 692 886 -2228 C ATOM 4451 CG GLN A 589 40.845 2.513 -63.093 1.00117.53 C ANISOU 4451 CG GLN A 589 15271 13684 15701 633 803 -2230 C ATOM 4452 CD GLN A 589 41.666 1.672 -62.136 1.00120.72 C ANISOU 4452 CD GLN A 589 15723 13936 16208 780 508 -2412 C ATOM 4453 OE1 GLN A 589 42.182 0.617 -62.507 1.00127.74 O ANISOU 4453 OE1 GLN A 589 16636 14817 17083 959 408 -2565 O ATOM 4454 NE2 GLN A 589 41.782 2.128 -60.894 1.00115.05 N ANISOU 4454 NE2 GLN A 589 15033 13091 15589 722 344 -2410 N ATOM 4455 N GLU A 590 37.877 0.446 -65.772 1.00 94.30 N ANISOU 4455 N GLU A 590 12924 10888 12018 641 936 -2115 N ATOM 4456 CA GLU A 590 37.309 -0.432 -66.788 1.00 94.81 C ANISOU 4456 CA GLU A 590 13135 11003 11887 719 932 -2167 C ATOM 4457 C GLU A 590 36.497 0.365 -67.803 1.00 94.17 C ANISOU 4457 C GLU A 590 13025 11090 11667 624 1155 -2016 C ATOM 4458 O GLU A 590 36.651 0.195 -69.022 1.00 95.50 O ANISOU 4458 O GLU A 590 13150 11429 11707 729 1284 -2060 O ATOM 4459 CB GLU A 590 36.451 -1.508 -66.116 1.00 94.21 C ANISOU 4459 CB GLU A 590 13360 10712 11724 673 671 -2186 C ATOM 4460 CG GLU A 590 37.201 -2.325 -65.064 1.00 95.16 C ANISOU 4460 CG GLU A 590 13565 10632 11960 761 406 -2305 C ATOM 4461 CD GLU A 590 36.323 -3.352 -64.365 1.00 95.36 C ANISOU 4461 CD GLU A 590 13912 10430 11890 670 153 -2269 C ATOM 4462 OE1 GLU A 590 35.135 -3.467 -64.728 1.00103.09 O ANISOU 4462 OE1 GLU A 590 15018 11418 12733 538 192 -2176 O ATOM 4463 OE2 GLU A 590 36.821 -4.043 -63.451 1.00 95.94 O ANISOU 4463 OE2 GLU A 590 14112 10312 12030 721 -95 -2326 O ATOM 4464 N LEU A 591 35.651 1.273 -67.311 1.00 92.45 N ANISOU 4464 N LEU A 591 12827 10831 11468 439 1194 -1846 N ATOM 4465 CA LEU A 591 34.843 2.092 -68.207 1.00 92.02 C ANISOU 4465 CA LEU A 591 12755 10902 11306 357 1360 -1697 C ATOM 4466 C LEU A 591 35.711 2.904 -69.162 1.00 93.53 C ANISOU 4466 C LEU A 591 12732 11285 11520 401 1597 -1633 C ATOM 4467 O LEU A 591 35.367 3.069 -70.339 1.00 94.35 O ANISOU 4467 O LEU A 591 12859 11541 11451 424 1725 -1565 O ATOM 4468 CB LEU A 591 33.939 3.016 -67.399 1.00 90.29 C ANISOU 4468 CB LEU A 591 12551 10599 11158 178 1343 -1563 C ATOM 4469 CG LEU A 591 33.165 4.009 -68.260 1.00 90.11 C ANISOU 4469 CG LEU A 591 12494 10674 11070 106 1480 -1406 C ATOM 4470 CD1 LEU A 591 32.188 3.271 -69.151 1.00 90.27 C ANISOU 4470 CD1 LEU A 591 12682 10744 10873 141 1433 -1429 C ATOM 4471 CD2 LEU A 591 32.452 5.027 -67.399 1.00 88.81 C ANISOU 4471 CD2 LEU A 591 12295 10423 11028 -36 1454 -1317 C ATOM 4472 N ALA A 592 36.837 3.427 -68.676 1.00 94.22 N ANISOU 4472 N ALA A 592 12610 11374 11817 403 1657 -1647 N ATOM 4473 CA ALA A 592 37.724 4.182 -69.556 1.00 96.15 C ANISOU 4473 CA ALA A 592 12624 11807 12101 410 1904 -1570 C ATOM 4474 C ALA A 592 38.305 3.285 -70.641 1.00 98.33 C ANISOU 4474 C ALA A 592 12876 12282 12204 591 1998 -1714 C ATOM 4475 O ALA A 592 38.258 3.617 -71.838 1.00 99.80 O ANISOU 4475 O ALA A 592 13034 12676 12211 596 2203 -1618 O ATOM 4476 CB ALA A 592 38.839 4.834 -68.743 1.00 96.74 C ANISOU 4476 CB ALA A 592 12454 11828 12477 368 1921 -1586 C ATOM 4477 N GLN A 593 38.850 2.134 -70.233 1.00 98.87 N ANISOU 4477 N GLN A 593 12968 12286 12312 754 1835 -1954 N ATOM 4478 CA GLN A 593 39.386 1.173 -71.190 1.00101.18 C ANISOU 4478 CA GLN A 593 13240 12751 12452 966 1883 -2154 C ATOM 4479 C GLN A 593 38.391 0.892 -72.306 1.00101.31 C ANISOU 4479 C GLN A 593 13457 12879 12158 991 1928 -2110 C ATOM 4480 O GLN A 593 38.752 0.890 -73.487 1.00103.60 O ANISOU 4480 O GLN A 593 13670 13431 12262 1087 2129 -2142 O ATOM 4481 CB GLN A 593 39.759 -0.128 -70.481 1.00101.44 C ANISOU 4481 CB GLN A 593 13362 12608 12573 1137 1598 -2414 C ATOM 4482 CG GLN A 593 40.959 -0.037 -69.560 1.00104.29 C ANISOU 4482 CG GLN A 593 13506 12895 13223 1186 1530 -2523 C ATOM 4483 CD GLN A 593 41.182 -1.320 -68.788 1.00119.04 C ANISOU 4483 CD GLN A 593 15525 14537 15166 1348 1189 -2747 C ATOM 4484 OE1 GLN A 593 40.490 -2.315 -69.006 1.00120.50 O ANISOU 4484 OE1 GLN A 593 15967 14621 15198 1421 1017 -2824 O ATOM 4485 NE2 GLN A 593 42.145 -1.303 -67.876 1.00131.40 N ANISOU 4485 NE2 GLN A 593 16942 16002 16981 1403 1062 -2849 N ATOM 4486 N VAL A 594 37.121 0.672 -71.955 1.00 99.17 N ANISOU 4486 N VAL A 594 13433 12429 11818 902 1746 -2042 N ATOM 4487 CA VAL A 594 36.168 0.314 -73.004 1.00 99.54 C ANISOU 4487 CA VAL A 594 13665 12565 11591 942 1741 -2037 C ATOM 4488 C VAL A 594 35.734 1.535 -73.822 1.00 99.74 C ANISOU 4488 C VAL A 594 13652 12758 11489 822 1961 -1787 C ATOM 4489 O VAL A 594 35.416 1.405 -75.012 1.00101.27 O ANISOU 4489 O VAL A 594 13928 13133 11417 901 2041 -1786 O ATOM 4490 CB VAL A 594 34.970 -0.443 -72.397 1.00 97.71 C ANISOU 4490 CB VAL A 594 13685 12090 11349 884 1461 -2071 C ATOM 4491 CG1 VAL A 594 34.342 0.345 -71.274 1.00 95.29 C ANISOU 4491 CG1 VAL A 594 13383 11617 11203 667 1416 -1892 C ATOM 4492 CG2 VAL A 594 33.942 -0.760 -73.458 1.00 98.21 C ANISOU 4492 CG2 VAL A 594 13920 12230 11164 917 1428 -2076 C ATOM 4493 N SER A 595 35.742 2.734 -73.235 1.00 98.59 N ANISOU 4493 N SER A 595 13392 12547 11521 643 2043 -1578 N ATOM 4494 CA SER A 595 35.304 3.942 -73.936 1.00 98.99 C ANISOU 4494 CA SER A 595 13427 12697 11486 521 2205 -1319 C ATOM 4495 C SER A 595 36.436 4.656 -74.683 1.00101.64 C ANISOU 4495 C SER A 595 13552 13264 11804 512 2497 -1208 C ATOM 4496 O SER A 595 36.242 5.787 -75.167 1.00102.36 O ANISOU 4496 O SER A 595 13619 13407 11867 379 2633 -948 O ATOM 4497 CB SER A 595 34.631 4.901 -72.952 1.00 96.74 C ANISOU 4497 CB SER A 595 13139 12203 11416 338 2116 -1161 C ATOM 4498 OG SER A 595 35.299 4.898 -71.702 1.00103.66 O ANISOU 4498 OG SER A 595 13892 12935 12558 304 2047 -1242 O ATOM 4499 N GLN A 596 37.610 4.024 -74.771 1.00103.43 N ANISOU 4499 N GLN A 596 13617 13622 12058 643 2588 -1397 N ATOM 4500 CA GLN A 596 38.709 4.528 -75.594 1.00106.62 C ANISOU 4500 CA GLN A 596 13795 14305 12410 641 2900 -1325 C ATOM 4501 C GLN A 596 38.265 4.998 -76.981 1.00108.67 C ANISOU 4501 C GLN A 596 14165 14799 12324 614 3089 -1127 C ATOM 4502 O GLN A 596 38.658 6.078 -77.435 1.00110.48 O ANISOU 4502 O GLN A 596 14275 15147 12557 460 3320 -865 O ATOM 4503 CB GLN A 596 39.773 3.436 -75.723 1.00119.34 C ANISOU 4503 CB GLN A 596 15262 16069 14015 860 2934 -1645 C ATOM 4504 CG GLN A 596 41.166 3.866 -75.307 1.00134.88 C ANISOU 4504 CG GLN A 596 16875 18110 16263 821 3098 -1676 C ATOM 4505 CD GLN A 596 42.055 2.691 -74.943 1.00144.29 C ANISOU 4505 CD GLN A 596 17941 19318 17564 1058 2987 -2046 C ATOM 4506 OE1 GLN A 596 41.753 1.540 -75.266 1.00149.57 O ANISOU 4506 OE1 GLN A 596 18779 19999 18052 1267 2840 -2281 O ATOM 4507 NE2 GLN A 596 43.154 2.975 -74.257 1.00143.48 N ANISOU 4507 NE2 GLN A 596 17540 19194 17783 1033 3025 -2114 N ATOM 4508 N LYS A 597 37.457 4.193 -77.677 1.00108.74 N ANISOU 4508 N LYS A 597 14415 14871 12029 759 2977 -1242 N ATOM 4509 CA LYS A 597 37.036 4.572 -79.025 1.00111.03 C ANISOU 4509 CA LYS A 597 14839 15398 11949 762 3127 -1073 C ATOM 4510 C LYS A 597 36.252 5.876 -79.013 1.00110.09 C ANISOU 4510 C LYS A 597 14808 15143 11879 545 3113 -714 C ATOM 4511 O LYS A 597 36.445 6.729 -79.885 1.00112.66 O ANISOU 4511 O LYS A 597 15127 15645 12031 451 3326 -452 O ATOM 4512 CB LYS A 597 36.202 3.463 -79.660 1.00111.12 C ANISOU 4512 CB LYS A 597 15105 15452 11663 962 2940 -1291 C ATOM 4513 CG LYS A 597 36.029 3.620 -81.164 1.00114.40 C ANISOU 4513 CG LYS A 597 15650 16186 11631 1033 3105 -1197 C ATOM 4514 CD LYS A 597 37.376 3.523 -81.872 1.00118.29 C ANISOU 4514 CD LYS A 597 15930 17052 11962 1120 3446 -1271 C ATOM 4515 CE LYS A 597 37.225 3.352 -83.380 1.00122.01 C ANISOU 4515 CE LYS A 597 16560 17886 11913 1252 3592 -1269 C ATOM 4516 NZ LYS A 597 36.916 4.627 -84.081 1.00123.65 N ANISOU 4516 NZ LYS A 597 16859 18199 11922 1054 3762 -838 N ATOM 4517 N LEU A 598 35.368 6.048 -78.030 1.00106.77 N ANISOU 4517 N LEU A 598 14469 14409 11691 465 2860 -700 N ATOM 4518 CA LEU A 598 34.601 7.284 -77.913 1.00105.94 C ANISOU 4518 CA LEU A 598 14426 14144 11682 288 2806 -408 C ATOM 4519 C LEU A 598 35.525 8.484 -77.734 1.00107.33 C ANISOU 4519 C LEU A 598 14387 14318 12075 107 3012 -165 C ATOM 4520 O LEU A 598 35.458 9.468 -78.495 1.00109.46 O ANISOU 4520 O LEU A 598 14696 14652 12239 -8 3134 134 O ATOM 4521 CB LEU A 598 33.631 7.164 -76.736 1.00102.40 C ANISOU 4521 CB LEU A 598 14043 13392 11471 250 2524 -502 C ATOM 4522 CG LEU A 598 32.261 7.837 -76.791 1.00101.32 C ANISOU 4522 CG LEU A 598 14063 13106 11328 179 2348 -356 C ATOM 4523 CD1 LEU A 598 31.511 7.438 -78.041 1.00102.86 C ANISOU 4523 CD1 LEU A 598 14471 13454 11157 291 2300 -351 C ATOM 4524 CD2 LEU A 598 31.459 7.457 -75.570 1.00 98.25 C ANISOU 4524 CD2 LEU A 598 13693 12486 11152 156 2117 -519 C ATOM 4525 N MET A 599 36.414 8.412 -76.735 1.00107.06 N ANISOU 4525 N MET A 599 14128 14195 12354 74 3034 -286 N ATOM 4526 CA MET A 599 37.339 9.520 -76.509 1.00116.76 C ANISOU 4526 CA MET A 599 15123 15402 13839 -107 3207 -81 C ATOM 4527 C MET A 599 38.173 9.807 -77.750 1.00119.79 C ANISOU 4527 C MET A 599 15414 16107 13995 -149 3538 90 C ATOM 4528 O MET A 599 38.548 10.959 -77.998 1.00123.07 O ANISOU 4528 O MET A 599 15732 16511 14518 -351 3688 392 O ATOM 4529 CB MET A 599 38.240 9.224 -75.311 1.00133.28 C ANISOU 4529 CB MET A 599 16980 17383 16277 -98 3161 -291 C ATOM 4530 CG MET A 599 37.485 9.037 -74.002 1.00150.98 C ANISOU 4530 CG MET A 599 19313 19325 18726 -85 2859 -430 C ATOM 4531 SD MET A 599 36.336 10.386 -73.655 1.00159.16 S ANISOU 4531 SD MET A 599 20463 20105 19905 -254 2711 -180 S ATOM 4532 CE MET A 599 35.819 9.968 -71.991 1.00145.15 C ANISOU 4532 CE MET A 599 18716 18074 18360 -221 2428 -421 C ATOM 4533 N GLU A 600 38.460 8.776 -78.546 1.00124.79 N ANISOU 4533 N GLU A 600 16079 17029 14306 35 3655 -99 N ATOM 4534 CA GLU A 600 39.083 9.003 -79.843 1.00134.60 C ANISOU 4534 CA GLU A 600 17274 18633 15233 10 3985 60 C ATOM 4535 C GLU A 600 38.145 9.758 -80.777 1.00141.65 C ANISOU 4535 C GLU A 600 18442 19542 15837 -78 3977 391 C ATOM 4536 O GLU A 600 38.580 10.643 -81.523 1.00150.82 O ANISOU 4536 O GLU A 600 19563 20856 16885 -247 4222 713 O ATOM 4537 CB GLU A 600 39.507 7.665 -80.453 1.00133.44 C ANISOU 4537 CB GLU A 600 17117 18792 14792 271 4073 -277 C ATOM 4538 CG GLU A 600 39.659 7.667 -81.967 1.00135.51 C ANISOU 4538 CG GLU A 600 17465 19460 14562 316 4349 -162 C ATOM 4539 CD GLU A 600 40.073 6.311 -82.515 1.00135.58 C ANISOU 4539 CD GLU A 600 17452 19764 14297 610 4407 -560 C ATOM 4540 OE1 GLU A 600 40.832 5.596 -81.826 1.00135.57 O ANISOU 4540 OE1 GLU A 600 17229 19739 14544 729 4377 -871 O ATOM 4541 OE2 GLU A 600 39.638 5.957 -83.631 1.00133.56 O ANISOU 4541 OE2 GLU A 600 17411 19755 13582 739 4457 -576 O ATOM 4542 N ILE A 601 36.847 9.442 -80.728 1.00116.80 N ANISOU 4542 N ILE A 601 15570 16226 12581 22 3684 326 N ATOM 4543 CA ILE A 601 35.887 10.042 -81.650 1.00118.10 C ANISOU 4543 CA ILE A 601 16011 16405 12458 -15 3621 595 C ATOM 4544 C ILE A 601 35.757 11.539 -81.408 1.00118.54 C ANISOU 4544 C ILE A 601 16049 16229 12763 -265 3605 978 C ATOM 4545 O ILE A 601 35.456 12.294 -82.342 1.00121.32 O ANISOU 4545 O ILE A 601 16570 16645 12880 -352 3660 1302 O ATOM 4546 CB ILE A 601 34.524 9.328 -81.548 1.00115.34 C ANISOU 4546 CB ILE A 601 15911 15909 12004 150 3283 395 C ATOM 4547 CG1 ILE A 601 34.626 7.901 -82.088 1.00115.99 C ANISOU 4547 CG1 ILE A 601 16059 16232 11779 396 3291 56 C ATOM 4548 CG2 ILE A 601 33.443 10.078 -82.315 1.00116.42 C ANISOU 4548 CG2 ILE A 601 16313 15989 11932 111 3146 665 C ATOM 4549 CD1 ILE A 601 33.341 7.109 -81.983 1.00113.63 C ANISOU 4549 CD1 ILE A 601 15981 15782 11410 538 2955 -156 C ATOM 4550 N ALA A 602 35.994 11.993 -80.170 1.00116.18 N ANISOU 4550 N ALA A 602 15561 15648 12934 -376 3510 946 N ATOM 4551 CA ALA A 602 35.971 13.425 -79.861 1.00116.85 C ANISOU 4551 CA ALA A 602 15603 15481 13315 -607 3473 1273 C ATOM 4552 C ALA A 602 36.647 14.279 -80.939 1.00128.88 C ANISOU 4552 C ALA A 602 17118 17189 14662 -790 3758 1666 C ATOM 4553 O ALA A 602 35.998 15.110 -81.586 1.00139.18 O ANISOU 4553 O ALA A 602 18640 18405 15835 -876 3678 1984 O ATOM 4554 CB ALA A 602 36.630 13.670 -78.501 1.00114.86 C ANISOU 4554 CB ALA A 602 15074 15009 13558 -694 3430 1143 C ATOM 4555 N GLN A 603 37.958 14.102 -81.127 1.00157.95 N ANISOU 4555 N GLN A 603 20543 21124 18347 -860 4086 1656 N ATOM 4556 CA GLN A 603 38.705 14.670 -82.256 1.00166.65 C ANISOU 4556 CA GLN A 603 21614 22508 19198 -1033 4434 2000 C ATOM 4557 C GLN A 603 38.663 16.195 -82.314 1.00177.60 C ANISOU 4557 C GLN A 603 23036 23635 20809 -1330 4409 2466 C ATOM 4558 O GLN A 603 38.929 16.779 -83.370 1.00184.05 O ANISOU 4558 O GLN A 603 23946 24634 21351 -1491 4632 2840 O ATOM 4559 CB GLN A 603 38.212 14.096 -83.589 1.00165.96 C ANISOU 4559 CB GLN A 603 21810 22754 18492 -877 4519 2032 C ATOM 4560 CG GLN A 603 38.724 12.704 -83.893 1.00165.86 C ANISOU 4560 CG GLN A 603 21702 23114 18205 -633 4684 1636 C ATOM 4561 CD GLN A 603 38.114 12.125 -85.152 1.00167.47 C ANISOU 4561 CD GLN A 603 22213 23615 17802 -450 4705 1622 C ATOM 4562 OE1 GLN A 603 37.298 12.768 -85.814 1.00163.09 O ANISOU 4562 OE1 GLN A 603 21953 22994 17018 -507 4591 1924 O ATOM 4563 NE2 GLN A 603 38.506 10.903 -85.491 1.00172.55 N ANISOU 4563 NE2 GLN A 603 22795 24576 18189 -210 4820 1252 N ATOM 4564 N GLN A 604 38.328 16.854 -81.203 1.00203.48 N ANISOU 4564 N GLN A 604 26254 26485 24572 -1405 4132 2453 N ATOM 4565 CA GLN A 604 38.284 18.321 -81.130 1.00207.54 C ANISOU 4565 CA GLN A 604 26792 26682 25381 -1673 4046 2855 C ATOM 4566 C GLN A 604 37.363 18.915 -82.194 1.00207.98 C ANISOU 4566 C GLN A 604 27222 26704 25095 -1701 3942 3216 C ATOM 4567 O GLN A 604 37.528 20.066 -82.607 1.00207.96 O ANISOU 4567 O GLN A 604 27283 26551 25182 -1949 3969 3649 O ATOM 4568 CB GLN A 604 39.689 18.926 -81.245 1.00211.50 C ANISOU 4568 CB GLN A 604 26986 27286 26090 -1960 4379 3085 C ATOM 4569 CG GLN A 604 40.733 18.298 -80.329 1.00211.54 C ANISOU 4569 CG GLN A 604 26597 27375 26404 -1921 4499 2725 C ATOM 4570 CD GLN A 604 40.549 18.662 -78.865 1.00210.33 C ANISOU 4570 CD GLN A 604 26321 26795 26800 -1914 4171 2523 C ATOM 4571 OE1 GLN A 604 39.622 19.383 -78.497 1.00212.98 O ANISOU 4571 OE1 GLN A 604 26848 26775 27301 -1930 3861 2625 O ATOM 4572 NE2 GLN A 604 41.444 18.162 -78.019 1.00206.75 N ANISOU 4572 NE2 GLN A 604 25547 26385 26625 -1876 4229 2218 N TER 4573 GLN A 604 ATOM 4574 N LYS B 3 54.189 37.087 4.870 1.00149.63 N ANISOU 4574 N LYS B 3 20993 19425 16435 -542 626 396 N ATOM 4575 CA LYS B 3 55.220 37.558 5.791 1.00154.57 C ANISOU 4575 CA LYS B 3 21606 20215 16908 -651 395 125 C ATOM 4576 C LYS B 3 55.531 39.034 5.542 1.00161.23 C ANISOU 4576 C LYS B 3 22485 20660 18115 -900 112 -77 C ATOM 4577 O LYS B 3 55.825 39.788 6.475 1.00160.52 O ANISOU 4577 O LYS B 3 22463 20554 17974 -921 -68 -436 O ATOM 4578 CB LYS B 3 56.492 36.710 5.656 1.00151.72 C ANISOU 4578 CB LYS B 3 21085 20245 16318 -777 364 374 C ATOM 4579 CG LYS B 3 56.375 35.296 6.207 1.00149.53 C ANISOU 4579 CG LYS B 3 20776 20425 15614 -531 605 498 C ATOM 4580 CD LYS B 3 57.502 34.401 5.703 1.00148.24 C ANISOU 4580 CD LYS B 3 20442 20585 15298 -672 608 841 C ATOM 4581 CE LYS B 3 57.348 34.087 4.215 1.00145.39 C ANISOU 4581 CE LYS B 3 19998 20050 15196 -789 705 1262 C ATOM 4582 NZ LYS B 3 58.307 33.040 3.753 1.00141.84 N ANISOU 4582 NZ LYS B 3 19387 19946 14558 -879 757 1617 N ATOM 4583 N GLN B 4 55.454 39.438 4.277 1.00170.24 N ANISOU 4583 N GLN B 4 23582 21479 19624 -1087 75 157 N ATOM 4584 CA GLN B 4 55.719 40.820 3.911 1.00170.83 C ANISOU 4584 CA GLN B 4 23684 21155 20070 -1332 -184 0 C ATOM 4585 C GLN B 4 54.528 41.699 4.272 1.00173.95 C ANISOU 4585 C GLN B 4 24247 21198 20647 -1195 -173 -307 C ATOM 4586 O GLN B 4 53.376 41.254 4.280 1.00173.09 O ANISOU 4586 O GLN B 4 24215 21050 20503 -956 58 -276 O ATOM 4587 CB GLN B 4 56.025 40.927 2.413 1.00161.68 C ANISOU 4587 CB GLN B 4 22420 19771 19241 -1574 -220 364 C ATOM 4588 CG GLN B 4 56.571 42.287 1.963 1.00164.24 C ANISOU 4588 CG GLN B 4 22740 19729 19934 -1872 -512 245 C ATOM 4589 CD GLN B 4 57.080 42.282 0.518 1.00164.09 C ANISOU 4589 CD GLN B 4 22596 19551 20197 -2126 -555 627 C ATOM 4590 OE1 GLN B 4 56.677 41.446 -0.298 1.00163.72 O ANISOU 4590 OE1 GLN B 4 22501 19545 20162 -2063 -349 968 O ATOM 4591 NE2 GLN B 4 57.976 43.219 0.202 1.00166.16 N ANISOU 4591 NE2 GLN B 4 22810 19635 20689 -2415 -826 572 N ATOM 4592 N ASP B 5 54.820 42.957 4.592 1.00177.30 N ANISOU 4592 N ASP B 5 24730 21371 21263 -1347 -426 -610 N ATOM 4593 CA ASP B 5 53.769 43.909 4.920 1.00182.64 C ANISOU 4593 CA ASP B 5 25566 21691 22138 -1244 -444 -916 C ATOM 4594 C ASP B 5 52.779 44.031 3.767 1.00190.88 C ANISOU 4594 C ASP B 5 26634 22379 23515 -1237 -311 -697 C ATOM 4595 O ASP B 5 53.166 44.259 2.617 1.00191.78 O ANISOU 4595 O ASP B 5 26660 22302 23907 -1466 -385 -439 O ATOM 4596 CB ASP B 5 54.369 45.279 5.250 1.00180.11 C ANISOU 4596 CB ASP B 5 25286 21133 22015 -1457 -760 -1229 C ATOM 4597 CG ASP B 5 53.315 46.309 5.625 1.00193.77 C ANISOU 4597 CG ASP B 5 27046 23161 23419 -1401 -879 -1547 C ATOM 4598 OD1 ASP B 5 52.653 46.123 6.670 1.00202.52 O ANISOU 4598 OD1 ASP B 5 28160 24635 24153 -1172 -706 -1556 O ATOM 4599 OD2 ASP B 5 53.140 47.298 4.873 1.00194.81 O ANISOU 4599 OD2 ASP B 5 27196 23157 23668 -1584 -1147 -1790 O ATOM 4600 N TYR B 6 51.497 43.852 4.085 1.00166.66 N ANISOU 4600 N TYR B 6 23684 19228 20412 -970 -109 -796 N ATOM 4601 CA TYR B 6 50.412 44.057 3.133 1.00156.61 C ANISOU 4601 CA TYR B 6 22458 17592 19454 -934 18 -645 C ATOM 4602 C TYR B 6 50.552 45.402 2.444 1.00151.01 C ANISOU 4602 C TYR B 6 21768 16427 19183 -1193 -213 -723 C ATOM 4603 O TYR B 6 50.766 45.480 1.231 1.00145.13 O ANISOU 4603 O TYR B 6 20940 15498 18705 -1385 -239 -430 O ATOM 4604 CB TYR B 6 49.056 44.008 3.836 1.00148.76 C ANISOU 4604 CB TYR B 6 21615 16531 18377 -621 204 -865 C ATOM 4605 CG TYR B 6 48.551 42.625 4.157 1.00142.53 C ANISOU 4605 CG TYR B 6 20814 16098 17245 -343 496 -703 C ATOM 4606 CD1 TYR B 6 48.665 41.590 3.236 1.00138.81 C ANISOU 4606 CD1 TYR B 6 20227 15777 16738 -359 659 -277 C ATOM 4607 CD2 TYR B 6 47.946 42.355 5.381 1.00143.66 C ANISOU 4607 CD2 TYR B 6 21063 16423 17099 -63 610 -978 C ATOM 4608 CE1 TYR B 6 48.192 40.318 3.523 1.00136.26 C ANISOU 4608 CE1 TYR B 6 19893 15778 16101 -103 928 -127 C ATOM 4609 CE2 TYR B 6 47.471 41.087 5.683 1.00141.14 C ANISOU 4609 CE2 TYR B 6 20734 16429 16465 195 879 -831 C ATOM 4610 CZ TYR B 6 47.597 40.070 4.750 1.00137.44 C ANISOU 4610 CZ TYR B 6 20147 16106 15967 174 1037 -405 C ATOM 4611 OH TYR B 6 47.127 38.805 5.042 1.00134.91 O ANISOU 4611 OH TYR B 6 19816 16110 15335 429 1304 -257 O ATOM 4612 N TYR B 7 50.424 46.464 3.242 1.00150.46 N ANISOU 4612 N TYR B 7 21811 16177 19181 -1195 -380 -1125 N ATOM 4613 CA TYR B 7 50.477 47.835 2.752 1.00155.24 C ANISOU 4613 CA TYR B 7 22455 16337 20191 -1419 -607 -1260 C ATOM 4614 C TYR B 7 51.661 48.077 1.829 1.00159.08 C ANISOU 4614 C TYR B 7 22799 16779 20863 -1752 -798 -1028 C ATOM 4615 O TYR B 7 51.530 48.729 0.791 1.00156.75 O ANISOU 4615 O TYR B 7 22490 16123 20946 -1932 -873 -900 O ATOM 4616 CB TYR B 7 50.544 48.793 3.942 1.00156.91 C ANISOU 4616 CB TYR B 7 22782 16486 20350 -1392 -791 -1731 C ATOM 4617 CG TYR B 7 49.314 48.782 4.829 1.00157.46 C ANISOU 4617 CG TYR B 7 23009 16524 20295 -1080 -628 -1998 C ATOM 4618 CD1 TYR B 7 48.033 48.807 4.285 1.00155.73 C ANISOU 4618 CD1 TYR B 7 22865 16029 20276 -941 -447 -1920 C ATOM 4619 CD2 TYR B 7 49.435 48.739 6.222 1.00159.85 C ANISOU 4619 CD2 TYR B 7 23386 17075 20276 -922 -656 -2328 C ATOM 4620 CE1 TYR B 7 46.901 48.803 5.098 1.00156.38 C ANISOU 4620 CE1 TYR B 7 23091 16080 20248 -653 -297 -2164 C ATOM 4621 CE2 TYR B 7 48.308 48.732 7.048 1.00160.53 C ANISOU 4621 CE2 TYR B 7 23617 17132 20245 -632 -506 -2575 C ATOM 4622 CZ TYR B 7 47.041 48.762 6.478 1.00158.91 C ANISOU 4622 CZ TYR B 7 23482 16649 20248 -499 -325 -2490 C ATOM 4623 OH TYR B 7 45.907 48.753 7.272 1.00165.65 O ANISOU 4623 OH TYR B 7 24478 17467 20994 -211 -171 -2727 O ATOM 4624 N GLU B 8 52.827 47.544 2.190 1.00184.80 N ANISOU 4624 N GLU B 8 25951 20406 23859 -1837 -875 -966 N ATOM 4625 CA GLU B 8 54.056 47.889 1.485 1.00186.12 C ANISOU 4625 CA GLU B 8 25990 20541 24188 -2162 -1091 -803 C ATOM 4626 C GLU B 8 54.192 47.187 0.137 1.00184.76 C ANISOU 4626 C GLU B 8 25693 20364 24144 -2267 -972 -332 C ATOM 4627 O GLU B 8 54.768 47.766 -0.792 1.00188.83 O ANISOU 4627 O GLU B 8 26136 20655 24957 -2538 -1131 -185 O ATOM 4628 CB GLU B 8 55.271 47.576 2.355 1.00182.25 C ANISOU 4628 CB GLU B 8 25428 20446 23374 -2218 -1220 -905 C ATOM 4629 CG GLU B 8 55.536 48.613 3.441 1.00182.24 C ANISOU 4629 CG GLU B 8 25522 20370 23351 -2248 -1448 -1356 C ATOM 4630 CD GLU B 8 56.816 48.327 4.213 1.00179.99 C ANISOU 4630 CD GLU B 8 25156 20465 22767 -2331 -1591 -1434 C ATOM 4631 OE1 GLU B 8 57.478 47.314 3.891 1.00174.54 O ANISOU 4631 OE1 GLU B 8 24335 20094 21888 -2362 -1508 -1133 O ATOM 4632 OE2 GLU B 8 57.162 49.107 5.135 1.00183.14 O ANISOU 4632 OE2 GLU B 8 25622 20843 23118 -2364 -1787 -1792 O ATOM 4633 N ILE B 9 53.682 45.960 -0.005 1.00176.98 N ANISOU 4633 N ILE B 9 24681 19617 22945 -2061 -697 -89 N ATOM 4634 CA ILE B 9 53.806 45.296 -1.300 1.00165.75 C ANISOU 4634 CA ILE B 9 23144 18185 21648 -2162 -584 361 C ATOM 4635 C ILE B 9 52.904 45.969 -2.331 1.00160.47 C ANISOU 4635 C ILE B 9 22532 17039 21401 -2218 -559 449 C ATOM 4636 O ILE B 9 53.247 46.039 -3.518 1.00159.06 O ANISOU 4636 O ILE B 9 22265 16698 21473 -2423 -599 744 O ATOM 4637 CB ILE B 9 53.531 43.783 -1.167 1.00154.54 C ANISOU 4637 CB ILE B 9 21680 17160 19879 -1929 -300 600 C ATOM 4638 CG1 ILE B 9 52.103 43.540 -0.658 1.00150.14 C ANISOU 4638 CG1 ILE B 9 20980 16667 19400 -2070 -222 1072 C ATOM 4639 CG2 ILE B 9 54.559 43.101 -0.275 1.00148.25 C ANISOU 4639 CG2 ILE B 9 21011 16277 19041 -1626 -62 517 C ATOM 4640 CD1 ILE B 9 51.678 42.081 -0.704 1.00146.89 C ANISOU 4640 CD1 ILE B 9 20435 16344 19031 -2372 -450 1178 C ATOM 4641 N LEU B 10 51.760 46.501 -1.903 1.00142.65 N ANISOU 4641 N LEU B 10 20422 14544 19236 -2043 -499 193 N ATOM 4642 CA LEU B 10 50.983 47.364 -2.782 1.00142.49 C ANISOU 4642 CA LEU B 10 20464 14036 19640 -2123 -525 214 C ATOM 4643 C LEU B 10 51.541 48.779 -2.812 1.00145.85 C ANISOU 4643 C LEU B 10 20910 14152 20353 -2377 -832 -21 C ATOM 4644 O LEU B 10 51.393 49.479 -3.820 1.00145.53 O ANISOU 4644 O LEU B 10 20864 13738 20694 -2555 -913 89 O ATOM 4645 CB LEU B 10 49.515 47.391 -2.349 1.00142.30 C ANISOU 4645 CB LEU B 10 20589 13865 19615 -1837 -338 40 C ATOM 4646 CG LEU B 10 48.593 46.291 -2.885 1.00138.43 C ANISOU 4646 CG LEU B 10 20091 13453 19051 -1630 -28 341 C ATOM 4647 CD1 LEU B 10 49.011 44.918 -2.395 1.00136.59 C ANISOU 4647 CD1 LEU B 10 19782 13733 18385 -1481 134 496 C ATOM 4648 CD2 LEU B 10 47.142 46.569 -2.537 1.00138.66 C ANISOU 4648 CD2 LEU B 10 20274 13255 19155 -1386 117 144 C ATOM 4649 N GLY B 11 52.185 49.208 -1.729 1.00175.90 N ANISOU 4649 N GLY B 11 24553 22769 19511 -378 -1580 -3998 N ATOM 4650 CA GLY B 11 52.732 50.546 -1.635 1.00178.81 C ANISOU 4650 CA GLY B 11 24819 22854 20265 -537 -1239 -4155 C ATOM 4651 C GLY B 11 51.678 51.587 -1.325 1.00180.20 C ANISOU 4651 C GLY B 11 25002 22649 20818 -483 -1055 -3835 C ATOM 4652 O GLY B 11 51.330 52.398 -2.188 1.00182.09 O ANISOU 4652 O GLY B 11 25262 22664 21260 -609 -873 -3441 O ATOM 4653 N VAL B 12 51.162 51.580 -0.095 1.00179.31 N ANISOU 4653 N VAL B 12 24870 22456 20802 -295 -1098 -3999 N ATOM 4654 CA VAL B 12 50.075 52.465 0.297 1.00180.33 C ANISOU 4654 CA VAL B 12 25012 22239 21268 -214 -953 -3698 C ATOM 4655 C VAL B 12 50.457 53.181 1.588 1.00181.31 C ANISOU 4655 C VAL B 12 25023 22193 21674 -174 -780 -4156 C ATOM 4656 O VAL B 12 51.346 52.753 2.329 1.00180.53 O ANISOU 4656 O VAL B 12 24856 22280 21457 -150 -842 -4684 O ATOM 4657 CB VAL B 12 48.741 51.699 0.458 1.00178.04 C ANISOU 4657 CB VAL B 12 24836 22001 20811 6 -1205 -3318 C ATOM 4658 CG1 VAL B 12 48.755 50.854 1.715 1.00175.72 C ANISOU 4658 CG1 VAL B 12 24527 21896 20343 212 -1417 -3707 C ATOM 4659 CG2 VAL B 12 47.549 52.652 0.446 1.00179.36 C ANISOU 4659 CG2 VAL B 12 25035 21803 21312 48 -1045 -2865 C ATOM 4660 N SER B 13 49.764 54.292 1.849 1.00194.54 N ANISOU 4660 N SER B 13 26681 23508 23728 -168 -559 -3943 N ATOM 4661 CA SER B 13 50.063 55.168 2.977 1.00194.99 C ANISOU 4661 CA SER B 13 26631 23348 24107 -151 -351 -4321 C ATOM 4662 C SER B 13 49.795 54.527 4.335 1.00195.86 C ANISOU 4662 C SER B 13 26731 23565 24124 79 -532 -4633 C ATOM 4663 O SER B 13 50.214 55.094 5.350 1.00200.34 O ANISOU 4663 O SER B 13 27202 24009 24908 97 -389 -5034 O ATOM 4664 CB SER B 13 49.247 56.458 2.859 1.00189.79 C ANISOU 4664 CB SER B 13 25972 22278 23861 -186 -90 -3953 C ATOM 4665 OG SER B 13 49.189 56.909 1.517 1.00188.20 O ANISOU 4665 OG SER B 13 25811 21986 23712 -363 29 -3541 O ATOM 4666 N LYS B 14 49.111 53.381 4.377 1.00179.63 N ANISOU 4666 N LYS B 14 24769 21727 21753 251 -837 -4459 N ATOM 4667 CA LYS B 14 48.662 52.637 5.552 1.00177.31 C ANISOU 4667 CA LYS B 14 24489 21551 21330 488 -1050 -4663 C ATOM 4668 C LYS B 14 47.422 53.265 6.188 1.00177.63 C ANISOU 4668 C LYS B 14 24552 21288 21649 633 -976 -4387 C ATOM 4669 O LYS B 14 46.808 52.638 7.053 1.00175.62 O ANISOU 4669 O LYS B 14 24330 21111 21287 844 -1165 -4443 O ATOM 4670 CB LYS B 14 49.747 52.471 6.637 1.00176.98 C ANISOU 4670 CB LYS B 14 24340 21641 21263 508 -1044 -5343 C ATOM 4671 CG LYS B 14 51.033 51.782 6.175 1.00176.48 C ANISOU 4671 CG LYS B 14 24246 21899 20911 382 -1131 -5685 C ATOM 4672 CD LYS B 14 51.973 51.529 7.365 1.00175.86 C ANISOU 4672 CD LYS B 14 24067 21958 20793 436 -1154 -6349 C ATOM 4673 CE LYS B 14 51.250 50.815 8.519 1.00173.48 C ANISOU 4673 CE LYS B 14 23797 21736 20380 697 -1374 -6451 C ATOM 4674 NZ LYS B 14 51.584 49.362 8.641 1.00170.68 N ANISOU 4674 NZ LYS B 14 23485 21783 19582 800 -1697 -6661 N ATOM 4675 N THR B 15 47.044 54.484 5.814 1.00180.07 N ANISOU 4675 N THR B 15 24846 21257 22316 530 -706 -4101 N ATOM 4676 CA THR B 15 45.788 55.066 6.254 1.00180.39 C ANISOU 4676 CA THR B 15 24921 21009 22609 661 -641 -3767 C ATOM 4677 C THR B 15 44.923 55.504 5.078 1.00181.43 C ANISOU 4677 C THR B 15 25138 20967 22832 587 -570 -3126 C ATOM 4678 O THR B 15 43.821 56.020 5.295 1.00181.81 O ANISOU 4678 O THR B 15 25223 20766 23092 684 -510 -2785 O ATOM 4679 CB THR B 15 46.044 56.257 7.199 1.00182.43 C ANISOU 4679 CB THR B 15 25070 20971 23276 637 -359 -4066 C ATOM 4680 OG1 THR B 15 47.196 55.987 8.012 1.00182.06 O ANISOU 4680 OG1 THR B 15 24927 21094 23154 627 -371 -4699 O ATOM 4681 CG2 THR B 15 44.845 56.502 8.119 1.00181.86 C ANISOU 4681 CG2 THR B 15 25024 20692 23384 842 -376 -3899 C ATOM 4682 N ALA B 16 45.384 55.303 3.845 1.00181.88 N ANISOU 4682 N ALA B 16 25227 21150 22731 422 -578 -2950 N ATOM 4683 CA ALA B 16 44.592 55.654 2.676 1.00182.79 C ANISOU 4683 CA ALA B 16 25425 21120 22907 349 -524 -2340 C ATOM 4684 C ALA B 16 43.304 54.840 2.648 1.00180.53 C ANISOU 4684 C ALA B 16 25257 20910 22425 548 -783 -1925 C ATOM 4685 O ALA B 16 43.230 53.732 3.186 1.00177.99 O ANISOU 4685 O ALA B 16 24969 20851 21809 705 -1054 -2097 O ATOM 4686 CB ALA B 16 45.401 55.420 1.401 1.00183.37 C ANISOU 4686 CB ALA B 16 25511 21364 22796 146 -521 -2273 C ATOM 4687 N GLU B 17 42.279 55.395 2.008 1.00181.46 N ANISOU 4687 N GLU B 17 25441 20797 22709 541 -700 -1372 N ATOM 4688 CA GLU B 17 40.954 54.797 2.078 1.00179.57 C ANISOU 4688 CA GLU B 17 25309 20574 22346 736 -912 -964 C ATOM 4689 C GLU B 17 40.796 53.692 1.025 1.00177.81 C ANISOU 4689 C GLU B 17 25190 20640 21730 728 -1167 -666 C ATOM 4690 O GLU B 17 41.607 53.547 0.096 1.00181.80 O ANISOU 4690 O GLU B 17 25690 21285 22100 555 -1147 -692 O ATOM 4691 CB GLU B 17 39.882 55.890 1.939 1.00181.32 C ANISOU 4691 CB GLU B 17 25552 20412 22927 744 -710 -510 C ATOM 4692 CG GLU B 17 38.388 55.497 2.192 1.00179.67 C ANISOU 4692 CG GLU B 17 25443 20148 22674 960 -885 -85 C ATOM 4693 CD GLU B 17 38.069 55.014 3.622 1.00177.81 C ANISOU 4693 CD GLU B 17 25190 19972 22399 1187 -1032 -393 C ATOM 4694 OE1 GLU B 17 38.878 54.261 4.215 1.00176.39 O ANISOU 4694 OE1 GLU B 17 24970 20050 22000 1228 -1173 -868 O ATOM 4695 OE2 GLU B 17 36.996 55.395 4.155 1.00177.78 O ANISOU 4695 OE2 GLU B 17 25213 19752 22584 1326 -1006 -156 O ATOM 4696 N GLU B 18 39.733 52.893 1.211 1.00158.76 N ANISOU 4696 N GLU B 18 26242 15214 18864 -4838 -1499 829 N ATOM 4697 CA GLU B 18 39.458 51.743 0.354 1.00158.94 C ANISOU 4697 CA GLU B 18 26220 15639 18531 -4525 -1336 781 C ATOM 4698 C GLU B 18 39.514 52.097 -1.132 1.00161.75 C ANISOU 4698 C GLU B 18 26311 16298 18848 -4357 -448 1006 C ATOM 4699 O GLU B 18 40.003 51.303 -1.946 1.00158.88 O ANISOU 4699 O GLU B 18 25582 16148 18636 -4155 -247 918 O ATOM 4700 CB GLU B 18 38.092 51.167 0.724 1.00150.68 C ANISOU 4700 CB GLU B 18 25841 14805 16607 -4398 -1627 814 C ATOM 4701 CG GLU B 18 37.643 49.954 -0.085 1.00158.00 C ANISOU 4701 CG GLU B 18 26817 16154 17063 -4078 -1507 774 C ATOM 4702 CD GLU B 18 36.298 49.429 0.383 1.00164.41 C ANISOU 4702 CD GLU B 18 28297 17145 17025 -3979 -1843 810 C ATOM 4703 OE1 GLU B 18 35.730 50.026 1.326 1.00164.79 O ANISOU 4703 OE1 GLU B 18 28761 16989 16861 -4156 -2152 868 O ATOM 4704 OE2 GLU B 18 35.809 48.424 -0.186 1.00168.35 O ANISOU 4704 OE2 GLU B 18 28911 17988 17068 -3726 -1799 783 O ATOM 4705 N ARG B 19 39.032 53.288 -1.506 1.00143.00 N ANISOU 4705 N ARG B 19 24112 13943 16278 -4437 95 1296 N ATOM 4706 CA ARG B 19 38.949 53.631 -2.924 1.00139.58 C ANISOU 4706 CA ARG B 19 23487 13821 15724 -4268 949 1528 C ATOM 4707 C ARG B 19 40.326 53.600 -3.584 1.00141.97 C ANISOU 4707 C ARG B 19 23059 14058 16824 -4260 1234 1437 C ATOM 4708 O ARG B 19 40.469 53.139 -4.726 1.00142.73 O ANISOU 4708 O ARG B 19 22901 14460 16869 -4030 1717 1482 O ATOM 4709 CB ARG B 19 38.291 55.005 -3.097 1.00135.81 C ANISOU 4709 CB ARG B 19 23301 13323 14979 -4390 1444 1846 C ATOM 4710 CG ARG B 19 38.179 55.475 -4.554 1.00136.75 C ANISOU 4710 CG ARG B 19 23235 13751 14971 -4233 2354 2106 C ATOM 4711 CD ARG B 19 37.888 56.982 -4.658 1.00137.28 C ANISOU 4711 CD ARG B 19 23441 13702 15015 -4409 2833 2392 C ATOM 4712 NE ARG B 19 38.963 57.804 -4.097 1.00141.60 N ANISOU 4712 NE ARG B 19 23617 13829 16357 -4688 2705 2324 N ATOM 4713 CZ ARG B 19 38.865 59.112 -3.862 1.00142.46 C ANISOU 4713 CZ ARG B 19 23841 13727 16561 -4901 2938 2514 C ATOM 4714 NH1 ARG B 19 37.734 59.757 -4.130 1.00139.25 N ANISOU 4714 NH1 ARG B 19 23913 13492 15505 -4865 3315 2787 N ATOM 4715 NH2 ARG B 19 39.897 59.777 -3.355 1.00146.56 N ANISOU 4715 NH2 ARG B 19 24000 13862 17824 -5154 2790 2436 N ATOM 4716 N GLU B 20 41.355 54.064 -2.863 1.00175.73 N ANISOU 4716 N GLU B 20 26991 17933 21844 -4510 925 1307 N ATOM 4717 CA GLU B 20 42.705 54.111 -3.417 1.00180.14 C ANISOU 4717 CA GLU B 20 26842 18399 23205 -4527 1177 1231 C ATOM 4718 C GLU B 20 43.315 52.713 -3.515 1.00181.20 C ANISOU 4718 C GLU B 20 26660 18632 23554 -4345 835 956 C ATOM 4719 O GLU B 20 43.893 52.350 -4.549 1.00180.30 O ANISOU 4719 O GLU B 20 26113 18716 23678 -4166 1276 961 O ATOM 4720 CB GLU B 20 43.581 55.032 -2.565 1.00176.97 C ANISOU 4720 CB GLU B 20 26193 17533 23513 -4860 918 1182 C ATOM 4721 CG GLU B 20 44.924 55.421 -3.210 1.00185.04 C ANISOU 4721 CG GLU B 20 26493 18446 25367 -4915 1306 1183 C ATOM 4722 CD GLU B 20 45.985 54.334 -3.073 1.00187.48 C ANISOU 4722 CD GLU B 20 26313 18691 26230 -4847 901 890 C ATOM 4723 OE1 GLU B 20 46.006 53.657 -2.021 1.00187.80 O ANISOU 4723 OE1 GLU B 20 26506 18560 26287 -4914 152 656 O ATOM 4724 OE2 GLU B 20 46.770 54.135 -4.031 1.00189.65 O ANISOU 4724 OE2 GLU B 20 26060 19096 26900 -4715 1339 898 O ATOM 4725 N ILE B 21 43.201 51.909 -2.447 1.00149.99 N ANISOU 4725 N ILE B 21 22923 14543 19523 -4385 50 715 N ATOM 4726 CA ILE B 21 43.792 50.569 -2.461 1.00150.84 C ANISOU 4726 CA ILE B 21 22742 14725 19845 -4222 -318 442 C ATOM 4727 C ILE B 21 43.200 49.743 -3.602 1.00148.61 C ANISOU 4727 C ILE B 21 22549 14908 19008 -3880 105 509 C ATOM 4728 O ILE B 21 43.855 48.835 -4.130 1.00150.48 O ANISOU 4728 O ILE B 21 22400 15271 19503 -3701 129 359 O ATOM 4729 CB ILE B 21 43.621 49.875 -1.085 1.00148.68 C ANISOU 4729 CB ILE B 21 22759 14238 19496 -4323 -1239 188 C ATOM 4730 CG1 ILE B 21 44.432 50.608 -0.006 1.00151.35 C ANISOU 4730 CG1 ILE B 21 22627 14498 20382 -4257 -1669 -117 C ATOM 4731 CG2 ILE B 21 43.996 48.399 -1.155 1.00142.92 C ANISOU 4731 CG2 ILE B 21 22699 13763 17840 -4174 -1422 232 C ATOM 4732 CD1 ILE B 21 44.130 50.172 1.428 1.00147.91 C ANISOU 4732 CD1 ILE B 21 22446 14314 19440 -4014 -2046 -291 C ATOM 4733 N ARG B 22 41.965 50.052 -4.016 1.00144.70 N ANISOU 4733 N ARG B 22 22558 14673 17749 -3784 455 741 N ATOM 4734 CA ARG B 22 41.366 49.361 -5.155 1.00147.00 C ANISOU 4734 CA ARG B 22 22948 15410 17493 -3470 904 833 C ATOM 4735 C ARG B 22 42.052 49.771 -6.454 1.00160.09 C ANISOU 4735 C ARG B 22 24101 17210 19517 -3369 1691 976 C ATOM 4736 O ARG B 22 42.351 48.925 -7.305 1.00161.67 O ANISOU 4736 O ARG B 22 24043 17656 19728 -3128 1916 910 O ATOM 4737 CB ARG B 22 39.862 49.646 -5.203 1.00137.53 C ANISOU 4737 CB ARG B 22 22426 14436 15394 -3415 1056 1058 C ATOM 4738 CG ARG B 22 39.119 48.933 -6.317 1.00138.33 C ANISOU 4738 CG ARG B 22 22700 15002 14858 -3101 1483 1165 C ATOM 4739 CD ARG B 22 37.620 49.136 -6.166 1.00139.07 C ANISOU 4739 CD ARG B 22 23489 15287 14065 -3067 1503 1364 C ATOM 4740 NE ARG B 22 36.878 48.648 -7.324 1.00144.88 N ANISOU 4740 NE ARG B 22 24390 16470 14186 -2787 2006 1518 N ATOM 4741 CZ ARG B 22 36.358 47.426 -7.421 1.00141.34 C ANISOU 4741 CZ ARG B 22 24170 16271 13262 -2576 1735 1404 C ATOM 4742 NH1 ARG B 22 36.497 46.556 -6.421 1.00132.23 N ANISOU 4742 NH1 ARG B 22 23101 14964 12176 -2609 962 1131 N ATOM 4743 NH2 ARG B 22 35.695 47.074 -8.519 1.00143.63 N ANISOU 4743 NH2 ARG B 22 24607 16962 13005 -2334 2234 1565 N ATOM 4744 N LYS B 23 42.310 51.074 -6.619 1.00148.60 N ANISOU 4744 N LYS B 23 22502 15597 18362 -3551 2118 1173 N ATOM 4745 CA LYS B 23 43.072 51.560 -7.768 1.00152.57 C ANISOU 4745 CA LYS B 23 22483 16187 19300 -3488 2842 1304 C ATOM 4746 C LYS B 23 44.432 50.871 -7.851 1.00156.94 C ANISOU 4746 C LYS B 23 22398 16622 20611 -3450 2662 1063 C ATOM 4747 O LYS B 23 44.871 50.453 -8.928 1.00158.89 O ANISOU 4747 O LYS B 23 22287 17096 20989 -3238 3125 1081 O ATOM 4748 CB LYS B 23 43.247 53.085 -7.679 1.00154.58 C ANISOU 4748 CB LYS B 23 22671 16211 19851 -3740 3190 1516 C ATOM 4749 CG LYS B 23 41.974 53.910 -7.440 1.00150.59 C ANISOU 4749 CG LYS B 23 22790 15758 18670 -3822 3325 1755 C ATOM 4750 CD LYS B 23 42.315 55.336 -6.982 1.00152.91 C ANISOU 4750 CD LYS B 23 23009 15714 19376 -4125 3443 1889 C ATOM 4751 CE LYS B 23 41.068 56.202 -6.794 1.00149.14 C ANISOU 4751 CE LYS B 23 23140 15288 18237 -4198 3623 2142 C ATOM 4752 NZ LYS B 23 40.288 56.378 -8.063 1.00147.28 N ANISOU 4752 NZ LYS B 23 23059 15462 17440 -3978 4385 2410 N ATOM 4753 N ALA B 24 45.113 50.749 -6.710 1.00158.57 N ANISOU 4753 N ALA B 24 22457 16469 21323 -3654 1988 840 N ATOM 4754 CA ALA B 24 46.430 50.124 -6.692 1.00162.81 C ANISOU 4754 CA ALA B 24 22385 16867 22610 -3638 1774 612 C ATOM 4755 C ALA B 24 46.325 48.645 -7.034 1.00161.30 C ANISOU 4755 C ALA B 24 22198 16943 22144 -3347 1582 428 C ATOM 4756 O ALA B 24 47.152 48.110 -7.779 1.00164.38 O ANISOU 4756 O ALA B 24 22100 17436 22921 -3186 1829 355 O ATOM 4757 CB ALA B 24 47.091 50.326 -5.324 1.00164.55 C ANISOU 4757 CB ALA B 24 22500 16639 23381 -3932 1056 419 C ATOM 4758 N TYR B 25 45.305 47.967 -6.502 1.00156.56 N ANISOU 4758 N TYR B 25 22154 16461 20872 -3274 1145 356 N ATOM 4759 CA TYR B 25 45.141 46.547 -6.795 1.00154.88 C ANISOU 4759 CA TYR B 25 21987 16504 20356 -3001 939 183 C ATOM 4760 C TYR B 25 44.965 46.307 -8.292 1.00155.08 C ANISOU 4760 C TYR B 25 21892 16924 20108 -2714 1694 340 C ATOM 4761 O TYR B 25 45.606 45.421 -8.870 1.00157.07 O ANISOU 4761 O TYR B 25 21783 17303 20595 -2515 1765 205 O ATOM 4762 CB TYR B 25 43.958 45.981 -6.006 1.00149.50 C ANISOU 4762 CB TYR B 25 21968 15896 18938 -2980 393 120 C ATOM 4763 CG TYR B 25 43.501 44.620 -6.485 1.00146.96 C ANISOU 4763 CG TYR B 25 21807 15910 18121 -2676 305 9 C ATOM 4764 CD1 TYR B 25 44.318 43.497 -6.342 1.00148.85 C ANISOU 4764 CD1 TYR B 25 21705 16111 18740 -2569 -85 -270 C ATOM 4765 CD2 TYR B 25 42.253 44.450 -7.064 1.00142.70 C ANISOU 4765 CD2 TYR B 25 21766 15721 16734 -2499 600 184 C ATOM 4766 CE1 TYR B 25 43.898 42.245 -6.773 1.00146.55 C ANISOU 4766 CE1 TYR B 25 21573 16120 17988 -2292 -172 -374 C ATOM 4767 CE2 TYR B 25 41.820 43.204 -7.498 1.00140.37 C ANISOU 4767 CE2 TYR B 25 21633 15731 15972 -2228 510 87 C ATOM 4768 CZ TYR B 25 42.648 42.102 -7.350 1.00142.32 C ANISOU 4768 CZ TYR B 25 21541 15929 16604 -2125 123 -196 C ATOM 4769 OH TYR B 25 42.230 40.858 -7.779 1.00140.08 O ANISOU 4769 OH TYR B 25 21423 15940 15859 -1855 29 -296 O ATOM 4770 N LYS B 26 44.113 47.106 -8.942 1.00154.91 N ANISOU 4770 N LYS B 26 22166 17096 19597 -2689 2276 629 N ATOM 4771 CA LYS B 26 43.814 46.871 -10.352 1.00152.85 C ANISOU 4771 CA LYS B 26 21858 17227 18993 -2414 2984 790 C ATOM 4772 C LYS B 26 45.062 47.019 -11.219 1.00158.18 C ANISOU 4772 C LYS B 26 21838 17880 20382 -2354 3469 790 C ATOM 4773 O LYS B 26 45.285 46.222 -12.140 1.00159.00 O ANISOU 4773 O LYS B 26 21737 18239 20436 -2092 3758 751 O ATOM 4774 CB LYS B 26 42.701 47.816 -10.822 1.00149.97 C ANISOU 4774 CB LYS B 26 21927 17043 18013 -2429 3511 1113 C ATOM 4775 CG LYS B 26 41.359 47.579 -10.151 1.00144.40 C ANISOU 4775 CG LYS B 26 21929 16441 16494 -2427 3124 1144 C ATOM 4776 CD LYS B 26 40.321 48.554 -10.674 1.00141.49 C ANISOU 4776 CD LYS B 26 21945 16388 15428 -2323 3760 1461 C ATOM 4777 CE LYS B 26 39.141 48.666 -9.725 1.00135.88 C ANISOU 4777 CE LYS B 26 21922 15844 13864 -2266 3402 1492 C ATOM 4778 NZ LYS B 26 38.432 47.358 -9.604 1.00133.12 N ANISOU 4778 NZ LYS B 26 21912 15857 12810 -2115 4044 1792 N ATOM 4779 N ARG B 27 45.891 48.031 -10.942 1.00161.90 N ANISOU 4779 N ARG B 27 21942 18046 21525 -2592 3566 836 N ATOM 4780 CA ARG B 27 47.100 48.221 -11.742 1.00167.10 C ANISOU 4780 CA ARG B 27 21927 18674 22890 -2545 4026 848 C ATOM 4781 C ARG B 27 48.142 47.153 -11.422 1.00169.81 C ANISOU 4781 C ARG B 27 21843 18899 23778 -2478 3557 547 C ATOM 4782 O ARG B 27 48.882 46.709 -12.310 1.00172.84 O ANISOU 4782 O ARG B 27 21773 19415 24485 -2291 3919 518 O ATOM 4783 CB ARG B 27 47.671 49.628 -11.526 1.00170.29 C ANISOU 4783 CB ARG B 27 22068 18784 23850 -2828 4258 993 C ATOM 4784 CG ARG B 27 48.721 50.069 -12.545 1.00171.05 C ANISOU 4784 CG ARG B 27 22171 18454 24366 -3140 3543 839 C ATOM 4785 CD ARG B 27 48.084 50.686 -13.788 1.00174.96 C ANISOU 4785 CD ARG B 27 22317 18659 25500 -3405 3810 973 C ATOM 4786 NE ARG B 27 46.875 51.443 -13.459 1.00180.12 N ANISOU 4786 NE ARG B 27 22272 19301 26864 -3337 4198 959 N ATOM 4787 CZ ARG B 27 46.876 52.712 -13.059 1.00183.79 C ANISOU 4787 CZ ARG B 27 22251 19530 28050 -3408 3797 741 C ATOM 4788 NH1 ARG B 27 45.723 53.323 -12.784 1.00188.43 N ANISOU 4788 NH1 ARG B 27 22212 20131 29253 -3331 4207 757 N ATOM 4789 NH2 ARG B 27 48.028 53.372 -12.933 1.00182.84 N ANISOU 4789 NH2 ARG B 27 22271 19163 28037 -3553 2988 513 N ATOM 4790 N LEU B 28 48.213 46.725 -10.160 1.00168.78 N ANISOU 4790 N LEU B 28 21853 18522 23754 -2625 2753 323 N ATOM 4791 CA LEU B 28 49.121 45.640 -9.798 1.00170.96 C ANISOU 4791 CA LEU B 28 21768 18695 24493 -2556 2261 30 C ATOM 4792 C LEU B 28 48.633 44.307 -10.359 1.00168.42 C ANISOU 4792 C LEU B 28 21633 18718 23640 -2228 2238 -73 C ATOM 4793 O LEU B 28 49.436 43.499 -10.846 1.00171.10 O ANISOU 4793 O LEU B 28 21553 19128 24330 -2050 2290 -211 O ATOM 4794 CB LEU B 28 49.274 45.576 -8.278 1.00170.37 C ANISOU 4794 CB LEU B 28 21822 18263 24647 -2810 1405 -174 C ATOM 4795 CG LEU B 28 49.993 46.741 -7.594 1.00173.60 C ANISOU 4795 CG LEU B 28 21968 18276 25717 -3147 1307 -131 C ATOM 4796 CD1 LEU B 28 50.030 46.532 -6.092 1.00172.50 C ANISOU 4796 CD1 LEU B 28 22022 17812 25708 -3371 424 -346 C ATOM 4797 CD2 LEU B 28 51.405 46.900 -8.151 1.00179.45 C ANISOU 4797 CD2 LEU B 28 21957 18909 27316 -3149 1621 -151 C ATOM 4798 N ALA B 29 47.319 44.064 -10.299 1.00163.29 N ANISOU 4798 N ALA B 29 21615 18286 22142 -2145 2164 -1 N ATOM 4799 CA ALA B 29 46.745 42.893 -10.952 1.00160.68 C ANISOU 4799 CA ALA B 29 21503 18313 21236 -1832 2226 -56 C ATOM 4800 C ALA B 29 47.069 42.882 -12.436 1.00163.03 C ANISOU 4800 C ALA B 29 21471 18884 21588 -1596 3031 88 C ATOM 4801 O ALA B 29 47.291 41.815 -13.017 1.00163.45 O ANISOU 4801 O ALA B 29 21388 19137 21577 -1341 3071 -32 O ATOM 4802 CB ALA B 29 45.232 42.856 -10.733 1.00154.92 C ANISOU 4802 CB ALA B 29 21506 17778 19579 -1804 2115 57 C ATOM 4803 N MET B 30 47.120 44.062 -13.058 1.00164.66 N ANISOU 4803 N MET B 30 21544 19097 21923 -1679 3675 344 N ATOM 4804 CA MET B 30 47.551 44.149 -14.449 1.00167.42 C ANISOU 4804 CA MET B 30 21524 19672 22416 -1476 4453 484 C ATOM 4805 C MET B 30 48.995 43.683 -14.595 1.00172.53 C ANISOU 4805 C MET B 30 21490 20174 23889 -1426 4403 301 C ATOM 4806 O MET B 30 49.313 42.868 -15.468 1.00173.77 O ANISOU 4806 O MET B 30 21428 20553 24046 -1158 4674 249 O ATOM 4807 CB MET B 30 47.389 45.582 -14.965 1.00168.38 C ANISOU 4807 CB MET B 30 21615 19785 22579 -1608 5106 787 C ATOM 4808 CG MET B 30 47.643 45.720 -16.459 1.00170.61 C ANISOU 4808 CG MET B 30 21597 20337 22890 -1388 5958 964 C ATOM 4809 SD MET B 30 46.334 44.947 -17.425 1.00165.93 S ANISOU 4809 SD MET B 30 21536 20235 21275 -1065 6294 1076 S ATOM 4810 CE MET B 30 44.963 46.037 -17.055 1.00161.46 C ANISOU 4810 CE MET B 30 21609 19696 20042 -1251 6385 1337 C ATOM 4811 N LYS B 31 49.875 44.162 -13.710 1.00175.51 N ANISOU 4811 N LYS B 31 21538 20176 24972 -1684 4030 199 N ATOM 4812 CA LYS B 31 51.309 43.920 -13.852 1.00180.81 C ANISOU 4812 CA LYS B 31 21518 20684 26498 -1671 4034 64 C ATOM 4813 C LYS B 31 51.658 42.450 -13.639 1.00180.78 C ANISOU 4813 C LYS B 31 21422 20731 26535 -1480 3546 -221 C ATOM 4814 O LYS B 31 52.501 41.896 -14.357 1.00184.11 O ANISOU 4814 O LYS B 31 21379 21236 27338 -1290 3801 -286 O ATOM 4815 CB LYS B 31 52.080 44.811 -12.869 1.00183.69 C ANISOU 4815 CB LYS B 31 21604 20625 27566 -2017 3704 30 C ATOM 4816 CG LYS B 31 53.603 44.666 -12.915 1.00189.39 C ANISOU 4816 CG LYS B 31 21592 21143 29225 -2042 3675 -96 C ATOM 4817 CD LYS B 31 54.288 45.532 -11.852 1.00191.92 C ANISOU 4817 CD LYS B 31 21689 21036 30196 -2403 3286 -132 C ATOM 4818 CE LYS B 31 55.782 45.672 -12.146 1.00197.99 C ANISOU 4818 CE LYS B 31 21692 21634 31903 -2435 3462 -170 C ATOM 4819 NZ LYS B 31 56.012 46.239 -13.515 1.00200.40 N ANISOU 4819 NZ LYS B 31 21698 22147 32297 -2292 4364 70 N ATOM 4820 N TYR B 32 51.012 41.799 -12.672 1.00177.05 N ANISOU 4820 N TYR B 32 21392 20214 25665 -1520 2852 -390 N ATOM 4821 CA TYR B 32 51.432 40.487 -12.201 1.00177.20 C ANISOU 4821 CA TYR B 32 21312 20201 25816 -1403 2260 -687 C ATOM 4822 C TYR B 32 50.475 39.355 -12.555 1.00172.99 C ANISOU 4822 C TYR B 32 21239 20003 24488 -1128 2175 -749 C ATOM 4823 O TYR B 32 50.706 38.219 -12.122 1.00172.62 O ANISOU 4823 O TYR B 32 21174 19941 24473 -1025 1649 -999 O ATOM 4824 CB TYR B 32 51.629 40.514 -10.682 1.00176.75 C ANISOU 4824 CB TYR B 32 21334 19784 26040 -1678 1424 -878 C ATOM 4825 CG TYR B 32 52.956 41.091 -10.247 1.00181.91 C ANISOU 4825 CG TYR B 32 21384 20083 27650 -1896 1315 -936 C ATOM 4826 CD1 TYR B 32 54.151 40.541 -10.703 1.00186.37 C ANISOU 4826 CD1 TYR B 32 21336 20626 28851 -1767 1422 -1052 C ATOM 4827 CD2 TYR B 32 53.019 42.163 -9.362 1.00182.35 C ANISOU 4827 CD2 TYR B 32 21486 19823 27976 -2232 1087 -877 C ATOM 4828 CE1 TYR B 32 55.377 41.055 -10.301 1.00191.17 C ANISOU 4828 CE1 TYR B 32 21380 20911 30343 -1969 1313 -1098 C ATOM 4829 CE2 TYR B 32 54.238 42.683 -8.947 1.00187.12 C ANISOU 4829 CE2 TYR B 32 21540 20098 29459 -2442 966 -928 C ATOM 4830 CZ TYR B 32 55.415 42.124 -9.422 1.00191.52 C ANISOU 4830 CZ TYR B 32 21481 20646 30642 -2310 1080 -1036 C ATOM 4831 OH TYR B 32 56.633 42.633 -9.021 1.00196.33 O ANISOU 4831 OH TYR B 32 21534 20934 32131 -2519 961 -1077 O ATOM 4832 N HIS B 33 49.414 39.619 -13.316 1.00169.85 N ANISOU 4832 N HIS B 33 21250 19903 23383 -1009 2664 -530 N ATOM 4833 CA HIS B 33 48.486 38.557 -13.690 1.00165.88 C ANISOU 4833 CA HIS B 33 21191 19726 22111 -751 2599 -574 C ATOM 4834 C HIS B 33 49.205 37.537 -14.569 1.00168.53 C ANISOU 4834 C HIS B 33 21144 20233 22658 -457 2822 -693 C ATOM 4835 O HIS B 33 49.887 37.926 -15.529 1.00173.37 O ANISOU 4835 O HIS B 33 21318 20905 23650 -371 3452 -573 O ATOM 4836 CB HIS B 33 47.278 39.126 -14.441 1.00162.46 C ANISOU 4836 CB HIS B 33 21221 19584 20924 -682 3156 -287 C ATOM 4837 CG HIS B 33 46.047 38.265 -14.376 1.00157.22 C ANISOU 4837 CG HIS B 33 21177 19181 19377 -528 2896 -317 C ATOM 4838 ND1 HIS B 33 46.092 36.886 -14.367 1.00156.34 N ANISOU 4838 ND1 HIS B 33 21112 19192 19098 -318 2532 -540 N ATOM 4839 CD2 HIS B 33 44.734 38.598 -14.316 1.00152.60 C ANISOU 4839 CD2 HIS B 33 21194 18760 18029 -556 2948 -143 C ATOM 4840 CE1 HIS B 33 44.861 36.409 -14.300 1.00151.42 C ANISOU 4840 CE1 HIS B 33 21091 18793 17648 -228 2365 -504 C ATOM 4841 NE2 HIS B 33 44.019 37.426 -14.276 1.00149.08 N ANISOU 4841 NE2 HIS B 33 21136 18530 16977 -368 2617 -260 N ATOM 4842 N PRO B 34 49.096 36.237 -14.276 1.00166.91 N ANISOU 4842 N PRO B 34 21083 20105 22228 -297 2330 -924 N ATOM 4843 CA PRO B 34 49.595 35.239 -15.241 1.00168.88 C ANISOU 4843 CA PRO B 34 21057 20571 22539 17 2609 -1009 C ATOM 4844 C PRO B 34 48.960 35.383 -16.614 1.00167.83 C ANISOU 4844 C PRO B 34 21088 20803 21876 240 3394 -770 C ATOM 4845 O PRO B 34 49.673 35.407 -17.622 1.00171.41 O ANISOU 4845 O PRO B 34 21112 21350 22665 398 3962 -706 O ATOM 4846 CB PRO B 34 49.235 33.903 -14.571 1.00165.98 C ANISOU 4846 CB PRO B 34 20997 20243 21826 122 1897 -1271 C ATOM 4847 CG PRO B 34 48.137 34.253 -13.586 1.00161.29 C ANISOU 4847 CG PRO B 34 20992 19583 20706 -80 1438 -1238 C ATOM 4848 CD PRO B 34 48.541 35.600 -13.071 1.00163.33 C ANISOU 4848 CD PRO B 34 21043 19548 21468 -389 1503 -1121 C ATOM 4849 N ASP B 35 47.631 35.501 -16.671 1.00163.03 N ANISOU 4849 N ASP B 35 21093 20401 20448 252 3441 -628 N ATOM 4850 CA ASP B 35 46.857 35.670 -17.899 1.00161.38 C ANISOU 4850 CA ASP B 35 21127 20548 19643 443 4147 -385 C ATOM 4851 C ASP B 35 47.471 36.715 -18.821 1.00165.21 C ANISOU 4851 C ASP B 35 21179 21032 20562 426 4928 -166 C ATOM 4852 O ASP B 35 47.548 36.513 -20.039 1.00166.46 O ANISOU 4852 O ASP B 35 21206 21441 20598 662 5542 -61 O ATOM 4853 CB ASP B 35 45.411 36.057 -17.548 1.00156.02 C ANISOU 4853 CB ASP B 35 21130 19989 18161 346 4039 -229 C ATOM 4854 CG ASP B 35 44.556 36.390 -18.770 1.00154.22 C ANISOU 4854 CG ASP B 35 21169 20115 17313 508 4780 54 C ATOM 4855 OD1 ASP B 35 44.664 37.517 -19.310 1.00155.89 O ANISOU 4855 OD1 ASP B 35 21214 20319 17698 424 5370 285 O ATOM 4856 OD2 ASP B 35 43.729 35.539 -19.164 1.00150.98 O ANISOU 4856 OD2 ASP B 35 21158 19989 16217 712 4756 50 O ATOM 4857 N ARG B 36 47.910 37.835 -18.245 1.00167.12 N ANISOU 4857 N ARG B 36 21202 20987 21309 146 4907 -97 N ATOM 4858 CA ARG B 36 48.432 38.931 -19.055 1.00170.56 C ANISOU 4858 CA ARG B 36 21254 21408 22141 101 5636 128 C ATOM 4859 C ARG B 36 49.786 38.577 -19.660 1.00175.89 C ANISOU 4859 C ARG B 36 21254 22032 23545 238 5891 30 C ATOM 4860 O ARG B 36 49.962 38.616 -20.885 1.00177.67 O ANISOU 4860 O ARG B 36 21282 22477 23747 441 6577 167 O ATOM 4861 CB ARG B 36 48.526 40.208 -18.218 1.00171.11 C ANISOU 4861 CB ARG B 36 21292 21173 22548 -246 5505 222 C ATOM 4862 CG ARG B 36 49.158 41.353 -18.973 1.00174.96 C ANISOU 4862 CG ARG B 36 21348 21613 23514 -312 6215 440 C ATOM 4863 CD ARG B 36 48.766 42.698 -18.410 1.00174.02 C ANISOU 4863 CD ARG B 36 21408 21310 23403 -614 6248 619 C ATOM 4864 NE ARG B 36 49.147 43.778 -19.310 1.00177.02 N ANISOU 4864 NE ARG B 36 21462 21717 24079 -642 7019 865 N ATOM 4865 CZ ARG B 36 48.395 44.192 -20.327 1.00175.38 C ANISOU 4865 CZ ARG B 36 21484 21800 23352 -516 7683 1115 C ATOM 4866 NH1 ARG B 36 47.218 43.617 -20.566 1.00170.78 N ANISOU 4866 NH1 ARG B 36 21458 21505 21925 -357 7664 1157 N ATOM 4867 NH2 ARG B 36 48.817 45.182 -21.109 1.00178.35 N ANISOU 4867 NH2 ARG B 36 21533 22181 24050 -549 8366 1329 N ATOM 4868 N ASN B 37 50.760 38.221 -18.816 1.00178.54 N ANISOU 4868 N ASN B 37 21226 22079 24533 134 5345 -205 N ATOM 4869 CA ASN B 37 52.090 37.910 -19.335 1.00183.80 C ANISOU 4869 CA ASN B 37 21226 22678 25930 254 5567 -293 C ATOM 4870 C ASN B 37 52.132 36.528 -19.987 1.00183.58 C ANISOU 4870 C ASN B 37 21205 22899 25647 596 5583 -438 C ATOM 4871 O ASN B 37 52.822 36.339 -20.997 1.00186.99 O ANISOU 4871 O ASN B 37 21231 23447 26368 799 6107 -397 O ATOM 4872 CB ASN B 37 53.136 38.016 -18.222 1.00186.85 C ANISOU 4872 CB ASN B 37 21208 22671 27116 22 4986 -484 C ATOM 4873 CG ASN B 37 52.875 37.049 -17.089 1.00184.16 C ANISOU 4873 CG ASN B 37 21154 22225 26595 -15 4114 -755 C ATOM 4874 OD1 ASN B 37 53.127 35.848 -17.206 1.00184.36 O ANISOU 4874 OD1 ASN B 37 21116 22346 26589 201 3883 -949 O ATOM 4875 ND2 ASN B 37 52.365 37.571 -15.975 1.00181.64 N ANISOU 4875 ND2 ASN B 37 21158 21703 26153 -288 3622 -768 N ATOM 4876 N GLN B 38 51.407 35.552 -19.433 1.00179.66 N ANISOU 4876 N GLN B 38 21166 22485 24612 667 5021 -604 N ATOM 4877 CA GLN B 38 51.330 34.164 -19.903 1.00178.86 C ANISOU 4877 CA GLN B 38 21155 22609 24196 977 4930 -763 C ATOM 4878 C GLN B 38 52.629 33.428 -19.590 1.00182.99 C ANISOU 4878 C GLN B 38 21131 22937 25458 1032 4597 -1013 C ATOM 4879 O GLN B 38 52.775 32.251 -19.935 1.00183.09 O ANISOU 4879 O GLN B 38 21131 23094 25340 1287 4498 -1168 O ATOM 4880 CB GLN B 38 51.016 34.050 -21.409 1.00179.02 C ANISOU 4880 CB GLN B 38 21212 22984 23821 1262 5727 -577 C ATOM 4881 CG GLN B 38 50.708 32.646 -21.959 1.00177.48 C ANISOU 4881 CG GLN B 38 21227 23059 23148 1587 5668 -710 C ATOM 4882 CD GLN B 38 49.453 32.028 -21.371 1.00171.82 C ANISOU 4882 CD GLN B 38 21196 22467 21619 1587 5157 -777 C ATOM 4883 OE1 GLN B 38 48.336 32.337 -21.791 1.00170.66 O ANISOU 4883 OE1 GLN B 38 21147 22200 21495 1562 4447 -1022 O ATOM 4884 NE2 GLN B 38 49.630 31.174 -20.370 1.00168.29 N ANISOU 4884 NE2 GLN B 38 21224 22273 20445 1623 5523 -555 N ATOM 4885 N GLY B 39 53.557 34.067 -18.883 1.00186.28 N ANISOU 4885 N GLY B 39 21117 23021 26641 792 4380 -1061 N ATOM 4886 CA GLY B 39 54.925 33.579 -18.875 1.00200.24 C ANISOU 4886 CA GLY B 39 22256 24626 29199 859 4278 -1229 C ATOM 4887 C GLY B 39 55.131 32.389 -17.953 1.00214.24 C ANISOU 4887 C GLY B 39 24086 26288 31028 891 3475 -1542 C ATOM 4888 O GLY B 39 55.628 31.335 -18.375 1.00218.81 O ANISOU 4888 O GLY B 39 24463 26967 31707 1143 3464 -1689 O ATOM 4889 N ASP B 40 54.747 32.532 -16.682 1.00187.75 N ANISOU 4889 N ASP B 40 21013 22722 27601 640 2794 -1646 N ATOM 4890 CA ASP B 40 55.242 31.646 -15.635 1.00188.07 C ANISOU 4890 CA ASP B 40 20959 22557 27941 595 2001 -1943 C ATOM 4891 C ASP B 40 54.232 31.604 -14.504 1.00183.15 C ANISOU 4891 C ASP B 40 20925 21858 26804 410 1344 -2020 C ATOM 4892 O ASP B 40 53.259 32.365 -14.480 1.00179.96 O ANISOU 4892 O ASP B 40 20946 21525 25904 292 1506 -1836 O ATOM 4893 CB ASP B 40 56.628 32.092 -15.114 1.00193.23 C ANISOU 4893 CB ASP B 40 20955 22865 29600 406 1838 -2019 C ATOM 4894 CG ASP B 40 56.690 33.601 -14.800 1.00194.26 C ANISOU 4894 CG ASP B 40 20992 22786 30030 88 2028 -1821 C ATOM 4895 OD1 ASP B 40 55.727 34.160 -14.210 1.00190.43 O ANISOU 4895 OD1 ASP B 40 20999 22270 29085 -99 1824 -1745 O ATOM 4896 OD2 ASP B 40 57.694 34.236 -15.182 1.00198.94 O ANISOU 4896 OD2 ASP B 40 21021 23254 31312 32 2406 -1730 O ATOM 4897 N LYS B 41 54.479 30.669 -13.578 1.00185.43 N ANISOU 4897 N LYS B 41 15778 33866 20811 1217 1039 -5884 N ATOM 4898 CA LYS B 41 53.813 30.614 -12.281 1.00176.86 C ANISOU 4898 CA LYS B 41 15673 31914 19612 1668 552 -5659 C ATOM 4899 C LYS B 41 54.311 31.689 -11.321 1.00187.83 C ANISOU 4899 C LYS B 41 17363 32790 21214 1286 351 -5717 C ATOM 4900 O LYS B 41 53.632 31.988 -10.327 1.00191.10 O ANISOU 4900 O LYS B 41 18686 32439 21484 1463 140 -5390 O ATOM 4901 CB LYS B 41 54.024 29.236 -11.630 1.00172.93 C ANISOU 4901 CB LYS B 41 15163 31372 19172 2417 -246 -6214 C ATOM 4902 CG LYS B 41 54.103 28.044 -12.597 1.00172.17 C ANISOU 4902 CG LYS B 41 14386 31987 19042 2776 -224 -6507 C ATOM 4903 CD LYS B 41 52.755 27.344 -12.737 1.00164.73 C ANISOU 4903 CD LYS B 41 14142 30804 17645 3246 -75 -5955 C ATOM 4904 CE LYS B 41 52.850 26.074 -13.571 1.00163.91 C ANISOU 4904 CE LYS B 41 13421 31347 17510 3668 -156 -6278 C ATOM 4905 NZ LYS B 41 51.563 25.318 -13.628 1.00156.86 N ANISOU 4905 NZ LYS B 41 13227 30207 16168 4142 -63 -5797 N ATOM 4906 N GLU B 42 55.499 32.242 -11.574 1.00184.21 N ANISOU 4906 N GLU B 42 16142 32757 21093 751 411 -6186 N ATOM 4907 CA GLU B 42 56.048 33.254 -10.678 1.00187.96 C ANISOU 4907 CA GLU B 42 16847 32780 21790 374 210 -6284 C ATOM 4908 C GLU B 42 55.116 34.447 -10.562 1.00185.10 C ANISOU 4908 C GLU B 42 17352 31809 21169 4 679 -5446 C ATOM 4909 O GLU B 42 54.877 34.954 -9.460 1.00184.16 O ANISOU 4909 O GLU B 42 17933 30973 21067 69 380 -5299 O ATOM 4910 CB GLU B 42 57.422 33.704 -11.167 1.00196.07 C ANISOU 4910 CB GLU B 42 16848 34464 23185 -250 347 -6921 C ATOM 4911 CG GLU B 42 58.534 32.722 -10.869 1.00200.55 C ANISOU 4911 CG GLU B 42 16582 35456 24164 143 -345 -7951 C ATOM 4912 CD GLU B 42 58.842 32.641 -9.391 1.00201.35 C ANISOU 4912 CD GLU B 42 17160 34869 24476 547 -1209 -8272 C ATOM 4913 OE1 GLU B 42 58.491 33.590 -8.658 1.00200.19 O ANISOU 4913 OE1 GLU B 42 17772 34054 24236 298 -1153 -7805 O ATOM 4914 OE2 GLU B 42 59.432 31.629 -8.963 1.00203.43 O ANISOU 4914 OE2 GLU B 42 17072 35232 24992 1116 -1982 -9003 O ATOM 4915 N ALA B 43 54.575 34.904 -11.690 1.00184.04 N ANISOU 4915 N ALA B 43 17204 31927 20795 -378 1377 -4917 N ATOM 4916 CA ALA B 43 53.625 36.007 -11.657 1.00181.65 C ANISOU 4916 CA ALA B 43 17739 31016 20263 -660 1749 -4149 C ATOM 4917 C ALA B 43 52.325 35.594 -10.981 1.00174.62 C ANISOU 4917 C ALA B 43 17719 29492 19136 -9 1565 -3765 C ATOM 4918 O ALA B 43 51.773 36.354 -10.179 1.00173.28 O ANISOU 4918 O ALA B 43 18293 28614 18932 -44 1497 -3457 O ATOM 4919 CB ALA B 43 53.364 36.515 -13.073 1.00182.78 C ANISOU 4919 CB ALA B 43 17712 31552 20183 -1199 2445 -3709 C ATOM 4920 N GLU B 44 51.821 34.392 -11.280 1.00231.00 N ANISOU 4920 N GLU B 44 24774 36889 26108 559 1494 -3823 N ATOM 4921 CA GLU B 44 50.590 33.946 -10.635 1.00223.81 C ANISOU 4921 CA GLU B 44 24680 35421 24937 1113 1357 -3533 C ATOM 4922 C GLU B 44 50.794 33.777 -9.136 1.00218.70 C ANISOU 4922 C GLU B 44 24520 34200 24375 1367 727 -3859 C ATOM 4923 O GLU B 44 49.883 34.043 -8.345 1.00215.92 O ANISOU 4923 O GLU B 44 24995 33198 23849 1512 690 -3591 O ATOM 4924 CB GLU B 44 50.089 32.646 -11.274 1.00217.00 C ANISOU 4924 CB GLU B 44 23611 34983 23858 1629 1399 -3569 C ATOM 4925 CG GLU B 44 50.528 31.362 -10.597 1.00210.95 C ANISOU 4925 CG GLU B 44 22733 34291 23127 2167 746 -4138 C ATOM 4926 CD GLU B 44 50.003 30.120 -11.290 1.00199.91 C ANISOU 4926 CD GLU B 44 21156 33304 21496 2648 809 -4140 C ATOM 4927 OE1 GLU B 44 49.061 30.229 -12.103 1.00189.76 O ANISOU 4927 OE1 GLU B 44 20003 32119 19976 2641 1353 -3646 O ATOM 4928 OE2 GLU B 44 50.543 29.030 -11.018 1.00201.23 O ANISOU 4928 OE2 GLU B 44 21065 33672 21723 3049 266 -4657 O ATOM 4929 N ALA B 45 51.995 33.363 -8.726 1.00168.57 N ANISOU 4929 N ALA B 45 17672 28077 18301 1398 213 -4483 N ATOM 4930 CA ALA B 45 52.281 33.220 -7.304 1.00169.50 C ANISOU 4930 CA ALA B 45 18291 27616 18495 1609 -461 -4812 C ATOM 4931 C ALA B 45 52.350 34.580 -6.625 1.00171.64 C ANISOU 4931 C ALA B 45 18979 27345 18890 1142 -372 -4598 C ATOM 4932 O ALA B 45 51.816 34.760 -5.525 1.00169.76 O ANISOU 4932 O ALA B 45 19560 26415 18524 1265 -620 -4497 O ATOM 4933 CB ALA B 45 53.586 32.449 -7.108 1.00174.25 C ANISOU 4933 CB ALA B 45 18206 28593 19408 1796 -1108 -5591 C ATOM 4934 N LYS B 46 52.997 35.550 -7.271 1.00175.86 N ANISOU 4934 N LYS B 46 18989 28183 19648 559 -6 -4540 N ATOM 4935 CA LYS B 46 53.019 36.908 -6.741 1.00177.99 C ANISOU 4935 CA LYS B 46 19669 27940 20018 81 120 -4284 C ATOM 4936 C LYS B 46 51.629 37.532 -6.772 1.00173.46 C ANISOU 4936 C LYS B 46 19889 26850 19170 85 530 -3614 C ATOM 4937 O LYS B 46 51.186 38.125 -5.781 1.00172.60 O ANISOU 4937 O LYS B 46 20478 26060 19042 75 387 -3481 O ATOM 4938 CB LYS B 46 54.012 37.758 -7.531 1.00183.97 C ANISOU 4938 CB LYS B 46 19715 29173 21012 -610 450 -4378 C ATOM 4939 CG LYS B 46 55.469 37.495 -7.192 1.00189.88 C ANISOU 4939 CG LYS B 46 19724 30285 22135 -717 -2 -5151 C ATOM 4940 CD LYS B 46 55.904 38.289 -5.969 1.00192.59 C ANISOU 4940 CD LYS B 46 20470 30024 22683 -903 -383 -5286 C ATOM 4941 CE LYS B 46 57.397 38.154 -5.728 1.00199.33 C ANISOU 4941 CE LYS B 46 20509 31272 23957 -1067 -806 -6097 C ATOM 4942 NZ LYS B 46 57.854 39.042 -4.628 1.00202.36 N ANISOU 4942 NZ LYS B 46 21254 31091 24544 -1323 -1121 -6199 N ATOM 4943 N PHE B 47 50.927 37.402 -7.905 1.00170.87 N ANISOU 4943 N PHE B 47 19445 26837 18642 111 1020 -3234 N ATOM 4944 CA PHE B 47 49.600 38.002 -8.046 1.00167.21 C ANISOU 4944 CA PHE B 47 19657 25909 17966 150 1375 -2667 C ATOM 4945 C PHE B 47 48.656 37.524 -6.954 1.00162.70 C ANISOU 4945 C PHE B 47 19820 24777 17223 637 1124 -2706 C ATOM 4946 O PHE B 47 47.906 38.322 -6.377 1.00161.75 O ANISOU 4946 O PHE B 47 20336 24048 17074 571 1203 -2476 O ATOM 4947 CB PHE B 47 49.013 37.682 -9.426 1.00165.04 C ANISOU 4947 CB PHE B 47 19118 26096 17494 207 1840 -2337 C ATOM 4948 CG PHE B 47 47.529 37.955 -9.546 1.00160.66 C ANISOU 4948 CG PHE B 47 19219 25098 16728 452 2099 -1881 C ATOM 4949 CD1 PHE B 47 47.066 39.213 -9.904 1.00162.35 C ANISOU 4949 CD1 PHE B 47 19788 24934 16963 98 2354 -1449 C ATOM 4950 CD2 PHE B 47 46.598 36.949 -9.316 1.00155.37 C ANISOU 4950 CD2 PHE B 47 18811 24383 15840 1031 2058 -1931 C ATOM 4951 CE1 PHE B 47 45.705 39.463 -10.018 1.00158.95 C ANISOU 4951 CE1 PHE B 47 19904 24092 16400 376 2525 -1129 C ATOM 4952 CE2 PHE B 47 45.236 37.198 -9.427 1.00151.87 C ANISOU 4952 CE2 PHE B 47 18892 23573 15241 1252 2306 -1616 C ATOM 4953 CZ PHE B 47 44.791 38.456 -9.780 1.00153.73 C ANISOU 4953 CZ PHE B 47 19414 23439 15557 954 2521 -1241 C ATOM 4954 N LYS B 48 48.676 36.219 -6.661 1.00160.33 N ANISOU 4954 N LYS B 48 19463 24669 16787 1099 816 -3033 N ATOM 4955 CA LYS B 48 47.806 35.675 -5.623 1.00156.61 C ANISOU 4955 CA LYS B 48 19753 23687 16066 1470 591 -3113 C ATOM 4956 C LYS B 48 47.984 36.401 -4.295 1.00158.69 C ANISOU 4956 C LYS B 48 20585 23285 16426 1266 282 -3243 C ATOM 4957 O LYS B 48 47.032 36.504 -3.507 1.00156.21 O ANISOU 4957 O LYS B 48 21006 22437 15912 1363 311 -3185 O ATOM 4958 CB LYS B 48 48.072 34.181 -5.441 1.00155.22 C ANISOU 4958 CB LYS B 48 19467 23783 15726 1912 173 -3498 C ATOM 4959 CG LYS B 48 47.524 33.302 -6.556 1.00151.73 C ANISOU 4959 CG LYS B 48 18687 23876 15086 2217 486 -3354 C ATOM 4960 CD LYS B 48 47.989 31.867 -6.383 1.00151.39 C ANISOU 4960 CD LYS B 48 18486 24103 14931 2632 -22 -3785 C ATOM 4961 CE LYS B 48 47.566 30.992 -7.552 1.00148.28 C ANISOU 4961 CE LYS B 48 17666 24300 14374 2922 282 -3666 C ATOM 4962 NZ LYS B 48 48.021 29.585 -7.353 1.00148.29 N ANISOU 4962 NZ LYS B 48 17554 24518 14272 3352 -284 -4111 N ATOM 4963 N GLU B 49 49.189 36.918 -4.033 1.00163.52 N ANISOU 4963 N GLU B 49 20848 23936 17344 955 7 -3460 N ATOM 4964 CA GLU B 49 49.422 37.642 -2.788 1.00165.74 C ANISOU 4964 CA GLU B 49 21647 23592 17734 745 -298 -3581 C ATOM 4965 C GLU B 49 48.937 39.086 -2.880 1.00166.52 C ANISOU 4965 C GLU B 49 22001 23325 17942 359 109 -3178 C ATOM 4966 O GLU B 49 48.391 39.623 -1.906 1.00165.98 O ANISOU 4966 O GLU B 49 22604 22634 17828 307 44 -3152 O ATOM 4967 CB GLU B 49 50.907 37.592 -2.422 1.00170.86 C ANISOU 4967 CB GLU B 49 21822 24410 18687 597 -806 -4033 C ATOM 4968 CG GLU B 49 51.393 36.219 -1.949 1.00170.96 C ANISOU 4968 CG GLU B 49 21800 24542 18617 1034 -1444 -4533 C ATOM 4969 CD GLU B 49 52.861 36.234 -1.532 1.00176.75 C ANISOU 4969 CD GLU B 49 22047 25393 19718 927 -2027 -5070 C ATOM 4970 OE1 GLU B 49 53.529 37.255 -1.798 1.00180.52 O ANISOU 4970 OE1 GLU B 49 22080 26004 20504 471 -1819 -5047 O ATOM 4971 OE2 GLU B 49 53.347 35.237 -0.939 1.00177.96 O ANISOU 4971 OE2 GLU B 49 22283 25483 19849 1287 -2720 -5541 O ATOM 4972 N ILE B 50 49.120 39.727 -4.041 1.00168.18 N ANISOU 4972 N ILE B 50 21728 23895 18279 64 508 -2882 N ATOM 4973 CA ILE B 50 48.587 41.072 -4.236 1.00169.22 C ANISOU 4973 CA ILE B 50 22179 23634 18483 -274 835 -2472 C ATOM 4974 C ILE B 50 47.075 41.066 -4.058 1.00164.78 C ANISOU 4974 C ILE B 50 22236 22660 17712 49 1043 -2263 C ATOM 4975 O ILE B 50 46.503 41.980 -3.453 1.00165.20 O ANISOU 4975 O ILE B 50 22816 22125 17829 -64 1072 -2158 O ATOM 4976 CB ILE B 50 49.004 41.621 -5.614 1.00172.08 C ANISOU 4976 CB ILE B 50 22009 24456 18917 -673 1201 -2182 C ATOM 4977 CG1 ILE B 50 50.507 41.918 -5.637 1.00177.72 C ANISOU 4977 CG1 ILE B 50 22147 25502 19875 -1142 1043 -2468 C ATOM 4978 CG2 ILE B 50 48.220 42.883 -5.967 1.00172.80 C ANISOU 4978 CG2 ILE B 50 22562 24086 19009 -928 1486 -1705 C ATOM 4979 CD1 ILE B 50 51.265 41.114 -6.653 1.00179.15 C ANISOU 4979 CD1 ILE B 50 21496 26516 20058 -1187 1155 -2685 C ATOM 4980 N LYS B 51 46.408 40.030 -4.570 1.00160.75 N ANISOU 4980 N LYS B 51 21645 22466 16965 454 1189 -2256 N ATOM 4981 CA LYS B 51 44.991 39.845 -4.280 1.00156.69 C ANISOU 4981 CA LYS B 51 21681 21610 16245 780 1367 -2203 C ATOM 4982 C LYS B 51 44.763 39.749 -2.775 1.00156.27 C ANISOU 4982 C LYS B 51 22253 21016 16105 826 1084 -2533 C ATOM 4983 O LYS B 51 44.037 40.559 -2.193 1.00156.46 O ANISOU 4983 O LYS B 51 22763 20509 16176 738 1182 -2512 O ATOM 4984 CB LYS B 51 44.462 38.599 -5.002 1.00152.66 C ANISOU 4984 CB LYS B 51 20950 21580 15474 1190 1528 -2210 C ATOM 4985 CG LYS B 51 42.956 38.383 -4.861 1.00148.73 C ANISOU 4985 CG LYS B 51 20930 20819 14762 1503 1784 -2196 C ATOM 4986 CD LYS B 51 42.517 37.107 -5.574 1.00144.89 C ANISOU 4986 CD LYS B 51 20209 20835 14009 1887 1932 -2211 C ATOM 4987 CE LYS B 51 43.220 35.883 -5.011 1.00144.34 C ANISOU 4987 CE LYS B 51 20100 20985 13758 2038 1550 -2552 C ATOM 4988 NZ LYS B 51 42.790 35.589 -3.618 1.00143.63 N ANISOU 4988 NZ LYS B 51 20744 20383 13444 2065 1326 -2877 N ATOM 4989 N GLU B 52 45.410 38.777 -2.125 1.00156.24 N ANISOU 4989 N GLU B 52 22267 21122 15975 944 693 -2870 N ATOM 4990 CA GLU B 52 45.255 38.503 -0.696 1.00156.17 C ANISOU 4990 CA GLU B 52 22940 20608 15789 954 367 -3200 C ATOM 4991 C GLU B 52 45.396 39.764 0.147 1.00159.16 C ANISOU 4991 C GLU B 52 23666 20420 16387 599 298 -3199 C ATOM 4992 O GLU B 52 44.703 39.920 1.155 1.00158.56 O ANISOU 4992 O GLU B 52 24251 19838 16155 555 289 -3371 O ATOM 4993 CB GLU B 52 46.278 37.455 -0.226 1.00157.46 C ANISOU 4993 CB GLU B 52 23019 20941 15866 1075 -201 -3545 C ATOM 4994 CG GLU B 52 46.104 37.026 1.235 1.00157.68 C ANISOU 4994 CG GLU B 52 23889 20413 15608 1064 -603 -3879 C ATOM 4995 CD GLU B 52 47.117 35.963 1.668 1.00159.56 C ANISOU 4995 CD GLU B 52 24116 20749 15762 1233 -1295 -4235 C ATOM 4996 OE1 GLU B 52 48.339 36.247 1.648 1.00163.35 O ANISOU 4996 OE1 GLU B 52 24115 21362 16588 1135 -1656 -4370 O ATOM 4997 OE2 GLU B 52 46.689 34.844 2.041 1.00157.70 O ANISOU 4997 OE2 GLU B 52 24373 20436 15111 1456 -1509 -4420 O ATOM 4998 N ALA B 53 46.274 40.680 -0.276 1.00162.65 N ANISOU 4998 N ALA B 53 23672 20955 17173 303 278 -3027 N ATOM 4999 CA ALA B 53 46.398 41.964 0.406 1.00165.62 C ANISOU 4999 CA ALA B 53 24352 20801 17776 -46 235 -2981 C ATOM 5000 C ALA B 53 45.211 42.873 0.096 1.00164.58 C ANISOU 5000 C ALA B 53 24492 20353 17690 -60 640 -2723 C ATOM 5001 O ALA B 53 44.711 43.577 0.984 1.00165.35 O ANISOU 5001 O ALA B 53 25101 19889 17835 -174 625 -2828 O ATOM 5002 CB ALA B 53 47.719 42.632 0.020 1.00170.10 C ANISOU 5002 CB ALA B 53 24381 21585 18664 -405 98 -2906 C ATOM 5003 N TYR B 54 44.745 42.871 -1.159 1.00163.22 N ANISOU 5003 N TYR B 54 23983 20517 17515 67 970 -2424 N ATOM 5004 CA TYR B 54 43.577 43.669 -1.528 1.00162.61 C ANISOU 5004 CA TYR B 54 24160 20122 17503 134 1265 -2227 C ATOM 5005 C TYR B 54 42.334 43.200 -0.785 1.00159.48 C ANISOU 5005 C TYR B 54 24248 19445 16900 425 1379 -2538 C ATOM 5006 O TYR B 54 41.447 44.004 -0.461 1.00160.11 O ANISOU 5006 O TYR B 54 24671 19065 17099 429 1496 -2607 O ATOM 5007 CB TYR B 54 43.346 43.601 -3.039 1.00161.87 C ANISOU 5007 CB TYR B 54 23652 20455 17398 235 1534 -1866 C ATOM 5008 CG TYR B 54 42.045 44.229 -3.495 1.00161.23 C ANISOU 5008 CG TYR B 54 23836 20053 17370 422 1757 -1718 C ATOM 5009 CD1 TYR B 54 41.847 45.600 -3.389 1.00166.28 C ANISOU 5009 CD1 TYR B 54 24768 20150 18263 202 1688 -1577 C ATOM 5010 CD2 TYR B 54 41.022 43.458 -4.046 1.00157.45 C ANISOU 5010 CD2 TYR B 54 23312 19802 16712 835 1992 -1752 C ATOM 5011 CE1 TYR B 54 40.670 46.195 -3.814 1.00169.15 C ANISOU 5011 CE1 TYR B 54 25368 20176 18725 425 1789 -1507 C ATOM 5012 CE2 TYR B 54 39.829 44.045 -4.478 1.00160.80 C ANISOU 5012 CE2 TYR B 54 23938 19922 17235 1048 2138 -1691 C ATOM 5013 CZ TYR B 54 39.663 45.420 -4.357 1.00164.32 C ANISOU 5013 CZ TYR B 54 24670 19801 17962 858 2006 -1584 C ATOM 5014 OH TYR B 54 38.495 46.029 -4.776 1.00162.80 O ANISOU 5014 OH TYR B 54 24682 19257 17918 1117 2046 -1589 O ATOM 5015 N GLU B 55 42.258 41.896 -0.503 1.00156.55 N ANISOU 5015 N GLU B 55 23920 19348 16215 646 1337 -2778 N ATOM 5016 CA GLU B 55 41.064 41.342 0.121 1.00153.84 C ANISOU 5016 CA GLU B 55 24043 18813 15597 844 1511 -3105 C ATOM 5017 C GLU B 55 41.028 41.668 1.609 1.00155.58 C ANISOU 5017 C GLU B 55 24870 18485 15758 595 1334 -3463 C ATOM 5018 O GLU B 55 39.961 41.974 2.160 1.00155.31 O ANISOU 5018 O GLU B 55 25230 18110 15670 589 1555 -3736 O ATOM 5019 CB GLU B 55 41.009 39.828 -0.113 1.00150.54 C ANISOU 5019 CB GLU B 55 23543 18849 14805 1110 1509 -3219 C ATOM 5020 CG GLU B 55 41.362 39.397 -1.543 1.00149.23 C ANISOU 5020 CG GLU B 55 22715 19293 14694 1311 1615 -2882 C ATOM 5021 CD GLU B 55 41.098 37.920 -1.832 1.00145.71 C ANISOU 5021 CD GLU B 55 22205 19274 13883 1626 1649 -3005 C ATOM 5022 OE1 GLU B 55 41.500 37.043 -1.031 1.00145.52 O ANISOU 5022 OE1 GLU B 55 22476 19217 13599 1630 1333 -3281 O ATOM 5023 OE2 GLU B 55 40.469 37.642 -2.876 1.00143.34 O ANISOU 5023 OE2 GLU B 55 21603 19313 13547 1872 1961 -2821 O ATOM 5024 N VAL B 56 42.189 41.641 2.269 1.00157.81 N ANISOU 5024 N VAL B 56 25216 18677 16066 371 932 -3510 N ATOM 5025 CA VAL B 56 42.216 41.901 3.703 1.00159.65 C ANISOU 5025 CA VAL B 56 26078 18377 16205 108 726 -3840 C ATOM 5026 C VAL B 56 42.048 43.392 3.987 1.00162.44 C ANISOU 5026 C VAL B 56 26525 18273 16923 -125 807 -3779 C ATOM 5027 O VAL B 56 41.461 43.771 5.007 1.00163.38 O ANISOU 5027 O VAL B 56 27171 17930 16977 -290 857 -4095 O ATOM 5028 CB VAL B 56 43.509 41.326 4.315 1.00161.41 C ANISOU 5028 CB VAL B 56 26363 18623 16342 -6 188 -3945 C ATOM 5029 CG1 VAL B 56 44.724 41.796 3.555 1.00163.69 C ANISOU 5029 CG1 VAL B 56 25973 19213 17009 -70 7 -3663 C ATOM 5030 CG2 VAL B 56 43.639 41.690 5.787 1.00163.85 C ANISOU 5030 CG2 VAL B 56 27358 18339 16560 -319 -74 -4247 C ATOM 5031 N LEU B 57 42.510 44.258 3.084 1.00168.40 N ANISOU 5031 N LEU B 57 26810 19135 18037 -170 831 -3399 N ATOM 5032 CA LEU B 57 42.505 45.696 3.331 1.00172.38 C ANISOU 5032 CA LEU B 57 27436 19172 18886 -413 815 -3308 C ATOM 5033 C LEU B 57 41.174 46.375 2.992 1.00179.03 C ANISOU 5033 C LEU B 57 28397 19762 19866 -244 1121 -3342 C ATOM 5034 O LEU B 57 40.901 47.459 3.523 1.00197.82 O ANISOU 5034 O LEU B 57 31039 21638 22485 -401 1079 -3440 O ATOM 5035 CB LEU B 57 43.653 46.361 2.556 1.00170.21 C ANISOU 5035 CB LEU B 57 26699 19082 18891 -632 670 -2907 C ATOM 5036 CG LEU B 57 45.035 46.526 3.218 1.00173.22 C ANISOU 5036 CG LEU B 57 27024 19415 19375 -955 297 -2965 C ATOM 5037 CD1 LEU B 57 45.434 45.300 4.042 1.00171.80 C ANISOU 5037 CD1 LEU B 57 27016 19351 18910 -850 18 -3311 C ATOM 5038 CD2 LEU B 57 46.123 46.857 2.179 1.00175.75 C ANISOU 5038 CD2 LEU B 57 26740 20143 19894 -1168 264 -2640 C ATOM 5039 N THR B 58 40.334 45.767 2.141 1.00164.18 N ANISOU 5039 N THR B 58 26322 18200 17860 93 1390 -3310 N ATOM 5040 CA THR B 58 38.994 46.291 1.887 1.00164.12 C ANISOU 5040 CA THR B 58 26415 17950 17993 317 1631 -3472 C ATOM 5041 C THR B 58 38.007 45.939 3.001 1.00163.26 C ANISOU 5041 C THR B 58 26735 17605 17692 333 1810 -4091 C ATOM 5042 O THR B 58 37.021 46.661 3.190 1.00164.77 O ANISOU 5042 O THR B 58 27059 17451 18096 415 1939 -4396 O ATOM 5043 CB THR B 58 38.476 45.785 0.531 1.00161.71 C ANISOU 5043 CB THR B 58 25729 18076 17637 668 1837 -3229 C ATOM 5044 OG1 THR B 58 37.144 46.287 0.286 1.00162.10 O ANISOU 5044 OG1 THR B 58 25860 17867 17862 937 2007 -3459 O ATOM 5045 CG2 THR B 58 38.454 44.263 0.485 1.00157.73 C ANISOU 5045 CG2 THR B 58 25128 18079 16722 836 1971 -3351 C ATOM 5046 N ASP B 59 38.241 44.846 3.729 1.00189.53 N ANISOU 5046 N ASP B 59 31219 17326 23470 -5466 7175 -2353 N ATOM 5047 CA ASP B 59 37.435 44.517 4.899 1.00191.93 C ANISOU 5047 CA ASP B 59 31330 18017 23577 -5428 7295 -2237 C ATOM 5048 C ASP B 59 37.858 45.409 6.057 1.00196.38 C ANISOU 5048 C ASP B 59 32516 18264 23834 -5711 7947 -2808 C ATOM 5049 O ASP B 59 39.043 45.489 6.385 1.00195.17 O ANISOU 5049 O ASP B 59 32699 17955 23501 -6292 7842 -3354 O ATOM 5050 CB ASP B 59 37.598 43.041 5.273 1.00187.21 C ANISOU 5050 CB ASP B 59 30160 18087 22883 -5846 6425 -2128 C ATOM 5051 CG ASP B 59 36.647 42.595 6.399 1.00189.38 C ANISOU 5051 CG ASP B 59 30155 18816 22985 -5757 6492 -1927 C ATOM 5052 OD1 ASP B 59 35.990 43.446 7.037 1.00194.64 O ANISOU 5052 OD1 ASP B 59 31123 19271 23560 -5456 7223 -1957 O ATOM 5053 OD2 ASP B 59 36.563 41.368 6.645 1.00185.73 O ANISOU 5053 OD2 ASP B 59 29163 18931 22477 -5995 5798 -1737 O ATOM 5054 N SER B 60 36.883 46.060 6.694 1.00201.51 N ANISOU 5054 N SER B 60 33310 18833 24422 -5305 8612 -2679 N ATOM 5055 CA SER B 60 37.190 47.025 7.747 1.00206.23 C ANISOU 5055 CA SER B 60 34527 19085 24747 -5501 9313 -3194 C ATOM 5056 C SER B 60 37.803 46.351 8.970 1.00205.03 C ANISOU 5056 C SER B 60 34353 19288 24262 -6164 8985 -3584 C ATOM 5057 O SER B 60 38.859 46.772 9.458 1.00205.54 O ANISOU 5057 O SER B 60 34895 19082 24117 -6665 9135 -4174 O ATOM 5058 CB SER B 60 35.924 47.788 8.135 1.00211.82 C ANISOU 5058 CB SER B 60 35337 19672 25475 -4890 10059 -2916 C ATOM 5059 OG SER B 60 34.855 46.896 8.412 1.00211.11 O ANISOU 5059 OG SER B 60 34642 20151 25420 -4639 9741 -2407 O ATOM 5060 N GLN B 61 37.148 45.307 9.483 1.00203.49 N ANISOU 5060 N GLN B 61 33609 19698 24011 -6174 8540 -3261 N ATOM 5061 CA GLN B 61 37.597 44.668 10.717 1.00202.73 C ANISOU 5061 CA GLN B 61 33472 19964 23592 -6760 8264 -3594 C ATOM 5062 C GLN B 61 38.944 43.981 10.533 1.00197.66 C ANISOU 5062 C GLN B 61 32803 19423 22875 -7434 7583 -3958 C ATOM 5063 O GLN B 61 39.852 44.144 11.356 1.00198.14 O ANISOU 5063 O GLN B 61 33232 19389 22664 -7989 7652 -4519 O ATOM 5064 CB GLN B 61 36.543 43.672 11.190 1.00201.99 C ANISOU 5064 CB GLN B 61 32759 20502 23486 -6577 7913 -3116 C ATOM 5065 CG GLN B 61 35.196 44.314 11.476 1.00207.11 C ANISOU 5065 CG GLN B 61 33424 21081 24187 -5932 8583 -2765 C ATOM 5066 CD GLN B 61 34.144 43.296 11.892 1.00206.20 C ANISOU 5066 CD GLN B 61 32672 21602 24072 -5744 8210 -2271 C ATOM 5067 OE1 GLN B 61 34.063 42.204 11.321 1.00201.52 O ANISOU 5067 OE1 GLN B 61 31513 21435 23621 -5778 7469 -1928 O ATOM 5068 NE2 GLN B 61 33.340 43.644 12.896 1.00210.65 N ANISOU 5068 NE2 GLN B 61 33328 22236 24476 -5550 8719 -2238 N ATOM 5069 N LYS B 62 39.093 43.213 9.451 1.00192.77 N ANISOU 5069 N LYS B 62 31752 18996 22494 -7396 6921 -3648 N ATOM 5070 CA LYS B 62 40.356 42.525 9.206 1.00187.74 C ANISOU 5070 CA LYS B 62 31062 18467 21804 -8018 6245 -3966 C ATOM 5071 C LYS B 62 41.481 43.515 8.933 1.00188.71 C ANISOU 5071 C LYS B 62 31839 17977 21887 -8279 6612 -4515 C ATOM 5072 O LYS B 62 42.655 43.201 9.159 1.00186.41 O ANISOU 5072 O LYS B 62 31691 17697 21440 -8901 6252 -4965 O ATOM 5073 CB LYS B 62 40.193 41.538 8.046 1.00182.50 C ANISOU 5073 CB LYS B 62 29794 18122 21425 -7864 5493 -3479 C ATOM 5074 CG LYS B 62 41.268 40.450 7.958 1.00176.72 C ANISOU 5074 CG LYS B 62 28811 17713 20621 -8507 4633 -3688 C ATOM 5075 CD LYS B 62 41.355 39.608 9.225 1.00175.98 C ANISOU 5075 CD LYS B 62 28512 18122 20229 -8972 4302 -3851 C ATOM 5076 CE LYS B 62 42.501 38.601 9.159 1.00170.41 C ANISOU 5076 CE LYS B 62 27609 17699 19440 -9634 3482 -4105 C ATOM 5077 NZ LYS B 62 42.677 37.869 10.449 1.00169.95 N ANISOU 5077 NZ LYS B 62 27417 18087 19069 -10122 3206 -4325 N ATOM 5078 N ARG B 63 41.147 44.719 8.466 1.00192.61 N ANISOU 5078 N ARG B 63 32738 17932 22515 -7817 7332 -4492 N ATOM 5079 CA ARG B 63 42.174 45.739 8.285 1.00194.04 C ANISOU 5079 CA ARG B 63 33575 17510 22641 -8052 7749 -5029 C ATOM 5080 C ARG B 63 42.667 46.253 9.627 1.00197.42 C ANISOU 5080 C ARG B 63 34495 17804 22713 -8478 8184 -5602 C ATOM 5081 O ARG B 63 43.869 46.493 9.804 1.00196.51 O ANISOU 5081 O ARG B 63 34768 17449 22447 -9008 8150 -6149 O ATOM 5082 CB ARG B 63 41.643 46.894 7.438 1.00197.43 C ANISOU 5082 CB ARG B 63 34304 17401 23308 -7427 8415 -4839 C ATOM 5083 CG ARG B 63 42.651 48.019 7.274 1.00199.29 C ANISOU 5083 CG ARG B 63 35244 16991 23487 -7639 8904 -5390 C ATOM 5084 CD ARG B 63 42.144 49.135 6.373 1.00202.41 C ANISOU 5084 CD ARG B 63 35923 16856 24129 -7019 9536 -5191 C ATOM 5085 NE ARG B 63 43.179 50.148 6.184 1.00203.81 N ANISOU 5085 NE ARG B 63 36759 16428 24251 -7259 9949 -5729 N ATOM 5086 CZ ARG B 63 43.034 51.240 5.441 1.00206.52 C ANISOU 5086 CZ ARG B 63 37474 16220 24772 -6838 10529 -5700 C ATOM 5087 NH1 ARG B 63 41.890 51.469 4.807 1.00208.15 N ANISOU 5087 NH1 ARG B 63 37461 16402 25226 -6146 10769 -5155 N ATOM 5088 NH2 ARG B 63 44.037 52.104 5.330 1.00207.60 N ANISOU 5088 NH2 ARG B 63 38207 15832 24839 -7110 10869 -6218 N ATOM 5089 N ALA B 64 41.752 46.426 10.586 1.00201.36 N ANISOU 5089 N ALA B 64 34980 18457 23070 -8257 8596 -5485 N ATOM 5090 CA ALA B 64 42.165 46.803 11.932 1.00204.42 C ANISOU 5090 CA ALA B 64 35782 18781 23107 -8674 8963 -6004 C ATOM 5091 C ALA B 64 43.113 45.767 12.523 1.00200.27 C ANISOU 5091 C ALA B 64 35071 18659 22364 -9405 8256 -6320 C ATOM 5092 O ALA B 64 44.056 46.114 13.247 1.00201.19 O ANISOU 5092 O ALA B 64 35630 18587 22225 -9924 8414 -6905 O ATOM 5093 CB ALA B 64 40.943 46.996 12.828 1.00208.85 C ANISOU 5093 CB ALA B 64 36266 19518 23569 -8299 9433 -5758 C ATOM 5094 N ALA B 65 42.897 44.493 12.202 1.00195.64 N ANISOU 5094 N ALA B 65 33835 18621 21877 -9458 7466 -5945 N ATOM 5095 CA ALA B 65 43.797 43.429 12.662 1.00191.25 C ANISOU 5095 CA ALA B 65 33057 18471 21137 -10141 6731 -6208 C ATOM 5096 C ALA B 65 45.139 43.434 11.908 1.00187.59 C ANISOU 5096 C ALA B 65 32799 17747 20728 -10563 6385 -6565 C ATOM 5097 O ALA B 65 45.350 44.206 10.964 1.00188.16 O ANISOU 5097 O ALA B 65 33151 17344 20999 -10314 6674 -6576 O ATOM 5098 CB ALA B 65 43.115 42.062 12.526 1.00187.44 C ANISOU 5098 CB ALA B 65 31808 18659 20753 -10047 5996 -5676 C TER 5099 ALA B 65 HETATM 5100 PG ATP A 700 24.665 26.526 -24.090 1.00 76.39 P HETATM 5101 O1G ATP A 700 25.257 27.912 -24.224 1.00 71.02 O HETATM 5102 O2G ATP A 700 25.686 25.412 -24.024 1.00 69.35 O HETATM 5103 O3G ATP A 700 23.561 26.418 -23.062 1.00 68.97 O HETATM 5104 PB ATP A 700 24.234 27.118 -26.824 1.00 90.92 P HETATM 5105 O1B ATP A 700 24.562 26.155 -27.937 1.00 63.25 O HETATM 5106 O2B ATP A 700 25.184 28.246 -26.482 1.00 78.25 O HETATM 5107 O3B ATP A 700 23.892 26.281 -25.488 1.00 71.89 O HETATM 5108 PA ATP A 700 22.571 28.803 -28.275 1.00 58.30 P HETATM 5109 O1A ATP A 700 23.247 28.323 -29.540 1.00 87.28 O HETATM 5110 O2A ATP A 700 22.937 30.155 -27.716 1.00 66.30 O HETATM 5111 O3A ATP A 700 22.778 27.717 -27.117 1.00 63.71 O HETATM 5112 O5' ATP A 700 20.977 28.709 -28.445 1.00 58.70 O HETATM 5113 C5' ATP A 700 20.379 27.419 -28.541 1.00 55.74 C HETATM 5114 C4' ATP A 700 18.929 27.449 -28.073 1.00 61.20 C HETATM 5115 O4' ATP A 700 18.294 28.665 -28.456 1.00 70.46 O HETATM 5116 C3' ATP A 700 18.121 26.325 -28.700 1.00 59.11 C HETATM 5117 O3' ATP A 700 17.551 25.505 -27.680 1.00 49.63 O HETATM 5118 C2' ATP A 700 17.011 26.996 -29.478 1.00 62.22 C HETATM 5119 O2' ATP A 700 15.766 26.340 -29.265 1.00 64.24 O HETATM 5120 C1' ATP A 700 16.971 28.398 -28.917 1.00 65.65 C HETATM 5121 N9 ATP A 700 16.550 29.388 -29.939 1.00 73.31 N HETATM 5122 C8 ATP A 700 17.208 29.736 -31.057 1.00 83.66 C HETATM 5123 N7 ATP A 700 16.523 30.679 -31.756 1.00 84.18 N HETATM 5124 C5 ATP A 700 15.399 30.946 -31.074 1.00 75.10 C HETATM 5125 C6 ATP A 700 14.232 31.836 -31.240 1.00 80.41 C HETATM 5126 N6 ATP A 700 14.131 32.652 -32.311 1.00 96.81 N HETATM 5127 N1 ATP A 700 13.273 31.811 -30.298 1.00 71.14 N HETATM 5128 C2 ATP A 700 13.376 30.999 -29.237 1.00 59.81 C HETATM 5129 N3 ATP A 700 14.402 30.167 -29.019 1.00 53.59 N HETATM 5130 C4 ATP A 700 15.426 30.092 -29.886 1.00 65.08 C HETATM 5131 MG MG A 701 26.461 29.509 -25.301 1.00 48.13 MG2+ HETATM 5132 O HOH A 801 26.893 30.945 -23.718 1.00 42.47 O HETATM 5133 O HOH A 802 27.724 28.394 -25.121 1.00 53.56 O HETATM 5134 O HOH A 803 24.770 30.478 -25.160 1.00 55.44 O HETATM 5135 O HOH A 804 26.610 30.919 -26.647 1.00 68.60 O CONECT 330 3997 CONECT 3997 330 CONECT 5100 5101 5102 5103 5107 CONECT 5101 5100 5131 CONECT 5102 5100 CONECT 5103 5100 CONECT 5104 5105 5106 5107 5111 CONECT 5105 5104 CONECT 5106 5104 5131 CONECT 5107 5100 5104 CONECT 5108 5109 5110 5111 5112 CONECT 5109 5108 CONECT 5110 5108 CONECT 5111 5104 5108 CONECT 5112 5108 5113 CONECT 5113 5112 5114 CONECT 5114 5113 5115 5116 CONECT 5115 5114 5120 CONECT 5116 5114 5117 5118 CONECT 5117 5116 CONECT 5118 5116 5119 5120 CONECT 5119 5118 CONECT 5120 5115 5118 5121 CONECT 5121 5120 5122 5130 CONECT 5122 5121 5123 CONECT 5123 5122 5124 CONECT 5124 5123 5125 5130 CONECT 5125 5124 5126 5127 CONECT 5126 5125 CONECT 5127 5125 5128 CONECT 5128 5127 5129 CONECT 5129 5128 5130 CONECT 5130 5121 5124 5129 CONECT 5131 5101 5106 5132 5134 CONECT 5131 5135 CONECT 5132 5131 CONECT 5134 5131 CONECT 5135 5131 MASTER 526 0 2 25 30 0 8 6 5133 2 38 56 END If you find results from this site helpful for your research, please 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